|
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: 1095.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 1 MGEFIYQMKNVRKAHG-DKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEPGATVGILLQEPPL 79
Cdd:PRK11819 2 MAQYIYTMNRVSKVVPpKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEPQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 80 NEEKTVRGNVEEGLGDIFEKKARFEAIAEEMATN--YTDELMEEMGKLQEELDAADAWELDSKIEQAMDALRCPPADEPV 157
Cdd:PRK11819 82 DPEKTVRENVEEGVAEVKAALDRFNEIYAAYAEPdaDFDALAAEQGELQEIIDAADAWDLDSQLEIAMDALRCPPWDAKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 158 THLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAESVLWLEQHLAKYPGAVLAVTHDRYFLDHVAGWICEVDRGKLYPY 237
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPW 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 238 EGNYSTYLEKKAERLEVAGKKDAKLQKRLKDELAWVRSGQKARQAKNKARLERYEQMVEEAEQyKKLDFEEIQIPTPPRL 317
Cdd:PRK11819 242 EGNYSSWLEQKAKRLAQEEKQEAARQKALKRELEWVRQSPKARQAKSKARLARYEELLSEEYQ-KRNETNEIFIPPGPRL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 318 GNQVVEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQTVQLSYVDQGRENID 397
Cdd:PRK11819 321 GDKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQSRDALD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 398 PEKTVWEVVSDGLDYIVVGQNEMPSRAYLSAFGFKGADQQKPSKVLSGGERNRLNLALTLKQGGNLILLDEPTNDLDVET 477
Cdd:PRK11819 401 PNKTVWEEISGGLDIIKVGNREIPSRAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVET 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 512463837 478 LSSLENALQNFPGCAVVISHDRWFLDRTCTHILAWEGnfeEGKWFWFEGNFEGYEKNKIERYGEEAARPSRVTHRRLTR 556
Cdd:PRK11819 481 LRALEEALLEFPGCAVVISHDRWFLDRIATHILAFEG---DSQVEWFEGNFQEYEEDKKRRLGADAARPHRIKYKKLTR 556
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-554 |
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: 931.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 3 EFIYQMKNVRKAH-GDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEPGATVGILLQEPPLNE 81
Cdd:TIGR03719 2 QYIYTMNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 82 EKTVRGNVEEGLGDIFEKKARFEAIAEEMA--TNYTDELMEEMGKLQEELDAADAWELDSKIEQAMDALRCPPADEPVTH 159
Cdd:TIGR03719 82 TKTVRENVEEGVAEIKDALDRFNEISAKYAepDADFDKLAAEQAELQEIIDAADAWDLDSQLEIAMDALRCPPWDADVTK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 160 LSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAESVLWLEQHLAKYPGAVLAVTHDRYFLDHVAGWICEVDRGKLYPYEG 239
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 240 NYSTYLEKKAERLEVAGKKDAKLQKRLKDELAWVRSGQKARQAKNKARLERYEQMVEEAEQyKKLDFEEIQIPTPPRLGN 319
Cdd:TIGR03719 242 NYSSWLEQKQKRLEQEEKEESARQKTLKRELEWVRQSPKGRQAKSKARLARYEELLSQEFQ-KRNETAEIYIPPGPRLGD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 320 QVVEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQTVQLSYVDQGRENIDPE 399
Cdd:TIGR03719 321 KVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRDALDPN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 400 KTVWEVVSDGLDYIVVGQNEMPSRAYLSAFGFKGADQQKPSKVLSGGERNRLNLALTLKQGGNLILLDEPTNDLDVETLS 479
Cdd:TIGR03719 401 KTVWEEISGGLDIIKLGKREIPSRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLR 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 512463837 480 SLENALQNFPGCAVVISHDRWFLDRTCTHILAWEGnfeEGKWFWFEGNFEGYEKNKIERYGEEAARPSRVTHRRL 554
Cdd:TIGR03719 481 ALEEALLNFAGCAVVISHDRWFLDRIATHILAFEG---DSHVEWFEGNFSEYEEDKKRRLGEDADQPHRIKYKKL 552
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-533 |
0e+00 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 711.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 8 MKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEPGATVGILLQEPPLNEEKTVRG 87
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 88 NVEEGLGDIFEKKARFEAIAEEMATnyTDELMEEMGKLQEELDAADAWELDSKIEQAMDALRCPPAD--EPVTHLSGGER 165
Cdd:COG0488 81 TVLDGDAELRALEAELEELEAKLAE--PDEDLERLAELQEEFEALGGWEAEARAEEILSGLGFPEEDldRPVSELSGGWR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 166 RRVALAKlllsepdllllDEPTNHLDAESVLWLEQHLAKYPGAVLAVTHDRYFLDHVAGWICEVDRGKLYPYEGNYSTYL 245
Cdd:COG0488 159 RRVALARallsepdllllDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 246 EKKAERLEVAGKKDAKLQKRLKDELAWV-RSGQKARQAK-NKARLERYEQMVEEAEQYKKLDFeEIQIPTPPRLGNQVVE 323
Cdd:COG0488 239 EQRAERLEQEAAAYAKQQKKIAKEEEFIrRFRAKARKAKqAQSRIKALEKLEREEPPRRDKTV-EIRFPPPERLGKKVLE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 324 VKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQTVQLSYVDQGRENIDPEKTVW 403
Cdd:COG0488 318 LEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEELDPDKTVL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 404 EVVSDGLDyivvGQNEMPSRAYLSAFGFKGADQQKPSKVLSGGERNRLNLALTLKQGGNLILLDEPTNDLDVETLSSLEN 483
Cdd:COG0488 398 DELRDGAP----GGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEE 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 512463837 484 ALQNFPGCAVVISHDRWFLDRTCTHILAwegnFEEGKWFWFEGNFEGYEK 533
Cdd:COG0488 474 ALDDFPGTVLLVSHDRYFLDRVATRILE----FEDGGVREYPGGYDDYLE 519
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
14-529 |
1.40e-134 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 405.10 E-value: 1.40e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 14 AHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGlDQP-SNGEAFLEPGATVGILLQEPPLNEEKTVRGNVEEG 92
Cdd:PRK11147 12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNG-EVLlDDGRIIYEQDLIVARLQQDPPRNVEGTVYDFVAEG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 93 LGDIFEKKARFEAIAEEMATNYTDELMEEMGKLQEELDAADAWELDSKIEQAMDALRCPPaDEPVTHLSGGERRRVALAK 172
Cdd:PRK11147 91 IEEQAEYLKRYHDISHLVETDPSEKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGLDP-DAALSSLSGGWLRKAALGR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 173 LLLSEPDLLLLDEPTNHLDAESVLWLEQHLAKYPGAVLAVTHDRYFLDHVAGWICEVDRGKLYPYEGNYSTYLEKKAERL 252
Cdd:PRK11147 170 ALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQYLLEKEEAL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 253 EVAGKKDAKLQKRLKDELAWVRSGQKARQAKNKARLERYEQM-VEEAEQYKKLDFEEIQIPTPPRLGNQVVEVKDLEKGF 331
Cdd:PRK11147 250 RVEELQNAEFDRKLAQEEVWIRQGIKARRTRNEGRVRALKALrRERSERREVMGTAKMQVEEASRSGKIVFEMENVNYQI 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 332 DGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQTVQLSYVDQGRENIDPEKTVWEVVSDGLD 411
Cdd:PRK11147 330 DGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRAELDPEKTVMDNLAEGKQ 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 412 YIVVGQNEMPSRAYLSAFGFKGADQQKPSKVLSGGERNRLNLALTLKQGGNLILLDEPTNDLDVETLSSLENALQNFPGC 491
Cdd:PRK11147 410 EVMVNGRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGT 489
|
490 500 510
....*....|....*....|....*....|....*...
gi 512463837 492 AVVISHDRWFLDRTCTHILAWEGNfeeGKWFWFEGNFE 529
Cdd:PRK11147 490 VLLVSHDRQFVDNTVTECWIFEGN---GKIGRYVGGYH 524
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
16-531 |
2.34e-71 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 237.87 E-value: 2.34e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 16 GDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEPGATVGILLQEPPLNEEKTVRGNVEEGLGD 95
Cdd:PRK15064 12 GAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFEEFTVLDTVIMGHTE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 96 IFEKKARFEAIaeematnYTD-ELMEEMGKLQEELDAADAwELDSKIEQAMdalrcppADE--------------PVTHL 160
Cdd:PRK15064 92 LWEVKQERDRI-------YALpEMSEEDGMKVADLEVKFA-EMDGYTAEAR-------AGElllgvgipeeqhygLMSEV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 161 SGGERRRVALAKLLLSEPDLLLLDEPTNHLDAESVLWLEQHLAKYPGAVLAVTHDRYFLDHVAGWICEVDRGKLYPYEGN 240
Cdd:PRK15064 157 APGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 241 YSTYLEKKAERLEVAGKKDAKLQKRLKDELAWVR----SGQKARQAKNKARleryeQM----VEE----AEQYKKLDFEE 308
Cdd:PRK15064 237 YDEYMTAATQARERLLADNAKKKAQIAELQSFVSrfsaNASKAKQATSRAK-----QIdkikLEEvkpsSRQNPFIRFEQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 309 IQiptppRLGNQVVEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQTVQLSY 388
Cdd:PRK15064 312 DK-----KLHRNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGY 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 389 VDQGRE-NIDPEKTVWEVVSdglDYIVVGQNEMPSRAYLSAFGFKGADQQKPSKVLSGGERNRLNLALTLKQGGNLILLD 467
Cdd:PRK15064 387 YAQDHAyDFENDLTLFDWMS---QWRQEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMD 463
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 512463837 468 EPTNDLDVETLSSLENALQNFPGCAVVISHDRWFLDRTCTHILawegNFEEGKWFWFEGNFEGY 531
Cdd:PRK15064 464 EPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRII----EITPDGVVDFSGTYEEY 523
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
16-533 |
9.30e-66 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 225.43 E-value: 9.30e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 16 GDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEPGATVGILLQEPPLNE----EKTVRGNVEe 91
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPqpalEYVIDGDRE- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 92 glgdifekkarFEAIAEEMATNYTDELMEEMGKLQEELDAADAWELDSKIEQAMDAL--RCPPADEPVTHLSGGERRRVA 169
Cdd:PRK10636 91 -----------YRQLEAQLHDANERNDGHAIATIHGKLDAIDAWTIRSRAASLLHGLgfSNEQLERPVSDFSGGWRMRLN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 170 LAKLLLSEPDLLLLDEPTNHLDAESVLWLEQHLAKYPGAVLAVTHDRYFLDHVAGWICEVDRGKLYPYEGNYSTYLEKKA 249
Cdd:PRK10636 160 LAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQRA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 250 ERL-------EVAGKKDAKLQKRLKDELAwvrSGQKARQAKNKAR-LERYEqMVEEAEQYKKLDFeeiQIPTPPRLGNQV 321
Cdd:PRK10636 240 TRLaqqqamyESQQERVAHLQSYIDRFRA---KATKAKQAQSRIKmLERME-LIAPAHVDNPFHF---SFRAPESLPNPL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQTVQLSYVDQGR-ENIDPEK 400
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQlEFLRADE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 401 TVWEvvsdGLDYIVVGQNEMPSRAYLSAFGFKGADQQKPSKVLSGGERNRLNLALTLKQGGNLILLDEPTNDLDVETLSS 480
Cdd:PRK10636 393 SPLQ----HLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQA 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 512463837 481 LENALQNFPGCAVVISHDRWFLDRTCTHI-LAWEGNFEEgkwfwFEGNFEGYEK 533
Cdd:PRK10636 469 LTEALIDFEGALVVVSHDRHLLRSTTDDLyLVHDGKVEP-----FDGDLEDYQQ 517
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
324-544 |
1.98e-58 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 202.99 E-value: 1.98e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 324 VKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQTVQLSYVDQgrE-NIDPEKTV 402
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQ--EpPLDDDLTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 403 WEVVSDGLDYIVVGQNEM--------------------------------PSRA--YLSAFGFKGADQQKPSKVLSGGER 448
Cdd:COG0488 79 LDTVLDGDAELRALEAELeeleaklaepdedlerlaelqeefealggweaEARAeeILSGLGFPEEDLDRPVSELSGGWR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 449 NRLNLALTLKQGGNLILLDEPTNDLDVETLSSLENALQNFPGCAVVISHDRWFLDRTCTHIlaWEgnFEEGKWFWFEGNF 528
Cdd:COG0488 159 RRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRI--LE--LDRGKLTLYPGNY 234
|
250
....*....|....*.
gi 512463837 529 EGYEKNKIERYGEEAA 544
Cdd:COG0488 235 SAYLEQRAERLEQEAA 250
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
322-520 |
3.12e-54 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 179.95 E-value: 3.12e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQTVQLSYVDQgrenidpekt 401
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 402 vwevvsdgldyivvgqnempsraylsafgfkgadqqkpskvLSGGERNRLNLALTLKQGGNLILLDEPTNDLDVETLSSL 481
Cdd:cd03221 71 -----------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEAL 109
|
170 180 190
....*....|....*....|....*....|....*....
gi 512463837 482 ENALQNFPGCAVVISHDRWFLDRTCTHILawegNFEEGK 520
Cdd:cd03221 110 EEALKEYPGTVILVSHDRYFLDQVATKII----ELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-247 |
4.67e-48 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 174.87 E-value: 4.67e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 1 MGEFIYQMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEPGATVGILLQEP-PL 79
Cdd:COG0488 311 LGKKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQeEL 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 80 NEEKTVRGNVEEGLGDIFEKKARfeaiaeematnytdELMEEMGklqeeLDAADAWEldskieqamdalrcppadePVTH 159
Cdd:COG0488 391 DPDKTVLDELRDGAPGGTEQEVR--------------GYLGRFL-----FSGDDAFK-------------------PVGV 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 160 LSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAESVLWLEQHLAKYPGAVLAVTHDRYFLDHVAGWICEVDRGKLYPYEG 239
Cdd:COG0488 433 LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPG 512
|
....*...
gi 512463837 240 NYSTYLEK 247
Cdd:COG0488 513 GYDDYLEK 520
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
16-533 |
1.70e-47 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 176.59 E-value: 1.70e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 16 GDKVILD-NVTMAFypGAKIGVVGPNGAGKSSILKIMA--GLDQ-PSNGEAFLEPGATVG--ILLQEPPLNE--EKTVRG 87
Cdd:PLN03073 189 GRDLIVDaSVTLAF--GRHYGLVGRNGTGKTTFLRYMAmhAIDGiPKNCQILHVEQEVVGddTTALQCVLNTdiERTQLL 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 88 NVEEGL----GDIFEKKARFEAIAEEMATNYTDELMEEMGKLQEELDAADAWELDSKIEQAMDALRCPP--ADEPVTHLS 161
Cdd:PLN03073 267 EEEAQLvaqqRELEFETETGKGKGANKDGVDKDAVSQRLEEIYKRLELIDAYTAEARAASILAGLSFTPemQVKATKTFS 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 162 GGERRRVALAKLLLSEPDLLLLDEPTNHLDAESVLWLEQHLAKYPGAVLAVTHDRYFLDHVAGWICEVDRGKLYPYEGNY 241
Cdd:PLN03073 347 GGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKLVTYKGDY 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 242 STYLEKKAERL-------EVAGKKDAKLQKRLkDELAWVRSGQKARQAKNKA--RLERYEQMVEEAEqYKkldFEeiqIP 312
Cdd:PLN03073 427 DTFERTREEQLknqqkafESNERSRSHMQAFI-DKFRYNAKRASLVQSRIKAldRLGHVDAVVNDPD-YK---FE---FP 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 313 TPP-RLGNQVVEVKDLEKGF-DGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQTVQLSYVD 390
Cdd:PLN03073 499 TPDdRPGPPIISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFS 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 391 QgrENIDPektvWEVVSDGLDYIV---VGQNEMPSRAYLSAFGFKGADQQKPSKVLSGGERNRLNLALTLKQGGNLILLD 467
Cdd:PLN03073 579 Q--HHVDG----LDLSSNPLLYMMrcfPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLD 652
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 512463837 468 EPTNDLDVETLSSLENALQNFPGCAVVISHDRWFLDRTCTHIlaWEgnFEEGKWFWFEGNFEGYEK 533
Cdd:PLN03073 653 EPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDEL--WV--VSEGKVTPFHGTFHDYKK 714
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
7-233 |
1.85e-39 |
|
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: 140.66 E-value: 1.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEPGATVGILLQepplneektvr 86
Cdd:cd03221 2 ELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 87 gnveeglgdifekkarfeaiaeematnytdelmeemgklqeeldaadaweldskieqamdalrcppadepvthLSGGERR 166
Cdd:cd03221 71 -------------------------------------------------------------------------LSGGEKM 77
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 512463837 167 RVALAKLLLSEPDLLLLDEPTNHLDAESVLWLEQHLAKYPGAVLAVTHDRYFLDHVAGWICEVDRGK 233
Cdd:cd03221 78 RLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
10-510 |
2.12e-39 |
|
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: 150.44 E-value: 2.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 10 NVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPS---NGEAFLEP-----------GATVGILLQ 75
Cdd:COG1123 11 SVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGrdllelsealrGRRIGMVFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 76 EPP--LNEEkTVRGNVEEGL--GDIFEKKARFEAIaeematnytdELMEEMGklqeeldaadaweldskIEQAMDAlrcP 151
Cdd:COG1123 91 DPMtqLNPV-TVGDQIAEALenLGLSRAEARARVL----------ELLEAVG-----------------LERRLDR---Y 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 152 PADepvthLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAES---VLWLEQHLAKYPG-AVLAVTHDryfLDHVAgwic 227
Cdd:COG1123 140 PHQ-----LSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTqaeILDLLRELQRERGtTVLLITHD---LGVVA---- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 228 evdrgklypyegnystylekkaerlevagkkdaklqkRLKDELAWVRSGQKARQAKNKARLERYEQMveeaEQYKKLDFE 307
Cdd:COG1123 208 -------------------------------------EIADRVVVMDDGRIVEDGPPEEILAAPQAL----AAVPRLGAA 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 308 EIQIPTPPRLGNQVVEVKDLEKGFDGR-----VLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-G 381
Cdd:COG1123 247 RGRAAPAAAAAEPLLEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFdG 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 382 QTV-------------QLSYVDQgreN----IDPEKTVWEVVSDGLD-YIVVGQNEMPSRAY--LSAFGFKGADQQKPSK 441
Cdd:COG1123 327 KDLtklsrrslrelrrRVQMVFQ---DpyssLNPRMTVGDIIAEPLRlHGLLSRAERRERVAelLERVGLPPDLADRYPH 403
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 512463837 442 VLSGGERNRLNLA--LTLKQggNLILLDEPTNDLDVET----LSSLENaLQNFPGCAVV-ISHDRWFLDRTCTHIL 510
Cdd:COG1123 404 ELSGGQRQRVAIAraLALEP--KLLILDEPTSALDVSVqaqiLNLLRD-LQRELGLTYLfISHDLAVVRYIADRVA 476
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
321-510 |
7.12e-36 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 134.45 E-value: 7.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 321 VVEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTV-----QLSYVDQgRE 394
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLfGKPPrrarrRIGYVPQ-RA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 395 NIDPEK--TVWEVVSDGLdYIVVGQNEMPSRAY-------LSAFGFKG-ADQQkpskV--LSGGERNRLNLALTLKQGGN 462
Cdd:COG1121 85 EVDWDFpiTVRDVVLMGR-YGRRGLFRRPSRADreavdeaLERVGLEDlADRP----IgeLSGGQQQRVLLARALAQDPD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 512463837 463 LILLDEPTNDLDVETLSSLENALQNFP--GCAV-VISHDRWFLDRTCTHIL 510
Cdd:COG1121 160 LLLLDEPFAGVDAATEEALYELLRELRreGKTIlVVTHDLGAVREYFDRVL 210
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1-267 |
1.92e-33 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 133.91 E-value: 1.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 1 MGEFIYQMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEafLEPGATVGIllqeppln 80
Cdd:TIGR03719 318 LGDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGT--IEIGETVKL-------- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 81 eektvrGNVEEGLGDIFEKKARFEAIAEEmatnyTDELmeEMGKlqeeldaadaWELDSKIEQAMDALRCPPADEPVTHL 160
Cdd:TIGR03719 388 ------AYVDQSRDALDPNKTVWEEISGG-----LDII--KLGK----------REIPSRAYVGRFNFKGSDQQKKVGQL 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 161 SGGERRRVALAKLLLSEPDLLLLDEPTNHLDAESVLWLEQHLAKYPGAVLAVTHDRYFLDHVAGWIC--EVDrGKLYPYE 238
Cdd:TIGR03719 445 SGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILafEGD-SHVEWFE 523
|
250 260
....*....|....*....|....*....
gi 512463837 239 GNYSTYLEKKAERLevagKKDAKLQKRLK 267
Cdd:TIGR03719 524 GNFSEYEEDKKRRL----GEDADQPHRIK 548
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
323-510 |
3.22e-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: 3.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 323 EVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTVQLS-----YVDQgRENI 396
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfGKPLEKErkrigYVPQ-RRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 397 DPEK--TVWEVVSDGLdYIVVGQNEMPSRAY------------LSAFgfkgADQQKPSkvLSGGERNRLNLALTLKQGGN 462
Cdd:cd03235 80 DRDFpiSVRDVVLMGL-YGHKGLFRRLSKADkakvdealervgLSEL----ADRQIGE--LSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 512463837 463 LILLDEPTNDLDVET---LSSLENALQNfPGCAV-VISHDRWFLDRTCTHIL 510
Cdd:cd03235 153 LLLLDEPFAGVDPKTqedIYELLRELRR-EGMTIlVVTHDLGLVLEYFDRVL 203
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
321-511 |
5.32e-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: 126.70 E-value: 5.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 321 VVEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTV----------QLSYV 389
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLdGRDLaslsrrelarRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 390 DQgrENIDPEK-TVWEVVSDGLdyivvgqnempsRAYLSAFG-FKGADQQKPSKV----------------LSGGERNRL 451
Cdd:COG1120 81 PQ--EPPAPFGlTVRELVALGR------------YPHLGLFGrPSAEDREAVEEAlertglehladrpvdeLSGGERQRV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 512463837 452 NLALTLKQGGNLILLDEPTNDLD----VETLSSLEnALQNFPGCAVVIS-HDrwfLD---RTCTHILA 511
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLDlahqLEVLELLR-RLARERGRTVVMVlHD---LNlaaRYADRLVL 210
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
323-514 |
1.01e-32 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 124.54 E-value: 1.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 323 EVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTV----------QLSYVDQ 391
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLdGKPLsampppewrrQVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 392 grenidpEKTVW-EVVSDGLDYIVVGQNEMPSR----AYLSAFGFKGADQQKPSKVLSGGERNRLNLALTLKQGGNLILL 466
Cdd:COG4619 82 -------EPALWgGTVRDNLPFPFQLRERKFDReralELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 512463837 467 DEPTNDLDVETLSSLENALQNFP----GCAVVISHDRWFLDRTCTHILAWEG 514
Cdd:COG4619 155 DEPTSALDPENTRRVEELLREYLaeegRAVLWVSHDPEQIERVADRVLTLEA 206
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
322-510 |
7.35e-32 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 122.86 E-value: 7.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTV---------QLSYVDQ 391
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVlGEDVardpaevrrRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 392 GReNIDPEKTVWEVvsdgLDYIV----VGQNEMPSRA--YLSAFGFKGAdQQKPSKVLSGGERNRLNLALTLKQGGNLIL 465
Cdd:COG1131 81 EP-ALYPDLTVREN----LRFFArlygLPRKEARERIdeLLELFGLTDA-ADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 512463837 466 LDEPTNDLDVETLSSLENALQNF--PGCAVVIS-HDRWFLDRTCTHIL 510
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELaaEGKTVLLStHYLEEAERLCDRVA 202
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
322-510 |
1.88e-31 |
|
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: 119.81 E-value: 1.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTV---------QLSYVDQ 391
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVlGKDIkkepeevkrRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 392 GRENIdPEKTVWEVVSdgldyivvgqnempsraylsafgfkgadqqkpskvLSGGERNRLNLALTLKQGGNLILLDEPTN 471
Cdd:cd03230 81 EPSLY-ENLTVRENLK-----------------------------------LSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 512463837 472 DLDVETLSSLENALQNFP--GCAVVI-SHDRWFLDRTCTHIL 510
Cdd:cd03230 125 GLDPESRREFWELLRELKkeGKTILLsSHILEEAERLCDRVA 166
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
337-471 |
2.06e-30 |
|
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: 116.21 E-value: 2.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 337 IKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTV----------QLSYVDQGrENIDPEKTVWEV 405
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLdGQDLtdderkslrkEIGYVFQD-PQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 512463837 406 VSDGLDYIVVGQNEMPSRAY--LSAFGFKGADQQKPS---KVLSGGERNRLNLALTLKQGGNLILLDEPTN 471
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARAEeaLEKLGLGDLADRPVGerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
321-498 |
7.01e-30 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 116.42 E-value: 7.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 321 VVEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQTVQLSYVDQGRENI---- 396
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLaylg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 397 -----DPEKTVWEVvsdgLDYIVVGQNEMPSRAY----LSAFGFKGAdQQKPSKVLSGGERNRLNLALTLKQGGNLILLD 467
Cdd:COG4133 82 hadglKPELTVREN----LRFWAALYGLRADREAideaLEAVGLAGL-ADLPVRQLSAGQKRRVALARLLLSPAPLWLLD 156
|
170 180 190
....*....|....*....|....*....|....
gi 512463837 468 EPTNDLDVETLSSLENALQNFP---GCAVVISHD 498
Cdd:COG4133 157 EPFTALDAAGVALLAELIAAHLargGAVLLTTHQ 190
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
323-511 |
7.56e-30 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 115.61 E-value: 7.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 323 EVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTV----------QLSYVDQ 391
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLdGKDLaslspkelarKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 392 GRENIDpektvwevvsdgldyivvgqnempsrayLSAFGFKGADQqkpskvLSGGERNRLNLALTLKQGGNLILLDEPTN 471
Cdd:cd03214 81 ALELLG----------------------------LAHLADRPFNE------LSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 512463837 472 DLD----VETLSSLENALQNFPGCAVVISHDRWFLDRTCTHILA 511
Cdd:cd03214 127 HLDiahqIELLELLRRLARERGKTVVMVLHDLNLAARYADRVIL 170
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
323-510 |
9.77e-30 |
|
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: 114.26 E-value: 9.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 323 EVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTVQLSYVDQGRENIdpekt 401
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIdGKDIAKLPLEELRRRI----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 402 vwevvsdgldyIVVGQnempsraylsafgfkgadqqkpskvLSGGERNRLNLALTLKQGGNLILLDEPTNDLDVETLSSL 481
Cdd:cd00267 76 -----------GYVPQ-------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERL 119
|
170 180 190
....*....|....*....|....*....|..
gi 512463837 482 ENALQNF--PGCAVV-ISHDRWFLDRTCTHIL 510
Cdd:cd00267 120 LELLRELaeEGRTVIiVTHDPELAELAADRVI 151
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
323-520 |
2.42e-29 |
|
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: 115.26 E-value: 2.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 323 EVKDLEKGFDG--RVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTVQLSYVDQGRENI--- 396
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVdGKDLTKLSLKELRRKVglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 397 --DPE-----KTVWEVVSDGLDYIVVGQNEMPSRA--YLSAFGFKGADQQKPSKvLSGGERNRLNLALTLKQGGNLILLD 467
Cdd:cd03225 81 fqNPDdqffgPTVEEEVAFGLENLGLPEEEIEERVeeALELVGLEGLRDRSPFT-LSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 512463837 468 EPTNDLDVETLSSLENALQNFPG---CAVVISHDRWFLDRTCTHILawegNFEEGK 520
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVI----VLEDGK 211
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
7-234 |
2.69e-29 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 114.91 E-value: 2.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLE-------PGAT----VGILLQ 75
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDgkplsamPPPEwrrqVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 76 EPPLNEEkTVRGNVEEGLgDIFEKKARFEAIaeematnytDELMEEMGkLQEELdaadaweLDSkieqamdalrcppade 155
Cdd:COG4619 82 EPALWGG-TVRDNLPFPF-QLRERKFDRERA---------LELLERLG-LPPDI-------LDK---------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 156 PVTHLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAESVLWLEQHLAKYP----GAVLAVTHDRYFLDHVAGWICEVDR 231
Cdd:COG4619 127 PVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLaeegRAVLWVSHDPEQIERVADRVLTLEA 206
|
...
gi 512463837 232 GKL 234
Cdd:COG4619 207 GRL 209
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
9-222 |
4.38e-29 |
|
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: 114.11 E-value: 4.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 9 KNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFL----------EPGATVGILLQEPP 78
Cdd:COG4133 6 ENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWngepirdareDYRRRLAYLGHADG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 79 LNEEKTVRGNVeeglgdifekkaRFEAiaeematnytdelmeemgKLQEELDAADAweldskIEQAMDALRCPP-ADEPV 157
Cdd:COG4133 86 LKPELTVRENL------------RFWA------------------ALYGLRADREA------IDEALEAVGLAGlADLPV 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 512463837 158 THLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAESVLWLEQHLAKYP---GAVLAVTHDRYFLDHV 222
Cdd:COG4133 130 RQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLargGAVLLTTHQPLELAAA 197
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
7-223 |
4.73e-29 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 115.53 E-value: 4.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEpGA------------TVGILL 74
Cdd:COG1120 3 EAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLD-GRdlaslsrrelarRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 75 QEPPLNEEKTVRgnveeglgdifekkarfEAIAeematnytdelmeeMG-----KLQEELDAADawelDSKIEQAMDALR 149
Cdd:COG1120 82 QEPPAPFGLTVR-----------------ELVA--------------LGryphlGLFGRPSAED----REAVEEALERTG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 150 CPP-ADEPVTHLSGGERRRVALAKlllsepdllllDEPTNHLD---AESVLWLEQHLAKYPG-AVLAVTHD-----RYFl 219
Cdd:COG1120 127 LEHlADRPVDELSGGERQRVLIARalaqeppllllDEPTSHLDlahQLEVLELLRRLARERGrTVVMVLHDlnlaaRYA- 205
|
....
gi 512463837 220 DHVA 223
Cdd:COG1120 206 DRLV 209
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
323-510 |
9.96e-29 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 114.18 E-value: 9.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 323 EVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTV---------QLSYVDQ- 391
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIdGEDVrkeprearrQIGVLPDe 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 392 --------GRENIDPEKTVWEVVSDGLDYIVvgqnempsRAYLSAFGFkGADQQKPSKVLSGGERNRLNLALTLKQGGNL 463
Cdd:COG4555 83 rglydrltVRENIRYFAELYGLFDEELKKRI--------EELIELLGL-EEFLDRRVGELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 512463837 464 ILLDEPTNDLDVETLSSLENALQNF--PGCAVVIS-HDRWFLDRTCTHIL 510
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRALkkEGKTVLFSsHIMQEVEALCDRVV 203
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
322-520 |
2.87e-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: 112.81 E-value: 2.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDLEKGF-DGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTVQLSYVDQGRENI--- 396
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVdGKDITKKNLRELRRKVglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 397 --DPE-----KTVWEVVSDGLDYIVVGQNEMPSRA--YLSAFGFKGADQQKPSKvLSGGERNRLNLALTLKQGGNLILLD 467
Cdd:COG1122 81 fqNPDdqlfaPTVEEDVAFGPENLGLPREEIRERVeeALELVGLEHLADRPPHE-LSGGQKQRVAIAGVLAMEPEVLVLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 512463837 468 EPTNDLDVETLSSLENALQNFP--GCAVV-ISHDRWFLDRTCTHILAwegnFEEGK 520
Cdd:COG1122 160 EPTAGLDPRGRRELLELLKRLNkeGKTVIiVTHDLDLVAELADRVIV----LDDGR 211
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
321-518 |
1.17e-27 |
|
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: 111.22 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 321 VVEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTV-------------QL 386
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVdGQDItglsekelyelrrRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 387 SYVDQG---------RENI---------DPEKTVWEVVsdgldyivvgqnempsRAYLSAFGFKGADQQKPSKvLSGGER 448
Cdd:COG1127 85 GMLFQGgalfdsltvFENVafplrehtdLSEAEIRELV----------------LEKLELVGLPGAADKMPSE-LSGGMR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 449 NRLNLA--LTLKQggNLILLDEPTNDLDVETLSSLEN---ALQ-NFPGCAVVISHDRWFLDRTCTHI-------LAWEGN 515
Cdd:COG1127 148 KRVALAraLALDP--EILLYDEPTAGLDPITSAVIDElirELRdELGLTSVVVTHDLDSAFAIADRVavladgkIIAEGT 225
|
...
gi 512463837 516 FEE 518
Cdd:COG1127 226 PEE 228
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
322-518 |
3.48e-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: 109.90 E-value: 3.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTV-------------QLS 387
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIdGEDIsglseaelyrlrrRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 388 YVDQG---------RENI---------DPEKTVWEVVSDGLDyivvgqnempsraylsAFGFKGADQQKPSKvLSGGERN 449
Cdd:cd03261 81 MLFQSgalfdsltvFENVafplrehtrLSEEEIREIVLEKLE----------------AVGLRGAEDLYPAE-LSGGMKK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 450 RLNLALTLKQGGNLILLDEPTNDLD-------VETLSSLENALQNfpgCAVVISHDRWFLDRTCTHI-------LAWEGN 515
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLDpiasgviDDLIRSLKKELGL---TSIMVTHDLDTAFAIADRIavlydgkIVAEGT 220
|
...
gi 512463837 516 FEE 518
Cdd:cd03261 221 PEE 223
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
322-499 |
9.72e-26 |
|
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: 104.91 E-value: 9.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTVQ--------LSYVDQG 392
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIdGRDVTgvpperrnIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 393 RENIdPEKTVWEVVSDGLDYIVVGQNEMPSRAYLSA--FGFKGADQQKPSKvLSGGERNRLNLALTLKQGGNLILLDEPT 470
Cdd:cd03259 81 YALF-PHLTVAENIAFGLKLRGVPKAEIRARVRELLelVGLEGLLNRYPHE-LSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190
....*....|....*....|....*....|...
gi 512463837 471 NDLDVETLSSLEN---ALQNFPGC-AVVISHDR 499
Cdd:cd03259 159 SALDAKLREELREelkELQRELGItTIYVTHDQ 191
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
323-510 |
1.48e-25 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 104.26 E-value: 1.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 323 EVKDLEKGF-DGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVG--------QTVQLSYVDQGR 393
Cdd:cd03226 1 RIENISFSYkKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNgkpikakeRRKSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 394 ENIDPEKTVWEVVSDGLDYIVVGQNEmpSRAYLSAFGFKGADQQKPsKVLSGGERNRLNLALTLKQGGNLILLDEPTNDL 473
Cdd:cd03226 81 DYQLFTDSVREELLLGLKELDAGNEQ--AETVLKDLDLYALKERHP-LSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 512463837 474 DVETLSSLENA---LQNFPGCAVVISHDRWFLDRTCTHIL 510
Cdd:cd03226 158 DYKNMERVGELireLAAQGKAVIVITHDYEFLAKVCDRVL 197
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
9-234 |
1.56e-25 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 105.15 E-value: 1.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 9 KNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFL----------EPGATVGILLQEPP 78
Cdd:COG1131 4 RGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVlgedvardpaEVRRRIGYVPQEPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 79 LNEEKTVRGNVEeglgdIFekkARFEAIAEEMATNYTDELMEEMGklqeeLDAAdaweldskieqamdalrcppADEPVT 158
Cdd:COG1131 84 LYPDLTVRENLR-----FF---ARLYGLPRKEARERIDELLELFG-----LTDA--------------------ADRKVG 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 512463837 159 HLSGGERRRVALAKlllsepdllllDEPTNHLDAESVLWLEQH---LAKYPGAVLAVTHDRYFLDHVAGWICEVDRGKL 234
Cdd:COG1131 131 TLSGGMKQRLGLALallhdpellilDEPTSGLDPEARRELWELlreLAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRI 209
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-223 |
8.09e-25 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 101.36 E-value: 8.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEaflepgatvgILLQEPPLNEEKtvr 86
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGE----------ILLDGKDLASLS--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 87 gnveeglgdifekkarFEAIAEEMATnytdelmeemgklqeeldaadaweldskIEQAMDALRCPP-ADEPVTHLSGGER 165
Cdd:cd03214 68 ----------------PKELARKIAY----------------------------VPQALELLGLAHlADRPFNELSGGER 103
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 512463837 166 RRVALAKLLLSEPDLLLLDEPTNHLD---AESVLWLEQHLAKYPG-AVLAVTHDryfLDHVA 223
Cdd:cd03214 104 QRVLLARALAQEPPILLLDEPTSHLDiahQIELLELLRRLARERGkTVVMVLHD---LNLAA 162
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
322-520 |
8.58e-25 |
|
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: 101.11 E-value: 8.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTVQlsyvdQGRENIDPEK 400
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIdGEDLT-----DLEDELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 401 TVWEVvsdgldyiVVGQNEMPSRayLSAFgfkgadqQKPSKVLSGGERNRLNLALTLKQGGNLILLDEPTNDLDVETLSS 480
Cdd:cd03229 76 RRIGM--------VFQDFALFPH--LTVL-------ENIALGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRRE 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 512463837 481 LE---NALQNFPGCAVV-ISHDRWFLDRTCTHILAwegnFEEGK 520
Cdd:cd03229 139 VRallKSLQAQLGITVVlVTHDLDEAARLADRVVV----LRDGK 178
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-503 |
1.06e-24 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 107.97 E-value: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 30 PGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEaflepgatvgilLQEPPLNEE--KTVRGNVeegLGDIFEKKARFEaIA 107
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGD------------YEEEPSWDEvlKRFRGTE---LQNYFKKLYNGE-IK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 108 EEMATNYTDELMEEM-GKLQEELDAAD-AWELDSKIEQ-AMDALRcppaDEPVTHLSGGERRRVALAKLLLSEPDLLLLD 184
Cdd:PRK13409 162 VVHKPQYVDLIPKVFkGKVRELLKKVDeRGKLDEVVERlGLENIL----DRDISELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 185 EPTNHLDAE---SVLWLEQHLA--KYpgaVLAVTHDRYFLDHVAGWIcEVdrgkLYPYEGNYSTYLEKKAERLEVagkkD 259
Cdd:PRK13409 238 EPTSYLDIRqrlNVARLIRELAegKY---VLVVEHDLAVLDYLADNV-HI----AYGEPGAYGVVSKPKGVRVGI----N 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 260 AKLQKRLKDELAWVRSgqkarqaknkarleryeqmveeaeqyKKLDFEEiqipTPPR---LGNQVVEVKDLEKGFDGRVL 336
Cdd:PRK13409 306 EYLKGYLPEENMRIRP--------------------------EPIEFEE----RPPRdesERETLVEYPDLTKKLGDFSL 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 337 IKDlSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKvgQTVQLSYVDQgRENIDPEKTVWEV---VSDGLD-- 411
Cdd:PRK13409 356 EVE-GGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD--PELKISYKPQ-YIKPDYDGTVEDLlrsITDDLGss 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 412 YIvvgQNEMPSRAYLSAFgfkgadQQKPSKVLSGGERNRLNLALTLKQGGNLILLDEPTNDLDVE----TLSSLENALQN 487
Cdd:PRK13409 432 YY---KSEIIKPLQLERL------LDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlaVAKAIRRIAEE 502
|
490
....*....|....*.
gi 512463837 488 FPGCAVVISHDRWFLD 503
Cdd:PRK13409 503 REATALVVDHDIYMID 518
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
313-518 |
1.24e-24 |
|
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: 107.92 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 313 TPPRLGNQVVEVKDLEKGF-DGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQTV------- 384
Cdd:COG4988 328 PLPAAGPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDlsdldpa 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 385 ----QLSYVDQ------G--RENI---DPEKT------------VWEVVS---DGLDYIVvGQNempsraylsAFGfkga 434
Cdd:COG4988 408 swrrQIAWVPQnpylfaGtiRENLrlgRPDASdeeleaaleaagLDEFVAalpDGLDTPL-GEG---------GRG---- 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 435 dqqkpskvLSGGERNRLNLALTLKQGGNLILLDEPTNDLDVETLSSLENALQN-FPGCAV-VISH--------DR-WFLD 503
Cdd:COG4988 474 --------LSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRlAKGRTViLITHrlallaqaDRiLVLD 545
|
250
....*....|....*
gi 512463837 504 RtctHILAWEGNFEE 518
Cdd:COG4988 546 D---GRIVEQGTHEE 557
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
322-497 |
2.50e-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: 99.76 E-value: 2.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDLEKGFDGR--VLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQtVQLSYVDQG--RENId 397
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDG-VDLRDLDLEslRKNI- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 398 pektvwevvsdgldyIVVGQNempsrAYLsafgFKG--ADQqkpskVLSGGERNRLNLALTLKQGGNLILLDEPTNDLDV 475
Cdd:cd03228 79 ---------------AYVPQD-----PFL----FSGtiREN-----ILSGGQRQRIAIARALLRDPPILILDEATSALDP 129
|
170 180
....*....|....*....|....
gi 512463837 476 ETLSSLENALQNFPGC--AVVISH 497
Cdd:cd03228 130 ETEALILEALRALAKGktVIVIAH 153
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-503 |
2.75e-24 |
|
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: 106.79 E-value: 2.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 30 PGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEaflepgatvgilLQEPPLNEE--KTVRGNveeGLGDIFEKkarfeaIA 107
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGD------------YDEEPSWDEvlKRFRGT---ELQDYFKK------LA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 108 EE-----MATNYTDELMEEM-GKLQEELDAADawE---LDSKIEQ-AMDALRcppaDEPVTHLSGGERRRVALAKLLLSE 177
Cdd:COG1245 157 NGeikvaHKPQYVDLIPKVFkGTVRELLEKVD--ErgkLDELAEKlGLENIL----DRDISELSGGELQRVAIAAALLRD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 178 PDLLLLDEPTNHLD-------AESVlwleQHLAKYPGAVLAVTHDRYFLDHVAGWIcEVdrgkLYPYEGNYSTylekkae 250
Cdd:COG1245 231 ADFYFFDEPSSYLDiyqrlnvARLI----RELAEEGKYVLVVEHDLAILDYLADYV-HI----LYGEPGVYGV------- 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 251 rleVAGKKDAK------LQKRLKDELAWVRSgqkarqaknkarleryeqmveeaeqyKKLDFEEIQiPTPPRLGNQVVEV 324
Cdd:COG1245 295 ---VSKPKSVRvginqyLDGYLPEENVRIRD--------------------------EPIEFEVHA-PRREKEEETLVEY 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 325 KDLEKGFDGRVLIKDlSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVgqTVQLSYVDQgRENIDPEKTVWE 404
Cdd:COG1245 345 PDLTKSYGGFSLEVE-GGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDE--DLKISYKPQ-YISPDYDGTVEE 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 405 VVSDgldyivVGQNEMPSRAYLSAFGFK-GADQ--QKPSKVLSGGERNRLNLALTLKQGGNLILLDEPTNDLDVETLSSL 481
Cdd:COG1245 421 FLRS------ANTDDFGSSYYKTEIIKPlGLEKllDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAV 494
|
490 500
....*....|....*....|....*.
gi 512463837 482 ENALQNF----PGCAVVISHDRWFLD 503
Cdd:COG1245 495 AKAIRRFaenrGKTAMVVDHDIYLID 520
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
322-509 |
2.91e-24 |
|
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: 101.04 E-value: 2.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDLEK--GFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQTVQLSYVDQGRENI--- 396
Cdd:cd03263 1 LQIRNLTKtyKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLgyc 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 397 ------DPEKTVWEVV--SDGLDYIVVGQNEMPSRAYLSAFGFKgADQQKPSKVLSGGERNRLNLALTLKQGGNLILLDE 468
Cdd:cd03263 81 pqfdalFDELTVREHLrfYARLKGLPKSEIKEEVELLLRVLGLT-DKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 512463837 469 PTNDLDVETLSSLENALQNF-PGCAVVI-SHDRWFLDRTCTHI 509
Cdd:cd03263 160 PTSGLDPASRRAIWDLILEVrKGRSIILtTHSMDEAEALCDRI 202
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-233 |
3.89e-24 |
|
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: 100.23 E-value: 3.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAHGD--KVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFL-----------EPGATVGIL 73
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVdgkdltklslkELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 74 LQEPplnE----EKTVRGNVEEGLgdifekkaRFEAIAEEMATNYTDELMEEMGklqeeldaadaweldskieqaMDALR 149
Cdd:cd03225 81 FQNP---DdqffGPTVEEEVAFGL--------ENLGLPEEEIEERVEEALELVG---------------------LEGLR 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 150 cppaDEPVTHLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAESVLWLEQHLAKYPGA---VLAVTHDRYFLDHVAGWI 226
Cdd:cd03225 129 ----DRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEgktIIIVTHDLDLLLELADRV 204
|
....*..
gi 512463837 227 CEVDRGK 233
Cdd:cd03225 205 IVLEDGK 211
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
334-551 |
4.40e-24 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 106.41 E-value: 4.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 334 RVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQTVQLSYVDQgrENIDPEKTVWEVVSDG---- 409
Cdd:PRK10636 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQ--ETPALPQPALEYVIDGdrey 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 410 --LDYIVVGQNE---------------------MPSRA--YLSAFGFKGADQQKPSKVLSGGERNRLNLALTLKQGGNLI 464
Cdd:PRK10636 92 rqLEAQLHDANErndghaiatihgkldaidawtIRSRAasLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 465 LLDEPTNDLDVETLSSLENALQNFPGCAVVISHDRWFLDRTCTHILawegNFEEGKWFWFEGNFEGYEKNKIERYGEEAA 544
Cdd:PRK10636 172 LLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKII----HIEQQSLFEYTGNYSSFEVQRATRLAQQQA 247
|
250
....*....|.
gi 512463837 545 ----RPSRVTH 551
Cdd:PRK10636 248 myesQQERVAH 258
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
2-300 |
5.46e-24 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 106.19 E-value: 5.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 2 GEFIYQMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEaflepgATVGILLQ------ 75
Cdd:PRK11147 316 GKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGR------IHCGTKLEvayfdq 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 76 -EPPLNEEKTVRGNVEEGlgdifeKKarfeaiaeEMATNYTDELMeeMGKLQEELdaadaweldskieqamdalrCPP-- 152
Cdd:PRK11147 390 hRAELDPEKTVMDNLAEG------KQ--------EVMVNGRPRHV--LGYLQDFL--------------------FHPkr 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 153 ADEPVTHLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAESVLWLEQHLAKYPGAVLAVTHDRYFLDHVA--GWICEVD 230
Cdd:PRK11147 434 AMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVteCWIFEGN 513
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 231 rGKLYPYEGNYSTYLEKKAERLEVAGKKDAKLQKRLKDELAWVRSGQKARQAKNKARLERYEQMVEEAEQ 300
Cdd:PRK11147 514 -GKIGRYVGGYHDARQQQAQYLALKQPAVKKKEEAAAPKAETVKRSSKKLSYKLQRELEQLPQLLEDLEA 582
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-188 |
9.07e-24 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 97.33 E-value: 9.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 21 LDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLE-----------PGATVGILLQEPPLNEEKTVRGNV 89
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDgqdltdderksLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 90 EEGLGDIFEKKARFEAIAEEmatnytdeLMEEMGklqeeldaadaweldskieqaMDALRCPPADEPVTHLSGGERRRVA 169
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEE--------ALEKLG---------------------LGDLADRPVGERPGTLSGGQRQRVA 131
|
170
....*....|....*....
gi 512463837 170 LAKLLLSEPDLLLLDEPTN 188
Cdd:pfam00005 132 IARALLTKPKLLLLDEPTA 150
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
285-498 |
1.61e-23 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 104.92 E-value: 1.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 285 KARLERYEQMVE-EAEQykklDFEEIQIPTPPRLGNqvVEVKDLEKGFDGRV--LIKDLSFTLPRNGIVGVIGPNGVGKS 361
Cdd:COG2274 442 KIALERLDDILDlPPER----EEGRSKLSLPRLKGD--IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKS 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 362 TLFKTIVGLEQPDSGEVKV-GQTV----------QLSYVDQG--------RENI---DPEKT---VWEVVSD-GL-DYIv 414
Cdd:COG2274 516 TLLKLLLGLYEPTSGRILIdGIDLrqidpaslrrQIGVVLQDvflfsgtiRENItlgDPDATdeeIIEAARLaGLhDFI- 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 415 vgqNEMPSRaYLSAFGFKGADqqkpskvLSGGERNRLNLALTLKQGGNLILLDEPTNDLDVETLSSLENALQN-FPGCA- 492
Cdd:COG2274 595 ---EALPMG-YDTVVGEGGSN-------LSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRlLKGRTv 663
|
....*.
gi 512463837 493 VVISHD 498
Cdd:COG2274 664 IIIAHR 669
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-506 |
1.75e-23 |
|
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: 104.11 E-value: 1.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQ--PSNGE-----------AFLEPGATVG-- 71
Cdd:TIGR03269 2 EVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRiiyhvalcekcGYVERPSKVGep 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 72 -------ILLQEPPL-NEEKTVRGNVEEGLGDIFEKKarFEAIAEEMATNYTDELMEEMGklqeeldaadaWELDSKIEQ 143
Cdd:TIGR03269 82 cpvcggtLEPEEVDFwNLSDKLRRRIRKRIAIMLQRT--FALYGDDTVLDNVLEALEEIG-----------YEGKEAVGR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 144 AMDALRCPPADEPVTH----LSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAESVLWLEQHL---AKYPGAVLAVThdr 216
Cdd:TIGR03269 149 AVDLIEMVQLSHRITHiardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALeeaVKASGISMVLT--- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 217 yfldhvagwicevdrgklypyeGNYSTYLEKkaerlevagkkdaklqkrLKDELAWVRSGQKARQAKNKARLERYEQMVE 296
Cdd:TIGR03269 226 ----------------------SHWPEVIED------------------LSDKAIWLENGEIKEEGTPDEVVAVFMEGVS 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 297 EAEQykkldFEEIQIptpprlGNQVVEVKDLEKGFDG--RVLIK---DLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLE 371
Cdd:TIGR03269 266 EVEK-----ECEVEV------GEPIIKVRNVSKRYISvdRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVL 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 372 QPDSGEVKVgqTVQLSYVDQGRENID-------------------PEKTVWEVVSD--GLDYivvgQNEMPSRAYLSAFG 430
Cdd:TIGR03269 335 EPTSGEVNV--RVGDEWVDMTKPGPDgrgrakryigilhqeydlyPHRTVLDNLTEaiGLEL----PDELARMKAVITLK 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 431 FKGADQQKPSKVL-------SGGERNRLNLALTLKQGGNLILLDEPTNDLD----VETLSSLENALQNFPGCAVVISHDR 499
Cdd:TIGR03269 409 MVGFDEEKAEEILdkypdelSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkVDVTHSILKAREEMEQTFIIVSHDM 488
|
....*..
gi 512463837 500 WFLDRTC 506
Cdd:TIGR03269 489 DFVLDVC 495
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
322-487 |
2.26e-23 |
|
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: 98.31 E-value: 2.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDLEKGFDGR----VLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV------GQTVQLSYVDQ 391
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVdgepvtGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 392 gRENIDPEKTVWEVVSDGLDYIVVGQNEMPSRA--YLSAFGFKGADQQKPSKvLSGGERNRLNLALTLKQGGNLILLDEP 469
Cdd:cd03293 81 -QDALLPWLTVLDNVALGLELQGVPKAEARERAeeLLELVGLSGFENAYPHQ-LSGGMRQRVALARALAVDPDVLLLDEP 158
|
170
....*....|....*...
gi 512463837 470 TNDLDVETLSSLENALQN 487
Cdd:cd03293 159 FSALDALTREQLQEELLD 176
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
7-215 |
5.39e-23 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 98.24 E-value: 5.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKA----HGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFL------EPGATVGILLQE 76
Cdd:COG1116 9 ELRGVSKRfptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVdgkpvtGPGPDRGVVFQE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 77 PPLNEEKTVRGNVEEGLGDIFEKKARFEAIAeematnytDELMEEMGkLQeelDAADAWeldskieqamdalrcpPADep 156
Cdd:COG1116 89 PALLPWLTVLDNVALGLELRGVPKAERRERA--------RELLELVG-LA---GFEDAY----------------PHQ-- 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 512463837 157 vthLSGGERRRVALAklllsepdllllDEPTNHLDAESVL----WLEQHLAKYPGAVLAVTHD 215
Cdd:COG1116 139 ---LSGGMRQRVAIAralandpevllmDEPFGALDALTRErlqdELLRLWQETGKTVLFVTHD 198
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
15-234 |
6.90e-23 |
|
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: 97.40 E-value: 6.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 15 HGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEpG------------ATVGILLQEPplnE- 81
Cdd:COG1122 11 PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVD-GkditkknlrelrRKVGLVFQNP---Dd 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 82 ---EKTVRGNVEEGLgdifekkarfeaiaeematnytdelmEEMGklqeeLDAAdawELDSKIEQAMDALRCPP-ADEPV 157
Cdd:COG1122 87 qlfAPTVEEDVAFGP--------------------------ENLG-----LPRE---EIRERVEEALELVGLEHlADRPP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 158 THLSGGERRRVALAklllsepdllllDEPTNHLDAESVLWLEQHLAKYPGA---VLAVTHDRYFLDHVAGWICEVDRGKL 234
Cdd:COG1122 133 HELSGGQKQRVAIAgvlamepevlvlDEPTAGLDPRGRRELLELLKRLNKEgktVIIVTHDLDLVAELADRVIVLDDGRI 212
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
321-498 |
9.49e-23 |
|
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: 96.81 E-value: 9.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 321 VVEVKDLEKGFDGR----VLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTV----------- 384
Cdd:cd03257 1 LLEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFdGKDLlklsrrlrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 385 --QLSYVDQG-RENIDPEKTVWEVVSDGL--DYIVVGQNEMPSRAYLSAFGFKGADQ---QKPSKvLSGGERNRLNLALT 456
Cdd:cd03257 81 rkEIQMVFQDpMSSLNPRMTIGEQIAEPLriHGKLSKKEARKEAVLLLLVGVGLPEEvlnRYPHE-LSGGQRQRVAIARA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 512463837 457 LKQGGNLILLDEPTNDLDV----ETLSSLENaLQNFPGCAVV-ISHD 498
Cdd:cd03257 160 LALNPKLLIADEPTSALDVsvqaQILDLLKK-LQEELGLTLLfITHD 205
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
7-215 |
1.42e-22 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 96.00 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAHGDK----VILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPS------NGEAFLEPGATVGILLQE 76
Cdd:cd03293 2 EVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTsgevlvDGEPVTGPGPDRGYVFQQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 77 PPLNEEKTVRGNVEEGLgdifekKARFEAIAEEMAtnYTDELMEEMGkLQeelDAADAWeldskieqamdalrcpPADep 156
Cdd:cd03293 82 DALLPWLTVLDNVALGL------ELQGVPKAEARE--RAEELLELVG-LS---GFENAY----------------PHQ-- 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 512463837 157 vthLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAESVL----WLEQHLAKYPGAVLAVTHD 215
Cdd:cd03293 132 ---LSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREqlqeELLDIWRETGKTVLLVTHD 191
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
322-509 |
1.78e-22 |
|
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: 95.36 E-value: 1.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQtvqlsyvdqgrENIDPEKT 401
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDG-----------KSYQKNIE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 402 VWEVVSDGLDY-IVVGqnEMPSRAYLSAF------------------GFKGADQQKpSKVLSGGERNRLNLALTLKQGGN 462
Cdd:cd03268 70 ALRRIGALIEApGFYP--NLTARENLRLLarllgirkkridevldvvGLKDSAKKK-VKGFSLGMKQRLGIALALLGNPD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 512463837 463 LILLDEPTNDLDVETLSSLENALQNFP--GCAVVI-SHDRWFLDRTCTHI 509
Cdd:cd03268 147 LLILDEPTNGLDPDGIKELRELILSLRdqGITVLIsSHLLSEIQKVADRI 196
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
330-498 |
2.28e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 94.61 E-value: 2.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 330 GFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQTVQLSYVDQGRENID--PeKTVWEVVS 407
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDslP-LTVRDLVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 408 DGL-------------DYIVVgqnempSRAyLSAFGFKG-ADQQKPSkvLSGGERNRLNLALTLKQGGNLILLDEPTNDL 473
Cdd:NF040873 80 MGRwarrglwrrltrdDRAAV------DDA-LERVGLADlAGRQLGE--LSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180
....*....|....*....|....*...
gi 512463837 474 DVETLSSLENALQNF--PGCAVV-ISHD 498
Cdd:NF040873 151 DAESRERIIALLAEEhaRGATVVvVTHD 178
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
7-250 |
3.33e-22 |
|
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: 95.69 E-value: 3.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEA--FLEPGAT--------VGILLQE 76
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSIliDGEDVRKeprearrqIGVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 77 PPLNEEKTVRGNVEeglgdifekkarfeaiaeematnYTDELMEEMGKlqeeldaadawELDSKIEQAMDALRC-PPADE 155
Cdd:COG4555 83 RGLYDRLTVRENIR-----------------------YFAELYGLFDE-----------ELKKRIEELIELLGLeEFLDR 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 156 PVTHLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAESVLWLEQHLAKY---PGAVLAVTHDRYFLDHVAGWICEVDRG 232
Cdd:COG4555 129 RVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEALCDRVVILHKG 208
|
250
....*....|....*...
gi 512463837 233 KLyPYEGNYSTYLEKKAE 250
Cdd:COG4555 209 KV-VAQGSLDELREEIGE 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
322-499 |
8.55e-22 |
|
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: 93.71 E-value: 8.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDLEKGFDG----RVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTV-QLSYVDQG--- 392
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVdGTDIsKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 393 RENID---------PEKTVWEVVSDGLDYIVVGQNEMPSRAY--LSAFGFKGADQQKPSKvLSGGERNRLNLALTLKQGG 461
Cdd:cd03255 81 RRHIGfvfqsfnllPDLTALENVELPLLLAGVPKKERRERAEelLERVGLGDRLNHYPSE-LSGGQQQRVAIARALANDP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 512463837 462 NLILLDEPTNDLDVETLSSLENALQNF---PGCAVVI-SHDR 499
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELnkeAGTTIVVvTHDP 201
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
7-234 |
1.78e-21 |
|
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: 92.94 E-value: 1.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAHGD----KVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEpG--------------- 67
Cdd:cd03255 2 ELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVD-Gtdisklsekelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 68 -ATVGILLQEPPLNEEKTVRGNVEegLGDIFEKKARFEAiaEEMATnytdELMEEMGklqeeldaadaweldskIEQAMD 146
Cdd:cd03255 81 rRHIGFVFQSFNLLPDLTALENVE--LPLLLAGVPKKER--RERAE----ELLERVG-----------------LGDRLN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 147 AlrcppadePVTHLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAES---VLWLEQHLAKYPG-AVLAVTHDRYFLDHv 222
Cdd:cd03255 136 H--------YPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETgkeVMELLRELNKEAGtTIVVVTHDPELAEY- 206
|
250
....*....|..
gi 512463837 223 AGWICEVDRGKL 234
Cdd:cd03255 207 ADRIIELRDGKI 218
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
307-510 |
2.43e-21 |
|
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: 97.53 E-value: 2.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 307 EEIQIPTPPRLgnqvvEVKDLEKGFDG--RVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVG--- 381
Cdd:COG4987 324 EPAPAPGGPSL-----ELEDVSFRYPGagRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGgvd 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 382 ------QTV--QLSYVDQG--------RENI---DPEKT---VWEVVS------------DGLDYIVvgqnempsrayls 427
Cdd:COG4987 399 lrdldeDDLrrRIAVVPQRphlfdttlRENLrlaRPDATdeeLWAALErvglgdwlaalpDGLDTWL------------- 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 428 afGFKGADqqkpskvLSGGERNRLNLALTLKQGGNLILLDEPTNDLDVET----LSSLENALQNfpGCAVVISHDRWFLD 503
Cdd:COG4987 466 --GEGGRR-------LSGGERRRLALARALLRDAPILLLDEPTEGLDAATeqalLADLLEALAG--RTVLLITHRLAGLE 534
|
....*..
gi 512463837 504 RtCTHIL 510
Cdd:COG4987 535 R-MDRIL 540
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
8-249 |
2.97e-21 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 97.27 E-value: 2.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 8 MKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEPGATVGILLQEPplneektvrg 87
Cdd:PRK15064 322 VENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDH---------- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 88 nveeglgdifekkarfeaiAEEMATNYTdeLMEEMGKlqeeldaadaWELDSKIEQAMDAL--RCP-PADE---PVTHLS 161
Cdd:PRK15064 392 -------------------AYDFENDLT--LFDWMSQ----------WRQEGDDEQAVRGTlgRLLfSQDDikkSVKVLS 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 162 GGERRRVALAKLLLSEPDLLLLDEPTNHLDAESVLWLEQHLAKYPGAVLAVTHDRYFLDHVAGWICEVDRGKLYPYEGNY 241
Cdd:PRK15064 441 GGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTY 520
|
....*...
gi 512463837 242 STYLEKKA 249
Cdd:PRK15064 521 EEYLRSQG 528
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
322-509 |
8.22e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 92.00 E-value: 8.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQTV-----------QLSYVD 390
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPismlssrqlarRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 391 QgrENIDPEK-TVWEVVSDGldyivvgqnempsRA-YLSAFG-FKGADQQ----------------KPSKVLSGGERNRL 451
Cdd:PRK11231 83 Q--HHLTPEGiTVRELVAYG-------------RSpWLSLWGrLSAEDNArvnqameqtrinhladRRLTDLSGGQRQRA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 512463837 452 NLALTLKQGGNLILLDEPTNDLD----VEtLSSLENALQNFPGCAVVISHDRWFLDRTCTHI 509
Cdd:PRK11231 148 FLAMVLAQDTPVVLLDEPTTYLDinhqVE-LMRLMRELNTQGKTVVTVLHDLNQASRYCDHL 208
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
7-234 |
8.62e-21 |
|
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: 91.41 E-value: 8.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEpGATVGILLQEpplnEEKTVR 86
Cdd:cd03261 2 ELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLID-GEDISGLSEA----ELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 87 GNVeeglGDIFEKKARFEA--IAEEMATnytdeLMEEMGKLQEEldaadawELDSKIEQAMDALRCPPADE--PvTHLSG 162
Cdd:cd03261 77 RRM----GMLFQSGALFDSltVFENVAF-----PLREHTRLSEE-------EIREIVLEKLEAVGLRGAEDlyP-AELSG 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 512463837 163 GERRRVALAKLLLSEPDLLLLDEPTNHLD---AESVLWLEQHLAKYPGA-VLAVTHDRYFLDHVAGWICEVDRGKL 234
Cdd:cd03261 140 GMKKRVALARALALDPELLLYDEPTAGLDpiaSGVIDDLIRSLKKELGLtSIMVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
323-498 |
1.67e-20 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 90.57 E-value: 1.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 323 EVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVK------------------VGQTV 384
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLfdgeditglppheiarlgIGRTF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 385 QLSyvdqgreNIDPEKTVWEVV----------SDGLDYIVVGQNEMPSRA--YLSAFGFKG-ADQqkPSKVLSGGERNRL 451
Cdd:cd03219 82 QIP-------RLFPELTVLENVmvaaqartgsGLLLARARREEREARERAeeLLERVGLADlADR--PAGELSYGQQRRL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 512463837 452 NLALTLKQGGNLILLDEPT---NDLDVETLSSLENALQNFpGCAVV-ISHD 498
Cdd:cd03219 153 EIARALATDPKLLLLDEPAaglNPEETEELAELIRELRER-GITVLlVEHD 202
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
321-498 |
1.89e-20 |
|
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: 94.58 E-value: 1.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 321 VVEVKDLEKGFDG--RVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPD---SGEVKVG--QTVQLSYVDQGR 393
Cdd:COG1123 4 LLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDgrDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 394 E----------NIDPEkTVWEVVSDGLDYIVVGQNEMPSRAY--LSAFGFKGADQQKPSKvLSGGERNRLNLALTLKQGG 461
Cdd:COG1123 84 RigmvfqdpmtQLNPV-TVGDQIAEALENLGLSRAEARARVLelLEAVGLERRLDRYPHQ-LSGGQRQRVAIAMALALDP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 512463837 462 NLILLDEPTNDLDVET---LSSLENALQNFPGCAVV-ISHD 498
Cdd:COG1123 162 DLLIADEPTTALDVTTqaeILDLLRELQRERGTTVLlITHD 202
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
9-234 |
3.01e-20 |
|
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: 88.22 E-value: 3.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 9 KNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFL-------EPGAT---VGILLQEPP 78
Cdd:cd03230 4 RNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVlgkdikkEPEEVkrrIGYLPEEPS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 79 LNEEKTVRGNVEeglgdifekkarfeaiaeematnytdelmeemgklqeeldaadaweldskieqamdalrcppadepvt 158
Cdd:cd03230 84 LYENLTVRENLK-------------------------------------------------------------------- 95
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 512463837 159 hLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAESVLWLEQHLAKY---PGAVLAVTHDRYFLDHVAGWICEVDRGKL 234
Cdd:cd03230 96 -LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELkkeGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
7-223 |
3.54e-20 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 89.76 E-value: 3.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFL------EPGATVGILLQEPPLN 80
Cdd:COG1121 8 ELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLfgkpprRARRRIGYVPQRAEVD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 81 EEKTVRgnVEE----------GLGDIFEKKARfEAIaeematnytDELMEEMGklqeeldaadaweldskieqaMDALrc 150
Cdd:COG1121 88 WDFPIT--VRDvvlmgrygrrGLFRRPSRADR-EAV---------DEALERVG---------------------LEDL-- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 151 ppADEPVTHLSGGERRRVALAKlllsepdllllDEPTNHLDAES------VLwleQHLAKYPGAVLAVTHD-----RYFl 219
Cdd:COG1121 133 --ADRPIGELSGGQQQRVLLARalaqdpdllllDEPFAGVDAATeealyeLL---RELRREGKTILVVTHDlgavrEYF- 206
|
....
gi 512463837 220 DHVA 223
Cdd:COG1121 207 DRVL 210
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
322-476 |
4.00e-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: 88.79 E-value: 4.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDLEKGFDGRVLIKDLSFTLPrNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTV---------QLSYVDQ 391
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLG-PGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIdGQDVlkqpqklrrRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 392 gRENIDPEKTVWEVvsdgLDYIVVGQNEMPSRAY------LSAFGFKGADQQKPSKvLSGGERNRLNLALTLKQGGNLIL 465
Cdd:cd03264 80 -EFGVYPNFTVREF----LDYIAWLKGIPSKEVKarvdevLELVNLGDRAKKKIGS-LSGGMRRRVGIAQALVGDPSILI 153
|
170
....*....|.
gi 512463837 466 LDEPTNDLDVE 476
Cdd:cd03264 154 VDEPTAGLDPE 164
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
323-504 |
4.26e-20 |
|
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: 89.55 E-value: 4.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 323 EVKDLEKGF-DGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQTVQLSYvdQGRENIDPEK- 400
Cdd:cd03256 2 EVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKL--KGKALRQLRRq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 401 --TVWEvvsdglDY-----IVVGQNEMPSR-AYLSAF-----GFKGADQQKP----SKV------------LSGGERNRL 451
Cdd:cd03256 80 igMIFQ------QFnlierLSVLENVLSGRlGRRSTWrslfgLFPKEEKQRAlaalERVglldkayqradqLSGGQQQRV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 512463837 452 NLALTLKQGGNLILLDEPTNDLDVET----LSSLENALQNFpGCAVVIS-HD----RWFLDR 504
Cdd:cd03256 154 AIARALMQQPKLILADEPVASLDPASsrqvMDLLKRINREE-GITVIVSlHQvdlaREYADR 214
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
322-474 |
5.37e-20 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 89.37 E-value: 5.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTV----------QLSYVD 390
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVdGLDVattpsrelakRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 391 QgrEN-IDPEKTVWEVVSDG-----------LDYIVVGQnempSRAYLSAFGFKGA--DQqkpskvLSGGERNRLNLALT 456
Cdd:COG4604 82 Q--ENhINSRLTVRELVAFGrfpyskgrltaEDREIIDE----AIAYLDLEDLADRylDE------LSGGQRQRAFIAMV 149
|
170
....*....|....*...
gi 512463837 457 LKQGGNLILLDEPTNDLD 474
Cdd:COG4604 150 LAQDTDYVLLDEPLNNLD 167
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-233 |
5.57e-20 |
|
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: 86.92 E-value: 5.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEaflepgatvgILLQEPPLNEEKTVR 86
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGE----------ILIDGKDIAKLPLEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 87 gnVEEGLGDIFEkkarfeaiaeematnytdelmeemgklqeeldaadaweldskieqamdalrcppadepvthLSGGERR 166
Cdd:cd00267 71 --LRRRIGYVPQ-------------------------------------------------------------LSGGQRQ 87
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 167 RVALAKLLLSEPDLLLLDEPTNHLDAESVLWLEQHLAKYPG---AVLAVTHDRYFLDHVAGWICEVDRGK 233
Cdd:cd00267 88 RVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEegrTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
9-216 |
6.96e-20 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 88.35 E-value: 6.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 9 KNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEpGATV----------GILLQEPP 78
Cdd:cd03259 4 KGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILID-GRDVtgvpperrniGMVFQDYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 79 LNEEKTVRGNVEEGLGDIFEKKARFEAIAEEMAtnytdelmeemgklqEELDAADaweldskieqamdalrcpPADEPVT 158
Cdd:cd03259 83 LFPHLTVAENIAFGLKLRGVPKAEIRARVRELL---------------ELVGLEG------------------LLNRYPH 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 512463837 159 HLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAESVLWLEQHLAKYPGA----VLAVTHDR 216
Cdd:cd03259 130 ELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRElgitTIYVTHDQ 191
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-215 |
1.39e-19 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 87.79 E-value: 1.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 1 MGEFIyQMKNVRKAHGDK----VILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEpGA-------- 68
Cdd:COG1136 1 MSPLL-ELRNLTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLID-GQdisslser 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 69 --------TVGILLQEPPLNEEKTVRGNVEegLGDIFEKKARfeAIAEEMAtnytDELMEEMGklqeeldaadaweLDSK 140
Cdd:COG1136 79 elarlrrrHIGFVFQFFNLLPELTALENVA--LPLLLAGVSR--KERRERA----RELLERVG-------------LGDR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 141 ieqamdalrcppADEPVTHLSGGERRRVA------------LAklllsepdllllDEPTNHLD---AESVLWLEQHLAKY 205
Cdd:COG1136 138 ------------LDHRPSQLSGGQQQRVAiaralvnrpkliLA------------DEPTGNLDsktGEEVLELLRELNRE 193
|
250
....*....|.
gi 512463837 206 PG-AVLAVTHD 215
Cdd:COG1136 194 LGtTIVMVTHD 204
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
326-498 |
1.90e-19 |
|
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: 86.97 E-value: 1.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 326 DLEKGFDGRVLikDLSFTLPRNgIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQTVqlsYVDqGRENID-------- 397
Cdd:cd03297 5 DIEKRLPDFTL--KIDFDLNEE-VTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTV---LFD-SRKKINlppqqrki 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 398 ----------PEKTVWEVVSDGLDYIVVGQNEMPSRAYLSAFGFKGADQQKPSKvLSGGERNRLNLALTLKQGGNLILLD 467
Cdd:cd03297 78 glvfqqyalfPHLNVRENLAFGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQ-LSGGEKQRVALARALAAQPELLLLD 156
|
170 180 190
....*....|....*....|....*....|....*
gi 512463837 468 EPTNDLDVETLSSLENAL----QNFPGCAVVISHD 498
Cdd:cd03297 157 EPFSALDRALRLQLLPELkqikKNLNIPVIFVTHD 191
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
321-510 |
2.29e-19 |
|
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: 87.25 E-value: 2.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 321 VVEVKDLEKGFDGR----VLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTVQLSYVDQGRE- 394
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVdGTDLTLLSGKELRKa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 395 -----------NIDPEKTVWEVVSDGLDYIVVGQNEMPSRAY--LSAFGFKGADQQKPSKvLSGGERNRLNLALTLKQGG 461
Cdd:cd03258 81 rrrigmifqhfNLLSSRTVFENVALPLEIAGVPKAEIEERVLelLELVGLEDKADAYPAQ-LSGGQKQRVGIARALANNP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 512463837 462 NLILLDEPTNDLDVETLSSLENAL----QNFPGCAVVISHDRWFLDRTCTHIL 510
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLrdinRELGLTIVLITHEMEVVKRICDRVA 212
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
334-497 |
3.26e-19 |
|
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: 84.96 E-value: 3.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 334 RVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTVQLSYVDQGRENIDpektvwevvsdgldy 412
Cdd:cd03246 15 PPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLdGADISQWDPNELGDHVG--------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 413 iVVGQNEMpsrayLsafgFKG--ADQqkpskVLSGGERNRLNLALTLKQGGNLILLDEPTNDLDVETLSSLENALQNFPG 490
Cdd:cd03246 80 -YLPQDDE-----L----FSGsiAEN-----ILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKA 144
|
170
....*....|
gi 512463837 491 C---AVVISH 497
Cdd:cd03246 145 AgatRIVIAH 154
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
323-498 |
3.71e-19 |
|
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: 87.02 E-value: 3.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 323 EVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVK------------------VGQTV 384
Cdd:COG0411 6 EVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILfdgrditglpphriarlgIARTF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 385 QLSyvdqgreNIDPEKTVWEVVsdgldyIVVGQNEMPSRAYLSAFGFKGADQQ----------------------KPSKV 442
Cdd:COG0411 86 QNP-------RLFPELTVLENV------LVAAHARLGRGLLAALLRLPRARREereareraeellervgladradEPAGN 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 443 LSGGERNRLNLALTLKQGGNLILLDEPT---NDLDVETLSSLENALQNFPGCAVV-ISHD 498
Cdd:COG0411 153 LSYGQQRRLEIARALATEPKLLLLDEPAaglNPEETEELAELIRRLRDERGITILlIEHD 212
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
322-499 |
4.10e-19 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 88.67 E-value: 4.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQTVQLSYVDQGRENID---- 397
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPRERRVGfvfq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 398 -----PEKTVWEVVSDGLDYIVVGQNEMPSRA--YLSAFGFKGADQQKPSKvLSGGERNRLNLALTLKQGGNLILLDEPT 470
Cdd:COG1118 83 hyalfPHMTVAENIAFGLRVRPPSKAEIRARVeeLLELVQLEGLADRYPSQ-LSGGQRQRVALARALAVEPEVLLLDEPF 161
|
170 180 190
....*....|....*....|....*....|...
gi 512463837 471 NDLDVETLSSLE----NALQNFPGCAVVISHDR 499
Cdd:COG1118 162 GALDAKVRKELRrwlrRLHDELGGTTVFVTHDQ 194
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
321-498 |
7.47e-19 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 86.32 E-value: 7.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 321 VVEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQTVQLSYVDQgRENIDPek 400
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQ-KLYLDT-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 401 TVWEVVSD--GLDYIVVGQNEMPSRAYLSAFGFKGADQQKpskvLSGGERNRLNLALTLKQGGNLILLDEPTNDLDVE-- 476
Cdd:PRK09544 81 TLPLTVNRflRLRPGTKKEDILPALKRVQAGHLIDAPMQK----LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNgq 156
|
170 180
....*....|....*....|....
gi 512463837 477 -TLSSLENALQNFPGCAVV-ISHD 498
Cdd:PRK09544 157 vALYDLIDQLRRELDCAVLmVSHD 180
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
21-222 |
1.70e-18 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 88.50 E-value: 1.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 21 LDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEaflepGATVGILLQEPplnEEKTVRgnveEGLGDIFEKK 100
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGS-----IAVNGVPLADA---DADSWR----DQIAWVPQHP 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 101 ARFEA-IAEE--MATNYTDELMeemgkLQEELDAADAWELDSKIEQAMDAlrcpPADEPVTHLSGGERRRVALAKLLLSE 177
Cdd:TIGR02857 406 FLFAGtIAENirLARPDASDAE-----IREALERAGLDEFVAALPQGLDT----PIGEGGAGLSGGQAQRLALARAFLRD 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 512463837 178 PDLLLLDEPTNHLDAESVLWLEQHLAKYPG--AVLAVTHDR---YFLDHV 222
Cdd:TIGR02857 477 APLLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVTHRLalaALADRI 526
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-223 |
1.88e-18 |
|
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: 84.12 E-value: 1.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFL------EPGATVGILLQEppLN 80
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfgkpleKERKRIGYVPQR--RS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 81 EEKTVRGNVEE----------GLGDIFeKKARFEAIaeematnytDELMEEMGklqeeldaadaweldskieqaMDALrc 150
Cdd:cd03235 79 IDRDFPISVRDvvlmglyghkGLFRRL-SKADKAKV---------DEALERVG---------------------LSEL-- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 151 ppADEPVTHLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAES---VLWLEQHLAKYPGAVLAVTHD----RYFLDHVA 223
Cdd:cd03235 126 --ADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTqedIYELLRELRREGMTILVVTHDlglvLEYFDRVL 203
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
227-306 |
2.43e-18 |
|
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: 79.93 E-value: 2.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 227 CEVDRGKLYPYEGNYSTYLEKKAERLEVAGKKDAKLQKRLKDELAWVRS----GQKARQAKNKA-RLERYEQMVEEAEQY 301
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRfrakASKAKQAQSRIkALEKMERIEKPERDK 80
|
....*
gi 512463837 302 KKLDF 306
Cdd:pfam12848 81 PKLRF 85
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
323-470 |
2.89e-18 |
|
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: 83.64 E-value: 2.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 323 EVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTVQ-----------LSYVD 390
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFdGRDITglppheraragIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 391 QGReNIDPEKTVwevvsdgLDYIVVGqnempsrAYlsaFGFKGADQQKPSKV-----------------LSGGERNRLNL 453
Cdd:cd03224 82 EGR-RIFPELTV-------EENLLLG-------AY---ARRRAKRKARLERVyelfprlkerrkqlagtLSGGEQQMLAI 143
|
170
....*....|....*..
gi 512463837 454 ALTLKQGGNLILLDEPT 470
Cdd:cd03224 144 ARALMSRPKLLLLDEPS 160
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
322-477 |
3.08e-18 |
|
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: 83.35 E-value: 3.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQTVqlsyVDQGRENID---- 397
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLK----LTDDKKNINelrq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 398 ------------PEKTVWEVVSDGLdYIVVGQN----EMPSRAYLSAFGFKGADQQKPSKvLSGGERNRLNLALTLKQGG 461
Cdd:cd03262 77 kvgmvfqqfnlfPHLTVLENITLAP-IKVKGMSkaeaEERALELLEKVGLADKADAYPAQ-LSGGQQQRVAIARALAMNP 154
|
170
....*....|....*.
gi 512463837 462 NLILLDEPTNDLDVET 477
Cdd:cd03262 155 KVMLFDEPTSALDPEL 170
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
322-498 |
3.18e-18 |
|
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: 83.77 E-value: 3.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGL-----EQPDSGEV------------------ 378
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVlldgkdiydldvdvlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 379 -KVGQTVQLSYVDQG--RENID---------PEKTVWEVVSDGLdyivvgqnempSRAYLSAfgfKGADQQKPSKvLSGG 446
Cdd:cd03260 81 rRVGMVFQKPNPFPGsiYDNVAyglrlhgikLKEELDERVEEAL-----------RKAALWD---EVKDRLHALG-LSGG 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 512463837 447 ERNRLNLALTLKQGGNLILLDEPTNDLDVETLSSLENALQNF--PGCAVVISHD 498
Cdd:cd03260 146 QQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELkkEYTIVIVTHN 199
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
319-510 |
3.23e-18 |
|
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: 83.64 E-value: 3.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 319 NQVVEVKDLEKGF-----DGRVL--IKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV---GQTVQLS- 387
Cdd:COG4778 2 TTLLEVENLSKTFtlhlqGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdGGWVDLAq 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 388 ---------------YVDQGRENIdPEKTVWEVVSDGLdyivVGQNEMPSRAY------LSAFGFKGADQQKPSKVLSGG 446
Cdd:COG4778 82 aspreilalrrrtigYVSQFLRVI-PRVSALDVVAEPL----LERGVDREEARararelLARLNLPERLWDLPPATFSGG 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 512463837 447 ERNRLNLALTLKQGGNLILLDEPTNDLDVET----LSSLENALQNfpGCAVV-ISHDRWFLDRTCTHIL 510
Cdd:COG4778 157 EQQRVNIARGFIADPPLLLLDEPTASLDAANravvVELIEEAKAR--GTAIIgIFHDEEVREAVADRVV 223
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
322-513 |
3.26e-18 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 83.61 E-value: 3.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDLEKGFDGRVL-IKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTV------QLSYVdqgR 393
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVnGQDVsdlrgrAIPYL---R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 394 ENID---------PEKTVWEVVSDGLDYIVVGQNEMPSR--AYLSAFGFKGADQQKPSKvLSGGERNRLNLALTLKQGGN 462
Cdd:cd03292 78 RKIGvvfqdfrllPDRNVYENVAFALEVTGVPPREIRKRvpAALELVGLSHKHRALPAE-LSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 512463837 463 LILLDEPTNDLDVETLSSLENALQ--NFPGCAVVIS-HDRWFLDRTCTHILAWE 513
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKkiNKAGTTVVVAtHAKELVDTTRHRVIALE 210
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
322-476 |
4.26e-18 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 84.03 E-value: 4.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQTV---------QLSYVDQG 392
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITidtarslsqQKGLIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 393 RE---------NIDPEKTVWEVVSDGlDYIVVG----QNEMPSRAYLSAFGFKGADQQKPSKvLSGGERNRLNLALTLKQ 459
Cdd:PRK11264 84 RQhvgfvfqnfNLFPHRTVLENIIEG-PVIVKGepkeEATARARELLAKVGLAGKETSYPRR-LSGGQQQRVAIARALAM 161
|
170
....*....|....*..
gi 512463837 460 GGNLILLDEPTNDLDVE 476
Cdd:PRK11264 162 RPEVILFDEPTSALDPE 178
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
16-215 |
4.33e-18 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 84.01 E-value: 4.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 16 GDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLE--------PGA---TVGILLQEPPLNEEKT 84
Cdd:COG4559 12 GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNgrplaawsPWElarRRAVLPQHSSLAFPFT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 85 VRGNVEEGLGDIFEKKARFEAIAEEMatnytdelmeemgklqeeLDAADAWELdskieqamdalrcppADEPVTHLSGGE 164
Cdd:COG4559 92 VEEVVALGRAPHGSSAAQDRQIVREA------------------LALVGLAHL---------------AGRSYQTLSGGE 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 512463837 165 RRRV----ALAKLLLSEPDLLLL---DEPTNHLD---AESVLWLEQHLAKYPGAVLAVTHD 215
Cdd:COG4559 139 QQRVqlarVLAQLWEPVDGGPRWlflDEPTSALDlahQHAVLRLARQLARRGGGVVAVLHD 199
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
16-215 |
4.41e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 84.05 E-value: 4.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 16 GDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFL-----------EPGATVGILLQEPPLNEEKT 84
Cdd:PRK13548 13 GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLngrpladwspaELARRRAVLPQHSSLSFPFT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 85 VRGNVEEGLGDIFEKKARFEAIAEEMatnytdelmeemgklqeeLDAADAWELdskieqamdalrcppADEPVTHLSGGE 164
Cdd:PRK13548 93 VEEVVAMGRAPHGLSRAEDDALVAAA------------------LAQVDLAHL---------------AGRDYPQLSGGE 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 512463837 165 RRRVALAK------LLLSEPDLLLLDEPTNHLD---AESVLWLEQHLA-KYPGAVLAVTHD 215
Cdd:PRK13548 140 QQRVQLARvlaqlwEPDGPPRWLLLDEPTSALDlahQHHVLRLARQLAhERGLAVIVVLHD 200
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
7-234 |
4.95e-18 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 87.51 E-value: 4.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAH--GDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFL-----------EPGATVGIL 73
Cdd:COG4987 335 ELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLggvdlrdldedDLRRRIAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 74 LQEPPL-NEekTVRGNVeeglgdifekkarfeAIAEEMATNytDELMEemgklqeeldAADAWELDSKIEQAMDALrcpp 152
Cdd:COG4987 415 PQRPHLfDT--TLRENL---------------RLARPDATD--EELWA----------ALERVGLGDWLAALPDGL---- 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 153 aDEPV----THLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAESVLWLEQHLAKY-PG-AVLAVTHDRYFLDHVAGwI 226
Cdd:COG4987 462 -DTWLgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAlAGrTVLLITHRLAGLERMDR-I 539
|
....*...
gi 512463837 227 CEVDRGKL 234
Cdd:COG4987 540 LVLEDGRI 547
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
322-481 |
4.95e-18 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 83.19 E-value: 4.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTV---------QLSYVDQ 391
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVaGHDVvreprevrrRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 392 GReNIDPEKTVWE-VVSDGLDYIVVGQnEMPSRA--YLSAFGFKGAdQQKPSKVLSGGERNRLNLALTLKQGGNLILLDE 468
Cdd:cd03265 81 DL-SVDDELTGWEnLYIHARLYGVPGA-ERRERIdeLLDFVGLLEA-ADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDE 157
|
170
....*....|...
gi 512463837 469 PTNDLDVETLSSL 481
Cdd:cd03265 158 PTIGLDPQTRAHV 170
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
323-498 |
5.49e-18 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 83.63 E-value: 5.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 323 EVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVkvgqtvqlSYVDQGRENIDPEK-- 400
Cdd:COG4559 3 EAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEV--------RLNGRPLAAWSPWEla 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 401 ----------------TVWEVVSDGLD-YIVVGQNEMP-SRAYLSAFGFKG-ADQQKPSkvLSGGERNRLNLALTLKQ-- 459
Cdd:COG4559 75 rrravlpqhsslafpfTVEEVVALGRApHGSSAAQDRQiVREALALVGLAHlAGRSYQT--LSGGEQQRVQLARVLAQlw 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 512463837 460 -----GGNLILLDEPTNDLDV-------ETLSSLenALQNFPGCAVVisHD 498
Cdd:COG4559 153 epvdgGPRWLFLDEPTSALDLahqhavlRLARQL--ARRGGGVVAVL--HD 199
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
311-474 |
5.49e-18 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 86.04 E-value: 5.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 311 IPTPP----RLGNQVVEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVkVGQTVQL 386
Cdd:PRK11607 5 IPRPQaktrKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQI-MLDGVDL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 387 SYVDQGRENID---------PEKTVWEVVSDGLDYIVVGQNEMPSRA--YLSAFGFKGADQQKPSKvLSGGERNRLNLAL 455
Cdd:PRK11607 84 SHVPPYQRPINmmfqsyalfPHMTVEQNIAFGLKQDKLPKAEIASRVneMLGLVHMQEFAKRKPHQ-LSGGQRQRVALAR 162
|
170
....*....|....*....
gi 512463837 456 TLKQGGNLILLDEPTNDLD 474
Cdd:PRK11607 163 SLAKRPKLLLLDEPMGALD 181
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
9-215 |
5.80e-18 |
|
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: 83.00 E-value: 5.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 9 KNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGL-----DQPSNGEAFLEPG-------------ATV 70
Cdd:cd03260 4 RDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKdiydldvdvlelrRRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 71 GILLQEPPLNeEKTVRGNVEEGLGDIFEK-KARFEAIAEematnytdELMEEMGKLQEELDAADAweldskieqamdalr 149
Cdd:cd03260 84 GMVFQKPNPF-PGSIYDNVAYGLRLHGIKlKEELDERVE--------EALRKAALWDEVKDRLHA--------------- 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 512463837 150 cppadepvTHLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAESVLWLEQHLAKY--PGAVLAVTHD 215
Cdd:cd03260 140 --------LGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELkkEYTIVIVTHN 199
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
7-296 |
7.49e-18 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 87.15 E-value: 7.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEPGATVGILLQepplNEEKTVR 86
Cdd:PRK10636 314 KMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQ----HQLEFLR 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 87 gnveeglgdifekkarfeaiAEEMAtnytdelMEEMGKLQEEldaadawELDSKIEQAMDA--LRCPPADEPVTHLSGGE 164
Cdd:PRK10636 390 --------------------ADESP-------LQHLARLAPQ-------ELEQKLRDYLGGfgFQGDKVTEETRRFSGGE 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 165 RRRVALAKLLLSEPDLLLLDEPTNHLDAESVLWLEQHLAKYPGAVLAVTHDRYFLDHVAGWICEVDRGKLYPYEGNYSTY 244
Cdd:PRK10636 436 KARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDY 515
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 512463837 245 LEKKAERLEVAGKKDAKlQKRLKDELAWVRSGQKARQAKNKA-------RLERYEQMVE 296
Cdd:PRK10636 516 QQWLSDVQKQENQTDEA-PKENNANSAQARKDQKRREAELRTqtqplrkEIARLEKEME 573
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
7-214 |
9.14e-18 |
|
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: 81.88 E-value: 9.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFL---------EPGATVGILLQEP 77
Cdd:cd03268 2 KTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFdgksyqkniEALRRIGALIEAP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 78 PLNEEKTVRGNVE-EGLGDIFEKKArfeaiaeematnyTDELMEEMGklqeeLDAAdaweldskieqamdalrcppADEP 156
Cdd:cd03268 82 GFYPNLTARENLRlLARLLGIRKKR-------------IDEVLDVVG-----LKDS--------------------AKKK 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 512463837 157 VTHLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAESVLWLEQ---HLAKYPGAVLAVTH 214
Cdd:cd03268 124 VKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRElilSLRDQGITVLISSH 184
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
7-234 |
1.15e-17 |
|
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: 82.03 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFL-------EPG---ATVGILLQE 76
Cdd:cd03265 2 EVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVaghdvvrEPRevrRRIGIVFQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 77 PPLNEEKTVRGNVEeglgdIFekkARFEAIAEEMATNYTDELmeemgklqeeLDAADAWELdskieqamdalrcppADEP 156
Cdd:cd03265 82 LSVDDELTGWENLY-----IH---ARLYGVPGAERRERIDEL----------LDFVGLLEA---------------ADRL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 157 VTHLSGGERRRVALAKLLLSEPDLLLLDEPTNHLD--AESVLW--LEQHLAKYPGAVLAVTHDRYFLDHVAGWICEVDRG 232
Cdd:cd03265 129 VKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDpqTRAHVWeyIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHG 208
|
..
gi 512463837 233 KL 234
Cdd:cd03265 209 RI 210
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
322-497 |
1.54e-17 |
|
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: 80.17 E-value: 1.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTVQ-LSYVDQGRENIdpe 399
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVdGKEVSfASPRDARRAGI--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 400 ktvwEVVSdgldyivvgQnempsraylsafgfkgadqqkpskvLSGGERNRLNLALTLKQGGNLILLDEPTNDLDVETLS 479
Cdd:cd03216 78 ----AMVY---------Q-------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVE 119
|
170 180
....*....|....*....|.
gi 512463837 480 SLENALQNF--PGCAVV-ISH 497
Cdd:cd03216 120 RLFKVIRRLraQGVAVIfISH 140
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
8-215 |
1.58e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 84.89 E-value: 1.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 8 MKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFL-----------EPGATVGILLQE 76
Cdd:PRK09536 6 VSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVagddvealsarAASRRVASVPQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 77 PPLNEEKTVRGNVEEGLGdifEKKARFEAIAEematnyTDelmeemgklqeeldaadawelDSKIEQAMDALRCPP-ADE 155
Cdd:PRK09536 86 TSLSFEFDVRQVVEMGRT---PHRSRFDTWTE------TD---------------------RAAVERAMERTGVAQfADR 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 512463837 156 PVTHLSGGERRRVALAKLLLSEPDLLLLDEPTNHLD---AESVLWLEQHLAKYPGAVLAVTHD 215
Cdd:PRK09536 136 PVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDinhQVRTLELVRRLVDDGKTAVAAIHD 198
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
322-475 |
1.82e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 84.51 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTV----------QLSYVD 390
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVaGDDVealsaraasrRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 391 QGrENIDPEKTVWEVVSDG-------LDyivvGQNEMPSRAYLSAFGFKGADQ--QKPSKVLSGGERNRLNLALTLKQGG 461
Cdd:PRK09536 84 QD-TSLSFEFDVRQVVEMGrtphrsrFD----TWTETDRAAVERAMERTGVAQfaDRPVTSLSGGERQRVLLARALAQAT 158
|
170
....*....|....
gi 512463837 462 NLILLDEPTNDLDV 475
Cdd:PRK09536 159 PVLLLDEPTASLDI 172
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
16-222 |
2.26e-17 |
|
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: 82.17 E-value: 2.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 16 GDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEPG-----------ATVGILLQEPPLNEEKT 84
Cdd:TIGR03873 12 GGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVdlhglsrraraRRVALVEQDSDTAVPLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 85 VRGNVeeGLGDIFEKKARFEAIAEEMATnyTDELMEEMGklqeeldaadaweldskieqaMDALrcppADEPVTHLSGGE 164
Cdd:TIGR03873 92 VRDVV--ALGRIPHRSLWAGDSPHDAAV--VDRALARTE---------------------LSHL----ADRDMSTLSGGE 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 512463837 165 RRRVALAKLLLSEPDLLLLDEPTNHLDAES---VLWLEQHLAKYPGAVLAVTHD----RYFLDHV 222
Cdd:TIGR03873 143 RQRVHVARALAQEPKLLLLDEPTNHLDVRAqleTLALVRELAATGVTVVAALHDlnlaASYCDHV 207
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
14-223 |
2.32e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 80.36 E-value: 2.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 14 AHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEPGATVGILLQEP------PLneekTVRG 87
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSevpdslPL----TVRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 88 NVEeglgdifekkarfeaiaeematnytdelmeeMGKLQEE-----LDAADawelDSKIEQAMDALRCPP-ADEPVTHLS 161
Cdd:NF040873 77 LVA-------------------------------MGRWARRglwrrLTRDD----RAAVDDALERVGLADlAGRQLGELS 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 512463837 162 GGERRRVALAKLLLSEPDLLLLDEPTNHLDAESVLWLEQHLAKYPG---AVLAVTHDryfLDHVA 223
Cdd:NF040873 122 GGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHArgaTVVVVTHD---LELVR 183
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
322-469 |
2.39e-17 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 81.44 E-value: 2.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQT------------VQLSYV 389
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQditklpmhkrarLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 390 DQgRENIDPEKTVWEVVSDGLDYIVVGQNEMPSR--AYLSAFGFKGADQQKPSKvLSGGERNRLNLALTLKQGGNLILLD 467
Cdd:cd03218 81 PQ-EASIFRKLTVEENILAVLEIRGLSKKEREEKleELLEEFHITHLRKSKASS-LSGGERRRVEIARALATNPKFLLLD 158
|
..
gi 512463837 468 EP 469
Cdd:cd03218 159 EP 160
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
9-216 |
2.69e-17 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 83.27 E-value: 2.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 9 KNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEpGAT-----------VGILLQEP 77
Cdd:COG1118 6 RNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLN-GRDlftnlpprerrVGFVFQHY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 78 PLNEEKTVRGNVEEGLGDIFEKKARFEAIAEEMAtnytdEL--MEEMGKlqeeldaadaweldskieqamdalRCPpade 155
Cdd:COG1118 85 ALFPHMTVAENIAFGLRVRPPSKAEIRARVEELL-----ELvqLEGLAD------------------------RYP---- 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 512463837 156 pvTHLSGGERRRVALAklllsepdllllDEPTNHLDAeSV-----LWLEQHLAKYPGAVLAVTHDR 216
Cdd:COG1118 132 --SQLSGGQRQRVALAralavepevlllDEPFGALDA-KVrkelrRWLRRLHDELGGTTVFVTHDQ 194
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-171 |
3.10e-17 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 81.18 E-value: 3.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 1 MGEFIYQMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLE----PGAT------- 69
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDgqdiTGLSekelyel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 70 ---VGILLQEPPLNEEKTVRGNVEEGLgdifekkarfeaiaeEMATNYTDELMEE--MGKLQE-ELDAAdaweldskiEQ 143
Cdd:COG1127 81 rrrIGMLFQGGALFDSLTVFENVAFPL---------------REHTDLSEAEIRElvLEKLELvGLPGA---------AD 136
|
170 180
....*....|....*....|....*...
gi 512463837 144 AMdalrcpPADepvthLSGGERRRVALA 171
Cdd:COG1127 137 KM------PSE-----LSGGMRKRVALA 153
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
328-505 |
3.45e-17 |
|
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: 80.47 E-value: 3.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 328 EKGFDGRVLiKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTVQ-LSYVDQGR-ENID------- 397
Cdd:TIGR02211 13 EGKLDTRVL-KGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFnGQSLSkLSSNERAKlRNKKlgfiyqf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 398 ----PEKTVWEVVSDGLdyIVVGQN--EMPSRAY--LSAFGFKGADQQKPSKvLSGGERNRLNLALTLKQGGNLILLDEP 469
Cdd:TIGR02211 92 hhllPDFTALENVAMPL--LIGKKSvkEAKERAYemLEKVGLEHRINHRPSE-LSGGERQRVAIARALVNQPSLVLADEP 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 512463837 470 TNDLDVETLSS-----LE-NALQN--FpgcaVVISHDRWFLDRT 505
Cdd:TIGR02211 169 TGNLDNNNAKIifdlmLElNRELNtsF----LVVTHDLELAKKL 208
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
322-498 |
4.69e-17 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 79.99 E-value: 4.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQTVqLSYVDQGRENID---- 397
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRD-VTDLPPKDRDIAmvfq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 398 -----PEKTVWEVVSDGLDYIVVGQNEMPSRAYLSA--FGFKGADQQKPsKVLSGGERNRLNLALTLKQGGNLILLDEPT 470
Cdd:cd03301 80 nyalyPHMTVYDNIAFGLKLRKVPKDEIDERVREVAelLQIEHLLDRKP-KQLSGGQRQRVALGRAIVREPKVFLMDEPL 158
|
170 180 190
....*....|....*....|....*....|..
gi 512463837 471 NDLD----VETLSSLENALQNFPGCAVVISHD 498
Cdd:cd03301 159 SNLDaklrVQMRAELKRLQQRLGTTTIYVTHD 190
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
343-514 |
6.34e-17 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 80.53 E-value: 6.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 343 TLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVgQTVQLSYVDQGREnIDPEKTVWEVVSDGLDyivvgqnemps 422
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI-ELDTVSYKPQYIK-ADYEGTVRDLLSSITK----------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 423 RAYLSAFgFKgADQQKPSKV----------LSGGERNRLNLALTLKQGGNLILLDEPTNDLDVETLSSLENALQNF---- 488
Cdd:cd03237 88 DFYTHPY-FK-TEIAKPLQIeqildrevpeLSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFaenn 165
|
170 180
....*....|....*....|....*.
gi 512463837 489 PGCAVVISHDRWFLDRTCTHILAWEG 514
Cdd:cd03237 166 EKTAFVVEHDIIMIDYLADRLIVFEG 191
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
337-488 |
7.41e-17 |
|
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: 80.07 E-value: 7.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 337 IKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQTVQLSYVDQGRENI-----DPEKTVWEV-VSDGL 410
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIgvvfgQKTQLWWDLpVIDSF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 411 dyivvgqnEMPSRAY-LSAFGFK------------GADQQKPSKVLSGGERNRLNLALTLKQGGNLILLDEPTNDLDVET 477
Cdd:cd03267 117 --------YLLAAIYdLPPARFKkrldelselldlEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVA 188
|
170
....*....|.
gi 512463837 478 lsslENALQNF 488
Cdd:cd03267 189 ----QENIRNF 195
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
7-234 |
7.49e-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: 79.50 E-value: 7.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGE-------------AFLEPGATVGIL 73
Cdd:cd03262 2 EIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTiiidglkltddkkNINELRQKVGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 74 LQEPPLNEEKTVRGNVEEGLGDIFeKKARFEAIAEEMatnytdELMEEMGKLqeelDAADAWeldskieqamdalrcpPA 153
Cdd:cd03262 82 FQQFNLFPHLTVLENITLAPIKVK-GMSKAEAEERAL------ELLEKVGLA----DKADAY----------------PA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 154 depvtHLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAE---SVLWLEQHLAKYPGAVLAVTHDRYFLDHVAGWICEVD 230
Cdd:cd03262 135 -----QLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPElvgEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMD 209
|
....
gi 512463837 231 RGKL 234
Cdd:cd03262 210 DGRI 213
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
322-510 |
1.09e-16 |
|
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: 78.86 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVgQTVQLSYVDQGRENIDPE-- 399
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLF-DGKPLDIAARNRIGYLPEer 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 400 ----KtvwEVVSDGLDYIV----VGQNEMPSRA--YLSAFGFkGADQQKPSKVLSGGERNRLNLALTLKQGGNLILLDEP 469
Cdd:cd03269 80 glypK---MKVIDQLVYLAqlkgLKKEEARRRIdeWLERLEL-SEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 512463837 470 TNDLD---VETLSSLENALQNfPGCAVVIS-HDRWFLDRTCTHIL 510
Cdd:cd03269 156 FSGLDpvnVELLKDVIRELAR-AGKTVILStHQMELVEELCDRVL 199
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
16-215 |
1.18e-16 |
|
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: 82.79 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 16 GDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFL-----------EPGATVGILLQEPPLNEeKT 84
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLdgvpvssldqdEVRRRVSVCAQDAHLFD-TT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 85 VRGNVEEGLGDIfekkarfeaiaeematnyTDElmeemgklqEELDAADAWELDSKIEQAMDALrcppaDEPVTH----L 160
Cdd:TIGR02868 425 VRENLRLARPDA------------------TDE---------ELWAALERVGLADWLRALPDGL-----DTVLGEggarL 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 512463837 161 SGGERRRVALAKLLLSEPDLLLLDEPTNHLDAESVL-WLEQHLAKYPG-AVLAVTHD 215
Cdd:TIGR02868 473 SGGERQRLALARALLADAPILLLDEPTEHLDAETADeLLEDLLAALSGrTVVLITHH 529
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
20-219 |
1.23e-16 |
|
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: 78.45 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 20 ILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFL--------EPGATVGILLQEPPLN-EEKTVRGNVE 90
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLngkpikakERRKSIGYVMQDVDYQlFTDSVREELL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 91 EGLGDIFEKKARFEAIAEEMATNYTDELMeemgklqeeldaadaweldskieqamdalrcpPADepvthLSGGERRRVAL 170
Cdd:cd03226 95 LGLKELDAGNEQAETVLKDLDLYALKERH--------------------------------PLS-----LSGGQKQRLAI 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 512463837 171 AKLLLSEPDLLLLDEPTNHLDA---ESVLWLEQHLAKYPGAVLAVTHDRYFL 219
Cdd:cd03226 138 AAALLSGKDLLIFDEPTSGLDYknmERVGELIRELAAQGKAVIVITHDYEFL 189
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
322-475 |
1.36e-16 |
|
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: 79.20 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGqtvqlsyvDQGRENIDPEK- 400
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLD--------GKDITNLPPHKr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 401 ---------------TVWEVVSDGLDYIVVGQNEMPSRA--YLSAFGFKGADQQKPSKvLSGGERNRLNLALTLKQGGNL 463
Cdd:cd03300 73 pvntvfqnyalfphlTVFENIAFGLRLKKLPKAEIKERVaeALDLVQLEGYANRKPSQ-LSGGQQQRVAIARALVNEPKV 151
|
170
....*....|..
gi 512463837 464 ILLDEPTNDLDV 475
Cdd:cd03300 152 LLLDEPLGALDL 163
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
7-223 |
1.38e-16 |
|
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: 82.64 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAH-----GDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGE--------------AFLEPG 67
Cdd:COG1123 262 EVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSilfdgkdltklsrrSLRELR 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 68 ATVGILLQEP--PLNEEKTVRGNVEEGLgdifekkarfeaiaeematnytdelmeemgKLQEELDAADAWEldsKIEQAM 145
Cdd:COG1123 342 RRVQMVFQDPysSLNPRMTVGDIIAEPL------------------------------RLHGLLSRAERRE---RVAELL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 146 DALRCPP--ADEPVTHLSGGERRRVALAklllsepdllllDEPTNHLDA---ESVLWLEQHLAKYPG-AVLAVTHD---- 215
Cdd:COG1123 389 ERVGLPPdlADRYPHELSGGQRQRVAIAralalepkllilDEPTSALDVsvqAQILNLLRDLQRELGlTYLFISHDlavv 468
|
....*...
gi 512463837 216 RYFLDHVA 223
Cdd:COG1123 469 RYIADRVA 476
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
321-476 |
1.57e-16 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 79.27 E-value: 1.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 321 VVEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTVQLSYVD--QGRENID 397
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVdGEDLTDSKKDinKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 398 ---------PEKTVWEVVSDGLdyIVVGQneMP-------SRAYLSAFGFKGADQQKPSKvLSGGERNRLNLALTLKQGG 461
Cdd:COG1126 81 mvfqqfnlfPHLTVLENVTLAP--IKVKK--MSkaeaeerAMELLERVGLADKADAYPAQ-LSGGQQQRVAIARALAMEP 155
|
170
....*....|....*
gi 512463837 462 NLILLDEPTNDLDVE 476
Cdd:COG1126 156 KVMLFDEPTSALDPE 170
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
7-215 |
1.65e-16 |
|
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: 78.92 E-value: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLE-PGAT--------VGILLQEP 77
Cdd:cd03296 4 EVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGgEDATdvpvqernVGFVFQHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 78 PLNEEKTVRGNVEEGLgdifEKKARFEAIAEEMATNYTDELMEEMGklqeeldaadaweldskieqaMDALrcppADEPV 157
Cdd:cd03296 84 ALFRHMTVFDNVAFGL----RVKPRSERPPEAEIRAKVHELLKLVQ---------------------LDWL----ADRYP 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 512463837 158 THLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDA----ESVLWLEQHLAKYPGAVLAVTHD 215
Cdd:cd03296 135 AQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAkvrkELRRWLRRLHDELHVTTVFVTHD 196
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
9-234 |
1.74e-16 |
|
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: 79.08 E-value: 1.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 9 KNVRKAHG----DKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLE--------PGA---TVGIL 73
Cdd:COG1124 5 RNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDgrpvtrrrRKAfrrRVQMV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 74 LQEPP--LNEEKTVRGNVEEGLgdifeKKARFEAIAEEMAtnytdELMEEMGkLQEELdaadaweLDSKIEQamdalrcp 151
Cdd:COG1124 85 FQDPYasLHPRHTVDRILAEPL-----RIHGLPDREERIA-----ELLEQVG-LPPSF-------LDRYPHQ-------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 152 padepvthLSGGERRRVALAKLLLSEPDLLLLDEPTNHLD----AEsVLWLEQHL-AKYPGAVLAVTHDRYFLDHVAGWI 226
Cdd:COG1124 139 --------LSGGQRQRVAIARALILEPELLLLDEPTSALDvsvqAE-ILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRV 209
|
....*...
gi 512463837 227 CEVDRGKL 234
Cdd:COG1124 210 AVMQNGRI 217
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
9-214 |
2.58e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 77.61 E-value: 2.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 9 KNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEPGATVGILLQEP--------PLN 80
Cdd:PRK13539 6 EDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAchylghrnAMK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 81 EEKTVRGNVEeglgdifekkarFEAiaeemATNYTDELMEEmgklqeelDAADAWELDskieqamdalrcPPADEPVTHL 160
Cdd:PRK13539 86 PALTVAENLE------------FWA-----AFLGGEELDIA--------AALEAVGLA------------PLAHLPFGYL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 512463837 161 SGGERRRVALAKLLLSEPDLLLLDEPTNHLDAESV-LWLE---QHLAKyPGAVLAVTH 214
Cdd:PRK13539 129 SAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVaLFAElirAHLAQ-GGIVIAATH 185
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
14-214 |
3.02e-16 |
|
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: 77.53 E-value: 3.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 14 AHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEaflepgatvgILLQEPPLNEektVRGNVEEG- 92
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGR----------VLLNGGPLDF---QRDSIARGl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 93 --LGDIFEKKARFEAIaeematnytdelmeemgklqEELDAADAWELDSKIEQAMDALRCPP-ADEPVTHLSGGERRRVA 169
Cdd:cd03231 76 lyLGHAPGIKTTLSVL--------------------ENLRFWHADHSDEQVEEALARVGLNGfEDRPVAQLSAGQQRRVA 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 512463837 170 LAKLLLSEPDLLLLDEPTNHLDAESVLWLEQHLAKYP---GAVLAVTH 214
Cdd:cd03231 136 LARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCargGMVVLTTH 183
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
8-215 |
3.17e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 78.57 E-value: 3.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 8 MKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEafLEPGAT--------VGILLQEPPL 79
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE--LLAGTAplaearedTRLMFQDARL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 80 NEEKTVRGNVEEGLGDIFEKKARfeaiaeematnytdELMEEMGkLQeelDAADAWeldskieqamdalrcPPAdepvth 159
Cdd:PRK11247 93 LPWKKVIDNVGLGLKGQWRDAAL--------------QALAAVG-LA---DRANEW---------------PAA------ 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 512463837 160 LSGGERRRVALAKLLLSEPDLLLLDEPTNHLDA----------ESvLWLEQHLakypgAVLAVTHD 215
Cdd:PRK11247 134 LSGGQKQRVALARALIHRPGLLLLDEPLGALDAltriemqdliES-LWQQHGF-----TVLLVTHD 193
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
312-474 |
3.19e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 80.26 E-value: 3.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 312 PTPPRLGNQVVEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTV------ 384
Cdd:PRK13536 32 SIPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVlGVPVpararl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 385 ---QLSYVDQgRENIDPEKTVWEvvsdglDYIVVGQN-EMPSR----AYLSAFGFKGADQQKPSKV--LSGGERNRLNLA 454
Cdd:PRK13536 112 araRIGVVPQ-FDNLDLEFTVRE------NLLVFGRYfGMSTReieaVIPSLLEFARLESKADARVsdLSGGMKRRLTLA 184
|
170 180
....*....|....*....|
gi 512463837 455 LTLKQGGNLILLDEPTNDLD 474
Cdd:PRK13536 185 RALINDPQLLILDEPTTGLD 204
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-248 |
3.63e-16 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 81.80 E-value: 3.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 6 YQMKNVRKAHGD--KVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAF--------LEPGA---TVGI 72
Cdd:COG2274 474 IELENVSFRYPGdsPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILidgidlrqIDPASlrrQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 73 LLQEPPLNEEkTVRGNVeeglgdifekkarfeAIAEEMATnytdelMEEMgklqeeLDAADAWELDSKIEQAMDALrcpp 152
Cdd:COG2274 554 VLQDVFLFSG-TIRENI---------------TLGDPDAT------DEEI------IEAARLAGLHDFIEALPMGY---- 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 153 aDEPVTH----LSGGERRRVALAklllsepdllllDEPTNHLDAESVLWLEQHLAKYPG--AVLAVTHDRYFLDHvAGWI 226
Cdd:COG2274 602 -DTVVGEggsnLSGGQRQRLAIArallrnprililDEATSALDAETEAIILENLRRLLKgrTVIIIAHRLSTIRL-ADRI 679
|
250 260
....*....|....*....|..
gi 512463837 227 CEVDRGKLYpYEGNYSTYLEKK 248
Cdd:COG2274 680 IVLDKGRIV-EDGTHEELLARK 700
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
323-469 |
3.87e-16 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 78.15 E-value: 3.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 323 EVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTVQ-----------LSYVD 390
Cdd:COG1137 5 EAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLdGEDIThlpmhkrarlgIGYLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 391 QG---------RENIdpektvwevvsdgldYIVVGQNEMPSR-------AYLSAFGFKG-ADQqkPSKVLSGGERNRLNL 453
Cdd:COG1137 85 QEasifrkltvEDNI---------------LAVLELRKLSKKereerleELLEEFGITHlRKS--KAYSLSGGERRRVEI 147
|
170
....*....|....*.
gi 512463837 454 ALTLKQGGNLILLDEP 469
Cdd:COG1137 148 ARALATNPKFILLDEP 163
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
322-474 |
4.17e-16 |
|
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: 77.76 E-value: 4.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVG---------QTVQLSYVDQg 392
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGgedatdvpvQERNVGFVFQ- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 393 RENIDPEKTVWEVVSDGLDyiVVGQNEMPSRA--------YLSAFGFKGADQQKPSKvLSGGERNRLNLALTLKQGGNLI 464
Cdd:cd03296 82 HYALFRHMTVFDNVAFGLR--VKPRSERPPEAeirakvheLLKLVQLDWLADRYPAQ-LSGGQRQRVALARALAVEPKVL 158
|
170
....*....|
gi 512463837 465 LLDEPTNDLD 474
Cdd:cd03296 159 LLDEPFGALD 168
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
322-481 |
6.45e-16 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 75.81 E-value: 6.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDLEKGFDG--RVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQTVQLSYVDQGRENIDpe 399
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLIS-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 400 ktvwevvsdgldyiVVGQnempsRAYLsafgFKGADQQKPSKVLSGGERNRLNLALTLKQGGNLILLDEPTNDLDVETLS 479
Cdd:cd03247 79 --------------VLNQ-----RPYL----FDTTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITER 135
|
..
gi 512463837 480 SL 481
Cdd:cd03247 136 QL 137
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
285-498 |
6.84e-16 |
|
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: 80.48 E-value: 6.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 285 KARLERYEQmVEEAEQYKKldfeEIQIPTPPRLGNQVV--EVKDLEKGFDG--RVLiKDLSFTLPRNGIVGVIGPNGVGK 360
Cdd:TIGR02868 301 RAAAERIVE-VLDAAGPVA----EGSAPAAGAVGLGKPtlELRDLSAGYPGapPVL-DGVSLDLPPGERVAILGPSGSGK 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 361 STLFKTIVGLEQPDSGEVKVGqTVQLSYVDQG--------------------RENI---DPEKT---VWEVVS------- 407
Cdd:TIGR02868 375 STLLATLAGLLDPLQGEVTLD-GVPVSSLDQDevrrrvsvcaqdahlfdttvRENLrlaRPDATdeeLWAALErvgladw 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 408 -----DGLDYIVVgqnEMPSRaylsafgfkgadqqkpskvLSGGERNRLNLALTLKQGGNLILLDEPTNDLDVETLSS-L 481
Cdd:TIGR02868 454 lralpDGLDTVLG---EGGAR-------------------LSGGERQRLALARALLADAPILLLDEPTEHLDAETADElL 511
|
250
....*....|....*...
gi 512463837 482 ENALQNFPGCAVV-ISHD 498
Cdd:TIGR02868 512 EDLLAALSGRTVVlITHH 529
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
321-498 |
7.28e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 77.50 E-value: 7.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 321 VVEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQtvqlsyvdQGRENIDPEK 400
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNG--------RPLADWSPAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 401 ------------------TVWEVVSDGLdyIVVGQNEMPSR----AYLSAFGFKG-ADQQKPSkvLSGGERNRLNLALTL 457
Cdd:PRK13548 74 larrravlpqhsslsfpfTVEEVVAMGR--APHGLSRAEDDalvaAALAQVDLAHlAGRDYPQ--LSGGEQQRVQLARVL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 512463837 458 KQ------GGNLILLDEPTNDLDV----ETLSSLENALQNFPGCAVVISHD 498
Cdd:PRK13548 150 AQlwepdgPPRWLLLDEPTSALDLahqhHVLRLARQLAHERGLAVIVVLHD 200
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
9-214 |
7.36e-16 |
|
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: 76.24 E-value: 7.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 9 KNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEaflepgatvgILLQEPPLNEEKTVRGN 88
Cdd:TIGR01189 4 RNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGE----------VRWNGTPLAEQRDEPHE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 89 VEEGLGDIFEKKARFEAiaeematnytdelMEEMGKLQEELDAADAWELDSKIEQAMDALrcppADEPVTHLSGGERRRV 168
Cdd:TIGR01189 74 NILYLGHLPGLKPELSA-------------LENLHFWAAIHGGAQRTIEDALAAVGLTGF----EDLPAAQLSAGQQRRL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 512463837 169 ALAKLLLSEPDLLLLDEPTNHLDAESVLWLEQHLAKY---PGAVLAVTH 214
Cdd:TIGR01189 137 ALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHlarGGIVLLTTH 185
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
271-510 |
7.56e-16 |
|
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: 80.56 E-value: 7.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 271 AWvRSGQKARQAKnkARLERYEQMVEEAEQYKKLdfeeiqiPTPprlgNQVVEVKDLEKGFDG--RVLIKDLSFTLPRNG 348
Cdd:COG4618 294 GW-KQFVSARQAY--RRLNELLAAVPAEPERMPL-------PRP----KGRLSVENLTVVPPGskRPILRGVSFSLEPGE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 349 IVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVG--------------------QTVQLsyVDqG--RENI------DPEK 400
Cdd:COG4618 360 VLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDgadlsqwdreelgrhigylpQDVEL--FD-GtiAENIarfgdaDPEK 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 401 tvweVVS---------------DGLDyIVVGQNEMPsraylsafgfkgadqqkpskvLSGGERNRLNLALTLKqgGN--L 463
Cdd:COG4618 437 ----VVAaaklagvhemilrlpDGYD-TRIGEGGAR---------------------LSGGQRQRIGLARALY--GDprL 488
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 512463837 464 ILLDEPTNDLDVETLSSLENALQNF---PGCAVVISHDRWFLdRTCTHIL 510
Cdd:COG4618 489 VVLDEPNSNLDDEGEAALAAAIRALkarGATVVVITHRPSLL-AAVDKLL 537
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
282-497 |
1.01e-15 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 80.21 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 282 AKNKARLERYEQMVEEAEqykklDFEEIQIPTPPRLGNQVVEVKDLekGF---DGRVLIKDLSFTLPRNGIVGVIGPNGV 358
Cdd:COG1132 305 QRALASAERIFELLDEPP-----EIPDPPGAVPLPPVRGEIEFENV--SFsypGDRPVLKDISLTIPPGETVALVGPSGS 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 359 GKSTLFKTIVGLEQPDSGEVKV-GQTV----------QLSYVDQG--------RENI---DPEKT------------VWE 404
Cdd:COG1132 378 GKSTLVNLLLRFYDPTSGRILIdGVDIrdltleslrrQIGVVPQDtflfsgtiRENIrygRPDATdeeveeaakaaqAHE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 405 VVS---DGLDYiVVGQNempsraylsafgfkGADqqkpskvLSGGERNRLNLA--LtLKqggN--LILLDEPTNDLDVET 477
Cdd:COG1132 458 FIEalpDGYDT-VVGER--------------GVN-------LSGGQRQRIAIAraL-LK---DppILILDEATSALDTET 511
|
250 260
....*....|....*....|..
gi 512463837 478 LSSLENALQNF-PGC-AVVISH 497
Cdd:COG1132 512 EALIQEALERLmKGRtTIVIAH 533
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
323-470 |
1.04e-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: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 323 EVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTVQ-----------LSYVD 390
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFdGEDITglpphriarlgIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 391 QGReNIDPEKTVWEvvsdgldyivvgqN-EMPSRaylsAFGFKGADQQKPSKV-----------------LSGGERNRLN 452
Cdd:COG0410 85 EGR-RIFPSLTVEE-------------NlLLGAY----ARRDRAEVRADLERVyelfprlkerrrqragtLSGGEQQMLA 146
|
170
....*....|....*...
gi 512463837 453 LALTLKQGGNLILLDEPT 470
Cdd:COG0410 147 IGRALMSRPKLLLLDEPS 164
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
16-234 |
1.06e-15 |
|
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: 80.19 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 16 GDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEaflepgatvgILLQEPPLNEEK------------ 83
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGS----------ILINGVDLSDLDpaswrrqiawvp 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 84 --------TVRGNVeeGLGdifekkarfeaiaeemATNYTDElmeemgKLQEELDAADAWELdskIEQAMDALrcppaDE 155
Cdd:COG4988 418 qnpylfagTIRENL--RLG----------------RPDASDE------ELEAALEAAGLDEF---VAALPDGL-----DT 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 156 PV----THLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAESVLWLEQHLAKYPG--AVLAVTHDRYFLDHvAGWICEV 229
Cdd:COG4988 466 PLgeggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKgrTVILITHRLALLAQ-ADRILVL 544
|
....*
gi 512463837 230 DRGKL 234
Cdd:COG4988 545 DDGRI 549
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
7-214 |
1.15e-15 |
|
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: 76.66 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSngeaflePGATVGILLQEpplneektvR 86
Cdd:COG1119 5 ELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPT-------YGNDVRLFGER---------R 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 87 GNVeeglgDIFEKKARFEAIAEEMATNYT-DELMEEM---GK-----LQEELDAADAweldSKIEQAMDALRCPP-ADEP 156
Cdd:COG1119 69 GGE-----DVWELRKRIGLVSPALQLRFPrDETVLDVvlsGFfdsigLYREPTDEQR----ERARELLELLGLAHlADRP 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 512463837 157 VTHLSGGERRRV----ALAKlllsepdllllDEPTNHLD---AESVLWLEQHLAKYPG-AVLAVTH 214
Cdd:COG1119 140 FGTLSQGEQRRVliarALVKdpel----lilDEPTAGLDlgaRELLLALLDKLAAEGApTLVLVTH 201
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
322-499 |
1.17e-15 |
|
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: 79.64 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDLEKGFDGR-VLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTV----------QLSYV 389
Cdd:TIGR02857 322 LEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVnGVPLadadadswrdQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 390 DQG--------RENI---DPEKTVWEVVsdgldyivvgqnEMPSRAYLSAFgFKGADQQKPSKV------LSGGERNRLN 452
Cdd:TIGR02857 402 PQHpflfagtiAENIrlaRPDASDAEIR------------EALERAGLDEF-VAALPQGLDTPIgeggagLSGGQAQRLA 468
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 512463837 453 LALTLKQGGNLILLDEPTNDLDVETLSSLENALQNFPGCA--VVISHDR 499
Cdd:TIGR02857 469 LARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRtvLLVTHRL 517
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
321-486 |
1.42e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 75.68 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 321 VVEVKDL--EKGfdGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV---GQTV-----QLSYVd 390
Cdd:PRK13539 2 MLEGEDLacVRG--GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLdggDIDDpdvaeACHYL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 391 qGREN-IDPEKTvwevVSDGLDY--IVVGQNEMPSRAYLSAFGFKGAdQQKPSKVLSGGERNRLNLALTLKQGGNLILLD 467
Cdd:PRK13539 79 -GHRNaMKPALT----VAENLEFwaAFLGGEELDIAAALEAVGLAPL-AHLPFGYLSAGQKRRVALARLLVSNRPIWILD 152
|
170
....*....|....*....
gi 512463837 468 EPTNDLDVETLSSLENALQ 486
Cdd:PRK13539 153 EPTAALDAAAVALFAELIR 171
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
285-521 |
1.48e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 79.47 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 285 KARLERYEQMVEEAEQYKKLDFEEIQIPTPPrlgNQVVEVKDLE-KGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTL 363
Cdd:COG4178 329 RATVDRLAGFEEALEAADALPEAASRIETSE---DGALALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTL 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 364 FKTIVGLEQPDSGEVKV--GQTV----QLSYVDQG--RENI--------DPEKTVWEVVSD-GLDYIVvgqnempSRayl 426
Cdd:COG4178 406 LRAIAGLWPYGSGRIARpaGARVlflpQRPYLPLGtlREALlypataeaFSDAELREALEAvGLGHLA-------ER--- 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 427 safgfkgADQQKP-SKVLSGGERNRLNLALTLKQGGNLILLDEPTNDLDVETLSSLENALQN-FPGCAVV-ISHdRWFLD 503
Cdd:COG4178 476 -------LDEEADwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREeLPGTTVIsVGH-RSTLA 547
|
250
....*....|....*...
gi 512463837 504 RTCTHILAWEGNfeeGKW 521
Cdd:COG4178 548 AFHDRVLELTGD---GSW 562
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-223 |
1.54e-15 |
|
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: 76.01 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 5 IYQMKNVRKAHGDK----VILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEP-------------- 66
Cdd:cd03257 1 LLEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdllklsrrlrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 67 GATVGILLQEPP--LNEEKTVRGNVEEGL---GDIFEKKARFEAIAEEMatnytdelmeemgklqEELDAADAWeLDSKI 141
Cdd:cd03257 81 RKEIQMVFQDPMssLNPRMTIGEQIAEPLrihGKLSKKEARKEAVLLLL----------------VGVGLPEEV-LNRYP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 142 EQamdalrcppadepvthLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAES---VLWLEQHLAK-YPGAVLAVTHD-- 215
Cdd:cd03257 144 HE----------------LSGGQRQRVAIARALALNPKLLIADEPTSALDVSVqaqILDLLKKLQEeLGLTLLFITHDlg 207
|
250
....*....|
gi 512463837 216 --RYFLDHVA 223
Cdd:cd03257 208 vvAKIADRVA 217
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
312-477 |
1.62e-15 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 76.64 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 312 PTPPRLGNQV-VEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQTVqlsyVD 390
Cdd:PRK11247 2 MNTARLNQGTpLLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAP----LA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 391 QGRENID---------PEKTVWEVVSDGLDyivvGQNEMPSRAYLSAFGFKGADQQKPSkVLSGGERNRLNLALTLKQGG 461
Cdd:PRK11247 78 EAREDTRlmfqdarllPWKKVIDNVGLGLK----GQWRDAALQALAAVGLADRANEWPA-ALSGGQKQRVALARALIHRP 152
|
170
....*....|....*.
gi 512463837 462 NLILLDEPTNDLDVET 477
Cdd:PRK11247 153 GLLLLDEPLGALDALT 168
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
7-234 |
1.98e-15 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 75.47 E-value: 1.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAH-GDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAF--------LEPGA------TVG 71
Cdd:COG2884 3 RFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLvngqdlsrLKRREipylrrRIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 72 ILLQEPPLNEEKTVRGNVeeglgdifekkarfeAIAeematnytdelMEEMGKLQEELDAadaweldsKIEQAMDAL--- 148
Cdd:COG2884 83 VVFQDFRLLPDRTVYENV---------------ALP-----------LRVTGKSRKEIRR--------RVREVLDLVgls 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 149 ---RCPPAdepvtHLSGGERRRVA------------LAklllsepdllllDEPTNHLDAESVLWLEQHLAKY--PG-AVL 210
Cdd:COG2884 129 dkaKALPH-----ELSGGEQQRVAiaralvnrpellLA------------DEPTGNLDPETSWEIMELLEEInrRGtTVL 191
|
250 260
....*....|....*....|....
gi 512463837 211 AVTHDRYFLDHVAGWICEVDRGKL 234
Cdd:COG2884 192 IATHDLELVDRMPKRVLELEDGRL 215
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-233 |
2.03e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 77.15 E-value: 2.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 1 MGEFIYQMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFL--EP--------GATV 70
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcgEPvpsrarhaRQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 71 GILLQEPPLNEEKTVRGNVEeglgdIFekkARFEAIAEEMATNYTDELMeEMGKLQEEldaadaweldskieqamdalrc 150
Cdd:PRK13537 83 GVVPQFDNLDPDFTVRENLL-----VF---GRYFGLSAAAARALVPPLL-EFAKLENK---------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 151 ppADEPVTHLSGGERRRVALAKLLLSEPDLLLLDEPTNHLD--AESVLW--LEQHLAKyPGAVLAVTHDRYFLDHVAGWI 226
Cdd:PRK13537 132 --ADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDpqARHLMWerLRSLLAR-GKTILLTTHFMEEAERLCDRL 208
|
....*..
gi 512463837 227 CEVDRGK 233
Cdd:PRK13537 209 CVIEEGR 215
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
17-234 |
2.88e-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: 75.20 E-value: 2.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 17 DKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEPG-----------ATVGILLQEPPLNEeKTV 85
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpisqyehkylhSKVSLVGQEPVLFA-RSL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 86 RGNVEEGLGDIfekkarfeaiaeematnytdelmeEMGKLQEELDAADAWELDSKIEQAMDAlrcpPADEPVTHLSGGER 165
Cdd:cd03248 105 QDNIAYGLQSC------------------------SFECVKEAAQKAHAHSFISELASGYDT----EVGEKGSQLSGGQK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 512463837 166 RRVALAKLLLSEPDLLLLDEPTNHLDAESVLWLEQHLAKYPG--AVLAVTHDRYFLDHvAGWICEVDRGKL 234
Cdd:cd03248 157 QRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPErrTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
16-214 |
3.20e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 74.46 E-value: 3.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 16 GDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEaflepgatvgILLQEPPLNeektvrgnveeglgd 95
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGE----------VLWQGEPIR--------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 96 ifekKARfEAIAEEM-----ATNYTDELM-EE----MGKLQEELDAADAWeldskieQAMDAL----RcppADEPVTHLS 161
Cdd:PRK13538 67 ----RQR-DEYHQDLlylghQPGIKTELTaLEnlrfYQRLHGPGDDEALW-------EALAQVglagF---EDVPVRQLS 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 512463837 162 GGERRRVALAKLLLSEPDLLLLDEPTNHLDAESVLWLEQHLAKYP---GAVLAVTH 214
Cdd:PRK13538 132 AGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAeqgGMVILTTH 187
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
321-497 |
3.45e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 74.46 E-value: 3.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 321 VVEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTV---------QLSYVd 390
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWqGEPIrrqrdeyhqDLLYL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 391 qGREN-IDPEKTVWEvvsdGLDY---IVVGQNEMPSRAYLSAFGFKG-ADQqkPSKVLSGGERNRLNLALTLKQGGNLIL 465
Cdd:PRK13538 80 -GHQPgIKTELTALE----NLRFyqrLHGPGDDEALWEALAQVGLAGfEDV--PVRQLSAGQQRRVALARLWLTRAPLWI 152
|
170 180 190
....*....|....*....|....*....|....*..
gi 512463837 466 LDEPTNDLD---VETLSSL--ENALQNfpGCAVVISH 497
Cdd:PRK13538 153 LDEPFTAIDkqgVARLEALlaQHAEQG--GMVILTTH 187
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
323-485 |
3.62e-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: 74.45 E-value: 3.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 323 EVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQTVQLSYVDQGRENI------ 396
Cdd:cd03231 2 EADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLlylgha 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 397 DPEKTVWEVVSDGLDYIVVGQNEMPSRAyLSAFGFKGAdQQKPSKVLSGGERNRLNLALTLKQGGNLILLDEPTNDLDVE 476
Cdd:cd03231 82 PGIKTTLSVLENLRFWHADHSDEQVEEA-LARVGLNGF-EDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
....*....
gi 512463837 477 TLSSLENAL 485
Cdd:cd03231 160 GVARFAEAM 168
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
9-215 |
4.62e-15 |
|
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: 74.78 E-value: 4.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 9 KNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFL--EP-------------GATVGIL 73
Cdd:COG4181 16 KTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLagQDlfaldedararlrARHVGFV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 74 LQEPPLNEEKTVRGNV-----EEGLGDifekkarfeaiAEEMATnytdELMEEMGkLQEELDAAdaweldskieqamdal 148
Cdd:COG4181 96 FQSFQLLPTLTALENVmlpleLAGRRD-----------ARARAR----ALLERVG-LGHRLDHY---------------- 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 512463837 149 rcpPAdepvtHLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDA---ESVLWL------EQHLAkypgAVLaVTHD 215
Cdd:COG4181 144 ---PA-----QLSGGEQQRVALARAFATEPAILFADEPTGNLDAatgEQIIDLlfelnrERGTT----LVL-VTHD 206
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
7-224 |
4.97e-15 |
|
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: 74.91 E-value: 4.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAHGD-KVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEPGAT--------------VG 71
Cdd:cd03256 2 EVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklkgkalrqlrrqIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 72 ILLQEPPLNEEKTVRGNVEEG-LGDI---------FEKKARFEAIaeematnytdELMEEMGklqeeldaadaweLDSKI 141
Cdd:cd03256 82 MIFQQFNLIERLSVLENVLSGrLGRRstwrslfglFPKEEKQRAL----------AALERVG-------------LLDKA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 142 EQamdalrcpPADEpvthLSGGERRRVALAKLLLSEPDLLLLDEPTNHLD---AESVLWLEQHLAKYPG-AVLAVTHD-- 215
Cdd:cd03256 139 YQ--------RADQ----LSGGQQQRVAIARALMQQPKLILADEPVASLDpasSRQVMDLLKRINREEGiTVIVSLHQvd 206
|
250
....*....|.
gi 512463837 216 --RYFLDHVAG 224
Cdd:cd03256 207 laREYADRIVG 217
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
333-514 |
5.22e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 75.21 E-value: 5.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 333 GRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKtIVGLEQPDS-GEVKVGQTV-----------QLSYVDQGRENIDpEK 400
Cdd:PRK10575 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLK-MLGRHQPPSeGEILLDAQPleswsskafarKVAYLPQQLPAAE-GM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 401 TVWEVVSDGldyivvgqnEMPSRAYLSAFGfkGADQQKPSKV----------------LSGGERNRLNLALTLKQGGNLI 464
Cdd:PRK10575 101 TVRELVAIG---------RYPWHGALGRFG--AADREKVEEAislvglkplahrlvdsLSGGERQRAWIAMLVAQDSRCL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 512463837 465 LLDEPTNDLD----VETLsSLENALQNFPGCAVV-ISHDRWFLDRTCTHILAWEG 514
Cdd:PRK10575 170 LLDEPTSALDiahqVDVL-ALVHRLSQERGLTVIaVLHDINMAARYCDYLVALRG 223
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-191 |
6.23e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 74.73 E-value: 6.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLE-------PGA----TVGILLQ 75
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDgldvattPSRelakRLAILRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 76 EPPLNEEKTVRGNVEEGlgdifekkaRFEaiaeematnYTDelmeemGKLQEElDAAdaweldsKIEQAMDALR-CPPAD 154
Cdd:COG4604 83 ENHINSRLTVRELVAFG---------RFP---------YSK------GRLTAE-DRE-------IIDEAIAYLDlEDLAD 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 512463837 155 EPVTHLSGGERRR--VA-----------LaklllsepdllllDEPTNHLD 191
Cdd:COG4604 131 RYLDELSGGQRQRafIAmvlaqdtdyvlL-------------DEPLNNLD 167
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
308-477 |
6.77e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 73.84 E-value: 6.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 308 EIQIPTPPRLGnQVVEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLE--QPDSGEVKVgQTVQ 385
Cdd:COG2401 18 SSVLDLSERVA-IVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDV-PDNQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 386 LSYVDQGRENIDPEKTVWEVVsdgldyivvgqnEMPSRAYLS-AFGFKgadqqKPSKVLSGGERNRLNLALTLKQGGNLI 464
Cdd:COG2401 96 FGREASLIDAIGRKGDFKDAV------------ELLNAVGLSdAVLWL-----RRFKELSTGQKFRFRLALLLAERPKLL 158
|
170
....*....|...
gi 512463837 465 LLDEPTNDLDVET 477
Cdd:COG2401 159 VIDEFCSHLDRQT 171
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
7-233 |
6.92e-15 |
|
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: 72.99 E-value: 6.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFL-------------EPGATVGIL 73
Cdd:cd03229 2 ELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIdgedltdledelpPLRRRIGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 74 LQEPPLNEEKTVRGNVEEGlgdifekkarfeaiaeematnytdelmeemgklqeeldaadaweldskieqamdalrcppa 153
Cdd:cd03229 82 FQDFALFPHLTVLENIALG------------------------------------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 154 depvthLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAE---SVLWLEQHLAKYPG-AVLAVTHDRYFLDHVAGWICEV 229
Cdd:cd03229 101 ------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPItrrEVRALLKSLQAQLGiTVVLVTHDLDEAARLADRVVVL 174
|
....
gi 512463837 230 DRGK 233
Cdd:cd03229 175 RDGK 178
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
321-498 |
8.29e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 74.73 E-value: 8.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 321 VVEVKDLEKGF-DGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEV---------------KVGQTV 384
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVlikgepikydkksllEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 385 QLSYVDQGRENIDPekTVWEVVSDGLDYIVVGQNEMPSRAY--LSAFGFKGADqQKPSKVLSGGERNRLNLALTLKQGGN 462
Cdd:PRK13639 81 GIVFQNPDDQLFAP--TVEEDVAFGPLNLGLSKEEVEKRVKeaLKAVGMEGFE-NKPPHHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 512463837 463 LILLDEPTNDLDVETLSSLENALQ--NFPGCAVVIS-HD 498
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYdlNKEGITIIIStHD 196
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
10-214 |
8.89e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 75.64 E-value: 8.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 10 NVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFL----EPG------ATVGILLQEPPL 79
Cdd:PRK13536 46 GVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVlgvpVPArarlarARIGVVPQFDNL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 80 NEEKTVRGNVEEgLGDIFEKKAR-FEAIAEEMatnytdelmeemgklqeeLDAAdawELDSKieqamdalrcppADEPVT 158
Cdd:PRK13536 126 DLEFTVRENLLV-FGRYFGMSTReIEAVIPSL------------------LEFA---RLESK------------ADARVS 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 159 HLSGGERRRVALAKLLLSEPDLLLLDEPTNHLD--AESVLW--LEQHLAKyPGAVLAVTH 214
Cdd:PRK13536 172 DLSGGMKRRLTLARALINDPQLLILDEPTTGLDphARHLIWerLRSLLAR-GKTILLTTH 230
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
332-497 |
9.20e-15 |
|
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: 72.19 E-value: 9.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 332 DGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVgqtvqlsyvdqgrenidPEKtvwevvsDGLD 411
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM-----------------PEG-------EDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 412 YIvvgqnemPSRAYLSAFGFKgadQQ--KP-SKVLSGGERNRLNLALTLKQGGNLILLDEPTNDLDVETLSSLENALQNF 488
Cdd:cd03223 68 FL-------PQRPYLPLGTLR---EQliYPwDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKEL 137
|
170
....*....|
gi 512463837 489 pGCAVV-ISH 497
Cdd:cd03223 138 -GITVIsVGH 146
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
313-518 |
1.11e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 74.00 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 313 TPPRLGNQVVEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQTvQLSYVDQ- 391
Cdd:COG4674 2 SLDTMHGPILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGT-DLTGLDEh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 392 -------GRE----NIDPEKTVWEvvsdGLDyIVVGQNempsRAYLSAFGFK------------------GADQQKPSKV 442
Cdd:COG4674 81 eiarlgiGRKfqkpTVFEELTVFE----NLE-LALKGD----RGVFASLFARltaeerdrieevletiglTDKADRLAGL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 443 LSGGERNRLNLALTLKQGGNLILLDEPTNDL-DVET--LSSLENALQnfPGCAV-VISHDRWFLDR-----TCTH---IL 510
Cdd:COG4674 152 LSHGQKQWLEIGMLLAQDPKLLLLDEPVAGMtDAETerTAELLKSLA--GKHSVvVVEHDMEFVRQiarkvTVLHqgsVL 229
|
....*...
gi 512463837 511 AwEGNFEE 518
Cdd:COG4674 230 A-EGSLDE 236
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-498 |
1.12e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 76.49 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 21 LDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEP------------GATVGILLQEPPLNEEKTVRGN 88
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGqemrfasttaalAAGVAIIYQELHLVPEMTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 89 VEEG-----LGDIFEKKARFEAiaeematnytdelMEEMGKLQEELDaadaweldskieqamdalrcppADEPVTHLSGG 163
Cdd:PRK11288 100 LYLGqlphkGGIVNRRLLNYEA-------------REQLEHLGVDID----------------------PDTPLKYLSIG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 164 ERRRVALAKLLLSEPDLLLLDEPTNHLDA---ESVLWLEQHLAKYPGAVLAVTHdRyfLDhvagwicEVDrgklypyegn 240
Cdd:PRK11288 145 QRQMVEIAKALARNARVIAFDEPTSSLSAreiEQLFRVIRELRAEGRVILYVSH-R--ME-------EIF---------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 241 ystylekkaerlevagkkdaklqkRLKDELAWVRSGQKARQAKNKARLERyEQMVEEAEQYkklDFEEIQIPTPPRLGNQ 320
Cdd:PRK11288 205 ------------------------ALCDAITVFKDGRYVATFDDMAQVDR-DQLVQAMVGR---EIGDIYGYRPRPLGEV 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 321 VVEVKDLEkgfdGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTVQL-SYVDQGRENID- 397
Cdd:PRK11288 257 RLRLDGLK----GPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLdGKPIDIrSPRDAIRAGIMl 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 398 -PE--KtvwevvSDGldyIV----VGQN-EMPSRAYLSAFGF--------KGADQQ-------KPS-----KVLSGGERN 449
Cdd:PRK11288 333 cPEdrK------AEG---IIpvhsVADNiNISARRHHLRAGClinnrweaENADRFirslnikTPSreqliMNLSGGNQQ 403
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 512463837 450 RLNLALTLKQGGNLILLDEPTNDLDVETLSSLENALQNFP--GCAV-VISHD 498
Cdd:PRK11288 404 KAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAaqGVAVlFVSSD 455
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
317-474 |
1.20e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 74.28 E-value: 1.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 317 LGNQVVEVKDLEKGFDG--RVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQTVqLSyvdqgre 394
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV-LS------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 395 nidpEKTVWEV-------------------VSD----GLDYIVVGQNEMPSR--AYLSAFGFKGADQQKPSKvLSGGERN 449
Cdd:PRK13635 73 ----EETVWDVrrqvgmvfqnpdnqfvgatVQDdvafGLENIGVPREEMVERvdQALRQVGMEDFLNREPHR-LSGGQKQ 147
|
170 180
....*....|....*....|....*
gi 512463837 450 RLNLALTLKQGGNLILLDEPTNDLD 474
Cdd:PRK13635 148 RVAIAGVLALQPDIIILDEATSMLD 172
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-227 |
1.50e-14 |
|
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: 73.55 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 30 PGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEaFLEPGATVGILlqepplneeKTVRGNveeGLGDIFEKkARFEAIAEE 109
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGK-FDDPPDWDEIL---------DEFRGS---ELQNYFTK-LLEGDVKVI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 110 MATNYTDELMEEM-GKLQEELDAADawELDsKIEQAMDALRCPPA-DEPVTHLSGGERRRVALAKLLLSEPDLLLLDEPT 187
Cdd:cd03236 91 VKPQYVDLIPKAVkGKVGELLKKKD--ERG-KLDELVDQLELRHVlDRNIDQLSGGELQRVAIAAALARDADFYFFDEPS 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 512463837 188 NHLDAE---SVLWLEQHLAKYPGAVLAVTHDRYFLDHVAGWIC 227
Cdd:cd03236 168 SYLDIKqrlNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIH 210
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
339-514 |
1.84e-14 |
|
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: 73.69 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 339 DLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEV----------------KVGQTVQLSYVDqGRENIDPEKTV 402
Cdd:TIGR02769 29 NVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVsfrgqdlyqldrkqrrAFRRDVQLVFQD-SPSAVNPRMTV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 403 WEVVSDGL-DYIVVGQNEMPSR--AYLSAFGFKGADQQKPSKVLSGGERNRLNLALTLKQGGNLILLDEPTNDLDV---- 475
Cdd:TIGR02769 108 RQIIGEPLrHLTSLDESEQKARiaELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMvlqa 187
|
170 180 190
....*....|....*....|....*....|....*....
gi 512463837 476 ETLSSLENALQNFPGCAVVISHDRWFLDRTCTHILAWEG 514
Cdd:TIGR02769 188 VILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDK 226
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
5-216 |
2.19e-14 |
|
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: 72.38 E-value: 2.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 5 IYQMKNVRKAHGDK----VILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEpgatvGILLQEPPLN 80
Cdd:TIGR02211 1 LLKCENLGKRYQEGkldtRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFN-----GQSLSKLSSN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 81 EEKTVRgnvEEGLGDIFEKK---ARFEAIAEEMatnytdelmeeMGKLQEELDAADAWELdskieqAMDALRCPPADEPV 157
Cdd:TIGR02211 76 ERAKLR---NKKLGFIYQFHhllPDFTALENVA-----------MPLLIGKKSVKEAKER------AYEMLEKVGLEHRI 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 512463837 158 TH----LSGGERRRVALAKLLLSEPDLLLLDEPTNHLD---AESVLWLEQHLAKYPG-AVLAVTHDR 216
Cdd:TIGR02211 136 NHrpseLSGGERQRVAIARALVNQPSLVLADEPTGNLDnnnAKIIFDLMLELNRELNtSFLVVTHDL 202
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
338-396 |
2.49e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 72.81 E-value: 2.49e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 512463837 338 KDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQTV------------QLSyvdqGRENI 396
Cdd:COG1134 43 KDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVsallelgagfhpELT----GRENI 109
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
9-223 |
2.49e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 73.12 E-value: 2.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 9 KNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFL-----------EPGATVGILLQEP 77
Cdd:PRK11231 6 ENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLgdkpismlssrQLARRLALLPQHH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 78 PLNEEKTVRGNVEEGlgdifekkarfeaiaeematnyTDELMEEMGKLQEElDAAdaweldsKIEQAMDALRCPP-ADEP 156
Cdd:PRK11231 86 LTPEGITVRELVAYG----------------------RSPWLSLWGRLSAE-DNA-------RVNQAMEQTRINHlADRR 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 512463837 157 VTHLSGGERRRVALAKLLLSEPDLLLLDEPTNHLD----AEsVLWLEQHLAKYPGAVLAVTHD-----RYfLDHVA 223
Cdd:PRK11231 136 LTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDinhqVE-LMRLMRELNTQGKTVVTVLHDlnqasRY-CDHLV 209
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
329-510 |
2.64e-14 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 72.18 E-value: 2.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 329 KGFDGRVLI-KDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQTV------------QLSyvdqGREN 395
Cdd:cd03220 29 KGEVGEFWAlKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVssllglgggfnpELT----GREN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 396 IDPEKTVWevvsdGLDyivvgQNEMPSR-AYLSAFGFKGADQQKPSKVLSGGERNRLNLALTLKQGGNLILLDEPTNDLD 474
Cdd:cd03220 105 IYLNGRLL-----GLS-----RKEIDEKiDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGD 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 512463837 475 VETLSSLENALQNF--PGCAVVI-SHDRWFLDRTCTHIL 510
Cdd:cd03220 175 AAFQEKCQRRLRELlkQGKTVILvSHDPSSIKRLCDRAL 213
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
334-510 |
2.79e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 73.18 E-value: 2.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 334 RVLiKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVK-----VGQ-----------TVQLSYVDqGRENID 397
Cdd:PRK10419 26 TVL-NNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSwrgepLAKlnraqrkafrrDIQMVFQD-SISAVN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 398 PEKTVWEVVSDGLDYIVV---GQNEMPSRAYLSAFGFKGADQQKPSKVLSGGERNRLNLALTLKQGGNLILLDEPTNDLD 474
Cdd:PRK10419 104 PRKTVREIIREPLRHLLSldkAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 512463837 475 V----ETLSSLENALQNFPGCAVVISHDRWFLDRTCTHIL 510
Cdd:PRK10419 184 LvlqaGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVM 223
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
12-108 |
2.87e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 72.42 E-value: 2.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 12 RKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGE--------AFLEPGAtvgillqepPLNEEK 83
Cdd:COG1134 33 RTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRvevngrvsALLELGA---------GFHPEL 103
|
90 100
....*....|....*....|....*....
gi 512463837 84 TVRGNVEEG---LG-DIFEKKARFEAIAE 108
Cdd:COG1134 104 TGRENIYLNgrlLGlSRKEIDEKFDEIVE 132
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
321-474 |
2.96e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 73.69 E-value: 2.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 321 VVEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTV---------QLSYVD 390
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcGEPVpsrarharqRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 391 QgRENIDPEKTVWEvvsdglDYIVVGQNEMPSRAYLSA-----FGFKGADQQKPSKV--LSGGERNRLNLALTLKQGGNL 463
Cdd:PRK13537 87 Q-FDNLDPDFTVRE------NLLVFGRYFGLSAAAARAlvpplLEFAKLENKADAKVgeLSGGMKRRLTLARALVNDPDV 159
|
170
....*....|.
gi 512463837 464 ILLDEPTNDLD 474
Cdd:PRK13537 160 LVLDEPTTGLD 170
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
7-193 |
3.06e-14 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 71.84 E-value: 3.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAHGDKVILDNVTMAFYPGAkIGVVGPNGAGKSSILKIMAGLDQPS------NGEAFLEPG----ATVGILLQE 76
Cdd:cd03264 2 QLENLTKRYGKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSsgtiriDGQDVLKQPqklrRRIGYLPQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 77 PPLNEEKTVRgnveeglgdifekkarfeaiaeematnytdELMEEMGKLQEELDAadawELDSKIEQAMDALRCPP-ADE 155
Cdd:cd03264 81 FGVYPNFTVR------------------------------EFLDYIAWLKGIPSK----EVKARVDEVLELVNLGDrAKK 126
|
170 180 190
....*....|....*....|....*....|....*...
gi 512463837 156 PVTHLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAE 193
Cdd:cd03264 127 KIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPE 164
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
321-380 |
3.35e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 73.22 E-value: 3.35e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 321 VVEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV 380
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLW 60
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
30-215 |
4.33e-14 |
|
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: 71.56 E-value: 4.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 30 PGAKIGVVGPNGAGKSSILKIMAGLDQPSNGE--------------AFLEPGA-TVGILLQEPPLNEEKTVRGNVEEGLG 94
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTivlngtvlfdsrkkINLPPQQrKIGLVFQQYALFPHLNVRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 95 DIFEKKARFEAiaeematnytDELMEEMGkLQEELDAadaweldskieqamdalrcppadePVTHLSGGERRRVALAKLL 174
Cdd:cd03297 102 RKRNREDRISV----------DELLDLLG-LDHLLNR------------------------YPAQLSGGEKQRVALARAL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 512463837 175 LSEPDLLLLDEPTNHLDAESVLWLEQHL----AKYPGAVLAVTHD 215
Cdd:cd03297 147 AAQPELLLLDEPFSALDRALRLQLLPELkqikKNLNIPVIFVTHD 191
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
304-496 |
4.46e-14 |
|
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: 71.04 E-value: 4.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 304 LDFEEIQIPTPPRLGNqvvevkdlekgfDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGL--EQPDSGEVKV- 380
Cdd:cd03213 4 LSFRNLTVTVKSSPSK------------SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLIn 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 381 GQTV-------QLSYVDQgrENI-DPEKTVWEVvsdgLDYIvvgqnempsrAYLsafgfkgadqqkpsKVLSGGERNRLN 452
Cdd:cd03213 72 GRPLdkrsfrkIIGYVPQ--DDIlHPTLTVRET----LMFA----------AKL--------------RGLSGGERKRVS 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 512463837 453 LALTLKQGGNLILLDEPTNDLD-------VETLSSLENAlqnfpGCAVVIS 496
Cdd:cd03213 122 IALELVSNPSLLFLDEPTSGLDsssalqvMSLLRRLADT-----GRTIICS 167
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
339-474 |
5.85e-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: 5.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 339 DLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQtVQLSYVDQGR--------EN-----IDPEKTVWEV 405
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING-VDVTAAPPADrpvsmlfqENnlfahLTVEQNVGLG 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 512463837 406 VSDGLDYIVVGQNEMpsRAYLSAFGFKGADQQKPSKvLSGGERNRLNLALTLKQGGNLILLDEPTNDLD 474
Cdd:cd03298 95 LSPGLKLTAEDRQAI--EVALARVGLAGLEKRLPGE-LSGGERQRVALARVLVRDKPVLLLDEPFAALD 160
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
322-498 |
6.24e-14 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 71.60 E-value: 6.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDLEKGFDGRVLiKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTV--------QLSYVDQG 392
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLnGKDItnlppekrDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 393 REnIDPEKTVWEVVSDGLDYIVVGQNEMPSRAYLSAfGFKGADQ---QKPsKVLSGGERNRLNLALTLKQGGNLILLDEP 469
Cdd:cd03299 80 YA-LFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIA-EMLGIDHllnRKP-ETLSGGEQQRVAIARALVVNPKILLLDEP 156
|
170 180 190
....*....|....*....|....*....|...
gi 512463837 470 TNDLDVETLSSLENAL----QNFPGCAVVISHD 498
Cdd:cd03299 157 FSALDVRTKEKLREELkkirKEFGVTVLHVTHD 189
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
336-474 |
6.49e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 71.95 E-value: 6.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 336 LIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTVQLSYVDQGRENI-----DPEK-----TVWE 404
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIdGITISKENLKEIRKKIgiifqNPDNqfigaTVED 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 512463837 405 VVSDGLDYIVVGQNEMPSRAYLSA--FGFKGADQQKPSKvLSGGERNRLNLALTLKQGGNLILLDEPTNDLD 474
Cdd:PRK13632 104 DIAFGLENKKVPPKKMKDIIDDLAkkVGMEDYLDKEPQN-LSGGQKQRVAIASVLALNPEIIIFDESTSMLD 174
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
7-216 |
7.14e-14 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 73.21 E-value: 7.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEpGAT----------VGILLQE 76
Cdd:COG3842 7 ELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLD-GRDvtglppekrnVGMVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 77 PPLNEEKTVRGNVEEGLGDIFEKKARFEAIAEEMAtnytdELMEemgklqeeldaadaweldskieqaMDALrcppADEP 156
Cdd:COG3842 86 YALFPHLTVAENVAFGLRMRGVPKAEIRARVAELL-----ELVG------------------------LEGL----ADRY 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 512463837 157 VTHLSGGERRRVALAklllsepdllllDEPTNHLDA---ESV-LWLEQHLAKYPGAVLAVTHDR 216
Cdd:COG3842 133 PHQLSGGQQQRVALAralapeprvlllDEPLSALDAklrEEMrEELRRLQRELGITFIYVTHDQ 196
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
7-475 |
1.03e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 73.51 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEpGATV-----------GILL- 74
Cdd:COG1129 6 EMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLD-GEPVrfrsprdaqaaGIAIi 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 75 -QEPPLNEEKTVRGNVeeGLGDIFEKKA--RFEAIAEEmatnyTDELMEEMGklqeeldaadaWELDskieqamdalrcp 151
Cdd:COG1129 85 hQELNLVPNLSVAENI--FLGREPRRGGliDWRAMRRR-----ARELLARLG-----------LDID------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 152 pADEPVTHLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAESVlwleQHL--------AKypG-AVLAVTHdryFLDhv 222
Cdd:COG1129 134 -PDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREV----ERLfriirrlkAQ--GvAIIYISH---RLD-- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 223 agwicEVdrgklypyegnystylekkaerLEVAgkkdaklqkrlkDELAWVRSGQKARQAK----NKARLERYeqMVEEa 298
Cdd:COG1129 202 -----EV----------------------FEIA------------DRVTVLRDGRLVGTGPvaelTEDELVRL--MVGR- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 299 eqykklDFEEIQIPTPPRLGNQVVEVKDLEKGfdGRVliKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEV 378
Cdd:COG1129 240 ------ELEDLFPKRAAAPGEVVLEVEGLSVG--GVV--RDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEI 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 379 KV-GQTVQLS-----------YV--DQGRENIDPEKTVWE-----VVSDGLDYIVVGQNEMPSRA--YLSAFGFKGADQQ 437
Cdd:COG1129 310 RLdGKPVRIRsprdairagiaYVpeDRKGEGLVLDLSIREnitlaSLDRLSRGGLLDRRRERALAeeYIKRLRIKTPSPE 389
|
490 500 510
....*....|....*....|....*....|....*...
gi 512463837 438 KPSKVLSGGERNRLNLALTLKQGGNLILLDEPTNDLDV 475
Cdd:COG1129 390 QPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDV 427
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
319-498 |
1.15e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 71.31 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 319 NQVVEVKDLEKGF-DGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTVQLSYVDQGRENI 396
Cdd:PRK13647 2 DNIIEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVmGREVNAENEKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 397 -----DPE-----KTVWEVVSDGLDYIVVGQNEMPSRA--YLSAFGFKgADQQKPSKVLSGGERNRLNLALTLKQGGNLI 464
Cdd:PRK13647 82 glvfqDPDdqvfsSTVWDDVAFGPVNMGLDKDEVERRVeeALKAVRMW-DFRDKPPYHLSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 512463837 465 LLDEPTNDLD---VETLSSLENALQNFPGCAVVISHD 498
Cdd:PRK13647 161 VLDEPMAYLDprgQETLMEILDRLHNQGKTVIVATHD 197
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
322-510 |
1.40e-13 |
|
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: 69.81 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDL-----EKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQTVqlSYVDQG---- 392
Cdd:cd03250 1 ISVEDAsftwdSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSI--AYVSQEpwiq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 393 ----RENI------DPEKtVWEVV------------SDGlDYIVVGQnempsraylsafgfKGADqqkpskvLSGGERNR 450
Cdd:cd03250 79 ngtiRENIlfgkpfDEER-YEKVIkacalepdleilPDG-DLTEIGE--------------KGIN-------LSGGQKQR 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 512463837 451 LNLALTLKQGGNLILLDEPTNDLDVETLSSL-ENALQNF---PGCAVVISHDRWFLDRtCTHIL 510
Cdd:cd03250 136 ISLARAVYSDADIYLLDDPLSAVDAHVGRHIfENCILGLllnNKTRILVTHQLQLLPH-ADQIV 198
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-503 |
1.50e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 73.14 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 1 MGEFIYQMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEpGATV---------- 70
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILID-GKPVrirsprdaia 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 71 -GILL--QEPPLNEEKTVRGNVEEGLGDIFEKKARFEAIAEEMAtnytdELMEEMGklqeeldaadaweldskieqamda 147
Cdd:COG3845 80 lGIGMvhQHFMLVPNLTVAENIVLGLEPTKGGRLDRKAARARIR-----ELSERYG------------------------ 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 148 LRCPPaDEPVTHLSGGERRRVALAKlllsepdllllDEPTNHL---DAESVLWLEQHLAKYPGAVLAVTHdryfldhvag 224
Cdd:COG3845 131 LDVDP-DAKVEDLSVGEQQRVEILKalyrgarililDEPTAVLtpqEADELFEILRRLAAEGKSIIFITH---------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 225 wicevdrgKLypyegnystylekkAERLEVAgkkdaklqkrlkDELAWVRSGQKARQAKNK-------ARLeryeqMVEE 297
Cdd:COG3845 200 --------KL--------------REVMAIA------------DRVTVLRRGKVVGTVDTAetseeelAEL-----MVGR 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 298 aeqykklDFEEIQIPTPPRLGNQVVEVKDLE-KGFDGRVLIKDLSFTLpRNG-IVGVIGPNGVGKSTLFKTIVGLEQPDS 375
Cdd:COG3845 241 -------EVLLRVEKAPAEPGEVVLEVENLSvRDDRGVPALKDVSLEV-RAGeILGIAGVAGNGQSELAEALAGLRPPAS 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 376 GEVKV-GQTVQ-----------LSYV--DQGRENIDPEKTVWE-----------VVSDG-LDYIVVGQNempSRAYLSAF 429
Cdd:COG3845 313 GSIRLdGEDITglsprerrrlgVAYIpeDRLGRGLVPDMSVAEnlilgryrrppFSRGGfLDRKAIRAF---AEELIEEF 389
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 430 GFKGADQQKPSKVLSGGERNRLNLALTLKQGGNLILLDEPTNDLDV-------ETLSSLENAlqnfpGCAV-VISHDrwf 501
Cdd:COG3845 390 DVRTPGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVgaiefihQRLLELRDA-----GAAVlLISED--- 461
|
..
gi 512463837 502 LD 503
Cdd:COG3845 462 LD 463
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
9-214 |
2.04e-13 |
|
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of this protein family are the ATP-binding subunit of an ABC transporter system that is associated with PQQ biosynthesis and PQQ-dependent alcohol dehydrogenases. While this family shows homology to several efflux ABC transporter subunits, the presence of a periplasmic substrate-binding protein and association with systems for catabolism of alcohols suggests a role in import rather than detoxification. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 274822 [Multi-domain] Cd Length: 236 Bit Score: 70.01 E-value: 2.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 9 KNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFL-------EPG---ATVGILLQEPP 78
Cdd:TIGR03864 5 AGLSFRYGARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVaghdlrrAPRaalARLGVVFQQPT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 79 LNEEKTVRGNVE--EGLGDIFEKKARfEAIAEEMAtnytdelmeemgklqeELDAADAweldskieqamdalrcppADEP 156
Cdd:TIGR03864 85 LDLDLSVRQNLRyhAALHGLSRAEAR-ARIAELLA----------------RLGLAER------------------ADDK 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 512463837 157 VTHLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAESVLWLEQH---LAKYPG-AVLAVTH 214
Cdd:TIGR03864 130 VRELNGGHRRRVEIARALLHRPALLLLDEPTVGLDPASRAAITAHvraLARDQGlSVLWATH 191
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
7-234 |
2.23e-13 |
|
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: 69.36 E-value: 2.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAHGDKVI-LDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEPGAT--------------VG 71
Cdd:cd03292 2 EFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlrgraipylrrkIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 72 ILLQEPPLNEEKTVRGNVEEGLgDIFEKKARfeAIAEEMAtnytdELMEEMGklqeeldaadaweLDSKIeqamdalRCP 151
Cdd:cd03292 82 VVFQDFRLLPDRNVYENVAFAL-EVTGVPPR--EIRKRVP-----AALELVG-------------LSHKH-------RAL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 152 PADepvthLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAES---VLWLEQHLAKYPGAVLAVTHDRYFLDHVAGWICE 228
Cdd:cd03292 134 PAE-----LSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTtweIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIA 208
|
....*.
gi 512463837 229 VDRGKL 234
Cdd:cd03292 209 LERGKL 214
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-223 |
2.35e-13 |
|
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: 70.13 E-value: 2.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 28 FYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEpGATVGILLQEPPLNEEKTVRGNveeglgdIFEKKARFEAIA 107
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIE-LDTVSYKPQYIKADYEGTVRDL-------LSSITKDFYTHP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 108 EematnYTDELMEEMgklqeeldaadaweldsKIEQAMDALrcppadepVTHLSGGERRRVALAKLLLSEPDLLLLDEPT 187
Cdd:cd03237 94 Y-----FKTEIAKPL-----------------QIEQILDRE--------VPELSGGELQRVAIAACLSKDADIYLLDEPS 143
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 512463837 188 NHLDAESVLWLEQHLAKY----PGAVLAVTHDRYFLDHVA 223
Cdd:cd03237 144 AYLDVEQRLMASKVIRRFaennEKTAFVVEHDIIMIDYLA 183
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
336-498 |
2.56e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 69.46 E-value: 2.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 336 LIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTV--------------QLSYVDQgRENIDPEK 400
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFnGQPMsklssaakaelrnqKLGFIYQ-FHHLLPDF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 401 TVWEVVSDGLDYIVVGQNEMPSRAY--LSAFGFKGADQQKPSKvLSGGERNRLNLALTLKQGGNLILLDEPTNDLDVETL 478
Cdd:PRK11629 103 TALENVAMPLLIGKKKPAEINSRALemLAAVGLEHRANHRPSE-LSGGERQRVAIARALVNNPRLVLADEPTGNLDARNA 181
|
170 180
....*....|....*....|....
gi 512463837 479 SSLENALQNF---PGCA-VVISHD 498
Cdd:PRK11629 182 DSIFQLLGELnrlQGTAfLVVTHD 205
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
6-234 |
3.05e-13 |
|
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: 69.16 E-value: 3.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 6 YQMKNVRKAHGDKVI--LDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLE--------PG---ATVGI 72
Cdd:cd03245 3 IEFRNVSFSYPNQEIpaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDgtdirqldPAdlrRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 73 LLQEPPLNEeKTVRGNVEEGLGDIfekkarfeaiaeematnyTDELMEEMGKLQ--EELDAADAWELDSKI-EQAMDalr 149
Cdd:cd03245 83 VPQDVTLFY-GTLRDNITLGAPLA------------------DDERILRAAELAgvTDFVNKHPNGLDLQIgERGRG--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 150 cppadepvthLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAESVLWLEQHLAKYPG--AVLAVTHDRYFLDHVAGWIC 227
Cdd:cd03245 141 ----------LSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITHRPSLLDLVDRIIV 210
|
....*..
gi 512463837 228 eVDRGKL 234
Cdd:cd03245 211 -MDSGRI 216
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
10-172 |
3.24e-13 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 69.11 E-value: 3.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 10 NVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEPG----------ATVGI--LLQEP 77
Cdd:cd03218 5 NLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQditklpmhkrARLGIgyLPQEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 78 PLNEEKTVRGNVeeglgdifekkarfeaiaeeMAtnytdeLMEEMGKlqeeldaaDAWELDSKIEQAMDALRCPP-ADEP 156
Cdd:cd03218 85 SIFRKLTVEENI--------------------LA------VLEIRGL--------SKKEREEKLEELLEEFHITHlRKSK 130
|
170
....*....|....*.
gi 512463837 157 VTHLSGGERRRVALAK 172
Cdd:cd03218 131 ASSLSGGERRRVEIAR 146
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
332-514 |
4.04e-13 |
|
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: 69.05 E-value: 4.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 332 DGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTV----------QLSYVDQG-------- 392
Cdd:cd03252 13 DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVdGHDLaladpawlrrQVGVVLQEnvlfnrsi 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 393 RENI---DPEKTVWEVV-----SDGLDYIVvgqnEMPsRAYLSAFGFKGADqqkpskvLSGGERNRLNLALTLKQGGNLI 464
Cdd:cd03252 93 RDNIalaDPGMSMERVIeaaklAGAHDFIS----ELP-EGYDTIVGEQGAG-------LSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 512463837 465 LLDEPTNDLDVETLSSLENALQNFpgCA----VVISHdRWFLDRTCTHILAWEG 514
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDI--CAgrtvIIIAH-RLSTVKNADRIIVMEK 211
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
319-474 |
4.09e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 70.90 E-value: 4.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 319 NQVVEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTVQLSYVdQGRE--- 394
Cdd:PRK11432 4 KNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIdGEDVTHRSI-QQRDicm 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 395 -----NIDPEKTVWEVVSDGLDYIVVGQNEMPSRAY-------LSAFGFKGADQqkpskvLSGGERNRLNL--ALTLKQg 460
Cdd:PRK11432 83 vfqsyALFPHMSLGENVGYGLKMLGVPKEERKQRVKealelvdLAGFEDRYVDQ------ISGGQQQRVALarALILKP- 155
|
170
....*....|....
gi 512463837 461 gNLILLDEPTNDLD 474
Cdd:PRK11432 156 -KVLLFDEPLSNLD 168
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
8-233 |
5.00e-13 |
|
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: 67.41 E-value: 5.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 8 MKNVRKAHGD--KVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGE--------AFLEPGA---TVGILL 74
Cdd:cd03228 3 FKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEilidgvdlRDLDLESlrkNIAYVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 75 QEPPL-NEekTVRGNVeeglgdifekkarfeaiaeematnytdelmeemgklqeeldaadaweldskieqamdalrcppa 153
Cdd:cd03228 83 QDPFLfSG--TIRENI---------------------------------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 154 depvthLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAESVLWLEQHLAKYPG--AVLAVTHDRYFLDHvAGWICEVDR 231
Cdd:cd03228 97 ------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKgkTVIVIAHRLSTIRD-ADRIIVLDD 169
|
..
gi 512463837 232 GK 233
Cdd:cd03228 170 GR 171
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
9-171 |
7.48e-13 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 70.10 E-value: 7.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 9 KNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAF--------LEPGA-TVGILLQEPPL 79
Cdd:COG3839 7 ENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILiggrdvtdLPPKDrNIAMVFQSYAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 80 NEEKTVRGNVEEGL---GdifEKKARFEAIAEEMAtnytdelmeEMgkLQ-EELdaadaweLDSKieqamdalrcpPADe 155
Cdd:COG3839 87 YPHMTVYENIAFPLklrK---VPKAEIDRRVREAA---------EL--LGlEDL-------LDRK-----------PKQ- 133
|
170
....*....|....*.
gi 512463837 156 pvthLSGGERRRVALA 171
Cdd:COG3839 134 ----LSGGQRQRVALG 145
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
340-508 |
9.03e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 68.42 E-value: 9.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 340 LSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLeQPDSGEVKVGQTV--QLSYVDQGRENIdpektvwevvsdgldYIVVGQ 417
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPleAWSAAELARHRA---------------YLSQQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 418 N---EMPSRAYLSAFGFKGADQQKPSKV--------------------LSGGERNRLNLALTLKQ-------GGNLILLD 467
Cdd:PRK03695 79 TppfAMPVFQYLTLHQPDKTRTEAVASAlnevaealglddklgrsvnqLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 512463837 468 EPTNDLDVETLSSLENALQNFP--GCAVVIS-HDrwfLDRTCTH 508
Cdd:PRK03695 159 EPMNSLDVAQQAALDRLLSELCqqGIAVVMSsHD---LNHTLRH 199
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
339-498 |
9.82e-13 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 69.76 E-value: 9.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 339 DLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV--------GQTVQLS-------YVDQgRENIDPEKTVW 403
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLngrtlfdsRKGIFLPpekrrigYVFQ-EARLFPHLSVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 404 EVVSDGLDYIVVGQNEMPSRAYLSAFGFKGADQQKPSKvLSGGERNRLNLALTLKQGGNLILLDEPTNDLDV----ETLS 479
Cdd:TIGR02142 94 GNLRYGMKRARPSERRISFERVIELLGIGHLLGRLPGR-LSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDprkyEILP 172
|
170
....*....|....*....
gi 512463837 480 SLENALQNFPGCAVVISHD 498
Cdd:TIGR02142 173 YLERLHAEFGIPILYVSHS 191
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
7-475 |
1.12e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 70.46 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGE--------AFLEPGAT--VGILL-- 74
Cdd:PRK15439 13 CARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTleiggnpcARLTPAKAhqLGIYLvp 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 75 QEPPLNEEKTVRGNVEEGLgdifekkARFEAIAEEMAtnytdELMEEMGkLQEELDAAdAWELDSKIEQAMDALRCPPAD 154
Cdd:PRK15439 93 QEPLLFPNLSVKENILFGL-------PKRQASMQKMK-----QLLAALG-CQLDLDSS-AGSLEVADRQIVEILRGLMRD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 155 EPVTHLsggerrrvalaklllsepdllllDEPTNHLDAESVLWLEQHLAkypgAVLAVTHDRYFLDH-------VAGWIc 227
Cdd:PRK15439 159 SRILIL-----------------------DEPTASLTPAETERLFSRIR----ELLAQGVGIVFISHklpeirqLADRI- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 228 EVDRGKLYPYEGNYSTYleKKAERLE----VAGKKDAKLQKRLKDELawvrSGQKARQAKNKARLeryeqmveeaeqykk 303
Cdd:PRK15439 211 SVMRDGTIALSGKTADL--STDDIIQaitpAAREKSLSASQKLWLEL----PGNRRQQAAGAPVL--------------- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 304 ldfeeiqiptpprlgnqvvEVKDLE-KGFdgrvliKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQ 382
Cdd:PRK15439 270 -------------------TVEDLTgEGF------RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNG 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 383 -------TVQ-----LSYVDQGRE----NIDPEKTvWEVVSdgldyivVGQNEMP-------SRA----YLSAFGFKGAD 435
Cdd:PRK15439 325 keinalsTAQrlargLVYLPEDRQssglYLDAPLA-WNVCA-------LTHNRRGfwikparENAvlerYRRALNIKFNH 396
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 512463837 436 QQKPSKVLSGGERNRLNLALTLKQGGNLILLDEPTNDLDV 475
Cdd:PRK15439 397 AEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
321-505 |
1.13e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 66.90 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 321 VVEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTV---------QLSYVD 390
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFeRQSIkkdlctyqkQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 391 QgRENIDPEKTVWEvvsDGLDYIVVGQNEMPSRAYLSAFGFkGADQQKPSKVLSGGERNRLNLALTLKQGGNLILLDEPT 470
Cdd:PRK13540 81 H-RSGINPYLTLRE---NCLYDIHFSPGAVGITELCRLFSL-EHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 512463837 471 NDLD---VETLSSLENALQNFPGCAVVISHDRWFLDRT 505
Cdd:PRK13540 156 VALDelsLLTIITKIQEHRAKGGAVLLTSHQDLPLNKA 193
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
323-503 |
1.17e-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: 66.78 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 323 EVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEqpdsgevkvgqtvqlsyvdqgreniDPEKTV 402
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHP-------------------------KYEVTE 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 403 WEVVSDGLDYIVVGQNEmpsRAYLSAF-GFkgadqQKPSKV---------------LSGGERNRLNLALTLKQGGNLILL 466
Cdd:cd03217 57 GEILFKGEDITDLPPEE---RARLGIFlAF-----QYPPEIpgvknadflryvnegFSGGEKKRNEILQLLLLEPDLAIL 128
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 512463837 467 DEPTNDLDVETLSSLENALQNF--PGCAV-VISHDRWFLD 503
Cdd:cd03217 129 DEPDSGLDIDALRLVAEVINKLreEGKSVlIITHYQRLLD 168
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
332-474 |
1.42e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 68.11 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 332 DGRVLiKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVkVGQTVQLSYVDQG----RENI-----DPEKTV 402
Cdd:PRK13638 13 DEPVL-KGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAV-LWQGKPLDYSKRGllalRQQVatvfqDPEQQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 403 W--EVVSD---GLDYIVVGQNEMPSR-----AYLSAFGFKgadqQKPSKVLSGGERNRLNLALTLKQGGNLILLDEPTND 472
Cdd:PRK13638 91 FytDIDSDiafSLRNLGVPEAEITRRvdealTLVDAQHFR----HQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
..
gi 512463837 473 LD 474
Cdd:PRK13638 167 LD 168
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
334-481 |
1.66e-12 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 66.91 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 334 RVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPD---SGEVKVG------QTVQ--LSYVDQgRENIDPEKTV 402
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNgqprkpDQFQkcVAYVRQ-DDILLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 403 WEVvsdgLDYIVV--GQNEMPS--RAYLSAFGFKG--ADQQKPSKV---LSGGERNRLNLALTLKQGGNLILLDEPTNDL 473
Cdd:cd03234 99 RET----LTYTAIlrLPRKSSDaiRKKRVEDVLLRdlALTRIGGNLvkgISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170
....*....|....*
gi 512463837 474 D-------VETLSSL 481
Cdd:cd03234 175 DsftalnlVSTLSQL 189
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
321-476 |
1.72e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 67.43 E-value: 1.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 321 VVEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTVQLSYVDQgRE----- 394
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVdGLKVNDPKVDE-RLirqea 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 395 -------NIDPEKTVWEVVSDGlDYIVVGQN----EMPSRAYLSAFGFKGADQQKPSKvLSGGERNRLNLALTLKQGGNL 463
Cdd:PRK09493 80 gmvfqqfYLFPHLTALENVMFG-PLRVRGASkeeaEKQARELLAKVGLAERAHHYPSE-LSGGQQQRVAIARALAVKPKL 157
|
170
....*....|...
gi 512463837 464 ILLDEPTNDLDVE 476
Cdd:PRK09493 158 MLFDEPTSALDPE 170
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
327-520 |
1.87e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 67.70 E-value: 1.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 327 LEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTVQlSYVDQ---------GRENI 396
Cdd:PRK10253 13 LTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLdGEHIQ-HYASKevarrigllAQNAT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 397 DP-EKTVWEVVSDG------LDYIVVGQNEMPSRAYLSAFGFKGADQQKpSKVLSGGERNRLNLALTLKQGGNLILLDEP 469
Cdd:PRK10253 92 TPgDITVQELVARGryphqpLFTRWRKEDEEAVTKAMQATGITHLADQS-VDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 512463837 470 TNDLDV-------ETLSSLeNALQNFPGCAVVisHDrwfLDRTC---THILAwegnFEEGK 520
Cdd:PRK10253 171 TTWLDIshqidllELLSEL-NREKGYTLAAVL--HD---LNQACryaSHLIA----LREGK 221
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
332-477 |
2.10e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.60 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 332 DGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTVQ-------LSYVDQGREnIDPEKTVw 403
Cdd:PRK15056 18 NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISIlGQPTRqalqknlVAYVPQSEE-VDWSFPV- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 404 eVVSDGLDYIVVGQNEMPSRAylsafgfKGADQQKPSKV----------------LSGGERNRLNLALTLKQGGNLILLD 467
Cdd:PRK15056 96 -LVEDVVMMGRYGHMGWLRRA-------KKRDRQIVTAAlarvdmvefrhrqigeLSGGQKKRVFLARAIAQQGQVILLD 167
|
170
....*....|
gi 512463837 468 EPTNDLDVET 477
Cdd:PRK15056 168 EPFTGVDVKT 177
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
5-221 |
2.34e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 66.66 E-value: 2.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 5 IYQMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLE--PGAT---------VGIL 73
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEgeDISTlkpeiyrqqVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 74 LQEPPLNEEkTVRGNVeeglgdIFEKKARFEAiaeematnytdelmEEMGKLQEELdaaDAWELDSKIeqamdalrcppA 153
Cdd:PRK10247 87 AQTPTLFGD-TVYDNL------IFPWQIRNQQ--------------PDPAIFLDDL---ERFALPDTI-----------L 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 512463837 154 DEPVTHLSGGERRRVALAKLLLSEPDLLLLDEPTNHLD---AESVLWLEQHLAKYPG-AVLAVTHDRYFLDH 221
Cdd:PRK10247 132 TKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDesnKHNVNEIIHRYVREQNiAVLWVTHDKDEINH 203
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
318-498 |
2.52e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 67.48 E-value: 2.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 318 GNQVVEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTV---QLSYVDQGR 393
Cdd:PRK11831 4 VANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFdGENIpamSRSRLYTVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 394 ENID---------PEKTVWEVVSdgldYIVVGQNEMPSRAY-------LSAFGFKGADQQKPSKvLSGGERNRLNLALTL 457
Cdd:PRK11831 84 KRMSmlfqsgalfTDMNVFDNVA----YPLREHTQLPAPLLhstvmmkLEAVGLRGAAKLMPSE-LSGGMARRAALARAI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 512463837 458 KQGGNLILLDEP-------TNDLDVETLSSLENALqnfpGCA-VVISHD 498
Cdd:PRK11831 159 ALEPDLIMFDEPfvgqdpiTMGVLVKLISELNSAL----GVTcVVVSHD 203
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
7-171 |
2.54e-12 |
|
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: 66.37 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAHGD--KVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFL----------EPGATVGILL 74
Cdd:cd03263 2 QIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYIngysirtdrkAARQSLGYCP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 75 QEPPLNEEKTVRGNVEeglgdIFekkARFEAIAEEMAtNYTDELMEEMGKLQeeldaadaweldskieqamdalrcPPAD 154
Cdd:cd03263 82 QFDALFDELTVREHLR-----FY---ARLKGLPKSEI-KEEVELLLRVLGLT------------------------DKAN 128
|
170
....*....|....*..
gi 512463837 155 EPVTHLSGGERRRVALA 171
Cdd:cd03263 129 KRARTLSGGMKRKLSLA 145
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
322-510 |
3.47e-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: 65.85 E-value: 3.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDLEKGFD---GRVL-IKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVG--QTVQ--------LS 387
Cdd:cd03266 2 ITADALTKRFRdvkKTVQaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDgfDVVKepaearrrLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 388 YVDQGReNIDPEKTVWEVVS--DGLdYIVVGQ------NEMPSRAYLSAFgfkgadQQKPSKVLSGGERNRLNLALTLKQ 459
Cdd:cd03266 82 FVSDST-GLYDRLTARENLEyfAGL-YGLKGDeltarlEELADRLGMEEL------LDRRVGGFSTGMRQKVAIARALVH 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 512463837 460 GGNLILLDEPTNDLDVETLSSLENALQNF--PGCAVVIShdrwfldrtcTHIL 510
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALREFIRQLraLGKCILFS----------THIM 196
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
8-223 |
3.60e-12 |
|
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: 66.07 E-value: 3.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 8 MKNVRK----AHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLE-------PGAT------- 69
Cdd:cd03258 4 LKNVSKvfgdTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDgtdltllSGKElrkarrr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 70 VGILLQEPPLNEEKTVRGNVEEGLGDIFEKKARFEAIAEEmatnytdeLMEEMGkLQeelDAADAWeldskieqamdalr 149
Cdd:cd03258 84 IGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLE--------LLELVG-LE---DKADAY-------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 150 cpPADepvthLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAE---SVLWLEQHLAKYPG-AVLAVTHD----RYFLDH 221
Cdd:cd03258 138 --PAQ-----LSGGQKQRVGIARALANNPKVLLCDEATSALDPEttqSILALLRDINRELGlTIVLITHEmevvKRICDR 210
|
..
gi 512463837 222 VA 223
Cdd:cd03258 211 VA 212
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
7-215 |
3.62e-12 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 65.74 E-value: 3.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAF--------LEPGA-TVGILLQEP 77
Cdd:cd03301 2 ELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYiggrdvtdLPPKDrDIAMVFQNY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 78 PLNEEKTVRGNVEEGLGdifEKKARFEAIaeematnytDELMEEMGKLQeeldaadaweldsKIEQAMDalRCPPAdepv 157
Cdd:cd03301 82 ALYPHMTVYDNIAFGLK---LRKVPKDEI---------DERVREVAELL-------------QIEHLLD--RKPKQ---- 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 512463837 158 thLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDA----ESVLWLEQHLAKYPGAVLAVTHD 215
Cdd:cd03301 131 --LSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAklrvQMRAELKRLQQRLGTTTIYVTHD 190
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
7-186 |
3.67e-12 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 66.14 E-value: 3.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLE-------P---GATVGI--LL 74
Cdd:TIGR04406 3 VAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDgqdithlPmheRARLGIgyLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 75 QEPPLNEEKTVRGNveeglgdifekkarFEAIAEematnytdelmeemgkLQEELDAAdawELDSKIEQAMDALR-CPPA 153
Cdd:TIGR04406 83 QEASIFRKLTVEEN--------------IMAVLE----------------IRKDLDRA---EREERLEALLEEFQiSHLR 129
|
170 180 190
....*....|....*....|....*....|...
gi 512463837 154 DEPVTHLSGGERRRVALAKLLLSEPDLLLLDEP 186
Cdd:TIGR04406 130 DNKAMSLSGGERRRVEIARALATNPKFILLDEP 162
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
331-477 |
4.03e-12 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 66.65 E-value: 4.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 331 FDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTVQLSYVDQG----RENIDPEKTVWEV 405
Cdd:PRK11248 11 YGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLdGKPVEGPGAERGvvfqNEGLLPWRNVQDN 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 512463837 406 VSDGLDYIVVG--QNEMPSRAYLSAFGFKGADQQKPSKvLSGGERNRLNLALTLKQGGNLILLDEPTNDLDVET 477
Cdd:PRK11248 91 VAFGLQLAGVEkmQRLEIAHQMLKKVGLEGAEKRYIWQ-LSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT 163
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
317-518 |
4.38e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 66.53 E-value: 4.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 317 LGNQVVEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTVQLSYVDQGREN 395
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVnGQTINLVRDKDGQLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 396 IDPEK----------------------TVWEVVSDG-LDYIVVGQNEMPSRA--YLSAFGFKGADQQKPSKVLSGGERNR 450
Cdd:PRK10619 81 VADKNqlrllrtrltmvfqhfnlwshmTVLENVMEApIQVLGLSKQEARERAvkYLAKVGIDERAQGKYPVHLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 512463837 451 LNLALTLKQGGNLILLDEPTNDLDVETLSSLENALQNFP---GCAVVISHDRWFLDRTCTH-ILAWEGNFEE 518
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAeegKTMVVVTHEMGFARHVSSHvIFLHQGKIEE 232
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
321-474 |
4.56e-12 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 67.66 E-value: 4.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 321 VVEVKDLEKGFDGRVLIKDLSFTLpRNG-IVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTVQlsyvdqgreNIDP 398
Cdd:PRK09452 14 LVELRGISKSFDGKEVISNLDLTI-NNGeFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLdGQDIT---------HVPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 399 EK----------------TVWEVVSDGLDYIVVGQNEMPSRAY-------LSAFGfkgadQQKPSKvLSGGERNRLNLAL 455
Cdd:PRK09452 84 ENrhvntvfqsyalfphmTVFENVAFGLRMQKTPAAEITPRVMealrmvqLEEFA-----QRKPHQ-LSGGQQQRVAIAR 157
|
170
....*....|....*....
gi 512463837 456 TLKQGGNLILLDEPTNDLD 474
Cdd:PRK09452 158 AVVNKPKVLLLDESLSALD 176
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
322-497 |
4.70e-12 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 65.71 E-value: 4.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDLEKGFD-GRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTV----------QLSYV 389
Cdd:cd03254 3 IEFENVNFSYDeKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIdGIDIrdisrkslrsMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 390 DQG--------RENI-----DPEKTVWEVVSD--GLDYIVvgqNEMPsRAYLSAFGFKGadqqkpsKVLSGGERNRLNLA 454
Cdd:cd03254 83 LQDtflfsgtiMENIrlgrpNATDEEVIEAAKeaGAHDFI---MKLP-NGYDTVLGENG-------GNLSQGERQLLAIA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 512463837 455 LTLKQGGNLILLDEPTNDLDVETLSSLENALQN-FPG-CAVVISH 497
Cdd:cd03254 152 RAMLRDPKILILDEATSNIDTETEKLIQEALEKlMKGrTSIIIAH 196
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
7-234 |
5.65e-12 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 65.80 E-value: 5.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFL---------EPGAT-------- 69
Cdd:COG4161 4 QLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIaghqfdfsqKPSEKairllrqk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 70 VGILLQEPPLNEEKTVRGNVEEG----LGdIFEKKARFEAiaeematnytDELMEEMgKLQeelDAADAWELdskieqam 145
Cdd:COG4161 84 VGMVFQQYNLWPHLTVMENLIEApckvLG-LSKEQAREKA----------MKLLARL-RLT---DKADRFPL-------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 146 dalrcppadepvtHLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAE---SVLWLEQHLAKYPGAVLAVTHDRYFLDHV 222
Cdd:COG4161 141 -------------HLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEitaQVVEIIRELSQTGITQVIVTHEVEFARKV 207
|
250
....*....|..
gi 512463837 223 AGWICEVDRGKL 234
Cdd:COG4161 208 ASQVVYMEKGRI 219
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
337-498 |
5.83e-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: 65.56 E-value: 5.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 337 IKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTVQLSYVDQ----GRENIDPEKTVWEVVSDGLD 411
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILeGKQITEPGPDRmvvfQNYSLLPWLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 412 YIVVGQNEMPSRA----YLSAFGFKGADQQKPSKvLSGGERNRLNLALTLKQGGNLILLDEPTNDLDVETLSSLENALQN 487
Cdd:TIGR01184 81 RVLPDLSKSERRAiveeHIALVGLTEAADKRPGQ-LSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQ 159
|
170
....*....|....*
gi 512463837 488 F---PGC-AVVISHD 498
Cdd:TIGR01184 160 IweeHRVtVLMVTHD 174
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
324-515 |
7.06e-12 |
|
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: 68.40 E-value: 7.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 324 VKDLEKGF--DGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDsGEVKV-----------------GQTV 384
Cdd:TIGR01271 1220 VQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIdgvswnsvtlqtwrkafGVIP 1298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 385 QLSYVDQG--RENIDP-----EKTVWEVVSDgldyivvgqnempsraylsaFGFKGADQQKPSK----------VLSGGE 447
Cdd:TIGR01271 1299 QKVFIFSGtfRKNLDPyeqwsDEEIWKVAEE--------------------VGLKSVIEQFPDKldfvlvdggyVLSNGH 1358
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 512463837 448 RNRLNLALTLKQGGNLILLDEPTNDLDVETLSSLENAL-QNFPGCAVVISHDRWFLDRTCTHILAWEGN 515
Cdd:TIGR01271 1359 KQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLkQSFSNCTVILSEHRVEALLECQQFLVIEGS 1427
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
322-503 |
7.29e-12 |
|
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: 64.92 E-value: 7.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDLEKGFDG--RVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVK-------------------- 379
Cdd:cd03245 3 IEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLldgtdirqldpadlrrnigy 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 380 VGQTVQLSYvdqG--RENI---DPEKTVWEVVS---------------DGLDYIVvgqnempsraylsafGFKGADqqkp 439
Cdd:cd03245 83 VPQDVTLFY---GtlRDNItlgAPLADDERILRaaelagvtdfvnkhpNGLDLQI---------------GERGRG---- 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 512463837 440 skvLSGGERNRLNLALTLKQGGNLILLDEPTNDLDVETLSSLENALQNFPG--CAVVISHDRWFLD 503
Cdd:cd03245 141 ---LSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITHRPSLLD 203
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
9-192 |
7.46e-12 |
|
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: 65.34 E-value: 7.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 9 KNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEPGATVGILLQEPPLNeekTVrgn 88
Cdd:cd03300 4 ENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVN---TV--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 89 veeglgdiFEKKARFE--AIAEEMATNYTdelmeeMGKLQEEldaadawELDSKIEQAMDALRCPP-ADEPVTHLSGGER 165
Cdd:cd03300 78 --------FQNYALFPhlTVFENIAFGLR------LKKLPKA-------EIKERVAEALDLVQLEGyANRKPSQLSGGQQ 136
|
170 180
....*....|....*....|....*..
gi 512463837 166 RRVALAKLLLSEPDLLLLDEPTNHLDA 192
Cdd:cd03300 137 QRVAIARALVNEPKVLLLDEPLGALDL 163
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
322-499 |
7.86e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 67.03 E-value: 7.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTV--------QLSYVDQG 392
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFhGTDVsrlhardrKVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 393 ----RenidpEKTVWEVVSDGLDyiVVGQNEMPSRAYLSAFGFKGAD--------QQKPSKvLSGGERNRLNLALTLKQG 460
Cdd:PRK10851 83 yalfR-----HMTVFDNIAFGLT--VLPRRERPNAAAIKAKVTQLLEmvqlahlaDRYPAQ-LSGGQKQRVALARALAVE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 512463837 461 GNLILLDEPTNDLDVETLSSLENALQN----FPGCAVVISHDR 499
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKELRRWLRQlheeLKFTSVFVTHDQ 197
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-222 |
8.56e-12 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 63.60 E-value: 8.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEaflepgatvgILLQepplneektvr 86
Cdd:cd03216 2 ELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGE----------ILVD----------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 87 gnveeglgdifekkarfeaiaeematnytdelmeemGKLQEELDAADAWELdsKIeqAMdalrcppadepVTHLSGGERR 166
Cdd:cd03216 61 ------------------------------------GKEVSFASPRDARRA--GI--AM-----------VYQLSVGERQ 89
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 512463837 167 RVALAKLLLSEPDLLLLDEPTNHLDAESVLWLEQH---LAKYPGAVLAVTHdryFLDHV 222
Cdd:cd03216 90 MVEIARALARNARLLILDEPTAALTPAEVERLFKVirrLRAQGVAVIFISH---RLDEV 145
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
321-496 |
8.99e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 65.98 E-value: 8.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 321 VVEVKDLEKGFDGRV-LIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTVQLSYVDQGRENI-- 396
Cdd:PRK13652 3 LIETRDLCYSYSGSKeALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIrGEPITKENIREVRKFVgl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 397 ---DPEKTVWE--VVSD--------GLDYIVVGQNempSRAYLSAFGFKGADQQKPSKvLSGGERNRLNLALTLKQGGNL 463
Cdd:PRK13652 83 vfqNPDDQIFSptVEQDiafgpinlGLDEETVAHR---VSSALHMLGLEELRDRVPHH-LSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 512463837 464 ILLDEPTNDLDVETLSSLENALQNFP---GCAVVIS 496
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPetyGMTVIFS 194
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
321-498 |
9.22e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 66.02 E-value: 9.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 321 VVEVKDLEKGF-DGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQTvQLSYVDQG----REN 395
Cdd:PRK13636 5 ILKVEELNYNYsDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGK-PIDYSRKGlmklRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 396 I-----DPEK-----TVWEVVSDGLDYIVVGQNEMPSRAYlSAFGFKGAD--QQKPSKVLSGGERNRLNLALTLKQGGNL 463
Cdd:PRK13636 84 VgmvfqDPDNqlfsaSVYQDVSFGAVNLKLPEDEVRKRVD-NALKRTGIEhlKDKPTHCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 512463837 464 ILLDEPTNDLD---VETLSSLENALQNFPGCAVVI-SHD 498
Cdd:PRK13636 163 LVLDEPTAGLDpmgVSEIMKLLVEMQKELGLTIIIaTHD 201
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-215 |
1.04e-11 |
|
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: 64.79 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 21 LDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLE------PGATVGILLQEPPLNEEKTVRGNVeeglg 94
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEgkqitePGPDRMVVFQNYSLLPWLTVRENI----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 95 difekkarfeAIAeematnyTDELMEEMGKLQEEldaadaweldSKIEQAMD--ALRcPPADEPVTHLSGGERRRVALAK 172
Cdd:TIGR01184 76 ----------ALA-------VDRVLPDLSKSERR----------AIVEEHIAlvGLT-EAADKRPGQLSGGMKQRVAIAR 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 512463837 173 LLLSEPDLLLLDEPTNHLDA-------ESVL--WLEQHLakypgAVLAVTHD 215
Cdd:TIGR01184 128 ALSIRPKVLLLDEPFGALDAltrgnlqEELMqiWEEHRV-----TVLMVTHD 174
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-498 |
1.12e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 67.04 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 12 RKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKS-SILKIMAGLDQPS----------NGEAFL---EP------GATVG 71
Cdd:PRK15134 16 RQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypsgdirfHGESLLhasEQtlrgvrGNKIA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 72 ILLQEP--PLNEEKTVRGNVEEGLGdiFEKKARFEAIAEEMATnytdeLMEEMGklqeeldaadaweldskIEQAMDALr 149
Cdd:PRK15134 96 MIFQEPmvSLNPLHTLEKQLYEVLS--LHRGMRREAARGEILN-----CLDRVG-----------------IRQAAKRL- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 150 cppADEPvtH-LSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAE---SVLWLEQHLAKYPG-AVLAVTHDryfLDHVag 224
Cdd:PRK15134 151 ---TDYP--HqLSGGERQRVMIAMALLTRPELLIADEPTTALDVSvqaQILQLLRELQQELNmGLLFITHN---LSIV-- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 225 wicevdrgklypyegnystylekkaerlevagkkdaklqKRLKDELAWVRSG----QKARQAKNKARLERYEQMVEEAEq 300
Cdd:PRK15134 221 ---------------------------------------RKLADRVAVMQNGrcveQNRAATLFSAPTHPYTQKLLNSE- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 301 yKKLDFEEIQIPTPPRLgnqvvEVKDLEKGFDGR-----------VLIKDLSFTLPRNGIVGVIGPNGVGKST----LFK 365
Cdd:PRK15134 261 -PSGDPVPLPEPASPLL-----DVEQLQVAFPIRkgilkrtvdhnVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLR 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 366 TIvgleqPDSGEV----------------KVGQTVQLSYVDQgRENIDPEKTVWEVVSDGLD----YIVVGQNEMPSRAY 425
Cdd:PRK15134 335 LI-----NSQGEIwfdgqplhnlnrrqllPVRHRIQVVFQDP-NSSLNPRLNVLQIIEEGLRvhqpTLSAAQREQQVIAV 408
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 512463837 426 LSAFGFKGADQQKPSKVLSGGERNRLNLALTLKQGGNLILLDEPTNDLD--VET-LSSLENALQNFPGCA-VVISHD 498
Cdd:PRK15134 409 MEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDktVQAqILALLKSLQQKHQLAyLFISHD 485
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-222 |
1.18e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 67.13 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 1 MGEFIYQMKNVRKAH-----GDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFL----------E 65
Cdd:TIGR03269 275 VGEPIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvdmtK 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 66 PGAT--------VGILLQEPPLNEEKTVRGNVEEGLG-DIFEKKARFEAIAEEMATNYTDELMEE-MGKLQEELdaadaw 135
Cdd:TIGR03269 355 PGPDgrgrakryIGILHQEYDLYPHRTVLDNLTEAIGlELPDELARMKAVITLKMVGFDEEKAEEiLDKYPDEL------ 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 136 eldskieqamdalrcppadepvthlSGGERRRVALAKLLLSEPDLLLLDEPTNHLD-------AESVLWLEQHLAKypgA 208
Cdd:TIGR03269 429 -------------------------SEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkvdvTHSILKAREEMEQ---T 480
|
250
....*....|....
gi 512463837 209 VLAVTHDRYFLDHV 222
Cdd:TIGR03269 481 FIIVSHDMDFVLDV 494
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
7-233 |
1.29e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 66.40 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLE------------PgatVGILL 74
Cdd:PRK11607 21 EIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDgvdlshvppyqrP---INMMF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 75 QEPPLNEEKTVRGNVEEGLGDIFEKKARFEAIAEEMATNYTdelMEEMGKlqeeldaadaweldskieqamdalRCPpad 154
Cdd:PRK11607 98 QSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVH---MQEFAK------------------------RKP--- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 155 epvTHLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAE--SVLWLE--QHLAKYPGAVLAVTHDRYFLDHVAGWICEVD 230
Cdd:PRK11607 148 ---HQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKlrDRMQLEvvDILERVGVTCVMVTHDQEEAMTMAGRIAIMN 224
|
...
gi 512463837 231 RGK 233
Cdd:PRK11607 225 RGK 227
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
322-381 |
1.30e-11 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 66.25 E-value: 1.30e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVG 381
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIG 63
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
332-508 |
1.33e-11 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 64.86 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 332 DGRVLikDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLeQPDSGEVKVGQT--VQLSYVDQGRenidpeKTVWevvsdg 409
Cdd:COG4138 9 AGRLG--PISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRplSDWSAAELAR------HRAY------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 410 ldyivVGQNEMPSRA-----YLSAFGFKGADQQKPSKV--------------------LSGGERNRLNLALTLKQ----- 459
Cdd:COG4138 74 -----LSQQQSPPFAmpvfqYLALHQPAGASSEAVEQLlaqlaealgledklsrpltqLSGGEWQRVRLAAVLLQvwpti 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 512463837 460 --GGNLILLDEPTNDLDVETLSSLENALQNF--PGCAVVIS-HDrwfLDRTCTH 508
Cdd:COG4138 149 npEGQLLLLDEPMNSLDVAQQAALDRLLRELcqQGITVVMSsHD---LNHTLRH 199
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
11-214 |
1.34e-11 |
|
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: 63.00 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 11 VRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFL-----------EPGATVGILLQEppl 79
Cdd:cd03246 8 FRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLdgadisqwdpnELGDHVGYLPQD--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 80 neektvrgnveeglgdifekkarfeaiaeematnytDELMEemGKLQEELdaadaweldskieqamdalrcppadepvth 159
Cdd:cd03246 85 ------------------------------------DELFS--GSIAENI------------------------------ 96
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 512463837 160 LSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAESVLWLEQ---HLAKYPGAVLAVTH 214
Cdd:cd03246 97 LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQaiaALKAAGATRIVIAH 154
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-234 |
1.46e-11 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 64.73 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 1 MGEFiyqmKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGE------AFLEPGATV---- 70
Cdd:PRK09493 1 MIEF----KNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDlivdglKVNDPKVDErlir 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 71 ---GILLQEPPLNEEKTVRGNVeeGLGDIFEKKARFEAiAEEMATnytdELMEEMGkLQEEldaadaweldskieqamda 147
Cdd:PRK09493 77 qeaGMVFQQFYLFPHLTALENV--MFGPLRVRGASKEE-AEKQAR----ELLAKVG-LAER------------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 148 lrcppADEPVTHLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAE---SVLWLEQHLAKYPGAVLAVTHDRYFLDHVAG 224
Cdd:PRK09493 130 -----AHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPElrhEVLKVMQDLAEEGMTMVIVTHEIGFAEKVAS 204
|
250
....*....|
gi 512463837 225 WICEVDRGKL 234
Cdd:PRK09493 205 RLIFIDKGRI 214
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
8-192 |
1.70e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 65.82 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 8 MKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEpgatvGILLQE-PPlneektvr 86
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIG-----EKRMNDvPP-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 87 gnVEEGLGDIFEKKARFE--AIAEEMATNYtdelmeemgklqeELDAADAWELDSKIEQAMDAL-------RCPPAdepv 157
Cdd:PRK11000 73 --AERGVGMVFQSYALYPhlSVAENMSFGL-------------KLAGAKKEEINQRVNQVAEVLqlahlldRKPKA---- 133
|
170 180 190
....*....|....*....|....*....|....*
gi 512463837 158 thLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDA 192
Cdd:PRK11000 134 --LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDA 166
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
20-215 |
1.86e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 64.07 E-value: 1.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 20 ILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEaflepgatvgILLQEPPLNE-EKTVRGNVE-EGLGDIF 97
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGD----------VIFNGQPMSKlSSAAKAELRnQKLGFIY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 98 EKK---ARFEAIaEEMAtnytdelmeeMGKLQEELDAADAWEldskieQAMDALRCPPADEPVTH----LSGGERRRVAL 170
Cdd:PRK11629 94 QFHhllPDFTAL-ENVA----------MPLLIGKKKPAEINS------RALEMLAAVGLEHRANHrpseLSGGERQRVAI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 512463837 171 AKLLLSEPDLLLLDEPTNHLD---AESVLWLEQHLAKYPG-AVLAVTHD 215
Cdd:PRK11629 157 ARALVNNPRLVLADEPTGNLDarnADSIFQLLGELNRLQGtAFLVVTHD 205
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
322-474 |
2.11e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 65.82 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQTvQLSYVDQGRENID---- 397
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK-RMNDVPPAERGVGmvfq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 398 -----PEKTVWEVVSDGLDYIVVGQNEMPSRAYLSAFGFKGAD--QQKPsKVLSGGERNRLNLALTLKQGGNLILLDEPT 470
Cdd:PRK11000 83 syalyPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHllDRKP-KALSGGQRQRVAIGRTLVAEPSVFLLDEPL 161
|
....
gi 512463837 471 NDLD 474
Cdd:PRK11000 162 SNLD 165
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
305-497 |
2.13e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 66.41 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 305 DFEEIQIPTPPRLGNQV-------VEVKDLE-KGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLeQPDSG 376
Cdd:PRK11174 326 TFLETPLAHPQQGEKELasndpvtIEAEDLEiLSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQG 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 377 EVKV-GQTV----------QLSYVDQG--------RENI---DPEKT------------VWEVVS---DGLDYIVvgqne 419
Cdd:PRK11174 405 SLKInGIELreldpeswrkHLSWVGQNpqlphgtlRDNVllgNPDASdeqlqqalenawVSEFLPllpQGLDTPI----- 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 420 mpsraylsafgfkgADQqkpSKVLSGGERNRLNLALTLKQGGNLILLDEPTNDLDVET----LSSLENALQNfpGCAVVI 495
Cdd:PRK11174 480 --------------GDQ---AAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSeqlvMQALNAASRR--QTTLMV 540
|
..
gi 512463837 496 SH 497
Cdd:PRK11174 541 TH 542
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
322-498 |
2.31e-11 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 63.86 E-value: 2.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDLEKGF-DGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTVQLSYVDQGRENID-- 397
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIdGEDIREQDPVELRRKIGyv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 398 -------PEKTVWEVVSDGLDYIVVGQNEMPSRAY-------LSAFGFKgadQQKPSKvLSGGERNRLNLALTLKQGGNL 463
Cdd:cd03295 81 iqqiglfPHMTVEENIALVPKLLKWPKEKIRERADellalvgLDPAEFA---DRYPHE-LSGGQQQRVGVARALAADPPL 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 512463837 464 ILLDEPTNDLDVETLSSLENA---LQNFPGCAVV-ISHD 498
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEfkrLQQELGKTIVfVTHD 195
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
319-498 |
2.57e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 64.44 E-value: 2.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 319 NQVVEVKDLEKGF--DGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGevkvgqtvqlsyvDQGRENI 396
Cdd:PRK13640 3 DNIVEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDN-------------PNSKITV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 397 D----PEKTVWEV-------------------VSD----GLDYIVVGQNEMPS--RAYLSAFGFKGADQQKPSKvLSGGE 447
Cdd:PRK13640 70 DgitlTAKTVWDIrekvgivfqnpdnqfvgatVGDdvafGLENRAVPRPEMIKivRDVLADVGMLDYIDSEPAN-LSGGQ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 512463837 448 RNRLNLALTLKQGGNLILLDEPTNDLDV---ETLSSLENALQNFPGCAVV-ISHD 498
Cdd:PRK13640 149 KQRVAIAGILAVEPKIIILDESTSMLDPagkEQILKLIRKLKKKNNLTVIsITHD 203
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
21-225 |
2.84e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 64.37 E-value: 2.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 21 LDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGeaflepgaTVGILLQEPPLNEEKTVRGNVeeglGDIFEK- 99
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRG--------RVKVMGREVNAENEKWVRSKV----GLVFQDp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 100 -KARFEAIAEEMATnytdelmeeMGKLQEELDAAdawELDSKIEQAMDALRCPP-ADEPVTHLSGGERRRVALAKLLLSE 177
Cdd:PRK13647 89 dDQVFSSTVWDDVA---------FGPVNMGLDKD---EVERRVEEALKAVRMWDfRDKPPYHLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 512463837 178 PDLLLLDEPTNHLD---AESVLWLEQHLAKYPGAVLAVTHDryfLDHVAGW 225
Cdd:PRK13647 157 PDVIVLDEPMAYLDprgQETLMEILDRLHNQGKTVIVATHD---VDLAAEW 204
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
323-474 |
2.91e-11 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 63.62 E-value: 2.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 323 EVKDLEKGFDGrvLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTVQLSYVDQgR-------- 393
Cdd:COG3840 3 RLDDLTYRYGD--FPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWnGQDLTALPPAE-Rpvsmlfqe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 394 ENIDPEKTVWEVV----SDGLDYIVVGQNEMpsRAYLSAFGFKGADQQKPSKvLSGGERNRLNLALTLKQGGNLILLDEP 469
Cdd:COG3840 80 NNLFPHLTVAQNIglglRPGLKLTAEQRAQV--EQALERVGLAGLLDRLPGQ-LSGGQRQRVALARCLVRKRPILLLDEP 156
|
....*
gi 512463837 470 TNDLD 474
Cdd:COG3840 157 FSALD 161
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-223 |
2.98e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 65.96 E-value: 2.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 29 YPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEafLEPGATVGILLQEPPLNEEKTVRGNVEEGLGDIFEkkarfeaiae 108
Cdd:COG1245 364 REGEVLGIVGPNGIGKTTFAKILAGVLKPDEGE--VDEDLKISYKPQYISPDYDGTVEEFLRSANTDDFG---------- 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 109 emATNYTDELMEEMGklqeeldaadaweldskIEQAMDalrcppadEPVTHLSGGERRRVALAKLLLSEPDLLLLDEPTN 188
Cdd:COG1245 432 --SSYYKTEIIKPLG-----------------LEKLLD--------KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSA 484
|
170 180 190
....*....|....*....|....*....|....*....
gi 512463837 189 HLDAE---SVLWLEQHLAKYPGA-VLAVTHDRYFLDHVA 223
Cdd:COG1245 485 HLDVEqrlAVAKAIRRFAENRGKtAMVVDHDIYLIDYIS 523
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
17-214 |
2.99e-11 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 66.28 E-value: 2.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 17 DKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFL--EP---------GATVGILLQEPPLnEEKTV 85
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLdgVPlvqydhhylHRQVALVGQEPVL-FSGSV 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 86 RGNVEEGLgdifekkarfeaiaeemaTNYTDELMEEMGKlqeeldAADAWELDSKIEQAMDAlrcpPADEPVTHLSGGER 165
Cdd:TIGR00958 572 RENIAYGL------------------TDTPDEEIMAAAK------AANAHDFIMEFPNGYDT----EVGEKGSQLSGGQK 623
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 512463837 166 RRVALAKLLLSEPDLLLLDEPTNHLDAESVLWLEQHLAKYPGAVLAVTH 214
Cdd:TIGR00958 624 QRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH 672
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
5-215 |
3.09e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 63.94 E-value: 3.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 5 IYQMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFL--EPGA------------TV 70
Cdd:PRK10419 12 HYAHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWrgEPLAklnraqrkafrrDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 71 GILLQEPP--LNEEKTVRGNVEEGLG-----DIFEKKARfeaiaeematnyTDELMEEMGklqeeLDAAdaweldskieq 143
Cdd:PRK10419 92 QMVFQDSIsaVNPRKTVREIIREPLRhllslDKAERLAR------------ASEMLRAVD-----LDDS----------- 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 512463837 144 amDALRCPPadepvtHLSGGERRRVALAKLLLSEPDLLLLDEPTNHLD----AESVLWLEQHLAKYPGAVLAVTHD 215
Cdd:PRK10419 144 --VLDKRPP------QLSGGQLQRVCLARALAVEPKLLILDEAVSNLDlvlqAGVIRLLKKLQQQFGTACLFITHD 211
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-475 |
3.62e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.58 E-value: 3.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 1 MGEFIYQMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPS------NGEAF--LEPGAT--- 69
Cdd:PRK09700 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTkgtitiNNINYnkLDHKLAaql 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 70 -VGILLQEPPLNEEKTVRGNVEegLGDIFEKKArfeaiaeeMATNYTDelMEEMGKLQEELdaadAWELDSKIEqamdal 148
Cdd:PRK09700 81 gIGIIYQELSVIDELTVLENLY--IGRHLTKKV--------CGVNIID--WREMRVRAAMM----LLRVGLKVD------ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 149 rcppADEPVTHLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAESVLWL---EQHLAKYPGAVLAVTH---------DR 216
Cdd:PRK09700 139 ----LDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLfliMNQLRKEGTAIVYISHklaeirricDR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 217 YfldhvagwicEVDRGKLYPYEGNYSTYLEKKAERLEVagkkdaklqkrlkdelawvrsgqkARQAKNkarleRYEQMVE 296
Cdd:PRK09700 215 Y----------TVMKDGSSVCSGMVSDVSNDDIVRLMV------------------------GRELQN-----RFNAMKE 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 297 EAEQYKkldfeeiqiptpprlGNQVVEVKDLEKGFDGRVliKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSG 376
Cdd:PRK09700 256 NVSNLA---------------HETVFEVRNVTSRDRKKV--RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGG 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 377 EVKVgqtvqlsyvdQGREnIDPeKTVWEVVSDGLDYIV-------------VGQNEMPSRAyLSAFGFKG---------- 433
Cdd:PRK09700 319 EIRL----------NGKD-ISP-RSPLDAVKKGMAYITesrrdngffpnfsIAQNMAISRS-LKDGGYKGamglfhevde 385
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 512463837 434 ---ADQQ------KPSKV------LSGGERNRLNLALTLKQGGNLILLDEPTNDLDV 475
Cdd:PRK09700 386 qrtAENQrellalKCHSVnqniteLSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDV 442
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
5-223 |
4.02e-11 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 63.67 E-value: 4.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 5 IYQMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAF--------LEPGA------TV 70
Cdd:TIGR02769 11 TYRTGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSfrgqdlyqLDRKQrrafrrDV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 71 GILLQEPP--LNEEKTVRgnveeglgdifekkarfEAIAEEMaTNYTDelMEEMGKLQEELDAADAWELDSKIEQamdal 148
Cdd:TIGR02769 91 QLVFQDSPsaVNPRMTVR-----------------QIIGEPL-RHLTS--LDESEQKARIAELLDMVGLRSEDAD----- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 149 RCPPadepvtHLSGGERRRVALAKLLLSEPDLLLLDEPTNHLD---AESVLWLEQHLAKYPG-AVLAVTHD----RYFLD 220
Cdd:TIGR02769 146 KLPR------QLSGGQLQRINIARALAVKPKLIVLDEAVSNLDmvlQAVILELLRKLQQAFGtAYLFITHDlrlvQSFCQ 219
|
...
gi 512463837 221 HVA 223
Cdd:TIGR02769 220 RVA 222
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
12-89 |
4.52e-11 |
|
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: 62.94 E-value: 4.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 12 RKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGE--------AFLEPGAtvGillqeppLNEEK 83
Cdd:cd03220 29 KGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTvtvrgrvsSLLGLGG--G-------FNPEL 99
|
....*.
gi 512463837 84 TVRGNV 89
Cdd:cd03220 100 TGRENI 105
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
7-193 |
4.90e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 63.11 E-value: 4.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGE------AF---LEPGAT-------- 69
Cdd:PRK11124 4 QLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTlniagnHFdfsKTPSDKairelrrn 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 70 VGILLQEPPLNEEKTVRGNveeglgdIFEKKARFEAIAEEMATNYTDELMEemgKLQEElDAADAWELdskieqamdalr 149
Cdd:PRK11124 84 VGMVFQQYNLWPHLTVQQN-------LIEAPCRVLGLSKDQALARAEKLLE---RLRLK-PYADRFPL------------ 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 512463837 150 cppadepvtHLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAE 193
Cdd:PRK11124 141 ---------HLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
8-216 |
5.40e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 64.36 E-value: 5.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 8 MKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEpGATVG----------ILLQEP 77
Cdd:PRK11432 9 LKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFID-GEDVThrsiqqrdicMVFQSY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 78 PLNEEKTVRGNVEEGLgdifekkaRFEAIAEEmatnytdelmEEMGKLQEELDAADaweLDSKieqamdalrcppADEPV 157
Cdd:PRK11432 88 ALFPHMSLGENVGYGL--------KMLGVPKE----------ERKQRVKEALELVD---LAGF------------EDRYV 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 512463837 158 THLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDA-------ESVLWLEQHLAKypgAVLAVTHDR 216
Cdd:PRK11432 135 DQISGGQQQRVALARALILKPKVLLFDEPLSNLDAnlrrsmrEKIRELQQQFNI---TSLYVTHDQ 197
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
321-497 |
5.59e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 65.04 E-value: 5.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 321 VVEVKDLEKGFDG-RVLiKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTVQLSYVDQGRE---- 394
Cdd:COG1129 4 LLEMRGISKSFGGvKAL-DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLdGEPVRFRSPRDAQAagia 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 395 ------NIDPEKTVWE-------VVSDGLdyivVGQNEMPSRA--YLSAFGFKgADQQKPSKVLSGGERNRLNLALTLKQ 459
Cdd:COG1129 83 iihqelNLVPNLSVAEniflgrePRRGGL----IDWRAMRRRAreLLARLGLD-IDPDTPVGDLSVAQQQLVEIARALSR 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 512463837 460 GGNLILLDEPT---NDLDVETLSSLENALQNfPGCAVV-ISH 497
Cdd:COG1129 158 DARVLILDEPTaslTEREVERLFRIIRRLKA-QGVAIIyISH 198
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
337-504 |
5.84e-11 |
|
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: 61.57 E-value: 5.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 337 IKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVgleqPDSGEVKVGQTVQLsYVDQGRENIDPEKTVWEVvsdGLDYIVVG 416
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL----YASGKARLISFLPK-FSRNKLIFIDQLQFLIDV---GLGYLTLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 417 QNeMPSraylsafgfkgadqqkpskvLSGGERNRLNLA--LTLKQGGNLILLDEPTNDLDVETLSSLENALQNFPGCA-- 492
Cdd:cd03238 83 QK-LST--------------------LSGGELQRVKLAseLFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGnt 141
|
170
....*....|...
gi 512463837 493 -VVISHDRWFLDR 504
Cdd:cd03238 142 vILIEHNLDVLSS 154
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
322-497 |
6.11e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 64.82 E-value: 6.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQ--PDSGEV--KVGQTVQLSYVDQ----GR 393
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyHVALCEKCGYVERpskvGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 394 ------ENIDPEKTVWEVVSDGLDYIVVGQNE-MPSRAY---------------LSAFGFKGADQQKP------------ 439
Cdd:TIGR03269 81 pcpvcgGTLEPEEVDFWNLSDKLRRRIRKRIAiMLQRTFalygddtvldnvleaLEEIGYEGKEAVGRavdliemvqlsh 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 512463837 440 -----SKVLSGGERNRLNLALTLKQGGNLILLDEPTNDLDVETL----SSLENALQNFPGCAVVISH 497
Cdd:TIGR03269 161 rithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAklvhNALEEAVKASGISMVLTSH 227
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
7-236 |
6.27e-11 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 62.46 E-value: 6.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAHGDKVIldNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAF--------LEPGA-TVGILLQEP 77
Cdd:COG3840 3 RLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILwngqdltaLPPAErPVSMLFQEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 78 PLNEEKTVRGNVeeGLGdiF--------EKKARFEAIAEEMAtnytdelMEEMGKlqeeldaadaweldskieqamdalR 149
Cdd:COG3840 81 NLFPHLTVAQNI--GLG--LrpglkltaEQRAQVEQALERVG-------LAGLLD------------------------R 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 150 CPPAdepvthLSGGERRRVALAKLLLSEPDLLLLDEPTNHLD----AESVLWLEQHLAKYPGAVLAVTHDryfLD---HV 222
Cdd:COG3840 126 LPGQ------LSGGQRQRVALARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCRERGLTVLMVTHD---PEdaaRI 196
|
250
....*....|....
gi 512463837 223 AGWICEVDRGKLYP 236
Cdd:COG3840 197 ADRVLLVADGRIAA 210
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
322-497 |
6.30e-11 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 62.63 E-value: 6.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDLEKGFD-GRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQ---TVQLSYVdqgRENI 396
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIdGQdirEVTLDSL---RRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 397 D--PEKTVweVVSDGLDY-IVVGQ----NEMPSRAYLSA----------FGFKgadqqkpSKV------LSGGERNRLNL 453
Cdd:cd03253 78 GvvPQDTV--LFNDTIGYnIRYGRpdatDEEVIEAAKAAqihdkimrfpDGYD-------TIVgerglkLSGGEKQRVAI 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 512463837 454 ALTLKQGGNLILLDEPTNDLDVET----LSSLENALQNfpGCAVVISH 497
Cdd:cd03253 149 ARAILKNPPILLLDEATSALDTHTereiQAALRDVSKG--RTTIVIAH 194
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
319-486 |
6.32e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 63.23 E-value: 6.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 319 NQVVEVKDLEKGF--DGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTVQLSYVDQGREN 395
Cdd:PRK13648 5 NSIIVFKNVSFQYqsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYnNQAITDDNFEKLRKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 396 I-----DPEK-----TVWEVVSDGLDYIVVGQNEMPSRA--YLSAFG-FKGADQQKPSkvLSGGERNRLNLALTLKQGGN 462
Cdd:PRK13648 85 IgivfqNPDNqfvgsIVKYDVAFGLENHAVPYDEMHRRVseALKQVDmLERADYEPNA--LSGGQKQRVAIAGVLALNPS 162
|
170 180
....*....|....*....|....
gi 512463837 463 LILLDEPTNDLDVETLSSLENALQ 486
Cdd:PRK13648 163 VIILDEATSMLDPDARQNLLDLVR 186
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
3-215 |
6.59e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 62.88 E-value: 6.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 3 EFIYQMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFL--EPGAT---------VG 71
Cdd:PRK10575 9 DTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLdaQPLESwsskafarkVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 72 ILLQEPPLNEEKTVRGNVEEGLGDIFEKKARFEAIAEEmatnytdelmeemgklqeeldaadaweldsKIEQAMDALRCP 151
Cdd:PRK10575 89 YLPQQLPAAEGMTVRELVAIGRYPWHGALGRFGAADRE------------------------------KVEEAISLVGLK 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 512463837 152 P-ADEPVTHLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAE---SVLWLEQHLAKYPG-AVLAVTHD 215
Cdd:PRK10575 139 PlAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAhqvDVLALVHRLSQERGlTVIAVLHD 207
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
322-381 |
6.60e-11 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 63.94 E-value: 6.60e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 512463837 322 VEVKDLEKGFDGR----VLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVG 381
Cdd:COG1135 2 IELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVD 65
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
319-485 |
8.59e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 62.55 E-value: 8.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 319 NQVVEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGL-----EQPDSGEVKV-GQTVQLSYVDQG 392
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLfGRNIYSPDVDPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 393 R-----------ENIDPEKTVWEVVSDGLDY--IVVGQNEMPSRAylsAFGFKGA---DQQK------PSKvLSGGERNR 450
Cdd:PRK14267 82 EvrrevgmvfqyPNPFPHLTIYDNVAIGVKLngLVKSKKELDERV---EWALKKAalwDEVKdrlndyPSN-LSGGQRQR 157
|
170 180 190
....*....|....*....|....*....|....*
gi 512463837 451 LNLALTLKQGGNLILLDEPTNDLDVETLSSLENAL 485
Cdd:PRK14267 158 LVIARALAMKPKILLMDEPTANIDPVGTAKIEELL 192
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
11-222 |
9.28e-11 |
|
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: 64.38 E-value: 9.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 11 VRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFL-----------EPGATVGILLQEPPL 79
Cdd:COG4618 338 VVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLdgadlsqwdreELGRHIGYLPQDVEL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 80 NEeKTVRGNVeeglgdifekkARFEAIaeematnyTDELMEEMGKLqeeldaADAWELdskIeqamdaLRCP-----PAD 154
Cdd:COG4618 418 FD-GTIAENI-----------ARFGDA--------DPEKVVAAAKL------AGVHEM---I------LRLPdgydtRIG 462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 512463837 155 EPVTHLSGGERRRVALAklllsepdllllDEPTNHLDAESvlwlEQHL------AKYPGA-VLAVTHDRYFLDHV 222
Cdd:COG4618 463 EGGARLSGGQRQRIGLAralygdprlvvlDEPNSNLDDEG----EAALaaairaLKARGAtVVVITHRPSLLAAV 533
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
322-497 |
1.03e-10 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 61.86 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDLEKGF--DGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTV----------QLSY 388
Cdd:cd03251 1 VEFKNVTFRYpgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIdGHDVrdytlaslrrQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 389 VDQG--------RENI---DPEKTVWEVVS-----DGLDYIvvgqNEMPSrAYLSAFGFKGadqqkpSKvLSGGERNRLN 452
Cdd:cd03251 81 VSQDvflfndtvAENIaygRPGATREEVEEaaraaNAHEFI----MELPE-GYDTVIGERG------VK-LSGGQRQRIA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 512463837 453 LALTLKQGGNLILLDEPTNDLDVET----LSSLENALQNfpGCAVVISH 497
Cdd:cd03251 149 IARALLKDPPILILDEATSALDTESerlvQAALERLMKN--RTTFVIAH 195
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
9-191 |
1.04e-10 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 61.61 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 9 KNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEPGATV----------GILLQEPP 78
Cdd:cd03266 9 KRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVkepaearrrlGFVSDSTG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 79 LNEEKTVRGNVEeglgdIFekkARFEAIAEEMATNYTDELMEEMGklqeeldaadaweldskieqaMDALRcppaDEPVT 158
Cdd:cd03266 89 LYDRLTARENLE-----YF---AGLYGLKGDELTARLEELADRLG---------------------MEELL----DRRVG 135
|
170 180 190
....*....|....*....|....*....|...
gi 512463837 159 HLSGGERRRVALAKLLLSEPDLLLLDEPTNHLD 191
Cdd:cd03266 136 GFSTGMRQKVAIARALVHDPPVLLLDEPTTGLD 168
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
16-215 |
1.09e-10 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 62.19 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 16 GDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLE------PGATVGILLQEPPLNEEKTVRGNV 89
Cdd:COG4525 18 QPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDgvpvtgPGADRGVVFQKDALLPWLNVLDNV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 90 EEGLGDIFEKKARFEAIAEEMatnytdelMEEMGkLQeelDAADAweldskieqamdalrcppadePVTHLSGGERRRVA 169
Cdd:COG4525 98 AFGLRLRGVPKAERRARAEEL--------LALVG-LA---DFARR---------------------RIWQLSGGMRQRVG 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 512463837 170 LAKLLLSEPDLLLLDEPTNHLDA---ESV------LWLEQHLakypgAVLAVTHD 215
Cdd:COG4525 145 IARALAADPRFLLMDEPFGALDAltrEQMqellldVWQRTGK-----GVFLITHS 194
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
7-172 |
1.18e-10 |
|
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: 61.68 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEpGATV-----------GIL-- 73
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFD-GEDItglppheiarlGIGrt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 74 LQEPPLNEEKTVRGNVE------EGLGDIFEKKARFEAIAEEMAtnytDELMEEMGklqeeldaadaweLDSKieqamda 147
Cdd:cd03219 81 FQIPRLFPELTVLENVMvaaqarTGSGLLLARARREEREARERA----EELLERVG-------------LADL------- 136
|
170 180
....*....|....*....|....*
gi 512463837 148 lrcppADEPVTHLSGGERRRVALAK 172
Cdd:cd03219 137 -----ADRPAGELSYGQQRRLEIAR 156
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
7-215 |
1.34e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 62.02 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLE------PGATVGILLQEPPLN 80
Cdd:PRK11248 3 QISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDgkpvegPGAERGVVFQNEGLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 81 EEKTVRGNVEEGLGDIFEKKARFEAIAEEMATnytdelmeemgklQEELDAADAweldskieqamdalrcppadEPVTHL 160
Cdd:PRK11248 83 PWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLK-------------KVGLEGAEK--------------------RYIWQL 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 512463837 161 SGGERRRVALAKLLLSEPDLLLLDEPTNHLDA-------ESVLWLEQHLAKypgAVLAVTHD 215
Cdd:PRK11248 130 SGGQRQRVGIARALAANPQLLLLDEPFGALDAftreqmqTLLLKLWQETGK---QVLLITHD 188
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
21-191 |
1.35e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 61.52 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 21 LDNVT-------MAF----YPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLE-------PGAT--VGILLQEPPLN 80
Cdd:PRK10771 4 LTDITwlyhhlpMRFdltvERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNgqdhtttPPSRrpVSMLFQENNLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 81 EEKTVRGNVEEGLGDIF----EKKARFEAIAEEMAtnytdelmeemgklqeeldaadaweldskIEQAMDALrcpPAdep 156
Cdd:PRK10771 84 SHLTVAQNIGLGLNPGLklnaAQREKLHAIARQMG-----------------------------IEDLLARL---PG--- 128
|
170 180 190
....*....|....*....|....*....|....*
gi 512463837 157 vtHLSGGERRRVALAKLLLSEPDLLLLDEPTNHLD 191
Cdd:PRK10771 129 --QLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
16-216 |
1.39e-10 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 64.03 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 16 GDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEpG------------ATVGILLQEPPL-NEe 82
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILID-GvdirdltleslrRQIGVVPQDTFLfSG- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 83 kTVRGNVeeGLGDIfekkarfeaiaeematNYTDELMEEMgklqeeLDAADAWELdskIEQAMDALrcppaDEPV----T 158
Cdd:COG1132 429 -TIRENI--RYGRP----------------DATDEEVEEA------AKAAQAHEF---IEALPDGY-----DTVVgergV 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 512463837 159 HLSGGERRRVALAklllsepdllllDEPTNHLDAESvlwlEQHLAKypgAVLAVTHDR 216
Cdd:COG1132 476 NLSGGQRQRIAIArallkdppililDEATSALDTET----EALIQE---ALERLMKGR 526
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
321-482 |
1.63e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 61.47 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 321 VVEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGL-----EQPDSGEVKV-GQTVQLSYVDQGRE 394
Cdd:PRK14247 3 KIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLdGQDIFKMDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 395 NID---------PEKTVWEVVSDG--LDYIVVGQNEMPSRAYLSAFGFKGADQQK-----PSKVLSGGERNRLNLALTLK 458
Cdd:PRK14247 83 RVQmvfqipnpiPNLSIFENVALGlkLNRLVKSKKELQERVRWALEKAQLWDEVKdrldaPAGKLSGGQQQRLCIARALA 162
|
170 180
....*....|....*....|....
gi 512463837 459 QGGNLILLDEPTNDLDVETLSSLE 482
Cdd:PRK14247 163 FQPEVLLADEPTANLDPENTAKIE 186
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
308-477 |
1.63e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 63.69 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 308 EIQIPT--PPRLGNQVVEVKDLEKGFDGR--VLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQT 383
Cdd:PRK11160 323 EVTFPTtsTAAADQVSLTLNNVSFTYPDQpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQ 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 384 -----------VQLSYVDQG--------RENI---DPEKT------VWEVVsdGLDYIVvgQNEMPSRAYLSafgfKGAD 435
Cdd:PRK11160 403 piadyseaalrQAISVVSQRvhlfsatlRDNLllaAPNASdealieVLQQV--GLEKLL--EDDKGLNAWLG----EGGR 474
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 512463837 436 QqkpskvLSGGERNRLNLALTLKQGGNLILLDEPTNDLDVET 477
Cdd:PRK11160 475 Q------LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAET 510
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
332-474 |
1.66e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 61.27 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 332 DGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTV----------QLSYVDQgrenidPEK 400
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFeGEDIstlkpeiyrqQVSYCAQ------TPT 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 512463837 401 TVWEVVSDGL--DYIVVGQNEMPSR--AYLSAFGFKGADQQKPSKVLSGGERNRLNLALTLKQGGNLILLDEPTNDLD 474
Cdd:PRK10247 92 LFGDTVYDNLifPWQIRNQQPDPAIflDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
324-498 |
1.67e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 61.87 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 324 VKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVkvgqtvqlSYVDQGRENID----PE 399
Cdd:PRK11701 9 VRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV--------HYRMRDGQLRDlyalSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 400 -------KTVWEVV----SDGLDYIV-----VGQNEMPS--RAYlsafgfkGADQQKPSKVL-----------------S 444
Cdd:PRK11701 81 aerrrllRTEWGFVhqhpRDGLRMQVsaggnIGERLMAVgaRHY-------GDIRATAGDWLerveidaariddlpttfS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 512463837 445 GGERNRLNLALTLKQGGNLILLDEPTNDLDVETLSSLENALQNFP---GCAVVI-SHD 498
Cdd:PRK11701 154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVrelGLAVVIvTHD 211
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
325-474 |
1.68e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 61.45 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 325 KDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQ--TVQLSYVDQGRENID---PE 399
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDedISLLPLHARARRGIGylpQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 400 KTVWEVVS--DGL-------DYIVVGQNEMPSRAYLSAFGFKGAdQQKPSKVLSGGERNRLNLALTLKQGGNLILLDEPT 470
Cdd:PRK10895 87 ASIFRRLSvyDNLmavlqirDDLSAEQREDRANELMEEFHIEHL-RDSMGQSLSGGERRRVEIARALAANPKFILLDEPF 165
|
....
gi 512463837 471 NDLD 474
Cdd:PRK10895 166 AGVD 169
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-254 |
2.28e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 61.31 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 1 MGEFIYQMKNVR-KAHGDKVI-LDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEPGAT--------- 69
Cdd:PRK13648 3 DKNSIIVFKNVSfQYQSDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAItddnfeklr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 70 --VGILLQEPPlNE--EKTVRGNVEEGLgdifekkarfeaiaEEMATNYtDELMEEMGKLQEELDAADAweldskieqam 145
Cdd:PRK13648 83 khIGIVFQNPD-NQfvGSIVKYDVAFGL--------------ENHAVPY-DEMHRRVSEALKQVDMLER----------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 146 dalrcppADEPVTHLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAE---SVLWLEQHL-AKYPGAVLAVTHDryfLDH 221
Cdd:PRK13648 136 -------ADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDarqNLLDLVRKVkSEHNITIISITHD---LSE 205
|
250 260 270
....*....|....*....|....*....|....*
gi 512463837 222 VAG--WICEVDRGKLYPyEGNYSTYLEKKAERLEV 254
Cdd:PRK13648 206 AMEadHVIVMNKGTVYK-EGTPTEIFDHAEELTRI 239
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
7-228 |
2.48e-10 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 60.78 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPS------NGEAFLEPGAT-------VGIL 73
Cdd:COG1126 3 EIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDsgtitvDGEDLTDSKKDinklrrkVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 74 LQEPPLNEEKTVRGNVEEGLgdIFEKKARFEAiAEEMAtnytDELMEEMGkLqeeLDAADAWeldskieqamdalrcpPA 153
Cdd:COG1126 83 FQQFNLFPHLTVLENVTLAP--IKVKKMSKAE-AEERA----MELLERVG-L---ADKADAY----------------PA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 154 depvtHLSGGERRRVA------------LaklllsepdlllLDEPTNHLDAESVlwleqhlakypGAVLA---------- 211
Cdd:COG1126 136 -----QLSGGQQQRVAiaralamepkvmL------------FDEPTSALDPELV-----------GEVLDvmrdlakegm 187
|
250 260 270
....*....|....*....|....*....|.
gi 512463837 212 ----VTH---------DR-YFLDHvaGWICE 228
Cdd:COG1126 188 tmvvVTHemgfarevaDRvVFMDG--GRIVE 216
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
337-497 |
2.72e-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: 60.59 E-value: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 337 IKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVG----QTV-------QLSYVDQ------G--RENID 397
Cdd:cd03244 20 LKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDgvdiSKIglhdlrsRISIIPQdpvlfsGtiRSNLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 398 P-----EKTVWEVVSD-GLDYIVVGQNEMpsraylsafgfKGADQQKPSKVLSGGERNRLNLALTLKQGGNLILLDEPTN 471
Cdd:cd03244 100 PfgeysDEELWQALERvGLKEFVESLPGG-----------LDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATA 168
|
170 180
....*....|....*....|....*...
gi 512463837 472 DLDVETLSSLENALQ-NFPGCAVV-ISH 497
Cdd:cd03244 169 SVDPETDALIQKTIReAFKDCTVLtIAH 196
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
8-215 |
3.45e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 60.51 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 8 MKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEPGATVGILLQEP------PLNE 81
Cdd:PRK09544 7 LENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLyldttlPLTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 82 EK--TVRGNVEEGlgDIFEKKARFEAiaeematnytdelmeemGKLqeeldaadaweldskieqamdalrcppADEPVTH 159
Cdd:PRK09544 87 NRflRLRPGTKKE--DILPALKRVQA-----------------GHL---------------------------IDAPMQK 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 160 LSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAESVLWL----EQHLAKYPGAVLAVTHD 215
Cdd:PRK09544 121 LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALydliDQLRRELDCAVLMVSHD 180
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
5-475 |
3.56e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.33 E-value: 3.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 5 IYQMKNVRKAH-GDKViLDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGE--------AFLEP----GATVG 71
Cdd:PRK10762 4 LLQLKGIDKAFpGVKA-LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSilylgkevTFNGPkssqEAGIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 72 ILLQEPPLNEEKTVRGNveeglgdIF---EKKARFEAIAeematnyTDELMEEMGKLQEELDAADAweldskieqamdal 148
Cdd:PRK10762 83 IIHQELNLIPQLTIAEN-------IFlgrEFVNRFGRID-------WKKMYAEADKLLARLNLRFS-------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 149 rcppADEPVTHLSGGERRRVALAKLLLSEPDLLLLDEPTNHL-DAESvlwlEQhlakypgavlavthdryfLDHVAGWIC 227
Cdd:PRK10762 135 ----SDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTET----ES------------------LFRVIRELK 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 228 EVDRGKLYpyegnystylekkaerlevagkkdakLQKRLK------DELAWVRSGQ----KARQAKNKARLerYEQMVEE 297
Cdd:PRK10762 189 SQGRGIVY--------------------------ISHRLKeifeicDDVTVFRDGQfiaeREVADLTEDSL--IEMMVGR 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 298 --AEQYKKLDfeeiQIPTPPRLgnqvvEVKDLeKGFDgrvlIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDS 375
Cdd:PRK10762 241 klEDQYPRLD----KAPGEVRL-----KVDNL-SGPG----VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTS 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 376 GEVKV-GQTVQ-----------LSYV--DQGRENIDPEKTVWEVVS-DGLDY-------IVVGQNEMPSRAYLSAFGFKG 433
Cdd:PRK10762 307 GYVTLdGHEVVtrspqdglangIVYIseDRKRDGLVLGMSVKENMSlTALRYfsraggsLKHADEQQAVSDFIRLFNIKT 386
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 512463837 434 ADQQKPSKVLSGGERNRLNLALTLKQGGNLILLDEPTNDLDV 475
Cdd:PRK10762 387 PSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDV 428
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
7-171 |
3.82e-10 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 60.44 E-value: 3.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEpGATV-----------GIL-- 73
Cdd:COG0411 6 EVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFD-GRDItglpphriarlGIArt 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 74 LQEPPLNEEKTVRGNVE--------EGLGDI---FEKKARFEAIAEEMAtnytDELMEEMGklqeeldaadaweLDSKie 142
Cdd:COG0411 85 FQNPRLFPELTVLENVLvaaharlgRGLLAAllrLPRARREEREARERA----EELLERVG-------------LADR-- 145
|
170 180
....*....|....*....|....*....
gi 512463837 143 qamdalrcppADEPVTHLSGGERRRVALA 171
Cdd:COG0411 146 ----------ADEPAGNLSYGQQRRLEIA 164
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
313-510 |
3.99e-10 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 62.43 E-value: 3.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 313 TPPRLgNQVVEVKDLEKGFDGR----VLiKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEV---------- 378
Cdd:TIGR00958 471 APLNL-EGLIEFQDVSFSYPNRpdvpVL-KGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVlldgvplvqy 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 379 ----------KVGQTVQLsYVDQGRENI--------DPEKTVWEVVSDGLDYIvvgqNEMPsRAYLSAFGFKGadQQkps 440
Cdd:TIGR00958 549 dhhylhrqvaLVGQEPVL-FSGSVRENIaygltdtpDEEIMAAAKAANAHDFI----MEFP-NGYDTEVGEKG--SQ--- 617
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 512463837 441 kvLSGGERNRLNLALTLKQGGNLILLDEPTNDLDVETlsslENALQNFPGCA----VVISHdRWFLDRTCTHIL 510
Cdd:TIGR00958 618 --LSGGQKQRIAIARALVRKPRVLILDEATSALDAEC----EQLLQESRSRAsrtvLLIAH-RLSTVERADQIL 684
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
15-203 |
4.00e-10 |
|
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: 58.86 E-value: 4.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 15 HGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEaflepgatvgILLQE-PPLNEEKTVRGNVeegl 93
Cdd:cd03247 12 EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGE----------ITLDGvPVSDLEKALSSLI---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 94 gdifekkarfeAIAEEMATNYTDELMEEMGKlqeeldaadaweldskieqamdalrcppadepvtHLSGGERRRVALAKL 173
Cdd:cd03247 78 -----------SVLNQRPYLFDTTLRNNLGR----------------------------------RFSGGERQRLALARI 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 512463837 174 LLSEPDLLLLDEPTNHLDAE----------------SVLWLEQHLA 203
Cdd:cd03247 113 LLQDAPIVLLDEPTVGLDPIterqllslifevlkdkTLIWITHHLT 158
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
321-380 |
4.49e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 61.26 E-value: 4.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 321 VVEVKDLEK---------GFDGRVL------------IKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVK 379
Cdd:COG4586 1 IIEVENLSKtyrvyekepGLKGALKglfrreyreveaVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
.
gi 512463837 380 V 380
Cdd:COG4586 81 V 81
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-270 |
5.36e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 60.37 E-value: 5.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 1 MGEFIYQMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEpgatvgillqepplN 80
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVN--------------G 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 81 EE-KTVRGNveEGLGDIFEKKaRFEAIAEEMATNYTD-ELMEEMGKLQEELDAADAWELDSKI---EQAMDALRCPPADE 155
Cdd:PRK10619 67 QTiNLVRDK--DGQLKVADKN-QLRLLRTRLTMVFQHfNLWSHMTVLENVMEAPIQVLGLSKQearERAVKYLAKVGIDE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 156 ------PVtHLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAE---SVLWLEQHLAKYPGAVLAVTHDRYFLDHVAGWI 226
Cdd:PRK10619 144 raqgkyPV-HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPElvgEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHV 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 512463837 227 CEVDRGKlypyegnystyLEKKAERLEVAGK-KDAKLQKRLKDEL 270
Cdd:PRK10619 223 IFLHQGK-----------IEEEGAPEQLFGNpQSPRLQQFLKGSL 256
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
16-234 |
5.61e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 60.59 E-value: 5.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 16 GDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFL-----------EPGATVGILLQEP------P 78
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIrgepitkenirEVRKFVGLVFQNPddqifsP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 79 LNEEKTVRGNVEEGLGdifekkarfeaiaEEMATNYTDELMEEMGklqeeldaadaweldskIEQAMDalRCPpadepvT 158
Cdd:PRK13652 95 TVEQDIAFGPINLGLD-------------EETVAHRVSSALHMLG-----------------LEELRD--RVP------H 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 159 HLSGGERRRVALAKLLLSEPDLLLLDEPTNHLD----AESVLWLEQHLAKYPGAVLAVTHDRYFLDHVAGWICEVDRGKL 234
Cdd:PRK13652 137 HLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDpqgvKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRI 216
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
329-473 |
5.93e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.85 E-value: 5.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 329 KGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTVQLSYVdqgRENID---------- 397
Cdd:PRK11288 12 KTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIdGQEMRFAST---TAALAagvaiiyqel 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 398 ---PEKTVWEvvsdgldYIVVGQneMPSRA--------------YLSAFGFKgADQQKPSKVLSGGERNRLNLALTLKQG 460
Cdd:PRK11288 89 hlvPEMTVAE-------NLYLGQ--LPHKGgivnrrllnyeareQLEHLGVD-IDPDTPLKYLSIGQRQMVEIAKALARN 158
|
170
....*....|...
gi 512463837 461 GNLILLDEPTNDL 473
Cdd:PRK11288 159 ARVIAFDEPTSSL 171
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
11-215 |
6.66e-10 |
|
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: 59.65 E-value: 6.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 11 VRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAflepgatvgillqepplneekTVRGNVE 90
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV---------------------RVAGLVP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 91 eglgdiFEKKARFEAiaeEMATnytdeLMEEMGKLQEELDAADAWELDSKI------------EQAMDALRCPP-ADEPV 157
Cdd:cd03267 86 ------WKRRKKFLR---RIGV-----VFGQKTQLWWDLPVIDSFYLLAAIydlpparfkkrlDELSELLDLEElLDTPV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 512463837 158 THLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAESVL----WLEQHLAKYPGAVLAVTHD 215
Cdd:cd03267 152 RQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQEnirnFLKEYNRERGTTVLLTSHY 213
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
321-497 |
6.77e-10 |
|
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: 59.71 E-value: 6.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 321 VVEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSG-EVKV-GQTVqlsyvdqGRENI-- 396
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLfGERR-------GGEDVwe 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 397 ----------------DPEKTVWEVVSDGL-DYIVVGQN---EMPSRA--YLSAFGFkGADQQKPSKVLSGGERNRLNLA 454
Cdd:COG1119 76 lrkriglvspalqlrfPRDETVLDVVLSGFfDSIGLYREptdEQRERAreLLELLGL-AHLADRPFGTLSQGEQRRVLIA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 512463837 455 LTLKQGGNLILLDEPTNDLDV---ETLSSLENALQNFPGCAVV-ISH 497
Cdd:COG1119 155 RALVKDPELLILDEPTAGLDLgarELLLALLDKLAAEGAPTLVlVTH 201
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
321-537 |
9.03e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 59.64 E-value: 9.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 321 VVEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGL----EQPDSGEVKVGQTVQ----------- 385
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdKSAGSHIELLGRTVQregrlardirk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 386 ----LSYVDQgRENIDPEKTVWEVVSDG-----------LDYIVVGQNEMPSRAyLSAFGFKGADQQKPSkVLSGGERNR 450
Cdd:PRK09984 84 sranTGYIFQ-QFNLVNRLSVLENVLIGalgstpfwrtcFSWFTREQKQRALQA-LTRVGMVHFAHQRVS-TLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 451 LNLALTLKQGGNLILLDEPTNDLDVET----LSSLENALQNFPGCAVVISHDRWFLDRTCTHILAwegnFEEGKWFwFEG 526
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESarivMDTLRDINQNDGITVVVTLHQVDYALRYCERIVA----LRQGHVF-YDG 235
|
250
....*....|.
gi 512463837 527 NFEGYEKNKIE 537
Cdd:PRK09984 236 SSQQFDNERFD 246
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
10-216 |
1.60e-09 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 59.71 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 10 NVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEafLEPGAT-----------VGILLQEPP 78
Cdd:PRK10851 7 NIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGH--IRFHGTdvsrlhardrkVGFVFQHYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 79 LNEEKTVRGNVEEGLgDIFEKKARfeaiaeematnytdelmeemgklqeeldaADAWELDSKIEQAMDALRCPP-ADEPV 157
Cdd:PRK10851 85 LFRHMTVFDNIAFGL-TVLPRRER-----------------------------PNAAAIKAKVTQLLEMVQLAHlADRYP 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 512463837 158 THLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDA----ESVLWLEQHLAKYPGAVLAVTHDR 216
Cdd:PRK10851 135 AQLSGGQKQRVALARALAVEPQILLLDEPFGALDAqvrkELRRWLRQLHEELKFTSVFVTHDQ 197
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-223 |
2.00e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.21 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 29 YPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEPgaTVGILLQEPPLNEEKTVRgnveeglgdifekkARFEAIAE 108
Cdd:PRK13409 363 YEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPEL--KISYKPQYIKPDYDGTVE--------------DLLRSITD 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 109 EMATNYTD-ELMEEMGklqeeldaadaweldskIEQAMDalrcppadEPVTHLSGGERRRVALAKLLLSEPDLLLLDEPT 187
Cdd:PRK13409 427 DLGSSYYKsEIIKPLQ-----------------LERLLD--------KNVKDLSGGELQRVAIAACLSRDADLYLLDEPS 481
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 512463837 188 NHLDAE---SVLWLEQHLAKYPGA-VLAVTHDRYFLDHVA 223
Cdd:PRK13409 482 AHLDVEqrlAVAKAIRRIAEEREAtALVVDHDIYMIDYIS 521
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
318-477 |
2.16e-09 |
|
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: 57.06 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 318 GNQVVEVKDLekgfDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTVQ----------- 385
Cdd:cd03215 1 GEPVLEVRGL----SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLdGKPVTrrsprdairag 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 386 LSYV--DQGRENIDPEKTVWEVVSdgldyivvgqnempSRAYLSafgfkGADQQkpsKVLsggernrlnLALTLKQGGNL 463
Cdd:cd03215 77 IAYVpeDRKREGLVLDLSVAENIA--------------LSSLLS-----GGNQQ---KVV---------LARWLARDPRV 125
|
170
....*....|....
gi 512463837 464 ILLDEPTNDLDVET 477
Cdd:cd03215 126 LILDEPTRGVDVGA 139
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
19-194 |
2.17e-09 |
|
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: 57.88 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 19 VILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGE--------AFLEPG---ATVGILLQEpplneektvrg 87
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRvlvdghdlALADPAwlrRQVGVVLQE----------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 88 NVeeglgdIFEKkarfeAIAEEMATnyTDELMEeMGKLQEELDAADAWELDSKIEQAMDALrcppADEPVTHLSGGERRR 167
Cdd:cd03252 85 NV------LFNR-----SIRDNIAL--ADPGMS-MERVIEAAKLAGAHDFISELPEGYDTI----VGEQGAGLSGGQRQR 146
|
170 180
....*....|....*....|....*..
gi 512463837 168 VALAKLLLSEPDLLLLDEPTNHLDAES 194
Cdd:cd03252 147 IAIARALIHNPRILIFDEATSALDYES 173
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
325-498 |
2.17e-09 |
|
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: 58.42 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 325 KDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTV------QLSYVDqgRENID 397
Cdd:cd03294 28 EEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIdGQDIaamsrkELRELR--RKKIS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 398 ---------PEKTVWEVVSDGLDYIVVGQNEMPSRAY--LSAFGFKGADQQKPSKvLSGGERNRLNLALTLKQGGNLILL 466
Cdd:cd03294 106 mvfqsfallPHRTVLENVAFGLEVQGVPRAEREERAAeaLELVGLEGWEHKYPDE-LSGGMQQRVGLARALAVDPDILLM 184
|
170 180 190
....*....|....*....|....*....|....*....
gi 512463837 467 DEPTNDLD-------VETLSSLENALQNfpgCAVVISHD 498
Cdd:cd03294 185 DEAFSALDplirremQDELLRLQAELQK---TIVFITHD 220
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
26-234 |
3.05e-09 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 57.12 E-value: 3.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 26 MAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGE--------AFLEPGA-TVGILLQEPPLNEEKTVRGNVEEGLGDI 96
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRvlingvdvTAAPPADrPVSMLFQENNLFAHLTVEQNVGLGLSPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 97 F----EKKARFEAIAEEMAtnytdeLMEEMGKLQEELdaadaweldskieqamdalrcppadepvthlSGGERRRVALAK 172
Cdd:cd03298 99 LkltaEDRQAIEVALARVG------LAGLEKRLPGEL-------------------------------SGGERQRVALAR 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 512463837 173 LLLSEPDLLLLDEPTNHLDAE-----SVLWLEQHlAKYPGAVLAVTHDRYFLDHVAGWICEVDRGKL 234
Cdd:cd03298 142 VLVRDKPVLLLDEPFAALDPAlraemLDLVLDLH-AETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
318-498 |
3.05e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 59.74 E-value: 3.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 318 GNQVVEVkdlekgfdgrvlIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTV------------ 384
Cdd:PRK10535 17 GEEQVEV------------LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVaGQDVatldadalaqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 385 --QLSYVDQgRENIDPEKTVWEVVSDGLDYIVVGQNEMPSRA--YLSAFGFKGADQQKPSKvLSGGERNRLNLALTLKQG 460
Cdd:PRK10535 85 reHFGFIFQ-RYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAqeLLQRLGLEDRVEYQPSQ-LSGGQQQRVSIARALMNG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 512463837 461 GNLILLDEPTNDLD----VETLSSLENaLQNFPGCAVVISHD 498
Cdd:PRK10535 163 GQVILADEPTGALDshsgEEVMAILHQ-LRDRGHTVIIVTHD 203
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
321-381 |
3.45e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 59.29 E-value: 3.45e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 512463837 321 VVEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVG 381
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIG 71
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
334-497 |
4.10e-09 |
|
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: 57.10 E-value: 4.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 334 RVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTV----------QLSYVDQG--------RE 394
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLdGKPIsqyehkylhsKVSLVGQEpvlfarslQD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 395 NID---PEKTVWEVV-----SDGLDYIvvgqNEMPSrAYLSAFGFKGAdqqkpskVLSGGERNRLNLALTLKQGGNLILL 466
Cdd:cd03248 107 NIAyglQSCSFECVKeaaqkAHAHSFI----SELAS-GYDTEVGEKGS-------QLSGGQKQRVAIARALIRNPQVLIL 174
|
170 180 190
....*....|....*....|....*....|...
gi 512463837 467 DEPTNDLDVETLSSLENALQNFPG--CAVVISH 497
Cdd:cd03248 175 DEATSALDAESEQQVQQALYDWPErrTVLVIAH 207
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
30-234 |
4.23e-09 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 58.58 E-value: 4.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 30 PGAKI-GVVGPNGAGKSSILKIMAGLDQPSNGEAFLEpGAT----------------VGILLQEPPLNEEKTVRGNVEEG 92
Cdd:TIGR02142 21 PGQGVtAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLN-GRTlfdsrkgiflppekrrIGYVFQEARLFPHLSVRGNLRYG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 93 L--GDIFEKKARFEAIAEEMAtnytdelmeeMGKLqeeldaadaweldskieqamdaLRCPPADepvthLSGGERRRVAL 170
Cdd:TIGR02142 100 MkrARPSERRISFERVIELLG----------IGHL----------------------LGRLPGR-----LSGGEKQRVAI 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 512463837 171 AKLLLSEPDLLLLDEPTNHLD----AESVLWLEQHLAKYPGAVLAVTHDRYFLDHVAGWICEVDRGKL 234
Cdd:TIGR02142 143 GRALLSSPRLLLMDEPLAALDdprkYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRV 210
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
322-497 |
4.66e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.03 E-value: 4.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQTV----------------- 384
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINynkldhklaaqlgigii 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 385 --QLSYVDQ--GRENI----DPEKTVWEVVsdgldyiVVGQNEMPSRA--YLSAFGFKgADQQKPSKVLSGGERNRLNLA 454
Cdd:PRK09700 86 yqELSVIDEltVLENLyigrHLTKKVCGVN-------IIDWREMRVRAamMLLRVGLK-VDLDEKVANLSISHKQMLEIA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 512463837 455 LTLKQGGNLILLDEPTNDL---DVETLSSLENALQNFPGCAVVISH 497
Cdd:PRK09700 158 KTLMLDAKVIIMDEPTSSLtnkEVDYLFLIMNQLRKEGTAIVYISH 203
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
30-171 |
4.84e-09 |
|
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: 58.19 E-value: 4.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 30 PGAKI-GVVGPNGAGKSSILKIMAGLDQPSNGEAFLEpGAT----------------VGILLQEPPLNEEKTVRGNVEEG 92
Cdd:COG4148 23 PGRGVtALFGPSGSGKTTLLRAIAGLERPDSGRIRLG-GEVlqdsargiflpphrrrIGYVFQEARLFPHLSVRGNLLYG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 93 L--GDIFEKKARFEAIAEematnytdelMEEMGKLqeeldaadaweLDSKIEQamdalrcppadepvthLSGGERRRVAL 170
Cdd:COG4148 102 RkrAPRAERRISFDEVVE----------LLGIGHL-----------LDRRPAT----------------LSGGERQRVAI 144
|
.
gi 512463837 171 A 171
Cdd:COG4148 145 G 145
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
328-474 |
4.96e-09 |
|
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: 56.50 E-value: 4.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 328 EKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPD---SGEVKVG----------QTVQLSYVDQGRE 394
Cdd:cd03233 14 GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNgipykefaekYPGEIIYVSEEDV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 395 NIdPEKTVWEVvsdgLDYIVVGQ-NEMpsraylsafgfkgadqqkpSKVLSGGERNRLNLALTLKQGGNLILLDEPTNDL 473
Cdd:cd03233 94 HF-PTLTVRET----LDFALRCKgNEF-------------------VRGISGGERKRVSIAEALVSRASVLCWDNSTRGL 149
|
.
gi 512463837 474 D 474
Cdd:cd03233 150 D 150
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
9-64 |
5.25e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 57.81 E-value: 5.25e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 512463837 9 KNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFL 64
Cdd:COG4152 5 KGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLW 60
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
321-498 |
5.55e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 57.43 E-value: 5.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 321 VVEVKDLEKGFDG---RVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTV----------QL 386
Cdd:PRK13650 4 IIEVKNLTFKYKEdqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIdGDLLteenvwdirhKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 387 SYVDQGRENIDPEKTVWEVVSDGLDYIVVGQNEMPSRAY--LSAFGFKGADQQKPSKvLSGGERNRLNLALTLKQGGNLI 464
Cdd:PRK13650 84 GMVFQNPDNQFVGATVEDDVAFGLENKGIPHEEMKERVNeaLELVGMQDFKEREPAR-LSGGQKQRVAIAGAVAMRPKII 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 512463837 465 LLDEPTNDLD----VETLSSLENALQNFPGCAVVISHD 498
Cdd:PRK13650 163 ILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHD 200
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
20-191 |
5.77e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 56.71 E-value: 5.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 20 ILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFL----------EPGA-----TVGILLQE----PPLN 80
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLvgqplhqmdeEARAklrakHVGFVFQSfmliPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 81 EEKTV------RGNVEeglgdifeKKARFEAIaeematnytdELMEEMGkLQEELDAADAweldskieqamdalrcppad 154
Cdd:PRK10584 105 ALENVelpallRGESS--------RQSRNGAK----------ALLEQLG-LGKRLDHLPA-------------------- 145
|
170 180 190
....*....|....*....|....*....|....*..
gi 512463837 155 epvtHLSGGERRRVALAKLLLSEPDLLLLDEPTNHLD 191
Cdd:PRK10584 146 ----QLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
284-521 |
5.84e-09 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 58.61 E-value: 5.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 284 NKARLERYEQMVEEAE-------------QYKKLDFEEIQIPTPprlgnqvvevkdlekgfDGRVLIKDLSFTLPRNGIV 350
Cdd:TIGR00954 419 KRPRVEEIESGREGGRnsnlvpgrgiveyQDNGIKFENIPLVTP-----------------NGDVLIESLSFEVPSGNNL 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 351 GVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQTVQLSYVDQG--------RENI----DPEKTVWEVVSDG--------- 409
Cdd:TIGR00954 482 LICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRpymtlgtlRDQIiypdSSEDMKRRGLSDKdleqildnv 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 410 -LDYIVvgQNEMpsraylsafGFKGAdqQKPSKVLSGGERNRLNLALTLKQGGNLILLDEPTNDLDVETLSSLENALQNF 488
Cdd:TIGR00954 562 qLTHIL--EREG---------GWSAV--QDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF 628
|
250 260 270
....*....|....*....|....*....|...
gi 512463837 489 PGCAVVISHdRWFLDRTCTHILAWEGnfeEGKW 521
Cdd:TIGR00954 629 GITLFSVSH-RKSLWKYHEYLLYMDG---RGGY 657
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
322-499 |
6.36e-09 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 57.17 E-value: 6.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDLEKGF--DGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDsGEVKV-----------------GQ 382
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIdgvswnsvplqkwrkafGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 383 TVQLSYVDQG--RENIDP-----EKTVWEVVSDgldyivvgqnempsraylsaFGFKGADQQKPSK----------VLSG 445
Cdd:cd03289 82 IPQKVFIFSGtfRKNLDPygkwsDEEIWKVAEE--------------------VGLKSVIEQFPGQldfvlvdggcVLSH 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 512463837 446 GERNRLNLALTLKQGGNLILLDEPTNDLDVETLSSLENAL-QNFPGCAVVISHDR 499
Cdd:cd03289 142 GHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLkQAFADCTVILSEHR 196
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
9-237 |
6.59e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 56.83 E-value: 6.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 9 KNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEPGAT------------VGILLQE 76
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDIsllplhararrgIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 77 PPLNEEKTVRGNveegLGDIFEKKarfEAIAEEMATNYTDELMEEMgklqeeldaadaweldsKIEQAMDALRcppadep 156
Cdd:PRK10895 87 ASIFRRLSVYDN----LMAVLQIR---DDLSAEQREDRANELMEEF-----------------HIEHLRDSMG------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 157 vTHLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAESVLWLE---QHLAKYPGAVLAVTHD-RYFLDhvagwICE---- 228
Cdd:PRK10895 136 -QSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKriiEHLRDSGLGVLITDHNvRETLA-----VCErayi 209
|
....*....
gi 512463837 229 VDRGKLYPY 237
Cdd:PRK10895 210 VSQGHLIAH 218
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
308-476 |
6.76e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 57.55 E-value: 6.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 308 EIQIPTPPRlGNQVVEVKDLEKGFDGR-----VLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQ 382
Cdd:PRK13631 9 KLKVPNPLS-DDIILRVKNLYCVFDEKqenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 383 TVQLSYVDQGRENIDPE-----------KTV--------WEVVSDGLDY------IVVGQNEMPSRA----YLSAFGFKG 433
Cdd:PRK13631 88 IYIGDKKNNHELITNPYskkiknfkelrRRVsmvfqfpeYQLFKDTIEKdimfgpVALGVKKSEAKKlakfYLNKMGLDD 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 512463837 434 ADQQKPSKVLSGGERNRLNLALTLKQGGNLILLDEPTNDLDVE 476
Cdd:PRK13631 168 SYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPK 210
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
326-526 |
7.61e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 57.03 E-value: 7.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 326 DLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQP-----DSGEVKVGQTVQLSYVDQ--------- 391
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYRDVlefrrrvgm 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 392 --GRENIDPEKTVWEVVSDGLDYIVVGQNEMP--SRAYLSAFGFKGADQQKPSKV---LSGGERNRLNLALTLKQGGNLI 464
Cdd:PRK14271 106 lfQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRgvAQARLTEVGLWDAVKDRLSDSpfrLSGGQQQLLCLARTLAVNPEVL 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 512463837 465 LLDEPTNDLDVETLSSLENALQNFPGCAVVIshdrwfldrTCTHILAWEGNFEEGKWFWFEG 526
Cdd:PRK14271 186 LLDEPTSALDPTTTEKIEEFIRSLADRLTVI---------IVTHNLAQAARISDRAALFFDG 238
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
36-215 |
7.66e-09 |
|
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: 56.58 E-value: 7.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 36 VVGPNGAGKSSILKIMAGLDQPSNGEAFLEpGA----------TVGILLQEPPLNEEKTVRGNVEEGLGDIFEKKARFEA 105
Cdd:cd03299 30 ILGPTGSGKSVLLETIAGFIKPDSGKILLN-GKditnlppekrDISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIER 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 106 IAEEMAtnytdelmeEMGKLQEELDaadaweldskieqamdalRCPpadepvTHLSGGERRRVALAKLLLSEPDLLLLDE 185
Cdd:cd03299 109 KVLEIA---------EMLGIDHLLN------------------RKP------ETLSGGEQQRVAIARALVVNPKILLLDE 155
|
170 180 190
....*....|....*....|....*....|....
gi 512463837 186 PTNHLDAESVLWLEQHLAK----YPGAVLAVTHD 215
Cdd:cd03299 156 PFSALDVRTKEKLREELKKirkeFGVTVLHVTHD 189
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
17-191 |
7.82e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 56.94 E-value: 7.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 17 DKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEaflepgatvgILLQEPPLNEEKTVRGNVEEGLGDI 96
Cdd:PRK13638 13 DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGA----------VLWQGKPLDYSKRGLLALRQQVATV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 97 FEKKarfeaiaeEMATNYTDeLMEEMGKLQEELDAADAwELDSKIEQAM---DALRCppADEPVTHLSGGERRRVALAKL 173
Cdd:PRK13638 83 FQDP--------EQQIFYTD-IDSDIAFSLRNLGVPEA-EITRRVDEALtlvDAQHF--RHQPIQCLSHGQKKRVAIAGA 150
|
170
....*....|....*...
gi 512463837 174 LLSEPDLLLLDEPTNHLD 191
Cdd:PRK13638 151 LVLQARYLLLDEPTAGLD 168
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
9-171 |
8.56e-09 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 56.19 E-value: 8.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 9 KNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEpG-----------ATVGI--LLQ 75
Cdd:COG1137 7 ENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLD-GedithlpmhkrARLGIgyLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 76 EPplneekTV-RG-NVEEGLGDIFE--KKARfEAIAEEMatnytDELMEEMGklqeeldaadaweldskIEQamdaLRCP 151
Cdd:COG1137 86 EA------SIfRKlTVEDNILAVLElrKLSK-KEREERL-----EELLEEFG-----------------ITH----LRKS 132
|
170 180
....*....|....*....|....
gi 512463837 152 PADEpvthLSGGERRRV----ALA 171
Cdd:COG1137 133 KAYS----LSGGERRRVeiarALA 152
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
5-191 |
1.15e-08 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 57.26 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 5 IYQMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLE------------PGATVgi 72
Cdd:PRK09452 14 LVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDgqdithvpaenrHVNTV-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 73 lLQEPPLNEEKTVRGNVEEGLgdifekkarfeaiaeematnytdelmeEMGKLQEEldaadawELDSKIeqaMDALRCPP 152
Cdd:PRK09452 92 -FQSYALFPHMTVFENVAFGL---------------------------RMQKTPAA-------EITPRV---MEALRMVQ 133
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 512463837 153 ----ADEPVTHLSGGERRRVALAKLLLSEPDLLLLDEPTNHLD 191
Cdd:PRK09452 134 leefAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
349-514 |
1.16e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 54.89 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 349 IVGVIGPNGVGKSTLFKTIVGLEQPDSgevkvgqtvqlsyvdqgrenidpEKTVWEVVSdgldyIVVgqnempsraylsa 428
Cdd:cd03222 27 VIGIVGPNGTGKTTAVKILAGQLIPNG-----------------------DNDEWDGIT-----PVY------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 429 fgfkgadqqKPSKV-LSGGERNRLNLALTLKQGGNLILLDEPTNDLDVETLSSLENALQNF----PGCAVVISHDRWFLD 503
Cdd:cd03222 66 ---------KPQYIdLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseegKKTALVVEHDLAVLD 136
|
170
....*....|.
gi 512463837 504 RTCTHILAWEG 514
Cdd:cd03222 137 YLSDRIHVFEG 147
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
21-221 |
1.26e-08 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 56.00 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 21 LDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLdQPSNGEaflepgatvgILLQEPPLNEEKTvrgnveeglgdifEKK 100
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGE----------ILLNGRPLSDWSA-------------AEL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 101 ARFEA-----------------IAEEMATNYTDELME-EMGKLQEELdaadawELDSKIeqamdalrcppaDEPVTHLSG 162
Cdd:COG4138 68 ARHRAylsqqqsppfampvfqyLALHQPAGASSEAVEqLLAQLAEAL------GLEDKL------------SRPLTQLSG 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 163 GERRRVALAK-------LLLSEPDLLLLDEPTNHLDA--ESVL--WLEQhLAKYPGAVLAVTHDryfLDH 221
Cdd:COG4138 130 GEWQRVRLAAvllqvwpTINPEGQLLLLDEPMNSLDVaqQAALdrLLRE-LCQQGITVVMSSHD---LNH 195
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
7-215 |
1.39e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 57.43 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAH----GDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGE--------AFLEPGATV---- 70
Cdd:PRK10535 6 ELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTyrvagqdvATLDADALAqlrr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 71 ---GILLQEPPLNEEKTVRGNVE-----EGLgdifEKKARFEAiaeematnyTDELMEEMGkLQEELDAadaweldskie 142
Cdd:PRK10535 86 ehfGFIFQRYHLLSHLTAAQNVEvpavyAGL----ERKQRLLR---------AQELLQRLG-LEDRVEY----------- 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 512463837 143 qamdalrcPPAdepvtHLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAES---VLWLEQHLAKYPGAVLAVTHD 215
Cdd:PRK10535 141 --------QPS-----QLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSgeeVMAILHQLRDRGHTVIIVTHD 203
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
322-498 |
1.44e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 55.81 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDsGEVKV-------GQTVQLSYVDQGR- 393
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVegrveffNQNIYERRVNLNRl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 394 ----ENIDPEKTVWEV-VSDGLDYIV--VGQNEMPSRAYLSAFGFKGADQ--------QKPSKVLSGGERNRLNLALTLK 458
Cdd:PRK14258 87 rrqvSMVHPKPNLFPMsVYDNVAYGVkiVGWRPKLEIDDIVESALKDADLwdeikhkiHKSALDLSGGQQQRLCIARALA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 512463837 459 QGGNLILLDEPTNDLDVETLSSLENALQNFP----GCAVVISHD 498
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrseLTMVIVSHN 210
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
7-61 |
1.92e-08 |
|
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: 54.59 E-value: 1.92e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 512463837 7 QMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGE 61
Cdd:cd03269 2 EVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGE 56
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
17-214 |
2.05e-08 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 56.74 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 17 DKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEPGATVGILLQEP--PLNeekTVRgnveeglg 94
Cdd:COG4178 375 GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQRPylPLG---TLR-------- 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 95 difekkarfEAIA-EEMATNYTDELMEE------MGKLQEELDAADAWeldSKIeqamdalrcppadepvthLSGGERRR 167
Cdd:COG4178 444 ---------EALLyPATAEAFSDAELREaleavgLGHLAERLDEEADW---DQV------------------LSLGEQQR 493
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 512463837 168 VALAKLLLSEPDLLLLDEPTNHLDAESVLWLEQHL-AKYPGA-VLAVTH 214
Cdd:COG4178 494 LAFARLLLHKPDWLFLDEATSALDEENEAALYQLLrEELPGTtVISVGH 542
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
332-497 |
2.13e-08 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 57.03 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 332 DGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEV--------------------KVGQTVQLsYVDQ 391
Cdd:TIGR02203 343 RDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQIlldghdladytlaslrrqvaLVSQDVVL-FNDT 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 392 GRENI---DPEKTVWEVVSDGL------DYIvvgqNEMPsraylsafgfKGADQQKPSK--VLSGGERNRLNLALTLKQG 460
Cdd:TIGR02203 422 IANNIaygRTEQADRAEIERALaaayaqDFV----DKLP----------LGLDTPIGENgvLLSGGQRQRLAIARALLKD 487
|
170 180 190
....*....|....*....|....*....|....*....
gi 512463837 461 GNLILLDEPTNDLDVETLSSLENALQNF-PG-CAVVISH 497
Cdd:TIGR02203 488 APILILDEATSALDNESERLVQAALERLmQGrTTLVIAH 526
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
321-487 |
2.14e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 55.17 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 321 VVEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTI--VGLEQPD---SGEVKVG---------QTVQL 386
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNghniysprtDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 387 syvdqgRENI-----DPEK---TVWEVVSDGL------DYIVVGQ------------NEMPSRAYLSAFGfkgadqqkps 440
Cdd:PRK14239 85 ------RKEIgmvfqQPNPfpmSIYENVVYGLrlkgikDKQVLDEavekslkgasiwDEVKDRLHDSALG---------- 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 512463837 441 kvLSGGERNRLNLALTLKQGGNLILLDEPTNDLDVETLSSLENALQN 487
Cdd:PRK14239 149 --LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLG 193
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
332-498 |
2.84e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 55.05 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 332 DGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQTVQlsYVDQGRENIDPEKTVWEVvsdglD 411
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVL--YFGKDIFQIDAIKLRKEV-----G 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 412 YIVVGQNEMP------SRAY-LSAFGFKGADQQK----------------------PSKVLSGGERNRLNLALTLKQGGN 462
Cdd:PRK14246 94 MVFQQPNPFPhlsiydNIAYpLKSHGIKEKREIKkiveeclrkvglwkevydrlnsPASQLSGGQQQRLTIARALALKPK 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 512463837 463 LILLDEPTNDLDVETLSSLENALQNFPG--CAVVISHD 498
Cdd:PRK14246 174 VLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHN 211
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
7-215 |
3.04e-08 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 54.02 E-value: 3.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAG-LDQP--SNGEAFLE-----PGAT----VGILL 74
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAfsASGEVLLNgrrltALPAeqrrIGILF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 75 QEPPLNEEKTVRGNVEEGLGDIFEKKARFEAIAEEMatnytdelmeemgklqEELDAADAWELDskieqamdalrcppad 154
Cdd:COG4136 83 QDDLLFPHLSVGENLAFALPPTIGRAQRRARVEQAL----------------EEAGLAGFADRD---------------- 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 512463837 155 ePVThLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDA---ESVL-WLEQHLAKYPGAVLAVTHD 215
Cdd:COG4136 131 -PAT-LSGGQRARVALLRALLAEPRALLLDEPFSKLDAalrAQFReFVFEQIRQRGIPALLVTHD 193
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-248 |
3.44e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 56.37 E-value: 3.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 20 ILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEaflepgatvgILLQEPPLNE--EKTVRGN---VEEGLg 94
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGE----------ILLNGQPIADysEAALRQAisvVSQRV- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 95 DIFEKKARFE-AIAEEMATnytDELMEEM------GKLQEELDAADAWeldskieqamdalrcppADEPVTHLSGGERRR 167
Cdd:PRK11160 424 HLFSATLRDNlLLAAPNAS---DEALIEVlqqvglEKLLEDDKGLNAW-----------------LGEGGRQLSGGEQRR 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 168 VALAKLLLSEPDLLLLDEPTNHLDAES---VLWLEQHLAKYPgAVLAVTHDRYFLDHVAGwICEVDRGKLYPYeGNYSTY 244
Cdd:PRK11160 484 LGIARALLHDAPLLLLDEPTEGLDAETerqILELLAEHAQNK-TVLMITHRLTGLEQFDR-ICVMDNGQIIEQ-GTHQEL 560
|
....
gi 512463837 245 LEKK 248
Cdd:PRK11160 561 LAQQ 564
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
8-234 |
3.82e-08 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 54.37 E-value: 3.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 8 MKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGE---AFLEPGAT--------------- 69
Cdd:PRK11264 6 VKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTirvGDITIDTArslsqqkglirqlrq 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 70 -VGILLQEPPLNEEKTVRGNVEEGlGDIFEKKARFEAIAEematnyTDELMEEMGKLQEEldaaDAWEldskieqamdal 148
Cdd:PRK11264 86 hVGFVFQNFNLFPHRTVLENIIEG-PVIVKGEPKEEATAR------ARELLAKVGLAGKE----TSYP------------ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 149 rcppadepvTHLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAE---SVLWLEQHLAKYPGAVLAVTHDRYFLDHVAGW 225
Cdd:PRK11264 143 ---------RRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPElvgEVLNTIRQLAQEKRTMVIVTHEMSFARDVADR 213
|
....*....
gi 512463837 226 ICEVDRGKL 234
Cdd:PRK11264 214 AIFMDQGRI 222
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
3-223 |
4.26e-08 |
|
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: 54.76 E-value: 4.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 3 EFIYQMK--NVRKAhgdkviLDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFL--------------EP 66
Cdd:TIGR04521 7 SYIYQPGtpFEKKA------LDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIdgrditakkkkklkDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 67 GATVGILLQEPplnE----EKTVRGNVEEG---LGdifekkarfeaIAEEMATNYTDELMEEMGkLQEELdaadawelds 139
Cdd:TIGR04521 81 RKKVGLVFQFP---EhqlfEETVYKDIAFGpknLG-----------LSEEEAEERVKEALELVG-LDEEY---------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 140 kieqamdALRCPpadepvTHLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAES---VLWLEQHLAKYPG-AVLAVTHD 215
Cdd:TIGR04521 136 -------LERSP------FELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGrkeILDLFKRLHKEKGlTVILVTHS 202
|
....*...
gi 512463837 216 ryfLDHVA 223
Cdd:TIGR04521 203 ---MEDVA 207
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
21-225 |
4.29e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 55.09 E-value: 4.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 21 LDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGeaflepgaTVGILLQEpplNEEKTVRGNVEEGLGDIFEKK 100
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTG--------TIEWIFKD---EKNKKKTKEKEKVLEKLVIQK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 101 ARFEAI----------------AEEMATNYTDELMEEMGKLQEELDAADAWELDSKIEQAM----DALRCPPADepvthL 160
Cdd:PRK13651 92 TRFKKIkkikeirrrvgvvfqfAEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVgldeSYLQRSPFE-----L 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 512463837 161 SGGERRRVALAKLLLSEPDLLLLDEPTNHLDAESV---LWLEQHLAKYPGAVLAVTHDryfLDHVAGW 225
Cdd:PRK13651 167 SGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVkeiLEIFDNLNKQGKTIILVTHD---LDNVLEW 231
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
322-499 |
4.99e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 55.74 E-value: 4.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDLEKGFDG-RVLIKDLSFTLPRNGIVGVIGPNGVGKSTLfktiVGLEQ----PDSGEVKV-GQ---TVQLS----- 387
Cdd:PRK13657 335 VEFDDVSFSYDNsRQGVEDVSFEAKPGQTVAIVGPTGAGKSTL----INLLQrvfdPQSGRILIdGTdirTVTRAslrrn 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 388 ----YVDQG------RENI---DPEKTVWEVV-----SDGLDYIvvgqnEMPSRAYLSAFGFKGadqqkpsKVLSGGERN 449
Cdd:PRK13657 411 iavvFQDAGlfnrsiEDNIrvgRPDATDEEMRaaaerAQAHDFI-----ERKPDGYDTVVGERG-------RQLSGGERQ 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 512463837 450 RLNLALTLKQGGNLILLDEPTNDLDVETLSSLENALQNfpgcavvISHDR 499
Cdd:PRK13657 479 RLAIARALLKDPPILILDEATSALDVETEAKVKAALDE-------LMKGR 521
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
321-387 |
5.21e-08 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 54.81 E-value: 5.21e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 512463837 321 VVEVKDLEKGFDGR----VLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTV-QLS 387
Cdd:PRK11153 1 MIELKNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVdGQDLtALS 73
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
16-214 |
5.30e-08 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 53.32 E-value: 5.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 16 GDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLdqpsngeafLEPGATVG-ILLQEPPLneektvrgnveeglg 94
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGR---------RTGLGVSGeVLINGRPL--------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 95 DIFEKKARFEAIAEEmatnytDELMEEMgKLQEELD-AAdaweldskieqamdALRCppadepvthLSGGERRRVALAKL 173
Cdd:cd03213 76 DKRSFRKIIGYVPQD------DILHPTL-TVRETLMfAA--------------KLRG---------LSGGERKRVSIALE 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 512463837 174 LLSEPDLLLLDEPTNHLD---AESVLWLEQHLAKYPGAVLAVTH 214
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDsssALQVMSLLRRLADTGRTIICSIH 169
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-475 |
5.78e-08 |
|
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: 55.46 E-value: 5.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 12 RKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKS----SILKIMAGLDQPSNGEAFLEpgatvGILLQEPPLNEEKTVRG 87
Cdd:COG4172 17 GQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFD-----GQDLLGLSERELRRIRG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 88 NveeGLGDIFEkkarfeaiaEEM-ATN--YT--DELMEEMgKLQEELDAADAWEldsKIEQAMDALRCPPADEPVT---H 159
Cdd:COG4172 92 N---RIAMIFQ---------EPMtSLNplHTigKQIAEVL-RLHRGLSGAAARA---RALELLERVGIPDPERRLDaypH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 160 -LSGGERRRV----AL--------AklllsepdllllDEPTNHLD----AEsVLWLEQHLAKYPG-AVLAVTHD----RY 217
Cdd:COG4172 156 qLSGGQRQRVmiamALanepdlliA------------DEPTTALDvtvqAQ-ILDLLKDLQRELGmALLLITHDlgvvRR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 218 FLDHVAgwiceV-DRGKLypyegnystylekkaerlevagkkdaklqkrlkdelawVRSGQKARqaknkarleryeqmVE 296
Cdd:COG4172 223 FADRVA-----VmRQGEI--------------------------------------VEQGPTAE--------------LF 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 297 EAEQ--YKK--LDFEEIQIPTPPRLGNQVV-EVKDL------EKGFDGRVL-----IKDLSFTLPRNGIVGVIGPNGVGK 360
Cdd:COG4172 246 AAPQhpYTRklLAAEPRGDPRPVPPDAPPLlEARDLkvwfpiKRGLFRRTVghvkaVDGVSLTLRRGETLGLVGESGSGK 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 361 STLFKTIVGLeQPDSGEVKV-GQTVQ-LSyvdqGREN-----------------IDPEKTVWEVVSDGLD--YIVVGQNE 419
Cdd:COG4172 326 STLGLALLRL-IPSEGEIRFdGQDLDgLS----RRALrplrrrmqvvfqdpfgsLSPRMTVGQIIAEGLRvhGPGLSAAE 400
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 420 MPSRAY--LSAFGFKGADQQKPSKVLSGGERNRLNLA--LTLKQggNLILLDEPTNDLDV 475
Cdd:COG4172 401 RRARVAeaLEEVGLDPAARHRYPHEFSGGQRQRIAIAraLILEP--KLLVLDEPTSALDV 458
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-234 |
6.80e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 53.76 E-value: 6.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 9 KNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGL-----DQPSNGEAFL-----------EPGATVGI 72
Cdd:PRK14247 7 RDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLdgqdifkmdviELRRRVQM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 73 LLQEPPLNEEKTVRGNVEEGLgdifeKKARFeaiaeemaTNYTDELMEemgKLQEELDAADAWEldsKIEQAMDAlrcpp 152
Cdd:PRK14247 87 VFQIPNPIPNLSIFENVALGL-----KLNRL--------VKSKKELQE---RVRWALEKAQLWD---EVKDRLDA----- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 153 adePVTHLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAESVLWLEQHL--AKYPGAVLAVTHDRYFLDHVAGWICEVD 230
Cdd:PRK14247 143 ---PAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFleLKKDMTIVLVTHFPQQAARISDYVAFLY 219
|
....
gi 512463837 231 RGKL 234
Cdd:PRK14247 220 KGQI 223
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
34-172 |
7.10e-08 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 53.09 E-value: 7.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 34 IGVVGPNGAGKSSILK-IMAGL-----DQPSNGEAFLEPGAT---VGILLQepplNEEKTVRGNVEEGLGDIF---EKKA 101
Cdd:COG0419 26 NLIVGPNGAGKSTILEaIRYALygkarSRSKLRSDLINVGSEeasVELEFE----HGGKRYRIERRQGEFAEFleaKPSE 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 512463837 102 RFEAIAEEMATNYTDELMEEMGKLQEELDAADAwELDSKIEQAMDALRCPPADEPVTHLSGGERRRVALAK 172
Cdd:COG0419 102 RKEALKRLLGLEIYEELKERLKELEEALESALE-ELAELQKLKQEILAQLSGLDPIETLSGGERLRLALAD 171
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
336-477 |
8.47e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 55.30 E-value: 8.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 336 LIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVK----VGQTVQLSYVDQGrenidpekTVWEVVSDGLD 411
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKhsgrISFSPQTSWIMPG--------TIKDNIIFGLS 512
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 512463837 412 YivvgqNEMPSRAYLSAFGFKGADQQKPSK----------VLSGGERNRLNLALTLKQGGNLILLDEPTNDLDVET 477
Cdd:TIGR01271 513 Y-----DEYRYTSVIKACQLEEDIALFPEKdktvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-214 |
8.67e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 53.63 E-value: 8.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 1 MGEFIYQMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKI---MAGLDqPS---------NGEAFLEPGA 68
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSinrMNDLN-PEvtitgsivyNGHNIYSPRT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 69 -TV------GILLQEP---PLneekTVRGNVEEGLgdifekkaRFEAIAEEmatNYTDELMEEmgklqeELDAADAWEld 138
Cdd:PRK14239 80 dTVdlrkeiGMVFQQPnpfPM----SIYENVVYGL--------RLKGIKDK---QVLDEAVEK------SLKGASIWD-- 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 512463837 139 skieQAMDALRcppadEPVTHLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAESVLWLEQHL--AKYPGAVLAVTH 214
Cdd:PRK14239 137 ----EVKDRLH-----DSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLlgLKDDYTMLLVTR 205
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
7-216 |
8.75e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 52.95 E-value: 8.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAH-GDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEPG--------------ATVG 71
Cdd:PRK10908 3 RFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHditrlknrevpflrRQIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 72 ILLQEPPLNEEKTVRGNVEEGLgdifekkarfeAIAeematnytdelmeemgklqeeldAADAWELDSKIEQAMD--ALR 149
Cdd:PRK10908 83 MIFQDHHLLMDRTVYDNVAIPL-----------IIA-----------------------GASGDDIRRRVSAALDkvGLL 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 150 CPPADEPVtHLSGGERRRVALAKLLLSEPDLLLLDEPTNHLD---AESVLWLEQHLAKYPGAVLAVTHDR 216
Cdd:PRK10908 129 DKAKNFPI-QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDdalSEGILRLFEEFNRVGVTVLMATHDI 197
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
337-497 |
9.81e-08 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 52.93 E-value: 9.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 337 IKDLSFTLPRNGIVGVIGPNGVGKStlfkTIVGLEQ----PDSGEVKV-GQTV----------QLSYVDQG--------R 393
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKS----TVVSLLErfydPTSGEILLdGVDIrdlnlrwlrsQIGLVSQEpvlfdgtiA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 394 ENI---DPEKTVWEVVS-----DGLDYIvvgqNEMPSRaYLSAFGFKGADqqkpskvLSGGERNRLNLALTLKQGGNLIL 465
Cdd:cd03249 95 ENIrygKPDATDEEVEEaakkaNIHDFI----MSLPDG-YDTLVGERGSQ-------LSGGQKQRIAIARALLRNPKILL 162
|
170 180 190
....*....|....*....|....*....|....
gi 512463837 466 LDEPTNDLDVETLSSLENALQNFPG--CAVVISH 497
Cdd:cd03249 163 LDEATSALDAESEKLVQEALDRAMKgrTTIVIAH 196
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
322-381 |
1.03e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 53.17 E-value: 1.03e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 512463837 322 VEVKDLEKGF-----DGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVG 381
Cdd:COG1101 2 LELKNLSKTFnpgtvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILID 66
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
320-385 |
1.04e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 53.07 E-value: 1.04e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 512463837 320 QVVEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTVQ 385
Cdd:PRK11300 4 PLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLrGQHIE 70
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
9-61 |
1.12e-07 |
|
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: 52.82 E-value: 1.12e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 512463837 9 KNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGE 61
Cdd:cd03224 4 ENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGS 56
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
266-496 |
1.13e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 55.02 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 266 LKDELAWVrsGQKARQAKNKARLERYEQMVEEAEQYKKLD-----FEEIQIP--TPPrlgnqvVEVKDLEKGFD--GRVL 336
Cdd:TIGR01257 874 LLQESYWL--GGEGCSTREERALEKTEPLTEEMEDPEHPEgindsFFERELPglVPG------VCVKNLVKIFEpsGRPA 945
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 337 IKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQTVQLSYVDQGRENID--PEKTV----WEVVSDGL 410
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGmcPQHNIlfhhLTVAEHIL 1025
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 411 DYIVV-------GQNEMpsRAYLSAFGFKgADQQKPSKVLSGGERNRLNLALTLKQGGNLILLDEPTNDLDVETLSSLEN 483
Cdd:TIGR01257 1026 FYAQLkgrsweeAQLEM--EAMLEDTGLH-HKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWD 1102
|
250
....*....|....
gi 512463837 484 ALQNF-PGCAVVIS 496
Cdd:TIGR01257 1103 LLLKYrSGRTIIMS 1116
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
331-474 |
1.18e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 53.58 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 331 FDGRVLIkDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQTVQLSYVDQgrENIDP------------ 398
Cdd:PRK13643 17 FASRALF-DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQ--KEIKPvrkkvgvvfqfp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 399 -----EKTVWEVVSDGLDYIVVGQNEMPSRAY--LSAFGFKGADQQKPSKVLSGGERNRLNLALTLKQGGNLILLDEPTN 471
Cdd:PRK13643 94 esqlfEETVLKDVAFGPQNFGIPKEKAEKIAAekLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTA 173
|
...
gi 512463837 472 DLD 474
Cdd:PRK13643 174 GLD 176
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
7-231 |
1.18e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 52.22 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAHgdkvilDNVTMAFYPGAKIgVVGPNGAGKSSILkimagldqpsngEAFLEpgATVGILlqePPlneektvR 86
Cdd:cd03240 5 SIRNIRSFH------ERSEIEFFSPLTL-IVGQNGAGKTTII------------EALKY--ALTGEL---PP-------N 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 87 GNVEEGLGDIFEKKARfeaiaeematnytdelmeemgKLQEELDAADAWELDSKIEQAMDALR----CP------PADEP 156
Cdd:cd03240 54 SKGGAHDPKLIREGEV---------------------RAQVKLAFENANGKKYTITRSLAILEnvifCHqgesnwPLLDM 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 157 VTHLSGGERR------RVALAKLLLSEPDLLLLDEPTNHLDAESVLW-----LEQHLAKYPGAVLAVTHDRYFLDHvAGW 225
Cdd:cd03240 113 RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEEslaeiIEERKSQKNFQLIVITHDEELVDA-ADH 191
|
....*.
gi 512463837 226 ICEVDR 231
Cdd:cd03240 192 IYRVEK 197
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
323-378 |
1.26e-07 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 52.76 E-value: 1.26e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 512463837 323 EVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLE--QPDSGEV 378
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSI 59
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
9-202 |
1.43e-07 |
|
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: 52.62 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 9 KNVRKA-HGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGeAFLEPG------------ATVGILLQ 75
Cdd:cd03253 4 ENVTFAyDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSG-SILIDGqdirevtldslrRAIGVVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 76 EPPL-NEekTVRGNVEEGlgdifekkaRFEAiaeematnyTDELMEEmgklqeeldAADAWELDSKIEQAMDALrcppaD 154
Cdd:cd03253 83 DTVLfND--TIGYNIRYG---------RPDA---------TDEEVIE---------AAKAAQIHDKIMRFPDGY-----D 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 512463837 155 EPV----THLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAESvlwlEQHL 202
Cdd:cd03253 129 TIVgergLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHT----EREI 176
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
14-215 |
1.51e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 53.07 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 14 AHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFL-----------EPGATVGILLQEPPLNEE 82
Cdd:PRK10253 16 GYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLdgehiqhyaskEVARRIGLLAQNATTPGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 83 KTVRgnveeglgdifEKKARFEAIAEEMATNYTdelmeemgklQEELDAadaweldskIEQAMDALRCPP-ADEPVTHLS 161
Cdd:PRK10253 96 ITVQ-----------ELVARGRYPHQPLFTRWR----------KEDEEA---------VTKAMQATGITHlADQSVDTLS 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 512463837 162 GGERRRVALAKLLLSEPDLLLLDEPTNHLDAE---SVLWLEQHLAKYPGAVL-AVTHD 215
Cdd:PRK10253 146 GGQRQRAWIAMVLAQETAIMLLDEPTTWLDIShqiDLLELLSELNREKGYTLaAVLHD 203
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
17-220 |
2.03e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 51.49 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 17 DKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEpgatvgillqepplneektvRGNVEEGLGdI 96
Cdd:PRK13540 13 DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFE--------------------RQSIKKDLC-T 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 97 FEKKARFeaIAEEMATNYTDELMEEMgkLQEELDAADAWELDS-----KIEQAMDAlrcppadePVTHLSGGERRRVALA 171
Cdd:PRK13540 72 YQKQLCF--VGHRSGINPYLTLRENC--LYDIHFSPGAVGITElcrlfSLEHLIDY--------PCGLLSSGQKRQVALL 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 512463837 172 KLLLSEPDLLLLDEPTNHLDAESVLW----LEQHLAKyPGAVLAVTHDRYFLD 220
Cdd:PRK13540 140 RLWMSKAKLWLLDEPLVALDELSLLTiitkIQEHRAK-GGAVLLTSHQDLPLN 191
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
313-474 |
2.09e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.01 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 313 TPPRLGNQVVEVKDlekgfdgRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQTVqlSYVDQG 392
Cdd:PTZ00243 659 TPKMKTDDFFELEP-------KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSI--AYVPQQ 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 393 --------RENI---DPEKTvwevvSDGLDYIVVGQNEmPSRAYLSA-----FGFKGADqqkpskvLSGGERNRLNLALT 456
Cdd:PTZ00243 730 awimnatvRGNIlffDEEDA-----ARLADAVRVSQLE-ADLAQLGGgleteIGEKGVN-------LSGGQKARVSLARA 796
|
170
....*....|....*...
gi 512463837 457 LKQGGNLILLDEPTNDLD 474
Cdd:PTZ00243 797 VYANRDVYLLDDPLSALD 814
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
3-205 |
2.85e-07 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 51.50 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 3 EFIYQMKNV----RKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQpsngeaflEPGATVG-ILLQEP 77
Cdd:cd03234 1 QRVLPWWDVglkaKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVE--------GGGTTSGqILFNGQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 78 PLNEEKTVR--GNVEEGlgDIFEKkarfEAIAEEMATnYTDELmeemgKLQEELDaadaweldSKIEQAMDA----LRCp 151
Cdd:cd03234 73 PRKPDQFQKcvAYVRQD--DILLP----GLTVRETLT-YTAIL-----RLPRKSS--------DAIRKKRVEdvllRDL- 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 512463837 152 pADEPVTH-----LSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAESVLWLEQHLAKY 205
Cdd:cd03234 132 -ALTRIGGnlvkgISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQL 189
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
9-223 |
3.07e-07 |
|
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: 51.67 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 9 KNVRKA---H--GDKVI--LDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEPGATVGILLQEPP--- 78
Cdd:COG4778 8 ENLSKTftlHlqGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDLAQASPrei 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 79 LNEEKTVRGNVEEGLG--------DIFEKKARFEAIAEEMATNYTDELMEEMGkLQEELdaadaWELdskieqamdalrc 150
Cdd:COG4778 88 LALRRRTIGYVSQFLRviprvsalDVVAEPLLERGVDREEARARARELLARLN-LPERL-----WDL------------- 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 512463837 151 PPAdepvThLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAES---VLWL-EQhlAKYPG-AVLAVTHDRYFLDHVA 223
Cdd:COG4778 149 PPA----T-FSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANravVVELiEE--AKARGtAIIGIFHDEEVREAVA 219
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
14-243 |
3.28e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 52.92 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 14 AHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGL--DQPS---NGEAF--LEPG------ATVGillQEPPLN 80
Cdd:PRK11174 359 SPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFlpYQGSlkiNGIELreLDPEswrkhlSWVG---QNPQLP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 81 EEkTVRGNVEegLGDIfekkarfeaiaeematNYTDElmeemgKLQEELDAADAWELDSKIEQAMDAlrcpPADEPVTHL 160
Cdd:PRK11174 436 HG-TLRDNVL--LGNP----------------DASDE------QLQQALENAWVSEFLPLLPQGLDT----PIGDQAAGL 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 161 SGGERRRVALAKLLLSEPDLLLLDEPTNHLDAESvlwlEQHL------AKYPGAVLAVTHDryfLDHVAGW--ICEVDRG 232
Cdd:PRK11174 487 SVGQAQRLALARALLQPCQLLLLDEPTASLDAHS----EQLVmqalnaASRRQTTLMVTHQ---LEDLAQWdqIWVMQDG 559
|
250
....*....|.
gi 512463837 233 KLYPyEGNYST 243
Cdd:PRK11174 560 QIVQ-QGDYAE 569
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
7-475 |
3.32e-07 |
|
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: 52.90 E-value: 3.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLdQPS---NGEAFLE------------PGATVG 71
Cdd:TIGR02633 3 EMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHgtwDGEIYWSgsplkasnirdtERAGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 72 ILLQEPPLNEEKTVRGNVEEGlGDIFEKKARfeaiaeemaTNYtDELMEEMGKLQEELDAADAweldskieqamdalrcp 151
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIFLG-NEITLPGGR---------MAY-NAMYLRAKNLLRELQLDAD----------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 152 PADEPVTHLSGGERRRVALAKLLLSEPDLLLLDEPTNHL---DAESVLWLEQHLAKYPGAVLAVTHDryfLDHVAGwICe 228
Cdd:TIGR02633 134 NVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLtekETEILLDIIRDLKAHGVACVYISHK---LNEVKA-VC- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 229 vdrgklypyegnystylekkaerlevagkkdaklqkrlkDELAWVRSGQK--ARQAKNKARLERYEQMV--EEAEQYkkl 304
Cdd:TIGR02633 209 ---------------------------------------DTICVIRDGQHvaTKDMSTMSEDDIITMMVgrEITSLY--- 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 305 dfeeiqiPTPPR-LGNQVVEVKDLEKGFDGRVLIK---DLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGL-EQPDSGEV- 378
Cdd:TIGR02633 247 -------PHEPHeIGDVILEARNLTCWDVINPHRKrvdDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVf 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 379 -------------KVGQTVQLSYVDQGRENIDPEKTVWEVVS-------DGLDYIVVGQNEMPSRAYLSAFGFKGADQQK 438
Cdd:TIGR02633 320 ingkpvdirnpaqAIRAGIAMVPEDRKRHGIVPILGVGKNITlsvlksfCFKMRIDAAAELQIIGSAIQRLKVKTASPFL 399
|
490 500 510
....*....|....*....|....*....|....*..
gi 512463837 439 PSKVLSGGERNRLNLALTLKQGGNLILLDEPTNDLDV 475
Cdd:TIGR02633 400 PIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-54 |
3.39e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.01 E-value: 3.39e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 512463837 1 MGEFIYQMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGL 54
Cdd:PRK13549 1 MMEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV 54
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-62 |
3.46e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 52.40 E-value: 3.46e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 512463837 21 LDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEA 62
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEV 79
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
24-222 |
3.57e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 51.47 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 24 VTMAFYPGAKIGVVGPNGAGKSSILKIMAGLdQPSNGEAFLEpgatvGILLQEPPLNEEKTVRG----------NVeegl 93
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFA-----GQPLEAWSAAELARHRAylsqqqtppfAM---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 94 gDIFEKKARFEAiaeemATNYTDELMEEMGKLQEELdaadawELDSKIEQamdalrcppadePVTHLSGGERRRVALA-- 171
Cdd:PRK03695 85 -PVFQYLTLHQP-----DKTRTEAVASALNEVAEAL------GLDDKLGR------------SVNQLSGGEWQRVRLAav 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 512463837 172 -----KLLLSEPDLLLLDEPTNHLDAESVLWLEQ---HLAKYPGAVLAVTHDryfLDHV 222
Cdd:PRK03695 141 vlqvwPDINPAGQLLLLDEPMNSLDVAQQAALDRllsELCQQGIAVVMSSHD---LNHT 196
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
321-380 |
4.00e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.20 E-value: 4.00e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 321 VVEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV 380
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEV 60
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
346-504 |
4.72e-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: 49.68 E-value: 4.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 346 RNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVgqtvqlsyvdqgrenIDPEKTVWEVVSDGLDYIVVGQNEMpsray 425
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY---------------IDGEDILEEVLDQLLLIIVGGKKAS----- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 426 lsafgfkgadqqkpskvLSGGERNRLNLALTLKQGGNLILLDEPTNDLDVET---------LSSLENALQNFPGCAVVIS 496
Cdd:smart00382 61 -----------------GSGELRLRLALALARKLKPDVLILDEITSLLDAEQeallllleeLRLLLLLKSEKNLTVILTT 123
|
....*...
gi 512463837 497 HDRWFLDR 504
Cdd:smart00382 124 NDEKDLGP 131
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-203 |
4.99e-07 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 52.36 E-value: 4.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 18 KVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDqpsngeaflEPGATVG--ILLQEPPLNEEK------------ 83
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRS---------PKGVKGSgsVLLNGMPIDAKEmraisayvqqdd 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 84 ------TVRGNV----EEGLGDIFEKKARFEAIaeematnytDELMEEMGKLqeelDAADaweldSKIEQAMDalrcppa 153
Cdd:TIGR00955 109 lfiptlTVREHLmfqaHLRMPRRVTKKEKRERV---------DEVLQALGLR----KCAN-----TRIGVPGR------- 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 512463837 154 depVTHLSGGERRRVALAKLLLSEPDLLLLDEPTNHLD---AESVLWLEQHLA 203
Cdd:TIGR00955 164 ---VKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDsfmAYSVVQVLKGLA 213
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
341-475 |
5.61e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 52.48 E-value: 5.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 341 SFTL-----PRNG-IVGVIGPNGVGKSTLFKTIVGLEQPD------------------------------SGEVKVGQTV 384
Cdd:COG1245 87 GFRLyglpvPKKGkVTGILGPNGIGKSTALKILSGELKPNlgdydeepswdevlkrfrgtelqdyfkklaNGEIKVAHKP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 385 QlsYVDQ------GR-----ENIDPEKTVWEVVSD-GLDYIVvgqnempsraylsafgfkgadqQKPSKVLSGGERNRLN 452
Cdd:COG1245 167 Q--YVDLipkvfkGTvrellEKVDERGKLDELAEKlGLENIL----------------------DRDISELSGGELQRVA 222
|
170 180
....*....|....*....|...
gi 512463837 453 LALTLKQGGNLILLDEPTNDLDV 475
Cdd:COG1245 223 IAAALLRDADFYFFDEPSSYLDI 245
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
5-215 |
5.83e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 51.23 E-value: 5.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 5 IYQMKNVRKAHGD-KVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAF-------------LEPGATV 70
Cdd:PRK13639 1 ILETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLikgepikydkkslLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 71 GILLQEP------PLNEEKTVRGNVEEGLGdifekkarfeaiaeematnytdelMEEMGK-LQEELDAADAWELDSKieq 143
Cdd:PRK13639 81 GIVFQNPddqlfaPTVEEDVAFGPLNLGLS------------------------KEEVEKrVKEALKAVGMEGFENK--- 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 512463837 144 amdalrcPPAdepvtHLSGGERRRVALAKLLLSEPDLLLLDEPTNHLD---AESVLWLEQHLAKYPGAVLAVTHD 215
Cdd:PRK13639 134 -------PPH-----HLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDpmgASQIMKLLYDLNKEGITIIISTHD 196
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
302-470 |
6.10e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 52.43 E-value: 6.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 302 KKLDFEEIQIPTPPRLGNQ--VVEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVK 379
Cdd:NF033858 245 KRRGHQPVVIPPRPADDDDepAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAW 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 380 V-GQTV---------QLSYVDQG---------RENID--------PEKTVWEVVsdgldyivvgqNEMPSRaylsaFGFK 432
Cdd:NF033858 325 LfGQPVdagdiatrrRVGYMSQAfslygeltvRQNLElharlfhlPAAEIAARV-----------AEMLER-----FDLA 388
|
170 180 190
....*....|....*....|....*....|....*...
gi 512463837 433 GADQQKPSKvLSGGERNRLNLALTLKQGGNLILLDEPT 470
Cdd:NF033858 389 DVADALPDS-LPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
336-477 |
6.90e-07 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 51.01 E-value: 6.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 336 LIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVK----VGQTVQLSYVDQG--RENIdpektVWEVVSDG 409
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKhsgrISFSSQFSWIMPGtiKENI-----IFGVSYDE 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 512463837 410 LDYIVVGQ--------NEMPSRAYlSAFGFKGAdqqkpskVLSGGERNRLNLALTLKQGGNLILLDEPTNDLDVET 477
Cdd:cd03291 127 YRYKSVVKacqleediTKFPEKDN-TVLGEGGI-------TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-253 |
7.13e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 50.82 E-value: 7.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 17 DKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSN------------GEAFLEPGAT-----VGILLQEPpl 79
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDskikvdgkvlyfGKDIFQIDAIklrkeVGMVFQQP-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 80 neektvrgnveeglgDIFEKKARFEAIAEEMATNYTDELMEEMGKLQEELDAADAWEldskieQAMDALrcppaDEPVTH 159
Cdd:PRK14246 100 ---------------NPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWK------EVYDRL-----NSPASQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 160 LSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAESVLWLEQHLA--KYPGAVLAVTHDRYFLDHVAGWICEVDRGKLYPY 237
Cdd:PRK14246 154 LSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITelKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEW 233
|
250
....*....|....*.
gi 512463837 238 EGNYSTYLEKKAERLE 253
Cdd:PRK14246 234 GSSNEIFTSPKNELTE 249
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
321-390 |
7.74e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 50.94 E-value: 7.74e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 512463837 321 VVEVKDLEKGFDGRV---------LIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQTvQLSYVD 390
Cdd:PRK15112 4 LLEVRNLSKTFRYRTgwfrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDH-PLHFGD 81
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
323-503 |
8.49e-07 |
|
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: 50.34 E-value: 8.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 323 EVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGleQPD----SGEVKV-GQTV-QLSYVDQGRENI 396
Cdd:TIGR01978 2 KIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAG--HPSyevtSGTILFkGQDLlELEPDERARAGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 397 -----DPEK----TVWEVVSDGLDYIVVGQNEMPsrayLSAFGFKGADQQKPSKV--------------LSGGERNRLNL 453
Cdd:TIGR01978 80 flafqYPEEipgvSNLEFLRSALNARRSARGEEP----LDLLDFEKLLKEKLALLdmdeeflnrsvnegFSGGEKKRNEI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 512463837 454 ALTLKQGGNLILLDEPTNDLDVETLSSLENALQNF--PGCA-VVISHDRWFLD 503
Cdd:TIGR01978 156 LQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLrePDRSfLIITHYQRLLN 208
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
20-194 |
8.80e-07 |
|
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: 50.31 E-value: 8.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 20 ILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEpgatvGILLQEPPLNEEKTVRGNVEEglgDIFek 99
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILID-----GHDVRDYTLASLRRQIGLVSQ---DVF-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 100 kaRF-EAIAEEMATNYTDELMEEMgklqeeLDAADAWELDSKIEQAMDALRCPPADEPVThLSGGERRRVALAKLLLSEP 178
Cdd:cd03251 87 --LFnDTVAENIAYGRPGATREEV------EEAARAANAHEFIMELPEGYDTVIGERGVK-LSGGQRQRIAIARALLKDP 157
|
170
....*....|....*.
gi 512463837 179 DLLLLDEPTNHLDAES 194
Cdd:cd03251 158 PILILDEATSALDTES 173
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
339-483 |
8.95e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 51.03 E-value: 8.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 339 DLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQTVqLSYVDQGrENIDPEK-TVWEVVSDGL---DYIV 414
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRV-LFDAEKG-ICLPPEKrRIGYVFQDARlfpHYKV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 415 VGQNEmpsraylsaFGFKGADQQKPSKV----------------LSGGERNRLNLALTLKQGGNLILLDEPTNDLDV--- 475
Cdd:PRK11144 94 RGNLR---------YGMAKSMVAQFDKIvallgieplldrypgsLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLprk 164
|
....*....
gi 512463837 476 -ETLSSLEN 483
Cdd:PRK11144 165 rELLPYLER 173
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
345-475 |
1.15e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.35 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 345 PRNG-IVGVIGPNGVGKSTLFKTIVGL---------EQPD---------------------SGEVKVGQTVQlsYVDQ-- 391
Cdd:PRK13409 96 PKEGkVTGILGPNGIGKTTAVKILSGElipnlgdyeEEPSwdevlkrfrgtelqnyfkklyNGEIKVVHKPQ--YVDLip 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 392 ----GR-----ENIDPEKTVWEVVSD-GLDYIVvgqnempsraylsafgfkgadqQKPSKVLSGGERNRLNLALTLKQGG 461
Cdd:PRK13409 174 kvfkGKvrellKKVDERGKLDEVVERlGLENIL----------------------DRDISELSGGELQRVAIAAALLRDA 231
|
170
....*....|....
gi 512463837 462 NLILLDEPTNDLDV 475
Cdd:PRK13409 232 DFYFFDEPTSYLDI 245
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
17-194 |
1.17e-06 |
|
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: 51.26 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 17 DKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEpgatvGILLQEPPLneeKTVRGNVEEGLGDI 96
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLD-----GHDLADYTL---ASLRRQVALVSQDV 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 97 FekkaRF-EAIAEEMATNYTDELMEEmgKLQEELDAADAWELDSKIEQAMDAlrcpPADEPVTHLSGGERRRVALAKLLL 175
Cdd:TIGR02203 416 V----LFnDTIANNIAYGRTEQADRA--EIERALAAAYAQDFVDKLPLGLDT----PIGENGVLLSGGQRQRLAIARALL 485
|
170
....*....|....*....
gi 512463837 176 SEPDLLLLDEPTNHLDAES 194
Cdd:TIGR02203 486 KDAPILILDEATSALDNES 504
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-223 |
1.22e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 50.40 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 1 MGEFIYQMKNV--RKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNG-----------EAFLEPG 67
Cdd:PRK13635 1 MKEEIIRVEHIsfRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGtitvggmvlseETVWDVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 68 ATVGILLQEPPlNE--EKTVRGNVEEGLGDIFEKKarfeaiaEEMATNyTDELMEEMGkLQEELDaadaweldskieqam 145
Cdd:PRK13635 81 RQVGMVFQNPD-NQfvGATVQDDVAFGLENIGVPR-------EEMVER-VDQALRQVG-MEDFLN--------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 146 dalrcppaDEPvTHLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDA---ESVLWLEQHLAKYPGA-VLAVTHDryfLDH 221
Cdd:PRK13635 136 --------REP-HRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPrgrREVLETVRQLKEQKGItVLSITHD---LDE 203
|
..
gi 512463837 222 VA 223
Cdd:PRK13635 204 AA 205
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
321-503 |
1.27e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 50.03 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 321 VVEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGleQPD----SGEVKV-GQTV----------- 384
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFkGESIldlepeerahl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 385 ---------------------QLSY----VDQGRENIDPeKTVWEVVSDGLDyiVVGQNEmpsrAYLSAF---GFkgadq 436
Cdd:CHL00131 85 giflafqypieipgvsnadflRLAYnskrKFQGLPELDP-LEFLEIINEKLK--LVGMDP----SFLSRNvneGF----- 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 512463837 437 qkpskvlSGGERNR---LNLALTLKQggnLILLDEPTNDLDVETLSSLENALQNFPG---CAVVISHDRWFLD 503
Cdd:CHL00131 153 -------SGGEKKRneiLQMALLDSE---LAILDETDSGLDIDALKIIAEGINKLMTsenSIILITHYQRLLD 215
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
331-474 |
1.75e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 50.02 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 331 FDGRVLiKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQTVqlsyVDQGRENID------------- 397
Cdd:PRK13634 18 FERRAL-YDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERV----ITAGKKNKKlkplrkkvgivfq 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 398 -PEKTVWE--VVSDgldyIVVG-QNempsraylsaFGFKGADQQKPSKV------------------LSGGERNRLNLAL 455
Cdd:PRK13634 93 fPEHQLFEetVEKD----ICFGpMN----------FGVSEEDAKQKAREmielvglpeellarspfeLSGGQMRRVAIAG 158
|
170
....*....|....*....
gi 512463837 456 TLKQGGNLILLDEPTNDLD 474
Cdd:PRK13634 159 VLAMEPEVLVLDEPTAGLD 177
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
352-485 |
1.81e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 49.08 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 352 VIGPNGVGKSTLFKTIVGLEQPDSGEVKVgQTVQLSYVDQGR--------ENIDPEKTVWEvvsdGLDYIVVGQ----NE 419
Cdd:PRK13543 42 VQGDNGAGKTTLLRVLAGLLHVESGQIQI-DGKTATRGDRSRfmaylghlPGLKADLSTLE----NLHFLCGLHgrraKQ 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 512463837 420 MPSRAyLSAFGFKGAdQQKPSKVLSGGERNRLNLALTLKQGGNLILLDEPTNDLDVETLSSLENAL 485
Cdd:PRK13543 117 MPGSA-LAIVGLAGY-EDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMI 180
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
334-474 |
2.01e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 49.66 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 334 RVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV------GQTVQLSY-------VDQGRENIDPEK 400
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIdgvditDKKVKLSDirkkvglVFQYPEYQLFEE 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 512463837 401 TVWEVVSDGLDYIVVGQNEMPSRAY--LSAFGFKGADQQKPSKV-LSGGERNRLNLALTLKQGGNLILLDEPTNDLD 474
Cdd:PRK13637 100 TIEKDIAFGPINLGLSEEEIENRVKraMNIVGLDYEDYKDKSPFeLSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
322-497 |
2.06e-06 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 50.49 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDLEKGF-DGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTVQ-LSY---------V 389
Cdd:PRK10790 341 IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLdGRPLSsLSHsvlrqgvamV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 390 DQ---------------GReNIDPEKtVWEVVSdgldyiVVGQNE----MPSRAYlSAFGFKGADqqkpskvLSGGERNR 450
Cdd:PRK10790 421 QQdpvvladtflanvtlGR-DISEEQ-VWQALE------TVQLAElarsLPDGLY-TPLGEQGNN-------LSVGQKQL 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 512463837 451 LNLALTLKQGGNLILLDEPTNDLDVETLSSLENALQNFPGCA--VVISH 497
Cdd:PRK10790 485 LALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTtlVVIAH 533
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
7-192 |
2.32e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 49.84 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAHGDKV-ILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAF--------LEPgATVGI--LLQ 75
Cdd:PRK11650 5 KLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWiggrvvneLEP-ADRDIamVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 76 EPPLNEEKTVRGNVEEGLgdifeKKARF--EAIAEEMAtnytdelmeemgklqeelDAADAWELDSKIEqamdalRCPPA 153
Cdd:PRK11650 84 NYALYPHMSVRENMAYGL-----KIRGMpkAEIEERVA------------------EAARILELEPLLD------RKPRE 134
|
170 180 190
....*....|....*....|....*....|....*....
gi 512463837 154 depvthLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDA 192
Cdd:PRK11650 135 ------LSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDA 167
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
331-474 |
2.38e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 49.36 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 331 FDGRVL------IKDLSFTlprngivGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQTV---------------QLSYV 389
Cdd:PRK13649 18 FEGRALfdvnltIEDGSYT-------AFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLitstsknkdikqirkKVGLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 390 DQGRENIDPEKTVWEVVSDGLDYIVVGQNEMPSRAY--LSAFGFKGADQQKPSKVLSGGERNRLNLALTLKQGGNLILLD 467
Cdd:PRK13649 91 FQFPESQLFEETVLKDVAFGPQNFGVSQEEAEALARekLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLD 170
|
....*..
gi 512463837 468 EPTNDLD 474
Cdd:PRK13649 171 EPTAGLD 177
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
7-196 |
2.50e-06 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 49.69 E-value: 2.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRK----AHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLE-------PGA------- 68
Cdd:COG1135 3 ELENLSKtfptKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDgvdltalSERelraarr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 69 TVGILLQEPPLNEEKTVRGNVE---EGLGdiFEKKARFEAIAeematnytdELMEEMGkLQeelDAADAWeldskieqam 145
Cdd:COG1135 83 KIGMIFQHFNLLSSRTVAENVAlplEIAG--VPKAEIRKRVA---------ELLELVG-LS---DKADAY---------- 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 512463837 146 dalrcpPAdepvtHLSGGERRRVA------------LAklllsepdllllDEPTNHLDAE---SVL 196
Cdd:COG1135 138 ------PS-----QLSGGQKQRVGiaralannpkvlLC------------DEATSALDPEttrSIL 180
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
7-53 |
3.16e-06 |
|
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: 47.91 E-value: 3.16e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 512463837 7 QMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAG 53
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG 48
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
16-215 |
3.28e-06 |
|
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: 48.97 E-value: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 16 GDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEPGAT------------VGILLQEPplnEEK 83
Cdd:TIGR04520 13 SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTldeenlweirkkVGMVFQNP---DNQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 84 TVRGNVEEglgDIfekkarfeAIAeematnytdelMEEMGKLQEELDAadaweldsKIEQA-----MDALRcppaDEPVT 158
Cdd:TIGR04520 90 FVGATVED---DV--------AFG-----------LENLGVPREEMRK--------RVDEAlklvgMEDFR----DREPH 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 512463837 159 HLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAES---VLWLEQHLAKYPG-AVLAVTHD 215
Cdd:TIGR04520 136 LLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGrkeVLETIRKLNKEEGiTVISITHD 196
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
3-191 |
3.50e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 48.86 E-value: 3.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 3 EFIYQMKN--VRKAhgdkviLDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNG-----EAFLEPGAT------ 69
Cdd:PRK13634 9 EHRYQYKTpfERRA------LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGtvtigERVITAGKKnkklkp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 70 ----VGILLQ--EPPLNEEkTVrgnveegLGDIFEKKARFeAIAEEMATNYTDELMEEMGkLQEELDAADAWEldskieq 143
Cdd:PRK13634 83 lrkkVGIVFQfpEHQLFEE-TV-------EKDICFGPMNF-GVSEEDAKQKAREMIELVG-LPEELLARSPFE------- 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 512463837 144 amdalrcppadepvthLSGGERRRVALAKLLLSEPDLLLLDEPTNHLD 191
Cdd:PRK13634 146 ----------------LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
339-476 |
3.80e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 48.67 E-value: 3.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 339 DLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTV--------------QLSYVDQGRENIDPEKTVW 403
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIaGYHItpetgnknlkklrkKVSLVFQFPEAQLFENTVL 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 512463837 404 EVVSDGLDYIVVGQNEMPSRA--YLSAFGFKGADQQKPSKVLSGGERNRLNLALTLKQGGNLILLDEPTNDLDVE 476
Cdd:PRK13641 105 KDVEFGPKNFGFSEDEAKEKAlkWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPE 179
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
332-477 |
4.49e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 48.44 E-value: 4.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 332 DGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVG--QTVQLSYVDQGRENI-----DPE----- 399
Cdd:PRK13644 13 DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSgiDTGDFSKLQGIRKLVgivfqNPEtqfvg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 400 KTVWEVVSDGLDYIVVGQNEMPSRA--YLSAFGFKGADQQKPsKVLSGGERNRLNLALTLKQGGNLILLDEPTNDLDVET 477
Cdd:PRK13644 93 RTVEEDLAFGPENLCLPPIEIRKRVdrALAEIGLEKYRHRSP-KTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDS 171
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
322-477 |
5.12e-06 |
|
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: 47.41 E-value: 5.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDLEKGF--DGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTV----------QLSY 388
Cdd:cd03369 7 IEVENLSVRYapDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIdGIDIstipledlrsSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 389 VDQG--------RENIDP-----EKTVWEV--VSDGldyivvGQNempsraylsafgfkgadqqkpskvLSGGERNRLNL 453
Cdd:cd03369 87 IPQDptlfsgtiRSNLDPfdeysDEEIYGAlrVSEG------GLN------------------------LSQGQRQLLCL 136
|
170 180
....*....|....*....|....
gi 512463837 454 ALTLKQGGNLILLDEPTNDLDVET 477
Cdd:cd03369 137 ARALLKRPRVLVLDEATASIDYAT 160
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
337-468 |
5.34e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 49.12 E-value: 5.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 337 IKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQTVQLSYVDQGR-------ENID--------PEKT 401
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLngqltgiENIElkglmmglTKEK 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 512463837 402 VWEVVSDGLDYIVVGqnempsraylsafgfKGADQqkPSKVLSGGERNRLNLALTLKQGGNLILLDE 468
Cdd:PRK13545 120 IKEIIPEIIEFADIG---------------KFIYQ--PVKTYSSGMKSRLGFAISVHINPDILVIDE 169
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
20-191 |
5.60e-06 |
|
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: 49.35 E-value: 5.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 20 ILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEPGATVGI-----------LLQEPPLneektVRGN 88
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIdrhtlrqfinyLPQEPYI-----FSGS 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 89 VEEGLgdifekkarfeaiaeematnytdeLMEEMGKL-QEELDAA-DAWELDSKIEQAMDALRCPPADEPvTHLSGGERR 166
Cdd:TIGR01193 564 ILENL------------------------LLGAKENVsQDEIWAAcEIAEIKDDIENMPLGYQTELSEEG-SSISGGQKQ 618
|
170 180
....*....|....*....|....*
gi 512463837 167 RVALAKLLLSEPDLLLLDEPTNHLD 191
Cdd:TIGR01193 619 RIALARALLTDSKVLILDESTSNLD 643
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
339-513 |
5.63e-06 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 47.70 E-value: 5.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 339 DLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-------GQTVQLSYVDQGRENID---------PEKTV 402
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagnhfdfSKTPSDKAIRELRRNVGmvfqqynlwPHLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 403 WEVVSD------GLDYIVVGQNEMP--SRAYLSAFgfkgADQQKPSkvLSGGERNRLNLALTLKQGGNLILLDEPTNDLD 474
Cdd:PRK11124 100 QQNLIEapcrvlGLSKDQALARAEKllERLRLKPY----ADRFPLH--LSGGQQQRVAIARALMMEPQVLLFDEPTAALD 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 512463837 475 VETLS---SLENALQNFPGCAVVISHDRWFLDRTCTHILAWE 513
Cdd:PRK11124 174 PEITAqivSIIRELAETGITQVIVTHEVEVARKTASRVVYME 215
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
321-497 |
5.77e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.85 E-value: 5.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 321 VVEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVK-VGQTVQLSYVDQGRE----- 394
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILyLGKEVTFNGPKSSQEagigi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 395 -----NIDPEKTVWEvvsdgldYIVVGqnempsRAYLSAFG-------FKGADQ-----------QKPSKVLSGGERNRL 451
Cdd:PRK10762 84 ihqelNLIPQLTIAE-------NIFLG------REFVNRFGridwkkmYAEADKllarlnlrfssDKLVGELSIGEQQMV 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 512463837 452 NLALTLKQGGNLILLDEPTNDL-DVETLS--SLENALQNfPGCAVV-ISH 497
Cdd:PRK10762 151 EIAKVLSFESKVIIMDEPTDALtDTETESlfRVIRELKS-QGRGIVyISH 199
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
21-216 |
5.87e-06 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 49.19 E-value: 5.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 21 LDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEPGATVGILLQepplneekTVRGNveegLGDIFEKK 100
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRA--------SLRRN----IAVVFQDA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 101 ARFE-AIAEEMATNYTDELMEEMgklQEELDAADAWELDSKIEQAMDALrcppADEPVTHLSGGERRRVALAKLLLSEPD 179
Cdd:PRK13657 419 GLFNrSIEDNIRVGRPDATDEEM---RAAAERAQAHDFIERKPDGYDTV----VGERGRQLSGGERQRLAIARALLKDPP 491
|
170 180 190
....*....|....*....|....*....|....*..
gi 512463837 180 LLLLDEPTNHLDAESvlwlEqhlAKYPGAVLAVTHDR 216
Cdd:PRK13657 492 ILILDEATSALDVET----E---AKVKAALDELMKGR 521
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
16-204 |
6.26e-06 |
|
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: 47.61 E-value: 6.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 16 GDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLE--PGATV---------GILLQEPPLNEekt 84
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDgiDIRDIsrkslrsmiGVVLQDTFLFS--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 85 vrgnveeglGDIFEKkarfeaIAeeMATNYTDElmeemgklQEELDAADAWELDSKIEQAMDALrcppaDEPVTH----L 160
Cdd:cd03254 91 ---------GTIMEN------IR--LGRPNATD--------EEVIEAAKEAGAHDFIMKLPNGY-----DTVLGEnggnL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 512463837 161 SGGERRRVALAKLLLSEPDLLLLDEPTNHLDAESVLWLEQHLAK 204
Cdd:cd03254 141 SQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEK 184
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
7-288 |
6.38e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 48.06 E-value: 6.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAHGDKV-ILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLE----------PG--ATVGIL 73
Cdd:PRK13644 3 RLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSgidtgdfsklQGirKLVGIV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 74 LQEPplnEEKTVRGNVEEGLgdifekkarfeAIAEEmatnytdELMEEMGKLQEELDAADAwelDSKIEQAMDalRCPPA 153
Cdd:PRK13644 83 FQNP---ETQFVGRTVEEDL-----------AFGPE-------NLCLPPIEIRKRVDRALA---EIGLEKYRH--RSPKT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 154 depvthLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAES---VLWLEQHLAKYPGAVLAVTHDRYFLdHVAGWICEVD 230
Cdd:PRK13644 137 ------LSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSgiaVLERIKKLHEKGKTIVYITHNLEEL-HDADRIIVMD 209
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 512463837 231 RGKLYpYEGNYSTYLEKKAER-LEVAGKKDAKLQKRLKD---ELAWVRSGQKARQAKNKARL 288
Cdd:PRK13644 210 RGKIV-LEGEPENVLSDVSLQtLGLTPPSLIELAENLKMhgvVIPWENTSSPSSFAEEICRL 270
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
350-498 |
6.90e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 47.47 E-value: 6.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 350 VGVIGPNGVGKSTLFKTIVGLEQPDSGEVK-VGQTvqLSYVDQ-GR-----ENID---------PEKTVWEVVSdgLDYI 413
Cdd:PRK10584 39 IALIGESGSGKSTLLAILAGLDDGSSGEVSlVGQP--LHQMDEeARaklraKHVGfvfqsfmliPTLNALENVE--LPAL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 414 VVGQNEMPSR----AYLSAFGFKGADQQKPSKvLSGGERNRLNLALTLKQGGNLILLDEPTNDLDVETLSSLENAL---- 485
Cdd:PRK10584 115 LRGESSRQSRngakALLEQLGLGKRLDHLPAQ-LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLfsln 193
|
170
....*....|...
gi 512463837 486 QNFPGCAVVISHD 498
Cdd:PRK10584 194 REHGTTLILVTHD 206
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
319-474 |
6.97e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 47.78 E-value: 6.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 319 NQVVEVKDLEKGFDGRVLIKDL---SFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTV---------- 384
Cdd:PRK13642 2 NKILEVENLVFKYEKESDVNQLngvSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIdGELLtaenvwnlrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 385 QLSYVDQGRENIDPEKTVWEVVSDGLDYIVVGQNEMPSRA--YLSAFGFKGADQQKPSKvLSGGERNRLNLALTLKQGGN 462
Cdd:PRK13642 82 KIGMVFQNPDNQFVGATVEDDVAFGMENQGIPREEMIKRVdeALLAVNMLDFKTREPAR-LSGGQKQRVAVAGIIALRPE 160
|
170
....*....|..
gi 512463837 463 LILLDEPTNDLD 474
Cdd:PRK13642 161 IIILDESTSMLD 172
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
313-367 |
7.34e-06 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 47.72 E-value: 7.34e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 512463837 313 TPPRLGNQVVEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTI 367
Cdd:COG1117 3 APASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCL 57
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
322-520 |
7.51e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 48.16 E-value: 7.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 322 VEVKDLEKGFDGRV-----LIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEV------------------ 378
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 379 -KVGQTVQLSY------VDQGRENIDP----------EKTVWEVVSDGLDYIVVGQNEMPSRA--YLSAFGFKGADQQKP 439
Cdd:PRK13651 83 vLEKLVIQKTRfkkikkIKEIRRRVGVvfqfaeyqlfEQTIEKDIIFGPVSMGVSKEEAKKRAakYIELVGLDESYLQRS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 440 SKVLSGGERNRLNLALTLKQGGNLILLDEPTNDLD----VETLSSLENALQNfpGCAVVI-SHDrwfLDrtctHILAWEG 514
Cdd:PRK13651 163 PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpqgvKEILEIFDNLNKQ--GKTIILvTHD---LD----NVLEWTK 233
|
....*....
gi 512463837 515 N---FEEGK 520
Cdd:PRK13651 234 RtifFKDGK 242
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
7-57 |
8.72e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.47 E-value: 8.72e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 512463837 7 QMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGlDQP 57
Cdd:PRK10938 262 VLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHP 311
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
20-194 |
8.89e-06 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 47.15 E-value: 8.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 20 ILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEpG------------ATVGILLQEPPLNEeKTVRG 87
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLD-GvdirdlnlrwlrSQIGLVSQEPVLFD-GTIAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 88 NVEEGLGDIfekkarfeaiaeematnyTDELMEEmgklqeeldAADAWELDSKIEQAMDALrcppaDEPV----THLSGG 163
Cdd:cd03249 96 NIRYGKPDA------------------TDEEVEE---------AAKKANIHDFIMSLPDGY-----DTLVgergSQLSGG 143
|
170 180 190
....*....|....*....|....*....|.
gi 512463837 164 ERRRVALAKLLLSEPDLLLLDEPTNHLDAES 194
Cdd:cd03249 144 QKQRIAIARALLRNPKILLLDEATSALDAES 174
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
17-203 |
9.29e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 48.34 E-value: 9.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 17 DKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSN--GEAFLEPGAT-------VGILLQEPPLNEEKTVRg 87
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPtkqilkrTGFVTQDDILYPHLTVR- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 88 nveEGLgdIFEKKARF-EAIAEEMATNYTDELMEEMGKlqeeldaadaweldSKIEQAMdalrcpPADEPVTHLSGGERR 166
Cdd:PLN03211 159 ---ETL--VFCSLLRLpKSLTKQEKILVAESVISELGL--------------TKCENTI------IGNSFIRGISGGERK 213
|
170 180 190
....*....|....*....|....*....|....*..
gi 512463837 167 RVALAKLLLSEPDLLLLDEPTNHLDAESVLWLEQHLA 203
Cdd:PLN03211 214 RVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLG 250
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
7-215 |
1.19e-05 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 46.84 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEPGATVGILLQEPPLNEEKT-- 84
Cdd:PRK11701 8 SVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEAERRRll 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 85 ------VRGNVEEGL-------GDIFEkkaRFEAIAEEmatNYtdelmeemGKLQEEldAADaWEldSKIEqaMDALRCp 151
Cdd:PRK11701 88 rtewgfVHQHPRDGLrmqvsagGNIGE---RLMAVGAR---HY--------GDIRAT--AGD-WL--ERVE--IDAARI- 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 512463837 152 paDEPVTHLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAeSV----------LWLEQHLakypgAVLAVTHD 215
Cdd:PRK11701 146 --DDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDV-SVqarlldllrgLVRELGL-----AVVIVTHD 211
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
17-54 |
1.20e-05 |
|
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: 45.61 E-value: 1.20e-05
10 20 30
....*....|....*....|....*....|....*...
gi 512463837 17 DKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGL 54
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGL 50
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
312-474 |
1.26e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 48.04 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 312 PTPPRLGN-QVVEVKDL-----EKGFDgrvlIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTV 384
Cdd:PRK10522 312 PRPQAFPDwQTLELRNVtfayqDNGFS----VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLdGKPV 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 385 QLSYVDQGRENIDpektvwEVVSDG--LDYIVVGQNEMPSRA----YLSAFGFKGADQQKPSKV----LSGGERNRLNLA 454
Cdd:PRK10522 388 TAEQPEDYRKLFS------AVFTDFhlFDQLLGPEGKPANPAlvekWLERLKMAHKLELEDGRIsnlkLSKGQKKRLALL 461
|
170 180
....*....|....*....|
gi 512463837 455 LTLKQGGNLILLDEPTNDLD 474
Cdd:PRK10522 462 LALAEERDILLLDEWAADQD 481
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
288-536 |
1.32e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.43 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 288 LERYEQMVeeaeqykkLDFEEIQIPTPP-RLGNQVVEVKDLEKGFDGRV---LIKDLSFTLPRNGIVGVIGPNGVGKSTL 363
Cdd:PLN03232 588 LQRIEELL--------LSEERILAQNPPlQPGAPAISIKNGYFSWDSKTskpTLSDINLEIPVGSLVAIVGGTGEGKTSL 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 364 FKTIVG-LEQPDSGEVKVGQTV----QLSYVDQG--RENI------DPEKtVWEVVSdgldyIVVGQNEM---PSRAyLS 427
Cdd:PLN03232 660 ISAMLGeLSHAETSSVVIRGSVayvpQVSWIFNAtvRENIlfgsdfESER-YWRAID-----VTALQHDLdllPGRD-LT 732
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 428 AFGFKGADqqkpskvLSGGERNRLNLALTLKQGGNLILLDEPTNDLDVETlsslenALQNFPGCA---------VVISHD 498
Cdd:PLN03232 733 EIGERGVN-------ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHV------AHQVFDSCMkdelkgktrVLVTNQ 799
|
250 260 270
....*....|....*....|....*....|....*...
gi 512463837 499 RWFLDRTCTHILAWEGNFEEgkwfwfEGNFEGYEKNKI 536
Cdd:PLN03232 800 LHFLPLMDRIILVSEGMIKE------EGTFAELSKSGS 831
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
21-269 |
1.50e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 46.92 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 21 LDNVTMAFYPGAKIGVVGPNGAGKSSILkimagldQPSNGEAFLEPGATV----GILLQEPPLNEEKTVRGNVeeGLGDI 96
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMI-------QLTNGLIISETGQTIvgdyAIPANLKKIKEVKRLRKEI--GLVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 97 FEKKARF-EAIAEEMAtnytdelmeeMGKLQEeldAADAWELDSKIEQAMDALRCPP--ADEPVTHLSGGERRRVALAKL 173
Cdd:PRK13645 98 FPEYQLFqETIEKDIA----------FGPVNL---GENKQEAYKKVPELLKLVQLPEdyVKRSPFELSGGQKRRVALAGI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 174 LLSEPDLLLLDEPTNHLDA---ESVLWLEQHLAK-YPGAVLAVTHDRYFLDHVAGWICEVDRGKLY----PYEGNYSTYL 245
Cdd:PRK13645 165 IAMDGNTLVLDEPTGGLDPkgeEDFINLFERLNKeYKKRIIMVTHNMDQVLRIADEVIVMHEGKVIsigsPFEIFSNQEL 244
|
250 260
....*....|....*....|....
gi 512463837 246 EKKaerLEVAGKKDAKLQKRLKDE 269
Cdd:PRK13645 245 LTK---IEIDPPKLYQLMYKLKNK 265
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
36-474 |
1.52e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.70 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 36 VVGPNGAGKSSILKIMAGldqpsngeaflepgatvgillQEPPLNEEKTVRgnveeglgdiFEKKAR--FEA----IAEE 109
Cdd:PRK10938 34 FVGANGSGKSALARALAG---------------------ELPLLSGERQSQ----------FSHITRlsFEQlqklVSDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 110 MATNYTDEL---MEEMGK-----LQEELDAADAWELDSKIEQAMDALrcppaDEPVTHLSGGERRRVALAKLLLSEPDLL 181
Cdd:PRK10938 83 WQRNNTDMLspgEDDTGRttaeiIQDEVKDPARCEQLAQQFGITALL-----DRRFKYLSTGETRKTLLCQALMSEPDLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 182 LLDEPTNHLDAESVLWLEQHLAKYP--GAVLAVTHDRY-----FLDHVAgwicevdrgklypyegnystYLEKKAerLEV 254
Cdd:PRK10938 158 ILDEPFDGLDVASRQQLAELLASLHqsGITLVLVLNRFdeipdFVQFAG--------------------VLADCT--LAE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 255 AGKKDAKLQKRLKDELAWvrsgqkARQAKNKARLEryeqmVEEAEQYKKLDFEEIQIptppRLGNQVVEVKDlekgfdgR 334
Cdd:PRK10938 216 TGEREEILQQALVAQLAH------SEQLEGVQLPE-----PDEPSARHALPANEPRI----VLNNGVVSYND-------R 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 335 VLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGlEQPD--------------SGE----VK-----VGQTVQLSYvdq 391
Cdd:PRK10938 274 PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQgysndltlfgrrrgSGEtiwdIKkhigyVSSSLHLDY--- 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 392 gRENIdpekTVWEVVSDG-LDYIVVGQ-----NEMPSRAYLSAFGFKGADQQKPSKVLSGGERNRLNLALTLKQGGNLIL 465
Cdd:PRK10938 350 -RVST----SVRNVILSGfFDSIGIYQavsdrQQKLAQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLI 424
|
....*....
gi 512463837 466 LDEPTNDLD 474
Cdd:PRK10938 425 LDEPLQGLD 433
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
345-503 |
1.60e-05 |
|
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: 46.59 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 345 PRNG-IVGVIGPNGVGKSTLFKTIVGLEQPD------------------------------SGEVKVGQTVQlsYVDQ-- 391
Cdd:cd03236 23 PREGqVLGLVGPNGIGKSTALKILAGKLKPNlgkfddppdwdeildefrgselqnyftkllEGDVKVIVKPQ--YVDLip 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 392 ------GRENIDP--EKTVWEVVSDGLDYIVVGQNEMPSraylsafgfkgadqqkpskvLSGGERNRLNLALTLKQGGNL 463
Cdd:cd03236 101 kavkgkVGELLKKkdERGKLDELVDQLELRHVLDRNIDQ--------------------LSGGELQRVAIAAALARDADF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 512463837 464 ILLDEPTNDLDVE---TLSSLENALQNFPGCAVVISHDRWFLD 503
Cdd:cd03236 161 YFFDEPSSYLDIKqrlNAARLIRELAEDDNYVLVVEHDLAVLD 203
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
7-61 |
1.63e-05 |
|
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: 46.51 E-value: 1.63e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 512463837 7 QMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGE 61
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGS 59
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
5-223 |
1.65e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 46.65 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 5 IYQMKNVR---KAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEPGA-----------TV 70
Cdd:PRK13650 4 IIEVKNLTfkyKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLlteenvwdirhKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 71 GILLQEPplnEEKTVRGNVEEGLGDIFEKKArfeaIAEEMATNYTDELMEEMGklqeeldaadaweldskieqaMDALRc 150
Cdd:PRK13650 84 GMVFQNP---DNQFVGATVEDDVAFGLENKG----IPHEEMKERVNEALELVG---------------------MQDFK- 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 512463837 151 ppADEPvTHLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAESVLWLEQHLAK----YPGAVLAVTHDryfLDHVA 223
Cdd:PRK13650 135 --EREP-ARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGirddYQMTVISITHD---LDEVA 205
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
321-498 |
1.69e-05 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 47.01 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 321 VVEVKDLEKGFD---GRVL----------IKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVK-VGQTVQL 386
Cdd:PRK15079 8 LLEVADLKVHFDikdGKQWfwqppktlkaVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAwLGKDLLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 387 SYVDQGRE--------------NIDPEKTVWEVVSDgldyivvgqnemPSRAY---LSAFGFKGADQQKPSKV------- 442
Cdd:PRK15079 88 MKDDEWRAvrsdiqmifqdplaSLNPRMTIGEIIAE------------PLRTYhpkLSRQEVKDRVKAMMLKVgllpnli 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 512463837 443 ------LSGGERNRLNLALTLKQGGNLILLDEPTNDLDVETLSSLENALQNFP---GCAVV-ISHD 498
Cdd:PRK15079 156 nrypheFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQremGLSLIfIAHD 221
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
351-509 |
1.78e-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: 48.09 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 351 GVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQTVQLSYVDQGRENID--PEktvwevvSDGLDYIVVGQNEMpsraYLSA 428
Cdd:TIGR01257 1969 GLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGycPQ-------FDAIDDLLTGREHL----YLYA 2037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 429 fGFKGADQQKPSKV--------------------LSGGERNRLNLALTLKQGGNLILLDEPTNDLDVETLSSLENALQNF 488
Cdd:TIGR01257 2038 -RLRGVPAEEIEKVanwsiqslglslyadrlagtYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSI 2116
|
170 180
....*....|....*....|....
gi 512463837 489 --PGCAVVI-SHDRWFLDRTCTHI 509
Cdd:TIGR01257 2117 irEGRAVVLtSHSMEECEALCTRL 2140
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
30-217 |
2.01e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 46.00 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 30 PGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAflepgatvgillqepPLNEEKTVRGNveeglgdifekKARFEAiaee 109
Cdd:PRK13543 36 AGEALLVQGDNGAGKTTLLRVLAGLLHVESGQI---------------QIDGKTATRGD-----------RSRFMA---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 110 matnytdeLMEEMGKLQEELDAADAWELDSKIeQAMDALRCPP-----------ADEPVTHLSGGERRRVALAKLLLSEP 178
Cdd:PRK13543 86 --------YLGHLPGLKADLSTLENLHFLCGL-HGRRAKQMPGsalaivglagyEDTLVRQLSAGQKKRLALARLWLSPA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 512463837 179 DLLLLDEPTNHLDAESVLWLEQHLAKY---PGAVLAVTHDRY 217
Cdd:PRK13543 157 PLWLLDEPYANLDLEGITLVNRMISAHlrgGGAALVTTHGAY 198
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
321-497 |
2.44e-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: 47.13 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 321 VVEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLeQPD---SGEVK-VGQTVQLSYV-DQGREN 395
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHgtwDGEIYwSGSPLKASNIrDTERAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 396 ID---------PEKTVWEVVSDGLDYIVVGQ----NEMPSRAY--LSAFGFKGADQQKPSKVLSGGERNRLNLALTLKQG 460
Cdd:TIGR02633 80 IViihqeltlvPELSVAENIFLGNEITLPGGrmayNAMYLRAKnlLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 512463837 461 GNLILLDEPTNDL---DVETLSSLENALQNFPGCAVVISH 497
Cdd:TIGR02633 160 ARLLILDEPSSSLtekETEILLDIIRDLKAHGVACVYISH 199
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
7-194 |
2.51e-05 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 45.56 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNV--RKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFL--EPGATVG---------IL 73
Cdd:cd03244 4 EFKNVslRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIdgVDISKIGlhdlrsrisII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 74 LQEPPLnEEKTVRGNVeeglgDIFEKkarfeaiaeematnYTDElmeemgKLQEELDAADAWELdskIEQAMDALRCPPA 153
Cdd:cd03244 84 PQDPVL-FSGTIRSNL-----DPFGE--------------YSDE------ELWQALERVGLKEF---VESLPGGLDTVVE 134
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 512463837 154 DEPvTHLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAES 194
Cdd:cd03244 135 EGG-ENLSVGQRQLLCLARALLRKSKILVLDEATASVDPET 174
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-215 |
2.55e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 46.38 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 1 MGEFIYQMKNVRKAHGDKV-ILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEaflepgatvgILLQEPPL 79
Cdd:PRK13636 1 MEDYILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGR----------ILFDGKPI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 80 NEEKTVRGNVEEGLGDIFEKKAR--FEAiaeemaTNYTDELMEEMG-KLQEEldaadawELDSKIEQAMDALRCPPADEP 156
Cdd:PRK13636 71 DYSRKGLMKLRESVGMVFQDPDNqlFSA------SVYQDVSFGAVNlKLPED-------EVRKRVDNALKRTGIEHLKDK 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 512463837 157 VTH-LSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAESV---LWLEQHLAKYPG-AVLAVTHD 215
Cdd:PRK13636 138 PTHcLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVseiMKLLVEMQKELGlTIIIATHD 201
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
21-223 |
2.68e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 46.50 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 21 LDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPS------NGEAFLEPGAT--------VGILLQEP--PLNEEKT 84
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTggelyyQGQDLLKADPEaqkllrqkIQIVFQNPygSLNPRKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 85 VrgnveeglGDIFEkkarfeaiaEEMATNyTDelmeemgklqeeLDAAdawELDSKIEQAMD--ALRCPPADEPVTHLSG 162
Cdd:PRK11308 111 V--------GQILE---------EPLLIN-TS------------LSAA---ERREKALAMMAkvGLRPEHYDRYPHMFSG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 512463837 163 GERRRVALAKLLLSEPDLLLLDEPTNHLDAE---SVLWLEQHLAKYPG-AVLAVTHDRYFLDHVA 223
Cdd:PRK11308 158 GQRQRIAIARALMLDPDVVVADEPVSALDVSvqaQVLNLMMDLQQELGlSYVFISHDLSVVEHIA 222
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
21-171 |
2.95e-05 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 46.14 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 21 LDNVTMAFYPGAKIGV-VGPNGAGKSSILKIMAGLDQPSNGEAFLEPGATVGI-------------------LLQEPPLN 80
Cdd:COG3950 14 FEDLEIDFDNPPRLTVlVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLLIrngefgdsaklilyygtsrLLLDGPLK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 81 EEKTVRGNVE---EGLGDIFEKKARFEAIAEEMATNYTDELMEEMGKLQEELDAA---------DAWELDSKIEQAMDAL 148
Cdd:COG3950 94 KLERLKEEYFsrlDGYDSLLDEDSNLREFLEWLREYLEDLENKLSDELDEKLEAVrealnkllpDFKDIRIDRDPGRLVI 173
|
170 180
....*....|....*....|....
gi 512463837 149 RCPPADE-PVTHLSGGERRRVALA 171
Cdd:COG3950 174 LDKNGEElPLNQLSDGERSLLALV 197
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
21-63 |
3.82e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 44.86 E-value: 3.82e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 512463837 21 LDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAF 63
Cdd:PRK13541 16 LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIY 58
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-194 |
4.50e-05 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 46.17 E-value: 4.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 4 FIYQMKnvrkahgDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEpgatvGILLQEPPL---- 79
Cdd:PRK11176 349 FTYPGK-------EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLD-----GHDLRDYTLaslr 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 80 NEEKTVRGNVEeglgdIFEkkarfEAIAEEMA----TNYTDELMEEMGKLqeeldaADAWELDSKIEQAMDALrcppADE 155
Cdd:PRK11176 417 NQVALVSQNVH-----LFN-----DTIANNIAyartEQYSREQIEEAARM------AYAMDFINKMDNGLDTV----IGE 476
|
170 180 190
....*....|....*....|....*....|....*....
gi 512463837 156 PVTHLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAES 194
Cdd:PRK11176 477 NGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTES 515
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
18-215 |
5.01e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 45.20 E-value: 5.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 18 KVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGldqpsngeAFLEPGATVGIllqepplneekTVRGNVE---EGLG 94
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG--------DLTGGGAPRGA-----------RVTGDVTlngEPLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 95 DIFEKK-ARFEAI---AEEMATNYTDELMEEMGKLQEELDAADAWELDSKIeqAMDALRCPPAD----EPVTHLSGGERR 166
Cdd:PRK13547 75 AIDAPRlARLRAVlpqAAQPAFAFSAREIVLLGRYPHARRAGALTHRDGEI--AWQALALAGATalvgRDVTTLSGGELA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 512463837 167 RVALAK---------LLLSEPDLLLLDEPTNHLD---AESVLWLEQHLAK-YPGAVLAVTHD 215
Cdd:PRK13547 153 RVQFARvlaqlwpphDAAQPPRYLLLDEPTAALDlahQHRLLDTVRRLARdWNLGVLAIVHD 214
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
17-77 |
5.13e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 45.37 E-value: 5.13e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 512463837 17 DKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEpGAT------------VGILLQEP 77
Cdd:PRK13632 21 ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKID-GITiskenlkeirkkIGIIFQNP 92
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
346-504 |
5.20e-05 |
|
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: 44.52 E-value: 5.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 346 RNGIVGVIGPNGVGKSTLFKTIV----GLEQPDS----------GEVKVGQTVQLSY-VDQGREnidpektvWEVV--SD 408
Cdd:cd03240 21 FSPLTLIVGQNGAGKTTIIEALKyaltGELPPNSkggahdpkliREGEVRAQVKLAFeNANGKK--------YTITrsLA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 409 GLDYIV-VGQNEMPSRAYLsafgfkgadqqkPSKVLSGGERN------RLNLALTLKQGGNLILLDEPTNDLDVETLSS- 480
Cdd:cd03240 93 ILENVIfCHQGESNWPLLD------------MRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEEs 160
|
170 180
....*....|....*....|....*...
gi 512463837 481 ----LENALQNFPGCAVVISHDRWFLDR 504
Cdd:cd03240 161 laeiIEERKSQKNFQLIVITHDEELVDA 188
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
18-191 |
5.21e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 45.08 E-value: 5.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 18 KVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEPGAT------------VGILLQEPplnEEKTV 85
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTsdeenlwdirnkAGMVFQNP---DNQIV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 86 RGNVEEglgDIfekkarfeAIAEEMATNYTDELMEemgKLQEELDAADAWELDskieqamdalRCPPadepvtH-LSGGE 164
Cdd:PRK13633 100 ATIVEE---DV--------AFGPENLGIPPEEIRE---RVDESLKKVGMYEYR----------RHAP------HlLSGGQ 149
|
170 180
....*....|....*....|....*..
gi 512463837 165 RRRVALAKLLLSEPDLLLLDEPTNHLD 191
Cdd:PRK13633 150 KQRVAIAGILAMRPECIIFDEPTAMLD 176
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
321-498 |
5.39e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 45.34 E-value: 5.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 321 VVEVKDLEK------G-FDGRVLIKDL---SFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTVQL--- 386
Cdd:PRK11308 5 LLQAIDLKKhypvkrGlFKPERLVKALdgvSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYqGQDLLKadp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 387 SYVDQGRENI-----------DPEKTVWEVVSDGLDY---IVVGQNEMPSRAYLSAFGFKGADQQKPSKVLSGGERNRLN 452
Cdd:PRK11308 85 EAQKLLRQKIqivfqnpygslNPRKKVGQILEEPLLIntsLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQRQRIA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 512463837 453 LALTLKQGGNLILLDEPTNDLDVETLSSLENA---LQNFPGCA-VVISHD 498
Cdd:PRK11308 165 IARALMLDPDVVVADEPVSALDVSVQAQVLNLmmdLQQELGLSyVFISHD 214
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
340-513 |
5.72e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.12 E-value: 5.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 340 LSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEV--------KVGQT---VQLSYVDQG--------RENIDP-- 398
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRImiddcdvaKFGLTdlrRVLSIIPQSpvlfsgtvRFNIDPfs 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 399 ---EKTVWEVVSDGLDYIVVGQNEMPsrayLSAFGFKGADQqkpskvLSGGERNRLNLALTLKQGGNLILLDEPTNDLDV 475
Cdd:PLN03232 1335 ehnDADLWEALERAHIKDVIDRNPFG----LDAEVSEGGEN------FSVGQRQLLSLARALLRRSKILVLDEATASVDV 1404
|
170 180 190
....*....|....*....|....*....|....*....
gi 512463837 476 ETLSSLENAL-QNFPGCAVVISHDRWFLDRTCTHILAWE 513
Cdd:PLN03232 1405 RTDSLIQRTIrEEFKSCTMLVIAHRLNTIIDCDKILVLS 1443
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
21-234 |
5.90e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 45.21 E-value: 5.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 21 LDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGE---------------AFLEPGATVGILLQEPPLNE-EKT 84
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTitiagyhitpetgnkNLKKLRKKVSLVFQFPEAQLfENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 85 VRGNVEEG---LGdIFEKKARFEAIaeematnytdELMEEMGkLQEELDAADAWELdskieqamdalrcppadepvthlS 161
Cdd:PRK13641 103 VLKDVEFGpknFG-FSEDEAKEKAL----------KWLKKVG-LSEDLISKSPFEL-----------------------S 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 512463837 162 GGERRRVALAKLLLSEPDLLLLDEPTNHLDAESVLWLEQHLAKYPGA---VLAVTHDryfLDHVAGWICEV---DRGKL 234
Cdd:PRK13641 148 GGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAghtVILVTHN---MDDVAEYADDVlvlEHGKL 223
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
17-191 |
6.11e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 45.04 E-value: 6.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 17 DKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEpgaTVGILLQEPPLNEektVRGNVeeGL--- 93
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIID---GVDITDKKVKLSD---IRKKV--GLvfq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 94 ---GDIFEkkarfEAIAEEMATNYTDelmeeMGkLQEEldaadawELDSKIEQAMDALRCPP---ADEPVTHLSGGERRR 167
Cdd:PRK13637 91 ypeYQLFE-----ETIEKDIAFGPIN-----LG-LSEE-------EIENRVKRAMNIVGLDYedyKDKSPFELSGGQKRR 152
|
170 180
....*....|....*....|....
gi 512463837 168 VALAKLLLSEPDLLLLDEPTNHLD 191
Cdd:PRK13637 153 VAIAGVVAMEPKILILDEPTAGLD 176
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
9-215 |
9.04e-05 |
|
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: 44.21 E-value: 9.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 9 KNVRKAHGD-KVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEPGAT-----------VGILLQE 76
Cdd:cd03295 4 ENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIreqdpvelrrkIGYVIQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 77 PPLNEEKTVRGNVEEGLGDIFEKKARFEAIAeematnytDELMEEMGklqeeldaadaweldskIEQAMDALRCPpaDEp 156
Cdd:cd03295 84 IGLFPHMTVEENIALVPKLLKWPKEKIRERA--------DELLALVG-----------------LDPAEFADRYP--HE- 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 512463837 157 vthLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDA-------ESVLWLEQHLAKypgAVLAVTHD 215
Cdd:cd03295 136 ---LSGGQQQRVGVARALAADPPLLLMDEPFGALDPitrdqlqEEFKRLQQELGK---TIVFVTHD 195
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-215 |
1.03e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 44.32 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 10 NVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAF-----------------LEPGATVGI 72
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYsgdvllggrsifnyrdvLEFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 73 LLQEP---PLneekTVRGNVEEGL-GDIFEKKARFEAIAeematnytdelmeemgklQEELDAADAWeldskieqamDAL 148
Cdd:PRK14271 106 LFQRPnpfPM----SIMDNVLAGVrAHKLVPRKEFRGVA------------------QARLTEVGLW----------DAV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 512463837 149 RCPPADEPVtHLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAESVLWLEQHLAKYPG--AVLAVTHD 215
Cdd:PRK14271 154 KDRLSDSPF-RLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHN 221
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
18-193 |
1.08e-04 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 43.79 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 18 KVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAG--LDQPSNGEaflepgatvgILLQEPPLNEEKTVRgnveEGLGD 95
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGC----------VDVPDNQFGREASLI----DAIGR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 96 IFEKKARFEAIAeematnytdelmeeMGKLqeeldaADAWELdskieqamdaLRCPPadepvtHLSGGERRRVALAKLLL 175
Cdd:COG2401 109 KGDFKDAVELLN--------------AVGL------SDAVLW----------LRRFK------ELSTGQKFRFRLALLLA 152
|
170
....*....|....*...
gi 512463837 176 SEPDLLLLDEPTNHLDAE 193
Cdd:COG2401 153 ERPKLLVIDEFCSHLDRQ 170
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
9-171 |
1.12e-04 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 44.81 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 9 KNVRKAH-GDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEpG------------ATVGILLQ 75
Cdd:COG5265 361 ENVSFGYdPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILID-GqdirdvtqaslrAAIGIVPQ 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 76 EPPL-NEekTVRGNVEEGlgdifekkaRFEAIAEEMAtnytdelmeemgklqeelDAADAWELDSKIEQAMDALrcppaD 154
Cdd:COG5265 440 DTVLfND--TIAYNIAYG---------RPDASEEEVE------------------AAARAAQIHDFIESLPDGY-----D 485
|
170 180
....*....|....*....|.
gi 512463837 155 EPVTH----LSGGERRRVALA 171
Cdd:COG5265 486 TRVGErglkLSGGEKQRVAIA 506
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
337-498 |
1.25e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 44.00 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 337 IKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQTVQLS-----YVDQGRENID-----PEKTVWEvv 406
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkYIRPVRKRIGmvfqfPESQLFE-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 407 sDGLDY-IVVGQ-------NEMPSRAY--LSAFGFKGADQQKPSKVLSGGERNRLNLALTLKQGGNLILLDEPTNDLDVE 476
Cdd:PRK13646 101 -DTVEReIIFGPknfkmnlDEVKNYAHrlLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQ 179
|
170 180
....*....|....*....|....*.
gi 512463837 477 T---LSSLENALQNFPGCAVV-ISHD 498
Cdd:PRK13646 180 SkrqVMRLLKSLQTDENKTIIlVSHD 205
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
321-478 |
1.30e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 44.00 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 321 VVEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEqpdsgEVKVGQTVQLSYVDQGRENIDPEK 400
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLN-----DLIPGFRVEGKVTFHGKNLYAPDV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 401 TVWEVVSD-GLdyivVGQ--NEMPSRAYLS-AF-----GFKG-------------------ADQQKPSKV-LSGGERNRL 451
Cdd:PRK14243 85 DPVEVRRRiGM----VFQkpNPFPKSIYDNiAYgarinGYKGdmdelverslrqaalwdevKDKLKQSGLsLSGGQQQRL 160
|
170 180
....*....|....*....|....*...
gi 512463837 452 NLALTLKQGGNLILLDEPTNDLD-VETL 478
Cdd:PRK14243 161 CIARAIAVQPEVILMDEPCSALDpISTL 188
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
9-65 |
1.30e-04 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 43.90 E-value: 1.30e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 512463837 9 KNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLD--QPSNGEAFLE 65
Cdd:COG0396 4 KNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLD 62
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
409-510 |
1.32e-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: 43.76 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 409 GLDYIVVGQnempsraylsafgfkgadqqkPSKVLSGGERNRLNLA--LTLKQGGN-LILLDEPTNDL---DVETLSSLE 482
Cdd:cd03271 157 GLGYIKLGQ---------------------PATTLSGGEAQRIKLAkeLSKRSTGKtLYILDEPTTGLhfhDVKKLLEVL 215
|
90 100 110
....*....|....*....|....*....|
gi 512463837 483 NALQNFPGCAVVISHDrwfLD--RTCTHIL 510
Cdd:cd03271 216 QRLVDKGNTVVVIEHN---LDviKCADWII 242
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
7-53 |
1.38e-04 |
|
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: 43.79 E-value: 1.38e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 512463837 7 QMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAG 53
Cdd:TIGR01978 2 KIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAG 48
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
7-194 |
1.47e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.02 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVR---KAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEPG------------ATVG 71
Cdd:PTZ00265 384 QFKNVRfhyDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShnlkdinlkwwrSKIG 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 72 ILLQEPPLNEeKTVRGNVEEGLGDIFEKKARFEAIAEE-------------------------MATNYTDELMEeMGKLQ 126
Cdd:PTZ00265 464 VVSQDPLLFS-NSIKNNIKYSLYSLKDLEALSNYYNEDgndsqenknkrnscrakcagdlndmSNTTDSNELIE-MRKNY 541
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 512463837 127 EELDAADAWELDSK--IEQAMDALrcPPADEPV-----THLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAES 194
Cdd:PTZ00265 542 QTIKDSEVVDVSKKvlIHDFVSAL--PDKYETLvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
10-53 |
1.48e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 44.73 E-value: 1.48e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 512463837 10 NVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAG 53
Cdd:NF033858 6 GVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAG 49
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
7-186 |
2.09e-04 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 43.22 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEpGATVgillqePPLNEEKTVr 86
Cdd:PRK11831 9 DMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFD-GENI------PAMSRSRLY- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 87 gNVEEGLGDIFEKKARFEAIaeematNYTDEL---MEEMGKLQEELdaadaweLDSKIEQAMDA--LRCPPADEPvTHLS 161
Cdd:PRK11831 81 -TVRKRMSMLFQSGALFTDM------NVFDNVaypLREHTQLPAPL-------LHSTVMMKLEAvgLRGAAKLMP-SELS 145
|
170 180
....*....|....*....|....*
gi 512463837 162 GGERRRVALAKLLLSEPDLLLLDEP 186
Cdd:PRK11831 146 GGMARRAALARAIALEPDLIMFDEP 170
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-200 |
2.25e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 43.10 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 7 QMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQpsngeaflepgatvgillqeppLNEEKTVR 86
Cdd:PRK14258 9 KVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE----------------------LESEVRVE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 87 GNVEEGLGDIFEKKARFEAIAEEMATNYTDELMEEM----------------------GKLQEELDAADAW-ELDSKIEQ 143
Cdd:PRK14258 67 GRVEFFNQNIYERRVNLNRLRRQVSMVHPKPNLFPMsvydnvaygvkivgwrpkleidDIVESALKDADLWdEIKHKIHK 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 512463837 144 -AMDalrcppadepvthLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAESVLWLEQ 200
Cdd:PRK14258 147 sALD-------------LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVES 191
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
21-225 |
2.33e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 43.18 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 21 LDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNG--------------EAFLEP-GATVGILLQEPPLNE-EKT 84
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGkvtvgdivvsstskQKEIKPvRKKVGVVFQFPESQLfEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 85 VRGNVEEGLGDIFEKKARFEAIAEEMAtnytdelmeEMGKLQEELdaadaWElDSKIEqamdalrcppadepvthLSGGE 164
Cdd:PRK13643 102 VLKDVAFGPQNFGIPKEKAEKIAAEKL---------EMVGLADEF-----WE-KSPFE-----------------LSGGQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 512463837 165 RRRVALAKLLLSEPDLLLLDEPTNHLDAES---VLWLEQHLAKYPGAVLAVTHdryFLDHVAGW 225
Cdd:PRK13643 150 MRRVAIAGILAMEPEVLVLDEPTAGLDPKArieMMQLFESIHQSGQTVVLVTH---LMDDVADY 210
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
20-194 |
2.65e-04 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 42.40 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 20 ILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEP-----------GATVGILLQEPPLnEEKTVRGN 88
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlRSSLTIIPQDPTL-FSGTIRSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 89 VeeglgDIFEKkarfeaiaeematnYTDelmeemgklqeeldaadaweldskiEQAMDALRcppADEPVTHLSGGERRRV 168
Cdd:cd03369 102 L-----DPFDE--------------YSD-------------------------EEIYGALR---VSEGGLNLSQGQRQLL 134
|
170 180
....*....|....*....|....*.
gi 512463837 169 ALAKLLLSEPDLLLLDEPTNHLDAES 194
Cdd:cd03369 135 CLARALLKRPRVLVLDEATASIDYAT 160
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
18-215 |
2.66e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 43.25 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 18 KVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPS--------------NGEAFLEPGATVGILLQEPplnEEK 83
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDdnpnskitvdgitlTAKTVWDIREKVGIVFQNP---DNQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 84 TVRGNVEEGLGDIFEKKArfeAIAEEMATNYTDELmEEMGKLqeelDAADAweldskieqamdalrcppadEPvTHLSGG 163
Cdd:PRK13640 97 FVGATVGDDVAFGLENRA---VPRPEMIKIVRDVL-ADVGML----DYIDS--------------------EP-ANLSGG 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 512463837 164 ERRRVALAKLLLSEPDLLLLDEPTNHLDA---ESVLWLEQHLAKYPG-AVLAVTHD 215
Cdd:PRK13640 148 QKQRVAIAGILAVEPKIIILDESTSMLDPagkEQILKLIRKLKKKNNlTVISITHD 203
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
322-384 |
2.86e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 43.29 E-value: 2.86e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 512463837 322 VEVKDLEKGFDGRVL-IKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQTV 384
Cdd:PRK11650 4 LKLQAVRKSYDGKTQvIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRV 67
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
16-214 |
3.16e-04 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 43.58 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 16 GDKVILDnVTMAFYPGAKIGVVGPNGAGKSSILKIMAGL--------DQPSNGEAFLEPgatvgillQEPPLNEeKTVRG 87
Cdd:TIGR00954 464 GDVLIES-LSFEVPSGNNLLICGPNGCGKSSLFRILGELwpvyggrlTKPAKGKLFYVP--------QRPYMTL-GTLRD 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 88 NV--EEGLGDIFEKKARfEAIAEEMATN--YTDELMEEMGklqeeLDAADAWeldskieqaMDALrcppadepvthlSGG 163
Cdd:TIGR00954 534 QIiyPDSSEDMKRRGLS-DKDLEQILDNvqLTHILEREGG-----WSAVQDW---------MDVL------------SGG 586
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 512463837 164 ERRRVALAKLLLSEPDLLLLDEPTNHLDAESVLWLEQHLAKYPGAVLAVTH 214
Cdd:TIGR00954 587 EKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
8-196 |
3.19e-04 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 42.25 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 8 MKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLdqpsngeaflePGATVGIllqepplnEEKTVRG 87
Cdd:cd03233 10 SFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR-----------TEGNVSV--------EGDIHYN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 88 NVEeglGDIFEKKARFEAI--AEEmatnytDELMEEMgklqeeldaadaweldsKIEQAMD-ALRCPpADEPVTHLSGGE 164
Cdd:cd03233 71 GIP---YKEFAEKYPGEIIyvSEE------DVHFPTL-----------------TVRETLDfALRCK-GNEFVRGISGGE 123
|
170 180 190
....*....|....*....|....*....|..
gi 512463837 165 RRRVALAKLLLSEPDLLLLDEPTNHLDAESVL 196
Cdd:cd03233 124 RKRVSIAEALVSRASVLCWDNSTRGLDSSTAL 155
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
21-171 |
3.35e-04 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 42.80 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 21 LDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLE-------PGAT-------VGILLQEP--PLNEEKT 84
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDgqditglSGRElrplrrrMQMVFQDPyaSLNPRMT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 85 VRGNVEEGLgDIFE---KKARFEAIAEematnytdeLMEEMGklqeeLDAADAweldskieqamdaLRCPpadepvtH-L 160
Cdd:COG4608 114 VGDIIAEPL-RIHGlasKAERRERVAE---------LLELVG-----LRPEHA-------------DRYP-------HeF 158
|
170
....*....|.
gi 512463837 161 SGGERRRVALA 171
Cdd:COG4608 159 SGGQRQRIGIA 169
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
23-504 |
3.67e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 43.31 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 23 NVTMAFYPGAKIGVVGPNGAGKS-SILKIMAGLDQP----SNGEAFLEPGATVGILLQEPPLNEEKTVRGnveEGLGDIF 97
Cdd:PRK10261 34 NLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQAgglvQCDKMLLRRRSRQVIELSEQSAAQMRHVRG---ADMAMIF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 98 EKKARF--------EAIAEEMatnytdELMEEMGKlQEELDAAdaweldskiEQAMDALRCPPADEPVT----HLSGGER 165
Cdd:PRK10261 111 QEPMTSlnpvftvgEQIAESI------RLHQGASR-EEAMVEA---------KRMLDQVRIPEAQTILSryphQLSGGMR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 166 RRVALAKLLLSEPDLLLLDEPTNHLDA-------ESVLWLEQHLAKypgAVLAVTHDryfldhvAGWICEVDRGKLYPYE 238
Cdd:PRK10261 175 QRVMIAMALSCRPAVLIADEPTTALDVtiqaqilQLIKVLQKEMSM---GVIFITHD-------MGVVAEIADRVLVMYQ 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 239 GnystyleKKAERLEVAGKKDAKLQKRLKDELAWV-RSGqkarqAKNKARLERYEQMV--EEAEQYKKLDFEEIQIPTPP 315
Cdd:PRK10261 245 G-------EAVETGSVEQIFHAPQHPYTRALLAAVpQLG-----AMKGLDYPRRFPLIslEHPAKQEPPIEQDTVVDGEP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 316 rlgnqVVEVKDL------EKGFDGRV-----LIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVG--- 381
Cdd:PRK10261 313 -----ILQVRNLvtrfplRSGLLNRVtrevhAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNgqr 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 382 -QTVQLSYVDQGRENI-----------DPEKTVWEVVSDGLDYIVVGQNEMPSRA---YLSAFGFKGADQQKPSKVLSGG 446
Cdd:PRK10261 388 iDTLSPGKLQALRRDIqfifqdpyaslDPRQTVGDSIMEPLRVHGLLPGKAAAARvawLLERVGLLPEHAWRYPHEFSGG 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 512463837 447 ERNRLNLALTLKQGGNLILLDEPTNDLDVETLSSLENA---LQNFPGCA-VVISHDRWFLDR 504
Cdd:PRK10261 468 QRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLlldLQRDFGIAyLFISHDMAVVER 529
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
16-228 |
3.68e-04 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 42.79 E-value: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 16 GDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLdQPSNGEafLEPGATVG---IL-LQEPPLNeektvrgnvee 91
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGL-LAANGR--IGGSATFNgreILnLPEKELN----------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 92 glgdifekKARFEAIA----EEMAT-----NYTDELMEEMgKLQEELDAADAWELDSKIeqaMDALRCPPADEPVT---H 159
Cdd:PRK09473 93 --------KLRAEQISmifqDPMTSlnpymRVGEQLMEVL-MLHKGMSKAEAFEESVRM---LDAVKMPEARKRMKmypH 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 512463837 160 -LSGGERRRVALAKLLLSEPDLLLLDEPTNHLD----AESVLWLEQHLAKYPGAVLAVTHDryfLDHVAGwICE 228
Cdd:PRK09473 161 eFSGGMRQRVMIAMALLCRPKLLIADEPTTALDvtvqAQIMTLLNELKREFNTAIIMITHD---LGVVAG-ICD 230
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
21-229 |
3.86e-04 |
|
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: 42.73 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 21 LDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQP---SNGEAFLEpgatvGILLQEPPLNEEKTVRGNveeGLGDIF 97
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFD-----GEDLLKLSEKELRKIRGR---EIQMIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 98 EkkarfeaiaEEMAT-N--YT-DELMEEMGKLQEELDAADAWEldsKIEQAMDALRCPPADE-----PvtH-LSGGERRR 167
Cdd:COG0444 93 Q---------DPMTSlNpvMTvGDQIAEPLRIHGGLSKAEARE---RAIELLERVGLPDPERrldryP--HeLSGGMRQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 512463837 168 VALAklllsepdlllLDEPTNHLDAE---SVLWLEQHLAKYPG-AVLAVTHD----RYFLDHV----AGWICEV 229
Cdd:COG0444 159 VMIAralalepklliADEPTTALDVTiqaQILNLLKDLQRELGlAILFITHDlgvvAEIADRVavmyAGRIVEE 232
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
337-502 |
4.61e-04 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 41.93 E-value: 4.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 337 IKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQTV--QLSYVDQGRENIDP----EKTVWEVVSDGL 410
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNesEPSFEATRSRNRYSvayaAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 411 DYIVVGQ--NEMPSRAYLSAFGFKG-------ADQQKPSKV---LSGGERNRLNLALTLKQGGNLILLDEPTNDLDVETL 478
Cdd:cd03290 97 ENITFGSpfNKQRYKAVTDACSLQPdidllpfGDQTEIGERginLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLS 176
|
170 180
....*....|....*....|....*....
gi 512463837 479 SSLENA-----LQNFPGCAVVISHDRWFL 502
Cdd:cd03290 177 DHLMQEgilkfLQDDKRTLVLVTHKLQYL 205
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
21-194 |
4.77e-04 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 42.31 E-value: 4.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 21 LDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLdqpSNGEAflEPGATVGILlqepplneEKTVRgnvEEG--LGDIFE 98
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL---ITGDK--SAGSHIELL--------GRTVQ---REGrlARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 99 KKARFEAIAEEMatNYTDELMEEMGKLQEELDAADAWEL------DSKIEQAMDALR----CPPADEPVTHLSGGERRRV 168
Cdd:PRK09984 84 SRANTGYIFQQF--NLVNRLSVLENVLIGALGSTPFWRTcfswftREQKQRALQALTrvgmVHFAHQRVSTLSGGQQQRV 161
|
170 180
....*....|....*....|....*.
gi 512463837 169 ALAKLLLSEPDLLLLDEPTNHLDAES 194
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPES 187
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-65 |
5.26e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 42.00 E-value: 5.26e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 512463837 18 KVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLE 65
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILID 66
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
14-222 |
5.87e-04 |
|
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: 43.01 E-value: 5.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 14 AHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEpgATVGILLQEPPLnEEKTVRGNVEegL 93
Cdd:TIGR00957 647 ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMK--GSVAYVPQQAWI-QNDSLRENIL--F 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 94 GDIFEKKaRFEAIAEEMAtnytdeLMEEMgklqEELDAADAWELDSKieqamdalrcppadepVTHLSGGERRRVALAKL 173
Cdd:TIGR00957 722 GKALNEK-YYQQVLEACA------LLPDL----EILPSGDRTEIGEK----------------GVNLSGGQKQRVSLARA 774
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 512463837 174 LLSEPDLLLLDEPTNHLDAesvlwleqHLAKY-------PGAVLA------VTHDRYFLDHV 222
Cdd:TIGR00957 775 VYSNADIYLFDDPLSAVDA--------HVGKHifehvigPEGVLKnktrilVTHGISYLPQV 828
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
321-503 |
5.90e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 41.70 E-value: 5.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 321 VVEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLE--QPDSGEVkvgqtvqlSYVDQGRENIDP 398
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTV--------EFKGKDLLELSP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 399 EKTVWEVVSDGLDYIVvgqnEMPS--------------RAY-----LSAFGFKGADQQK------PSKVL--------SG 445
Cdd:PRK09580 73 EDRAGEGIFMAFQYPV----EIPGvsnqfflqtalnavRSYrgqepLDRFDFQDLMEEKiallkmPEDLLtrsvnvgfSG 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 512463837 446 GERNRLNLALTLKQGGNLILLDEPTNDLDVETLSSLE---NALQNFPGCAVVISHDRWFLD 503
Cdd:PRK09580 149 GEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVAdgvNSLRDGKRSFIIVTHYQRILD 209
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
8-475 |
6.06e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.41 E-value: 6.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 8 MKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAF--------------LEPGatVGIL 73
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILfqgkeidfksskeaLENG--ISMV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 74 LQEPPLNEEKTVRGNVEEGLgdiFEKKARFEAiaeematnyTDELMEEMGKLQEELDAadawELDSKieqamdalrcppa 153
Cdd:PRK10982 79 HQELNLVLQRSVMDNMWLGR---YPTKGMFVD---------QDKMYRDTKAIFDELDI----DIDPR------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 154 dEPVTHLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAESVlwleQHLAKypgaVLAVTHDRyfldhvagwicevdrgk 233
Cdd:PRK10982 130 -AKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEV----NHLFT----IIRKLKER----------------- 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 234 lypyeGNYSTYLEKKAERLevagkkdaklqKRLKDELAWVRSGQ-KARQAKNKARLERYEQMVEEAEQYKKLDfEEIQIP 312
Cdd:PRK10982 184 -----GCGIVYISHKMEEI-----------FQLCDEITILRDGQwIATQPLAGLTMDKIIAMMVGRSLTQRFP-DKENKP 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 313 tpprlGNQVVEVKDLEKGfdGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTVQlsyvdq 391
Cdd:PRK10982 247 -----GEVILEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLhGKKIN------ 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 392 greNIDPEKTV--------WEVVSDGL-DYIVVGQNEMPS--RAYLSAFGF-------------------KGADQQKPSK 441
Cdd:PRK10982 314 ---NHNANEAInhgfalvtEERRSTGIyAYLDIGFNSLISniRNYKNKVGLldnsrmksdtqwvidsmrvKTPGHRTQIG 390
|
490 500 510
....*....|....*....|....*....|....
gi 512463837 442 VLSGGERNRLNLALTLKQGGNLILLDEPTNDLDV 475
Cdd:PRK10982 391 SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDV 424
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
21-90 |
6.26e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 41.73 E-value: 6.26e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 21 LDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEafLEPGATVGILLQEPPLNEEKTVRGNVE 90
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGK--VDRNGEVSVIAISAGLSGQLTGIENIE 107
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
321-497 |
6.30e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 42.61 E-value: 6.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 321 VVEVKDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLeQPD---SGEVKV-GQTVQLSYV-DQGREN 395
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFeGEELQASNIrDTERAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 396 ID---------PEKTVWEVVSDG--------LDYivvgqNEMPSRAY--LSAFGFkGADQQKPSKVLSGGERNRLNLALT 456
Cdd:PRK13549 84 IAiihqelalvKELSVLENIFLGneitpggiMDY-----DAMYLRAQklLAQLKL-DINPATPVGNLGLGQQQLVEIAKA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 512463837 457 LKQGGNLILLDEPTNDL---DVETLSSLENALQNFPGCAVVISH 497
Cdd:PRK13549 158 LNKQARLLILDEPTASLtesETAVLLDIIRDLKAHGIACIYISH 201
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
20-89 |
6.57e-04 |
|
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: 41.30 E-value: 6.57e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 512463837 20 ILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEPgaTVGILLQEPPL-NEekTVRGNV 89
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--SIAYVSQEPWIqNG--TIRENI 86
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
339-378 |
7.06e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 41.01 E-value: 7.06e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 512463837 339 DLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEV 378
Cdd:PRK13541 18 DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNI 57
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
337-498 |
7.81e-04 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 41.94 E-value: 7.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 337 IKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGE-----VKVGQTVQLSYVDQGRENID---------PEKTV 402
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQvlidgVDIAKISDAELREVRRKKIAmvfqsfalmPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 403 WEVVSDGLDYIVVGQNEMPSRAY--LSAFGFKGADQQKPSKvLSGGERNRLNLALTLKQGGNLILLDEPTNDLDVETLSS 480
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALdaLRQVGLENYAHSYPDE-LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180
....*....|....*....|..
gi 512463837 481 LENALQNFPG----CAVVISHD 498
Cdd:PRK10070 203 MQDELVKLQAkhqrTIVFISHD 224
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
409-478 |
8.73e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 42.32 E-value: 8.73e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 512463837 409 GLDYIVVGQnempsraylsafgfkgadqqkPSKVLSGGERNRLNLALTL---KQGGNLILLDEPTNDL---DVETL 478
Cdd:COG0178 814 GLGYIKLGQ---------------------PATTLSGGEAQRVKLASELskrSTGKTLYILDEPTTGLhfhDIRKL 868
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
16-137 |
9.56e-04 |
|
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: 40.69 E-value: 9.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 16 GDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAG------------LDQPSNGEAFLEpgaTVGILLQEPPLNEEK 83
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrktagvitgeilINGRPLDKNFQR---STGYVEQQDVHSPNL 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 512463837 84 TVRGNVE-----EGLGdiFEKKARFeAIAEEMATNYTDELMEE--MGklqeeLDAADAWEL 137
Cdd:cd03232 95 TVREALRfsallRGLS--VEQRKRL-TIGVELAAKPSILFLDEptSG-----LDSQAAYNI 147
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-191 |
1.08e-03 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 41.73 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 1 MGEFIYQMKNVRKAHGD---KVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLdqpsngeaflEPGATVG-ILLQE 76
Cdd:TIGR02633 253 IGDVILEARNLTCWDVInphRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGA----------YPGKFEGnVFING 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 77 PPLNEeKTVRGNVEEGLGDIFEKKARfEAIAEEMAT--NYTDELMEEMGKLQEELDAADAWELDSKIEQAmdALRCPPAD 154
Cdd:TIGR02633 323 KPVDI-RNPAQAIRAGIAMVPEDRKR-HGIVPILGVgkNITLSVLKSFCFKMRIDAAAELQIIGSAIQRL--KVKTASPF 398
|
170 180 190
....*....|....*....|....*....|....*..
gi 512463837 155 EPVTHLSGGERRRVALAKLLLSEPDLLLLDEPTNHLD 191
Cdd:TIGR02633 399 LPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-234 |
1.13e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 40.98 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 3 EFIYQMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQpSNGEAFLEPGATV-GILLQEPPLNE 81
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLE-LNEEARVEGEVRLfGRNIYSPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 82 EKtvrgnVEEGLGDIFEKKARFE--AIAEEMATNYTdelMEEMGKLQEELDAADAWELDSKI--EQAMDALRCPPADepv 157
Cdd:PRK14267 81 IE-----VRREVGMVFQYPNPFPhlTIYDNVAIGVK---LNGLVKSKKELDERVEWALKKAAlwDEVKDRLNDYPSN--- 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 512463837 158 thLSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAESVLWLEQHL--AKYPGAVLAVTHDRYFLDHVAGWICEVDRGKL 234
Cdd:PRK14267 150 --LSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLfeLKKEYTIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-223 |
1.28e-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: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 12 RKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLdQPSNGEAFLEpGATVG---------------ILLQE 76
Cdd:COG4172 293 RRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFD-GQDLDglsrralrplrrrmqVVFQD 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 77 P--PLNEEKTVRGNVEEGL---GDIFEKKARFEAIAEematnytdeLMEEMGklqeeLDAADAWeldskieqamdalRCP 151
Cdd:COG4172 371 PfgSLSPRMTVGQIIAEGLrvhGPGLSAAERRARVAE---------ALEEVG-----LDPAARH-------------RYP 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 152 padepvtH-LSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAeSV----LWLEQHL-AKYPGAVLAVTHD----RYFLDH 221
Cdd:COG4172 424 -------HeFSGGQRQRIAIARALILEPKLLVLDEPTSALDV-SVqaqiLDLLRDLqREHGLAYLFISHDlavvRALAHR 495
|
..
gi 512463837 222 VA 223
Cdd:COG4172 496 VM 497
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-61 |
1.35e-03 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 40.94 E-value: 1.35e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 512463837 7 QMKNVRK----AHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGE 61
Cdd:PRK11153 3 ELKNISKvfpqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGR 61
|
|
| DotB_TraJ |
cd19516 |
dot/icm secretion system protein DotB-like; Defect in organelle trafficking (Dot)B is part of ... |
344-376 |
1.38e-03 |
|
dot/icm secretion system protein DotB-like; Defect in organelle trafficking (Dot)B is part of the type IVb secretion (T4bS) system, also known as the dot/icm system, and is the main energy supplier of the secretion system. It is an ATPase, similar to the VirB11 component of the T4aS systems. This family also includes Escherichia coli IncI plasmid-encoded conjugative transfer ATPase TraJ encoded on the tra (transfer) operon.
Pssm-ID: 410924 [Multi-domain] Cd Length: 179 Bit Score: 40.05 E-value: 1.38e-03
10 20 30
....*....|....*....|....*....|....*
gi 512463837 344 LPRNGIVGVIGPNGVGKSTLFKTIVG--LEQPDSG 376
Cdd:cd19516 8 FPREGLVYVAGATGSGKSTLLAAIYRyiLENDPPD 42
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
336-487 |
1.44e-03 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 41.57 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 336 LIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDsgeVKVGQTVQL--------------SYVDQGRENIdPEKT 401
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKG---VKGSGSVLLngmpidakemraisAYVQQDDLFI-PTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 402 VWEvvsdglDYIVVGQNEMPSRAY-----------LSAFGFKGADQQK-----PSKVLSGGERNRLNLALTLKQGGNLIL 465
Cdd:TIGR00955 116 VRE------HLMFQAHLRMPRRVTkkekrervdevLQALGLRKCANTRigvpgRVKGLSGGERKRLAFASELLTDPPLLF 189
|
170 180
....*....|....*....|..
gi 512463837 466 LDEPTNDLDVETLSSLENALQN 487
Cdd:TIGR00955 190 CDEPTSGLDSFMAYSVVQVLKG 211
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
5-53 |
1.53e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 40.40 E-value: 1.53e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 512463837 5 IYQMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAG 53
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG 55
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
22-65 |
1.67e-03 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 40.36 E-value: 1.67e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 512463837 22 DNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLE 65
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLR 65
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-99 |
1.68e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 39.28 E-value: 1.68e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 512463837 30 PGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFL---EPGATVGILLQEPPLNEEKTVRGNVEEGLGDIFEK 99
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYidgEDILEEVLDQLLLIIVGGKKASGSGELRLRLALAL 73
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
4-65 |
1.89e-03 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 40.16 E-value: 1.89e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 512463837 4 FIYQMKNVRKAHGDKVilDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLE 65
Cdd:PRK15112 14 FRYRTGWFRRQTVEAV--KPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLID 73
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
322-390 |
2.33e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.17 E-value: 2.33e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 512463837 322 VEVKDLEKGFDGRV---LIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKVGQTVQLSYVD 390
Cdd:PTZ00265 383 IQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDIN 454
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-191 |
2.72e-03 |
|
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: 40.66 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 2 GEFIYQMKNVRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLdQPSNGEAFLEpgatvGILLQEPPLNE 81
Cdd:TIGR01271 1216 GQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQID-----GVSWNSVTLQT 1289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 82 EKTVRGNVEEglgDIFEKKARFEAIAEEMAtNYTDElmeEMGKLQEELDaadaweLDSKIEQAMDALRCPPADEPVThLS 161
Cdd:TIGR01271 1290 WRKAFGVIPQ---KVFIFSGTFRKNLDPYE-QWSDE---EIWKVAEEVG------LKSVIEQFPDKLDFVLVDGGYV-LS 1355
|
170 180 190
....*....|....*....|....*....|
gi 512463837 162 GGERRRVALAKLLLSEPDLLLLDEPTNHLD 191
Cdd:TIGR01271 1356 NGHKQLMCLARSILSKAKILLLDEPSAHLD 1385
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
28-61 |
2.80e-03 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 39.09 E-value: 2.80e-03
10 20 30
....*....|....*....|....*....|....
gi 512463837 28 FYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGE 61
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDN 55
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
409-497 |
3.06e-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: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 409 GLDYIVVGQnempsraylsafgfkgadqqkPSKVLSGGERNRLNLALTLKQ---GGNLILLDEPTNDLDVETLSSLENAL 485
Cdd:TIGR00630 817 GLGYIRLGQ---------------------PATTLSGGEAQRIKLAKELSKrstGRTLYILDEPTTGLHFDDIKKLLEVL 875
|
90
....*....|....*
gi 512463837 486 QNFPG---CAVVISH 497
Cdd:TIGR00630 876 QRLVDkgnTVVVIEH 890
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
350-474 |
3.23e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 40.53 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 350 VGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTV----------QLSYVDQG--------RENIDP--EKT---VW-- 403
Cdd:PTZ00243 1339 VGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVnGREIgayglrelrrQFSMIPQDpvlfdgtvRQNVDPflEASsaeVWaa 1418
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 512463837 404 -EVVsdGLDYIVVGQNEmpsraylsafgfkGADqqkpSKVLSG------GERNRLNLALT-LKQGGNLILLDEPTNDLD 474
Cdd:PTZ00243 1419 lELV--GLRERVASESE-------------GID----SRVLEGgsnysvGQRQLMCMARAlLKKGSGFILMDEATANID 1478
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
325-497 |
3.48e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.10 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 325 KDLEKGFDGRVLIKDLSFTLPRNGIVGVIGPNGVGKSTLFKTIVGLEQPDSGEVKV-GQTVQLSYVDQGRE--------- 394
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFqGKEIDFKSSKEALEngismvhqe 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 395 -NIDPEKTVWEVVSDG---LDYIVVGQNEMpSRAYLSAFGFKGADQQKPSKV--LSGGERNRLNLALTLKQGGNLILLDE 468
Cdd:PRK10982 82 lNLVLQRSVMDNMWLGrypTKGMFVDQDKM-YRDTKAIFDELDIDIDPRAKVatLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190
....*....|....*....|....*....|...
gi 512463837 469 PTNDL---DVETLSSLENALQNfPGCAVV-ISH 497
Cdd:PRK10982 161 PTSSLtekEVNHLFTIIRKLKE-RGCGIVyISH 192
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-215 |
3.80e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 39.38 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 3 EFIYQMKNVRKAHGDKVILDNVTMAFyPGAKI-GVVGPNGAGKSSILKIMAGLDQpsngeafLEPGATV--GILLQEPPL 79
Cdd:PRK14243 8 ETVLRTENLNVYYGSFLAVKNVWLDI-PKNQItAFIGPSGCGKSTILRCFNRLND-------LIPGFRVegKVTFHGKNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 80 NEEKTVRGNVEEGLGDIFEK-----KARFEAIAEEMATNYTDELMEEMgkLQEELDAADAW-ELDSKIEQAMDALrcppa 153
Cdd:PRK14243 80 YAPDVDPVEVRRRIGMVFQKpnpfpKSIYDNIAYGARINGYKGDMDEL--VERSLRQAALWdEVKDKLKQSGLSL----- 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 512463837 154 depvthlSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAESVLWLEQ--HLAKYPGAVLAVTHD 215
Cdd:PRK14243 153 -------SGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEElmHELKEQYTIIIVTHN 209
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
21-232 |
3.86e-03 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 38.85 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 21 LDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAF------LEPGA---------TVGILLQEPPLneektV 85
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnkneSEPSFeatrsrnrySVAYAAQKPWL-----L 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 86 RGNVEEGL--GDIFEKKaRFEAIAEEMAtnytdelmeemgkLQEELDA---ADAWELDskieqamdalrcppadEPVTHL 160
Cdd:cd03290 92 NATVEENItfGSPFNKQ-RYKAVTDACS-------------LQPDIDLlpfGDQTEIG----------------ERGINL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 161 SGGERRRVALAKLLLSEPDLLLLDEP--------TNHLDAESVLWLEQHLAKypgAVLAVTHDRYFLDHvAGWICEVDRG 232
Cdd:cd03290 142 SGGQRQRICVARALYQNTNIVFLDDPfsaldihlSDHLMQEGILKFLQDDKR---TLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
13-48 |
4.40e-03 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 38.60 E-value: 4.40e-03
10 20 30
....*....|....*....|....*....|....*.
gi 512463837 13 KAHGDKVILDNVTMAFYPGAkIGVVGPNGAGKSSIL 48
Cdd:cd03278 5 ELKGFKSFADKTTIPFPPGL-TAIVGPNGSGKSNII 39
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
330-364 |
5.80e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 35.27 E-value: 5.80e-03
10 20 30
....*....|....*....|....*....|....*
gi 512463837 330 GFDGRVlikdlsFTLPRNGIVGVIGPNGVGKSTLF 364
Cdd:pfam13555 11 TFDGHT------IPIDPRGNTLLTGPSGSGKSTLL 39
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
21-215 |
6.05e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 38.92 E-value: 6.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 21 LDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNG-----------EAFLEPGATVGILLQEPplnEEKTVRGNV 89
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGkvkidgelltaENVWNLRRKIGMVFQNP---DNQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 90 EEGLGDIFEKkarfEAIAEEmatnytdelmEEMGKLQEELDAADAWELDSKieqamdalrcppadEPvTHLSGGERRRVA 169
Cdd:PRK13642 100 EDDVAFGMEN----QGIPRE----------EMIKRVDEALLAVNMLDFKTR--------------EP-ARLSGGQKQRVA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 512463837 170 LAKLLLSEPDLLLLDEPTNHLD----AESVLWLEQHLAKYPGAVLAVTHD 215
Cdd:PRK13642 151 VAGIIALRPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQLTVLSITHD 200
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-269 |
7.88e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 39.19 E-value: 7.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 17 DKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEPGaTVGILLQEPPLNEeKTVRGNVEegLGDI 96
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRG-SVAYVPQVSWIFN-ATVRENIL--FGSD 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 97 FEKKARFEAIaeematnytdelmeEMGKLQEELDAADAWELDSKIEQAMDalrcppadepvthLSGGERRRVALAKLLLS 176
Cdd:PLN03232 705 FESERYWRAI--------------DVTALQHDLDLLPGRDLTEIGERGVN-------------ISGGQKQRVSMARAVYS 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 177 EPDLLLLDEPTNHLDAESVLWL----EQHLAKYPGAVLaVTHDRYFLDHVAGWICeVDRGkLYPYEGNY-----STYLEK 247
Cdd:PLN03232 758 NSDIYIFDDPLSALDAHVAHQVfdscMKDELKGKTRVL-VTNQLHFLPLMDRIIL-VSEG-MIKEEGTFaelskSGSLFK 834
|
250 260
....*....|....*....|..
gi 512463837 248 KAerLEVAGKKDAKLQKRLKDE 269
Cdd:PLN03232 835 KL--MENAGKMDATQEVNTNDE 854
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
160-238 |
8.53e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 38.68 E-value: 8.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 160 LSGGERRRVALAKLLLSEPDLLLLDEPTNHLDAESvlwlEQHL------AKYPG-AVLAVTHDRYFLDHVAGWICEVDRG 232
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKG----EHEMmqlildAKANNkTVFVITHTMEHVLEVADEVIVMDKG 252
|
90
....*....|
gi 512463837 233 KLY----PYE 238
Cdd:PRK13631 253 KILktgtPYE 262
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
11-215 |
8.86e-03 |
|
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: 38.39 E-value: 8.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 11 VRKAHGDKVILDNVTMAFYPGAKIGVVGPNGAGKSSILKIMAGLDQPSNGEAFLEPGA---------------TVGILLQ 75
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDiaamsrkelrelrrkKISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512463837 76 EPPLNEEKTVRGNVEEGLgdifEKKARFEAIAEEMATnytdELMEEMGklqeeldaADAWElDSKIEQamdalrcppade 155
Cdd:cd03294 110 SFALLPHRTVLENVAFGL----EVQGVPRAEREERAA----EALELVG--------LEGWE-HKYPDE------------ 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 512463837 156 pvthLSGGERRRVALAKLLLSEPDLLLLDEPTNHLD-------AESVLWLEqhlAKYPGAVLAVTHD 215
Cdd:cd03294 161 ----LSGGMQQRVGLARALAVDPDILLMDEAFSALDplirremQDELLRLQ---AELQKTIVFITHD 220
|
|
| |
