|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-526 |
0e+00 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 650.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 6 VENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKMAIEYLSQNPEFDPNATILE 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 86 QVFKSDSQIMNVIRDYENILEEISQNPDDstlQKKLLYLTDNMNAQDAWEIENQVKTILTKLGIHN--FHQKIETLSGGQ 163
Cdd:COG0488 81 TVLDGDAELRALEAELEELEAKLAEPDED---LERLAELQEEFEALGGWEAEARAEEILSGLGFPEedLDRPVSELSGGW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 164 KKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYLTNRTGSLLMITHDRYFLDRVVNKTLELDDGKIYSYIGNYSQF 243
Cdd:COG0488 158 RRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 244 IEKKLERKTLESSIERKRERLYKKELEWI-RAGAQAR-STKQKARIQRFEELKNTSSPIHDSNIDICV-AHSRLGQKIIE 320
Cdd:COG0488 238 LEQRAERLEQEAAAYAKQQKKIAKEEEFIrRFRAKARkAKQAQSRIKALEKLEREEPPRRDKTVEIRFpPPERLGKKVLE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 321 INHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIGPTVKIGYFSQESEDMDINLRAI 400
Cdd:COG0488 318 LEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEELDPDKTVL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 401 EYIKEKAeyittEDGIKISASQMMENFLFSKDLQWTYISKLSGGERRRLYLLRILMDAPNVLILDEPTNDLDIDTLKVLE 480
Cdd:COG0488 398 DELRDGA-----PGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALE 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 928932812 481 NYIDDFNGIVICVSHDRYFLDRICNKIFFFAgDGKIIEHTGNYSDF 526
Cdd:COG0488 473 EALDDFPGTVLLVSHDRYFLDRVATRILEFE-DGGVREYPGGYDDY 517
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-556 |
1.75e-154 |
|
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: 456.32 E-value: 1.75e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISKSY-GEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKMAIEYLSQNPEFDPNA 81
Cdd:TIGR03719 4 IYTMNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQLDPTK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 82 TILEQVFKSDSQIMNVIRDYENILEEISQNPDD-STLQKKLLYLTDNMNAQDAWEIENQVKTILTKLGIHNFHQKIETLS 160
Cdd:TIGR03719 84 TVRENVEEGVAEIKDALDRFNEISAKYAEPDADfDKLAAEQAELQEIIDAADAWDLDSQLEIAMDALRCPPWDADVTKLS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 161 GGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYLTNRTGSLLMITHDRYFLDRVVNKTLELDDGKIYSYIGNY 240
Cdd:TIGR03719 164 GGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 241 SQFIEKKLERKTLESSIERKRERLYKKELEWIRAGAQARSTKQKARIQRFEEL--KNTSSPIHDSNIDICVAhSRLGQKI 318
Cdd:TIGR03719 244 SSWLEQKQKRLEQEEKEESARQKTLKRELEWVRQSPKGRQAKSKARLARYEELlsQEFQKRNETAEIYIPPG-PRLGDKV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIGPTVKIGYFSQESEDMDINLR 398
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRDALDPNKT 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 399 AIEYIKEKAEYITTeDGIKISASQMMENFLFSKDLQWTYISKLSGGERRRLYLLRILMDAPNVLILDEPTNDLDIDTLKV 478
Cdd:TIGR03719 403 VWEEISGGLDIIKL-GKREIPSRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRA 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 928932812 479 LENYIDDFNGIVICVSHDRYFLDRICNKIFFFAGDGKIIEHTGNYSDFyksgrwiHEEIKEEKNTKKSAPQKPKEKKL 556
Cdd:TIGR03719 482 LEEALLNFAGCAVVISHDRWFLDRIATHILAFEGDSHVEWFEGNFSEY-------EEDKKRRLGEDADQPHRIKYKKL 552
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-556 |
1.80e-146 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 435.70 E-value: 1.80e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISKSYG-EKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKMAIEYLSQNPEFDPNA 81
Cdd:PRK11819 6 IYTMNRVSKVVPpKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEPQLDPEK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 82 TILEQVFKSDSQIMNVIRDYENILEEISQNPDDS-TLQKKLLYLTDNMNAQDAWEIENQVKTILTKLGIHNFHQKIETLS 160
Cdd:PRK11819 86 TVRENVEEGVAEVKAALDRFNEIYAAYAEPDADFdALAAEQGELQEIIDAADAWDLDSQLEIAMDALRCPPWDAKVTKLS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 161 GGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYLTNRTGSLLMITHDRYFLDRVVNKTLELDDGKIYSYIGNY 240
Cdd:PRK11819 166 GGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 241 SQFIEKKLERKTLESSIERKRERLYKKELEWIRAGAQARSTKQKARIQRFEELKNTSSP--IHDSNIDICVAhSRLGQKI 318
Cdd:PRK11819 246 SSWLEQKAKRLAQEEKQEAARQKALKRELEWVRQSPKARQAKSKARLARYEELLSEEYQkrNETNEIFIPPG-PRLGDKV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIGPTVKIGYFSQESEDMDINLR 398
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQSRDALDPNKT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 399 AIEYIKEKAEYITTeDGIKISASQMMENFLFSKDLQWTYISKLSGGERRRLYLLRILMDAPNVLILDEPTNDLDIDTLKV 478
Cdd:PRK11819 405 VWEEISGGLDIIKV-GNREIPSRAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRA 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 928932812 479 LENYIDDFNGIVICVSHDRYFLDRICNKIFFFAGDGKIIEHTGNYSDFyksgrwihEEIKEEKNTKKSA-PQKPKEKKL 556
Cdd:PRK11819 484 LEEALLEFPGCAVVISHDRWFLDRIATHILAFEGDSQVEWFEGNFQEY--------EEDKKRRLGADAArPHRIKYKKL 554
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-631 |
5.65e-123 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 378.14 E-value: 5.65e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 1 MNILSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKMAIEYLSQNPEFDPN 80
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPRNVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 81 ATILEQVFKSDSQIMNVIRDYENILEEISQNPDDSTLqKKLLYLTDNMNAQDAWEIENQVKTILTKLGIhNFHQKIETLS 160
Cdd:PRK11147 81 GTVYDFVAEGIEEQAEYLKRYHDISHLVETDPSEKNL-NELAKLQEQLDHHNLWQLENRINEVLAQLGL-DPDAALSSLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 161 GGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYLTNRTGSLLMITHDRYFLDRVVNKTLELDDGKIYSYIGNY 240
Cdd:PRK11147 159 GGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 241 SQFIEKKLERKTLEssiERKRERLYKK---ELEWIRAGAQARSTKQKARIQRFEELKNTSSPIHD--SNIDICVAH-SRL 314
Cdd:PRK11147 239 DQYLLEKEEALRVE---ELQNAEFDRKlaqEEVWIRQGIKARRTRNEGRVRALKALRRERSERREvmGTAKMQVEEaSRS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 315 GQKIIEINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIGPTVKIGYFSQESEDMD 394
Cdd:PRK11147 316 GKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRAELD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 395 INLRAIEYIKEKAEYITTeDGIKISASQMMENFLFSKDLQWTYISKLSGGERRRLYLLRILMDAPNVLILDEPTNDLDID 474
Cdd:PRK11147 396 PEKTVMDNLAEGKQEVMV-NGRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVE 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 475 TLKVLENYIDDFNGIVICVSHDRYFLDRICNKIFFFAGDGKIIEHTGNYSDF------YKSGRWIHEEIKEEKNTKKSAP 548
Cdd:PRK11147 475 TLELLEELLDSYQGTVLLVSHDRQFVDNTVTECWIFEGNGKIGRYVGGYHDArqqqaqYLALKQPAVKKKEEAAAPKAET 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 549 QKPKEKKLkfTYNEQREYETIDQEIENLENKLSTLEEEMKkySTDF---------TKLQELMNEkdyiEEELLLKMERQE 619
Cdd:PRK11147 555 VKRSSKKL--SYKLQRELEQLPQLLEDLEAEIEALQAQVA--DADFfsqpheqtqKVLADLADA----EQELEVAFERWE 626
|
650
....*....|..
gi 928932812 620 YLndlaEKIKND 631
Cdd:PRK11147 627 EL----EALKNG 634
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
14-626 |
5.07e-77 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 257.79 E-value: 5.07e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 14 GEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKMAIEYLSQ-NPEFDPNAtiLEQVFKSDS 92
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQeTPALPQPA--LEYVIDGDR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 93 QImnviRDYENILEEISQNPDD---STLQKKLlyltdnmNAQDAWEIENQVKTILTKLGIHN--FHQKIETLSGGQKKRV 167
Cdd:PRK10636 90 EY----RQLEAQLHDANERNDGhaiATIHGKL-------DAIDAWTIRSRAASLLHGLGFSNeqLERPVSDFSGGWRMRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 168 ALASALISPCDLLILDEPTNHMDHDTIDWLEKYLTNRTGSLLMITHDRYFLDRVVNKTLELDDGKIYSYIGNYSQFIEKK 247
Cdd:PRK10636 159 NLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 248 LERKTLESSI-ERKRERLYKKELEWIRAGAQARSTKQ-KARIQRFEELK-----NTSSPIHDSnidiCVAHSRLGQKIIE 320
Cdd:PRK10636 239 ATRLAQQQAMyESQQERVAHLQSYIDRFRAKATKAKQaQSRIKMLERMEliapaHVDNPFHFS----FRAPESLPNPLLK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 321 INHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIGPTVKIGYFSQESEDMdinLRAI 400
Cdd:PRK10636 315 MEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEF---LRAD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 401 EYIKEKAEYITTEDgikisASQMMENFL----FSKDLQWTYISKLSGGERRRLYLLRILMDAPNVLILDEPTNDLDIDTL 476
Cdd:PRK10636 392 ESPLQHLARLAPQE-----LEQKLRDYLggfgFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMR 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 477 KVLENYIDDFNGIVICVSHDRYFLdRICNKIFFFAGDGKIIEHTGNYSDFYksgRWIHEEIKEE--------KNTKKSAP 548
Cdd:PRK10636 467 QALTEALIDFEGALVVVSHDRHLL-RSTTDDLYLVHDGKVEPFDGDLEDYQ---QWLSDVQKQEnqtdeapkENNANSAQ 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 549 QKPKEKKLKFTYNEQ-----REYETIDQEIENLENKLSTLEEEM-------KKYSTDFTK-LQELMNEKDYIEEELLLKM 615
Cdd:PRK10636 543 ARKDQKRREAELRTQtqplrKEIARLEKEMEKLNAQLAQAEEKLgdselydQSRKAELTAcLQQQASAKSGLEECEMAWL 622
|
650
....*....|.
gi 928932812 616 ERQEYLNDLAE 626
Cdd:PRK10636 623 EAQEQLEQMLL 633
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-529 |
1.06e-74 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 248.65 E-value: 1.06e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKMAIEYLSQNPEFDPNAT 82
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFEEFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 83 ILEQVFKSDSQIMNVI--RDyenileEISQNPDDSTlqkkllylTDNMNA---------QDAWEIENQVKTILTKLGIH- 150
Cdd:PRK15064 81 VLDTVIMGHTELWEVKqeRD------RIYALPEMSE--------EDGMKVadlevkfaeMDGYTAEARAGELLLGVGIPe 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 151 NFHQ-KIETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYLTNRTGSLLMITHDRYFLDRVVNKTLELD 229
Cdd:PRK15064 147 EQHYgLMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 230 DGKIYSYIGNYSQFIE-KKLERKTLESSIERKRERLykKELEWI--RAGA------QARS-TKQKARIQrFEELKNTS-- 297
Cdd:PRK15064 227 YGELRVYPGNYDEYMTaATQARERLLADNAKKKAQI--AELQSFvsRFSAnaskakQATSrAKQIDKIK-LEEVKPSSrq 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 298 SPIHDSNIDicvahSRLGQKIIEINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDI 377
Cdd:PRK15064 304 NPFIRFEQD-----KKLHRNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 378 GPTVKIGYFSQESE---DMDINLraIEYIkekAEYITTEDGIKISASqMMENFLFSKDLQWTYISKLSGGERRRLYLLRI 454
Cdd:PRK15064 379 SENANIGYYAQDHAydfENDLTL--FDWM---SQWRQEGDDEQAVRG-TLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKL 452
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 928932812 455 LMDAPNVLILDEPTNDLDIDTLKVLENYIDDFNGIVICVSHDRYFLDRICNKIFFFAGDGkIIEHTGNYSDFYKS 529
Cdd:PRK15064 453 MMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDG-VVDFSGTYEEYLRS 526
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-246 |
9.92e-63 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 216.47 E-value: 9.92e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKMAIEYLSQNPE-FDPNA 81
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEeLDPDK 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 82 TILEqvfksdsqimnVIRDYenileeisqNPDDStlqkkllyltdnmnaqdaweiENQVKTILTKLGihnF-----HQKI 156
Cdd:COG0488 395 TVLD-----------ELRDG---------APGGT---------------------EQEVRGYLGRFL---FsgddaFKPV 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 157 ETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYLTNRTGSLLMITHDRYFLDRVVNKTLELDDGKIYSY 236
Cdd:COG0488 431 GVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREY 510
|
250
....*....|
gi 928932812 237 IGNYSQFIEK 246
Cdd:COG0488 511 PGGYDDYLEK 520
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
6-528 |
5.98e-49 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 181.98 E-value: 5.98e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 6 VENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADtgkvhMPSKMAIEYLSQNPEFDpNATILE 85
Cdd:PLN03073 180 MENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMHAIDG-----IPKNCQILHVEQEVVGD-DTTALQ 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 86 QVFKSDSQIMNVIRDYENILEE-----------ISQNPDDSTLQK-----KLLYLTDNMNAQDAWEIENQVKTILTKLGI 149
Cdd:PLN03073 254 CVLNTDIERTQLLEEEAQLVAQqrelefetetgKGKGANKDGVDKdavsqRLEEIYKRLELIDAYTAEARAASILAGLSF 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 150 --HNFHQKIETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYLTNRTGSLLMITHDRYFLDRVVNKTLE 227
Cdd:PLN03073 334 tpEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILH 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 228 LDDGKIYSYIGNYSQFIEKKLER-----KTLESSiERKRERLyKKELEWIRAGAQaRSTKQKARIQRFEELKNTSSPIHD 302
Cdd:PLN03073 414 LHGQKLVTYKGDYDTFERTREEQlknqqKAFESN-ERSRSHM-QAFIDKFRYNAK-RASLVQSRIKALDRLGHVDAVVND 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 303 SN--IDICVAHSRLGQKIIEINHISKSFEQNKVI-EDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIGP 379
Cdd:PLN03073 491 PDykFEFPTPDDRPGPPIISFSDASFGYPGGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSA 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 380 TVKIGYFSQESED-MDINLRAIEYIKEKAEYITTEdgiKISASqmMENFLFSKDLQWTYISKLSGGERRRLYLLRILMDA 458
Cdd:PLN03073 571 KVRMAVFSQHHVDgLDLSSNPLLYMMRCFPGVPEQ---KLRAH--LGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKK 645
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 459 PNVLILDEPTNDLDIDTLKVLENYIDDFNGIVICVSHDRYFLDRICNKIFFFAgDGKIIEHTGNYSDFYK 528
Cdd:PLN03073 646 PHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVS-EGKVTPFHGTFHDYKK 714
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
319-514 |
2.20e-48 |
|
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: 165.70 E-value: 2.20e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIGPTVKIGYFSQesedmdinlr 398
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 399 aieyikekaeyittedgikisasqmmenflfskdlqwtyiskLSGGERRRLYLLRILMDAPNVLILDEPTNDLDIDTLKV 478
Cdd:cd03221 71 ------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEA 108
|
170 180 190
....*....|....*....|....*....|....*.
gi 928932812 479 LENYIDDFNGIVICVSHDRYFLDRICNKIFFFAGDG 514
Cdd:cd03221 109 LEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
321-577 |
1.00e-47 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 175.25 E-value: 1.00e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 321 INHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIGPTVKIGYFSQE---SEDMDI-- 395
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEpplDDDLTVld 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 396 -------NLRAIEYIKEKAE---YITTEDGIKIS-----------------ASQMMENFLFSKDLQWTYISKLSGGERrr 448
Cdd:COG0488 81 tvldgdaELRALEAELEELEaklAEPDEDLERLAelqeefealggweaearAEEILSGLGFPEEDLDRPVSELSGGWR-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 449 lyllrilM---------DAPNVLILDEPTNDLDIDTLKVLENYIDDFNGIVICVSHDRYFLDRICNKIFFFAgDGKIIEH 519
Cdd:COG0488 159 -------RrvalarallSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELD-RGKLTLY 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 928932812 520 TGNYSDFYKSgrwiheeikeekntkksapqkpKEKKLKftyNEQREYETIDQEIENLE 577
Cdd:COG0488 231 PGNYSAYLEQ----------------------RAERLE---QEAAAYAKQQKKIAKEE 263
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-232 |
1.53e-46 |
|
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: 160.69 E-value: 1.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKMAIEYLSQnpefdpnati 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 84 leqvfksdsqimnvirdyenileeisqnpddstlqkkllyltdnmnaqdaweienqvktiltklgihnfhqkietLSGGQ 163
Cdd:cd03221 71 ---------------------------------------------------------------------------LSGGE 75
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 928932812 164 KKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYLTNRTGSLLMITHDRYFLDRVVNKTLELDDGK 232
Cdd:cd03221 76 KMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-232 |
1.74e-37 |
|
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: 138.37 E-value: 1.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 5 SVENISKSY--GEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKmAIEYLS---------- 72
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGK-DLTKLSlkelrrkvgl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 73 --QNPefdpnatileqvfksDSQIMNvirdyENILEEISQNPddstlqkKLLYLTDNmnaqdawEIENQVKTILTKLGIH 150
Cdd:cd03225 80 vfQNP---------------DDQFFG-----PTVEEEVAFGL-------ENLGLPEE-------EIEERVEEALELVGLE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 151 NF-HQKIETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYLT--NRTG-SLLMITHDRYFLDRVVNKTL 226
Cdd:cd03225 126 GLrDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKklKAEGkTIIIVTHDLDLLLELADRVI 205
|
....*.
gi 928932812 227 ELDDGK 232
Cdd:cd03225 206 VLEDGK 211
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-267 |
3.63e-36 |
|
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: 143.15 E-value: 3.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 2 NILSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKMAIEYLSQNPE-FDPN 80
Cdd:TIGR03719 321 KVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRDaLDPN 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 81 ATILEQVfkSDSQIMNVIRDYEnileeisqnpddstlqkkllyltdnMNAQdaweienqvktilTKLGIHNF-----HQK 155
Cdd:TIGR03719 401 KTVWEEI--SGGLDIIKLGKRE-------------------------IPSR-------------AYVGRFNFkgsdqQKK 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 156 IETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYLTNRTGSLLMITHDRYFLDRVVNKTLELD-DGKIY 234
Cdd:TIGR03719 441 VGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEgDSHVE 520
|
250 260 270
....*....|....*....|....*....|...
gi 928932812 235 SYIGNYSQFIEKKLERKTlESSIERKRERlYKK 267
Cdd:TIGR03719 521 WFEGNFSEYEEDKKRRLG-EDADQPHRIK-YKK 551
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-232 |
1.61e-35 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 132.99 E-value: 1.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVH------------MPSKMAieYL 71
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLwngepirdaredYRRRLA--YL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 72 SQNPEFDPNATILEQvfksdsqimnvirdyenileeisqnpddstlqkkLLYLTDNMNAQDAweiENQVKTILTKLGIHN 151
Cdd:COG4133 81 GHADGLKPELTVREN----------------------------------LRFWAALYGLRAD---REAIDEALEAVGLAG 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 152 F-HQKIETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYL---TNRTGSLLMITHDRYFLDRVvnKTLE 227
Cdd:COG4133 124 LaDLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIaahLARGGAVLLTTHQPLELAAA--RVLD 201
|
....*
gi 928932812 228 LDDGK 232
Cdd:COG4133 202 LGDFK 206
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-235 |
4.37e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 127.13 E-value: 4.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 1 MNILSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKMA------IEYLSQN 74
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPrrarrrIGYVPQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 75 PEFDPN--ATILEQVfksdsqIMNVIRdyenileeisqnpddstlQKKLLYLtdnMNAQDaWEIenqVKTILTKLGIHNF 152
Cdd:COG1121 84 AEVDWDfpITVRDVV------LMGRYG------------------RRGLFRR---PSRAD-REA---VDEALERVGLEDL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 153 -HQKIETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYLT--NRTG-SLLMITHDRYFLDRVVNKTLEL 228
Cdd:COG1121 133 aDRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRelRREGkTILVVTHDLGAVREYFDRVLLL 212
|
....*..
gi 928932812 229 DDGKIYS 235
Cdd:COG1121 213 NRGLVAH 219
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-267 |
5.32e-32 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 130.62 E-value: 5.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 2 NILSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKMAIEYLSQNPE-FDPN 80
Cdd:PRK11819 323 KVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQSRDaLDPN 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 81 ATILEQVfkSDSQIMNVIRDYEnileeisqnpddstlqkkllyltdnMNAQdAWeienqvktiltkLGIHNF-----HQK 155
Cdd:PRK11819 403 KTVWEEI--SGGLDIIKVGNRE-------------------------IPSR-AY------------VGRFNFkggdqQKK 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 156 IETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYLTNRTGSLLMITHDRYFLDRVVNKTL--ElDDGKI 233
Cdd:PRK11819 443 VGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHILafE-GDSQV 521
|
250 260 270
....*....|....*....|....*....|....
gi 928932812 234 YSYIGNYSQFIEKKLERKTlESSIERKRERlYKK 267
Cdd:PRK11819 522 EWFEGNFQEYEEDKKRRLG-ADAARPHRIK-YKK 553
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-233 |
7.27e-32 |
|
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: 123.21 E-value: 7.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSY-GEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHM----PSKMAIEYLS------ 72
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVdgkdITKKNLRELRrkvglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 73 -QNPefdpnatileqvfksDSQIMNvirdyENILEEISQNPddstLQKKLlyltdnmnaqDAWEIENQVKTILTKLGIHN 151
Cdd:COG1122 81 fQNP---------------DDQLFA-----PTVEEDVAFGP----ENLGL----------PREEIRERVEEALELVGLEH 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 152 FHQK-IETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYLT--NRTG-SLLMITHDRYFLDRVVNKTLE 227
Cdd:COG1122 127 LADRpPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKrlNKEGkTVIIVTHDLDLVAELADRVIV 206
|
....*.
gi 928932812 228 LDDGKI 233
Cdd:COG1122 207 LDDGRI 212
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-236 |
2.57e-31 |
|
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: 122.46 E-value: 2.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKV--------HMPSK-----MAie 69
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVlldgrdlaSLSRRelarrIA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 70 YLSQNPEFDPNATILEQVfksdsqimnvirdyenileEISQNPDDSTLQKkllyltdnMNAQDaweiENQVKTILTKLGI 149
Cdd:COG1120 79 YVPQEPPAPFGLTVRELV-------------------ALGRYPHLGLFGR--------PSAED----REAVEEALERTGL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 150 HNF-HQKIETLSGGQKKRVALASALISPCDLLILDEPTNHMD----HDTIDWLEKyLTNRTG-SLLMITHD-----RYFl 218
Cdd:COG1120 128 EHLaDRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDlahqLEVLELLRR-LARERGrTVVMVLHDlnlaaRYA- 205
|
250
....*....|....*...
gi 928932812 219 DRVVnktLeLDDGKIYSY 236
Cdd:COG1120 206 DRLV---L-LKDGRIVAQ 219
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-226 |
5.83e-31 |
|
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: 120.33 E-value: 5.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 5 SVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKMA------IEYLSQNPEFD 78
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLekerkrIGYVPQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 79 PN--ATILEQVfksdsqiMNVIRDYENILEEISQnpddstlqkkllyltdnmnaqDAWEIenqVKTILTKLGIHNF-HQK 155
Cdd:cd03235 81 RDfpISVRDVV-------LMGLYGHKGLFRRLSK---------------------ADKAK---VDEALERVGLSELaDRQ 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 156 IETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDT----IDWLEKYltNRTG-SLLMITHD----RYFLDRVV--NK 224
Cdd:cd03235 130 IGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTqediYELLREL--RREGmTILVVTHDlglvLEYFDRVLllNR 207
|
..
gi 928932812 225 TL 226
Cdd:cd03235 208 TV 209
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-249 |
7.98e-31 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 120.55 E-value: 7.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHM----PSKMAIE------YLSQ 73
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVlgedVARDPAEvrrrigYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 74 NPEFDPNATILEqvfksdsqimnvirdyenileeisqnpddstlqkkLLYLTDNMNAQDAWEIENQVKTILTKLGIHNF- 152
Cdd:COG1131 81 EPALYPDLTVRE-----------------------------------NLRFFARLYGLPRKEARERIDELLELFGLTDAa 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 153 HQKIETLSGGQKKRVALASALISPCDLLILDEPTNHMD----HDTIDWLEKyLTNRTGSLLMITHD----RYFLDRVVnk 224
Cdd:COG1131 126 DRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDpearRELWELLRE-LAAEGKTVLLSTHYleeaERLCDRVA-- 202
|
250 260
....*....|....*....|....*
gi 928932812 225 tlELDDGKIYsYIGNYSQFIEKKLE 249
Cdd:COG1131 203 --IIDKGRIV-ADGTPDELKARLLE 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-519 |
1.70e-30 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 125.79 E-value: 1.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISKSY--GEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGY---DVADTGKVH--------MPSKM--- 66
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLldgrdlleLSEALrgr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 67 AIEYLSQNPE--FDPnATILEQVfksdsqimnvirdyenilEEISQNPDDStlqkkllyltdnmnaqdAWEIENQVKTIL 144
Cdd:COG1123 84 RIGMVFQDPMtqLNP-VTVGDQI------------------AEALENLGLS-----------------RAEARARVLELL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 145 TKLGI-HNFHQKIETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDT---IDWLEKYLTNRTG-SLLMITHDRYFLD 219
Cdd:COG1123 128 EAVGLeRRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTqaeILDLLRELQRERGtTVLLITHDLGVVA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 220 RVVNKTLELDDGKIysyignysqfiekkLERKTLEsSIERKRERLykkelewiragaqarstkqkariqrfeelknTSSP 299
Cdd:COG1123 208 EIADRVVVMDDGRI--------------VEDGPPE-EILAAPQAL-------------------------------AAVP 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 300 IHDSNIDICVAHSRLGQKIIEINHISKSFEQN-----KVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGS 374
Cdd:COG1123 242 RLGAARGRAAPAAAAAEPLLEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGS 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 375 I-----DIGPTV---------KIGYFSQESEDMdIN--LRAIEYIKE--KAEYITTEDGIKISASQMMENFLFSKDLQWT 436
Cdd:COG1123 322 IlfdgkDLTKLSrrslrelrrRVQMVFQDPYSS-LNprMTVGDIIAEplRLHGLLSRAERRERVAELLERVGLPPDLADR 400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 437 YISKLSGG-------------ErrrlyllrilmdaPNVLILDEPTNDLDIDT----LKVLENYIDDFNGIVICVSHDRYF 499
Cdd:COG1123 401 YPHELSGGqrqrvaiaralalE-------------PKLLILDEPTSALDVSVqaqiLNLLRDLQRELGLTYLFISHDLAV 467
|
570 580
....*....|....*....|
gi 928932812 500 LDRICNKIFFFAgDGKIIEH 519
Cdd:COG1123 468 VRYIADRVAVMY-DGRIVED 486
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-233 |
2.28e-28 |
|
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: 112.74 E-value: 2.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 5 SVENISKSYGEKI-LFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHM-----PSKM---AIEYLSQNP 75
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLngkpiKAKErrkSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 76 EFdpnatileQVFkSDSqimnvirdyenILEEisqnpddstlqkklLYLtdnmNAQDAWEIENQVKTILTKLGIHNFHQK 155
Cdd:cd03226 81 DY--------QLF-TDS-----------VREE--------------LLL----GLKELDAGNEQAETVLKDLDLYALKER 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 156 I-ETLSGGQKKRVALASALISPCDLLILDEPTNHMDH---DTIDWLEKYLTNRTGSLLMITHDRYFLDRVVNKTLELDDG 231
Cdd:cd03226 123 HpLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYknmERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
..
gi 928932812 232 KI 233
Cdd:cd03226 203 AI 204
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-233 |
4.83e-28 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 112.20 E-value: 4.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYGE-----KILfENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKV--------HMPSKMAIEY 70
Cdd:cd03255 1 IELKNLSKTYGGggekvQAL-KGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVrvdgtdisKLSEKELAAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 71 LSQNPEFdpnatileqVFksdsQIMNVIRD---YENILeeisqnpddstlqkkllyLTDNMNAQDAWEIENQVKTILTKL 147
Cdd:cd03255 80 RRRHIGF---------VF----QSFNLLPDltaLENVE------------------LPLLLAGVPKKERRERAEELLERV 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 148 GI-HNFHQKIETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDT----IDWLEKYLTNRTGSLLMITHDRYFL---D 219
Cdd:cd03255 129 GLgDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETgkevMELLRELNKEAGTTIVVVTHDPELAeyaD 208
|
250
....*....|....
gi 928932812 220 RVVnktlELDDGKI 233
Cdd:cd03255 209 RII----ELRDGKI 218
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-233 |
5.25e-28 |
|
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: 110.57 E-value: 5.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKV----------HMPSKMAIEYLSQ 73
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIkvlgkdikkePEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 74 NPEFDPNATIleqvfksdsqimnvirdYENIleeisqnpddstlqkkllyltdnmnaqdaweienqvktiltklgihnfh 153
Cdd:cd03230 81 EPSLYENLTV-----------------RENL------------------------------------------------- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 154 qkieTLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKY---LTNRTGSLLMITHDRYFLDRVVNKTLELDD 230
Cdd:cd03230 95 ----KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELlreLKKEGKTILLSSHILEEAERLCDRVAILNN 170
|
...
gi 928932812 231 GKI 233
Cdd:cd03230 171 GRI 173
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-232 |
1.79e-27 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 108.49 E-value: 1.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 5 SVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHmpskmaieylsqnpefdpnatil 84
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 85 eqvfksdsqimnvirdyenILEEISQNPDDSTLQKKLLYLtdnmnaqdaweienqvktiltklgihnfHQkietLSGGQK 164
Cdd:cd00267 58 -------------------IDGKDIAKLPLEELRRRIGYV----------------------------PQ----LSGGQR 86
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 928932812 165 KRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYL-----TNRTgsLLMITHDRYFLDRVVNKTLELDDGK 232
Cdd:cd00267 87 QRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLrelaeEGRT--VIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-236 |
6.73e-27 |
|
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: 107.52 E-value: 6.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 5 SVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMpskmaieylsqnpefdpnatil 84
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILL---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 85 eqvfksDSQIMNVIRDYEnileeisqnpddstLQKKLLYltdnmnaqdaweienqVKTILTKLGIHNF-HQKIETLSGGQ 163
Cdd:cd03214 59 ------DGKDLASLSPKE--------------LARKIAY----------------VPQALELLGLAHLaDRPFNELSGGE 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 164 KKRVALASALISPCDLLILDEPTNHMD----HDTIDWLEKyLTNRTG-SLLMITHD-----RYFlDRVVnktLeLDDGKI 233
Cdd:cd03214 103 RQRVLLARALAQEPPILLLDEPTSHLDiahqIELLELLRR-LARERGkTVVMVLHDlnlaaRYA-DRVI---L-LKDGRI 176
|
...
gi 928932812 234 YSY 236
Cdd:cd03214 177 VAQ 179
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-247 |
1.01e-26 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 114.60 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 2 NILSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKMAIEYLSQNPEFDpna 81
Cdd:PRK15064 318 NALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHAYD--- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 82 tileqvFKSDSQIMNVIRDYenileeiSQNPDDstlqkkllyltdnmnaqdaweiENQVKTILTKL--GIHNFHQKIETL 159
Cdd:PRK15064 395 ------FENDLTLFDWMSQW-------RQEGDD----------------------EQAVRGTLGRLlfSQDDIKKSVKVL 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 160 SGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYLTNRTGSLLMITHDRYFLDRVVNKTLELDDGKIYSYIGN 239
Cdd:PRK15064 440 SGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGT 519
|
....*...
gi 928932812 240 YSQFIEKK 247
Cdd:PRK15064 520 YEEYLRSQ 527
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-233 |
1.49e-26 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 107.83 E-value: 1.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISKSYGEKIL-FENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVH--------MPSKmAIEYLSQ 73
Cdd:COG2884 1 MIRFENVSKRYPGGREaLSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLvngqdlsrLKRR-EIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 74 NpefdpnatiLEQVFKsDSQI---MNVirdYENI---LEEISQNPDdstlqkkllyltdnmnaqdawEIENQVKTILTKL 147
Cdd:COG2884 80 R---------IGVVFQ-DFRLlpdRTV---YENValpLRVTGKSRK---------------------EIRRRVREVLDLV 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 148 GIHNF-HQKIETLSGGQKKRVALASALI-SPcDLLILDEPTNHMDHDTIDWLEKYLT--NRTG-SLLMITHDRYFLDRVV 222
Cdd:COG2884 126 GLSDKaKALPHELSGGEQQRVAIARALVnRP-ELLLADEPTGNLDPETSWEIMELLEeiNRRGtTVLIATHDLELVDRMP 204
|
250
....*....|.
gi 928932812 223 NKTLELDDGKI 233
Cdd:COG2884 205 KRVLELEDGRL 215
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-249 |
2.81e-26 |
|
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: 107.64 E-value: 2.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPS----------KMAIEYLSQ 73
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrkepreaRRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 74 NPEFDPNATIleqvfksdsqimnviRDYENILEEISQNPDDstlqkkllyltdnmnaqdawEIENQVKTILTKLGIHNF- 152
Cdd:COG4555 82 ERGLYDRLTV---------------RENIRYFAELYGLFDE--------------------ELKKRIEELIELLGLEEFl 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 153 HQKIETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYLTNRTGSLLMI---THDRYFLDRVVNKTLELD 229
Cdd:COG4555 127 DRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVlfsSHIMQEVEALCDRVVILH 206
|
250 260
....*....|....*....|
gi 928932812 230 DGKIySYIGNYSQFIEKKLE 249
Cdd:COG4555 207 KGKV-VAQGSLDELREEIGE 225
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-233 |
3.08e-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: 106.83 E-value: 3.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVH---------MPSKMAIEYLSQN 74
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILidgrdvtgvPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 75 PEFDPNatileqvfksdsqiMNVirdYENILeeisqnpddSTLQKKLLyltdnmnaqDAWEIENQVKTILTKLGIHNF-H 153
Cdd:cd03259 81 YALFPH--------------LTV---AENIA---------FGLKLRGV---------PKAEIRARVRELLELVGLEGLlN 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 154 QKIETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYLT---NRTG-SLLMITHDR---YFL-DRVVnkt 225
Cdd:cd03259 126 RYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKelqRELGiTTIYVTHDQeeaLALaDRIA--- 202
|
....*...
gi 928932812 226 lELDDGKI 233
Cdd:cd03259 203 -VMNEGRI 209
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
319-540 |
6.12e-26 |
|
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: 106.87 E-value: 6.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFEQNKVIEDFSYiALKDDRI-GIIGKNGTGKSTLLNLITGKLTPDLGSIDI--------GPTVK--IGYFS 387
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSF-TAKDGEItGLLGPNGAGKTTLLRMLAGLLKPDSGSILIdgedvrkePREARrqIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 388 QESEdMDINLRAIEYIKEKAE-YITTEDGIKISASQMMENFLFSKDLQwTYISKLSGGERRRLYLLRILMDAPNVLILDE 466
Cdd:COG4555 81 DERG-LYDRLTVRENIRYFAElYGLFDEELKKRIEELIELLGLEEFLD-RRVGELSTGMKKKVALARALVHDPKVLLLDE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 928932812 467 PTNDLDIDT----LKVLENYIDDfNGIVICVSHDRYFLDRICNKIFFFAgDGKIIEHtGNYSDFYKSGRwiHEEIKEE 540
Cdd:COG4555 159 PTNGLDVMArrllREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILH-KGKVVAQ-GSLDELREEIG--EENLEDA 231
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-233 |
2.42e-25 |
|
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: 104.51 E-value: 2.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISKSYGEKILF----ENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKV--------HMPSKM---- 66
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSvkalDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIifdgkdllKLSRRLrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 67 --AIEYLSQNP--EFDPNATILEQVfksdsqimnvirdyENILEEISQNPDDSTLQKKLLYLTDNMNaqdaweienQVKT 142
Cdd:cd03257 81 rkEIQMVFQDPmsSLNPRMTIGEQI--------------AEPLRIHGKLSKKEARKEAVLLLLVGVG---------LPEE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 143 ILTKLGihnfHQkietLSGGQKKRVALASALISPCDLLILDEPTNHMDHDT----IDWLEKyLTNRTG-SLLMITHD--- 214
Cdd:cd03257 138 VLNRYP----HE----LSGGQRQRVAIARALALNPKLLIADEPTSALDVSVqaqiLDLLKK-LQEELGlTLLFITHDlgv 208
|
250 260
....*....|....*....|
gi 928932812 215 -RYFLDRVvnktLELDDGKI 233
Cdd:cd03257 209 vAKIADRV----AVMYAGKI 224
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-187 |
5.01e-25 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 101.19 E-value: 5.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 19 FENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVH-----MPSKMA------IEYLSQNPEFDPNATIleqv 87
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILldgqdLTDDERkslrkeIGYVFQDPQLFPRLTV---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 88 fksdsqimnvirdYENILEEisqnpddstlqkklLYLTDNMNAqdawEIENQVKTILTKLGIHNF-----HQKIETLSGG 162
Cdd:pfam00005 77 -------------RENLRLG--------------LLLKGLSKR----EKDARAEEALEKLGLGDLadrpvGERPGTLSGG 125
|
170 180
....*....|....*....|....*
gi 928932812 163 QKKRVALASALISPCDLLILDEPTN 187
Cdd:pfam00005 126 QRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-235 |
6.64e-25 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 103.20 E-value: 6.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 1 MN-ILSVENISKSYGE-----KILfENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHM---------PSK 65
Cdd:COG1136 1 MSpLLELRNLTKSYGTgegevTAL-RGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIdgqdisslsERE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 66 MA------IEYLSQNPEFDPNATILEQVfksdsqimnvirdyenileEISqnpddstlqkkLLYltdnmNAQDAWEIENQ 139
Cdd:COG1136 80 LArlrrrhIGFVFQFFNLLPELTALENV-------------------ALP-----------LLL-----AGVSRKERRER 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 140 VKTILTKLGIHNF-HQKIETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDT----IDWLEKyLTNRTG-SLLMITH 213
Cdd:COG1136 125 ARELLERVGLGDRlDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTgeevLELLRE-LNRELGtTIVMVTH 203
|
250 260
....*....|....*....|..
gi 928932812 214 DRYFLDRvVNKTLELDDGKIYS 235
Cdd:COG1136 204 DPELAAR-ADRVIRLRDGRIVS 224
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-186 |
9.47e-25 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 102.27 E-value: 9.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYGEKILFENISFSIGdTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKV--------HMPSKM--AIEYLSQ 73
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLG-PGMYGLLGPNGAGKTTLMRILATLTPPSSGTIridgqdvlKQPQKLrrRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 74 NPEFDPNATILEQVfksdsqimnvirDYENILEEISQNpddstlqkkllyltdnmnaqdawEIENQVKTILTKLGIHNF- 152
Cdd:cd03264 80 EFGVYPNFTVREFL------------DYIAWLKGIPSK-----------------------EVKARVDEVLELVNLGDRa 124
|
170 180 190
....*....|....*....|....*....|....
gi 928932812 153 HQKIETLSGGQKKRVALASALISPCDLLILDEPT 186
Cdd:cd03264 125 KKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-247 |
1.45e-24 |
|
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: 108.77 E-value: 1.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYG--EKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVH---MPSKM--------AIEY 70
Cdd:COG2274 474 IELENVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILidgIDLRQidpaslrrQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 71 LSQNPE-FdpNATILE-------QVfkSDSQIMNVIRDYeNILEEISQNPddstlqkkllyltdnmnaqdaweieNQVKT 142
Cdd:COG2274 554 VLQDVFlF--SGTIREnitlgdpDA--TDEEIIEAARLA-GLHDFIEALP-------------------------MGYDT 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 143 ILTKLGihnfhqkiETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDT----IDWLEKYLTNRTgsLLMITHDRYFL 218
Cdd:COG2274 604 VVGEGG--------SNLSGGQRQRLAIARALLRNPRILILDEATSALDAETeaiiLENLRRLLKGRT--VIIIAHRLSTI 673
|
250 260
....*....|....*....|....*....
gi 928932812 219 dRVVNKTLELDDGKIySYIGNYSQFIEKK 247
Cdd:COG2274 674 -RLADRIIVLDKGRI-VEDGTHEELLARK 700
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-233 |
6.85e-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: 106.00 E-value: 6.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSY-GEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKV----------HMPSKMA-IEYL 71
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIlingvdlsdlDPASWRRqIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 72 SQNPEFdPNATILEqvfksdsqimnvirdyeNILeeisqnpddstlqkklLYltdNMNAQDAweienQVKTILTKLGIHN 151
Cdd:COG4988 417 PQNPYL-FAGTIRE-----------------NLR----------------LG---RPDASDE-----ELEAALEAAGLDE 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 152 F----HQKIET--------LSGGQKKRVALASALISPCDLLILDEPTNHMDHDT----IDWLEKYLTNRTgsLLMITHDR 215
Cdd:COG4988 455 FvaalPDGLDTplgeggrgLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETeaeiLQALRRLAKGRT--VILITHRL 532
|
250
....*....|....*...
gi 928932812 216 YFLDRvVNKTLELDDGKI 233
Cdd:COG4988 533 ALLAQ-ADRILVLDDGRI 549
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-233 |
1.23e-23 |
|
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: 100.26 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYGEKI----LFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKV-------HMPSKMA----I 68
Cdd:COG1124 2 LEVRNLSVSYGQGGrrvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVtfdgrpvTRRRRKAfrrrV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 69 EYLSQNPE--FDPNATILEqvfksdsqimnvirdyenILEEisqnpddsTLqkKLLYLTDnmnaqdaweIENQVKTILTK 146
Cdd:COG1124 82 QMVFQDPYasLHPRHTVDR------------------ILAE--------PL--RIHGLPD---------REERIAELLEQ 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 147 LGIH-NF-----HQkietLSGGQKKRVALASALISPCDLLILDEPTNHMDHDT----IDWLEKYLTNRTGSLLMITHDRY 216
Cdd:COG1124 125 VGLPpSFldrypHQ----LSGGQRQRVAIARALILEPELLLLDEPTSALDVSVqaeiLNLLKDLREERGLTYLFVSHDLA 200
|
250
....*....|....*..
gi 928932812 217 FLDRVVNKTLELDDGKI 233
Cdd:COG1124 201 VVAHLCDRVAVMQNGRI 217
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
319-516 |
1.23e-23 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 99.12 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSI--------DIGPTV---KIGYFS 387
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIyldgkplsAMPPPEwrrQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 388 QES-------EDmdiNLRAIEYIKEKAeyITTEDgikisASQMMENFLFSKD-LQWTyISKLSGGERRRLYLLRILMDAP 459
Cdd:COG4619 81 QEPalwggtvRD---NLPFPFQLRERK--FDRER-----ALELLERLGLPPDiLDKP-VERLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 928932812 460 NVLILDEPTNDLDIDTLKVLENYIDDF----NGIVICVSHDRYFLDRICNKIFFFAgDGKI 516
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYlaeeGRAVLWVSHDPEQIERVADRVLTLE-AGRL 209
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-236 |
3.41e-23 |
|
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: 98.56 E-value: 3.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYGEKILfENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHM---------PSKMAIEYLSQN 74
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLngkditnlpPEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 75 PEFDPNatileqvfksdsqiMNVirdYENIleeisqnpdDSTLQKKLlyltdnmnaQDAWEIENQVKTILTKLGI-HNFH 153
Cdd:cd03299 80 YALFPH--------------MTV---YKNI---------AYGLKKRK---------VDKKEIERKVLEIAEMLGIdHLLN 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 154 QKIETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDT----IDWLEKYLTNRTGSLLMITHDRYFLDRVVNKTLELD 229
Cdd:cd03299 125 RKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTkeklREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIML 204
|
....*..
gi 928932812 230 DGKIYSY 236
Cdd:cd03299 205 NGKLIQV 211
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-233 |
2.69e-22 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 101.00 E-value: 2.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSY--GEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVH-------------MPSKMAi 68
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITlggvdlrdldeddLRRRIA- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 69 eYLSQNPE-FdpNATILEqvfksdsqimnvirdyeNILeeISqNPDdstlqkkllyltdnmnAQDAweienQVKTILTKL 147
Cdd:COG4987 413 -VVPQRPHlF--DTTLRE-----------------NLR--LA-RPD----------------ATDE-----ELWAALERV 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 148 GIHNFHQKI------------ETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDT----IDWLEKYLTNRTgsLLMI 211
Cdd:COG4987 449 GLGDWLAALpdgldtwlgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATeqalLADLLEALAGRT--VLLI 526
|
250 260
....*....|....*....|..
gi 928932812 212 THDRYFLDRvVNKTLELDDGKI 233
Cdd:COG4987 527 THRLAGLER-MDRILVLEDGRI 547
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-233 |
3.33e-22 |
|
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: 95.82 E-value: 3.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 2 NILSVENISKSYGEKILFENISFSI--GDTdkIGLIGVNGTGKSSLLKIIAGYDVADTGKvhmpskmaIEYLSQN-PEFD 78
Cdd:COG1127 4 PMIEVRNLTKSFGDRVVLDGVSLDVprGEI--LAIIGGSGSGKSVLLKLIIGLLRPDSGE--------ILVDGQDiTGLS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 79 PNAtiLEQ-------VFKS----DSqiMNVirdYENI---LEEISQNPDDstlqkkllyltdnmnaqdawEIENQVKTIL 144
Cdd:COG1127 74 EKE--LYElrrrigmLFQGgalfDS--LTV---FENVafpLREHTDLSEA--------------------EIRELVLEKL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 145 TKLGIHNFHQKI--EtLSGGQKKRVALASALISPCDLLILDEPTNHMD---HDTIDWLEKYLTNRTG-SLLMITHD---- 214
Cdd:COG1127 127 ELVGLPGAADKMpsE-LSGGMRKRVALARALALDPEILLYDEPTAGLDpitSAVIDELIRELRDELGlTSVVVTHDldsa 205
|
250
....*....|....*....
gi 928932812 215 RYFLDRVVnktlELDDGKI 233
Cdd:COG1127 206 FAIADRVA----VLADGKI 220
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-233 |
5.21e-22 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 95.26 E-value: 5.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVhmpskmaieYLSQNPEFDPNATI 83
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEV---------LIDGEDISGLSEAE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 84 LEQ-------VFKS----DSqiMNVirdYENI---LEEISQNPDdstlqkkllyltdnmnaqdaWEIENQVKTILTKLGI 149
Cdd:cd03261 72 LYRlrrrmgmLFQSgalfDS--LTV---FENVafpLREHTRLSE--------------------EEIREIVLEKLEAVGL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 150 HNFHQKI-ETLSGGQKKRVALASALISPCDLLILDEPTNHMD---HDTIDWLEKYLTNRTG-SLLMITHDRYFLDRVVNK 224
Cdd:cd03261 127 RGAEDLYpAELSGGMKKRVALARALALDPELLLYDEPTAGLDpiaSGVIDDLIRSLKKELGlTSIMVTHDLDTAFAIADR 206
|
....*....
gi 928932812 225 TLELDDGKI 233
Cdd:cd03261 207 IAVLYDGKI 215
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-233 |
1.42e-21 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 93.05 E-value: 1.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVhmpskmaieylsqnpefdpnaTI 83
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEI---------------------TF 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 84 LEQVFKSDSQIMNVIrdyENILEEISqnpddstlqkkllyLTDNMNAQDAWEI--------ENQVKTILTKLGIHNF-HQ 154
Cdd:cd03268 60 DGKSYQKNIEALRRI---GALIEAPG--------------FYPNLTARENLRLlarllgirKKRIDEVLDVVGLKDSaKK 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 155 KIETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYLTN---RTGSLLMITHDRYFLDRVVNKTLELDDG 231
Cdd:cd03268 123 KVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSlrdQGITVLISSHLLSEIQKVADRIGIINKG 202
|
..
gi 928932812 232 KI 233
Cdd:cd03268 203 KL 204
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
319-516 |
1.47e-21 |
|
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: 92.08 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIgptvkigyfsqesEDMDINLR 398
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKV-------------LGKDIKKE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 399 AIEYIKekaeyittedgiKISAsqMMENFLFSKDLQ-WTYIsKLSGGERRRLYLLRILMDAPNVLILDEPTNDLDIDTLK 477
Cdd:cd03230 68 PEEVKR------------RIGY--LPEEPSLYENLTvRENL-KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRR 132
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 928932812 478 VLENYIDDFN---GIVICVSHDRYFLDRICNKIFFFAgDGKI 516
Cdd:cd03230 133 EFWELLRELKkegKTILLSSHILEEAERLCDRVAILN-NGRI 173
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
6-233 |
6.98e-21 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 91.50 E-value: 6.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 6 VENISKSY-GEKIL-FENISFSIGDTDKIGLIGVNGTGKSSLLKIIAG----------YDVADTGKVHMPSKMA-IEYLS 72
Cdd:cd03245 5 FRNVSFSYpNQEIPaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGlykptsgsvlLDGTDIRQLDPADLRRnIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 73 QNPE-FdpNATILEQV-----FKSDSQIMNVIRdYENILEEISQNPDDSTLQkkllyltdnmnaqdaweienqvktiltk 146
Cdd:cd03245 85 QDVTlF--YGTLRDNItlgapLADDERILRAAE-LAGVTDFVNKHPNGLDLQ---------------------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 147 LGIHNFhqkieTLSGGQKKRVALASALISPCDLLILDEPTNHMDHDT----IDWLEKYLTNRTgsLLMITHdRYFLDRVV 222
Cdd:cd03245 134 IGERGR-----GLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSeerlKERLRQLLGDKT--LIIITH-RPSLLDLV 205
|
250
....*....|.
gi 928932812 223 NKTLELDDGKI 233
Cdd:cd03245 206 DRIIVMDSGRI 216
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-234 |
1.13e-20 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 91.35 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYGEKILfeNISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKmaiEYLSQNPEFDPnATI 83
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQ---DLTALPPAERP-VSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 84 LEQ---VFKSdsqiMNVirdYENILEEISqnPDdstlqkklLYLTDnmnAQDAweienQVKTILTKLGIHNFHQ-KIETL 159
Cdd:COG3840 76 LFQennLFPH----LTV---AQNIGLGLR--PG--------LKLTA---EQRA-----QVEQALERVGLAGLLDrLPGQL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 160 SGGQKKRVALASALISPCDLLILDEPTNHMD----HDTIDWLEKYLTNRTGSLLMITHDryfLD---RVVNKTLELDDGK 232
Cdd:COG3840 131 SGGQRQRVALARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCRERGLTVLMVTHD---PEdaaRIADRVLLVADGR 207
|
..
gi 928932812 233 IY 234
Cdd:COG3840 208 IA 209
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-233 |
1.65e-20 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 93.29 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKV---------HMPSKM-AIEYLSQ 73
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIvlngrdlftNLPPRErRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 74 NPEFDPNatileqvfksdsqiMNVirdYENILEEISQNPDDSTlqkkllyltdnmnaqdawEIENQVKTILTKLGIHNF- 152
Cdd:COG1118 83 HYALFPH--------------MTV---AENIAFGLRVRPPSKA------------------EIRARVEELLELVQLEGLa 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 153 ----HQkietLSGGQKKRVALASALISPCDLLILDEPTNHMD----HDTIDWLEKYLTNRTGSLLMITHDR---YFL-DR 220
Cdd:COG1118 128 drypSQ----LSGGQRQRVALARALAVEPEVLLLDEPFGALDakvrKELRRWLRRLHDELGGTTVFVTHDQeeaLELaDR 203
|
250
....*....|...
gi 928932812 221 VVnktlELDDGKI 233
Cdd:COG1118 204 VV----VMNQGRI 212
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-236 |
2.62e-20 |
|
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: 89.65 E-value: 2.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHM-------PSKMAIEYLSQNPE 76
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFdgkpldiAARNRIGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 77 FDPNATILEQvfksdsqimnvirdyenileeisqnpddstlqkkLLYLTD--NMNAQDAweiENQVKTILTKLGIHNF-H 153
Cdd:cd03269 81 LYPKMKVIDQ----------------------------------LVYLAQlkGLKKEEA---RRRIDEWLERLELSEYaN 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 154 QKIETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYLTN--RTG-SLLMITHDRYFLDRVVNKTLELDD 230
Cdd:cd03269 124 KRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRElaRAGkTVILSTHQMELVEELCDRVLLLNK 203
|
....*.
gi 928932812 231 GKIYSY 236
Cdd:cd03269 204 GRAVLY 209
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-222 |
4.75e-20 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 89.42 E-value: 4.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHM---------PSKMAIEYLS-- 72
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFdgeditglpPHEIARLGIGrt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 73 -QNPEFDPNATILEqvfksdsqimNVIRdyenileeisqnpddSTLQKKLLYLTDNMNAQDAWEIENQVKTILTKLGIHN 151
Cdd:cd03219 81 fQIPRLFPELTVLE----------NVMV---------------AAQARTGSGLLLARARREEREARERAEELLERVGLAD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 152 F-HQKIETLSGGQKKRVALASALISPCDLLILDEPTNHMDH----DTIDWLEKyLTNRTGSLLMITHDRYFL----DRVV 222
Cdd:cd03219 136 LaDRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPeeteELAELIRE-LRERGITVLLVEHDMDVVmslaDRVT 214
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-222 |
5.23e-20 |
|
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: 89.07 E-value: 5.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYG----EKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHM-------PSKmAIEYLS 72
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVdgepvtgPGP-DRGYVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 73 QNPEFDPNATILeqvfksdsqimnvirdyENILeeisqnpddstlqkkllyLTDNMNAQDAWEIENQVKTILTKLGIHNF 152
Cdd:cd03293 80 QQDALLPWLTVL-----------------DNVA------------------LGLELQGVPKAEARERAEELLELVGLSGF 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 153 -----HQkietLSGGQKKRVALASALISPCDLLILDEPTNHMDHDT----IDWLEKyLTNRTG-SLLMITHD---RYFL- 218
Cdd:cd03293 125 enaypHQ----LSGGMRQRVALARALAVDPDVLLLDEPFSALDALTreqlQEELLD-IWRETGkTVLLVTHDideAVFLa 199
|
....
gi 928932812 219 DRVV 222
Cdd:cd03293 200 DRVV 203
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-231 |
5.64e-20 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 89.03 E-value: 5.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 1 MN-ILSVENISKSY-----GEKIL--FENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGkvhmpskmAIEYLS 72
Cdd:COG4778 1 MTtLLEVENLSKTFtlhlqGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSG--------SILVRH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 73 QNPEFDpnatiLEQVfkSDSQIMNVIRDyenileEI---SQN----PDDSTLQ---KKLLylTDNMNAQDAweiENQVKT 142
Cdd:COG4778 73 DGGWVD-----LAQA--SPREILALRRR------TIgyvSQFlrviPRVSALDvvaEPLL--ERGVDREEA---RARARE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 143 ILTKLGIHnfhqkiE--------TLSGGQKKRVALASALISPCDLLILDEPTNHMDHDT----IDWLEKYLTNRTgSLLM 210
Cdd:COG4778 135 LLARLNLP------ErlwdlppaTFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANravvVELIEEAKARGT-AIIG 207
|
250 260
....*....|....*....|.
gi 928932812 211 ITHDRYFLDRVVNKTLELDDG 231
Cdd:COG4778 208 IFHDEEVREAVADRVVDVTPF 228
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-232 |
8.00e-20 |
|
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: 87.24 E-value: 8.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVhmpskmaieylsqnpEFD--PNA 81
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSI---------------LIDgeDLT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 82 TILEQVFKSDSQIMNVIRDYEnileeisqnpddstlqkkllyLTDNMNAqdaweIENQVktiltkLGihnfhqkietLSG 161
Cdd:cd03229 66 DLEDELPPLRRRIGMVFQDFA---------------------LFPHLTV-----LENIA------LG----------LSG 103
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 928932812 162 GQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYLTN---RTG-SLLMITHDRYFLDRVVNKTLELDDGK 232
Cdd:cd03229 104 GQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSlqaQLGiTVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-232 |
8.52e-20 |
|
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: 87.05 E-value: 8.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYGEKI--LFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKV----HMPSKMAIEYLSQNpef 77
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEIlidgVDLRDLDLESLRKN--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 78 dpnATILEQvfksDSQIMN-VIRdyENILeeisqnpddstlqkkllyltdnmnaqdaweienqvktiltklgihnfhqki 156
Cdd:cd03228 78 ---IAYVPQ----DPFLFSgTIR--ENIL--------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 157 etlSGGQKKRVALASALISPCDLLILDEPTNHMDHDT----IDWLEKYLTNRTgsLLMITHdRYFLDRVVNKTLELDDGK 232
Cdd:cd03228 98 ---SGGQRQRIAIARALLRDPPILILDEATSALDPETealiLEALRALAKGKT--VIVIAH-RLSTIRDADRIIVLDDGR 171
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-518 |
9.55e-20 |
|
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: 92.94 E-value: 9.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAG------------YDVA---DTGKVHMPSKMAI 68
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdqyeptsgriiYHVAlceKCGYVERPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 69 -------EYLSQNPEF----DP--------NATILEQVF---KSDSQIMNVIRDyeniLEEISQNPDDSTlqKKLLYLTD 126
Cdd:TIGR03269 81 pcpvcggTLEPEEVDFwnlsDKlrrrirkrIAIMLQRTFalyGDDTVLDNVLEA----LEEIGYEGKEAV--GRAVDLIE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 127 nmnaqdaweienqvktiLTKLGiHNFHQKIETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDW----LEKYLT 202
Cdd:TIGR03269 155 -----------------MVQLS-HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLvhnaLEEAVK 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 203 NRTGSLLMITHDRYFLDRVVNKTLELDDGKIYSyIGNYSQFIEKKLErktLESSIERKRERLYKKElewiragaqarstk 282
Cdd:TIGR03269 217 ASGISMVLTSHWPEVIEDLSDKAIWLENGEIKE-EGTPDEVVAVFME---GVSEVEKECEVEVGEP-------------- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 283 qkarIQRFEELKNtsspiHDSNIDICVAhsrlgqkiieinhisksfeqnKVIEDFSYIALKDDRIGIIGKNGTGKSTLLN 362
Cdd:TIGR03269 279 ----IIKVRNVSK-----RYISVDRGVV---------------------KAVDNVSLEVKEGEIFGIVGTSGAGKTTLSK 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 363 LITGKLTPDLGSIDigptVKIGyfsQESEDM-----DINLRAIEYI----KEKAEY--------ITTEDGI-------KI 418
Cdd:TIGR03269 329 IIAGVLEPTSGEVN----VRVG---DEWVDMtkpgpDGRGRAKRYIgilhQEYDLYphrtvldnLTEAIGLelpdelaRM 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 419 SASQMMENFLFSKD----LQWTYISKLSGGERRRLYLLRILMDAPNVLILDEPTNDLDIDTLKVLENYI----DDFNGIV 490
Cdd:TIGR03269 402 KAVITLKMVGFDEEkaeeILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkarEEMEQTF 481
|
570 580
....*....|....*....|....*...
gi 928932812 491 ICVSHDRYFLDRICNKIFFFAgDGKIIE 518
Cdd:TIGR03269 482 IIVSHDMDFVLDVCDRAALMR-DGKIVK 508
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-234 |
1.16e-19 |
|
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: 88.60 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 1 MNILSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYdvadtgkvhMPskmaieylsqnPEFDPN 80
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGD---------LP-----------PTYGND 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 81 ATIL------EQVFK-------SDSQIMNVIRDYENILE----------EISQNPDDstlqkkllyltdnmnaqdawEIE 137
Cdd:COG1119 61 VRLFgerrggEDVWElrkriglVSPALQLRFPRDETVLDvvlsgffdsiGLYREPTD--------------------EQR 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 138 NQVKTILTKLGIHNF-HQKIETLSGGQKKRVALASALISPCDLLILDEPTNHMD----HDTIDWLEKYLTNRTGSLLMIT 212
Cdd:COG1119 121 ERARELLELLGLAHLaDRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDlgarELLLALLDKLAAEGAPTLVLVT 200
|
250 260
....*....|....*....|..
gi 928932812 213 HDRYFLDRVVNKTLELDDGKIY 234
Cdd:COG1119 201 HHVEEIPPGITHVLLLKDGRVV 222
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-233 |
1.37e-19 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 90.54 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 1 MNILSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHM---------PSKMAIEYL 71
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLdgrdvtglpPEKRNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 72 SQNPEFDPNatileqvfksdsqiMNVirdYENI---LEeisqnpddstlQKKLlyltdnmnaqDAWEIENQVKTILTKLG 148
Cdd:COG3842 83 FQDYALFPH--------------LTV---AENVafgLR-----------MRGV----------PKAEIRARVAELLELVG 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 149 IHNF-HQKIETLSGGQKKRVALASAL-ISPcDLLILDEPTNHMD----HDTIDWLEKYLTnRTG-SLLMITHDRY----F 217
Cdd:COG3842 125 LEGLaDRYPHQLSGGQQQRVALARALaPEP-RVLLLDEPLSALDaklrEEMREELRRLQR-ELGiTFIYVTHDQEealaL 202
|
250
....*....|....*.
gi 928932812 218 LDRVVnktlELDDGKI 233
Cdd:COG3842 203 ADRIA----VMNDGRI 214
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
320-517 |
2.64e-19 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 85.95 E-value: 2.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 320 EINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIGptvkigyfsqeseDMDINLRA 399
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLD-------------GKDLASLS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 400 IeyiKEKAEYITTedgikisASQMMENF-LFSKDLQwtYISKLSGGERRRLYLLRILMDAPNVLILDEPTNDLDI----D 474
Cdd:cd03214 68 P---KELARKIAY-------VPQALELLgLAHLADR--PFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIahqiE 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 928932812 475 TLKVLENYIDDFNGIVICVSHDryfLD---RICNKIFFFaGDGKII 517
Cdd:cd03214 136 LLELLRRLARERGKTVVMVLHD---LNlaaRYADRVILL-KDGRIV 177
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-222 |
3.51e-19 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 91.19 E-value: 3.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSY-GEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKV--------HMPSKM---AIEYL 71
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIavngvplaDADADSwrdQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 72 SQNPeFDPNATILEqvfksdsqimnvirdyeNILeeisqnpddstlqkklLYLTDnmnAQDAweienQVKTILTKLGIHN 151
Cdd:TIGR02857 402 PQHP-FLFAGTIAE-----------------NIR----------------LARPD---ASDA-----EIREALERAGLDE 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 152 F----HQKIET--------LSGGQKKRVALASALISPCDLLILDEPTNHMDHDT----IDWLEKYLTNRTgsLLMITHDR 215
Cdd:TIGR02857 440 FvaalPQGLDTpigeggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETeaevLEALRALAQGRT--VLLVTHRL 517
|
250
....*....|
gi 928932812 216 ---YFLDRVV 222
Cdd:TIGR02857 518 alaALADRIV 527
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-222 |
8.28e-19 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 86.68 E-value: 8.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 1 MNILSVENISKSY----GEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKmaieylsQNPE 76
Cdd:COG1116 5 APALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGK-------PVTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 77 FDPNATIleqVFksdsqimnvirdyenileeisQNPddstlqkkLLY--LT--DN------MNAQDAWEIENQVKTILTK 146
Cdd:COG1116 78 PGPDRGV---VF---------------------QEP--------ALLpwLTvlDNvalgleLRGVPKAERRERARELLEL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 147 LGIHNF-----HQkietLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTI----DWLEKYLTNRTGSLLMITHDRY- 216
Cdd:COG1116 126 VGLAGFedaypHQ----LSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRerlqDELLRLWQETGKTVLFVTHDVDe 201
|
....*....
gi 928932812 217 --FL-DRVV 222
Cdd:COG1116 202 avFLaDRVV 210
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
21-236 |
8.70e-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: 85.42 E-value: 8.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 21 NISFSIgDTDKIGLIGVNGTGKSSLLKIIAGYDVADTG--------------KVHMPS-KMAIEYLSQNPEFDPNatile 85
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGtivlngtvlfdsrkKINLPPqQRKIGLVFQQYALFPH----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 86 qvfksdsqiMNVirdYENI---LEEISQNPDdstlqkkllyltdnmnaqdaweiENQVKTILTKLGI-HNFHQKIETLSG 161
Cdd:cd03297 90 ---------LNV---RENLafgLKRKRNRED-----------------------RISVDELLDLLGLdHLLNRYPAQLSG 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 928932812 162 GQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYLTNRTGSL----LMITHDRYFLDRVVNKTLELDDGKIYSY 236
Cdd:cd03297 135 GEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNLnipvIFVTHDLSEAEYLADRIVVMEDGRLQYI 213
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-233 |
9.80e-19 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 85.56 E-value: 9.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 2 NILSVENISKSYGE-----KILfENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMpskmAIEYLSQNPE 76
Cdd:COG4181 7 PIIELRGLTKTVGTgagelTIL-KGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRL----AGQDLFALDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 77 fDPNATILEQ----VFKSdSQI---MNVIrdyENI---LEeisqnpddstlqkkllyLTDNMNAQDaweienQVKTILTK 146
Cdd:COG4181 82 -DARARLRARhvgfVFQS-FQLlptLTAL---ENVmlpLE-----------------LAGRRDARA------RARALLER 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 147 LGI-HNFHQKIETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDT----IDWLEKyLTNRTGS-LLMITHDRYFLDR 220
Cdd:COG4181 134 VGLgHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATgeqiIDLLFE-LNRERGTtLVLVTHDPALAAR 212
|
250
....*....|...
gi 928932812 221 vVNKTLELDDGKI 233
Cdd:COG4181 213 -CDRVLRLRAGRL 224
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
20-233 |
1.45e-18 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 89.93 E-value: 1.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 20 ENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHM---------PSKM--AIEYLSQNPE-FdpNATI---- 83
Cdd:TIGR03375 482 DNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLdgvdirqidPADLrrNIGYVPQDPRlF--YGTLrdni 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 84 -LEQVFKSDSQIMNVIRDYeNILEEISQNPDDSTLQkkllyltdnmnaqdaweienqvktiltklgihnFHQKIETLSGG 162
Cdd:TIGR03375 560 aLGAPYADDEEILRAAELA-GVTEFVRRHPDGLDMQ---------------------------------IGERGRSLSGG 605
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 928932812 163 QKKRVALASALISPCDLLILDEPTNHMDHDT----IDWLEKYLTNRTgsLLMITHDRYFLDrVVNKTLELDDGKI 233
Cdd:TIGR03375 606 QRQAVALARALLRDPPILLLDEPTSAMDNRSeerfKDRLKRWLAGKT--LVLVTHRTSLLD-LVDRIIVMDNGRI 677
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
4-213 |
1.45e-18 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 84.33 E-value: 1.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKM----------AIEYLSQ 73
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPlaeqrdepheNILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 74 NPEFDPNATILEQvfksdsqimnvIRDYENILEEISQNPDDSTLQKKLLYLTDNMNAQdaweienqvktiltklgihnfh 153
Cdd:TIGR01189 81 LPGLKPELSALEN-----------LHFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQ---------------------- 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 928932812 154 qkietLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYLTN---RTGSLLMITH 213
Cdd:TIGR01189 128 -----LSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAhlaRGGIVLLTTH 185
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-185 |
1.65e-18 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 87.44 E-value: 1.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 1 MNILSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHM---------PSKMAIEYL 71
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIggrdvtdlpPKDRNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 72 SQNPEFDPNatileqvfksdsqiMNVirdYENI---LEeisqnpddstLQKkllyltdnMNAQdawEIENQVKTILTKLG 148
Cdd:COG3839 81 FQSYALYPH--------------MTV---YENIafpLK----------LRK--------VPKA---EIDRRVREAAELLG 122
|
170 180 190
....*....|....*....|....*....|....*...
gi 928932812 149 IHNF-HQKIETLSGGQKKRVALASALISPCDLLILDEP 185
Cdd:COG3839 123 LEDLlDRKPKQLSGGQRQRVALGRALVREPKVFLLDEP 160
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-300 |
1.81e-18 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 89.46 E-value: 1.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKMAIEYLSQNPefdpnat 82
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQ------- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 83 ileqvfksdsqimnvirdyeniLEEIsqNPDDSTLQkKLLYLTDNmnaqdawEIENQVKTILTKLGIH--NFHQKIETLS 160
Cdd:PRK10636 385 ----------------------LEFL--RADESPLQ-HLARLAPQ-------ELEQKLRDYLGGFGFQgdKVTEETRRFS 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 161 GGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYLTNRTGSLLMITHDRYFLDRVVNKTLELDDGKIYSYIG-- 238
Cdd:PRK10636 433 GGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGdl 512
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 928932812 239 -NYSQFIekklerktleSSIERKRERLYKKELEWIRAGAQARstkqKARIQRFEELKNTSSPI 300
Cdd:PRK10636 513 eDYQQWL----------SDVQKQENQTDEAPKENNANSAQAR----KDQKRREAELRTQTQPL 561
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-190 |
2.81e-18 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 83.84 E-value: 2.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHM---------PSKMAIEYLSQN 74
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIggrdvtdlpPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 75 PEFDPNatileqvfksdsqiMNVirdYENI---LEEISQNPDdstlqkkllyltdnmnaqdawEIENQVKTILTKLGI-H 150
Cdd:cd03301 81 YALYPH--------------MTV---YDNIafgLKLRKVPKD---------------------EIDERVREVAELLQIeH 122
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 928932812 151 NFHQKIETLSGGQKKRVALASALISPCDLLILDEPTNHMD 190
Cdd:cd03301 123 LLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLD 162
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
320-515 |
3.11e-18 |
|
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: 81.91 E-value: 3.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 320 EINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIgptvkigyfsqesedmdinlra 399
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILI---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 400 ieyikekaeyitteDGIKISasqmmENFLFSKDLQWTYISKLSGGERRRLYLLRILMDAPNVLILDEPTNDLDIDTLKVL 479
Cdd:cd00267 59 --------------DGKDIA-----KLPLEELRRRIGYVPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERL 119
|
170 180 190
....*....|....*....|....*....|....*....
gi 928932812 480 ENYIDDFNG---IVICVSHDRYFLDRICNKIFFFAgDGK 515
Cdd:cd00267 120 LELLRELAEegrTVIIVTHDPELAELAADRVIVLK-DGK 157
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-185 |
4.00e-18 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 83.75 E-value: 4.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKV--------HMP----SKMAIEYL 71
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIlldgqditKLPmhkrARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 72 SQNPefdpnatileQVFKSdsqiMNVirdYENILEEISQNPDDSTLQKKLLyltdnmnaqdaweienqvKTILTKLGI-H 150
Cdd:cd03218 81 PQEA----------SIFRK----LTV---EENILAVLEIRGLSKKEREEKL------------------EELLEEFHItH 125
|
170 180 190
....*....|....*....|....*....|....*
gi 928932812 151 NFHQKIETLSGGQKKRVALASALISPCDLLILDEP 185
Cdd:cd03218 126 LRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
320-515 |
4.04e-18 |
|
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: 83.29 E-value: 4.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 320 EINHISKSFE--QNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIGPTV-----------KIGYF 386
Cdd:cd03225 1 ELKNLSFSYPdgARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDltklslkelrrKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 387 SQESEDMDINLRAIEYIKEKAEYI-TTEDGIKISASQMMENFLFSkDLQWTYISKLSGGERRRLYLLRILMDAPNVLILD 465
Cdd:cd03225 81 FQNPDDQFFGPTVEEEVAFGLENLgLPEEEIEERVEEALELVGLE-GLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 928932812 466 EPTNDLDIDTLKVLENYIDDFN--GI-VICVSHDRYFLDRICNKIFFFAgDGK 515
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKKLKaeGKtIIIVTHDLDLLLELADRVIVLE-DGK 211
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-222 |
5.48e-18 |
|
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: 83.93 E-value: 5.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 1 MNILSVENISKSYGE-KILfENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHM---------PSKMAIEY 70
Cdd:COG0411 2 DPLLEVRGLTKRFGGlVAV-DDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFdgrditglpPHRIARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 71 LS---QNPefdpnatileQVFKSdsqiMNVIrdyENILeeIS-QNPDDSTLQKKLLYLtdNMNAQDAWEIENQVKTILTK 146
Cdd:COG0411 81 IArtfQNP----------RLFPE----LTVL---ENVL--VAaHARLGRGLLAALLRL--PRARREEREARERAEELLER 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 147 LGIHNF-HQKIETLSGGQKKRVALASALISPCDLLILDEPT---NHMD-HDTIDWLEKyLTNRTG-SLLMITHDRYFL-- 218
Cdd:COG0411 140 VGLADRaDEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAaglNPEEtEELAELIRR-LRDERGiTILLIEHDMDLVmg 218
|
....*.
gi 928932812 219 --DRVV 222
Cdd:COG0411 219 laDRIV 224
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
4-213 |
7.90e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 82.16 E-value: 7.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVH---MP-SKMAIEYLSQ------ 73
Cdd:PRK13538 2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLwqgEPiRRQRDEYHQDllylgh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 74 ----NPEFDPnatileqvfksdsqimnvirdYEN--ILEEISQNPDDstlqkkllyltdnmnaQDAWEienqvktILTKL 147
Cdd:PRK13538 82 qpgiKTELTA---------------------LENlrFYQRLHGPGDD----------------EALWE-------ALAQV 117
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 148 GIHNF-HQKIETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYL---TNRTGSLLMITH 213
Cdd:PRK13538 118 GLAGFeDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLaqhAEQGGMVILTTH 187
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-233 |
1.17e-17 |
|
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: 82.67 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVhmpskmaieYLSQNP--EFDPNA 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEI---------LLDGKDitNLPPHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 82 TILEQVFKSDSQI--MNVirdYENI---LeeisqnpddsTLQKKllyltdnmnaqDAWEIENQVKTILTKLGIHNF-HQK 155
Cdd:cd03300 72 RPVNTVFQNYALFphLTV---FENIafgL----------RLKKL-----------PKAEIKERVAEALDLVQLEGYaNRK 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 156 IETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLE---KYLTNRTG-SLLMITHDR----YFLDRVVnktlE 227
Cdd:cd03300 128 PSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQlelKRLQKELGiTFVFVTHDQeealTMSDRIA----V 203
|
....*.
gi 928932812 228 LDDGKI 233
Cdd:cd03300 204 MNKGKI 209
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
7-233 |
1.30e-17 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 82.07 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 7 ENISKSYGEKIL-FENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKV--------HMPSKmAIEYLSQNpef 77
Cdd:cd03292 4 INVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIrvngqdvsDLRGR-AIPYLRRK--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 78 dpnatiLEQVFKsDSQIMNVIRDYENIL--EEISQNPDDstlqkkllyltdnmnaqdawEIENQVKTILTKLGI-HNFHQ 154
Cdd:cd03292 80 ------IGVVFQ-DFRLLPDRNVYENVAfaLEVTGVPPR--------------------EIRKRVPAALELVGLsHKHRA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 155 KIETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDT----IDWLEKYltNRTG-SLLMITHDRYFLDRVVNKTLELD 229
Cdd:cd03292 133 LPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTtweiMNLLKKI--NKAGtTVVVATHAKELVDTTRHRVIALE 210
|
....
gi 928932812 230 DGKI 233
Cdd:cd03292 211 RGKL 214
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-233 |
2.29e-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: 79.78 E-value: 2.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVhmpskmaieylsqnpefdpnaTI 83
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEI---------------------LV 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 84 LEQVFKSDSqimnvirdyenileeisqnpddstlqkkllyltdnmnAQDAWeienqvktiltKLGIHNFHQkietLSGGQ 163
Cdd:cd03216 60 DGKEVSFAS-------------------------------------PRDAR-----------RAGIAMVYQ----LSVGE 87
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 928932812 164 KKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKY---LTNRTGSLLMITH----DRYFLDRVVnktlELDDGKI 233
Cdd:cd03216 88 RQMVEIARALARNARLLILDEPTAALTPAEVERLFKVirrLRAQGVAVIFISHrldeVFEIADRVT----VLRDGRV 160
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-238 |
2.40e-17 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 81.40 E-value: 2.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYG--EKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKmaieylsqnpefdpna 81
Cdd:cd03263 1 LQIRNLTKTYKkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGY---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 82 tileqvfksdsqimNVIRDYENILEEISQNPddstlQKKLLYltDNMNAQD------------AWEIENQVKTILTKLGI 149
Cdd:cd03263 65 --------------SIRTDRKAARQSLGYCP-----QFDALF--DELTVREhlrfyarlkglpKSEIKEEVELLLRVLGL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 150 HNF-HQKIETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDT--IDW--LEKYLTNRtgSLLMITHDRYFLDRVVNK 224
Cdd:cd03263 124 TDKaNKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASrrAIWdlILEVRKGR--SIILTTHSMDEAEALCDR 201
|
250
....*....|....
gi 928932812 225 TLELDDGKIYsYIG 238
Cdd:cd03263 202 IAIMSDGKLR-CIG 214
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
4-232 |
2.76e-17 |
|
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: 80.59 E-value: 2.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYGEK-----ILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKMAieYLSQNPeFD 78
Cdd:cd03250 1 ISVEDASFTWDSGeqetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIA--YVSQEP-WI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 79 PNATILEqvfksdsqimNVI-------RDYENILEEISQNPDdstlqkkllylTDNMNAQDAWEI-ENqvktiltklGIh 150
Cdd:cd03250 78 QNGTIRE----------NILfgkpfdeERYEKVIKACALEPD-----------LEILPDGDLTEIgEK---------GI- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 151 nfhqkieTLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWL------EKYLTNRTgsLLMITHDRYFL---DRV 221
Cdd:cd03250 127 -------NLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIfencilGLLLNNKT--RILVTHQLQLLphaDQI 197
|
250
....*....|.
gi 928932812 222 VnktlELDDGK 232
Cdd:cd03250 198 V----VLDNGR 204
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-250 |
6.47e-17 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 80.69 E-value: 6.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSY--GEKILfENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHmpskmaieylsqnpeFDPNA 81
Cdd:cd03256 1 IEVENLSKTYpnGKKAL-KDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVL---------------IDGTD 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 82 tiLEQVFKSD-----SQIMNVIRDYeNILEEIS--QN------PDDSTLQKkLLYLTDNMNAQDAWEIenqvktiLTKLG 148
Cdd:cd03256 65 --INKLKGKAlrqlrRQIGMIFQQF-NLIERLSvlENvlsgrlGRRSTWRS-LFGLFPKEEKQRALAA-------LERVG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 149 I-HNFHQKIETLSGGQKKRVALASALISPCDLLILDEPTNHMD----HDTIDWLEKYLTNRTGSLLMITHD----RYFLD 219
Cdd:cd03256 134 LlDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDpassRQVMDLLKRINREEGITVIVSLHQvdlaREYAD 213
|
250 260 270
....*....|....*....|....*....|.
gi 928932812 220 RVVNktleLDDGKIYsYIGNYSQFIEKKLER 250
Cdd:cd03256 214 RIVG----LKDGRIV-FDGPPAELTDEVLDE 239
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
316-512 |
8.22e-17 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 80.13 E-value: 8.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 316 QKIIEINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDI-GPTV-----KIGYFSQE 389
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLfGKPPrrarrRIGYVPQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 390 SE-DMDINLRAIEYI------------------KEKAEYITTEDGikisasqmMENFlfsKDLQwtyISKLSGGErrrly 450
Cdd:COG1121 84 AEvDWDFPITVRDVVlmgrygrrglfrrpsradREAVDEALERVG--------LEDL---ADRP---IGELSGGQqqrvl 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 928932812 451 llrilMDAPNVLILDEPTNDLDIDTLKVLENYIDDFN--GI-VICVSHDRYFLDRICNKIFFFAG 512
Cdd:COG1121 150 laralAQDPDLLLLDEPFAGVDAATEEALYELLRELRreGKtILVVTHDLGAVREYFDRVLLLNR 214
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-233 |
8.64e-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: 8.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVhmpskmaieylsqnpEFDPnati 83
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTI---------------IIDG---- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 84 lEQVFKSDSQIMNVIRD----------YEN--ILEEISQNPddstlqKKLLyltdNMNAQDAWEIENQvktILTKLGIHN 151
Cdd:cd03262 62 -LKLTDDKKNINELRQKvgmvfqqfnlFPHltVLENITLAP------IKVK----GMSKAEAEERALE---LLEKVGLAD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 152 F-HQKIETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYLTN--RTG-SLLMITHDRYFLDRVVNKTLE 227
Cdd:cd03262 128 KaDAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDlaEEGmTMVVVTHEMGFAREVADRVIF 207
|
....*.
gi 928932812 228 LDDGKI 233
Cdd:cd03262 208 MDDGRI 213
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
22-214 |
9.92e-17 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 78.62 E-value: 9.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 22 ISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSK-------------MAIEYLSQNPEfdpnatilEQVF 88
Cdd:TIGR01166 11 LNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEpldysrkgllerrQRVGLVFQDPD--------DQLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 89 KSDsqimnvirdyenILEEISQNPDdstlqkkllyltdNMNAQDAwEIENQVKTILTKLGIHNF-HQKIETLSGGQKKRV 167
Cdd:TIGR01166 83 AAD------------VDQDVAFGPL-------------NLGLSEA-EVERRVREALTAVGASGLrERPTHCLSGGEKKRV 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 928932812 168 ALASALISPCDLLILDEPTNHMD----HDTIDWLEKyLTNRTGSLLMITHD 214
Cdd:TIGR01166 137 AIAGAVAMRPDVLLLDEPTAGLDpagrEQMLAILRR-LRAEGMTVVISTHD 186
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
320-517 |
1.22e-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: 78.84 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 320 EINHISKSF-EQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIGPTV--------KIGYFSQES 390
Cdd:cd03226 1 RIENISFSYkKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPikakerrkSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 391 ----------EDMDINLRAIEYIKEKAEYITTedgiKISASQMMENFLFSkdlqwtyiskLSGGERRRLYLLRILMDAPN 460
Cdd:cd03226 81 dyqlftdsvrEELLLGLKELDAGNEQAETVLK----DLDLYALKERHPLS----------LSGGQKQRLAIAAALLSGKD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 461 VLILDEPTNDLDIDTLKVLENYIDDFNG---IVICVSHDRYFLDRICNKIFFFAgDGKII 517
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELIRELAAqgkAVIVITHDYEFLAKVCDRVLLLA-NGAIV 205
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-228 |
1.37e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 79.77 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 1 MNILSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKMAIEYLSQNPEFDPn 80
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDT- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 81 aTILEQVfksdsqimnvirdyenileeisqnpddstlqKKLLYLTDNMNAQDAWEIENQVKtiltklGIHNFHQKIETLS 160
Cdd:PRK09544 81 -TLPLTV-------------------------------NRFLRLRPGTKKEDILPALKRVQ------AGHLIDAPMQKLS 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 928932812 161 GGQKKRVALASALISPCDLLILDEPTNHMD-------HDTIDWLEKYLtnrTGSLLMITHDryfLDRVVNKTLEL 228
Cdd:PRK09544 123 GGETQRVLLARALLNRPQLLVLDEPTQGVDvngqvalYDLIDQLRREL---DCAVLMVSHD---LHLVMAKTDEV 191
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-190 |
1.38e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 80.92 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVH-----MPSKMA--IEYLsqnP 75
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLwdgepLDPEDRrrIGYL---P 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 76 E---FDPNATILEQvfksdsqimnvirdyenileeisqnpddstlqkkLLYLTD--NMNAQDAweiENQVKTILTKLGI- 149
Cdd:COG4152 78 EergLYPKMKVGEQ----------------------------------LVYLARlkGLSKAEA---KRRADEWLERLGLg 120
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 928932812 150 HNFHQKIETLSGGQKKRVALASALISPCDLLILDEPTNHMD 190
Cdd:COG4152 121 DRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLD 161
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
319-517 |
1.51e-16 |
|
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: 79.30 E-value: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSF-EQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIG--PTV---------KIGY- 385
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDgkDITkknlrelrrKVGLv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 386 FsQESEDM--------DI-----NLR-AIEYIKEKAEYITTEDGIKisasqmmenflfskDLQWTYISKLSGGErrrly- 450
Cdd:COG1122 81 F-QNPDDQlfaptveeDVafgpeNLGlPREEIRERVEEALELVGLE--------------HLADRPPHELSGGQkqrvai 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 451 llrilMDaPNVLILDEPTNDLDIDTLKVLENYIDDFN--GI-VICVSHDRYFLDRICNKIFFFAgDGKII 517
Cdd:COG1122 146 agvlaME-PEVLVLDEPTAGLDPRGRRELLELLKRLNkeGKtVIIVTHDLDLVAELADRVIVLD-DGRIV 213
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-233 |
1.64e-16 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 79.05 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 2 NILSVENISKSYGE-----KILfENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKMaieyLSQNPE 76
Cdd:PRK10584 5 NIVEVHHLKKSVGQgehelSIL-TGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQP----LHQMDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 77 fDPNATILEQ----VFKSDSQIMNVirdyeNILEEIsqnpddstlqkKLLYLTDNMNAQDAweiENQVKTILTKLGI-HN 151
Cdd:PRK10584 80 -EARAKLRAKhvgfVFQSFMLIPTL-----NALENV-----------ELPALLRGESSRQS---RNGAKALLEQLGLgKR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 152 FHQKIETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYL--TNR--TGSLLMITHDRYFLDRvVNKTLE 227
Cdd:PRK10584 140 LDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLfsLNRehGTTLILVTHDLQLAAR-CDRRLR 218
|
....*.
gi 928932812 228 LDDGKI 233
Cdd:PRK10584 219 LVNGQL 224
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4-213 |
1.79e-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: 78.30 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMpskmaieylsqnpefdpNATI 83
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLL-----------------NGGP 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 84 LEQVFKSDSQIMNVIRDYENIleeisqnpddstlqKKLLYLTDNMNAQDAWEIENQVKTILTKLGIHNF-HQKIETLSGG 162
Cdd:cd03231 64 LDFQRDSIARGLLYLGHAPGI--------------KTTLSVLENLRFWHADHSDEQVEEALARVGLNGFeDRPVAQLSAG 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 928932812 163 QKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYL---TNRTGSLLMITH 213
Cdd:cd03231 130 QQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMaghCARGGMVVLTTH 183
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-233 |
2.15e-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: 77.35 E-value: 2.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYGE--KILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVhmpskmaieYLSQNPefdpna 81
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI---------TLDGVP------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 82 tileqvfksdsqimnvIRDYENILEE----ISQNPddstlqkkllYLTDNmnaqdaweienqvkTILTKLGIHnfhqkie 157
Cdd:cd03247 66 ----------------VSDLEKALSSlisvLNQRP----------YLFDT--------------TLRNNLGRR------- 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 158 tLSGGQKKRVALASALISPCDLLILDEPTNHMDHDT----IDWLEKYLTNRTgsLLMITHDRYFLDRvVNKTLELDDGKI 233
Cdd:cd03247 99 -FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITerqlLSLIFEVLKDKT--LIWITHHLTGIEH-MDKILFLENGKI 174
|
|
| ABC_tran_CTD |
pfam16326 |
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. ... |
557-623 |
2.74e-16 |
|
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. It has a coiled coil structure with an atypical 3(10)-helix in the alpha-hairpin region. It is involved in DNA_binding.
Pssm-ID: 465095 [Multi-domain] Cd Length: 69 Bit Score: 73.65 E-value: 2.74e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 928932812 557 KFTYNEQREYETIDQEIENLENKLSTLEEEMKKYS--TDFTKLQELMNEKDYIEEELLLKMERQEYLND 623
Cdd:pfam16326 1 KLSYKEQRELEELEAEIEKLEEEIAELEAQLADPElySDYEKLQELSAELEELEAELEELYERWEELEE 69
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
4-230 |
3.02e-16 |
|
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: 76.42 E-value: 3.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENIS-KSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKMAIEYLSQNPEFdPNAT 82
Cdd:cd03223 1 IELENLSlATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRPYL-PLGT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 83 ILEQvfksdsqimnvirdyenileeisqnpddstlqkkLLYltdnmnaqdAWEienqvktiltklgihnfhqkiETLSGG 162
Cdd:cd03223 80 LREQ----------------------------------LIY---------PWD---------------------DVLSGG 95
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 928932812 163 QKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYLTNRTGSLLMITHdRYFLDRVVNKTLELDD 230
Cdd:cd03223 96 EQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVLDLDG 162
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-186 |
3.06e-16 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 78.24 E-value: 3.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYGE-KILFeNISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKV--------HMPS----KMAIEY 70
Cdd:cd03224 1 LEVENLNAGYGKsQILF-GVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIrfdgrditGLPPheraRAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 71 LSQNpefdpnatilEQVFKSdsqiMNVirdYENIleeisqnpddstlqkkLLYLTDNMNAQDAWEIEnQVKTILTKLGiH 150
Cdd:cd03224 80 VPEG----------RRIFPE----LTV---EENL----------------LLGAYARRRAKRKARLE-RVYELFPRLK-E 124
|
170 180 190
....*....|....*....|....*....|....*.
gi 928932812 151 NFHQKIETLSGGQKKRVALASALISPCDLLILDEPT 186
Cdd:cd03224 125 RRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
319-519 |
3.62e-16 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 78.18 E-value: 3.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFEQNKVIEDFSyIALKDDRI-GIIGKNGTGKSTLLNLITGKLTPDLGSIDI--------GPTVK--IGYFS 387
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVS-LTVEPGEIfGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVlgedvardPAEVRrrIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 388 QESEDMDiNLRAIEYIKEKAE-YITTEDGIKISASQMMENFLFSKDLQwTYISKLSGGerrrlyllrilM---------- 456
Cdd:COG1131 80 QEPALYP-DLTVRENLRFFARlYGLPRKEARERIDELLELFGLTDAAD-RKVGTLSGG-----------Mkqrlglalal 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 928932812 457 --DaPNVLILDEPTNDLDIDTLKVLENYIDDFNG---IVICVSHDRYFLDRICNKIFFFAgDGKIIEH 519
Cdd:COG1131 147 lhD-PELLILDEPTSGLDPEARRELWELLRELAAegkTVLLSTHYLEEAERLCDRVAIID-KGRIVAD 212
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-234 |
3.67e-16 |
|
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: 79.01 E-value: 3.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSY--GEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVhmpskmaieylsqnpefdpna 81
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKV--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 82 TILEQVFKSDSQIMNvIRDYENIleeISQNPDD----STLQKKLLYLTDNMNAqDAWEIENQVKTILTKLGIHNF-HQKI 156
Cdd:TIGR04520 60 TVDGLDTLDEENLWE-IRKKVGM---VFQNPDNqfvgATVEDDVAFGLENLGV-PREEMRKRVDEALKLVGMEDFrDREP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 157 ETLSGGQKKRVALASAL-ISPcDLLILDEPTNHMDH-------DTIDWL--EKYLTnrtgsLLMITHDryfLDRVVN--K 224
Cdd:TIGR04520 135 HLLSGGQKQRVAIAGVLaMRP-DIIILDEATSMLDPkgrkevlETIRKLnkEEGIT-----VISITHD---MEEAVLadR 205
|
250
....*....|
gi 928932812 225 TLELDDGKIY 234
Cdd:TIGR04520 206 VIVMNKGKIV 215
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
4-233 |
4.06e-16 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 77.53 E-value: 4.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYGEKILFENISFSIGDtdKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPskmAIEYLSQNPEFDPNATI 83
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFDLTFAQGE--ITAIVGPSGSGKSTLLNLIAGFETPQSGRVLIN---GVDVTAAPPADRPVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 84 LEQ--VFKSDSQIMNVirdyenileEISQNPDdstlqkklLYLtdnmNAQDaweiENQVKTILTKLGIHNFHQKI-ETLS 160
Cdd:cd03298 76 FQEnnLFAHLTVEQNV---------GLGLSPG--------LKL----TAED----RQAIEVALARVGLAGLEKRLpGELS 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 928932812 161 GGQKKRVALASALISPCDLLILDEPTNHMD----HDTIDWLEKYLTNRTGSLLMITHDRYFLDRVVNKTLELDDGKI 233
Cdd:cd03298 131 GGERQRVALARVLVRDKPVLLLDEPFAALDpalrAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-233 |
4.20e-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: 78.15 E-value: 4.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 1 MNILsVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKMAieylSQNPEFDPN 80
Cdd:cd03296 1 MSIE-VRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA----TDVPVQERN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 81 ATILEQ---VFKSdsqiMNVirdYENI---LEE--ISQNPDDSTLQKKLLYLTDNMNaqdaweienqvktiLTKLGIHNF 152
Cdd:cd03296 76 VGFVFQhyaLFRH----MTV---FDNVafgLRVkpRSERPPEAEIRAKVHELLKLVQ--------------LDWLADRYP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 153 HQkietLSGGQKKRVALASALISPCDLLILDEPTNHMD----HDTIDWLEKyLTNRTG-SLLMITHDRYFLDRVVNKTLE 227
Cdd:cd03296 135 AQ----LSGGQRQRVALARALAVEPKVLLLDEPFGALDakvrKELRRWLRR-LHDELHvTTVFVTHDQEEALEVADRVVV 209
|
....*.
gi 928932812 228 LDDGKI 233
Cdd:cd03296 210 MNKGRI 215
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
346-469 |
4.43e-16 |
|
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: 75.76 E-value: 4.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 346 RIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIG-----------PTVKIGYFSQESEDmDINLRAIEYIKEKAE-YITTE 413
Cdd:pfam00005 13 ILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDgqdltdderksLRKEIGYVFQDPQL-FPRLTVRENLRLGLLlKGLSK 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 928932812 414 DGIKISASQMMENF---LFSKDLQWTYISKLSGGERRRLYLLRILMDAPNVLILDEPTN 469
Cdd:pfam00005 92 REKDARAEEALEKLglgDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
346-547 |
8.04e-16 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 80.71 E-value: 8.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 346 RIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIGPTVKIGYFSQES---EDMDINLRAI----EYIKEKAE----Y----I 410
Cdd:PRK15064 29 RYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQfafEEFTVLDTVImghtELWEVKQErdriYalpeM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 411 TTEDGIKIS-----------------ASQMMENFLFSKDLQWTYISKLSGGERRRLYLLRILMDAPNVLILDEPTNDLDI 473
Cdd:PRK15064 109 SEEDGMKVAdlevkfaemdgytaearAGELLLGVGIPEEQHYGLMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDI 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 928932812 474 DTLKVLENYIDDFNGIVICVSHDRYFLDRICNKIfffaGD---GKIIEHTGNYSDFYKSGRWIHEEIKEEkNTKKSA 547
Cdd:PRK15064 189 NTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHM----ADldyGELRVYPGNYDEYMTAATQARERLLAD-NAKKKA 260
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
318-517 |
9.82e-16 |
|
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: 77.39 E-value: 9.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 318 IIEINHISKSFEQNKVIEDFSyIALKDDRI-GIIGKNGTGKSTLLNLITGKLTPDLGSIDIG-------PTV----KIGY 385
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVS-LSLPPGEVtALLGPNGSGKSTLLRALAGLLKPSSGEVLLDgrdlaslSRRelarRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 386 FSQESEDmDINLRAIEYIK------EKAEYITTEDGIKIsASQMMEnfLFS-KDLQWTYISKLSGGErrrlyllrilmdA 458
Cdd:COG1120 80 VPQEPPA-PFGLTVRELVAlgryphLGLFGRPSAEDREA-VEEALE--RTGlEHLADRPVDELSGGErqrvliaralaqE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 928932812 459 PNVLILDEPTNDLDI----DTLKVLENYIDDFNGIVICVSHDryfLD---RICNKIFFFAgDGKII 517
Cdd:COG1120 156 PPLLLLDEPTSHLDLahqlEVLELLRRLARERGRTVVMVLHD---LNlaaRYADRLVLLK-DGRIV 217
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
3-233 |
1.08e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 76.78 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISKSYGEKIL----FENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKMaieyLSQnpefd 78
Cdd:PRK11629 5 LLQCDNLCKRYQEGSVqtdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQP----MSK----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 79 pnatiLEQVFKSD--SQIMNVIRDYENILeeisqnPDDSTLQK-KLLYLTDNMNAQdawEIENQVKTILTKLGI-HNFHQ 154
Cdd:PRK11629 76 -----LSSAAKAElrNQKLGFIYQFHHLL------PDFTALENvAMPLLIGKKKPA---EINSRALEMLAAVGLeHRANH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 155 KIETLSGGQKKRVALASALISPCDLLILDEPTNHMDH---DTIDWLEKYLTNRTGS-LLMITHDRYFLDRvVNKTLELDD 230
Cdd:PRK11629 142 RPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDArnaDSIFQLLGELNRLQGTaFLVVTHDLQLAKR-MSRQLEMRD 220
|
...
gi 928932812 231 GKI 233
Cdd:PRK11629 221 GRL 223
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
342-517 |
1.14e-15 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 76.18 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 342 LKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIGPTVkigYF-SQESEDMDINLRAIEYI------------KEKAE 408
Cdd:cd03297 21 LNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTV---LFdSRKKINLPPQQRKIGLVfqqyalfphlnvRENLA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 409 YITTEDG---IKISASQMMENFLFSKdLQWTYISKLSGGERRRLYLLRILMDAPNVLILDEPTNDLDIDTLKVLENYID- 484
Cdd:cd03297 98 FGLKRKRnreDRISVDELLDLLGLDH-LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKq 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 928932812 485 ---DFNGIVICVSHDRYFLDRICNKIFFFAgDGKII 517
Cdd:cd03297 177 ikkNLNIPVIFVTHDLSEAEYLADRIVVME-DGRLQ 211
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
2-247 |
1.16e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 77.04 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 2 NILSVENISKSY----------------------GEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGK 59
Cdd:COG1134 3 SMIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 60 VHMPSKMA--IEyLSQNpeFDPNATILEQVFKSdSQIMNVIR-DYENILEEIsqnpddstlqkkllyltdnmnaqdaweI 136
Cdd:COG1134 83 VEVNGRVSalLE-LGAG--FHPELTGRENIYLN-GRLLGLSRkEIDEKFDEI---------------------------V 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 137 EnqvktiLTKLGIHnFHQKIETLSGGQKKRVALASALISPCDLLILDEPTNHMDHD----TIDWLEKyLTNRTGSLLMIT 212
Cdd:COG1134 132 E------FAELGDF-IDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIRE-LRESGRTVIFVS 203
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 928932812 213 HDRYFLDRVVNKTLELDDGKIYSY------IGNYSQFIEKK 247
Cdd:COG1134 204 HSMGAVRRLCDRAIWLEKGRLVMDgdpeevIAAYEALLAGR 244
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-247 |
1.16e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 80.25 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSY--GEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVhmpskmaieYLSQNP--EFDp 79
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEI---------LLNGQPiaDYS- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 80 natilEQVFKsdsQIMNVIrdyenileeiSQNPD--DSTLQKKLLYLTDNmnAQDAweienQVKTILTKLGIHNFHQKIE 157
Cdd:PRK11160 409 -----EAALR---QAISVV----------SQRVHlfSATLRDNLLLAAPN--ASDE-----ALIEVLQQVGLEKLLEDDK 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 158 -----------TLSGGQKKRVALASALISPCDLLILDEPTNHMDHDT----IDWLEKYLTNRTgsLLMITHDRYFL---D 219
Cdd:PRK11160 464 glnawlgeggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETerqiLELLAEHAQNKT--VLMITHRLTGLeqfD 541
|
250 260
....*....|....*....|....*...
gi 928932812 220 RVVnktlELDDGKIYSYiGNYSQFIEKK 247
Cdd:PRK11160 542 RIC----VMDNGQIIEQ-GTHQELLAQQ 564
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
2-213 |
1.21e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 76.07 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 2 NILSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSK--------MAIEYLSQ 73
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGdiddpdvaEACHYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 74 NPEFDPNATILEQV-FKSDsqimnvirdyenileeisqnpddstlqkklLYLTDNMNAQDAweienqvktiLTKLGIHN- 151
Cdd:PRK13539 81 RNAMKPALTVAENLeFWAA------------------------------FLGGEELDIAAA----------LEAVGLAPl 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 928932812 152 FHQKIETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYLT---NRTGSLLMITH 213
Cdd:PRK13539 121 AHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRahlAQGGIVIAATH 185
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-512 |
1.24e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 80.24 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 32 IGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKMA--IEYLSqnpefdpnATILEQVFK--SDSQImNVIRDYENIlEE 107
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSGELIPNLGDYEEEPSWDevLKRFR--------GTELQNYFKklYNGEI-KVVHKPQYV-DL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 108 ISQNPDDSTlqKKLLYLTDNMNAQDAweienqvktILTKLGIHNF-HQKIETLSGGQKKRVALASALISPCDLLILDEPT 186
Cdd:PRK13409 172 IPKVFKGKV--RELLKKVDERGKLDE---------VVERLGLENIlDRDISELSGGELQRVAIAAALLRDADFYFFDEPT 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 187 NHMD-------HDTIdwlEKYLTNRtgSLLMITHDRYFLDR----------------VVNKTLELDDGkIYSYIGNYsqf 243
Cdd:PRK13409 241 SYLDirqrlnvARLI---RELAEGK--YVLVVEHDLAVLDYladnvhiaygepgaygVVSKPKGVRVG-INEYLKGY--- 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 244 iekklerktLESsiERKRERlyKKELEwiragaqarstkqkariqrFEElkntSSPIHDSNIDIcvahsrlgqkIIEINH 323
Cdd:PRK13409 312 ---------LPE--ENMRIR--PEPIE-------------------FEE----RPPRDESERET----------LVEYPD 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 324 ISKSFEQNKVIEDFSYIAlKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDigPTVKIGYFSQesedmdinlraieYI 403
Cdd:PRK13409 346 LTKKLGDFSLEVEGGEIY-EGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD--PELKISYKPQ-------------YI 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 404 KEKAEyITTEDGIKISASQMMENFLFS---KDLQWT-----YISKLSGGERRRLYLLRI-LMDApNVLILDEPTNDLDID 474
Cdd:PRK13409 410 KPDYD-GTVEDLLRSITDDLGSSYYKSeiiKPLQLErlldkNVKDLSGGELQRVAIAAClSRDA-DLYLLDEPSAHLDVE 487
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 928932812 475 ----TLKVLENYIDDFNGIVICVSHDRYFLDRICNKIFFFAG 512
Cdd:PRK13409 488 qrlaVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMVFEG 529
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-250 |
1.32e-15 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 76.59 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 1 MNIlSVENISKSYGE-KILFeNISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMpskmaieylsQNPEFDP 79
Cdd:COG4161 1 MSI-QLKNINCFYGShQALF-DINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNI----------AGHQFDF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 80 NATIleqvfkSDSQIMNVIRDYENILEEISQNPDDSTLQK------KLLyltdNMNAQDAWEienQVKTILTKLGIHNFH 153
Cdd:COG4161 69 SQKP------SEKAIRLLRQKVGMVFQQYNLWPHLTVMENlieapcKVL----GLSKEQARE---KAMKLLARLRLTDKA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 154 QKIET-LSGGQKKRVALASALISPCDLLILDEPTNHMDH-------DTIDWLEKyltnrTG-SLLMITHDRYFLDRVVNK 224
Cdd:COG4161 136 DRFPLhLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPeitaqvvEIIRELSQ-----TGiTQVIVTHEVEFARKVASQ 210
|
250 260
....*....|....*....|....*.
gi 928932812 225 TLELDDGKIYSYiGNYSQFIEKKLER 250
Cdd:COG4161 211 VVYMEKGRIIEQ-GDASHFTQPQTEA 235
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-233 |
1.56e-15 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the 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: 77.11 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYGEKILFE-----NISFSIGDTDKIGLIGVNGTGKSSLLK-------------IIAGYDVADTGKVHMPS- 64
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPFEkkaldDVSLTIEDGEFVAIIGHTGSGKSTLIQhlngllkptsgtvTIDGRDITAKKKKKLKDl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 65 KMAIEYLSQNPEfdpnatilEQVFKsdsqimnvirdyENILEEISQNPDdstlqkkllyltdNMNAQDAwEIENQVKTIL 144
Cdd:TIGR04521 81 RKKVGLVFQFPE--------HQLFE------------ETVYKDIAFGPK-------------NLGLSEE-EAEERVKEAL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 145 TKLGI--HNFHQKIETLSGGQKKRVALASALISPCDLLILDEPTNHMD---HDTI-DWLEKYLTNRTGSLLMITHDRYFL 218
Cdd:TIGR04521 127 ELVGLdeEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDpkgRKEIlDLFKRLHKEKGLTVILVTHSMEDV 206
|
250
....*....|....*
gi 928932812 219 DRVVNKTLELDDGKI 233
Cdd:TIGR04521 207 AEYADRVIVMHKGKI 221
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
11-236 |
1.72e-15 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 76.03 E-value: 1.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 11 KSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKMA--IEYlsqNPEFDPNATILEQVF 88
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSslLGL---GGGFNPELTGRENIY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 89 KSDSqIMNVIRDY-ENILEEISQnpddstlqkkllyltdnmnaqdaweienqvktiLTKLGIHnFHQKIETLSGGQKKRV 167
Cdd:cd03220 107 LNGR-LLGLSRKEiDEKIDEIIE---------------------------------FSELGDF-IDLPVKTYSSGMKARL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 928932812 168 ALASALISPCDLLILDEPTNHMD-------HDTIdwleKYLTNRTGSLLMITHDRYFLDRVVNKTLELDDGKIYSY 236
Cdd:cd03220 152 AFAIATALEPDILLIDEVLAVGDaafqekcQRRL----RELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
12-233 |
1.86e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 79.50 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 12 SYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGY-----------------DVADTGKvhmpskmAIEYLSQN 74
Cdd:PRK11174 359 SPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFlpyqgslkingielrelDPESWRK-------HLSWVGQN 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 75 PEFdPNATILEQVF-----KSDSQIMNVIRDyENILEEISQNPD--DSTLQKkllyltdnmnaQDAweienqvktiltkl 147
Cdd:PRK11174 432 PQL-PHGTLRDNVLlgnpdASDEQLQQALEN-AWVSEFLPLLPQglDTPIGD-----------QAA-------------- 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 148 gihnfhqkieTLSGGQKKRVALASALISPCDLLILDEPTNHMDHDT----IDWLEKYLTNRTgsLLMITHDRYFLDRvVN 223
Cdd:PRK11174 485 ----------GLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSeqlvMQALNAASRRQT--TLMVTHQLEDLAQ-WD 551
|
250
....*....|
gi 928932812 224 KTLELDDGKI 233
Cdd:PRK11174 552 QIWVMQDGQI 561
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
318-496 |
2.34e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 76.31 E-value: 2.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 318 IIEINHISKSFEQNKVIEDFSyIALKDDRI-GIIGKNGTGKSTLLNLITGKLTPDLGSIDIGPTVKIGYFSQE-SEDMDI 395
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVS-LELKPGKIlTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKlYLDTTL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 396 NLRAIEYIKEKAEyiTTEDGIKISASQMMENFLFSKDLQwtyisKLSGGERRRLYLLRILMDAPNVLILDEPTNDLDIDT 475
Cdd:PRK09544 83 PLTVNRFLRLRPG--TKKEDILPALKRVQAGHLIDAPMQ-----KLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNG 155
|
170 180
....*....|....*....|....*
gi 928932812 476 LKVLENYID----DFNGIVICVSHD 496
Cdd:PRK09544 156 QVALYDLIDqlrrELDCAVLMVSHD 180
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
320-507 |
2.44e-15 |
|
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: 75.26 E-value: 2.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 320 EINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDI--GPTVK----IGYFSQ-ESED 392
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfgKPLEKerkrIGYVPQrRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 393 MDINLRAIEYIKeKAEYITTEDGIKISASQM-----------MENFlfsKDLQwtyISKLSGGERRRLYLLRILMDAPNV 461
Cdd:cd03235 81 RDFPISVRDVVL-MGLYGHKGLFRRLSKADKakvdealervgLSEL---ADRQ---IGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 928932812 462 LILDEPTNDLDIDT----LKVLENYIDDFNGIVIcVSHDRYFLDRICNKI 507
Cdd:cd03235 154 LLLDEPFAGVDPKTqediYELLRELRREGMTILV-VTHDLGLVLEYFDRV 202
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
319-519 |
2.73e-15 |
|
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: 76.00 E-value: 2.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSF----EQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDI-GPTV----------KI 383
Cdd:COG1124 2 LEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFdGRPVtrrrrkafrrRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 384 GYFSQESED-MDINLRAIEYIKEkAEYITTEDGIKISASQMMENFLFSKDLQWTYISKLSGGERRRLYLLRILMDAPNVL 462
Cdd:COG1124 82 QMVFQDPYAsLHPRHTVDRILAE-PLRIHGLPDREERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARALILEPELL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 928932812 463 ILDEPTNDLDIDT----LKVLENYIDDFNGIVICVSHDRYFLDRICNKIFFFAgDGKIIEH 519
Cdd:COG1124 161 LLDEPTSALDVSVqaeiLNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQ-NGRIVEE 220
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
318-539 |
4.76e-15 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 75.02 E-value: 4.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 318 IIEINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSI-----DIGPTV---------KI 383
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEIlvdgqDITGLSekelyelrrRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 384 GYFSQES---EDMDI--N----LRaiEY-------IKEKAEYittedgiKISASQMmenflfsKDLQWTYISKLSGGerr 447
Cdd:COG1127 85 GMLFQGGalfDSLTVfeNvafpLR--EHtdlseaeIRELVLE-------KLELVGL-------PGAADKMPSELSGG--- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 448 rlyllrilM------------DaPNVLILDEPTNDLDIDTLKVLENYI----DDFNGIVICVSHDRYFLDRICNKIFFFA 511
Cdd:COG1127 146 --------MrkrvalaralalD-PEILLYDEPTAGLDPITSAVIDELIrelrDELGLTSVVVTHDLDSAFAIADRVAVLA 216
|
250 260
....*....|....*....|....*...
gi 928932812 512 gDGKIIEHtGNYSDFYKSGrwiHEEIKE 539
Cdd:COG1127 217 -DGKIIAE-GTPEELLASD---DPWVRQ 239
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
8-213 |
6.93e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 76.41 E-value: 6.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 8 NISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGK-----VHMPSK-----MAIEYLSQNPEF 77
Cdd:PRK13536 46 GVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKitvlgVPVPARarlarARIGVVPQFDNL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 78 DPNATILEQVFKSDSQIMNVIRDYENILeeisqnpddstlqKKLLyltdnmnaqDAWEIENQVKTiltklgihnfhqKIE 157
Cdd:PRK13536 126 DLEFTVRENLLVFGRYFGMSTREIEAVI-------------PSLL---------EFARLESKADA------------RVS 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 158 TLSGGQKKRVALASALISPCDLLILDEPTNHMD----HDTIDWLEKYLTnRTGSLLMITH 213
Cdd:PRK13536 172 DLSGGMKRRLTLARALINDPQLLILDEPTTGLDpharHLIWERLRSLLA-RGKTILLTTH 230
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-250 |
7.95e-15 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 74.64 E-value: 7.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISKSYGE-KILFENISFSIGDTDKIGLIGVNGTGKSSLLKII-------------AGYDVADTGKVHMPS-KMA 67
Cdd:TIGR02315 1 MLEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCInrlvepssgsillEGTDITKLRGKKLRKlRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 68 IEYLSQNPEFDPNATILEQVFKSDSQIMNVIRDYENILEEisqnpddstlqkkllylTDNMNAQDAweienqvktiLTKL 147
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHGRLGYKPTWRSLLGRFSE-----------------EDKERALSA----------LERV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 148 GIHNF-HQKIETLSGGQKKRVALASALISPCDLLILDEPTNHMD----HDTIDWLeKYLTNRTGSLLMIT-HD----RYF 217
Cdd:TIGR02315 134 GLADKaYQRADQLSGGQQQRVAIARALAQQPDLILADEPIASLDpktsKQVMDYL-KRINKEDGITVIINlHQvdlaKKY 212
|
250 260 270
....*....|....*....|....*....|...
gi 928932812 218 LDRVVNktleLDDGKIYsYIGNYSQFIEKKLER 250
Cdd:TIGR02315 213 ADRIVG----LKAGEIV-FDGAPSELDDEVLRH 240
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-233 |
8.57e-15 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 74.32 E-value: 8.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISKSY-GEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMpskmaieyLSQNPEFDPNA 81
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILV--------DGQDVTALRGR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 82 TILEQ------VFksdsQIMNVIRD---YENILeeISQNPDDSTLQK--KLLYLTDNMNAQDAweienqvktiLTKLGIH 150
Cdd:COG3638 74 ALRRLrrrigmIF----QQFNLVPRlsvLTNVL--AGRLGRTSTWRSllGLFPPEDRERALEA----------LERVGLA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 151 NF-HQKIETLSGGQKKRVALASALISPCDLLILDEPTNHMD----HDTIDWLEKyLTNRTG-SLLMITHD-----RYFlD 219
Cdd:COG3638 138 DKaYQRADQLSGGQQQRVAIARALVQEPKLILADEPVASLDpktaRQVMDLLRR-IAREDGiTVVVNLHQvdlarRYA-D 215
|
250
....*....|....
gi 928932812 220 RVVNktleLDDGKI 233
Cdd:COG3638 216 RIIG----LRDGRV 225
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
319-515 |
1.04e-14 |
|
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: 72.60 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIGptvkigyfsqeSEDMDINLR 398
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILID-----------GEDLTDLED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 399 AIEYIKEKAEYITtEDGIKISASQMMENFLFSkdlqwtyiskLSGGERRRLYLLRILMDAPNVLILDEPTNDLD----ID 474
Cdd:cd03229 70 ELPPLRRRIGMVF-QDFALFPHLTVLENIALG----------LSGGQQQRVALARALAMDPDVLLLDEPTSALDpitrRE 138
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 928932812 475 TLKVLENYIDDFNGIVICVSHDRYFLDRICNKIFFFAgDGK 515
Cdd:cd03229 139 VRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLR-DGK 178
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-215 |
1.18e-14 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 76.03 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKV--------HMPS-KMAIEYLSQ 73
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQImldgvdlsHVPPyQRPINMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 74 NPEFDPNATIlEQvfksdsqimnvirdyeNILEEISQNpddsTLQKKllyltdnmnaqdawEIENQVKTILTKLGIHNF- 152
Cdd:PRK11607 99 SYALFPHMTV-EQ----------------NIAFGLKQD----KLPKA--------------EIASRVNEMLGLVHMQEFa 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 928932812 153 HQKIETLSGGQKKRVALASALISPCDLLILDEPT--------NHMDHDTIDWLEkyltnRTG-SLLMITHDR 215
Cdd:PRK11607 144 KRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMgaldkklrDRMQLEVVDILE-----RVGvTCVMVTHDQ 210
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-233 |
1.50e-14 |
|
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: 71.86 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYG--EKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKV---HMPSKMA--------IEY 70
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVrldGADISQWdpnelgdhVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 71 LSQNPE-FDpnATILEqvfksdsqimnvirdyeNILeeisqnpddstlqkkllyltdnmnaqdaweienqvktiltklgi 149
Cdd:cd03246 81 LPQDDElFS--GSIAE-----------------NIL-------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 150 hnfhqkietlSGGQKKRVALASALI-SPCdLLILDEPTNHMDHDTIDWLE---KYLTNRTGSLLMITHdRYFLDRVVNKT 225
Cdd:cd03246 98 ----------SGGQRQRLGLARALYgNPR-ILVLDEPNSHLDVEGERALNqaiAALKAAGATRIVIAH-RPETLASADRI 165
|
....*...
gi 928932812 226 LELDDGKI 233
Cdd:cd03246 166 LVLEDGRV 173
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-232 |
1.52e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 74.84 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKMAieylsqnPEFDPNAt 82
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV-------PSRARHA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 83 ileqvfksdSQIMNVIRDYENIleeisqNPDDSTLQKKLLYltDNMNAQDAWEIENQVKTILTKLGIHN-FHQKIETLSG 161
Cdd:PRK13537 79 ---------RQRVGVVPQFDNL------DPDFTVRENLLVF--GRYFGLSAAAARALVPPLLEFAKLENkADAKVGELSG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 928932812 162 GQKKRVALASALISPCDLLILDEPTNHMD----HDTIDWLeKYLTNRTGSLLMITHDRYFLDRVVNKTLELDDGK 232
Cdd:PRK13537 142 GMKRRLTLARALVNDPDVLVLDEPTTGLDpqarHLMWERL-RSLLARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-214 |
1.73e-14 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 73.58 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHmpskmaieyLSQNPEFDPNAt 82
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSIT---------LDGKPVEGPGA- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 83 ilEQ--VFKSDSQImnvirDYENILEEISQNpddstLQkkllyltdnMNAQDAWEIENQVKTILTKLGIHNFHQK-IETL 159
Cdd:PRK11248 71 --ERgvVFQNEGLL-----PWRNVQDNVAFG-----LQ---------LAGVEKMQRLEIAHQMLKKVGLEGAEKRyIWQL 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 928932812 160 SGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYLT---NRTGS-LLMITHD 214
Cdd:PRK11248 130 SGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLklwQETGKqVLLITHD 188
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-233 |
2.09e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 73.58 E-value: 2.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISKSYG-----EKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKV--------HMPS-KMAi 68
Cdd:COG1101 1 MLELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSIlidgkdvtKLPEyKRA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 69 EYLS---QNPEFD--PNATILeqvfksdsqimnvirdyENILeeISQNpddstlQKKLLYLTDNMNAQDAWEIENQVKTI 143
Cdd:COG1101 80 KYIGrvfQDPMMGtaPSMTIE-----------------ENLA--LAYR------RGKRRGLRRGLTKKRRELFRELLATL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 144 ltKLGIHN-FHQKIETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKyLTNR---TGSL--LMITHD-RY 216
Cdd:COG1101 135 --GLGLENrLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLE-LTEKiveENNLttLMVTHNmEQ 211
|
250
....*....|....*..
gi 928932812 217 FLDrVVNKTLELDDGKI 233
Cdd:COG1101 212 ALD-YGNRLIMMHEGRI 227
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-214 |
2.35e-14 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 73.36 E-value: 2.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 1 MNILSVENISKSYG----EKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHmpskmaieyLSQNPE 76
Cdd:COG4525 1 MSMLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEIT---------LDGVPV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 77 FDPNAtilEQ--VFKSDSQI--MNVIrdyENIleeisqnpddsTLQKKLlyltdnmNAQDAWEIENQVKTILTKLGIHNF 152
Cdd:COG4525 72 TGPGA---DRgvVFQKDALLpwLNVL---DNV-----------AFGLRL-------RGVPKAERRARAEELLALVGLADF 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 928932812 153 HQK-IETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYLT---NRTG-SLLMITHD 214
Cdd:COG4525 128 ARRrIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLdvwQRTGkGVFLITHS 194
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
318-519 |
2.92e-14 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 72.54 E-value: 2.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 318 IIEINHISKSFE----QNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIGPTV------------ 381
Cdd:cd03257 1 LLEVKNLSVSFPtgggSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDllklsrrlrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 382 --KIGYFSQES-EDMDINLRAIEYIKEKAEYITTEDG---IKISASQMMENFLFSKDLQWTYISKLSGGerrrlyllril 455
Cdd:cd03257 81 rkEIQMVFQDPmSSLNPRMTIGEQIAEPLRIHGKLSKkeaRKEAVLLLLVGVGLPEEVLNRYPHELSGG----------- 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 928932812 456 M-------DA----PNVLILDEPTNDLDIDT----LKVLENYIDDFNGIVICVSHDRYFLDRICNKIFFFAgDGKIIEH 519
Cdd:cd03257 150 QrqrvaiaRAlalnPKLLIADEPTSALDVSVqaqiLDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMY-AGKIVEE 227
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-185 |
3.18e-14 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 72.75 E-value: 3.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 1 MNILSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKV--------HMP----SKMAI 68
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIfldgeditHLPmhkrARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 69 EYLSQNPefdpnatileQVFKSdsqiMNVirdYENILeeisqnpddSTLQkkLLYLtdnmnaqDAWEIENQVKTILTKLG 148
Cdd:COG1137 81 GYLPQEA----------SIFRK----LTV---EDNIL---------AVLE--LRKL-------SKKEREERLEELLEEFG 125
|
170 180 190
....*....|....*....|....*....|....*...
gi 928932812 149 I-HNFHQKIETLSGGQKKRVALASALISPCDLLILDEP 185
Cdd:COG1137 126 ItHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-233 |
3.76e-14 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 75.59 E-value: 3.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSY-GEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAG-YDVaDTGKV--------HMP-----SKMAi 68
Cdd:COG1132 340 IEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRfYDP-TSGRIlidgvdirDLTleslrRQIG- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 69 eYLSQNPE-FdpNATILEQV--FK---SDSQIMNVIRDyENILEEISQNPD--Dstlqkkllyltdnmnaqdaweienqv 140
Cdd:COG1132 418 -VVPQDTFlF--SGTIRENIryGRpdaTDEEVEEAAKA-AQAHEFIEALPDgyD-------------------------- 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 141 kTILTKLGIhnfhqkieTLSGGQKKRVALASALISPCDLLILDEPTNHMDHDT----IDWLEKYLTNRTgsLLMITHdRy 216
Cdd:COG1132 468 -TVVGERGV--------NLSGGQRQRIAIARALLKDPPILILDEATSALDTETealiQEALERLMKGRT--TIVIAH-R- 534
|
250 260
....*....|....*....|...
gi 928932812 217 fL------DRVvnktLELDDGKI 233
Cdd:COG1132 535 -LstirnaDRI----LVLDDGRI 552
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
319-508 |
4.12e-14 |
|
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: 71.54 E-value: 4.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSI-------DIGPTVKIGYFSQESe 391
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVlfdgkplDIAARNRIGYLPEER- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 392 dmdiNLRAIEYIKEKAEYITTEDGIKISASQMMENFLFSK----DLQWTYISKLSGGERRRLYLLRILMDAPNVLILDEP 467
Cdd:cd03269 80 ----GLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERlelsEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 928932812 468 TNDLDIDTLKVLENYIDDF---NGIVICVSHDRYFLDRICNKIF 508
Cdd:cd03269 156 FSGLDPVNVELLKDVIRELaraGKTVILSTHQMELVEELCDRVL 199
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
4-231 |
5.43e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 74.84 E-value: 5.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENIS-KSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKMAIEYLSQNPEFdPNAT 82
Cdd:COG4178 363 LALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQRPYL-PLGT 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 83 ILEQVFksdsqimnvirdYENILEEISqnpDD---STLQK-KLLYLTDNMNAQDAWEienqvktiltklgihnfhqkiET 158
Cdd:COG4178 442 LREALL------------YPATAEAFS---DAelrEALEAvGLGHLAERLDEEADWD---------------------QV 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 928932812 159 LSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYLTNR--TGSLLMITHdRYFLDRVVNKTLELDDG 231
Cdd:COG4178 486 LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREElpGTTVISVGH-RSTLAAFHDRVLELTGD 559
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-186 |
6.26e-14 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 71.56 E-value: 6.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHM------PSKMAIEYLS---- 72
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVdgedltDSKKDINKLRrkvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 73 ---QNPEFDPNATILEqvfksdsqimNVirdyenileeisqnpddsTL-QKKLLyltdNMNAQDAweiENQVKTILTKLG 148
Cdd:COG1126 81 mvfQQFNLFPHLTVLE----------NV------------------TLaPIKVK----KMSKAEA---EERAMELLERVG 125
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 928932812 149 I-HNFHQKIETLSGGQKKRVALASAL-ISPcDLLILDEPT 186
Cdd:COG1126 126 LaDKADAYPAQLSGGQQQRVAIARALaMEP-KVMLFDEPT 164
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-214 |
7.16e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 72.08 E-value: 7.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 2 NILSVENISKSY--GEKILfENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMpskMAIEYLSQNPEFDP 79
Cdd:PRK13647 3 NIIEVEDLHFRYkdGTKAL-KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKV---MGREVNAENEKWVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 80 NATILeqVFksdsqimnvirdyenileeisQNPDD----STLQKKLLYLTDNMNAqDAWEIENQVKTILTKLGIHNFHQK 155
Cdd:PRK13647 79 SKVGL--VF---------------------QDPDDqvfsSTVWDDVAFGPVNMGL-DKDEVERRVEEALKAVRMWDFRDK 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 928932812 156 IET-LSGGQKKRVALASALISPCDLLILDEPTNHMD---HDTIDWLEKYLTNRTGSLLMITHD 214
Cdd:PRK13647 135 PPYhLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDprgQETLMEILDRLHNQGKTVIVATHD 197
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
319-529 |
1.12e-13 |
|
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: 70.99 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSI-----DIGPTV---------KIG 384
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVlidgeDISGLSeaelyrlrrRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 385 YFSQES---EDMDI------NLRaiEYIKEKAEYITtedgiKISASQM-MENFLFSKDLqwtYISKLSGGERRRLYLLRI 454
Cdd:cd03261 81 MLFQSGalfDSLTVfenvafPLR--EHTRLSEEEIR-----EIVLEKLeAVGLRGAEDL---YPAELSGGMKKRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 928932812 455 LMDAPNVLILDEPTNDLDIDTLKVLENYI----DDFNGIVICVSHDRYFLDRICNKIFFFAgDGKIIEhTGNYSDFYKS 529
Cdd:cd03261 151 LALDPELLLYDEPTAGLDPIASGVIDDLIrslkKELGLTSIMVTHDLDTAFAIADRIAVLY-DGKIVA-EGTPEELRAS 227
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-264 |
1.20e-13 |
|
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: 70.57 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 20 ENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKmaieylsQNPEFDPNATIleqVFKSDSQI--MNV 97
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGK-------QITEPGPDRMV---VFQNYSLLpwLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 98 irdYENI-LEEISQNPDDSTLQKKLLyltdnmnaqdaweIENQVKtiLTKLGiHNFHQKIETLSGGQKKRVALASALISP 176
Cdd:TIGR01184 72 ---RENIaLAVDRVLPDLSKSERRAI-------------VEEHIA--LVGLT-EAADKRPGQLSGGMKQRVAIARALSIR 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 177 CDLLILDEPTNHMDHDTIDWLEKYLTN----RTGSLLMITHD---RYFL-DRVVNKTleldDGKiYSYIGnysqfiekkl 248
Cdd:TIGR01184 133 PKVLLLDEPFGALDALTRGNLQEELMQiweeHRVTVLMVTHDvdeALLLsDRVVMLT----NGP-AANIG---------- 197
|
250
....*....|....*.
gi 928932812 249 erKTLESSIERKRERL 264
Cdd:TIGR01184 198 --QILEVPFPRPRDRL 211
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
13-233 |
1.46e-13 |
|
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: 70.44 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 13 YGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHM----PSKMAIEYLSQnpefdpnatiLEQVF 88
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVaglvPWKRRKKFLRR----------IGVVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 89 KSDSQI---MNVIRDYeNILEEISQNPDDStLQKKLLYLTDNMNAQDaweienqvktILtklgihnfHQKIETLSGGQKK 165
Cdd:cd03267 101 GQKTQLwwdLPVIDSF-YLLAAIYDLPPAR-FKKRLDELSELLDLEE----------LL--------DTPVRQLSLGQRM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 928932812 166 RVALASALISPCDLLILDEPTNHMD----HDTIDWLEKYLTNRTGSLLMITHDRYFLDRVVNKTLELDDGKI 233
Cdd:cd03267 161 RAEIAAALLHEPEILFLDEPTIGLDvvaqENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-234 |
1.47e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 70.38 E-value: 1.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 23 SFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHM---------PSKMAIEYLSQNPEFDPNATIlEQvfksdsq 93
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLngqdhtttpPSRRPVSMLFQENNLFSHLTV-AQ------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 94 imnvirdyeNIleEISQNPDdstlqkklLYLTDnmnAQDAweienQVKTILTKLGIHNFHQKIET-LSGGQKKRVALASA 172
Cdd:PRK10771 91 ---------NI--GLGLNPG--------LKLNA---AQRE-----KLHAIARQMGIEDLLARLPGqLSGGQRQRVALARC 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 928932812 173 LISPCDLLILDEPTNHMD----HDTIDWLEKYLTNRTGSLLMITHDryfLD---RVVNKTLELDDGKIY 234
Cdd:PRK10771 144 LVREQPILLLDEPFSALDpalrQEMLTLVSQVCQERQLTLLMVSHS---LEdaaRIAPRSLVVADGRIA 209
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-512 |
1.73e-13 |
|
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: 73.28 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 32 IGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPS--KMAIEYLSqnpefdpnATILEQVFK--SDSQImNVIRDYENIlEE 107
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGELKPNLGDYDEEPswDEVLKRFR--------GTELQDYFKklANGEI-KVAHKPQYV-DL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 108 ISQNPDDSTlqKKLLYLTDNmnaqdaweiENQVKTILTKLGIHNF-HQKIETLSGGQKKRVALASALISPCDLLILDEPT 186
Cdd:COG1245 172 IPKVFKGTV--RELLEKVDE---------RGKLDELAEKLGLENIlDRDISELSGGELQRVAIAAALLRDADFYFFDEPS 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 187 NHMD-------HDTIdwleKYLTNRTGSLLMITHDRYFLDrvvnktlelddgkiysYIgnySQFIEkklerktlessIer 259
Cdd:COG1245 241 SYLDiyqrlnvARLI----RELAEEGKYVLVVEHDLAILD----------------YL---ADYVH-----------I-- 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 260 krerLYKKElewiraGAQARSTKQK-AR--IQRFEE--LKNTSSPIHDSNIDICVAHSRLGQK---IIEINHISKSFEQN 331
Cdd:COG1245 285 ----LYGEP------GVYGVVSKPKsVRvgINQYLDgyLPEENVRIRDEPIEFEVHAPRREKEeetLVEYPDLTKSYGGF 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 332 KVIEDFSYIAlKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDigPTVKIGYFSQE-SEDMDINLRAI--EYIKEKAE 408
Cdd:COG1245 355 SLEVEGGEIR-EGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD--EDLKISYKPQYiSPDYDGTVEEFlrSANTDDFG 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 409 --YITTEDGIKISASQMMENflfskdlqwtYISKLSGGERRRLYLLRILMDAPNVLILDEPTNDLDID----TLKVLENY 482
Cdd:COG1245 432 ssYYKTEIIKPLGLEKLLDK----------NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlaVAKAIRRF 501
|
490 500 510
....*....|....*....|....*....|
gi 928932812 483 IDDFNGIVICVSHDRYFLDRICNKIFFFAG 512
Cdd:COG1245 502 AENRGKTAMVVDHDIYLIDYISDRLMVFEG 531
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
319-516 |
1.84e-13 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 69.83 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFEQNKViedfSYIALKD--------DRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIGPTVkigyFSQES 390
Cdd:cd03255 1 IELKNLSKTYGGGGE----KVQALKGvslsiekgEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTD----ISKLS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 391 EDMDINLRA--IEYI------------------------------KEKAEYITTEDGIKisasqmmenflfskDLQWTYI 438
Cdd:cd03255 73 EKELAAFRRrhIGFVfqsfnllpdltalenvelplllagvpkkerRERAEELLERVGLG--------------DRLNHYP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 439 SKLSGGERRRLYLLRILMDAPNVLILDEPTNDLDIDT----LKVLENYIDDFNGIVICVSHDRyFLDRICNKIFFFAgDG 514
Cdd:cd03255 139 SELSGGQQQRVAIARALANDPKIILADEPTGNLDSETgkevMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELR-DG 216
|
..
gi 928932812 515 KI 516
Cdd:cd03255 217 KI 218
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-235 |
2.08e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 70.81 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 2 NILSVENISKSY--GEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKV---HMPskmaieyLSQnpe 76
Cdd:PRK13635 4 EIIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTItvgGMV-------LSE--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 77 fdpnatilEQVFKSDSQIMNVIrdyenileeisQNPDD----STLQkkllyltDNMnaqdAWEIENQ----------VKT 142
Cdd:PRK13635 74 --------ETVWDVRRQVGMVF-----------QNPDNqfvgATVQ-------DDV----AFGLENIgvpreemverVDQ 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 143 ILTKLGIHNF-HQKIETLSGGQKKRVALASALISPCDLLILDEPTNHMDH-------DTIDWL--EKYLTnrtgsLLMIT 212
Cdd:PRK13635 124 ALRQVGMEDFlNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPrgrrevlETVRQLkeQKGIT-----VLSIT 198
|
250 260
....*....|....*....|....*
gi 928932812 213 HDryfLDRVV--NKTLELDDGKIYS 235
Cdd:PRK13635 199 HD---LDEAAqaDRVIVMNKGEILE 220
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-233 |
3.04e-13 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 69.53 E-value: 3.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISKSYGEK----ILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMpskmaieylsqnpefd 78
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLV---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 79 pNATILEQVFKSD----SQIMNVIRDYENILEE--ISQNpddSTLQKKLLYLTDNmnaqdawEIENQVKTILTKLGIHNF 152
Cdd:cd03258 65 -DGTDLTLLSGKElrkaRRRIGMIFQHFNLLSSrtVFEN---VALPLEIAGVPKA-------EIEERVLELLELVGLEDK 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 153 HQK-IETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDT---IDWLEKYLTNRTG-SLLMITHDRYFLDRVVNKTLE 227
Cdd:cd03258 134 ADAyPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETtqsILALLRDINRELGlTIVLITHEMEVVKRICDRVAV 213
|
....*.
gi 928932812 228 LDDGKI 233
Cdd:cd03258 214 MEKGEV 219
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-190 |
3.35e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 70.04 E-value: 3.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKmAIEYLSQNpEFDPNAT 82
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDK-PISMLSSR-QLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 83 ILEQVFKSDSQImnVIRDyeniLEEISQNPddstlqkkLLYLTDNMNAQDaweiENQVKTILTKLGIHNFHQK-IETLSG 161
Cdd:PRK11231 80 LLPQHHLTPEGI--TVRE----LVAYGRSP--------WLSLWGRLSAED----NARVNQAMEQTRINHLADRrLTDLSG 141
|
170 180
....*....|....*....|....*....
gi 928932812 162 GQKKRVALASALISPCDLLILDEPTNHMD 190
Cdd:PRK11231 142 GQRQRAFLAMVLAQDTPVVLLDEPTTYLD 170
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-236 |
3.48e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 70.22 E-value: 3.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 1 MNILSVENISKSY-GEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSkmaieylsqnpefdp 79
Cdd:PRK13652 1 MHLIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRG--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 80 natilEQVFKSDsqimnvIRDYENILEEISQNPDD----STLQKKLLYLTDNMNAqDAWEIENQVKTILTKLGIHNFHQK 155
Cdd:PRK13652 66 -----EPITKEN------IREVRKFVGLVFQNPDDqifsPTVEQDIAFGPINLGL-DEETVAHRVSSALHMLGLEELRDR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 156 I-ETLSGGQKKRVALASALISPCDLLILDEPTNHMD----HDTIDWLEKYLTNRTGSLLMITHDRYFLDRVVNKTLELDD 230
Cdd:PRK13652 134 VpHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDpqgvKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDK 213
|
....*.
gi 928932812 231 GKIYSY 236
Cdd:PRK13652 214 GRIVAY 219
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-233 |
3.55e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 70.10 E-value: 3.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 1 MNILSVENISKSYGEKILF---------ENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKmAIEYL 71
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGGLSgkhqhqtvlNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGE-PLAKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 72 SQNPEFDPNATIlEQVFKSDSQIMNVIRDYENILEEisqnPddstlQKKLLYLTDNMNAQDAWEIENQVK---TILTKLG 148
Cdd:PRK10419 80 NRAQRKAFRRDI-QMVFQDSISAVNPRKTVREIIRE----P-----LRHLLSLDKAERLARASEMLRAVDlddSVLDKRP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 149 ihnfhqkiETLSGGQKKRVALASALISPCDLLILDEPTNHMD----HDTIDWLEKyLTNRTG-SLLMITHD----RYFLD 219
Cdd:PRK10419 150 --------PQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDlvlqAGVIRLLKK-LQQQFGtACLFITHDlrlvERFCQ 220
|
250
....*....|....
gi 928932812 220 RVvnktLELDDGKI 233
Cdd:PRK10419 221 RV----MVMDNGQI 230
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
34-214 |
3.56e-13 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 68.41 E-value: 3.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 34 LIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKMAIEYLSQNPEFDPN--ATILEQVfksdsqimnvirdyenileEISQN 111
Cdd:NF040873 23 VVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDSlpLTVRDLV-------------------AMGRW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 112 PDDSTLQKkllyltdnMNAQDAWEIENqvktILTKLGIHNF-HQKIETLSGGQKKRVALASALISPCDLLILDEPTNHMD 190
Cdd:NF040873 84 ARRGLWRR--------LTRDDRAAVDD----ALERVGLADLaGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180
....*....|....*....|....*..
gi 928932812 191 HDTIDWLEKYLTNRTG---SLLMITHD 214
Cdd:NF040873 152 AESRERIIALLAEEHArgaTVVVVTHD 178
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
23-233 |
4.63e-13 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 68.73 E-value: 4.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 23 SFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHM---------PSKMAIEYLSQNPEFDPNATIleqvfksdsq 93
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVndqshtglaPYQRPVSMLFQENNLFAHLTV---------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 94 imnvirdYENILEEISQNPDDSTLQKKllyltdnmnaqdaweienQVKTILTKLGIHNFHQKI-ETLSGGQKKRVALASA 172
Cdd:TIGR01277 88 -------RQNIGLGLHPGLKLNAEQQE------------------KVVDAAQQVGIADYLDRLpEQLSGGQRQRVALARC 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 928932812 173 LISPCDLLILDEPTNHMD----HDTIDWLEKYLTNRTGSLLMITHDRYFLDRVVNKTLELDDGKI 233
Cdd:TIGR01277 143 LVRPNPILLLDEPFSALDpllrEEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-214 |
5.19e-13 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 71.62 E-value: 5.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSY-GEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSkmaiEYLSQNPEFDPNAT 82
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDG----VPVSSLDQDEVRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 83 ILeqVFKSDSQIMnvirdyenileeisqnpdDSTLQKKLLYLTDNMNAQDAWEIENQVK-------------TILTKLGI 149
Cdd:TIGR02868 411 VS--VCAQDAHLF------------------DTTVRENLRLARPDATDEELWAALERVGladwlralpdgldTVLGEGGA 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 928932812 150 hnfhqkieTLSGGQKKRVALASALISPCDLLILDEPTNHMDHDT----IDWLEKYLTNRTgsLLMITHD 214
Cdd:TIGR02868 471 --------RLSGGERQRLALARALLADAPILLLDEPTEHLDAETadelLEDLLAALSGRT--VVLITHH 529
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-262 |
5.44e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 69.27 E-value: 5.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGkvhmpSKMAIEYLSQNPEFDpnAT 82
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKS-----AGSHIELLGRTVQRE--GR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 83 ILEQVFKSDSQIMNVIRDYE-----NILEEISQNPDDST-LQKKLLYLTDNMNAQDAWEIenqvktiLTKLGIHNF-HQK 155
Cdd:PRK09984 77 LARDIRKSRANTGYIFQQFNlvnrlSVLENVLIGALGSTpFWRTCFSWFTREQKQRALQA-------LTRVGMVHFaHQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 156 IETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDT----IDWLEKYLTNRTGSLLMITHDRYFLDRVVNKTLELDDG 231
Cdd:PRK09984 150 VSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESarivMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQG 229
|
250 260 270
....*....|....*....|....*....|.
gi 928932812 232 KIYsYIGNYSQFIEKKLERktLESSIERKRE 262
Cdd:PRK09984 230 HVF-YDGSSQQFDNERFDH--LYRSINRVEE 257
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
7-233 |
7.85e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 68.86 E-value: 7.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 7 ENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKMAIEYLSQNpefdpnatileq 86
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKE------------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 87 vfksdsqimnVIRDYeNILEEISQNPDDSTLQKKLL---YLTDNMNAQDAWEIENQVKTILTKLGI-HNFHQKIETLSGG 162
Cdd:PRK10253 79 ----------VARRI-GLLAQNATTPGDITVQELVArgrYPHQPLFTRWRKEDEEAVTKAMQATGItHLADQSVDTLSGG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 928932812 163 QKKRVALASALISPCDLLILDEPTNHMD-HDTIDWLE--KYLTNRTG-SLLMITHDRYFLDRVVNKTLELDDGKI 233
Cdd:PRK10253 148 QRQRAWIAMVLAQETAIMLLDEPTTWLDiSHQIDLLEllSELNREKGyTLAAVLHDLNQACRYASHLIALREGKI 222
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3-233 |
7.92e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 69.34 E-value: 7.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISKSY--GEKILfENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKmAIEYlsqnpefdpn 80
Cdd:PRK13639 1 ILETRDLKYSYpdGTEAL-KGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGE-PIKY---------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 81 atileqvfkSDSQIMNViRDYENIleeISQNPDDS----TLQKKLLYLTDNMNAQDAwEIENQVKTILTKLGIHNFHQKI 156
Cdd:PRK13639 69 ---------DKKSLLEV-RKTVGI---VFQNPDDQlfapTVEEDVAFGPLNLGLSKE-EVEKRVKEALKAVGMEGFENKP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 157 -ETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYLT--NRTGSLLMI-THDRYFLDRVVNKTLELDDGK 232
Cdd:PRK13639 135 pHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYdlNKEGITIIIsTHDVDLVPVYADKVYVMSDGK 214
|
.
gi 928932812 233 I 233
Cdd:PRK13639 215 I 215
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
3-233 |
9.41e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 68.86 E-value: 9.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISKSYGEKI-LFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVhmpskmaieylsqnpefdpna 81
Cdd:PRK13644 1 MIRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKV--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 82 tILEQVFKSDSQIMNVIRDYENIleeISQNPDDS----TLQKKLLYLTDNMnAQDAWEIENQVKTILTKLGIHNF-HQKI 156
Cdd:PRK13644 60 -LVSGIDTGDFSKLQGIRKLVGI---VFQNPETQfvgrTVEEDLAFGPENL-CLPPIEIRKRVDRALAEIGLEKYrHRSP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 157 ETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDT-IDWLE--KYLTNRTGSLLMITHDRYFLdRVVNKTLELDDGKI 233
Cdd:PRK13644 135 KTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSgIAVLEriKKLHEKGKTIVYITHNLEEL-HDADRIIVMDRGKI 213
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-233 |
1.08e-12 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 68.12 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 1 MNIlSVENISKSYGE-KILFeNISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMpskmaieylsQNPEFDP 79
Cdd:PRK11124 1 MSI-QLNGINCFYGAhQALF-DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNI----------AGNHFDF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 80 NATIleqvfkSDSQIMNVIRDYENILEEISQNPDDSTLQK------KLLYLTDNmnaqdawEIENQVKTILTKLGIHNFH 153
Cdd:PRK11124 69 SKTP------SDKAIRELRRNVGMVFQQYNLWPHLTVQQNlieapcRVLGLSKD-------QALARAEKLLERLRLKPYA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 154 QKIET-LSGGQKKRVALASALISPCDLLILDEPTNHMDH-------DTIDWLEKyltnrTG-SLLMITHDRYFLDRVVNK 224
Cdd:PRK11124 136 DRFPLhLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPeitaqivSIIRELAE-----TGiTQVIVTHEVEVARKTASR 210
|
....*....
gi 928932812 225 TLELDDGKI 233
Cdd:PRK11124 211 VVYMENGHI 219
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-233 |
1.39e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 70.22 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISKSY-----GEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHM--------------- 62
Cdd:TIGR03269 279 IIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvdmtkpgpd 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 63 ---PSKMAIEYLSQNPEFDPNATILEqvfksdsqimnvirdyeNILEEIS-QNPDDSTLQKKLLYLtdnmnaQDAWEIEN 138
Cdd:TIGR03269 359 grgRAKRYIGILHQEYDLYPHRTVLD-----------------NLTEAIGlELPDELARMKAVITL------KMVGFDEE 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 139 QVKTILTKLGihnfhqkiETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDT-IDWLEKYLTNR---TGSLLMITHD 214
Cdd:TIGR03269 416 KAEEILDKYP--------DELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITkVDVTHSILKAReemEQTFIIVSHD 487
|
250
....*....|....*....
gi 928932812 215 RYFLDRVVNKTLELDDGKI 233
Cdd:TIGR03269 488 MDFVLDVCDRAALMRDGKI 506
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
319-528 |
1.43e-12 |
|
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: 70.63 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFEQNK--VIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSI--------DIGPTV---KIGY 385
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIlidgidlrQIDPASlrrQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 386 FSQESE-------------DMDINLRAIEYIKEKA---EYITT-EDGIKisaSQMMENFlfskdlqwtyiSKLSGGErrr 448
Cdd:COG2274 554 VLQDVFlfsgtirenitlgDPDATDEEIIEAARLAglhDFIEAlPMGYD---TVVGEGG-----------SNLSGGQ--- 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 449 lyllrilmdA------------PNVLILDEPTNDLDIDT-LKVLENYIDDFNGI-VICVSHDRYFLdRICNKIFFFAgDG 514
Cdd:COG2274 617 ---------RqrlaiarallrnPRILILDEATSALDAETeAIILENLRRLLKGRtVIIIAHRLSTI-RLADRIIVLD-KG 685
|
250 260
....*....|....*....|...
gi 928932812 515 KIIE---------HTGNYSDFYK 528
Cdd:COG2274 686 RIVEdgtheellaRKGLYAELVQ 708
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
319-518 |
2.22e-12 |
|
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: 66.47 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIdigpTVKIGYFSQESEDmdinLR 398
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEI----TFDGKSYQKNIEA----LR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 399 AIEYIKEKAE---YITTEDGIKISASQMM---------ENFLFSKDLQWTYISKLSGGERRRLYLLRILMDAPNVLILDE 466
Cdd:cd03268 73 RIGALIEAPGfypNLTARENLRLLARLLGirkkridevLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 928932812 467 PTNDLDIDTLKVLENYI---DDFNGIVICVSHDRYFLDRICNKIFFFaGDGKIIE 518
Cdd:cd03268 153 PTNGLDPDGIKELRELIlslRDQGITVLISSHLLSEIQKVADRIGII-NKGKLIE 206
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
319-519 |
2.25e-12 |
|
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: 66.45 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFEQNKVIEDFSYIaLKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDI-GPTVK---------IGYFSQ 388
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLT-LGPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIdGQDVLkqpqklrrrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 389 ESeDMDINLRAIEYIkekaEYITTEDGI-----KISASQMME--NFLFSKDlqwTYISKLSGGERRRLYLLRILMDAPNV 461
Cdd:cd03264 80 EF-GVYPNFTVREFL----DYIAWLKGIpskevKARVDEVLElvNLGDRAK---KKIGSLSGGMRRRVGIAQALVGDPSI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 462 LILDEPTNDLDIDTLKVLENYIDDF--NGIVICVSHDRYFLDRICNKIFFFAGdGKIIEH 519
Cdd:cd03264 152 LIVDEPTAGLDPEERIRFRNLLSELgeDRIVILSTHIVEDVESLCNQVAVLNK-GKLVFE 210
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
319-518 |
2.42e-12 |
|
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: 65.80 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFEQN--KVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIGPTvkigyfsqesedmdin 396
Cdd:cd03247 1 LSINNVSFSYPEQeqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGV---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 397 lRAIEYIKEKAEYITTEDgikisasqmMENFLFSKDLQWTYISKLSGGERRRLYLLRILM-DAPnVLILDEPTNDLDIDT 475
Cdd:cd03247 65 -PVSDLEKALSSLISVLN---------QRPYLFDTTLRNNLGRRFSGGERQRLALARILLqDAP-IVLLDEPTVGLDPIT 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 928932812 476 LKVLENYIDDF--NGIVICVSHDRYFLDRIcNKIFFFAgDGKIIE 518
Cdd:cd03247 134 ERQLLSLIFEVlkDKTLIWITHHLTGIEHM-DKILFLE-NGKIIM 176
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
5-233 |
2.74e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 67.32 E-value: 2.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 5 SVENISKSYG--EKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVhmpskmaieylsqnpefdpnat 82
Cdd:PRK13632 9 KVENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEI---------------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 83 ileqvfksdsQIMNVIRDYENILEE------ISQNPDD----STLQKKLLYLTDNMNAqDAWEIENQVKTILTKLGIHNF 152
Cdd:PRK13632 67 ----------KIDGITISKENLKEIrkkigiIFQNPDNqfigATVEDDIAFGLENKKV-PPKKMKDIIDDLAKKVGMEDY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 153 HQK-IETLSGGQKKRVALASALISPCDLLILDEPTNHMD----HDTIDWLEKYLTNRTGSLLMITHDryfLDRVVN--KT 225
Cdd:PRK13632 136 LDKePQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDpkgkREIKKIMVDLRKTRKKTLISITHD---MDEAILadKV 212
|
....*...
gi 928932812 226 LELDDGKI 233
Cdd:PRK13632 213 IVFSEGKL 220
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
8-233 |
3.43e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 66.65 E-value: 3.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 8 NISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKvhmpskMAIEYLSQNpefDPNATILE-- 85
Cdd:PRK09493 6 NVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGD------LIVDGLKVN---DPKVDERLir 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 86 ----QVFksdsQIMNVIrDYENILEEISQNPDDSTLQKKllyltdnmnaQDAweiENQVKTILTKLGI--HNFHQKIEtL 159
Cdd:PRK09493 77 qeagMVF----QQFYLF-PHLTALENVMFGPLRVRGASK----------EEA---EKQARELLAKVGLaeRAHHYPSE-L 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 928932812 160 SGGQKKRVALASALISPCDLLILDEPTNHMD----HDTIDWLeKYLTNRTGSLLMITHDRYFLDRVVNKTLELDDGKI 233
Cdd:PRK09493 138 SGGQQQRVAIARALAVKPKLMLFDEPTSALDpelrHEVLKVM-QDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
4-233 |
3.58e-12 |
|
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: 69.38 E-value: 3.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYG--EKILfENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKM-----------AIEY 70
Cdd:TIGR01193 474 IVINDVSYSYGygSNIL-SDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSlkdidrhtlrqFINY 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 71 LSQNPeFDPNATILEqvfksdsqimnvirdyeNILeeISQNPDDStlQKKLLYLTDNMNAQDawEIENQVKTILTKLGIH 150
Cdd:TIGR01193 553 LPQEP-YIFSGSILE-----------------NLL--LGAKENVS--QDEIWAACEIAEIKD--DIENMPLGYQTELSEE 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 151 NFhqkieTLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYLTNRTGSLLMITHDRYFLDRVVNKTLELDD 230
Cdd:TIGR01193 609 GS-----SISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDKTIIFVAHRLSVAKQSDKIIVLDH 683
|
...
gi 928932812 231 GKI 233
Cdd:TIGR01193 684 GKI 686
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
319-517 |
3.98e-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: 66.07 E-value: 3.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSF--EQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSI-----DIG---PTV---KIGY 385
Cdd:cd03245 3 IEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVlldgtDIRqldPADlrrNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 386 FSQESEDMDINLRaiEYIKEKAEYITTEDGIKIS----ASQMMENFLFSKDLQwtyISK----LSGGERRRLYLLRILMD 457
Cdd:cd03245 83 VPQDVTLFYGTLR--DNITLGAPLADDERILRAAelagVTDFVNKHPNGLDLQ---IGErgrgLSGGQRQAVALARALLN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 928932812 458 APNVLILDEPTNDLDIDT----LKVLENYIDDfnGIVICVSHdRYFLDRICNKIFFFaGDGKII 517
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSeerlKERLRQLLGD--KTLIIITH-RPSLLDLVDRIIVM-DSGRIV 217
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-198 |
5.06e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 67.94 E-value: 5.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 1 MNILSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKmAIEYLSqnpefdpn 80
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGD-DVEALS-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 81 ATILEQVFKSDSQIMNVIRDY--ENILeEISQNPDDSTLqkkllyltDNMNAQDaweiENQVKTILTKLGIHNF-HQKIE 157
Cdd:PRK09536 72 ARAASRRVASVPQDTSLSFEFdvRQVV-EMGRTPHRSRF--------DTWTETD----RAAVERAMERTGVAQFaDRPVT 138
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 928932812 158 TLSGGQKKRVALASALISPCDLLILDEPTNHMD-HDTIDWLE 198
Cdd:PRK09536 139 SLSGGERQRVLLARALAQATPVLLLDEPTASLDiNHQVRTLE 180
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
226-303 |
5.08e-12 |
|
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: 61.82 E-value: 5.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 226 LELDDGKIYSYIGNYSQFIEKKLERKTLESSIERKRERLYKKELEWI-RAGAQARSTKQ-KARIQRFEELKNTSSPIHDS 303
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIdRFRAKASKAKQaQSRIKALEKMERIEKPERDK 80
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
4-214 |
5.52e-12 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 65.58 E-value: 5.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGY---DVADTGKV--------HMPS-KMAIEYL 71
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTlspAFSASGEVllngrrltALPAeQRRIGIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 72 SQNPEFDPNatileqvfksdsqiMNVirdYENIL----EEISQNpddstlQKKllyltdnmnaqdaweieNQVKTILTKL 147
Cdd:COG4136 82 FQDDLLFPH--------------LSV---GENLAfalpPTIGRA------QRR-----------------ARVEQALEEA 121
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 928932812 148 GIHNFHQK-IETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKY----LTNRTGSLLMITHD 214
Cdd:COG4136 122 GLAGFADRdPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFvfeqIRQRGIPALLVTHD 193
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
318-378 |
5.67e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 66.26 E-value: 5.67e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 928932812 318 IIEINHISKSFEQNKVIEDfsyIALKD--------DRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIG 378
Cdd:COG1101 1 MLELKNLSKTFNPGTVNEK---RALDGlnltieegDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILID 66
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-233 |
5.74e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 66.15 E-value: 5.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 2 NILSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSK---MAIEYLSQNPEFD 78
Cdd:PRK10619 4 NKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQtinLVRDKDGQLKVAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 79 PNA-----TILEQVFKSDS--QIMNVIrdyENILEEISQnpddstlqkkLLYLTDNmnaqdawEIENQVKTILTKLGIHN 151
Cdd:PRK10619 84 KNQlrllrTRLTMVFQHFNlwSHMTVL---ENVMEAPIQ----------VLGLSKQ-------EARERAVKYLAKVGIDE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 152 FHQKIET--LSGGQKKRVALASALISPCDLLILDEPTNHMDHDTID---WLEKYLTNRTGSLLMITHDRYFLDRVVNKTL 226
Cdd:PRK10619 144 RAQGKYPvhLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGevlRIMQQLAEEGKTMVVVTHEMGFARHVSSHVI 223
|
....*..
gi 928932812 227 ELDDGKI 233
Cdd:PRK10619 224 FLHQGKI 230
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
7-233 |
6.06e-12 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 65.97 E-value: 6.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 7 ENISKSYG--EKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKV----HMPSKMAIEYLSQNpefdpn 80
Cdd:cd03252 4 EHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVlvdgHDLALADPAWLRRQ------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 81 atiLEQVFKSDSQIMNVIRDyeNIleeISQNPDDStlQKKLLYLTDNMNAQD-AWEIENQVKTILTKLGIhnfhqkieTL 159
Cdd:cd03252 78 ---VGVVLQENVLFNRSIRD--NI---ALADPGMS--MERVIEAAKLAGAHDfISELPEGYDTIVGEQGA--------GL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 928932812 160 SGGQKKRVALASALISPCDLLILDEPTNHMD----HDTIDWLEKYLTNRTgsLLMITHdRYFLDRVVNKTLELDDGKI 233
Cdd:cd03252 140 SGGQRQRIAIARALIHNPRILIFDEATSALDyeseHAIMRNMHDICAGRT--VIIIAH-RLSTVKNADRIIVMEKGRI 214
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
319-515 |
6.18e-12 |
|
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: 64.33 E-value: 6.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSF--EQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIGptvkigyfsqesedmDIN 396
Cdd:cd03228 1 IEFKNVSFSYpgRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILID---------------GVD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 397 LRAI--EYIKEKAEYIttedgikisaSQmmENFLFSKDLqwtyisK---LSGGErrrlyllrilmdA------------P 459
Cdd:cd03228 66 LRDLdlESLRKNIAYV----------PQ--DPFLFSGTI------ReniLSGGQ------------RqriaiarallrdP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 928932812 460 NVLILDEPTNDLDIDTLKVLENYIDDFNG--IVICVSHdRYFLDRICNKIFFFaGDGK 515
Cdd:cd03228 116 PILILDEATSALDPETEALILEALRALAKgkTVIVIAH-RLSTIRDADRIIVL-DDGR 171
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-222 |
6.54e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 67.42 E-value: 6.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 1 MNIlSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMpskmaieylsqnpefdpN 80
Cdd:PRK10851 1 MSI-EIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRF-----------------H 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 81 ATILEQVFKSDSQIMNVIRDY---------ENILEEIS-----QNPDDSTLQKKLLYLTDnmnaqdaweienqvktiLTK 146
Cdd:PRK10851 63 GTDVSRLHARDRKVGFVFQHYalfrhmtvfDNIAFGLTvlprrERPNAAAIKAKVTQLLE-----------------MVQ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 147 LGiHNFHQKIETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYLTNRTGSL----LMITHDRY----FL 218
Cdd:PRK10851 126 LA-HLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELkftsVFVTHDQEeameVA 204
|
....
gi 928932812 219 DRVV 222
Cdd:PRK10851 205 DRVV 208
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
317-377 |
6.55e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 65.87 E-value: 6.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 317 KIIEINHISKSF-----EQNKVIEDFS---------YIALKD--------DRIGIIGKNGTGKSTLLNLITGKLTPDLGS 374
Cdd:COG1134 3 SMIEVENVSKSYrlyhePSRSLKELLLrrrrtrreeFWALKDvsfevergESVGIIGRNGAGKSTLLKLIAGILEPTSGR 82
|
...
gi 928932812 375 IDI 377
Cdd:COG1134 83 VEV 85
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-233 |
7.19e-12 |
|
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: 65.28 E-value: 7.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKvhmPSKMAIEYLSQNPeFDPNATI 83
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGA---PDEGEVLLDGKDI-YDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 84 LE------QVFksdsQIMNVIRD--YENI-----LEEISQNPDDSTLQKKLL---YLTDNmnaqdaweienqVKTILTKL 147
Cdd:cd03260 77 LElrrrvgMVF----QKPNPFPGsiYDNVayglrLHGIKLKEELDERVEEALrkaALWDE------------VKDRLHAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 148 GihnfhqkietLSGGQKKRVALASALISPCDLLILDEPTNHMD-------HDTIDWLEKYLTnrtgsLLMITHDRYFLDR 220
Cdd:cd03260 141 G----------LSGGQQQRLCLARALANEPEVLLLDEPTSALDpistakiEELIAELKKEYT-----IVIVTHNMQQAAR 205
|
250
....*....|...
gi 928932812 221 VVNKTLELDDGKI 233
Cdd:cd03260 206 VADRTAFLLNGRL 218
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
6-266 |
7.82e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 66.57 E-value: 7.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 6 VENISKSYGEKILFE-----NISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGkvhmpskmaieylsqnpefdpn 80
Cdd:PRK13645 9 LDNVSYTYAKKTPFEfkalnNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETG---------------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 81 atileQVFKSDSQI---MNVIRDYENILEEIS---QNPD----DSTLQKKLLYLTDNMNAqDAWEIENQVKTILTKLGIH 150
Cdd:PRK13645 67 -----QTIVGDYAIpanLKKIKEVKRLRKEIGlvfQFPEyqlfQETIEKDIAFGPVNLGE-NKQEAYKKVPELLKLVQLP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 151 NFHQKIE--TLSGGQKKRVALASALISPCDLLILDEPTNHMD----HDTIDWLEKYLTNRTGSLLMITHDRYFLDRVVNK 224
Cdd:PRK13645 141 EDYVKRSpfELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDpkgeEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADE 220
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 928932812 225 TLELDDGKIYSYIGNYSQFIEKKLERKtlessIERKRERLYK 266
Cdd:PRK13645 221 VIVMHEGKVISIGSPFEIFSNQELLTK-----IEIDPPKLYQ 257
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-186 |
9.10e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 67.74 E-value: 9.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISKSY-GEKILfENISFSI--GdtdKI-GLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKmaieylsqnpefd 78
Cdd:COG1129 4 LLEMRGISKSFgGVKAL-DGVSLELrpG---EVhALLGENGAGKSTLMKILSGVYQPDSGEILLDGE------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 79 pnatilEQVFKS--DS---------QIMNVIRD---YENIL--EEISQNPddsTLQKKLLYltdnmnaQDAweienqvKT 142
Cdd:COG1129 67 ------PVRFRSprDAqaagiaiihQELNLVPNlsvAENIFlgREPRRGG---LIDWRAMR-------RRA-------RE 123
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 928932812 143 ILTKLGIH-NFHQKIETLSGGQKKRVALASALISPCDLLILDEPT 186
Cdd:COG1129 124 LLARLGLDiDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPT 168
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
34-251 |
9.38e-12 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 66.75 E-value: 9.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 34 LIGVNGTGKSSLLKIIAGYDVADTGKVhmpsKMAIEYLSQNPefdPNATILEQVFKSDSQI--MNVirdYENILEEIsqn 111
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSI----MLDGEDVTNVP---PHLRHINMVFQSYALFphMTV---EENVAFGL--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 112 pddstlqkkllyltdNMNAQDAWEIENQVKTILTKLGIHNFHQ-KIETLSGGQKKRVALASALISPCDLLILDEPTNHMD 190
Cdd:TIGR01187 68 ---------------KMRKVPRAEIKPRVLEALRLVQLEEFADrKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALD 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 191 HDTIDWLE---KYLTNRTG-SLLMITHDR----YFLDRVV----NKTLELDDGK-IYS---------YIGNYSQFIEKKL 248
Cdd:TIGR01187 133 KKLRDQMQlelKTIQEQLGiTFVFVTHDQeeamTMSDRIAimrkGKIAQIGTPEeIYEepanlfvarFIGEINVFEATVI 212
|
...
gi 928932812 249 ERK 251
Cdd:TIGR01187 213 ERK 215
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-233 |
1.00e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 65.47 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGkvhmpskmaiEYLSQNpefdpnaTI 83
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG----------ELLAGT-------AP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 84 LEQVfKSDSQIMnvirdyeniLEEISQNPDDSTLQKKLLYLTDNM--NAQDAweienqvktiLTKLGIHNFHQKI-ETLS 160
Cdd:PRK11247 76 LAEA-REDTRLM---------FQDARLLPWKKVIDNVGLGLKGQWrdAALQA----------LAAVGLADRANEWpAALS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 161 GGQKKRVALASALISPCDLLILDEPTNHMD-------HDTID--WLEKYLTnrtgsLLMITHDRY----FLDRVvnktLE 227
Cdd:PRK11247 136 GGQKQRVALARALIHRPGLLLLDEPLGALDaltriemQDLIEslWQQHGFT-----VLLVTHDVSeavaMADRV----LL 206
|
....*.
gi 928932812 228 LDDGKI 233
Cdd:PRK11247 207 IEEGKI 212
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
4-236 |
1.09e-11 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 67.76 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENIS--KSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSkMAIEYLSQNpEFDPNA 81
Cdd:TIGR01842 317 LSVENVTivPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDG-ADLKQWDRE-TFGKHI 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 82 TILEQvfksDSQIMnvirdyenileeisqnpdDSTLQKKLLYLTDNMNAQDAWEIenqvktilTKL-GIHNFHQKI---- 156
Cdd:TIGR01842 395 GYLPQ----DVELF------------------PGTVAENIARFGENADPEKIIEA--------AKLaGVHELILRLpdgy 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 157 --------ETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYLTN---RTGSLLMITHdRYFLDRVVNKT 225
Cdd:TIGR01842 445 dtvigpggATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKAlkaRGITVVVITH-RPSLLGCVDKI 523
|
250
....*....|.
gi 928932812 226 LELDDGKIYSY 236
Cdd:TIGR01842 524 LVLQDGRIARF 534
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-233 |
1.14e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 66.67 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 2 NILSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSkmaieylsqnpefdpna 81
Cdd:PRK11432 5 NFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDG----------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 82 tilEQVfkSDSQIMNviRDYENILEEISQNPDDStlqkkllyLTDN------MNAQDAWEIENQVKTILTKLGIHNFHQK 155
Cdd:PRK11432 68 ---EDV--THRSIQQ--RDICMVFQSYALFPHMS--------LGENvgyglkMLGVPKEERKQRVKEALELVDLAGFEDR 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 156 -IETLSGGQKKRVALASALISPCDLLILDEPTNHMD-------HDTIDWLEKYLtNRTGslLMITHDRYFLDRVVNKTLE 227
Cdd:PRK11432 133 yVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDanlrrsmREKIRELQQQF-NITS--LYVTHDQSEAFAVSDTVIV 209
|
....*.
gi 928932812 228 LDDGKI 233
Cdd:PRK11432 210 MNKGKI 215
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-266 |
1.30e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 65.88 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 1 MNIlSVENISKSYGEKILFE-----NISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKvhmpskmaIEYLSQNP 75
Cdd:PRK13651 1 MQI-KVKNIVKIFNKKLPTElkaldNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGT--------IEWIFKDE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 76 EFDPNATILEQVFKSDSQIMNVIRDYENIlEEISQNPD-----------DSTLQKKLLYLTDNMNAQDAwEIENQVKTIL 144
Cdd:PRK13651 72 KNKKKTKEKEKVLEKLVIQKTRFKKIKKI-KEIRRRVGvvfqfaeyqlfEQTIEKDIIFGPVSMGVSKE-EAKKRAAKYI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 145 TKLGI-HNFHQKIE-TLSGGQKKRVALASALISPCDLLILDEPTNHMD-HDTIDWLE--KYLTNRTGSLLMITHDryfLD 219
Cdd:PRK13651 150 ELVGLdESYLQRSPfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpQGVKEILEifDNLNKQGKTIILVTHD---LD 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 928932812 220 RVV---NKTLELDDGKI------YSYIGNYSQFIEKKLERKTLESSIERKRERLYK 266
Cdd:PRK13651 227 NVLewtKRTIFFKDGKIikdgdtYDILSDNKFLIENNMEPPKLLNFVNKLEKKGID 282
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
7-247 |
1.31e-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: 64.94 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 7 ENISKSYG-EKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAG-YDVaDTGKVHMP----SKMAIEYLSQNPEFDPN 80
Cdd:cd03253 4 ENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRfYDV-SSGSILIDgqdiREVTLDSLRRAIGVVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 81 ATILeqvFksDSQIMNVIRdYENIleeisqnpddstlqkkllyltdnmNAQDAwEIENQVKtiltKLGIH----NFHQKI 156
Cdd:cd03253 83 DTVL---F--NDTIGYNIR-YGRP------------------------DATDE-EVIEAAK----AAQIHdkimRFPDGY 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 157 ET--------LSGGQKKRVALASALISPCDLLILDEPTNHMDHDT----IDWLEKYLTNRTgsLLMITHDryfLDRVVN- 223
Cdd:cd03253 128 DTivgerglkLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTereiQAALRDVSKGRT--TIVIAHR---LSTIVNa 202
|
250 260
....*....|....*....|....*
gi 928932812 224 -KTLELDDGKIySYIGNYSQFIEKK 247
Cdd:cd03253 203 dKIIVLKDGRI-VERGTHEELLAKG 226
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-235 |
1.41e-11 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 65.18 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHM---------PSKMAieylsqn 74
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLngrpladwsPAELA------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 75 pefdpnatileqvfksdsQIMNVIRDYENI-----LEEI----------SQNPDDSTLQKKLLyLTDnmnaqdaweienq 139
Cdd:PRK13548 76 ------------------RRRAVLPQHSSLsfpftVEEVvamgraphglSRAEDDALVAAALA-QVD------------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 140 vktiLTKLGIHNFHQkietLSGGQKKRVALASAL--ISPCD----LLILDEPTNHMD----HDTIDWLEKYLTNRTGSLL 209
Cdd:PRK13548 124 ----LAHLAGRDYPQ----LSGGEQQRVQLARVLaqLWEPDgpprWLLLDEPTSALDlahqHHVLRLARQLAHERGLAVI 195
|
250 260 270
....*....|....*....|....*....|.
gi 928932812 210 MITHD-----RYfLDRVVnktLeLDDGKIYS 235
Cdd:PRK13548 196 VVLHDlnlaaRY-ADRIV---L-LHQGRLVA 221
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-190 |
1.84e-11 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 63.93 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISKSYGEK----ILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKMAIEylsqnpefD 78
Cdd:cd03266 1 MITADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK--------E 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 79 PNATILEQVFKSDSQimnviRDYENIleeisqnpddsTLQKKLLYLTD--NMNAQdawEIENQVKTILTKLGIHNF-HQK 155
Cdd:cd03266 73 PAEARRRLGFVSDST-----GLYDRL-----------TARENLEYFAGlyGLKGD---ELTARLEELADRLGMEELlDRR 133
|
170 180 190
....*....|....*....|....*....|....*
gi 928932812 156 IETLSGGQKKRVALASALISPCDLLILDEPTNHMD 190
Cdd:cd03266 134 VGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLD 168
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-233 |
1.99e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 65.21 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 2 NILSVENISKSY--GEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVadtgkvhmpskmaieylsqnPEFDP 79
Cdd:PRK13640 4 NIVEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLL--------------------PDDNP 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 80 NATILEQVFKSDSQIMNVIRDYENIleeISQNPDD----STLQKKLLYLTDNmNAQDAWEIENQVKTILTKLGIHNFhQK 155
Cdd:PRK13640 64 NSKITVDGITLTAKTVWDIREKVGI---VFQNPDNqfvgATVGDDVAFGLEN-RAVPRPEMIKIVRDVLADVGMLDY-ID 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 156 IE--TLSGGQKKRVALASALISPCDLLILDEPTNHMD----HDTIDWLEKYLTNRTGSLLMITHDryfLDRVV--NKTLE 227
Cdd:PRK13640 139 SEpaNLSGGQKQRVAIAGILAVEPKIIILDESTSMLDpagkEQILKLIRKLKKKNNLTVISITHD---IDEANmaDQVLV 215
|
....*.
gi 928932812 228 LDDGKI 233
Cdd:PRK13640 216 LDDGKL 221
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
319-519 |
2.07e-11 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 64.33 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFEQNKVIEDFSyIALKDDRI-GIIGKNGTGKSTLLNLITGKLTPDLGSIDIGptvkiGY--FSQESEDM-- 393
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVS-LTIPKGGItALIGPNGAGKSTLLSMISRLLPPDSGEVLVD-----GLdvATTPSRELak 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 394 ---------DINLR-AIE---------YIKEKaeyITTEDGIKIsaSQMMEnFLFSKDLQWTYISKLSGGErrrlyllrI 454
Cdd:COG4604 76 rlailrqenHINSRlTVRelvafgrfpYSKGR---LTAEDREII--DEAIA-YLDLEDLADRYLDELSGGQ--------R 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 455 LM---------DAPNVLiLDEPTNDLDI----DTLKVLENYIDDFNGIVICVSHD-----RYfLDRICnkifffA-GDGK 515
Cdd:COG4604 142 QRafiamvlaqDTDYVL-LDEPLNNLDMkhsvQMMKLLRRLADELGKTVVIVLHDinfasCY-ADHIV------AmKDGR 213
|
....
gi 928932812 516 IIEH 519
Cdd:COG4604 214 VVAQ 217
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-191 |
2.11e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 66.12 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 1 MNILSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSkmaiEYLSQNPefdPN 80
Cdd:PRK09452 12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDG----QDITHVP---AE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 81 ATILEQVFKSDSQI--MNVirdYENI---LEeisqnpddstLQKKllyltdnmnaqDAWEIENQVKTILTKLGIHNFHQ- 154
Cdd:PRK09452 85 NRHVNTVFQSYALFphMTV---FENVafgLR----------MQKT-----------PAAEITPRVMEALRMVQLEEFAQr 140
|
170 180 190
....*....|....*....|....*....|....*..
gi 928932812 155 KIETLSGGQKKRVALASALISPCDLLILDEPTNHMDH 191
Cdd:PRK09452 141 KPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDY 177
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-525 |
2.14e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 66.73 E-value: 2.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGydvadtgkVHMPSKMAIEYLSQN-PEFDPN-- 80
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSG--------IHEPTKGTITINNINyNKLDHKla 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 81 ATILEQVFKSDSQIMNVIRDYENILeeISQNPddstlQKKLLyltdNMNAQDAWEIENQVKTILTKLGIH-NFHQKIETL 159
Cdd:PRK09700 78 AQLGIGIIYQELSVIDELTVLENLY--IGRHL-----TKKVC----GVNIIDWREMRVRAAMMLLRVGLKvDLDEKVANL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 160 SGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWL---EKYLTNRTGSLLMITHDRYFLDRVVNKTLELDDGkiySY 236
Cdd:PRK09700 147 SISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLfliMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG---SS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 237 IGNysqfiekkleRKTLESSIERKRERLYKKELEwiragaqarstkqkariQRFEELKNTsspihdsnidicvaHSRLGQ 316
Cdd:PRK09700 224 VCS----------GMVSDVSNDDIVRLMVGRELQ-----------------NRFNAMKEN--------------VSNLAH 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 317 KII-EINHISKsfEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSI-----DIGP-----TVK--I 383
Cdd:PRK09700 263 ETVfEVRNVTS--RDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIrlngkDISPrspldAVKkgM 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 384 GYFSQESED------MDI--NLRAIEYIK------------EKAEYITTEDG---IKISASQMMENflfskdlqwtyISK 440
Cdd:PRK09700 341 AYITESRRDngffpnFSIaqNMAISRSLKdggykgamglfhEVDEQRTAENQrelLALKCHSVNQN-----------ITE 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 441 LSGGERRRLYLLRILMDAPNVLILDEPTNDLDIDT----LKVLENYIDDFNGIVIcVSHDRYFLDRICNKIFFFAgDGKI 516
Cdd:PRK09700 410 LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAkaeiYKVMRQLADDGKVILM-VSSELPEIITVCDRIAVFC-EGRL 487
|
....*....
gi 928932812 517 IEHTGNYSD 525
Cdd:PRK09700 488 TQILTNRDD 496
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-222 |
2.18e-11 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 65.46 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISKSY--GEKILF--ENISFSI--GDTdkIGLIGVNGTGKSSLLKIIAG---YDVADTGKV--------HMPSK 65
Cdd:COG0444 1 LLEVRNLKVYFptRRGVVKavDGVSFDVrrGET--LGLVGESGSGKSTLARAILGllpPPGITSGEIlfdgedllKLSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 66 MAIEYLS-------QNPE--FDPNATILEQvfksdsqIMNVIRdyenileeisqnpddstlqkkllyLTDNMNAQDAWEi 136
Cdd:COG0444 79 ELRKIRGreiqmifQDPMtsLNPVMTVGDQ-------IAEPLR------------------------IHGGLSKAEARE- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 137 enQVKTILTKLGI-------HNF-HQkietLSGGQKKRVALASALI-SPcDLLILDEPTNHMD----HDTIDWLEKyLTN 203
Cdd:COG0444 127 --RAIELLERVGLpdperrlDRYpHE----LSGGMRQRVMIARALAlEP-KLLIADEPTTALDvtiqAQILNLLKD-LQR 198
|
250 260
....*....|....*....|....
gi 928932812 204 RTG-SLLMITHD----RYFLDRVV 222
Cdd:COG0444 199 ELGlAILFITHDlgvvAEIADRVA 222
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
3-233 |
2.19e-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: 64.83 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISKSYGEKILF---------ENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVhmpsKMAIEYLSQ 73
Cdd:TIGR02769 2 LLEVRDVTHTYRTGGLFgakqrapvlTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTV----SFRGQDLYQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 74 npeFDPNAtilEQVFKSDSQImnVIRDYENileeiSQNPDDS---TLQKKLLYLTDnmnaQDAWEIENQVKTILTKLGIH 150
Cdd:TIGR02769 78 ---LDRKQ---RRAFRRDVQL--VFQDSPS-----AVNPRMTvrqIIGEPLRHLTS----LDESEQKARIAELLDMVGLR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 151 NFH-QKI-ETLSGGQKKRVALASALISPCDLLILDEPTNHMD---HDTIDWLEKYLTNRTG-SLLMITHDRYFLDRVVNK 224
Cdd:TIGR02769 141 SEDaDKLpRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDmvlQAVILELLRKLQQAFGtAYLFITHDLRLVQSFCQR 220
|
....*....
gi 928932812 225 TLELDDGKI 233
Cdd:TIGR02769 221 VAVMDKGQI 229
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
318-519 |
2.54e-11 |
|
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: 64.22 E-value: 2.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 318 IIEINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIGPT------------VKIGY 385
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQdithlpmherarLGIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 386 FSQES--------EDmdiNLRAIEYIKEKaeyiTTEDGIKISASQMMENFLFSKDLQWTYISkLSGGERRRLYLLRILMD 457
Cdd:TIGR04406 81 LPQEAsifrkltvEE---NIMAVLEIRKD----LDRAEREERLEALLEEFQISHLRDNKAMS-LSGGERRRVEIARALAT 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 928932812 458 APNVLILDEPTNDLD---IDTLKVLENYIDDFN-GIVICVSHDRYFLDrICNKIFFFAgDGKIIEH 519
Cdd:TIGR04406 153 NPKFILLDEPFAGVDpiaVGDIKKIIKHLKERGiGVLITDHNVRETLD-ICDRAYIIS-DGKVLAE 216
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
316-521 |
2.91e-11 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 63.52 E-value: 2.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 316 QKIIEINHISKSFEQNKViedfSYIALKD--------DRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIGPTV------ 381
Cdd:COG1136 2 SPLLELRNLTKSYGTGEG----EVTALRGvslsieagEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDisslse 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 382 ---------KIGYFSQesedmDINL------------------RAIEYIKEKAEYITTEDGIkisasqmmenflfsKDLQ 434
Cdd:COG1136 78 relarlrrrHIGFVFQ-----FFNLlpeltalenvalplllagVSRKERRERARELLERVGL--------------GDRL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 435 WTYISKLSGGErrrlyllrilmdA------------PNVLILDEPTNDLDIDT----LKVLENYIDDFNGIVICVSHDRy 498
Cdd:COG1136 139 DHRPSQLSGGQ------------QqrvaiaralvnrPKLILADEPTGNLDSKTgeevLELLRELNRELGTTIVMVTHDP- 205
|
250 260
....*....|....*....|...
gi 928932812 499 FLDRICNKIFFFAgDGKIIEHTG 521
Cdd:COG1136 206 ELAARADRVIRLR-DGRIVSDER 227
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-233 |
3.80e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 65.05 E-value: 3.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 1 MNILSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMpskmaieylsqnpefdpn 80
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFI------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 81 atileqvfksDSQIMNVIrdyenileEISQNPDDSTLQKKLLY----LTDNMN------AQDAWEIE---NQVKTILtKL 147
Cdd:PRK11000 63 ----------GEKRMNDV--------PPAERGVGMVFQSYALYphlsVAENMSfglklaGAKKEEINqrvNQVAEVL-QL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 148 GiHNFHQKIETLSGGQKKRVALASALISPCDLLILDEPTNHMD-------HDTIDWLEKYLtNRTgsllMI--THDRYFL 218
Cdd:PRK11000 124 A-HLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaalrvqmRIEISRLHKRL-GRT----MIyvTHDQVEA 197
|
250
....*....|....*
gi 928932812 219 DRVVNKTLELDDGKI 233
Cdd:PRK11000 198 MTLADKIVVLDAGRV 212
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
8-233 |
3.93e-11 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 65.13 E-value: 3.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 8 NISKSYGEKILfeNISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHM---------------PSKMAIEYLS 72
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLngrtlfdsrkgiflpPEKRRIGYVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 73 QNPEFDPNATIleqvfksdsqimnvirdyenileeiSQNpddstlqkkLLYltdNMNAQDAWEIENQVKTILTKLGI-HN 151
Cdd:TIGR02142 82 QEARLFPHLSV-------------------------RGN---------LRY---GMKRARPSERRISFERVIELLGIgHL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 152 FHQKIETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYLTNRTGSL----LMITHDRYFLDRVVNKTLE 227
Cdd:TIGR02142 125 LGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEFgipiLYVSHSLQEVLRLADRVVV 204
|
....*.
gi 928932812 228 LDDGKI 233
Cdd:TIGR02142 205 LEDGRV 210
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
7-247 |
4.05e-11 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 63.40 E-value: 4.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 7 ENISKSYGEKIL-FENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMpSKMAIEYLSQNPEFDPNATILE 85
Cdd:cd03254 6 ENVNFSYDEKKPvLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILI-DGIDIRDISRKSLRSMIGVVLQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 86 QVFKSDSQIMnvirdyENILeeisqnpddstlqkkllyLTDNMNAQDAWEIENQVktiltkLGIHNFHQKIE-------- 157
Cdd:cd03254 85 DTFLFSGTIM------ENIR------------------LGRPNATDEEVIEAAKE------AGAHDFIMKLPngydtvlg 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 158 ----TLSGGQKKRVALASALISPCDLLILDEPTNHMDHDT----IDWLEKYLTNRTgsLLMITHdRYFLDRVVNKTLELD 229
Cdd:cd03254 135 enggNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETekliQEALEKLMKGRT--SIIIAH-RLSTIKNADKILVLD 211
|
250
....*....|....*...
gi 928932812 230 DGKIYSYiGNYSQFIEKK 247
Cdd:cd03254 212 DGKIIEE-GTHDELLAKK 228
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
347-512 |
4.18e-11 |
|
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: 63.58 E-value: 4.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 347 IGIIGKNGTGKSTLLNLITGKLTPDLGSIDIgPTVKIGYFSQE-SEDMDINLRAIEYIKEKAEYITTEDGIKISASQMME 425
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLAGVLKPDEGDIEI-ELDTVSYKPQYiKADYEGTVRDLLSSITKDFYTHPYFKTEIAKPLQIE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 426 NFLfskDLQwtyISKLSGGERRRLYLLRILMDAPNVLILDEPTNDLDID----TLKVLENYIDDFNGIVICVSHDRYFLD 501
Cdd:cd03237 107 QIL---DRE---VPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEqrlmASKVIRRFAENNEKTAFVVEHDIIMID 180
|
170
....*....|.
gi 928932812 502 RICNKIFFFAG 512
Cdd:cd03237 181 YLADRLIVFEG 191
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
35-472 |
4.46e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 65.42 E-value: 4.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 35 IGVNGTGKSSLLKIIAGYDVADTGKV----HMPSKMAIEYLSQnpefdpnatILEQVFKSDSQIMnvirdyenileeISQ 110
Cdd:PRK10938 35 VGANGSGKSALARALAGELPLLSGERqsqfSHITRLSFEQLQK---------LVSDEWQRNNTDM------------LSP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 111 NPDD---STLQKKLLYLTDNMNAQdawEIENQvktiltkLGI-HNFHQKIETLSGGQKKRVALASALISPCDLLILDEPT 186
Cdd:PRK10938 94 GEDDtgrTTAEIIQDEVKDPARCE---QLAQQ-------FGItALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 187 NHMDHDTidwlEKYLTNRTGSLlmiTHDRYFLDRVVNKtleLDDgkiysyIGNYSQFIeKKLERKTLESSIERKR---ER 263
Cdd:PRK10938 164 DGLDVAS----RQQLAELLASL---HQSGITLVLVLNR---FDE------IPDFVQFA-GVLADCTLAETGEREEilqQA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 264 LYkkelewiragAQ-ARStkqkariqrfEELKNTSSPIHDSNidicVAHSRL--GQKIIEINHISKSFEQNKVIEDFSYI 340
Cdd:PRK10938 227 LV----------AQlAHS----------EQLEGVQLPEPDEP----SARHALpaNEPRIVLNNGVVSYNDRPILHNLSWQ 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 341 ALKDDRIGIIGKNGTGKSTLLNLITGK----LTPDL-------GSidiGPTV-----KIGYFSQeSEDMD----INLRAI 400
Cdd:PRK10938 283 VNPGEHWQIVGPNGAGKSTLLSLITGDhpqgYSNDLtlfgrrrGS---GETIwdikkHIGYVSS-SLHLDyrvsTSVRNV 358
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 928932812 401 ---EYIKEKAEYITTEDGIKISASQMMENFLFSKDLQWTYISKLSGGERRRLYLLRILMDAPNVLILDEPTNDLD 472
Cdd:PRK10938 359 ilsGFFDSIGIYQAVSDRQQKLAQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
3-228 |
5.32e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 62.56 E-value: 5.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKMA--------IEYLSQN 74
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAtrgdrsrfMAYLGHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 75 PEFDPNATILEQVfksdsQIMNVIRDYENileeiSQNPDDStlqkkllyltdnmnaqdaweienqvktiLTKLGIHNFHQ 154
Cdd:PRK13543 91 PGLKADLSTLENL-----HFLCGLHGRRA-----KQMPGSA----------------------------LAIVGLAGYED 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 928932812 155 K-IETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYLTN--RT-GSLLMITHDRYFLDRVVNKTLEL 228
Cdd:PRK13543 133 TlVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAhlRGgGAALVTTHGAYAAPPVRTRMLTL 210
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-235 |
5.66e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 63.60 E-value: 5.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 1 MNILSVENISKSYG---EKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKMAIEylsqnpef 77
Cdd:PRK13650 2 SNIIEVKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTE-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 78 dpnatilEQVFKSDSQIMNVIrdyenileeisQNPDD----STLQKKLLYLTDNmNAQDAWEIENQVKTILTKLGIHNFH 153
Cdd:PRK13650 74 -------ENVWDIRHKIGMVF-----------QNPDNqfvgATVEDDVAFGLEN-KGIPHEEMKERVNEALELVGMQDFK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 154 QKIET-LSGGQKKRVALASALISPCDLLILDEPTNHMD----HDTIDWLEKYLTNRTGSLLMITHDryfLDRVV--NKTL 226
Cdd:PRK13650 135 EREPArLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHD---LDEVAlsDRVL 211
|
....*....
gi 928932812 227 ELDDGKIYS 235
Cdd:PRK13650 212 VMKNGQVES 220
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
319-503 |
6.04e-11 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 62.97 E-value: 6.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFEQNK-VIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIGPTV--------------KI 383
Cdd:cd03256 1 IEVENLSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDinklkgkalrqlrrQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 384 GYFSQESEDMDiNLRAIEYI----------------------KEKAEYITTEDGIKISASQMmenflfskdlqwtyISKL 441
Cdd:cd03256 81 GMIFQQFNLIE-RLSVLENVlsgrlgrrstwrslfglfpkeeKQRALAALERVGLLDKAYQR--------------ADQL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 442 SGGERRRLYLLRILMDAPNVLILDEPTNDLDIDTLKVLENYIDDFN---GI-VICVSHD----RYFLDRI 503
Cdd:cd03256 146 SGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINreeGItVIVSLHQvdlaREYADRI 215
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
318-517 |
9.58e-11 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 62.00 E-value: 9.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 318 IIEINHISKSFEQNK----VIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDI-GPTV---------KI 383
Cdd:cd03266 1 MITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVdGFDVvkepaearrRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 384 GYFSqESEDMDINLRAieyiKEKAEYITTEDGIKISASQMMENFLFS----KDLQWTYISKLSGGERRRLYLLRILMDAP 459
Cdd:cd03266 81 GFVS-DSTGLYDRLTA----RENLEYFAGLYGLKGDELTARLEELADrlgmEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 928932812 460 NVLILDEPTNDLDIDTLKVLENYIDDFNGIVICV---SHDRYFLDRICNKIFFFAgDGKII 517
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQLRALGKCIlfsTHIMQEVERLCDRVVVLH-RGRVV 215
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-233 |
9.77e-11 |
|
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: 62.00 E-value: 9.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 6 VENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKI-------------IAGYDVA-DTGKVhmpsKMAIEYL 71
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMlttllkptsgratVAGHDVVrEPREV----RRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 72 SQNPEFDPNATILEQVFksdsqIMNVIRDYENileeisqnpddSTLQKKLLYLTDNMnaqDAWEIENQVktiltklgihn 151
Cdd:cd03265 79 FQDLSVDDELTGWENLY-----IHARLYGVPG-----------AERRERIDELLDFV---GLLEAADRL----------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 152 fhqkIETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTID--W--LEKYLTNRTGSLLMITHDRYFLDRVVNKTLE 227
Cdd:cd03265 129 ----VKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAhvWeyIEKLKEEFGMTILLTTHYMEEAEQLCDRVAI 204
|
....*.
gi 928932812 228 LDDGKI 233
Cdd:cd03265 205 IDHGRI 210
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-496 |
1.08e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 64.25 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISKSY-GEKILfENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGkvhmpskmAIEYLSQNPEFD--- 78
Cdd:PRK10762 4 LLQLKGIDKAFpGVKAL-SGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAG--------SILYLGKEVTFNgpk 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 79 -----------------PNATILEQVFKSdsqimnviRDYENILEEIsqnpddstlqkkllyLTDNMNAQ-DAweienqv 140
Cdd:PRK10762 75 ssqeagigiihqelnliPQLTIAENIFLG--------REFVNRFGRI---------------DWKKMYAEaDK------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 141 ktILTKLGI-HNFHQKIETLSGGQKKRVALASALISPCDLLILDEPTNHM-DHDT------IDWLEK------YLTNRTG 206
Cdd:PRK10762 125 --LLARLNLrFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETeslfrvIRELKSqgrgivYISHRLK 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 207 SLLMIThdryflDRVvnkTLeLDDGkiysyignysQFI-EKKLERKTLESSIE----RKRERLYKKelewiragaqarst 281
Cdd:PRK10762 203 EIFEIC------DDV---TV-FRDG----------QFIaEREVADLTEDSLIEmmvgRKLEDQYPR-------------- 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 282 kqkariqrfeelkntsspihdsnidICVAHsrlGQKIIEINHISKSFeqnkvIEDFSYIALKDDRIGIIGKNGTGKSTLL 361
Cdd:PRK10762 249 -------------------------LDKAP---GEVRLKVDNLSGPG-----VNDVSFTLRKGEILGVSGLMGAGRTELM 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 362 NLITGKLTPDLGSIDI-GPTVK-----------IGYFSQE------------SEDMdiNLRAIEY-------IKEKAEYI 410
Cdd:PRK10762 296 KVLYGALPRTSGYVTLdGHEVVtrspqdglangIVYISEDrkrdglvlgmsvKENM--SLTALRYfsraggsLKHADEQQ 373
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 411 TTEDGIKisasqmmenfLF-----SKDLQwtyISKLSGGERRRLYLLRILMDAPNVLILDEPTNDLDIDTLKVLENYIDD 485
Cdd:PRK10762 374 AVSDFIR----------LFniktpSMEQA---IGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQ 440
|
570
....*....|....
gi 928932812 486 F--NGI-VICVSHD 496
Cdd:PRK10762 441 FkaEGLsIILVSSE 454
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-186 |
1.09e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 64.30 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHM---------PSK---MAIEY 70
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIggnpcarltPAKahqLGIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 71 LSQNPEFDPNATILeqvfksdsqimnvirdyENILEEISQNPDDstlqkkllyltdnmnaqdaweiENQVKTILTKLGIH 150
Cdd:PRK15439 91 VPQEPLLFPNLSVK-----------------ENILFGLPKRQAS----------------------MQKMKQLLAALGCQ 131
|
170 180 190
....*....|....*....|....*....|....*..
gi 928932812 151 -NFHQKIETLSGGQKKRVALASALISPCDLLILDEPT 186
Cdd:PRK15439 132 lDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPT 168
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
33-190 |
1.10e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 62.72 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 33 GLIGVNGTGKSSLLKIIAGydvadtgkVHMPSKMAIEYLSQNPEFDPNATI-LEQvfksdsQIMNVIRDYEnilEEISQN 111
Cdd:PRK13638 31 GLVGANGCGKSTLFMNLSG--------LLRPQKGAVLWQGKPLDYSKRGLLaLRQ------QVATVFQDPE---QQIFYT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 112 PDDSTLQKKLlyltDNMNAQDAwEIENQVKTILTKLGIHNF-HQKIETLSGGQKKRVALASALISPCDLLILDEPTNHMD 190
Cdd:PRK13638 94 DIDSDIAFSL----RNLGVPEA-EITRRVDEALTLVDAQHFrHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
318-518 |
1.12e-10 |
|
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: 61.83 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 318 IIEINHISKSFEQNKViedfSYIALKD--------DRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIGPTV-------- 381
Cdd:cd03258 1 MIELKNVSKVFGDTGG----KVTALKDvslsvpkgEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDltllsgke 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 382 ------KIGYFSQEsedmdINLRAIEYIKEKAEY---ITTEDGIKIsASQMME--NFLFSKDLQWTYISKLSGGERRRLY 450
Cdd:cd03258 77 lrkarrRIGMIFQH-----FNLLSSRTVFENVALpleIAGVPKAEI-EERVLEllELVGLEDKADAYPAQLSGGQKQRVG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 928932812 451 LLRILMDAPNVLILDEPTNDLDIDT----LKVLENYIDDFNGIVICVSHDRYFLDRICNKIFFFAgDGKIIE 518
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETtqsiLALLRDINRELGLTIVLITHEMEVVKRICDRVAVME-KGEVVE 221
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
319-507 |
1.17e-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: 61.96 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSF---------------------EQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDI 377
Cdd:cd03267 1 IEVSNLSKSYrvyskepgligslkslfkrkyREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 378 GPTV----------KIGY-FSQESE---DMDIN-----LRAIeYIKEKAEYITTEDGIkisaSQMMEnflfSKDLQWTYI 438
Cdd:cd03267 81 AGLVpwkrrkkflrRIGVvFGQKTQlwwDLPVIdsfylLAAI-YDLPPARFKKRLDEL----SELLD----LEELLDTPV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 928932812 439 SKLSGGERRRLYLLRILMDAPNVLILDEPTNDLDIDTLKVLENYIDDFN---GIVICV-SHDRYFLDRICNKI 507
Cdd:cd03267 152 RQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNrerGTTVLLtSHYMKDIEALARRV 224
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-247 |
1.37e-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: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSY---GEKILfENISFSIGDTDKIGLIGVNGTGKSSLLKIIA-------------GYDVADTGKVHMPSKMA 67
Cdd:cd03251 1 VEFKNVTFRYpgdGPPVL-RDISLDIPAGETVALVGPSGSGKSTLVNLIPrfydvdsgrilidGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 68 IeyLSQNpefdpnaTILeqvFksdsqimnvirdYENILEEISQNPDDSTlQKKLLYLTDNMNAQD-AWEIENQVKTILTK 146
Cdd:cd03251 80 L--VSQD-------VFL---F------------NDTVAENIAYGRPGAT-REEVEEAARAANAHEfIMELPEGYDTVIGE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 147 LGIhnfhqkieTLSGGQKKRVALASALISPCDLLILDEPTNHMDHDT----IDWLEKYLTNRTGslLMITHdRYFLDRVV 222
Cdd:cd03251 135 RGV--------KLSGGQRQRIAIARALLKDPPILILDEATSALDTESerlvQAALERLMKNRTT--FVIAH-RLSTIENA 203
|
250 260
....*....|....*....|....*
gi 928932812 223 NKTLELDDGKIYSyIGNYSQFIEKK 247
Cdd:cd03251 204 DRIVVLEDGKIVE-RGTHEELLAQG 227
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
7-234 |
1.41e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 61.43 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 7 ENISKSY-GEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKV----HMPSKMaieylsQNPEFDPNA 81
Cdd:PRK10908 5 EHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsgHDITRL------KNREVPFLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 82 TILEQVFKSDSQIMNVIRdYENIleeisqnpddstlqkKLLYLTDNMNAQDaweIENQVKTILTKLGI----HNFHQKie 157
Cdd:PRK10908 79 RQIGMIFQDHHLLMDRTV-YDNV---------------AIPLIIAGASGDD---IRRRVSAALDKVGLldkaKNFPIQ-- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 158 tLSGGQKKRVALASALISPCDLLILDEPTNHMD----HDTIDWLEKYltNRTG-SLLMITHDRYFLDRVVNKTLELDDGK 232
Cdd:PRK10908 138 -LSGGEQQRVGIARAVVNKPAVLLADEPTGNLDdalsEGILRLFEEF--NRVGvTVLMATHDIGLISRRSYRMLTLSDGH 214
|
..
gi 928932812 233 IY 234
Cdd:PRK10908 215 LH 216
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-190 |
1.46e-10 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 62.02 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 5 SVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVH--------MPS-----KMAIeyL 71
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLvdgldvatTPSrelakRLAI--L 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 72 SQNPEFDPNATILEQV----FksdsqimnvirdyenileeisqnPddstlqkkllYLTDNMNAQDaWEIenqVKTILTKL 147
Cdd:COG4604 81 RQENHINSRLTVRELVafgrF-----------------------P----------YSKGRLTAED-REI---IDEAIAYL 123
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 928932812 148 GIHNF-HQKIETLSGGQKKRVALASALISPCDLLILDEPTNHMD 190
Cdd:COG4604 124 DLEDLaDRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLD 167
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-214 |
1.59e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.96 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISKSY-----------GEKILFENISFSIGDTDKIGLIGVNGTGKSS----LLKIIA--GYDVADTGKVH---- 61
Cdd:PRK15134 275 LLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINsqGEIWFDGQPLHnlnr 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 62 ---MPSKMAIEYLSQnpefDPNATILEQvfksdsqiMNVirdyENILEEISQnpddsTLQKKLlyltdnmnaqDAWEIEN 138
Cdd:PRK15134 355 rqlLPVRHRIQVVFQ----DPNSSLNPR--------LNV----LQIIEEGLR-----VHQPTL----------SAAQREQ 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 139 QVKTILTKLGI--HNFHQKIETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDT---IDWLEKYLTNRTG-SLLMIT 212
Cdd:PRK15134 404 QVIAVMEEVGLdpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVqaqILALLKSLQQKHQlAYLFIS 483
|
..
gi 928932812 213 HD 214
Cdd:PRK15134 484 HD 485
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
3-219 |
1.65e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.06 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISKSYGEkilfenisFSI----GDTDK---IGLIGVNGTGKSSLLKIIAGYDVADTGKVHmpSKMAIEYLSQNP 75
Cdd:PRK13409 340 LVEYPDLTKKLGD--------FSLevegGEIYEgevIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD--PELKISYKPQYI 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 76 EFDPNATIleqvfksdsqimnvirdyENILEEISQNPDDStlqkklLYLTDnmnaqdaweienqvktILTKLGIHN-FHQ 154
Cdd:PRK13409 410 KPDYDGTV------------------EDLLRSITDDLGSS------YYKSE----------------IIKPLQLERlLDK 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 928932812 155 KIETLSGGQKKRVALASALISPCDLLILDEPTNHMD-------HDTIdwlEKYLTNRTGSLLMITHDRYFLD 219
Cdd:PRK13409 450 NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrlavAKAI---RRIAEEREATALVVDHDIYMID 518
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
323-519 |
1.80e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 61.45 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 323 HISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIG------------PTVKIGYFSQES 390
Cdd:PRK10895 8 NLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDdedisllplharARRGIGYLPQEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 391 E-----DMDINLRAIEYIKEKaeyiTTEDGIKISASQMMENFLFSKdLQWTYISKLSGGERRRLYLLRILMDAPNVLILD 465
Cdd:PRK10895 88 SifrrlSVYDNLMAVLQIRDD----LSAEQREDRANELMEEFHIEH-LRDSMGQSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 928932812 466 EPTNDLD----IDTLKVLENYIDDFNGIVICVSHDRYFLDrICNKIFFFAgDGKIIEH 519
Cdd:PRK10895 163 EPFAGVDpisvIDIKRIIEHLRDSGLGVLITDHNVRETLA-VCERAYIVS-QGHLIAH 218
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-229 |
2.05e-10 |
|
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: 61.66 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 25 SIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPskmaIEYLSQNPefdpnatileQVFKSDSQimnvirdyeni 104
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIE----LDTVSYKP----------QYIKADYE----------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 105 leeisqnpddSTLQKKLLYLTDNMNAQDAWEIEnqvktILTKLGIHN-FHQKIETLSGGQKKRVALASALISPCDLLILD 183
Cdd:cd03237 76 ----------GTVRDLLSSITKDFYTHPYFKTE-----IAKPLQIEQiLDREVPELSGGELQRVAIAACLSKDADIYLLD 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 928932812 184 EPTNHMDHD----TIDWLEKYLTNRTGSLLMITHDRYFLDRVVNKTLELD 229
Cdd:cd03237 141 EPSAYLDVEqrlmASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFE 190
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-190 |
2.09e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 61.99 E-value: 2.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 1 MNIlSVENISKSYGEKILFE-----NISFSIGDTDKIGLIGVNGTGKSSLLK-------------IIAGYDVADTGKVHM 62
Cdd:PRK13637 1 MSI-KIENLTHIYMEGTPFEkkaldNVNIEIEDGEFVGLIGHTGSGKSTLIQhlngllkptsgkiIIDGVDITDKKVKLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 63 PSKMAIEYLSQNPEFdpnatileQVFKsdsqimnvirdyENILEEISQNPddstlqkKLLYLTDNmnaqdawEIENQVKT 142
Cdd:PRK13637 80 DIRKKVGLVFQYPEY--------QLFE------------ETIEKDIAFGP-------INLGLSEE-------EIENRVKR 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 928932812 143 ILTKLGIHNFHQKIET---LSGGQKKRVALASALISPCDLLILDEPTNHMD 190
Cdd:PRK13637 126 AMNIVGLDYEDYKDKSpfeLSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-233 |
2.17e-10 |
|
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: 63.58 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYG--EKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKMAIEYLSQN--PEFdp 79
Cdd:TIGR02203 331 VEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASlrRQV-- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 80 nATILEQVFKSDSQIMNVIRDYEniLEEISQNPDDSTLQKKllYLTDNMNAQDaweienqvktiltkLGIH-NFHQKIET 158
Cdd:TIGR02203 409 -ALVSQDVVLFNDTIANNIAYGR--TEQADRAEIERALAAA--YAQDFVDKLP--------------LGLDtPIGENGVL 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 928932812 159 LSGGQKKRVALASALISPCDLLILDEPTNHMDHDT----IDWLEKYLTNRTGslLMITHdRYFLDRVVNKTLELDDGKI 233
Cdd:TIGR02203 470 LSGGQRQRLAIARALLKDAPILILDEATSALDNESerlvQAALERLMQGRTT--LVIAH-RLSTIEKADRIVVMDDGRI 545
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-186 |
2.30e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 63.12 E-value: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISKSYGEKILFENISFSI--GdtdKI-GLIGVNGTGKSSLLKIIAGYDVADTG-------KVHMPS-KMAIEY- 70
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVrpG---EIhALLGENGAGKSTLMKILYGLYQPDSGeilidgkPVRIRSpRDAIALg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 71 ---LSQNPEFDPNATILEqvfksdsqimNVIRDYENileeisqnpddstlqKKLLYLtdNMNaqdawEIENQVKTILTKL 147
Cdd:COG3845 82 igmVHQHFMLVPNLTVAE----------NIVLGLEP---------------TKGGRL--DRK-----AARARIRELSERY 129
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 928932812 148 GIH-NFHQKIETLSGGQKKRVALASALISPCDLLILDEPT 186
Cdd:COG3845 130 GLDvDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPT 169
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-190 |
2.40e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 61.06 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 1 MNILSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKV------------HMPSKMAI 68
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIiiddedisllplHARARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 69 EYLSQnpefdpNATILEQVFKSDSqIMNVIRDYENILEEISQNPDDSTLQK-KLLYLTDNMNaqdaweienqvktiltkl 147
Cdd:PRK10895 81 GYLPQ------EASIFRRLSVYDN-LMAVLQIRDDLSAEQREDRANELMEEfHIEHLRDSMG------------------ 135
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 928932812 148 gihnfhqkiETLSGGQKKRVALASALISPCDLLILDEPTNHMD 190
Cdd:PRK10895 136 ---------QSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
33-190 |
2.52e-10 |
|
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: 61.37 E-value: 2.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 33 GLIGVNGTGKSSLLKIIAGYDVADTGKV-------HMPSKMA----IEYLSQNPEFDPNATILEQVFksdsqimnvirdy 101
Cdd:TIGR03873 31 GLLGPNGSGKSTLLRLLAGALRPDAGTVdlagvdlHGLSRRArarrVALVEQDSDTAVPLTVRDVVA------------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 102 enileeISQNPDDSTLqkkllyltdnmnAQDAWEIENQVKTILTKLGIHNFHQK-IETLSGGQKKRVALASALISPCDLL 180
Cdd:TIGR03873 98 ------LGRIPHRSLW------------AGDSPHDAAVVDRALARTELSHLADRdMSTLSGGERQRVHVARALAQEPKLL 159
|
170
....*....|
gi 928932812 181 ILDEPTNHMD 190
Cdd:TIGR03873 160 LLDEPTNHLD 169
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
319-501 |
2.91e-10 |
|
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: 60.19 E-value: 2.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFEQNKVIEDFSYiALKD-DRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIgptvkigyfsqesEDMDINL 397
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSF-TLAAgEALALTGPNGSGKTTLLRILAGLLPPSAGEVLW-------------NGEPIRD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 398 RAIEYiKEKAEYITTEDGIK--ISAsqmMENFLFS----------------------KDLQWTYISKLSGGerrrlyllr 453
Cdd:COG4133 69 AREDY-RRRLAYLGHADGLKpeLTV---RENLRFWaalyglradreaidealeavglAGLADLPVRQLSAG--------- 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 928932812 454 ilM------------DAPnVLILDEPTNDLDIDTLKVLENYIDDFN---GIVICVSHDRYFLD 501
Cdd:COG4133 136 --QkrrvalarlllsPAP-LWLLDEPFTALDAAGVALLAELIAAHLargGAVLLTTHQPLELA 195
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
319-525 |
3.39e-10 |
|
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: 62.86 E-value: 3.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFEQNK--VIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIG---------PTV--KIGY 385
Cdd:COG4987 334 LELEDVSFRYPGAGrpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGgvdlrdldeDDLrrRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 386 FSQESE--DMDI--NLR-AieyiKEKAeyitTEDgikisasQMME--------NFLFSKDLQW-TYI----SKLSGGErr 447
Cdd:COG4987 414 VPQRPHlfDTTLreNLRlA----RPDA----TDE-------ELWAalervglgDWLAALPDGLdTWLgeggRRLSGGErr 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 448 rlyl-lrilmDAPnVLILDEPTNDLDIDT-LKVLENYIDDFNG-IVICVSHDRYFLDRiCNKIFFFaGDGKIIEHtGNYS 524
Cdd:COG4987 479 rlalarallrDAP-ILLLDEPTEGLDAATeQALLADLLEALAGrTVLLITHRLAGLER-MDRILVL-EDGRIVEQ-GTHE 554
|
.
gi 928932812 525 D 525
Cdd:COG4987 555 E 555
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
319-517 |
3.83e-10 |
|
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: 60.21 E-value: 3.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFE--QNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSI-----DIGPTVK-----IGYF 386
Cdd:cd03263 1 LQIRNLTKTYKkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAyingySIRTDRKaarqsLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 387 SQEsedmDI---NLRAIEYIkekaEYIT-----TEDGIKISASQMMENFLFSKDLQwTYISKLSGGERRRLYLLRILMDA 458
Cdd:cd03263 81 PQF----DAlfdELTVREHL----RFYArlkglPKSEIKEEVELLLRVLGLTDKAN-KRARTLSGGMKRKLSLAIALIGG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 928932812 459 PNVLILDEPTNDLDIDTLKVLENYIDDF--NGIVICVSHDRYFLDRICNKIFFFAgDGKII 517
Cdd:cd03263 152 PSVLLLDEPTSGLDPASRRAIWDLILEVrkGRSIILTTHSMDEAEALCDRIAIMS-DGKLR 211
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-222 |
3.84e-10 |
|
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: 62.78 E-value: 3.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 1 MNILSVENISKSYG----EKILFENISFSIGDTDKIGLIGVNGTGKS----SLLKIIAGYDVADTGKVHmpskmaieyls 72
Cdd:COG4172 4 MPLLSVEDLSVAFGqgggTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSIL----------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 73 qnpeFDPnatilEQVFKSDSQIMNVIRDyenilEEIS---QNPDDS-----TLQKKL---LYLTDNMNAQDAWEienQVK 141
Cdd:COG4172 73 ----FDG-----QDLLGLSERELRRIRG-----NRIAmifQEPMTSlnplhTIGKQIaevLRLHRGLSGAAARA---RAL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 142 TILTKLGIHN-------F-HQkietLSGGQKKRVALASALISPCDLLILDEPTNHMDHdTI-----DWLEKyLTNRTG-S 207
Cdd:COG4172 136 ELLERVGIPDperrldaYpHQ----LSGGQRQRVMIAMALANEPDLLIADEPTTALDV-TVqaqilDLLKD-LQRELGmA 209
|
250
....*....|....*....
gi 928932812 208 LLMITHD----RYFLDRVV 222
Cdd:COG4172 210 LLLITHDlgvvRRFADRVA 228
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
319-375 |
4.34e-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: 60.14 E-value: 4.34e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 928932812 319 IEINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSI 375
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSV 57
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-186 |
4.46e-10 |
|
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: 60.38 E-value: 4.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 1 MNILSVENISKSYGE-KILFeNISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKV--------HMPS----KMA 67
Cdd:COG0410 1 MPMLEVENLHAGYGGiHVLH-GVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIrfdgeditGLPPhriaRLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 68 IEYLSQNpefdpnatilEQVFKSdsqiMNVirdYENILeeisqnpddstlqkkLLYLTDNMNAQDAWEIEnQVKTILTKL 147
Cdd:COG0410 80 IGYVPEG----------RRIFPS----LTV---EENLL---------------LGAYARRDRAEVRADLE-RVYELFPRL 126
|
170 180 190
....*....|....*....|....*....|....*....
gi 928932812 148 GiHNFHQKIETLSGGQKKRVALASALISPCDLLILDEPT 186
Cdd:COG0410 127 K-ERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
13-247 |
5.31e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 63.01 E-value: 5.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 13 YGEKILfENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKmaIEYLSQNPEFDPNAtileqvfksds 92
Cdd:TIGR01271 437 YVTPVL-KNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR--ISFSPQTSWIMPGT----------- 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 93 qimnvIRDyeNILEEISQNPDDSTLQKKLLYLTdnmnaQDAWEIENQVKTILTKLGIhnfhqkieTLSGGQKKRVALASA 172
Cdd:TIGR01271 503 -----IKD--NIIFGLSYDEYRYTSVIKACQLE-----EDIALFPEKDKTVLGEGGI--------TLSGGQRARISLARA 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 173 LISPCDLLILDEPTNHMDHDTidwlEKYLTNRTGSLLMITHDRYFLD------RVVNKTLELDDGKIYSYiGNYSQFIEK 246
Cdd:TIGR01271 563 VYKDADLYLLDSPFTHLDVVT----EKEIFESCLCKLMSNKTRILVTsklehlKKADKILLLHEGVCYFY-GTFSELQAK 637
|
.
gi 928932812 247 K 247
Cdd:TIGR01271 638 R 638
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1-190 |
5.53e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 60.53 E-value: 5.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 1 MNIlSVENISKSYGEKILFE-----NISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMpSKMAIEYLSQNP 75
Cdd:PRK13649 1 MGI-NLQNVSYTYQAGTPFEgralfDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRV-DDTLITSTSKNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 76 EFDPNATILEQVFK-SDSQIMNvirdyENILEEISQNPDDSTLQKKllyltdnmnaqdawEIENQVKTILTKLGIHN--F 152
Cdd:PRK13649 79 DIKQIRKKVGLVFQfPESQLFE-----ETVLKDVAFGPQNFGVSQE--------------EAEALAREKLALVGISEslF 139
|
170 180 190
....*....|....*....|....*....|....*...
gi 928932812 153 HQKIETLSGGQKKRVALASALISPCDLLILDEPTNHMD 190
Cdd:PRK13649 140 EKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
3-220 |
5.81e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.19 E-value: 5.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGydvadtgkVHMPSKMAIEYLSQNPEFDPNAT 82
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAG--------LLNPEKGEILFERQSIKKDLCTY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 83 ILEQVFksdsqimnvirdyenILEEISQNPdDSTLQKKLLYltDNMNAQDAWEIENQVKtiLTKLGiHNFHQKIETLSGG 162
Cdd:PRK13540 73 QKQLCF---------------VGHRSGINP-YLTLRENCLY--DIHFSPGAVGITELCR--LFSLE-HLIDYPCGLLSSG 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 928932812 163 QKKRVALASALISPCDLLILDEPTNHMDHDTID-WLEKYLTNRT--GSLLMITHDRYFLDR 220
Cdd:PRK13540 132 QKRQVALLRLWMSKAKLWLLDEPLVALDELSLLtIITKIQEHRAkgGAVLLTSHQDLPLNK 192
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-233 |
6.02e-10 |
|
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: 59.08 E-value: 6.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAG---YDVADtGKV--------HMP----SKMAI 68
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpkYEVTE-GEIlfkgeditDLPpeerARLGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 69 EYLSQNPEFDPNATIleqvfksdsqiMNVIRdyenileeisqnpddstlqkkllyltdNMNaqdaweienqvktiltklg 148
Cdd:cd03217 80 FLAFQYPPEIPGVKN-----------ADFLR---------------------------YVN------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 149 ihnfhqkiETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEK---YLTNRTGSLLMITHDRYFLDRVV-NK 224
Cdd:cd03217 103 --------EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEvinKLREEGKSVLIITHYQRLLDYIKpDR 174
|
....*....
gi 928932812 225 TLELDDGKI 233
Cdd:cd03217 175 VHVLYDGRI 183
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
319-497 |
6.91e-10 |
|
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: 59.46 E-value: 6.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFEQNKVIEDFSyIALKD-DRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIG-------PTVK--IGYFSQ 388
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLS-LTVEPgEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDgrdvtgvPPERrnIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 389 ESEDMDiNLRAIEYI----KEKAeyiTTEDGIKISASQMMENFLFSKDLQwTYISKLSGGERRRLYLLRILMDAPNVLIL 464
Cdd:cd03259 80 DYALFP-HLTVAENIafglKLRG---VPKAEIRARVRELLELVGLEGLLN-RYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 928932812 465 DEPTNDLDIDT----LKVLENYIDDFNGIVICVSHDR 497
Cdd:cd03259 155 DEPLSALDAKLreelREELKELQRELGITTIYVTHDQ 191
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
319-507 |
1.01e-09 |
|
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: 57.82 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFEQNKVIEDFSyIALKDDRI-GIIGKNGTGKSTLLNLITGKLTPDLGSIDIgptvkigyfsqesedmdinl 397
Cdd:cd03216 1 LELRGITKRFGGVKALDGVS-LSVRRGEVhALLGENGAGKSTLMKILSGLYKPDSGEILV-------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 398 raieyikekaeyitteDGIKISASQMMEnflfSKDLQWTYISKLSGGERRRLYLLRILMDAPNVLILDEPTNDLDIDTLK 477
Cdd:cd03216 60 ----------------DGKEVSFASPRD----ARRAGIAMVYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVE 119
|
170 180 190
....*....|....*....|....*....|....*.
gi 928932812 478 VLENYIDDF--NGI-VICVSHdryFLD---RICNKI 507
Cdd:cd03216 120 RLFKVIRRLraQGVaVIFISH---RLDevfEIADRV 152
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
349-496 |
1.29e-09 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 58.01 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 349 IIGKNGTGKSTLLNLITGKLTPDLGSIDIGPTVKIGYFSQESEDMD-INLRAIEYI-------KEKAEYITTEDgiKISA 420
Cdd:NF040873 23 VVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDsLPLTVRDLVamgrwarRGLWRRLTRDD--RAAV 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 928932812 421 SQMMENfLFSKDLQWTYISKLSGGERRRLYLLRILMDAPNVLILDEPTNDLDIDTLKVLENYIDDFNG---IVICVSHD 496
Cdd:NF040873 101 DDALER-VGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHArgaTVVVVTHD 178
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-214 |
1.60e-09 |
|
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: 58.85 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYGE-KILFENISFSIGDTDKIGLIGVNGTGKSSLLK-------------IIAGYDVADTGKVHMPSKmaIE 69
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKminrlieptsgeiFIDGEDIREQDPVELRRK--IG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 70 YLSQNPEFDPNATILeqvfksdsqimnvirdyENIleeisqnpddsTLQKKLLyltdnmnaqdAWE---IENQVKTI--L 144
Cdd:cd03295 79 YVIQQIGLFPHMTVE-----------------ENI-----------ALVPKLL----------KWPkekIRERADELlaL 120
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 928932812 145 TKLGIHNFHQKI-ETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYLTN------RTgsLLMITHD 214
Cdd:cd03295 121 VGLDPAEFADRYpHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRlqqelgKT--IVFVTHD 195
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
319-516 |
1.69e-09 |
|
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: 58.31 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIGPTV-------------KIGY 385
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKltddkkninelrqKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 386 FSQeSEDMDINLRAIEYI---------------KEKAEYITTEDGIKISASQmmenflfskdlqwtYISKLSGGERRRLY 450
Cdd:cd03262 81 VFQ-QFNLFPHLTVLENItlapikvkgmskaeaEERALELLEKVGLADKADA--------------YPAQLSGGQQQRVA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 928932812 451 LLRILMDAPNVLILDEPTNDLDI----DTLKVLENYIDDfnGI-VICVSHDRYFLDRICNKIFFFAgDGKI 516
Cdd:cd03262 146 IARALAMNPKVMLFDEPTSALDPelvgEVLDVMKDLAEE--GMtMVVVTHEMGFAREVADRVIFMD-DGRI 213
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
318-375 |
1.81e-09 |
|
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: 58.90 E-value: 1.81e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 928932812 318 IIEINHISKSFEQNKVIEDFSyIALKDDRI-GIIGKNGTGKSTLLNLITGKLTPDLGSI 375
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVS-LEVERGEIvGLIGPNGAGKTTLFNLITGFYRPTSGRI 61
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
2-234 |
2.01e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 58.99 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 2 NILSVENISKSY--GEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVhmpskmaieylsqnpeFDP 79
Cdd:PRK13648 6 SIIVFKNVSFQYqsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEI----------------FYN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 80 NATILEQVFKSdsqimnvIRDYENIleeISQNPDD----STLQKKLLY-LTDNMNAQDawEIENQVKTILTKLGIHNF-H 153
Cdd:PRK13648 70 NQAITDDNFEK-------LRKHIGI---VFQNPDNqfvgSIVKYDVAFgLENHAVPYD--EMHRRVSEALKQVDMLERaD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 154 QKIETLSGGQKKRVALASALISPCDLLILDEPTNHMD----HDTIDWLEKYLTNRTGSLLMITHDryfLDRVV--NKTLE 227
Cdd:PRK13648 138 YEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDpdarQNLLDLVRKVKSEHNITIISITHD---LSEAMeaDHVIV 214
|
....*..
gi 928932812 228 LDDGKIY 234
Cdd:PRK13648 215 MNKGTVY 221
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
4-213 |
2.07e-09 |
|
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: 57.56 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYGEKILfENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGY--DVADTGKVH---MPSKM-----AIEYLSQ 73
Cdd:cd03213 11 VTVKSSPSKSGKQLL-KNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLingRPLDKrsfrkIIGYVPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 74 NPEFDPNATILEqvfksdsqimnvirdyenileeisqnpddsTLQkkllyltdnmnaqdaweienqvktiltklgihnFH 153
Cdd:cd03213 90 DDILHPTLTVRE------------------------------TLM---------------------------------FA 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 928932812 154 QKIETLSGGQKKRVALASALISPCDLLILDEPTNHMD----HDTIDWLEKY-LTNRTgsLLMITH 213
Cdd:cd03213 107 AKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDsssaLQVMSLLRRLaDTGRT--IICSIH 169
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-247 |
2.14e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 60.42 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSY--GEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAG-YDVaDTGKVHMPSKMAIEYLSQNPEfDPN 80
Cdd:PRK11176 342 IEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRfYDI-DEGEILLDGHDLRDYTLASLR-NQV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 81 ATILEQVFKSDSQIMNVI---RDYENILEEISQnpddstlQKKLLYLTDNMNaqdawEIENQVKTILTKLGIhnfhqkie 157
Cdd:PRK11176 420 ALVSQNVHLFNDTIANNIayaRTEQYSREQIEE-------AARMAYAMDFIN-----KMDNGLDTVIGENGV-------- 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 158 TLSGGQKKRVALASALISPCDLLILDEPTNHMD-------HDTIDWLEKyltNRTgsLLMITHdRYFLDRVVNKTLELDD 230
Cdd:PRK11176 480 LLSGGQRQRIAIARALLRDSPILILDEATSALDteseraiQAALDELQK---NRT--SLVIAH-RLSTIEKADEILVVED 553
|
250
....*....|....*..
gi 928932812 231 GKIYSYiGNYSQFIEKK 247
Cdd:PRK11176 554 GEIVER-GTHAELLAQN 569
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
156-220 |
2.19e-09 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 57.62 E-value: 2.19e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 928932812 156 IETLSGGQKK------RVALASALISPCDLLILDEPTNHMDHDTIDW-----LEKYLTNRTGSLLMITHDRYFLDR 220
Cdd:cd03240 113 RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEEslaeiIEERKSQKNFQLIVITHDEELVDA 188
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2-251 |
2.35e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 58.71 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 2 NILSVENISKSYGEKI-LFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKmAIEYLSQN-PEFDP 79
Cdd:PRK13636 4 YILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGK-PIDYSRKGlMKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 80 NATIleqVFKS-DSQIMNVirdyeNILEEISQNPDDSTLQKKllyltdnmnaqdawEIENQVKTILTKLGI-HNFHQKIE 157
Cdd:PRK13636 83 SVGM---VFQDpDNQLFSA-----SVYQDVSFGAVNLKLPED--------------EVRKRVDNALKRTGIeHLKDKPTH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 158 TLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYLTNRTG----SLLMITHDRYFLDRVVNKTLELDDGKI 233
Cdd:PRK13636 141 CLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelglTIIIATHDIDIVPLYCDNVFVMKEGRV 220
|
250
....*....|....*...
gi 928932812 234 YSYIGNYSQFIEKKLERK 251
Cdd:PRK13636 221 ILQGNPKEVFAEKEMLRK 238
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1-193 |
2.37e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 58.05 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 1 MNILSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAG--YDVADTGKVHMPskmaieylsqNPEFD 78
Cdd:COG2401 28 AIVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVP----------DNQFG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 79 PNATILEQVFKSDSqimnvirdyenileeisqnPDDStlqkklLYLTDNMNAQDAWeienqvktiltklgihNFHQKIET 158
Cdd:COG2401 98 REASLIDAIGRKGD-------------------FKDA------VELLNAVGLSDAV----------------LWLRRFKE 136
|
170 180 190
....*....|....*....|....*....|....*
gi 928932812 159 LSGGQKKRVALASALISPCDLLILDEPTNHMDHDT 193
Cdd:COG2401 137 LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-233 |
2.70e-09 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 58.22 E-value: 2.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 1 MNILSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHM------------PSKMAI 68
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidtarslsQQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 69 EYLSQNPEFdpnatileqVFKSdsqiMNVIrDYENILEEISQNPddsTLQKKllyltdnmnaQDAWEIENQVKTILTKLG 148
Cdd:PRK11264 81 RQLRQHVGF---------VFQN----FNLF-PHRTVLENIIEGP---VIVKG----------EPKEEATARARELLAKVG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 149 IHNFHQKI-ETLSGGQKKRVALASALISPCDLLILDEPTNHMDHD-------TIDWLEKylTNRTgsLLMITHDRYFLDR 220
Cdd:PRK11264 134 LAGKETSYpRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPElvgevlnTIRQLAQ--EKRT--MVIVTHEMSFARD 209
|
250
....*....|...
gi 928932812 221 VVNKTLELDDGKI 233
Cdd:PRK11264 210 VADRAIFMDQGRI 222
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
316-519 |
3.84e-09 |
|
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: 59.53 E-value: 3.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 316 QKIIEINHISKSF--EQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGkLTPDLGSI------------DIGPTV 381
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMG-LLPHGGRIsgevlldgrdllELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 382 ---KIGYFSQESEDMDINLRAIEYIKEKAE-YITTEDGIKISASQMMENFLFSKDLQwTYISKLSGGERRRLYLLRILMD 457
Cdd:COG1123 81 rgrRIGMVFQDPMTQLNPVTVGDQIAEALEnLGLSRAEARARVLELLEAVGLERRLD-RYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 928932812 458 APNVLILDEPTNDLDIDT----LKVLENYIDDFNGIVICVSHDRYFLDRICNKIFFFAgDGKIIEH 519
Cdd:COG1123 160 DPDLLIADEPTTALDVTTqaeiLDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMD-DGRIVED 224
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
15-212 |
4.41e-09 |
|
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: 57.28 E-value: 4.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 15 EKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVAD---TGKV---HMPSKMA-----IEYLSQNPEFDPNATI 83
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQIlfnGQPRKPDqfqkcVAYVRQDDILLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 84 LEQVFksdsqimnvirdYENILeeisqnpddstlqkKLLYLTDNMNAQDAWEIENQVKTILTKLGihnfHQKIETLSGGQ 163
Cdd:cd03234 99 RETLT------------YTAIL--------------RLPRKSSDAIRKKRVEDVLLRDLALTRIG----GNLVKGISGGE 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 928932812 164 KKRVALASALISPCDLLILDEPTNHMD----HDTIDWLEKYLtnRTGSLLMIT 212
Cdd:cd03234 149 RRRVSIAVQLLWDPKVLILDEPTSGLDsftaLNLVSTLSQLA--RRNRIVILT 199
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
319-530 |
4.56e-09 |
|
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: 59.39 E-value: 4.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFEQNK-VIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIGPTV-----------KIGYF 386
Cdd:COG4988 337 IELEDVSFSYPGGRpALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDlsdldpaswrrQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 387 SQES-------EDmdiNLR---------AIEYIKEKA---EYITT-EDGIkisASQMMENFlfskdlqwtyiSKLSGGEr 446
Cdd:COG4988 417 PQNPylfagtiRE---NLRlgrpdasdeELEAALEAAgldEFVAAlPDGL---DTPLGEGG-----------RGLSGGQ- 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 447 rrlyllrilmdA------------PNVLILDEPTNDLDIDTLKVLENYIDDF--NGIVICVSHDRYFLDRiCNKIFFFAg 512
Cdd:COG4988 479 -----------AqrlalarallrdAPLLLLDEPTAHLDAETEAEILQALRRLakGRTVILITHRLALLAQ-ADRILVLD- 545
|
250
....*....|....*...
gi 928932812 513 DGKIIEhTGNYSDFYKSG 530
Cdd:COG4988 546 DGRIVE-QGTHEELLAKN 562
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
319-496 |
5.15e-09 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 57.35 E-value: 5.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIG------PTVK---IGYFSQE 389
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGgedatdVPVQernVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 390 ---------SEDMDINLRaieyIKEKAEYiTTEDGIKISASQMMENFLFSKdLQWTYISKLSGGERRRLYLLRILMDAPN 460
Cdd:cd03296 83 yalfrhmtvFDNVAFGLR----VKPRSER-PPEAEIRAKVHELLKLVQLDW-LADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 928932812 461 VLILDEPTNDLDIDTLKVLENYI----DDFNGIVICVSHD 496
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLrrlhDELHVTTVFVTHD 196
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-260 |
5.67e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 57.09 E-value: 5.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIagydvadtgkvhmpSKMAieylsqnpEFDPNAT 82
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSI--------------NRMN--------DLNPEVT 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 83 ILEQVFKSDSQIMNVIRDYENILEEISQ-----NPDDSTLQKKLLYLTDNMNAQDAWEIENQVKTILTKLGIHN-----F 152
Cdd:PRK14239 63 ITGSIVYNGHNIYSPRTDTVDLRKEIGMvfqqpNPFPMSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDevkdrL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 153 HQKIETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYLTN--RTGSLLMITHDRYFLDRVVNKTLELDD 230
Cdd:PRK14239 143 HDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGlkDDYTMLLVTRSMQQASRISDRTGFFLD 222
|
250 260 270
....*....|....*....|....*....|
gi 928932812 231 GKIYSYIGNYSQFIEKKleRKTLESSIERK 260
Cdd:PRK14239 223 GDLIEYNDTKQMFMNPK--HKETEDYISGK 250
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-472 |
5.86e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 58.95 E-value: 5.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 1 MNILSVENISKSY----GEKILFENISFSIGDTDKIGLIGVNGTGKS----SLLKIiagydvadtgkvhMPSKmAIEYLS 72
Cdd:PRK15134 3 QPLLAIENLSVAFrqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRL-------------LPSP-PVVYPS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 73 QNPEFDPnatilEQVFKSDSQIMNVIRDyeNILEEISQNPDDS-----TLQKKL---LYLTDNMNAQDAweiENQVKTIL 144
Cdd:PRK15134 69 GDIRFHG-----ESLLHASEQTLRGVRG--NKIAMIFQEPMVSlnplhTLEKQLyevLSLHRGMRREAA---RGEILNCL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 145 TKLGIHNFHQKI----ETLSGGQKKRVALASALISPCDLLILDEPTNHMD---HDTIDWLEKYLTNRTG-SLLMITHD-- 214
Cdd:PRK15134 139 DRVGIRQAAKRLtdypHQLSGGERQRVMIAMALLTRPELLIADEPTTALDvsvQAQILQLLRELQQELNmGLLFITHNls 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 215 --RYFLDRVVnktlelddgkiysyIGNYSQFIEKKLERKTLESSIERKRERLYKKELEwiraGAQARSTKQKARIQRFEE 292
Cdd:PRK15134 219 ivRKLADRVA--------------VMQNGRCVEQNRAATLFSAPTHPYTQKLLNSEPS----GDPVPLPEPASPLLDVEQ 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 293 LkNTSSPIHDSNIDICVAHsrlgqkiieinhisksfeqNKVIEDFSYIALKDDRIGIIGKNGTGKST----LLNLITGKl 368
Cdd:PRK15134 281 L-QVAFPIRKGILKRTVDH-------------------NVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQ- 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 369 tpdlGSI--DIGPTVKIG-------------YFSQESEDMDINLRAIEYIKEkaeyittedGIKI-----SASQ------ 422
Cdd:PRK15134 340 ----GEIwfDGQPLHNLNrrqllpvrhriqvVFQDPNSSLNPRLNVLQIIEE---------GLRVhqptlSAAQreqqvi 406
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 928932812 423 -MMENFLFSKDLQWTYISKLSGGERRRLYLLRILMDAPNVLILDEPTNDLD 472
Cdd:PRK15134 407 aVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
319-472 |
5.97e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 58.30 E-value: 5.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDI-GPTV---------KIGYFSQ 388
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVlGVPVpararlaraRIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 389 -ESEDMDINLRAIEYIKEKAEYITTEDgIKISASQMMEnFLFSKDLQWTYISKLSGGERRRLYLLRILMDAPNVLILDEP 467
Cdd:PRK13536 122 fDNLDLEFTVRENLLVFGRYFGMSTRE-IEAVIPSLLE-FARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEP 199
|
....*
gi 928932812 468 TNDLD 472
Cdd:PRK13536 200 TTGLD 204
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
319-518 |
6.24e-09 |
|
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: 56.77 E-value: 6.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFEQNK----------------------VIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSID 376
Cdd:cd03220 1 IELENVSKSYPTYKggssslkklgilgrkgevgefwALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 377 IGPTVK----IGYFSQES---EDmDINLRAI------EYIKEKAEYIttedgikISASQMmENFLfskDLQwtyISKLSG 443
Cdd:cd03220 81 VRGRVSsllgLGGGFNPEltgRE-NIYLNGRllglsrKEIDEKIDEI-------IEFSEL-GDFI---DLP---VKTYSS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 444 GerrrlyllrilMDA-----------PNVLILDEPTNDLDIDT----LKVLENYIDDfNGIVICVSHDRYFLDRICNKIF 508
Cdd:cd03220 146 G-----------MKArlafaiatalePDILLIDEVLAVGDAAFqekcQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRAL 213
|
250
....*....|
gi 928932812 509 FFAgDGKIIE 518
Cdd:cd03220 214 VLE-KGKIRF 222
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
17-213 |
6.91e-09 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 58.99 E-value: 6.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 17 ILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKMAIEYLSQNPEFDpNATILEQVFKSDS---Q 93
Cdd:TIGR00954 466 VLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPYMT-LGTLRDQIIYPDSsedM 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 94 IMNVIRDYEniLEEISQNpddstlqkklLYLTDNMNAQDAWEIENQVKtiltklgihnfhqkiETLSGGQKKRVALASAL 173
Cdd:TIGR00954 545 KRRGLSDKD--LEQILDN----------VQLTHILEREGGWSAVQDWM---------------DVLSGGEKQRIAMARLF 597
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 928932812 174 ISPCDLLILDEPTNHMDHDTIDWLEKYLTNRTGSLLMITH 213
Cdd:TIGR00954 598 YHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
21-214 |
1.28e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 56.43 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 21 NISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKV---HMPSKMA-----IEYLSQNPEFDPNATILEQ--VFKS 90
Cdd:PRK15056 25 DASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKIsilGQPTRQAlqknlVAYVPQSEEVDWSFPVLVEdvVMMG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 91 DSQIMNVIRDYENILEEIsqnpddstlqkkllyltdnmnaqdaweienqVKTILTKLGIHNF-HQKIETLSGGQKKRVAL 169
Cdd:PRK15056 105 RYGHMGWLRRAKKRDRQI-------------------------------VTAALARVDMVEFrHRQIGELSGGQKKRVFL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 928932812 170 ASALISPCDLLILDEPTNHMDHDT---IDWLEKYLTNRTGSLLMITHD 214
Cdd:PRK15056 154 ARAIAQQGQVILLDEPFTGVDVKTearIISLLRELRDEGKTMLVSTHN 201
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-236 |
1.30e-08 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 55.50 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYG---EKILfENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMpskmaieylsqnpefdpn 80
Cdd:cd03369 7 IEVENLSVRYApdlPPVL-KNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEI------------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 81 atileqvfksDSQIMNVI--RDYENILEEISQNPD--DSTLQKKLlyltDNMNAQDAWEIENQVKtilTKLGIHNfhqki 156
Cdd:cd03369 68 ----------DGIDISTIplEDLRSSLTIIPQDPTlfSGTIRSNL----DPFDEYSDEEIYGALR---VSEGGLN----- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 157 etLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYL----TNRTgsLLMITHD-RYFLDrvVNKTLELDDG 231
Cdd:cd03369 126 --LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIreefTNST--ILTIAHRlRTIID--YDKILVMDAG 199
|
....*
gi 928932812 232 KIYSY 236
Cdd:cd03369 200 EVKEY 204
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-190 |
1.35e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 56.22 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 32 IGLIGVNGTGKSSLLKIIAGYDVADTGKvhmpskmaieyLSQNPEFDpnaTILEQVFKSDSQI---------MNVIRDYE 102
Cdd:cd03236 29 LGLVGPNGIGKSTALKILAGKLKPNLGK-----------FDDPPDWD---EILDEFRGSELQNyftkllegdVKVIVKPQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 103 NIlEEISQNPDDSTLQkkLLYLTDNMNAQDaweienqvkTILTKLGIHN-FHQKIETLSGGQKKRVALASALISPCDLLI 181
Cdd:cd03236 95 YV-DLIPKAVKGKVGE--LLKKKDERGKLD---------ELVDQLELRHvLDRNIDQLSGGELQRVAIAAALARDADFYF 162
|
....*....
gi 928932812 182 LDEPTNHMD 190
Cdd:cd03236 163 FDEPSSYLD 171
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
319-516 |
1.41e-08 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 57.16 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIG-----------PTVKIGYFS 387
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAgddvealsaraASRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 388 QE-SEDMDINLRAI------EYIKEKAEYITTEDGIKISASQMMENFLFSKdlqwTYISKLSGGERRRLYLLRILMDAPN 460
Cdd:PRK09536 84 QDtSLSFEFDVRQVvemgrtPHRSRFDTWTETDRAAVERAMERTGVAQFAD----RPVTSLSGGERQRVLLARALAQATP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 461 VLILDEPTNDLDID----TLKVLENYIDDFNGIVICVsHDRYFLDRICNKIFFFAgDGKI 516
Cdd:PRK09536 160 VLLLDEPTASLDINhqvrTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLA-DGRV 217
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-186 |
1.42e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 57.72 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISKSYGekilFENISFSI--GDTdkIGLIGVNGTGKSSLLKIIAGYDVADTGKVHM---------PSKmAIE-- 69
Cdd:COG1129 256 VLEVEGLSVGGV----VRDVSFSVraGEI--LGIAGLVGAGRTELARALFGADPADSGEIRLdgkpvrirsPRD-AIRag 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 70 --YLSQNPefdpnatileqvfKSDS--QIMNVirdYENI-LeeisqnpddSTLQKkllyLTDNMNAQDAWEIEnQVKTIL 144
Cdd:COG1129 329 iaYVPEDR-------------KGEGlvLDLSI---RENItL---------ASLDR----LSRGGLLDRRRERA-LAEEYI 378
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 928932812 145 TKLGI--HNFHQKIETLSGG--QKkrVALASALISPCDLLILDEPT 186
Cdd:COG1129 379 KRLRIktPSPEQPVGNLSGGnqQK--VVLAKWLATDPKVLILDEPT 422
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
319-389 |
1.43e-08 |
|
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: 55.56 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFEQN----KVIEDFSyIALKD-DRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDI------GPTVKIGYFS 387
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDIS-LSVEEgEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVdgepvtGPGPDRGYVF 79
|
..
gi 928932812 388 QE 389
Cdd:cd03293 80 QQ 81
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
15-233 |
1.44e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 56.25 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 15 EKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHmpskmaieylsqnpefdpnatileqVFKSDSQI 94
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVY-------------------------VDGLDTSD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 95 MNVIRDYENILEEISQNPDD----STLQKKLLYLTDNMNAQdAWEIENQVKTILTKLGIHNFHQKI-ETLSGGQKKRVAL 169
Cdd:PRK13633 77 EENLWDIRNKAGMVFQNPDNqivaTIVEEDVAFGPENLGIP-PEEIRERVDESLKKVGMYEYRRHApHLLSGGQKQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 170 ASALISPCDLLILDEPTNHMD----HDTIDWLEKYLTNRTGSLLMITHdryFLDRVV--NKTLELDDGKI 233
Cdd:PRK13633 156 AGILAMRPECIIFDEPTAMLDpsgrREVVNTIKELNKKYGITIILITH---YMEEAVeaDRIIVMDSGKV 222
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-252 |
1.49e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 56.78 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISKSYGEK-----ILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHmpskmaIEYLSQNPEF 77
Cdd:PRK13631 21 ILRVKNLYCVFDEKqenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQ------VGDIYIGDKK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 78 DPNATILEQVFKSdsqimnvIRDYENILEEIS---QNPD----DSTLQKKLLYLTDNMnAQDAWEIENQVKTILTKLGIH 150
Cdd:PRK13631 95 NNHELITNPYSKK-------IKNFKELRRRVSmvfQFPEyqlfKDTIEKDIMFGPVAL-GVKKSEAKKLAKFYLNKMGLD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 151 NFHQKIET--LSGGQKKRVALASALISPCDLLILDEPTNHMD----HDTIDW-LEKYLTNRTgsLLMITHDRYFLDRVVN 223
Cdd:PRK13631 167 DSYLERSPfgLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDpkgeHEMMQLiLDAKANNKT--VFVITHTMEHVLEVAD 244
|
250 260
....*....|....*....|....*....
gi 928932812 224 KTLELDDGKIYSYIGNYSQFIEKKLERKT 252
Cdd:PRK13631 245 EVIVMDKGKILKTGTPYEIFTDQHIINST 273
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
283-530 |
1.80e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 57.28 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 283 QKARIQRFEELKNTSSPIHD--SNIDIcvahSRLgQKIIEINHISKSFEQNK-VIEDFSYIALKDDRIGIIGKNGTGKST 359
Cdd:PRK13657 302 AAPKLEEFFEVEDAVPDVRDppGAIDL----GRV-KGAVEFDDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKST 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 360 LLNLITGKLTPDLGSIDI------GPTVK-----IGYFSQESEDMDinlRAI-EYI---KEKAeyitTEDGIKISAS--Q 422
Cdd:PRK13657 377 LINLLQRVFDPQSGRILIdgtdirTVTRAslrrnIAVVFQDAGLFN---RSIeDNIrvgRPDA----TDEEMRAAAEraQ 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 423 MMEnFLFSKDLQW-TYI----SKLSGGERRRLYLLRILMDAPNVLILDEPTNDLDIDTLKVLENYIDdfngiviCVSHDR 497
Cdd:PRK13657 450 AHD-FIERKPDGYdTVVgergRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALD-------ELMKGR 521
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 928932812 498 ------YFLDRICN--KIFFFAgDGKIIEhTGNYSDFYKSG 530
Cdd:PRK13657 522 ttfiiaHRLSTVRNadRILVFD-NGRVVE-SGSFDELVARG 560
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-186 |
2.13e-08 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 55.22 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKV--------HMPS----KMAIEYL 71
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIrldgeditKLPPheraRAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 72 SQNPEFDPNATIleqvfksdsqimnvirdYENILEEISQNPDDSTLQKKLLY-----LTDNMnaqdaweienqvktiltk 146
Cdd:TIGR03410 81 PQGREIFPRLTV-----------------EENLLTGLAALPRRSRKIPDEIYelfpvLKEML------------------ 125
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 928932812 147 lgihnfHQKIETLSGGQKKRVALASALISPCDLLILDEPT 186
Cdd:TIGR03410 126 ------GRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
315-472 |
2.39e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 56.01 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 315 GQKIIEINHISKSFEQN-----KVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIGPTVKIGYFSQE 389
Cdd:PRK13631 18 DDIILRVKNLYCVFDEKqenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 390 SEDMDINLRAIEYIKEK----------AEYITTEDGI--------------KISASQMMENFLFSKDLQWTYISK----L 441
Cdd:PRK13631 98 ELITNPYSKKIKNFKELrrrvsmvfqfPEYQLFKDTIekdimfgpvalgvkKSEAKKLAKFYLNKMGLDDSYLERspfgL 177
|
170 180 190
....*....|....*....|....*....|.
gi 928932812 442 SGGERRRLYLLRILMDAPNVLILDEPTNDLD 472
Cdd:PRK13631 178 SGGQKRRVAIAGILAIQPEILIFDEPTAGLD 208
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
318-495 |
2.96e-08 |
|
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: 55.09 E-value: 2.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 318 IIEINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTP-----------DLGSIDIgPTVK--IG 384
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPtygndvrlfgeRRGGEDV-WELRkrIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 385 YFSQE-SEDMDINLRAIEYI-----------KEkaeyITTEDgiKISASQMMENFLFSkDLQWTYISKLSGGErrrlyll 452
Cdd:COG1119 82 LVSPAlQLRFPRDETVLDVVlsgffdsiglyRE----PTDEQ--RERARELLELLGLA-HLADRPFGTLSQGEqrrvlia 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 928932812 453 rilMDAPNVLILDEPTNDLDI----DTLKVLENYIDDFNGIVICVSH 495
Cdd:COG1119 155 ralVKDPELLILDEPTAGLDLgareLLLALLDKLAAEGAPTLVLVTH 201
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-186 |
3.12e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 57.06 E-value: 3.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISKSYGEKILFENISFSI--GDTdkIGLIGVNGTGKSSLLKIIAGYDVADTGKVHmpskmaieylsqnpefdpn 80
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIpaGCM--VGLIGPDGVGKSSLLSLIAGARKIQQGRVE------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 81 atileqVFKSDsqiMNVIRDYENILEEISQNPddstlQ--KKLLYLT----DNMN------AQDAWEIENQVKTILTKLG 148
Cdd:NF033858 60 ------VLGGD---MADARHRRAVCPRIAYMP-----QglGKNLYPTlsvfENLDffgrlfGQDAAERRRRIDELLRATG 125
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 928932812 149 IHNFH----QKietLSGGQKKRVALASALISPCDLLILDEPT 186
Cdd:NF033858 126 LAPFAdrpaGK---LSGGMKQKLGLCCALIHDPDLLILDEPT 164
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
311-519 |
3.40e-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: 54.09 E-value: 3.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 311 HSRLGQKIIEINHISKSFEQNK-VIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTP--DLGSIDI-GPTVK---- 382
Cdd:cd03213 1 GVTLSFRNLTVTVKSSPSKSGKqLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLInGRPLDkrsf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 383 ---IGYFSQEsedmDINLraieyikekaEYITTEdgikisasqmmENFLFSKDLQwtyisKLSGGERRRLYLLRILMDAP 459
Cdd:cd03213 81 rkiIGYVPQD----DILH----------PTLTVR-----------ETLMFAAKLR-----GLSGGERKRVSIALELVSNP 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 928932812 460 NVLILDEPTNDLD----IDTLKVLENYIDDfNGIVICVSHD-RYFLDRICNKIFFFAgDGKIIEH 519
Cdd:cd03213 131 SLLFLDEPTSGLDsssaLQVMSLLRRLADT-GRTIICSIHQpSSEIFELFDKLLLLS-QGRVIYF 193
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
318-385 |
3.42e-08 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 55.10 E-value: 3.42e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 928932812 318 IIEINHISKSFEQNK----VIEDFSyIALKD-DRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDI------GPTVKIGY 385
Cdd:COG1116 7 ALELRGVSKRFPTGGggvtALDDVS-LTVAAgEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVdgkpvtGPGPDRGV 84
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-186 |
3.85e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 54.50 E-value: 3.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 1 MNILSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVhmpskmaieylsqnpEFDPN 80
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRI---------------VFDGK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 81 ATileqvfkSDSQIMNVIRDYENILEEISQNPDDSTLQKKLL---YLTDNMNAQDAWEienQVKTILTKLgIHNFHQKIE 157
Cdd:PRK11614 68 DI-------TDWQTAKIMREAVAIVPEGRRVFSRMTVEENLAmggFFAERDQFQERIK---WVYELFPRL-HERRIQRAG 136
|
170 180
....*....|....*....|....*....
gi 928932812 158 TLSGGQKKRVALASALISPCDLLILDEPT 186
Cdd:PRK11614 137 TMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
319-524 |
3.86e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 55.48 E-value: 3.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFEQN-----KVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSI-----DIGPTVKIGYFSQ 388
Cdd:PRK13651 3 IKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 389 ESEDMDINL---RAIEYIKEK----------AEYITTEDGI--------------KISASQMMENFLFSKDLQWTYISK- 440
Cdd:PRK13651 83 VLEKLVIQKtrfKKIKKIKEIrrrvgvvfqfAEYQLFEQTIekdiifgpvsmgvsKEEAKKRAAKYIELVGLDESYLQRs 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 441 ---LSGGERRRLYLLRILMDAPNVLILDEPTNDLD----IDTLKVLENyIDDFNGIVICVSHDryfLDRI---CNKIFFF 510
Cdd:PRK13651 163 pfeLSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpqgvKEILEIFDN-LNKQGKTIILVTHD---LDNVlewTKRTIFF 238
|
250
....*....|....
gi 928932812 511 AgDGKIIEHTGNYS 524
Cdd:PRK13651 239 K-DGKIIKDGDTYD 251
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-215 |
4.07e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 54.33 E-value: 4.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 2 NILSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKmaiEYLSQNPEfdpna 81
Cdd:PRK10247 6 PLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGE---DISTLKPE----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 82 TILEQVFKSdSQIMNVIRD--YENIL---EEISQNPDDSTLQKKLLYLtdnmnaqdaweieNQVKTILTKlgihnfhqKI 156
Cdd:PRK10247 78 IYRQQVSYC-AQTPTLFGDtvYDNLIfpwQIRNQQPDPAIFLDDLERF-------------ALPDTILTK--------NI 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 928932812 157 ETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTI----DWLEKYLTNRTGSLLMITHDR 215
Cdd:PRK10247 136 AELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKhnvnEIIHRYVREQNIAVLWVTHDK 198
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
318-472 |
4.14e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 55.20 E-value: 4.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 318 IIEINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDI-GPTV---------KIGYFS 387
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcGEPVpsrarharqRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 388 QeSEDMDINLRAIEYIKEKAEYITTEDGIKISASQMMENF--LFSK-DLQwtyISKLSGGERRRLYLLRILMDAPNVLIL 464
Cdd:PRK13537 87 Q-FDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFakLENKaDAK---VGELSGGMKRRLTLARALVNDPDVLVL 162
|
....*...
gi 928932812 465 DEPTNDLD 472
Cdd:PRK13537 163 DEPTTGLD 170
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
316-507 |
4.65e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 54.63 E-value: 4.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 316 QKIIEINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLL----NLITGKLTPDLGSIDIGPTVK--------- 382
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsGLITGDKSAGSHIELLGRTVQregrlardi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 383 ------IGYFSQE---------SEDMDIN-LRAIEYIKEKAEYITTEDgiKISASQM-----MENFLFSKdlqwtyISKL 441
Cdd:PRK09984 82 rksranTGYIFQQfnlvnrlsvLENVLIGaLGSTPFWRTCFSWFTREQ--KQRALQAltrvgMVHFAHQR------VSTL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 442 SGGERRRLYLLRILMDAPNVLILDEPTNDLDIDTLKVLENYIDDFN---GIVICVS-HDRYFLDRICNKI 507
Cdd:PRK09984 154 SGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINqndGITVVVTlHQVDYALRYCERI 223
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
346-496 |
5.13e-08 |
|
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: 55.12 E-value: 5.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 346 RIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIGPTVkigyfSQESE---DMDINLRAIEYIKEKA------------EY- 409
Cdd:TIGR02142 25 VTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRT-----LFDSRkgiFLPPEKRRIGYVFQEArlfphlsvrgnlRYg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 410 --ITTEDGIKISASQMMENFLFSKDLQwTYISKLSGGERRRLYLLRILMDAPNVLILDEPTNDLDI----DTLKVLENYI 483
Cdd:TIGR02142 100 mkRARPSERRISFERVIELLGIGHLLG-RLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDprkyEILPYLERLH 178
|
170
....*....|...
gi 928932812 484 DDFNGIVICVSHD 496
Cdd:TIGR02142 179 AEFGIPILYVSHS 191
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
22-236 |
5.20e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 54.17 E-value: 5.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 22 ISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYdVADTGKVHM---------PSKMAIE--YLSQNPefdpNATILEQVFK- 89
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFagqpleawsAAELARHraYLSQQQ----TPPFAMPVFQy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 90 -----SDSqimNVIRDYENILEEISQnpddstlqkkLLYLTDnmnaqdaweienqvktiltKLgihnfHQKIETLSGGQK 164
Cdd:PRK03695 90 ltlhqPDK---TRTEAVASALNEVAE----------ALGLDD-------------------KL-----GRSVNQLSGGEW 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 165 KRVALASAL--ISP-----CDLLILDEPTNHMD---HDTIDWLEKYLTNRTGSLLMITHDryfldrvVNKTLE------- 227
Cdd:PRK03695 133 QRVRLAAVVlqVWPdinpaGQLLLLDEPMNSLDvaqQAALDRLLSELCQQGIAVVMSSHD-------LNHTLRhadrvwl 205
|
....*....
gi 928932812 228 LDDGKIYSY 236
Cdd:PRK03695 206 LKQGKLLAS 214
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
7-233 |
5.35e-08 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 54.01 E-value: 5.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 7 ENISKSYGEK---ILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKMAIEY-----------LS 72
Cdd:cd03248 15 QNVTFAYPTRpdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYehkylhskvslVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 73 QNPefdpnatileQVFKSDSQimnvirdyENILEEISQNPDDSTLQkkllyLTDNMNAQDAweIENQVKTILTKLGihnf 152
Cdd:cd03248 95 QEP----------VLFARSLQ--------DNIAYGLQSCSFECVKE-----AAQKAHAHSF--ISELASGYDTEVG---- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 153 hQKIETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEK--YLTNRTGSLLMITHDRYFLDRvVNKTLELDD 230
Cdd:cd03248 146 -EKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQalYDWPERRTVLVIAHRLSTVER-ADQILVLDG 223
|
...
gi 928932812 231 GKI 233
Cdd:cd03248 224 GRI 226
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
318-385 |
6.10e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 54.73 E-value: 6.10e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 928932812 318 IIEINHISKSFEQNKVIEDFSyIALKDDRI-GIIGKNGTGKSTLLNLITGKLTPDLGSI-----DIGPTV--KIGY 385
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVS-FTVPKGEIfGLLGPNGAGKTTTIRIILGILAPDSGEVlwdgePLDPEDrrRIGY 75
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
272-529 |
6.29e-08 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 55.56 E-value: 6.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 272 IRAGAQARSTKQKAR--IQRFEELKNTSSPIHDSNIDICVAHSRLGqkiIEINHISksF---EQNKVIEDFSYIALKDDR 346
Cdd:COG1132 294 LRQLANVLNQLQRALasAERIFELLDEPPEIPDPPGAVPLPPVRGE---IEFENVS--FsypGDRPVLKDISLTIPPGET 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 347 IGIIGKNGTGKSTLLNLITGKLTPDLGSI--------DIGPTV---KIGYFSQESE--DMDI--NLRaieYIKEKAeyit 411
Cdd:COG1132 369 VALVGPSGSGKSTLVNLLLRFYDPTSGRIlidgvdirDLTLESlrrQIGVVPQDTFlfSGTIreNIR---YGRPDA---- 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 412 TEDGIkISASQM--MENFL--FSKDLQwTYI----SKLSGGErrrly-llrilMDAPnVLILDEPTNDLDIDTLKVLENY 482
Cdd:COG1132 442 TDEEV-EEAAKAaqAHEFIeaLPDGYD-TVVgergVNLSGGQrqriaiarallKDPP-ILILDEATSALDTETEALIQEA 518
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 928932812 483 IDDF--NGIVICVSHdryfldRI-----CNKIFFFAgDGKIIE---HT------GNYSDFYKS 529
Cdd:COG1132 519 LERLmkGRTTIVIAH------RLstirnADRILVLD-DGRIVEqgtHEellargGLYARLYRL 574
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3-61 |
6.69e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 54.16 E-value: 6.69e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 928932812 3 ILSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVH 61
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVH 64
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
319-503 |
6.93e-08 |
|
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: 55.37 E-value: 6.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFE-QNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIGpTVKIGYFSQesedmDINL 397
Cdd:TIGR02857 322 LEFSGVSVAYPgRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVN-GVPLADADA-----DSWR 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 398 RAIEYIKEK--------AEYI------TTEDGIKISASQ--MMEnflFSKDLQWTYISK-------LSGGERRRLYLLRI 454
Cdd:TIGR02857 396 DQIAWVPQHpflfagtiAENIrlarpdASDAEIREALERagLDE---FVAALPQGLDTPigeggagLSGGQAQRLALARA 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 928932812 455 LMDAPNVLILDEPTNDLDIDTLKVLENYIDDF--NGIVICVSHDR---YFLDRI 503
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLDAETEAEVLEALRALaqGRTVLLVTHRLalaALADRI 526
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
319-378 |
7.04e-08 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 54.01 E-value: 7.04e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIG 378
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLN 62
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
4-214 |
7.96e-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: 7.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENIsKSYGEKilfENISFSIGdtdKIGLIGVNGTGKSSLLKIIAgydVADTGKVHMPSKMAIEYLSQNPEfdpnATI 83
Cdd:COG0419 5 LRLENF-RSYRDT---ETIDFDDG---LNLIVGPNGAGKSTILEAIR---YALYGKARSRSKLRSDLINVGSE----EAS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 84 LEQVFKSDSQIMNVIRDYENILEEISQNPDD--------------STLQKKLLYLTDNMNAQ--DAWEIENQVKTILTKL 147
Cdd:COG0419 71 VELEFEHGGKRYRIERRQGEFAEFLEAKPSErkealkrllgleiyEELKERLKELEEALESAleELAELQKLKQEILAQL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 928932812 148 giHNFhQKIETLSGGQKKRVALASALispcdLLILDepTNHMDHDTIDWLEKYLTnrtgSLLMITHD 214
Cdd:COG0419 151 --SGL-DPIETLSGGERLRLALADLL-----SLILD--FGSLDEERLERLLDALE----ELAIITHV 203
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-246 |
1.10e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 55.34 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 22 ISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMpsKMAIEYLSQNPEFDpNATILEQVFKSDSqiMNVIRdY 101
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM--KGSVAYVPQQAWIQ-NDSLRENILFGKA--LNEKY-Y 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 102 ENILEEISQNPDDSTLQkkllyltdnmnAQDAWEIENQvktiltklGIHnfhqkietLSGGQKKRVALASALISPCDLLI 181
Cdd:TIGR00957 731 QQVLEACALLPDLEILP-----------SGDRTEIGEK--------GVN--------LSGGQKQRVSLARAVYSNADIYL 783
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 928932812 182 LDEPTNHMD-------HDTIDWLEKYLTNRTgsLLMITHDRYFLDRvVNKTLELDDGKIySYIGNYSQFIEK 246
Cdd:TIGR00957 784 FDDPLSAVDahvgkhiFEHVIGPEGVLKNKT--RILVTHGISYLPQ-VDVIIVMSGGKI-SEMGSYQELLQR 851
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
319-467 |
1.11e-07 |
|
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: 52.93 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIG-------PTVK-----IGYF 386
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDgqditklPMHKrarlgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 387 SQES---EDMDI--NLRAI--------EYIKEKAEYITTEDGIKISASQMMenflfskdlqwtyiSKLSGGERRRLYLLR 453
Cdd:cd03218 81 PQEAsifRKLTVeeNILAVleirglskKEREEKLEELLEEFHITHLRKSKA--------------SSLSGGERRRVEIAR 146
|
170
....*....|....
gi 928932812 454 ILMDAPNVLILDEP 467
Cdd:cd03218 147 ALATNPKFLLLDEP 160
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-213 |
1.14e-07 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 54.72 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSY-GEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKmaieylsqnpefdPNAT 82
Cdd:PRK10790 341 IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGR-------------PLSS 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 83 ILEQVFKSDSQImnvirdyenileeISQNP---DDSTLQKklLYLTDNMNAQDAWEIENQVKtiLTKL------GIHN-F 152
Cdd:PRK10790 408 LSHSVLRQGVAM-------------VQQDPvvlADTFLAN--VTLGRDISEEQVWQALETVQ--LAELarslpdGLYTpL 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 928932812 153 HQKIETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYLT--NRTGSLLMITH 213
Cdd:PRK10790 471 GEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAavREHTTLVVIAH 533
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
14-242 |
1.15e-07 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 55.05 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 14 GEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADT---------GKVHMPSKM-AIE-YLSQNPEFDPNAT 82
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVkgsgsvllnGMPIDAKEMrAISaYVQQDDLFIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 83 ILEQVfksdsQIMNVIRDYENILEEISQNPDDSTLQKklLYLTDnmnAQDaweienqvktilTKLGIHNFHQkieTLSGG 162
Cdd:TIGR00955 116 VREHL-----MFQAHLRMPRRVTKKEKRERVDEVLQA--LGLRK---CAN------------TRIGVPGRVK---GLSGG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 163 QKKRVALASALISPCDLLILDEPTNHMD----HDTIDWLEKYLTNRTGSLLMITHDRYFLDRVVNKTLELDDGKIySYIG 238
Cdd:TIGR00955 171 ERKRLAFASELLTDPPLLFCDEPTSGLDsfmaYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRV-AYLG 249
|
....
gi 928932812 239 NYSQ 242
Cdd:TIGR00955 250 SPDQ 253
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
33-190 |
1.17e-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: 55.40 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 33 GLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKmaieylsqnpefdpnaTILEQVfkSD-SQIMNVIRDYENIleeisqn 111
Cdd:TIGR01257 1969 GLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGK----------------SILTNI--SDvHQNMGYCPQFDAI------- 2023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 112 pDDSTLQKKLLYLTDNMNAQDAWEIENQVKTILTKLGIHNFHQKIE-TLSGGQKKRVALASALISPCDLLILDEPTNHMD 190
Cdd:TIGR01257 2024 -DDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAgTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMD 2102
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-186 |
1.50e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 53.55 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISKSY-----------GEKILF----------ENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKV- 60
Cdd:COG4586 1 IIEVENLSKTYrvyekepglkgALKGLFrreyreveavDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 61 ---HMPSKMAIEYLSQnpefdpnatiLEQVFKSDSQI---MNVIRDYEnILEEISQNPDDsTLQKKLLYLTDnmnaqdaw 134
Cdd:COG4586 81 vlgYVPFKRRKEFARR----------IGVVFGQRSQLwwdLPAIDSFR-LLKAIYRIPDA-EYKKRLDELVE-------- 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 928932812 135 eienqvktiltKLGIHNF-HQKIETLSGGQKKRVALASALI-SPcDLLILDEPT 186
Cdd:COG4586 141 -----------LLDLGELlDTPVRQLSLGQRMRCELAAALLhRP-KILFLDEPT 182
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
319-507 |
1.75e-07 |
|
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: 52.37 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDI-GPTV---------KIGYFSQ 388
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVaGHDVvreprevrrRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 389 ES---------EDMDINLRAIEYIKEKAEYITTEdgiKISASQMMEnflfSKDlqwTYISKLSGGERRRLYLLRILMDAP 459
Cdd:cd03265 81 DLsvddeltgwENLYIHARLYGVPGAERRERIDE---LLDFVGLLE----AAD---RLVKTYSGGMRRRLEIARSLVHRP 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 928932812 460 NVLILDEPTNDLDIDTLKVLENYI----DDFNGIVICVSHDRYFLDRICNKI 507
Cdd:cd03265 151 EVLFLDEPTIGLDPQTRAHVWEYIeklkEEFGMTILLTTHYMEEAEQLCDRV 202
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
8-233 |
1.77e-07 |
|
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: 53.57 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 8 NISKSYGEkilFE-NISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHM---------------PSKMAIEYL 71
Cdd:COG4148 6 DFRLRRGG---FTlDVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLggevlqdsargiflpPHRRRIGYV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 72 SQNPEFDPNATILeqvfksdsqimnvirdyenileeisQNpddstlqkkLLYltdNMNAQDAWEIENQVKTILTKLGI-H 150
Cdd:COG4148 83 FQEARLFPHLSVR-------------------------GN---------LLY---GRKRAPRAERRISFDEVVELLGIgH 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 151 NFHQKIETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDT----IDWLEKyLTNRTG-SLLMITHD----RYFLDRV 221
Cdd:COG4148 126 LLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARkaeiLPYLER-LRDELDiPILYVSHSldevARLADHV 204
|
250
....*....|..
gi 928932812 222 VnktLeLDDGKI 233
Cdd:COG4148 205 V---L-LEQGRV 212
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
314-496 |
2.10e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 52.71 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 314 LGQKIIEINHISKSFEQNK--VIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIG------PTV---- 381
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGgmvlseETVwdvr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 382 -KIGYFSQESEDMDINlraieyikekaeyITTEDGIK-------ISASQM------------MENFLFSKDlqwtyiSKL 441
Cdd:PRK13635 81 rQVGMVFQNPDNQFVG-------------ATVQDDVAfglenigVPREEMvervdqalrqvgMEDFLNREP------HRL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 928932812 442 SGGERRRLYLLRILMDAPNVLILDEPTNDLD-------IDTLKVLEnyiDDFNGIVICVSHD 496
Cdd:PRK13635 142 SGGQKQRVAIAGVLALQPDIIILDEATSMLDprgrrevLETVRQLK---EQKGITVLSITHD 200
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
319-530 |
2.19e-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: 52.23 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFE--QNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDI-GPTV----------KIGY 385
Cdd:cd03251 1 VEFKNVTFRYPgdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIdGHDVrdytlaslrrQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 386 FSQESEDMDINLRA-IEYIKEKAEYITTEDGIKISASQmmeNFLFSKDLQW-TYI----SKLSGGERRRLYLLRILMDAP 459
Cdd:cd03251 81 VSQDVFLFNDTVAEnIAYGRPGATREEVEEAARAANAH---EFIMELPEGYdTVIgergVKLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 928932812 460 NVLILDEPTNDLDIDTLKVLENYIDDF--NGIVICVSHDryfLDRICN--KIFFFAgDGKIIEHtGNYSDFYKSG 530
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERLmkNRTTFVIAHR---LSTIENadRIVVLE-DGKIVER-GTHEELLAQG 227
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-233 |
2.34e-07 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 52.11 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSY--GEKILFENISFSIGDTDKIGLIGVNGTGKSSLLK-------------IIAGYDVADTGKVHMPSKMAI 68
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLalfrlvelssgsiLIDGVDISKIGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 69 eyLSQNP---------EFDPnatiLEQvfKSDSQIMNVIRDYeNILEEISQNPDdstlqkKLlyltdnmnaqDAWEIENQ 139
Cdd:cd03244 83 --IPQDPvlfsgtirsNLDP----FGE--YSDEELWQALERV-GLKEFVESLPG------GL----------DTVVEEGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 140 vktiltklgihnfhqkiETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEK----YLTNRTgsLLMITHdR 215
Cdd:cd03244 138 -----------------ENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKtireAFKDCT--VLTIAH-R 197
|
250 260
....*....|....*....|
gi 928932812 216 yfLDRVV--NKTLELDDGKI 233
Cdd:cd03244 198 --LDTIIdsDRILVLDKGRV 215
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
8-247 |
2.45e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 53.96 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 8 NISKSY---GEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKMAIEYLSQNPEFDPNATIL 84
Cdd:TIGR00958 483 DVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQ 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 85 EQVFKSDSqimnvIRDyeNILEEISQNPDDSTLQKKLLYLTDNMnaqdaweIENQVKTILTKLGihnfhQKIETLSGGQK 164
Cdd:TIGR00958 563 EPVLFSGS-----VRE--NIAYGLTDTPDEEIMAAAKAANAHDF-------IMEFPNGYDTEVG-----EKGSQLSGGQK 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 165 KRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYLTNRTGSLLMITHdRYFLDRVVNKTLELDDGKIYSyIGNYSQFI 244
Cdd:TIGR00958 624 QRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH-RLSTVERADQILVLKKGSVVE-MGTHKQLM 701
|
...
gi 928932812 245 EKK 247
Cdd:TIGR00958 702 EDQ 704
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
349-518 |
2.55e-07 |
|
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: 51.37 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 349 IIGKNGTGKSTLLNLITG--KLTPDLGSIdigptvkigYFSQES-EDMDINLRAIEYI----KEKAEYitteDGIKisas 421
Cdd:cd03217 31 LMGPNGSGKSTLAKTIMGhpKYEVTEGEI---------LFKGEDiTDLPPEERARLGIflafQYPPEI----PGVK---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 422 qmMENFLFSKDLqwtyisKLSGGERRRLYLLRILMDAPNVLILDEPTNDLDIDTLKVLENYIDDF---NGIVICVSHDRY 498
Cdd:cd03217 94 --NADFLRYVNE------GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLreeGKSVLIITHYQR 165
|
170 180
....*....|....*....|
gi 928932812 499 FLDRICNKIFFFAGDGKIIE 518
Cdd:cd03217 166 LLDYIKPDRVHVLYDGRIVK 185
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-249 |
2.58e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 52.36 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 6 VENISKSY---GEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKmaIEYLSQNpefdpnat 82
Cdd:PRK14246 10 VFNISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGK--VLYFGKD-------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 83 ileqVFKSDSqiMNVIRDYENILEEISQNPDDStLQKKLLYLTDNMNAQDAWEIENQVKTILTKLGI-HNFHQKIET--- 158
Cdd:PRK14246 80 ----IFQIDA--IKLRKEVGMVFQQPNPFPHLS-IYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwKEVYDRLNSpas 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 159 -LSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYLT--NRTGSLLMITHDRYFLDRVVNKTLELDDGKIYS 235
Cdd:PRK14246 153 qLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITelKNEIAIVIVSHNPQQVARVADYVAFLYNGELVE 232
|
250
....*....|....
gi 928932812 236 YIGNYSQFIEKKLE 249
Cdd:PRK14246 233 WGSSNEIFTSPKNE 246
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
319-519 |
3.45e-07 |
|
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: 51.41 E-value: 3.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITG-----KLTPDLGSIDIGPTV------------ 381
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDiydldvdvlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 382 -KIGYFSQES--------EDMDINLRAIEYIKEKAEYITTEDGIKISAsqmmenfLFSKDLQWTYISKLSGGERRRLYLL 452
Cdd:cd03260 81 rRVGMVFQKPnpfpgsiyDNVAYGLRLHGIKLKEELDERVEEALRKAA-------LWDEVKDRLHALGLSGGQQQRLCLA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 928932812 453 RILMDAPNVLILDEPTNDLD-IDTLKVlENYIDDFNG---IVIcVSHDRYFLDRICNKIFFFAgDGKIIEH 519
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDpISTAKI-EELIAELKKeytIVI-VTHNMQQAARVADRTAFLL-NGRLVEF 221
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
318-486 |
3.86e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 52.11 E-value: 3.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 318 IIEINHISKSFEQNK-VIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDI--GPTVK---------IGY 385
Cdd:PRK13652 3 LIETRDLCYSYSGSKeALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIrgEPITKenirevrkfVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 386 FSQESED--------MDINLRAI------EYIKEKAEYITTEDGIkisasqmmenflfsKDLQWTYISKLSGGERRRLYL 451
Cdd:PRK13652 83 VFQNPDDqifsptveQDIAFGPInlgldeETVAHRVSSALHMLGL--------------EELRDRVPHHLSGGEKKRVAI 148
|
170 180 190
....*....|....*....|....*....|....*
gi 928932812 452 LRILMDAPNVLILDEPTNDLDIDTLKVLENYIDDF 486
Cdd:PRK13652 149 AGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDL 183
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
18-242 |
3.96e-07 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 52.17 E-value: 3.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 18 LFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKmaIEYLSQNPEFDPnATILEQVfksdsqIMNV 97
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--ISFSSQFSWIMP-GTIKENI------IFGV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 98 IRD---YENILEEISQNPDDSTLQKKllyltDNmnaqdaweienqvkTILTKLGIhnfhqkieTLSGGQKKRVALASALI 174
Cdd:cd03291 123 SYDeyrYKSVVKACQLEEDITKFPEK-----DN--------------TVLGEGGI--------TLSGGQRARISLARAVY 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 928932812 175 SPCDLLILDEPTNHMDHDTidwlEKYLTNRTGSLLMITHDRYFLD------RVVNKTLELDDGKIYSYiGNYSQ 242
Cdd:cd03291 176 KDADLYLLDSPFGYLDVFT----EKEIFESCVCKLMANKTRILVTskmehlKKADKILILHEGSSYFY-GTFSE 244
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
4-233 |
3.96e-07 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 51.61 E-value: 3.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAG---YDVADtGKVH--------MP----SKMAI 68
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpkYEVTS-GSILldgedileLSpderARAGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 69 EYLSQNP-EFD--PNATILeqvfksdSQIMNVIRDYEnileeisqnpddstlqkkllyltdnmnaQDAWEIENQVKTILT 145
Cdd:COG0396 80 FLAFQYPvEIPgvSVSNFL-------RTALNARRGEE----------------------------LSAREFLKLLKEKMK 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 146 KLGIH--------NfhqkiETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKY---LTNRTGSLLMITHD 214
Cdd:COG0396 125 ELGLDedfldryvN-----EGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGvnkLRSPDRGILIITHY 199
|
250 260
....*....|....*....|
gi 928932812 215 RYFLDRVV-NKTLELDDGKI 233
Cdd:COG0396 200 QRILDYIKpDFVHVLVDGRI 219
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-236 |
4.09e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 53.41 E-value: 4.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 17 ILFENISFSIGDTDKIGLIGVNGTGKSSLLK-------------IIAGYDVADTGKVHMPSKMAIeyLSQNPefdpnati 83
Cdd:TIGR00957 1300 LVLRHINVTIHGGEKVGIVGRTGAGKSSLTLglfrinesaegeiIIDGLNIAKIGLHDLRFKITI--IPQDP-------- 1369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 84 leqVFKSDSQIMNvirdyeniLEEISQNPDDST-LQKKLLYLTDNMNAQDAweienqvktiltKLGiHNFHQKIETLSGG 162
Cdd:TIGR00957 1370 ---VLFSGSLRMN--------LDPFSQYSDEEVwWALELAHLKTFVSALPD------------KLD-HECAEGGENLSVG 1425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 928932812 163 QKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYLTNR--TGSLLMITHDryfLDRVVNKT--LELDDGKIYSY 236
Cdd:TIGR00957 1426 QRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQfeDCTVLTIAHR---LNTIMDYTrvIVLDKGEVAEF 1500
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
319-518 |
4.86e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 51.58 E-value: 4.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITgKLTPDLGSIDIgpTVKIGYFSQESEDMDINL- 397
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLN-RMNELESEVRV--EGRVEFFNQNIYERRVNLn 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 398 ---RAIEYIKEKAE------YITTEDGIKI-------SASQMMENFLFSKDLqWTYIS--------KLSGGERRRLYLLR 453
Cdd:PRK14258 85 rlrRQVSMVHPKPNlfpmsvYDNVAYGVKIvgwrpklEIDDIVESALKDADL-WDEIKhkihksalDLSGGQQQRLCIAR 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 928932812 454 ILMDAPNVLILDEPTNDLD-IDTLKVlENYIDDFN-----GIVIcVSHDRYFLDRICNKIFFFAGD----GKIIE 518
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLDpIASMKV-ESLIQSLRlrselTMVI-VSHNLHQVSRLSDFTAFFKGNenriGQLVE 236
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
318-503 |
5.04e-07 |
|
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: 50.81 E-value: 5.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 318 IIEINHISKSFEQNK----VIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIdigpTVKIGYFSQESEDM 393
Cdd:TIGR02211 1 LLKCENLGKRYQEGKldtrVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEV----LFNGQSLSKLSSNE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 394 DINLR------------------AIEYI--------KEKAEyittedgIKISASQMMENFLFSKDLQWtYISKLSGGERR 447
Cdd:TIGR02211 77 RAKLRnkklgfiyqfhhllpdftALENVamplligkKSVKE-------AKERAYEMLEKVGLEHRINH-RPSELSGGERQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 928932812 448 RLYLLRILMDAPNVLILDEPTNDLDIDTLKVLENYIDDFN-----GIVIcVSHDRYFLDRI 503
Cdd:TIGR02211 149 RVAIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNrelntSFLV-VTHDLELAKKL 208
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
4-197 |
5.85e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.61 E-value: 5.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSY-GEKILfENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKmAIEYLSQNPEFDPNAT 82
Cdd:PRK11288 5 LSFDGIGKTFpGVKAL-DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ-EMRFASTTAALAAGVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 83 ILEQvfksDSQI---MNVIrdyENILeeISQNP------DDSTLQKkllyltdnmnaqdaweienQVKTILTKLGIH-NF 152
Cdd:PRK11288 83 IIYQ----ELHLvpeMTVA---ENLY--LGQLPhkggivNRRLLNY-------------------EAREQLEHLGVDiDP 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 928932812 153 HQKIETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWL 197
Cdd:PRK11288 135 DTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQL 179
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
317-496 |
5.90e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 51.27 E-value: 5.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 317 KIIEINHISKSFEQNK---VIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIgptvkigyfsqesedm 393
Cdd:PRK13650 3 NIIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIII---------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 394 DINLRAIEYIKEKAEYI--------------TTEDGIK-------ISASQMME------NFLFSKDLQWTYISKLSGGER 446
Cdd:PRK13650 67 DGDLLTEENVWDIRHKIgmvfqnpdnqfvgaTVEDDVAfglenkgIPHEEMKErvnealELVGMQDFKEREPARLSGGQK 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 928932812 447 RRLYLLRILMDAPNVLILDEPTNDLD----IDTLKVLENYIDDFNGIVICVSHD 496
Cdd:PRK13650 147 QRVAIAGAVAMRPKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHD 200
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
18-212 |
6.13e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 52.72 E-value: 6.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 18 LFENISFSIGDTDKIGLIGVNGTGKSSLLKIIA--------------GYDVADTGKVHMPSKMAIeyLSQNPEFDPNaTI 83
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIErlydptegdiiindSHNLKDINLKWWRSKIGV--VSQDPLLFSN-SI 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 84 LEQVFKSdsqiMNVIRDYENILEEISQNPDDS---------TLQKKLLYLTDNMNAQDAWEI-----------ENQVKTI 143
Cdd:PTZ00265 477 KNNIKYS----LYSLKDLEALSNYYNEDGNDSqenknkrnsCRAKCAGDLNDMSNTTDSNELiemrknyqtikDSEVVDV 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 144 LTKLGIHNF----HQKIET--------LSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYLTNRTGSLLMI 211
Cdd:PTZ00265 553 SKKVLIHDFvsalPDKYETlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRI 632
|
.
gi 928932812 212 T 212
Cdd:PTZ00265 633 T 633
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
349-502 |
6.24e-07 |
|
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: 50.48 E-value: 6.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 349 IIGKNGTGKSTLLNLITGKLTPDLGSIDIGPTvkigyfsqesEDMDINLRAIEYIKEKAEyITTEDGIKISASQMMENFL 428
Cdd:cd03292 32 LVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQ----------DVSDLRGRAIPYLRRKIG-VVFQDFRLLPDRNVYENVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 429 FS------------------------KDLQWTYISKLSGGERRRLYLLRILMDAPNVLILDEPTNDLDIDTLKVLENYID 484
Cdd:cd03292 101 FAlevtgvppreirkrvpaalelvglSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLK 180
|
170 180
....*....|....*....|.
gi 928932812 485 DFN--GIVICVS-HDRYFLDR 502
Cdd:cd03292 181 KINkaGTTVVVAtHAKELVDT 201
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-473 |
6.33e-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: 52.13 E-value: 6.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGydvadtgkVHmpskmaieylsqnpefdPNAT 82
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG--------VY-----------------PHGT 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 83 ILEQVFKSDSQIM-NVIRDYEN-----ILEEISQNPDDSTLQKKLL--YLTDNMNAQDAWEIENQVKTIL--TKLGIHNF 152
Cdd:TIGR02633 56 WDGEIYWSGSPLKaSNIRDTERagiviIHQELTLVPELSVAENIFLgnEITLPGGRMAYNAMYLRAKNLLreLQLDADNV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 153 HQKIETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLE---KYLTNRTGSLLMITHDRYFLDRVVNKTLELD 229
Cdd:TIGR02633 136 TRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLdiiRDLKAHGVACVYISHKLNEVKAVCDTICVIR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 230 DGKiysYIGnySQFIEKKLERKTLESSIERKRERLYKKElewiragaqarstkqkariqrfeelkntssPiHDsnidicv 309
Cdd:TIGR02633 216 DGQ---HVA--TKDMSTMSEDDIITMMVGREITSLYPHE------------------------------P-HE------- 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 310 ahsrLGQKIIEINHISKSFEQN---KVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLI--------TGKLTPDLGSIDI- 377
Cdd:TIGR02633 253 ----IGDVILEARNLTCWDVINphrKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALfgaypgkfEGNVFINGKPVDIr 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 378 GPTVKI--------------GYFSQESEDMDINLRAIE-YIKEKAEYITTEDGIKISASQMMENFLFSKDLQwtyISKLS 442
Cdd:TIGR02633 329 NPAQAIragiamvpedrkrhGIVPILGVGKNITLSVLKsFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLP---IGRLS 405
|
490 500 510
....*....|....*....|....*....|.
gi 928932812 443 GGERRRLYLLRILMDAPNVLILDEPTNDLDI 473
Cdd:TIGR02633 406 GGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
318-495 |
6.57e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 51.27 E-value: 6.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 318 IIEINHISKSFEQN-----KVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIGPTV----------- 381
Cdd:PRK13643 1 MIKFEKVNYTYQPNspfasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVvsstskqkeik 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 382 ----KIGYFSQESEDM---DINLRAIEYIKEKAEyITTEDGIKISASQMmENFLFSKDLQWTYISKLSGGERRRLYLLRI 454
Cdd:PRK13643 81 pvrkKVGVVFQFPESQlfeETVLKDVAFGPQNFG-IPKEKAEKIAAEKL-EMVGLADEFWEKSPFELSGGQMRRVAIAGI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 928932812 455 LMDAPNVLILDEPTNDLD----IDTLKVLENyIDDFNGIVICVSH 495
Cdd:PRK13643 159 LAMEPEVLVLDEPTAGLDpkarIEMMQLFES-IHQSGQTVVLVTH 202
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
319-525 |
6.93e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 52.13 E-value: 6.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSF--EQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIGpTVKIGYFSQESedmdin 396
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLN-GQPIADYSEAA------ 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 397 LR-AIEYIKEKaeyittedgIKISASQMMENFLFSKD----------LQWTYISK------------------LSGGERR 447
Cdd:PRK11160 412 LRqAISVVSQR---------VHLFSATLRDNLLLAAPnasdealievLQQVGLEKlleddkglnawlgeggrqLSGGEQR 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 448 RLYLLRILM-DAPnVLILDEPTNDLDIDT----LKVLENYIDDfnGIVICVSHDRYFL---DRICnkiffFAGDGKIIEH 519
Cdd:PRK11160 483 RLGIARALLhDAP-LLLLDEPTEGLDAETerqiLELLAEHAQN--KTVLMITHRLTGLeqfDRIC-----VMDNGQIIEQ 554
|
....*.
gi 928932812 520 tGNYSD 525
Cdd:PRK11160 555 -GTHQE 559
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-233 |
8.58e-07 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 51.23 E-value: 8.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISKSY----GEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVhmpskmaieylsqnpefd 78
Cdd:COG1135 1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSV------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 79 pnaTILEQVFK--SDSQIMNVIRD----------------YENI---LEeisqnpddstLQKKllyltdnmnaqDAWEIE 137
Cdd:COG1135 63 ---LVDGVDLTalSERELRAARRKigmifqhfnllssrtvAENValpLE----------IAGV-----------PKAEIR 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 138 NQVKTILTKLGIHNF-HQKIETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTidwlekyltnrTGSLL------- 209
Cdd:COG1135 119 KRVAELLELVGLSDKaDAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPET-----------TRSILdllkdin 187
|
250 260 270
....*....|....*....|....*....|....*.
gi 928932812 210 --------MITHD----RYFLDRVVnktlELDDGKI 233
Cdd:COG1135 188 relgltivLITHEmdvvRRICDRVA----VLENGRI 219
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-214 |
8.96e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 51.28 E-value: 8.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 1 MNILSVENISKSYG-EKILF---ENISFSIGDTDKIGLIGVNGTGKS-SLLKIIagydvadtGKVHMPSKMAIEYLsqnp 75
Cdd:PRK11022 1 MALLNVDKLSVHFGdESAPFravDRISYSVKQGEVVGIVGESGSGKSvSSLAIM--------GLIDYPGRVMAEKL---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 76 EFDpNATILEQVFKSDSQImnVIRDYENILEE--ISQNPDDSTLQKKLLYLTDNMNAQDAWEIENQVKtILTKLGIHNFH 153
Cdd:PRK11022 69 EFN-GQDLQRISEKERRNL--VGAEVAMIFQDpmTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAID-LLNQVGIPDPA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 928932812 154 QKIET----LSGGQKKRVALASALISPCDLLILDEPTNHMD----HDTIDWLEKYLTNRTGSLLMITHD 214
Cdd:PRK11022 145 SRLDVyphqLSGGMSQRVMIAMAIACRPKLLIADEPTTALDvtiqAQIIELLLELQQKENMALVLITHD 213
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
319-378 |
9.14e-07 |
|
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: 49.95 E-value: 9.14e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIG 378
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIG 60
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-186 |
9.37e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.85 E-value: 9.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAG------YD--------------VADTgkvhm 62
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvyphgtYEgeiifegeelqasnIRDT----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 63 pSKMAIEYLSQNPEFDPNATILEQVFKSDSQIMNVIRDYenileeisqnpddstlqkkllyltDNMNAqdaweienQVKT 142
Cdd:PRK13549 80 -ERAGIAIIHQELALVKELSVLENIFLGNEITPGGIMDY------------------------DAMYL--------RAQK 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 928932812 143 ILTKLGIH-NFHQKIETLSGGQKKRVALASALISPCDLLILDEPT 186
Cdd:PRK13549 127 LLAQLKLDiNPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPT 171
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
319-481 |
1.00e-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: 50.30 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFEQNK-VIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIGPT-----------VKIGYF 386
Cdd:cd03254 3 IEFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIdirdisrkslrSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 387 SQESEDMDINLRaiEYIKEKAEYITTEDGIKISASQMMENFL-FSKDLQWTYISK----LSGGERRRLYLLRILMDAPNV 461
Cdd:cd03254 83 LQDTFLFSGTIM--ENIRLGRPNATDEEVIEAAKEAGAHDFImKLPNGYDTVLGEnggnLSQGERQLLAIARAMLRDPKI 160
|
170 180
....*....|....*....|
gi 928932812 462 LILDEPTNDLDIDTLKVLEN 481
Cdd:cd03254 161 LILDEATSNIDTETEKLIQE 180
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
319-378 |
1.09e-06 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 51.23 E-value: 1.09e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 928932812 319 IEINHISKSFEQNKVIEDFSyIALKD-DRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIG 378
Cdd:COG3839 4 LELENVSKSYGGVEALKDID-LDIEDgEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIG 63
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
13-213 |
1.14e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 50.50 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 13 YGEKILFEnISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMpSKMAIEYLSQNPEFDPNATILEQVFK-SD 91
Cdd:PRK13643 17 FASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVSSTSKQKEIKPVRKKVGVVFQfPE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 92 SQIMNvirdyENILEEISQNPDDSTLQKKllyltdnmnaqdawEIENQVKTILTKLGI-HNFHQKIE-TLSGGQKKRVAL 169
Cdd:PRK13643 95 SQLFE-----ETVLKDVAFGPQNFGIPKE--------------KAEKIAAEKLEMVGLaDEFWEKSPfELSGGQMRRVAI 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 928932812 170 ASALISPCDLLILDEPTNHMDHDT-IDWLEKYLT-NRTG-SLLMITH 213
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDPKArIEMMQLFESiHQSGqTVVLVTH 202
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
319-496 |
1.23e-06 |
|
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: 50.03 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFeQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSI-----DIG--PTVK--IGYFSQE 389
Cdd:cd03299 1 LKVENLSKDW-KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKIllngkDITnlPPEKrdISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 390 S---EDMDInLRAIEY--IKEKAEYITTEDGIK-ISASQMMENFLFSKDLqwtyisKLSGGERRRLYLLRILMDAPNVLI 463
Cdd:cd03299 80 YalfPHMTV-YKNIAYglKKRKVDKKEIERKVLeIAEMLGIDHLLNRKPE------TLSGGEQQRVAIARALVVNPKILL 152
|
170 180 190
....*....|....*....|....*....|....*..
gi 928932812 464 LDEPTNDLDIDT----LKVLENYIDDFNGIVICVSHD 496
Cdd:cd03299 153 LDEPFSALDVRTkeklREELKKIRKEFGVTVLHVTHD 189
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
321-496 |
1.31e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 50.55 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 321 INHISKSFEQNKviedfsYIAlkddrigIIGKNGTGKSTLLNLITGKLTPDLGSIDIGPTV---------------KIGY 385
Cdd:PRK13646 23 IHDVNTEFEQGK------YYA-------IVGQTGSGKSTLIQNINALLKPTTGTVTVDDITithktkdkyirpvrkRIGM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 386 FSQ--ESEDMDINL-RAIEYIKEKaeYITTEDGIKISASQMMENFLFSKDLQWTYISKLSGGERRRLYLLRILMDAPNVL 462
Cdd:PRK13646 90 VFQfpESQLFEDTVeREIIFGPKN--FKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDII 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 928932812 463 ILDEPTNDLD----IDTLKVLENYIDDFNGIVICVSHD 496
Cdd:PRK13646 168 VLDEPTAGLDpqskRQVMRLLKSLQTDENKTIILVSHD 205
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
347-495 |
1.60e-06 |
|
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: 49.58 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 347 IGIIGKNGTGKSTLLNLITGKLtpDLGSIDIGptvKIGYFSQESeDMDINLRAIEYIKEK---AEYITTEDGIKISA--- 420
Cdd:cd03234 36 MAILGSSGSGKTTLLDAISGRV--EGGGTTSG---QILFNGQPR-KPDQFQKCVAYVRQDdilLPGLTVRETLTYTAilr 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 421 ---------SQMMENFLFSKDLQWT-----YISKLSGGERRRLYLLRILMDAPNVLILDEPTNDLD----IDTLKVLENY 482
Cdd:cd03234 110 lprkssdaiRKKRVEDVLLRDLALTriggnLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDsftaLNLVSTLSQL 189
|
170
....*....|...
gi 928932812 483 IDDfNGIVICVSH 495
Cdd:cd03234 190 ARR-NRIVILTIH 201
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
21-218 |
1.65e-06 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 49.25 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 21 NISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKM---------------AIEYLSQNPEFdPNATILE 85
Cdd:cd03290 19 NINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNesepsfeatrsrnrySVAYAAQKPWL-LNATVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 86 QV-FKSDsqiMNVIRdYENILEEISQNPDdstlqkkllylTDNMNAQDAWEIENQvktiltklGIHnfhqkietLSGGQK 164
Cdd:cd03290 98 NItFGSP---FNKQR-YKAVTDACSLQPD-----------IDLLPFGDQTEIGER--------GIN--------LSGGQR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 928932812 165 KRVALASALISPCDLLILDEPTNHMDHDTIDWLE-----KYLTNRTGSLLMITHDRYFL 218
Cdd:cd03290 147 QRICVARALYQNTNIVFLDDPFSALDIHLSDHLMqegilKFLQDDKRTLVLVTHKLQYL 205
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
318-522 |
1.72e-06 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 49.71 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 318 IIEINHISKSFEQNKVIEDfsyIALKDDR---IGIIGKNGTGKSTLLNLI-------TGKLTPDLGSIDiGPTVKIGYFS 387
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHN---IDLNIDQgevVVIIGPSGSGKSTLLRCInkleeitSGDLIVDGLKVN-DPKVDERLIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 388 QESeDM---DINL----RAIEYI-----------KEKAEYITTEDGIKISASQMMENflfskdlqwtYISKLSGGERRRL 449
Cdd:PRK09493 77 QEA-GMvfqQFYLfphlTALENVmfgplrvrgasKEEAEKQARELLAKVGLAERAHH----------YPSELSGGQQQRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 928932812 450 YLLRILMDAPNVLILDEPTNDLDI----DTLKVLENYIDDFNGIVIcVSHDRYFLDRICNKIFFFagDGKIIEHTGN 522
Cdd:PRK09493 146 AIARALAVKPKLMLFDEPTSALDPelrhEVLKVMQDLAEEGMTMVI-VTHEIGFAEKVASRLIFI--DKGRIAEDGD 219
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
7-233 |
1.81e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 50.21 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 7 ENISKSYG-----EKILFENISFSIGDTDKIGLIGVNGTGKSSLLK-------------IIAGYDV-ADTGKVHMPS-KM 66
Cdd:PRK13641 6 ENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQhfnallkpssgtiTIAGYHItPETGNKNLKKlRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 67 AIEYLSQNPEfdpnatilEQVFKsdsqimnvirdyENILEEISQNPDdstlqkkllyltdNMNAQDAwEIENQVKTILTK 146
Cdd:PRK13641 86 KVSLVFQFPE--------AQLFE------------NTVLKDVEFGPK-------------NFGFSED-EAKEKALKWLKK 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 147 LGIHN---FHQKIEtLSGGQKKRVALASALISPCDLLILDEPTNHMD----HDTIDWLEKYltNRTG-SLLMITHDRYFL 218
Cdd:PRK13641 132 VGLSEdliSKSPFE-LSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDpegrKEMMQLFKDY--QKAGhTVILVTHNMDDV 208
|
250
....*....|....*
gi 928932812 219 DRVVNKTLELDDGKI 233
Cdd:PRK13641 209 AEYADDVLVLEHGKL 223
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
318-502 |
1.89e-06 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 49.28 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 318 IIEINHISKSFEQNKViedfsyiALKD-----DRiG----IIGKNGTGKSTLLNLITGKLTPDLGSIDIG---------- 378
Cdd:COG2884 1 MIRFENVSKRYPGGRE-------ALSDvsleiEK-GefvfLTGPSGAGKSTLLKLLYGEERPTSGQVLVNgqdlsrlkrr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 379 --PTV--KIGYFSQES---EDMDI--N----LRAIEyiKEKAEyittedgIKISASQMMENF-LfsKDLQWTYISKLSGG 444
Cdd:COG2884 73 eiPYLrrRIGVVFQDFrllPDRTVyeNvalpLRVTG--KSRKE-------IRRRVREVLDLVgL--SDKAKALPHELSGG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 928932812 445 E------------RrrlyllrilmdaPNVLILDEPTNDLDIDT-LKVLEnYIDDFN--GI-VICVSHDRYFLDR 502
Cdd:COG2884 142 EqqrvaiaralvnR------------PELLLADEPTGNLDPETsWEIME-LLEEINrrGTtVLIATHDLELVDR 202
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
318-375 |
1.91e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 50.79 E-value: 1.91e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 928932812 318 IIEINHISKSFEQNKVIEDFSyIALKDDRI-GIIGKNGTGKSTLLNLITGKLTPDLGSI 375
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVS-LELRPGEVhALLGENGAGKSTLMKILSGVYQPDSGEI 61
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
319-526 |
1.99e-06 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 49.63 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIGptvkiGY---FSQESEDMDI 395
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIA-----GHqfdFSQKPSEKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 396 ------------------------NL-----RAIEYIKEKAEyittEDGIKISASQMMENFLFSKDLQwtyiskLSGGER 446
Cdd:COG4161 78 rllrqkvgmvfqqynlwphltvmeNLieapcKVLGLSKEQAR----EKAMKLLARLRLTDKADRFPLH------LSGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 447 RRLYLLRILMDAPNVLILDEPTNDLDIDTLKVLENYIDDFN--GIV-ICVSHDRYFLDRICNKIFFFAgDGKIIEHtGNY 523
Cdd:COG4161 148 QRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSqtGITqVIVTHEVEFARKVASQVVYME-KGRIIEQ-GDA 225
|
...
gi 928932812 524 SDF 526
Cdd:COG4161 226 SHF 228
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
319-495 |
2.10e-06 |
|
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: 48.37 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFEQNK--VIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIGptvkigyfsqeseDMDIN 396
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLD-------------GADIS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 397 LRAIEYIKEKAEYITTEDgiKISASQMMENFLfskdlqwtyisklSGGERRRLYLLRILMDAPNVLILDEPTNDLDIDTL 476
Cdd:cd03246 68 QWDPNELGDHVGYLPQDD--ELFSGSIAENIL-------------SGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGE 132
|
170 180
....*....|....*....|..
gi 928932812 477 KVLENYIDDFN---GIVICVSH 495
Cdd:cd03246 133 RALNQAIAALKaagATRIVIAH 154
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
135-233 |
2.27e-06 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 50.45 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 135 EIENQVKTILTKLGI---------HNFhqkietlSGGQKKRVALASALISPCDLLILDEPTNHMD----HDTIDWLEKyL 201
Cdd:COG4172 400 ERRARVAEALEEVGLdpaarhrypHEF-------SGGQRQRIAIARALILEPKLLVLDEPTSALDvsvqAQILDLLRD-L 471
|
90 100 110
....*....|....*....|....*....|....*..
gi 928932812 202 TNRTG-SLLMITHD----RYFLDRVvnktLELDDGKI 233
Cdd:COG4172 472 QREHGlAYLFISHDlavvRALAHRV----MVMKDGKV 504
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-237 |
2.39e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 49.38 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 1 MNILSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKmAIEYLSQNPEFDPN 80
Cdd:PRK11831 5 ANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGE-NIPAMSRSRLYTVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 81 ATiLEQVFKSDSQI--MNVirdYENI---LEEISQNPDdstlqkKLLYLTDNMNaqdaweienqvktiLTKLGIHNFHQK 155
Cdd:PRK11831 84 KR-MSMLFQSGALFtdMNV---FDNVaypLREHTQLPA------PLLHSTVMMK--------------LEAVGLRGAAKL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 156 IET-LSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYLTNRTGSL----LMITHDryfldrvVNKTLELDD 230
Cdd:PRK11831 140 MPSeLSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALgvtcVVVSHD-------VPEVLSIAD 212
|
....*..
gi 928932812 231 gkiYSYI 237
Cdd:PRK11831 213 ---HAYI 216
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
318-446 |
2.45e-06 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 49.26 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 318 IIEINHISKSFEQNKVIEDFSyiaLKDDR---IGIIGKNGTGKSTLLNLITGKLTPDLGSI-----DI-----------G 378
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVS---LEVNQgeiVGLLGPNGAGKTTTFYMIVGLVKPDSGRIfldgeDIthlpmhkrarlG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 379 ptvkIGYFSQES--------EDmdiNLRAI-EYIKEKAEYITtedgikisasQMMENFLfsKDLQWTYISK-----LSGG 444
Cdd:COG1137 80 ----IGYLPQEAsifrkltvED---NILAVlELRKLSKKERE----------ERLEELL--EEFGITHLRKskaysLSGG 140
|
..
gi 928932812 445 ER 446
Cdd:COG1137 141 ER 142
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
154-220 |
2.57e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 48.09 E-value: 2.57e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 928932812 154 QKIETLSGGQKKRVALASALISPCD--LLILDEPTNHMDHDTIDWLE---KYLTNRTGSLLMITHDRYFLDR 220
Cdd:cd03238 83 QKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLeviKGLIDLGNTVILIEHNLDVLSS 154
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
337-375 |
3.07e-06 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 48.81 E-value: 3.07e-06
10 20 30
....*....|....*....|....*....|....*....
gi 928932812 337 FSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSI 375
Cdd:PRK10771 18 FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSL 56
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
347-501 |
3.33e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 48.90 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 347 IGIIGKNGTGKSTLLNLITGKLTPDLGSID----------------------------IGPTVKIGYFSQESEDMDINlr 398
Cdd:cd03236 29 LGLVGPNGIGKSTALKILAGKLKPNLGKFDdppdwdeildefrgselqnyftkllegdVKVIVKPQYVDLIPKAVKGK-- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 399 AIEYIKEKAEYITTEDGIK-ISASQMMENflfskdlqwtYISKLSGGERRRLYLLRILMDAPNVLILDEPTNDLDI---- 473
Cdd:cd03236 107 VGELLKKKDERGKLDELVDqLELRHVLDR----------NIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIkqrl 176
|
170 180
....*....|....*....|....*...
gi 928932812 474 DTLKVLENYIDDFNGIVIcVSHDRYFLD 501
Cdd:cd03236 177 NAARLIRELAEDDNYVLV-VEHDLAVLD 203
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
319-390 |
3.36e-06 |
|
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: 48.23 E-value: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFEQNKVIEDFsyiALKDDRI--------GIIGKNGTGKSTLLNLITGKLTPDLGSIDIGPTvkIGYFSQES 390
Cdd:cd03250 1 ISVEDASFTWDSGEQETSF---TLKDINLevpkgelvAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--IAYVSQEP 75
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
21-234 |
3.66e-06 |
|
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: 50.40 E-value: 3.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 21 NISFSigDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKmaieylsqnpEFDPNATILEQVFKSDSQiMNVIRD 100
Cdd:TIGR01257 950 NITFY--ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGK----------DIETNLDAVRQSLGMCPQ-HNILFH 1016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 101 YENILEEIsqnpddstlqkkLLYLTDNMNAQDAWEIEnqVKTILTKLGIHN-FHQKIETLSGGQKKRVALASALISPCDL 179
Cdd:TIGR01257 1017 HLTVAEHI------------LFYAQLKGRSWEEAQLE--MEAMLEDTGLHHkRNEEAQDLSGGMQRKLSVAIAFVGDAKV 1082
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 928932812 180 LILDEPTNHMD----HDTIDWLEKYLTNRTgsLLMITHDRYFLDRVVNKTLELDDGKIY 234
Cdd:TIGR01257 1083 VVLDEPTSGVDpysrRSIWDLLLKYRSGRT--IIMSTHHMDEADLLGDRIAIISQGRLY 1139
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
318-378 |
3.83e-06 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 49.33 E-value: 3.83e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 928932812 318 IIEINHISKSFEQNKVIEDFS-------YIALkddrigiIGKNGTGKSTLLNLITGKLTPDLGSIDIG 378
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSlsiepgeFVAL-------LGPSGCGKTTLLRMIAGFETPDSGRILLD 65
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
318-375 |
4.37e-06 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 49.18 E-value: 4.37e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 928932812 318 IIEINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSI 375
Cdd:PRK09452 14 LVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRI 71
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
319-496 |
4.42e-06 |
|
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: 48.39 E-value: 4.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIGptvkigyfSQESEDMDINLR 398
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLD--------GKDITNLPPHKR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 399 AIEYIKEK---------AEYI--------TTEDGIKISASQMMEnFLFSKDLQWTYISKLSGGERRRLYLLRILMDAPNV 461
Cdd:cd03300 73 PVNTVFQNyalfphltvFENIafglrlkkLPKAEIKERVAEALD-LVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKV 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 928932812 462 LILDEPTNDLDIDTLKVLENYIDDFN---GI-VICVSHD 496
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQLELKRLQkelGItFVFVTHD 190
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-190 |
4.91e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 48.63 E-value: 4.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISKSYGEKI-LF--------ENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKV----HMPSKMAIE 69
Cdd:PRK15112 4 LLEVRNLSKTFRYRTgWFrrqtveavKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELliddHPLHFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 70 YLSQNpefdpnatiLEQVFKSDSQIMNVirdyeniLEEISQnpddsTLQKKLLYLTDnmnaQDAWEIENQVKTILTKLGI 149
Cdd:PRK15112 84 YRSQR---------IRMIFQDPSTSLNP-------RQRISQ-----ILDFPLRLNTD----LEPEQREKQIIETLRQVGL 138
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 928932812 150 HNFHQKI--ETLSGGQKKRVALASALISPCDLLILDEPTNHMD 190
Cdd:PRK15112 139 LPDHASYypHMLAPGQKQRLGLARALILRPKVIIADEALASLD 181
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
318-508 |
5.46e-06 |
|
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: 47.81 E-value: 5.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 318 IIEINHISKSF---EQN----KVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDI---GPTV------ 381
Cdd:COG4778 4 LLEVENLSKTFtlhLQGgkrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdGGWVdlaqas 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 382 ----------KIGYFSQesedmdiNLRAI------EYIKEKAeyitTEDGIKIS-----ASQMMENFLFSKDLqWT-YIS 439
Cdd:COG4778 84 preilalrrrTIGYVSQ-------FLRVIprvsalDVVAEPL----LERGVDREeararARELLARLNLPERL-WDlPPA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 928932812 440 KLSGGERRRLYLLRILMDAPNVLILDEPTNDLDIDT-LKVLEnYIDDF--NGI-VICVSHDRYFLDRICNKIF 508
Cdd:COG4778 152 TFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANrAVVVE-LIEEAkaRGTaIIGIFHDEEVREAVADRVV 223
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
330-586 |
6.08e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 48.29 E-value: 6.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 330 QNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDI-GPTV--------------KIGYFSQESEDM- 393
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIaGYHItpetgnknlkklrkKVSLVFQFPEAQl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 394 --DINLRAIEYikEKAEYITTEDGIKISASQMMENFLFSKDLQWTYISKLSGGERRRLYLLRILMDAPNVLILDEPTNDL 471
Cdd:PRK13641 99 feNTVLKDVEF--GPKNFGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 472 D----IDTLKVLENYiDDFNGIVICVSHDryfLDRICNkiffFAGD------GKIIEHTGNySDFYKSGRWIHEEIKEEK 541
Cdd:PRK13641 177 DpegrKEMMQLFKDY-QKAGHTVILVTHN---MDDVAE----YADDvlvlehGKLIKHASP-KEIFSDKEWLKKHYLDEP 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 928932812 542 NTKKSApQKPKEKKLKFTYNEQreyeTIDQEIENLENKLSTLEEE 586
Cdd:PRK13641 248 ATSRFA-SKLEKGGFKFSEMPL----TIDELVDGIKNNLKGGFHE 287
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
336-378 |
7.03e-06 |
|
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: 47.49 E-value: 7.03e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 928932812 336 DFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIG 378
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLIN 58
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
349-495 |
7.27e-06 |
|
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: 46.97 E-value: 7.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 349 IIGKNGTGKSTLLNLITGKLTPDLGSIDIGPTvkigyfsQESEDMDINLRAIEYIKE----KAEYITTED-----GIKIS 419
Cdd:TIGR01189 31 VTGPNGIGKTTLLRILAGLLRPDSGEVRWNGT-------PLAEQRDEPHENILYLGHlpglKPELSALENlhfwaAIHGG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 420 ASQMMENFLFS---KDLQWTYISKLSGGERRRLYLLRILMDAPNVLILDEPTNDLDIDTLKVLENYIDDF---NGIVICV 493
Cdd:TIGR01189 104 AQRTIEDALAAvglTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHlarGGIVLLT 183
|
..
gi 928932812 494 SH 495
Cdd:TIGR01189 184 TH 185
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
345-375 |
7.55e-06 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 47.44 E-value: 7.55e-06
10 20 30
....*....|....*....|....*....|.
gi 928932812 345 DRIGIIGKNGTGKSTLLNLITGKLTPDLGSI 375
Cdd:COG3840 26 ERVAILGPSGAGKSTLLNLIAGFLPPDSGRI 56
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
319-518 |
8.55e-06 |
|
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: 47.64 E-value: 8.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKltpdlgsidigPTVKI--GYFSQESED---M 393
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGH-----------PSYEVtsGTILFKGQDlleL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 394 DINLRA-------------------IEYIKEKAEYITTEDGI-KISASQ---MMENFLFSKDLQWTYISK-----LSGGE 445
Cdd:TIGR01978 70 EPDERAraglflafqypeeipgvsnLEFLRSALNARRSARGEePLDLLDfekLLKEKLALLDMDEEFLNRsvnegFSGGE 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 928932812 446 RRRLYLLRILMDAPNVLILDEPTNDLDIDTLKVLENYIDDF----NGIVIcVSHDRYFLDRICNKIFFFAGDGKIIE 518
Cdd:TIGR01978 150 KKRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLrepdRSFLI-ITHYQRLLNYIKPDYVHVLLDGRIVK 225
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
316-375 |
8.70e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 47.61 E-value: 8.70e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 316 QKIIEINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSI 375
Cdd:PRK11701 4 QPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV 63
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
3-235 |
9.81e-06 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 48.57 E-value: 9.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISKSY--GEKIL--FENISFSIGDTDKIGLIGVNGTGKSSLLKI-------------IAGYDVADTGKvhmpsk 65
Cdd:PRK10535 4 LLELKDIRRSYpsGEEQVevLKGISLDIYAGEMVAIVGASGSGKSTLMNIlgcldkptsgtyrVAGQDVATLDA------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 66 maieylsqnpefDPNATILEQVFksdsqimNVIRDYENILEEIS--QNpddstLQKKLLYLTDNMNAQDAWEIEnqvktI 143
Cdd:PRK10535 78 ------------DALAQLRREHF-------GFIFQRYHLLSHLTaaQN-----VEVPAVYAGLERKQRLLRAQE-----L 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 144 LTKLGIHN-FHQKIETLSGGQKKRVALASALISPCDLLILDEPTNHMD-HDTIDWLE--KYLTNRTGSLLMITHDRYFLD 219
Cdd:PRK10535 129 LQRLGLEDrVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDsHSGEEVMAilHQLRDRGHTVIIVTHDPQVAA 208
|
250
....*....|....*.
gi 928932812 220 RvVNKTLELDDGKIYS 235
Cdd:PRK10535 209 Q-AERVIEIRDGEIVR 223
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
7-213 |
9.93e-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: 9.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 7 ENISKSYGEK---ILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYdvadtgkvhmpskmaieylsqnpeFDPNATi 83
Cdd:cd03249 4 KNVSFRYPSRpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERF------------------------YDPTSG- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 84 leQVFKSDSQIMNV-IRDYENILEEISQNPD--DSTLQKKLLYltdnmNAQDAweIENQVKTILTKLGIHNF----HQKI 156
Cdd:cd03249 59 --EILLDGVDIRDLnLRWLRSQIGLVSQEPVlfDGTIAENIRY-----GKPDA--TDEEVEEAAKKANIHDFimslPDGY 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 928932812 157 ET--------LSGGQKKRVALASALISPCDLLILDEPTNHMDHDT----IDWLEKYLTNRTgsLLMITH 213
Cdd:cd03249 130 DTlvgergsqLSGGQKQRIAIARALLRNPKILLLDEATSALDAESeklvQEALDRAMKGRT--TIVIAH 196
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
319-496 |
9.96e-06 |
|
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: 48.51 E-value: 9.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFE-QNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDlgsidiGPTVKIGYFSQESEDMDINL 397
Cdd:TIGR02868 335 LELRDLSAGYPgAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPL------QGEVTLDGVPVSSLDQDEVR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 398 RAIEYIKEKAEyittedgikISASQMMENFLFSK------DLQW-------------------TYI----SKLSGGERRR 448
Cdd:TIGR02868 409 RRVSVCAQDAH---------LFDTTVRENLRLARpdatdeELWAalervgladwlralpdgldTVLgeggARLSGGERQR 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 928932812 449 LYLLRILM-DAPnVLILDEPTNDLDIDT-LKVLENYIDDFNG-IVICVSHD 496
Cdd:TIGR02868 480 LALARALLaDAP-ILLLDEPTEHLDAETaDELLEDLLAALSGrTVVLITHH 529
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
319-519 |
1.26e-05 |
|
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: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSF---EQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDI-GPTVK----------IG 384
Cdd:cd03249 1 IEFKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLdGVDIRdlnlrwlrsqIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 385 YFSQESEDMDINLRaiEYIKEKAEYITTEDGIKISASQMMENFLFSKDLQW-TYI----SKLSGGERRRLYLLRILMDAP 459
Cdd:cd03249 81 LVSQEPVLFDGTIA--ENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYdTLVgergSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 928932812 460 NVLILDEPTNDLDIDTLKVLENYIDDF--NGIVICVSHdRYFLDRICNKIFFFaGDGKIIEH 519
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAmkGRTTIVIAH-RLSTIRNADLIAVL-QNGQVVEQ 218
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
319-366 |
1.32e-05 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 47.77 E-value: 1.32e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 928932812 319 IEINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITG 366
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAG 50
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
158-236 |
1.43e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 47.56 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 158 TLSGGQKKRVALASALISPCDLLILDEPTNHMD----HDTIDWLEKyLTNRTG-SLLMITHDryfLD---RVVNKTLELD 229
Cdd:PRK11144 128 SLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlprkRELLPYLER-LAREINiPILYVSHS---LDeilRLADRVVVLE 203
|
....*..
gi 928932812 230 DGKIYSY 236
Cdd:PRK11144 204 QGKVKAF 210
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-251 |
1.60e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 46.94 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 2 NILSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAG---YDVADtGKV------------HMPSKM 66
Cdd:CHL00131 6 PILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpaYKILE-GDIlfkgesildlepEERAHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 67 AIEYLSQNPEFDP---NATILEQVFKSDSQIMNV-----IRDYENILEEISQNPDDSTlqkkllYLTDNMNaqdaweien 138
Cdd:CHL00131 85 GIFLAFQYPIEIPgvsNADFLRLAYNSKRKFQGLpeldpLEFLEIINEKLKLVGMDPS------FLSRNVN--------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 139 qvktiltklgihnfhqkiETLSGGQKKRVALASALISPCDLLILDEPTNHMDhdtIDWLE------KYLTNRTGSLLMIT 212
Cdd:CHL00131 150 ------------------EGFSGGEKKRNEILQMALLDSELAILDETDSGLD---IDALKiiaegiNKLMTSENSIILIT 208
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 928932812 213 HDRYFLDRVV-NKTLELDDGKIYsYIGNYSqfIEKKLERK 251
Cdd:CHL00131 209 HYQRLLDYIKpDYVHVMQNGKII-KTGDAE--LAKELEKK 245
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
316-517 |
1.62e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 46.91 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 316 QKIIEINHISKSF--EQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIgptvkigyfsqesEDM 393
Cdd:PRK13632 5 SVMIKVENVSFSYpnSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKI-------------DGI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 394 DINLRAIEYIKEKAEYI-----------TTEDGI-------KISASQM------------MENFLfSKDLQwtyisKLSG 443
Cdd:PRK13632 72 TISKENLKEIRKKIGIIfqnpdnqfigaTVEDDIafglenkKVPPKKMkdiiddlakkvgMEDYL-DKEPQ-----NLSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 444 GERRRLYLLRILMDAPNVLILDEPTNDLD----IDTLKVLENYIDDFNGIVICVSHDryfLDRI--CNKIFFFAGdGKII 517
Cdd:PRK13632 146 GQKQRVAIASVLALNPEIIIFDESTSMLDpkgkREIKKIMVDLRKTRKKTLISITHD---MDEAilADKVIVFSE-GKLI 221
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
318-378 |
1.71e-05 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 47.38 E-value: 1.71e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 928932812 318 IIEINHISKSFEQNKViedfSYIALKD--------DRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIG 378
Cdd:COG1135 1 MIELENLSKTFPTKGG----PVTALDDvsltiekgEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVD 65
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
319-529 |
2.12e-05 |
|
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: 47.81 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFEQN-KVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIGPTV-----------KIGYF 386
Cdd:TIGR01193 474 IVINDVSYSYGYGsNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSlkdidrhtlrqFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 387 SQES--------EDMDINLR---AIEYIKEKAEYITTEDGIKisasQMMENFlfSKDLQwTYISKLSGGERRRLYLLRIL 455
Cdd:TIGR01193 554 PQEPyifsgsilENLLLGAKenvSQDEIWAACEIAEIKDDIE----NMPLGY--QTELS-EEGSSISGGQKQRIALARAL 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 456 MDAPNVLILDEPTNDLDIDT-LKVLENYIDDFNGIVICVSHdRYFLDRICNKIFFFAgDGKIIEhTGNYSD------FYK 528
Cdd:TIGR01193 627 LTDSKVLILDESTSNLDTITeKKIVNNLLNLQDKTIIFVAH-RLSVAKQSDKIIVLD-HGKIIE-QGSHDElldrngFYA 703
|
.
gi 928932812 529 S 529
Cdd:TIGR01193 704 S 704
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
347-468 |
2.18e-05 |
|
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: 45.89 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 347 IGIIGKNGTGKSTLLNLITGKLTPDLGSI-----DIG--PTVK-----IGYFSQESE---DMDI--NLRAieyikekAEY 409
Cdd:cd03224 29 VALLGRNGAGKTTLLKTIMGLLPPRSGSIrfdgrDITglPPHEraragIGYVPEGRRifpELTVeeNLLL-------GAY 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 928932812 410 ITTEDGIKISASQMMENFLFSKDLQWTYISKLSGGERRRLYLLRILMDAPNVLILDEPT 468
Cdd:cd03224 102 ARRRAKRKARLERVYELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
5-233 |
2.19e-05 |
|
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: 46.48 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 5 SVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMpskmaieylsqnpEFDPNATIl 84
Cdd:cd03294 26 SKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLI-------------DGQDIAAM- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 85 eqvfkSDSQIMNVIRDYenileeIS---QN----PDDSTLQkkllyltdnmNAQDAWEIENQVKTI--------LTKLGI 149
Cdd:cd03294 92 -----SRKELRELRRKK------ISmvfQSfallPHRTVLE----------NVAFGLEVQGVPRAEreeraaeaLELVGL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 150 HNF-HQKIETLSGGQKKRVALASALISPCDLLILDEPTNHMD----HDTIDWLEKYLTNRTGSLLMITHDryfLD---RV 221
Cdd:cd03294 151 EGWeHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDplirREMQDELLRLQAELQKTIVFITHD---LDealRL 227
|
250
....*....|..
gi 928932812 222 VNKTLELDDGKI 233
Cdd:cd03294 228 GDRIAIMKDGRL 239
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-186 |
3.13e-05 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 45.12 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISKsygeKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHM--------PSKMAIE----Y 70
Cdd:cd03215 4 VLEVRGLSV----KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLdgkpvtrrSPRDAIRagiaY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 71 LsqnPEfDP--NATILEqvfksdsqiMNVirdYENILeeisqnpddstlqkkllyltdnmnaqdaweienqvktiltkLG 148
Cdd:cd03215 80 V---PE-DRkrEGLVLD---------LSV---AENIA-----------------------------------------LS 102
|
170 180 190
....*....|....*....|....*....|....*...
gi 928932812 149 IHnfhqkietLSGGQKKRVALASALISPCDLLILDEPT 186
Cdd:cd03215 103 SL--------LSGGNQQKVVLARWLARDPRVLILDEPT 132
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
328-472 |
3.50e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 45.89 E-value: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 328 FEQNKVIEDFSYIALkddrigiIGKNGTGKSTLLNLITGKLTPDLGSIDIGPTV---------------KIGYFSQ--ES 390
Cdd:PRK13649 24 FDVNLTIEDGSYTAF-------IGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLitstsknkdikqirkKVGLVFQfpES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 391 --------EDMDINLRAIEYIKEKAEYITTEdgiKISASQMMENfLFSKDlqwtyISKLSGGERRRLYLLRILMDAPNVL 462
Cdd:PRK13649 97 qlfeetvlKDVAFGPQNFGVSQEEAEALARE---KLALVGISES-LFEKN-----PFELSGGQMRRVAIAGILAMEPKIL 167
|
170
....*....|
gi 928932812 463 ILDEPTNDLD 472
Cdd:PRK13649 168 VLDEPTAGLD 177
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
22-221 |
3.70e-05 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 46.24 E-value: 3.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 22 ISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVhmpskmaiEYLSQNpefdpnatILEQvfkSDSQIMNVIRDY 101
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEV--------AWLGKD--------LLGM---KDDEWRAVRSDI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 102 ENILEE--ISQNPD---DSTLQKKLLYLTDNMNAQdawEIENQVKTILTKLGI---------HNFhqkietlSGGQKKRV 167
Cdd:PRK15079 101 QMIFQDplASLNPRmtiGEIIAEPLRTYHPKLSRQ---EVKDRVKAMMLKVGLlpnlinrypHEF-------SGGQCQRI 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 928932812 168 ALASALISPCDLLILDEPTNHMD---HDTIDWLEKYLTNRTG-SLLMITHD----RYFLDRV 221
Cdd:PRK15079 171 GIARALILEPKLIICDEPVSALDvsiQAQVVNLLQQLQREMGlSLIFIAHDlavvKHISDRV 232
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-201 |
3.71e-05 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 46.00 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYGE--KILFENISFSIGDTDKIGLIGVNGTGKSSLLKiiagydvADTGKVHMPSKMAIEYLSQnpefdpNA 81
Cdd:cd03289 3 MTVKDLTAKYTEggNAVLENISFSISPGQRVGLLGRTGSGKSTLLS-------AFLRLLNTEGDIQIDGVSW------NS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 82 TILEQVFKSdsqiMNVIRDYENILE-EISQNPDDStlqkkllyltDNMNAQDAWEIENQVKtilTKLGIHNFHQKIE--- 157
Cdd:cd03289 70 VPLQKWRKA----FGVIPQKVFIFSgTFRKNLDPY----------GKWSDEEIWKVAEEVG---LKSVIEQFPGQLDfvl 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 928932812 158 -----TLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYL 201
Cdd:cd03289 133 vdggcVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTL 181
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
331-472 |
3.80e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 45.78 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 331 NKVIEDFSYIAlkddrigIIGKNGTGKSTLLNLITGKLTPDLGSIDIGPTV---------------KIGYFSQ------- 388
Cdd:PRK13634 27 NVSIPSGSYVA-------IIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVitagkknkklkplrkKVGIVFQfpehqlf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 389 -ESEDMDINLRAIEY--IKEKAeyittedgiKISASQMMENFLFSKDLQWTYISKLSGGERRRLYLLRILMDAPNVLILD 465
Cdd:PRK13634 100 eETVEKDICFGPMNFgvSEEDA---------KQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLD 170
|
....*..
gi 928932812 466 EPTNDLD 472
Cdd:PRK13634 171 EPTAGLD 177
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
316-496 |
4.81e-05 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 45.16 E-value: 4.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 316 QKIIEINHISKSFEQNK----VIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGkltpdlgsIDIGPTVKIGYFSQESE 391
Cdd:PRK10584 4 ENIVEVHHLKKSVGQGEhelsILTGVELVVKRGETIALIGESGSGKSTLLAILAG--------LDDGSSGEVSLVGQPLH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 392 DMDINLRA------IEYIKEKAEYITT-----------------EDGIKISASQMMENFLFSKDLQwTYISKLSGGERRR 448
Cdd:PRK10584 76 QMDEEARAklrakhVGFVFQSFMLIPTlnalenvelpallrgesSRQSRNGAKALLEQLGLGKRLD-HLPAQLSGGEQQR 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 928932812 449 LYLLRILMDAPNVLILDEPTNDLDIDT----LKVLENYIDDFNGIVICVSHD 496
Cdd:PRK10584 155 VALARAFNGRPDVLFADEPTGNLDRQTgdkiADLLFSLNREHGTTLILVTHD 206
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
319-496 |
5.24e-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: 44.98 E-value: 5.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSF-EQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIG-------PTV----KIGYF 386
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDgedireqDPVelrrKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 387 SQE---------SEDMDINLRAIEYIKEKaeyittedgIKISASQMMENF-LFSKDLQWTYISKLSGGERRRLYLLRILM 456
Cdd:cd03295 81 IQQiglfphmtvEENIALVPKLLKWPKEK---------IRERADELLALVgLDPAEFADRYPHELSGGQQQRVGVARALA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 928932812 457 DAPNVLILDEPTNDLDIDTLKVLEnyiDDFNGI-------VICVSHD 496
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQ---EEFKRLqqelgktIVFVTHD 195
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
320-521 |
5.55e-05 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 45.06 E-value: 5.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 320 EINHISKSFEQNKVIEDFSyIALKDDRI-GIIGKNGTGKSTLLNLITG--KLTPDLGSI-----DIGptvkigyfsqese 391
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVN-LTIKPGEVhAIMGPNGSGKSTLAKVLMGhpKYEVTSGSIlldgeDIL------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 392 DMDINLRA-----------IEyIKEkaeyITTEDGIKISASQMMEN----FLFSKDLQwTYISKL--------------- 441
Cdd:COG0396 68 ELSPDERAragiflafqypVE-IPG----VSVSNFLRTALNARRGEelsaREFLKLLK-EKMKELgldedfldryvnegf 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 442 SGGERRRLYLLRILMDAPNVLILDEPTNDLDIDTLKVLENYIDDF----NGIVIcVSHDRYFLDRI-CNKIFFFAgDGKI 516
Cdd:COG0396 142 SGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLrspdRGILI-ITHYQRILDYIkPDFVHVLV-DGRI 219
|
....*
gi 928932812 517 IEHTG 521
Cdd:COG0396 220 VKSGG 224
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
18-203 |
5.67e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.56 E-value: 5.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 18 LFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAG-YDVAD----TGKVHMPSKMAIEYLSQNPEfdPNATILEQ------ 86
Cdd:PTZ00265 1183 IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRfYDLKNdhhiVFKNEHTNDMTNEQDYQGDE--EQNVGMKNvnefsl 1260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 87 -----------VFKSDSQIM----NV----IRDYENILEEISQNPddsTLQKKLLYLTDNMNAQDAweIENQVKTILTKL 147
Cdd:PTZ00265 1261 tkeggsgedstVFKNSGKILldgvDIcdynLKDLRNLFSIVSQEP---MLFNMSIYENIKFGKEDA--TREDVKRACKFA 1335
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 928932812 148 GIHNFHQKI------------ETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYLTN 203
Cdd:PTZ00265 1336 AIDEFIESLpnkydtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVD 1403
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-507 |
6.05e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 46.00 E-value: 6.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 2 NILSVENISKSYGEKILF----ENISFSIGDTDKIGLIGVNGTGKS----SLLKII--AGYDV-ADTGKVHMPSKMAIEY 70
Cdd:PRK10261 11 DVLAVENLNIAFMQEQQKiaavRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGLVqCDKMLLRRRSRQVIEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 71 LSQNPE-------------FDPNATILEQVFKSDSQIMNVIRDYENILEEisqnpDDSTLQKKLLyltDNMNAQDAweie 137
Cdd:PRK10261 91 SEQSAAqmrhvrgadmamiFQEPMTSLNPVFTVGEQIAESIRLHQGASRE-----EAMVEAKRML---DQVRIPEA---- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 138 nqvKTILTKLGihnfHQkietLSGGQKKRVALASALISPCDLLILDEPTNHMD---HDTIDWLEKYLTNRTG-SLLMITH 213
Cdd:PRK10261 159 ---QTILSRYP----HQ----LSGGMRQRVMIAMALSCRPAVLIADEPTTALDvtiQAQILQLIKVLQKEMSmGVIFITH 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 214 DRYFLDRVVNKTLELDDGkiysyignysqfieKKLERKTLEsSIERKRERLYKKELewIRAGAQARSTKQKARIQRFE-- 291
Cdd:PRK10261 228 DMGVVAEIADRVLVMYQG--------------EAVETGSVE-QIFHAPQHPYTRAL--LAAVPQLGAMKGLDYPRRFPli 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 292 ELKNTSSPIHDSNIDICVAhsrlGQKIIEINHISKSFEQ-----NKV------IEDFSYIALKDDRIGIIGKNGTGKST- 359
Cdd:PRK10261 291 SLEHPAKQEPPIEQDTVVD----GEPILQVRNLVTRFPLrsgllNRVtrevhaVEKVSFDLWPGETLSLVGESGSGKSTt 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 360 ---LLNLI---TGKLTPDLGSIDIGPTVKIG--------YFSQESEDMDINLRAIEYIKE--KAEYITTEDGIKISASQM 423
Cdd:PRK10261 367 graLLRLVesqGGEIIFNGQRIDTLSPGKLQalrrdiqfIFQDPYASLDPRQTVGDSIMEplRVHGLLPGKAAAARVAWL 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 424 MENFLFSKDLQWTYISKLSGGERRRLYLLRILMDAPNVLILDEPTNDLDIDTLKVLENYIDDFN---GIV-ICVSHDRYF 499
Cdd:PRK10261 447 LERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQrdfGIAyLFISHDMAV 526
|
....*...
gi 928932812 500 LDRICNKI 507
Cdd:PRK10261 527 VERISHRV 534
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-190 |
6.92e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 45.93 E-value: 6.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISKSYGEKIlfENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHM------PS------KMAIEY 70
Cdd:PRK09700 265 VFEVRNVTSRDRKKV--RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLngkdisPRspldavKKGMAY 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 71 LSQNPE---FDPNATILEQVfksdsqimnvirdyenileEISQNPDDSTLQKKLLYLTDNMNAQDAweiENQVKtiLTKL 147
Cdd:PRK09700 343 ITESRRdngFFPNFSIAQNM-------------------AISRSLKDGGYKGAMGLFHEVDEQRTA---ENQRE--LLAL 398
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 928932812 148 GIHNFHQKIETLSGGQKKRVALASALISPCDLLILDEPTNHMD 190
Cdd:PRK09700 399 KCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGID 441
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
333-518 |
6.99e-05 |
|
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: 44.78 E-value: 6.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 333 VIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSI-----DIGPTVK------IGYFSQESedMDINLRAIE 401
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVlvdghDLALADPawlrrqVGVVLQEN--VLFNRSIRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 402 YIKEKAEYITTEDgiKISASQMMENFLFSKDLQWTYI-------SKLSGGERRRLYLLRILMDAPNVLILDEPTNDLDID 474
Cdd:cd03252 95 NIALADPGMSMER--VIEAAKLAGAHDFISELPEGYDtivgeqgAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 928932812 475 TLKVLENYIDDF--NGIVICVSHdRYFLDRICNKIFFFAGdGKIIE 518
Cdd:cd03252 173 SEHAIMRNMHDIcaGRTVIIIAH-RLSTVKNADRIIVMEK-GRIVE 216
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-233 |
7.84e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 45.81 E-value: 7.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISksyGEKilFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVhmpskmaieylsqnpefdpnat 82
Cdd:PRK15439 268 VLTVEDLT---GEG--FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRI---------------------- 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 83 ILEQvfksdsqimnvirdyenilEEISQNPDDSTLQKKLLYLTDNMNAQ----DA----------------WEIENQVKT 142
Cdd:PRK15439 321 MLNG-------------------KEINALSTAQRLARGLVYLPEDRQSSglylDAplawnvcalthnrrgfWIKPARENA 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 143 ILTK----LGIHNFH--QKIETLSGGQKKRVALASALISPCDLLILDEPTNHMD---HDTIDWLEKYLTNRTGSLLMITH 213
Cdd:PRK15439 382 VLERyrraLNIKFNHaeQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDvsaRNDIYQLIRSIAAQNVAVLFISS 461
|
250 260
....*....|....*....|
gi 928932812 214 DRYFLDRVVNKTLELDDGKI 233
Cdd:PRK15439 462 DLEEIEQMADRVLVMHQGEI 481
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
317-507 |
8.08e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 45.55 E-value: 8.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 317 KIIEINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIGPT------------VKIG 384
Cdd:PRK09700 4 PYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNInynkldhklaaqLGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 385 YFSQESEDMD--------------------INLRAIEYIKEKAEYITTEDGIKISASQMMENFLFSKDlQWTYISKlsgg 444
Cdd:PRK09700 84 IIYQELSVIDeltvlenlyigrhltkkvcgVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHK-QMLEIAK---- 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 928932812 445 errrlyllrILMDAPNVLILDEPTNDL---DIDTLKVLENYIDDFNGIVICVSHDRYFLDRICNKI 507
Cdd:PRK09700 159 ---------TLMLDAKVIIMDEPTSSLtnkEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRY 215
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
318-547 |
8.20e-05 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 45.21 E-value: 8.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 318 IIEINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIGptvkigyfSQESEDMDINL 397
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLD--------GVDLSHVPPYQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 398 RAIEYIKEKAE---YITTEDGIKISASQ-------------------MMENFLFSKDLQwtyiskLSGGERRRLYLLRIL 455
Cdd:PRK11607 91 RPINMMFQSYAlfpHMTVEQNIAFGLKQdklpkaeiasrvnemlglvHMQEFAKRKPHQ------LSGGQRQRVALARSL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 456 MDAPNVLILDEPTNDLD--------IDTLKVLENyiddFNGIVICVSHDRyfldricNKIFFFAGDGKIIehtgNYSDFY 527
Cdd:PRK11607 165 AKRPKLLLLDEPMGALDkklrdrmqLEVVDILER----VGVTCVMVTHDQ-------EEAMTMAGRIAIM----NRGKFV 229
|
250 260
....*....|....*....|
gi 928932812 528 KSGRwiHEEIKEEKNTKKSA 547
Cdd:PRK11607 230 QIGE--PEEIYEHPTTRYSA 247
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
319-483 |
8.86e-05 |
|
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: 44.20 E-value: 8.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIG----------PTVKIG-YFS 387
Cdd:TIGR03864 2 LEVAGLSFRYGARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVAghdlrrapraALARLGvVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 388 QESEDMDI----NLR---AIEYI--KEKAEYITTEdgikiSASQMMENFLFSKdlqwtyISKLSGGERRRLYLLRILMDA 458
Cdd:TIGR03864 82 QPTLDLDLsvrqNLRyhaALHGLsrAEARARIAEL-----LARLGLAERADDK------VRELNGGHRRRVEIARALLHR 150
|
170 180
....*....|....*....|....*
gi 928932812 459 PNVLILDEPTNDLDIDTLKVLENYI 483
Cdd:TIGR03864 151 PALLLLDEPTVGLDPASRAAITAHV 175
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
349-503 |
9.00e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 45.25 E-value: 9.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 349 IIGKNGTGKSTLLNLITGKLTPDLGSIDIGPTV---------------KIGYFSQESE-----DMDINLR--AIEYIKEK 406
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVlfdaekgiclppekrRIGYVFQDARlfphyKVRGNLRygMAKSMVAQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 407 AEYITTEDGIKisasqmmenflfskDLQWTYISKLSGGERRRLYLLRILMDAPNVLILDEPTNDLDI----DTLKVLENY 482
Cdd:PRK11144 109 FDKIVALLGIE--------------PLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLprkrELLPYLERL 174
|
170 180
....*....|....*....|.
gi 928932812 483 IDDFNGIVICVSHDryfLDRI 503
Cdd:PRK11144 175 AREINIPILYVSHS---LDEI 192
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
159-233 |
9.13e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 44.69 E-value: 9.13e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 928932812 159 LSGGQKKRVALASALISPCDLLILDEPTNHMD----HDTIDWLEKYLTNRTGSLLMITHDRYFLDRVVNKTLELDDGKI 233
Cdd:PRK10418 141 MSGGMLQRMMIALALLCEAPFIIADEPTTDLDvvaqARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
319-518 |
9.24e-05 |
|
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: 44.14 E-value: 9.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFEQNK-VIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDI-GPTVK----------IGYF 386
Cdd:cd03253 1 IEFENVTFAYDPGRpVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIdGQDIRevtldslrraIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 387 SQESEDMDINLRA-IEYIKEKAeyiTTEDGIKIS-ASQMMENFLFSKDLQWTYIS----KLSGGERRRLYLLRILMDAPN 460
Cdd:cd03253 81 PQDTVLFNDTIGYnIRYGRPDA---TDEEVIEAAkAAQIHDKIMRFPDGYDTIVGerglKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 928932812 461 VLILDEPTNDLDIDT-LKVLENYIDDFNG-IVICVSHDryfLDRI--CNKIFFFaGDGKIIE 518
Cdd:cd03253 158 ILLLDEATSALDTHTeREIQAALRDVSKGrTTIVIAHR---LSTIvnADKIIVL-KDGRIVE 215
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
318-378 |
9.32e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 45.43 E-value: 9.32e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 928932812 318 IIEINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIG 378
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIG 71
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-233 |
9.32e-05 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 45.18 E-value: 9.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 7 ENISKSY----GEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSkmaiEYLSQnpeFDPNAT 82
Cdd:PRK11153 5 KNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDG----QDLTA---LSEKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 83 ILEQ-----VFksdsQIMNVIRD---YENI---LEeisqnpddstlqkkllylTDNMNAQdawEIENQVKTILTKLGIHN 151
Cdd:PRK11153 78 RKARrqigmIF----QHFNLLSSrtvFDNValpLE------------------LAGTPKA---EIKARVTELLELVGLSD 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 152 FHQKIET-LSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYLT--NRTGSL--LMITHDRYFLDRVVNKTL 226
Cdd:PRK11153 133 KADRYPAqLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKdiNRELGLtiVLITHEMDVVKRICDRVA 212
|
....*..
gi 928932812 227 ELDDGKI 233
Cdd:PRK11153 213 VIDAGRL 219
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-214 |
9.38e-05 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 44.90 E-value: 9.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 1 MNILSVEN----ISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYdVADTGKVH-------------MP 63
Cdd:COG4170 1 MPLLDIRNltieIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGI-TKDNWHVTadrfrwngidllkLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 64 SK---------MAIEYlsQNPE--FDPNATILEQvfksdsqimnvirdyenileeISQNPDDSTLQKKLlyltdnmnaqd 132
Cdd:COG4170 80 PRerrkiigreIAMIF--QEPSscLDPSAKIGDQ---------------------LIEAIPSWTFKGKW----------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 133 aWEIENQVKTI----LTKLGIHNfHQKI-----ETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYLT- 202
Cdd:COG4170 126 -WQRFKWRKKRaielLHRVGIKD-HKDImnsypHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLAr 203
|
250
....*....|....*
gi 928932812 203 ---NRTGSLLMITHD 214
Cdd:COG4170 204 lnqLQGTSILLISHD 218
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
319-518 |
1.03e-04 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 44.36 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIGPTV----------------- 381
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITidtarslsqqkglirql 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 382 --KIGYFSQesedmDINL----RAIEYIKEKAEYITTEDgiKISASQMMENFLFSKDL---QWTYISKLSGGERRRLYLL 452
Cdd:PRK11264 84 rqHVGFVFQ-----NFNLfphrTVLENIIEGPVIVKGEP--KEEATARARELLAKVGLagkETSYPRRLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 453 RILMDAPNVLILDEPTNDLDI----DTLKVLENYIDDFNGIVIcVSHDRYFLDRICNKIFFFAGdGKIIE 518
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDPelvgEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQ-GRIVE 224
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
320-378 |
1.14e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 44.90 E-value: 1.14e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 928932812 320 EINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIG 378
Cdd:PRK11288 6 SFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILID 64
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
4-233 |
1.16e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 45.35 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYGEKI---LFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAG-YDVADTGKVHMPSKMAieYLSQNPeFDP 79
Cdd:PLN03232 615 ISIKNGYFSWDSKTskpTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRGSVA--YVPQVS-WIF 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 80 NATILEQV-FKSDsqimnvirdYENilEEISQNPDDSTLQKKLlyltDNMNAQDaweienqvktiLTKLGihnfhQKIET 158
Cdd:PLN03232 692 NATVRENIlFGSD---------FES--ERYWRAIDVTALQHDL----DLLPGRD-----------LTEIG-----ERGVN 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 159 LSGGQKKRVALASALISPCDLLILDEPTN----HMDHDTIDWLEKY-LTNRTgsLLMITHDRYFLDrVVNKTLELDDGKI 233
Cdd:PLN03232 741 ISGGQKQRVSMARAVYSNSDIYIFDDPLSaldaHVAHQVFDSCMKDeLKGKT--RVLVTNQLHFLP-LMDRIILVSEGMI 817
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
318-496 |
1.28e-04 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 44.37 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 318 IIEINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSI----DIGPTVKIGYFSQESEDM 393
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEIlfdgENIPAMSRSRLYTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 394 -----------DIN--------LRaiEYIKEKAEYITTEDGIKIS------ASQMMEnflfskdlqwtyiSKLSGGERRR 448
Cdd:PRK11831 87 smlfqsgalftDMNvfdnvaypLR--EHTQLPAPLLHSTVMMKLEavglrgAAKLMP-------------SELSGGMARR 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 928932812 449 LYLLRILMDAPNVLILDEPTNDLDIDTLKVLENYIDDFN---GIV-ICVSHD 496
Cdd:PRK11831 152 AALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNsalGVTcVVVSHD 203
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
347-517 |
1.30e-04 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 45.04 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 347 IGIIGKNGTGKSTLLNLITGKLTPDLgsiDIGPTVKIGYFSQESEDMdinlRAIE-YIKEKAEYI---TTEDGIKISASQ 422
Cdd:TIGR00955 54 LAVMGSSGAGKTTLMNALAFRSPKGV---KGSGSVLLNGMPIDAKEM----RAISaYVQQDDLFIptlTVREHLMFQAHL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 423 MMENFLFSK----------------DLQWTYI------SKLSGGERRRLYLLRILMDAPNVLILDEPTNDLD-------I 473
Cdd:TIGR00955 127 RMPRRVTKKekrervdevlqalglrKCANTRIgvpgrvKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDsfmaysvV 206
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 928932812 474 DTLKVLENyiddfNG-IVICVSHD-RYFLDRICNKIFFFAgDGKII 517
Cdd:TIGR00955 207 QVLKGLAQ-----KGkTIICTIHQpSSELFELFDKIILMA-EGRVA 246
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
343-509 |
1.31e-04 |
|
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: 42.75 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 343 KDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIdigptvkigyfsqesedmdinlraieyikekaeyittedgIKISASQ 422
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV----------------------------------------IYIDGED 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 423 MMENFLFSKDLQWTYISKLSGGERRRLYLLRILMDAPN--VLILDEPTNDLDIDTLKVLENYIDDF---------NGIVI 491
Cdd:smart00382 41 ILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKpdVLILDEITSLLDAEQEALLLLLEELRlllllksekNLTVI 120
|
170
....*....|....*...
gi 928932812 492 CVSHDRYFLDRICNKIFF 509
Cdd:smart00382 121 LTTNDEKDLGPALLRRRF 138
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
318-377 |
1.41e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 44.31 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 318 IIEINHISKSFEQNKVIE------------DFSYI-ALKD--------DRIGIIGKNGTGKSTLLNLITGKLTPDLGSID 376
Cdd:COG4586 1 IIEVENLSKTYRVYEKEPglkgalkglfrrEYREVeAVDDisftiepgEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
.
gi 928932812 377 I 377
Cdd:COG4586 81 V 81
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
347-375 |
1.51e-04 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 44.79 E-value: 1.51e-04
10 20
....*....|....*....|....*....
gi 928932812 347 IGIIGKNGTGKSTLLNLITGKLTPDLGSI 375
Cdd:COG4615 361 VFIVGGNGSGKSTLAKLLTGLYRPESGEI 389
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
319-514 |
1.63e-04 |
|
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: 43.36 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHIsKSFEQNKVIEDFSYIALkddrigIIGKNGTGKSTLLNLI----TGKLTPDLGSIDIGPTVkigyFSQESEDMD 394
Cdd:cd03240 4 LSIRNI-RSFHERSEIEFFSPLTL------IVGQNGAGKTTIIEALkyalTGELPPNSKGGAHDPKL----IREGEVRAQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 395 INLRAIEYIKEKaeyittedgIKISAS-QMMENFLFSK--DLQWTY---ISKLSGGERRRLYLL-----RILMDAP-NVL 462
Cdd:cd03240 73 VKLAFENANGKK---------YTITRSlAILENVIFCHqgESNWPLldmRGRCSGGEKVLASLIirlalAETFGSNcGIL 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 928932812 463 ILDEPTNDLDIDTL-KVLENYIDDFNGI----VICVSHDRYFLDRIcNKIFFFAGDG 514
Cdd:cd03240 144 ALDEPTTNLDEENIeESLAEIIEERKSQknfqLIVITHDEELVDAA-DHIYRVEKDG 199
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
4-190 |
1.67e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 44.52 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISksyGEKiLFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKmAIEYLSqnpefdPNATI 83
Cdd:PRK11288 258 LRLDGLK---GPG-LREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGK-PIDIRS------PRDAI 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 84 LEQVF------KSDSqIMNVIRDYENIleEISQNPDDSTLqkkllyltdNMNAQDAWEIENQVKTIlTKLGIH--NFHQK 155
Cdd:PRK11288 327 RAGIMlcpedrKAEG-IIPVHSVADNI--NISARRHHLRA---------GCLINNRWEAENADRFI-RSLNIKtpSREQL 393
|
170 180 190
....*....|....*....|....*....|....*
gi 928932812 156 IETLSGGQKKRVALASALISPCDLLILDEPTNHMD 190
Cdd:PRK11288 394 IMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGID 428
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
384-557 |
1.71e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.02 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 384 GYFSQESEDMDINlraiEYIKEKAEYITTEDG--IKISASQMMENFLFS-----KDLQWTYISKLSGGERRRLYLLRILM 456
Cdd:PTZ00265 520 GDLNDMSNTTDSN----ELIEMRKNYQTIKDSevVDVSKKVLIHDFVSAlpdkyETLVGSNASKLSGGQKQRISIARAII 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 457 DAPNVLILDEPTNDLDIDTLKVLENYIDDFNG----IVICVSHdRYFLDRICNKIFFFAGDGKiiehtGNYSDFYKSGRW 532
Cdd:PTZ00265 596 RNPKILILDEATSSLDNKSEYLVQKTINNLKGnenrITIIIAH-RLSTIRYANTIFVLSNRER-----GSTVDVDIIGED 669
|
170 180
....*....|....*....|....*..
gi 928932812 533 IHEEIKE--EKNTKKSAPQKPKEKKLK 557
Cdd:PTZ00265 670 PTKDNKEnnNKNNKDDNNNNNNNNNNK 696
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
316-522 |
1.77e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 43.48 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 316 QKIIEINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITG-------------------KLTPDLGS-- 374
Cdd:CHL00131 5 KPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpaykilegdilfkgesilDLEPEERAhl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 375 ---------IDIgPTV------KIGYFSQESEDMDINLRAIEYIkekaEYITTedgiKISASQMMENFLfSKDLQwtyiS 439
Cdd:CHL00131 85 giflafqypIEI-PGVsnadflRLAYNSKRKFQGLPELDPLEFL----EIINE----KLKLVGMDPSFL-SRNVN----E 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 440 KLSGGERRRLYLLRILMDAPNVLILDEPTNDLDIDTLKVLENYIDDF----NGIVIcVSHDRYFLDRICNKIFFFAGDGK 515
Cdd:CHL00131 151 GFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLmtseNSIIL-ITHYQRLLDYIKPDYVHVMQNGK 229
|
....*..
gi 928932812 516 IIEhTGN 522
Cdd:CHL00131 230 IIK-TGD 235
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
314-518 |
1.77e-04 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 43.80 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 314 LGQKIIEINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIGptvkiGYFSQESEDM 393
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVN-----GQTINLVRDK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 394 DINLRAIEyiKEKAEYITT----------------------EDGIKI---SASQMMENFLFSKD-------LQWTYISKL 441
Cdd:PRK10619 76 DGQLKVAD--KNQLRLLRTrltmvfqhfnlwshmtvlenvmEAPIQVlglSKQEARERAVKYLAkvgiderAQGKYPVHL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 442 SGGERRRLYLLRILMDAPNVLILDEPTNDLDI----DTLKVLENYIDDFNGIVIcVSHDRYFLDRICNKIFFFAgDGKII 517
Cdd:PRK10619 154 SGGQQQRVSIARALAMEPEVLLFDEPTSALDPelvgEVLRIMQQLAEEGKTMVV-VTHEMGFARHVSSHVIFLH-QGKIE 231
|
.
gi 928932812 518 E 518
Cdd:PRK10619 232 E 232
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
334-376 |
1.82e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 43.65 E-value: 1.82e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 928932812 334 IEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSID 376
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD 82
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
349-472 |
1.82e-04 |
|
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: 42.87 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 349 IIGKNGTGKSTLLNLITGKLTPDLGSIDIGPTvkigyfsQESEDMDINLRAIEYIKEkaeyittEDGIKISASqMMENFL 428
Cdd:cd03231 31 VTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG-------PLDFQRDSIARGLLYLGH-------APGIKTTLS-VLENLR 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 928932812 429 F-----SKDLQWTYISK-------------LSGGERRRLYLLRILMDAPNVLILDEPTNDLD 472
Cdd:cd03231 96 FwhadhSDEQVEEALARvglngfedrpvaqLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
319-526 |
1.96e-04 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 43.46 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTL---LNLITgklTPDLGSIDIGptvkiGY---FSQESED 392
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLlrvLNLLE---MPRSGTLNIA-----GNhfdFSKTPSD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 393 MDI------------------------NL-----RAIEYIKEKAEyittEDGIKISASQMMENFLFSKDLQwtyiskLSG 443
Cdd:PRK11124 75 KAIrelrrnvgmvfqqynlwphltvqqNLieapcRVLGLSKDQAL----ARAEKLLERLRLKPYADRFPLH------LSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 444 GERRRLYLLRILMDAPNVLILDEPTNDLD-------IDTLKVLENyiddfNGI--VIcVSHDRYFLDRICNKIFFFAgDG 514
Cdd:PRK11124 145 GQQQRVAIARALMMEPQVLLFDEPTAALDpeitaqiVSIIRELAE-----TGItqVI-VTHEVEVARKTASRVVYME-NG 217
|
250
....*....|..
gi 928932812 515 KIIEHtGNYSDF 526
Cdd:PRK11124 218 HIVEQ-GDASCF 228
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
348-520 |
2.47e-04 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 43.24 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 348 GIIGKNGTGKSTLLNLITGKLTPDLGSIDIGPTV-----------KIGYFSQE---SEDMDI-NLRAI-EYI-------- 403
Cdd:PRK10575 41 GLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPleswsskafarKVAYLPQQlpaAEGMTVrELVAIgRYPwhgalgrf 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 404 ----KEKAEYITTEDGIKISASQMMENflfskdlqwtyiskLSGGERRRLYLLRILMDAPNVLILDEPTNDLDI----DT 475
Cdd:PRK10575 121 gaadREKVEEAISLVGLKPLAHRLVDS--------------LSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIahqvDV 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 928932812 476 LKVLENYIDDFNGIVICVSHDRYFLDRICNKIFFFAGDGKIIEHT 520
Cdd:PRK10575 187 LALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGT 231
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
347-513 |
2.47e-04 |
|
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: 42.17 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 347 IGIIGKNGTGKSTLLNLITGKLTPDLGSIDIgPTVKIGYfsqesedmdinlraieyikeKAEYIttedgikisasqmmen 426
Cdd:cd03222 28 IGIVGPNGTGKTTAVKILAGQLIPNGDNDEW-DGITPVY--------------------KPQYI---------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 427 flfskdlqwtyisKLSGGERRRLYLLRILMDAPNVLILDEPTNDLDID----TLKVLENYIDDFNGIVICVSHDRYFLDR 502
Cdd:cd03222 71 -------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlnAARAIRRLSEEGKKTALVVEHDLAVLDY 137
|
170
....*....|.
gi 928932812 503 ICNKIFFFAGD 513
Cdd:cd03222 138 LSDRIHVFEGE 148
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
318-384 |
3.10e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 43.86 E-value: 3.10e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 928932812 318 IIEINHISKSFeqNKVIedfsyiALkdDRI----------GIIGKNGTGKSTLLNLITGKLTPDLGSIDI-GPTVKIG 384
Cdd:COG3845 5 ALELRGITKRF--GGVV------AN--DDVsltvrpgeihALLGENGAGKSTLMKILYGLYQPDSGEILIdGKPVRIR 72
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
10-190 |
3.44e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 43.71 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 10 SKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAG---------YDVADTGKVHMPSKMAIEYLSQNPEFDPN 80
Cdd:PLN03211 75 TRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGriqgnnftgTILANNRKPTKQILKRTGFVTQDDILYPH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 81 ATILEQ-VFKSdsqimnvirdyenileeISQNPDDSTLQKKLLYLTDNMNAQDAWEIENQVktiltklgIHNfhQKIETL 159
Cdd:PLN03211 155 LTVRETlVFCS-----------------LLRLPKSLTKQEKILVAESVISELGLTKCENTI--------IGN--SFIRGI 207
|
170 180 190
....*....|....*....|....*....|..
gi 928932812 160 SGGQKKRVALA-SALISPcDLLILDEPTNHMD 190
Cdd:PLN03211 208 SGGERKRVSIAhEMLINP-SLLILDEPTSGLD 238
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-186 |
3.46e-04 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 42.72 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLK-------IIAGYDVadTGKvhmpskmaIEYLSQN- 74
Cdd:COG1117 11 KIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGARV--EGE--------ILLDGEDi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 75 --PEFDPNAtiLEQ----VF-------KSdsqImnvirdYENI--------------LEEISQnpddSTLQKKLLyltdn 127
Cdd:COG1117 81 ydPDVDVVE--LRRrvgmVFqkpnpfpKS---I------YDNVayglrlhgikskseLDEIVE----ESLRKAAL----- 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 128 mnaqdaWEienQVKTILTKLGIHnfhqkietLSGGQKKRVALASAL-ISPcDLLILDEPT 186
Cdd:COG1117 141 ------WD---EVKDRLKKSALG--------LSGGQQQRLCIARALaVEP-EVLLMDEPT 182
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
319-375 |
3.87e-04 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 42.87 E-value: 3.87e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 928932812 319 IEINHISKSFEQNKViedfSYIALKD--------DRIGIIGKNGTGKSTLLNLITGKLTPDLGSI 375
Cdd:PRK11153 2 IELKNISKVFPQGGR----TIHALNNvslhipagEIFGVIGASGAGKSTLIRCINLLERPTSGRV 62
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
317-517 |
3.97e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 42.73 E-value: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 317 KIIEINHI---SKSFEQnKVIEDFSyIALKD-DRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIGpTVKIgyfsqesED 392
Cdd:PRK13637 4 KIENLTHIymeGTPFEK-KALDNVN-IEIEDgEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIID-GVDI-------TD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 393 MDINLRAI-----------------EYIKEKAEYIT-----TEDGIKISASQMMENFLFSKDlqwTYISK----LSGGER 446
Cdd:PRK13637 74 KKVKLSDIrkkvglvfqypeyqlfeETIEKDIAFGPinlglSEEEIENRVKRAMNIVGLDYE---DYKDKspfeLSGGQK 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 928932812 447 RRLYLLRILMDAPNVLILDEPTNDLDI----DTLKVLENYIDDFNGIVICVSHDRYFLDRICNKIFFFaGDGKII 517
Cdd:PRK13637 151 RRVAIAGVVAMEPKILILDEPTAGLDPkgrdEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVM-NKGKCE 224
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
153-212 |
4.05e-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: 41.86 E-value: 4.05e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 928932812 153 HQKIETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDT-IDWLE--KYLTNRTGSLLMIT 212
Cdd:cd03233 113 NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTaLEILKciRTMADVLKTTTFVS 175
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
159-233 |
4.18e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 42.78 E-value: 4.18e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 928932812 159 LSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYLTNRTGSL--LMITHDRYFLDRVVNKTLELDDGKI 233
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLtvIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-51 |
4.34e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 42.91 E-value: 4.34e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 928932812 1 MNILSVENISKSYGEKIL-FENISFSIGDTDKIGLIGVNGTGKSSLLKIIAG 51
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKTQvIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAG 52
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
349-496 |
5.53e-04 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 42.23 E-value: 5.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 349 IIGKNGTGKSTLLNLITGkLTPDLGSIDIG-------PTVKI----GYFSQESE---DMDInlraieyikekAEYITTE- 413
Cdd:PRK03695 27 LVGPNGAGKSTLLARMAG-LLPGSGSIQFAgqpleawSAAELarhrAYLSQQQTppfAMPV-----------FQYLTLHq 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 414 -DGIKISASQ----MMENFLFSKDLQWTYISKLSGGERRRLYLLRILMDA-----PN--VLILDEPTNDLDIDTLKVLEN 481
Cdd:PRK03695 95 pDKTRTEAVAsalnEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQVwpdinPAgqLLLLDEPMNSLDVAQQAALDR 174
|
170
....*....|....*...
gi 928932812 482 YIDDF--NGIVICVS-HD 496
Cdd:PRK03695 175 LLSELcqQGIAVVMSsHD 192
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
21-214 |
6.04e-04 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 42.40 E-value: 6.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 21 NISFSIGDTdkIGLIGVNGTGKSSLLKIIAGYdVADTGKVHMPSKMAIEYLSQNPEFDPNATILEQVfksdSQI----MN 96
Cdd:PRK09473 36 NFSLRAGET--LGIVGESGSGKSQTAFALMGL-LAANGRIGGSATFNGREILNLPEKELNKLRAEQI----SMIfqdpMT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 97 VIRDYENILEEISQnpddstlqkkLLYLTDNMNAQDAWEieNQVKtILTKLGIHNFHQKIET----LSGGQKKRVALASA 172
Cdd:PRK09473 109 SLNPYMRVGEQLME----------VLMLHKGMSKAEAFE--ESVR-MLDAVKMPEARKRMKMypheFSGGMRQRVMIAMA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 928932812 173 LISPCDLLILDEPTNHMDHdTIDWLEKYLTNR-----TGSLLMITHD 214
Cdd:PRK09473 176 LLCRPKLLIADEPTTALDV-TVQAQIMTLLNElkrefNTAIIMITHD 221
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
318-375 |
6.14e-04 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 41.99 E-value: 6.14e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 928932812 318 IIEINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSI 375
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSI 58
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
289-472 |
6.17e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 42.94 E-value: 6.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 289 RFEELKNTSSpihdsNIDICVAHsrlGQKIIEInhiSKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKL 368
Cdd:PLN03211 50 KFENMKNKGS-----NIKRILGH---KPKISDE---TRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 369 TPD--LGSIDIG------PTVK-IGYFSQEsedmDI---NLRAIEYI--------------KEK---AEYITTEDGIKIS 419
Cdd:PLN03211 119 QGNnfTGTILANnrkptkQILKrTGFVTQD----DIlypHLTVRETLvfcsllrlpksltkQEKilvAESVISELGLTKC 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 928932812 420 ASQMMENflfskdlqwTYISKLSGGERRRLYLLRILMDAPNVLILDEPTNDLD 472
Cdd:PLN03211 195 ENTIIGN---------SFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
15-233 |
7.22e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 42.07 E-value: 7.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 15 EKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMpSKMAIEYLSQNPEFDPNATILEQVFK-SDSQ 93
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTV-DDITITHKTKDKYIRPVRKRIGMVFQfPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 94 IMNvirdyENILEEISQNPDDStlqkkllyltdNMNAQdawEIENQVKTILTKLGihnFHQKIETLS-----GGQKKRVA 168
Cdd:PRK13646 98 LFE-----DTVEREIIFGPKNF-----------KMNLD---EVKNYAHRLLMDLG---FSRDVMSQSpfqmsGGQMRKIA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 928932812 169 LASALISPCDLLILDEPTNHMD----HDTIDWLEKYLTNRTGSLLMITHDRYFLDRVVNKTLELDDGKI 233
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDpqskRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
317-496 |
7.25e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 42.00 E-value: 7.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 317 KIIEINHISKSFEQNKVIEDF---SYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDI-GPTV----------K 382
Cdd:PRK13642 3 KILEVENLVFKYEKESDVNQLngvSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIdGELLtaenvwnlrrK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 383 IGYFSQESEDMDINLRAIEYIKEKAEY--ITTEDGIK-ISASQMMENFLfskDLQWTYISKLSGGERRRLYLLRILMDAP 459
Cdd:PRK13642 83 IGMVFQNPDNQFVGATVEDDVAFGMENqgIPREEMIKrVDEALLAVNML---DFKTREPARLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 928932812 460 NVLILDEPTNDLD----IDTLKVLENYIDDFNGIVICVSHD 496
Cdd:PRK13642 160 EIIILDESTSMLDptgrQEIMRVIHEIKEKYQLTVLSITHD 200
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
296-507 |
7.62e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 42.69 E-value: 7.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 296 TSSPIHDSNIDICVAHSRL---GQK--IIEINHISKSFE--QNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKL 368
Cdd:TIGR01257 1910 AKEPIFDEDDDVAEERQRIisgGNKtdILRLNELTKVYSgtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDT 1989
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 369 TPDLGSIDI-GPTV---------KIGYFSQ-ESEDMDINLRAIEYIKEKAEYITTEDGIKIS--ASQMMENFLFSKDLQW 435
Cdd:TIGR01257 1990 TVTSGDATVaGKSIltnisdvhqNMGYCPQfDAIDDLLTGREHLYLYARLRGVPAEEIEKVAnwSIQSLGLSLYADRLAG 2069
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 928932812 436 TYisklSGGERRRLYLLRILMDAPNVLILDEPTNDLDIDTLKVLENYIDDF---NGIVICVSHDRYFLDRICNKI 507
Cdd:TIGR01257 2070 TY----SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIireGRAVVLTSHSMEECEALCTRL 2140
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
334-377 |
8.10e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 42.57 E-value: 8.10e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 928932812 334 IEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDI 377
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI 83
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
318-517 |
8.53e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 41.60 E-value: 8.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 318 IIEINHISKSF-EQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDI-GPTVK------------I 383
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIkGEPIKydkksllevrktV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 384 GYFSQESEDMDINLRAIEYI----------KEKAEYITTEDGIKISasqmMENFlfskdlQWTYISKLSGGERRRLYLLR 453
Cdd:PRK13639 81 GIVFQNPDDQLFAPTVEEDVafgplnlglsKEEVEKRVKEALKAVG----MEGF------ENKPPHHLSGGQKKRVAIAG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 928932812 454 ILMDAPNVLILDEPTNDLDIDTLKVLENYIDDFN--GIVICVS-HDRYFLDRICNKIFFFAgDGKII 517
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNkeGITIIIStHDVDLVPVYADKVYVMS-DGKII 216
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
349-495 |
8.80e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 41.01 E-value: 8.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 349 IIGKNGTGKSTLLNLITGKLTPDLGSIDIGPtvkigyfsQESEDMDInlraieyiKEKAEYITTEDGIKISASqMMENFL 428
Cdd:PRK13539 33 LTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG--------GDIDDPDV--------AEACHYLGHRNAMKPALT-VAENLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 429 FskdlqWtyiSKLSGGERRRLYLLRILMDAPNVL----------------------------ILDEPTNDLDIDTLKVLE 480
Cdd:PRK13539 96 F-----W---AAFLGGEELDIAAALEAVGLAPLAhlpfgylsagqkrrvalarllvsnrpiwILDEPTAALDAAAVALFA 167
|
170
....*....|....*...
gi 928932812 481 NYIDDF---NGIVICVSH 495
Cdd:PRK13539 168 ELIRAHlaqGGIVIAATH 185
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
316-518 |
9.40e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 41.30 E-value: 9.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 316 QKIIEINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLIT--GKLTPDL---GSIDI------GPTV--- 381
Cdd:PRK14239 3 EPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEVtitGSIVYnghniySPRTdtv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 382 ----KIGYFSQES--------EDMDINLRaIEYIKEKAEYITTEDGIKISASQMMEnflfSKDLQWTYISKLSGGERRRL 449
Cdd:PRK14239 83 dlrkEIGMVFQQPnpfpmsiyENVVYGLR-LKGIKDKQVLDEAVEKSLKGASIWDE----VKDRLHDSALGLSGGQQQRV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 928932812 450 YLLRILMDAPNVLILDEPTNDLD-IDTLKV---LENYIDDFNgiVICVSHDRYFLDRICNKIFFFAgDGKIIE 518
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDpISAGKIeetLLGLKDDYT--MLLVTRSMQQASRISDRTGFFL-DGDLIE 227
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
318-378 |
9.67e-04 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 41.54 E-value: 9.67e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 928932812 318 IIEINHISKSFEQNKVIEDFSyIALKDDRI-GIIGKNGTGKSTLLNLITGKLTPDLGSIDIG 378
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLS-LSLPTGKItALIGPNGCGKSTLLKCFARLLTPQSGTVFLG 62
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
318-518 |
9.84e-04 |
|
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: 41.33 E-value: 9.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 318 IIEINHISKSFEQN---------KVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIG--PTVKIGYF 386
Cdd:TIGR02769 2 LLEVRDVTHTYRTGglfgakqraPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRgqDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 387 SQESEDMDINL------------RAIEY-IKEKAEYITTEDGI--KISASQMMENFLFSKDLQWTYISKLSGGERRRLYL 451
Cdd:TIGR02769 82 QRRAFRRDVQLvfqdspsavnprMTVRQiIGEPLRHLTSLDESeqKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 928932812 452 LRILMDAPNVLILDEPTNDLDI----DTLKVLENYIDDFNGIVICVSHDRYFLDRICNKIFFFAGdGKIIE 518
Cdd:TIGR02769 162 ARALAVKPKLIVLDEAVSNLDMvlqaVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDK-GQIVE 231
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
349-502 |
1.01e-03 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 41.01 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 349 IIGKNGTGKSTLLNLITGKLTPDLGSI-----DIG-------PTVK--IGYFSQESED-MDINLR---AIEYIKEKAeyi 410
Cdd:PRK10908 33 LTGHSGAGKSTLLKLICGIERPSAGKIwfsghDITrlknrevPFLRrqIGMIFQDHHLlMDRTVYdnvAIPLIIAGA--- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 411 tTEDGIKISASQMMENF-LFSKdlQWTYISKLSGGERRRLYLLRILMDAPNVLILDEPTNDLDIDTLKVLENYIDDFNGI 489
Cdd:PRK10908 110 -SGDDIRRRVSAALDKVgLLDK--AKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRV 186
|
170
....*....|....*.
gi 928932812 490 ---VICVSHDRYFLDR 502
Cdd:PRK10908 187 gvtVLMATHDIGLISR 202
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
159-213 |
1.11e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 41.54 E-value: 1.11e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 928932812 159 LSGGQKKRVALASALISPCDLLILDEPTNHMD----HDTIDWLEKYLTNRTGSLLMITH 213
Cdd:PRK13634 146 LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDpkgrKEMMEMFYKLHKEKGLTTVLVTH 204
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
3-190 |
1.38e-03 |
|
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: 40.30 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 3 ILSVENISksY------GEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVAD--TGKVHM---PSKMAIE-- 69
Cdd:cd03232 3 VLTWKNLN--YtvpvkgGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILIngrPLDKNFQrs 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 70 --YLSQNPEFDPNATILEqvfksdsqimnvirdyenileeisqnpddsTLQkkllyltdnmnaqdaweienqvktiltkl 147
Cdd:cd03232 81 tgYVEQQDVHSPNLTVRE------------------------------ALR----------------------------- 101
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 928932812 148 gihnFHQKIETLSGGQKKRVALASALISPCDLLILDEPTNHMD 190
Cdd:cd03232 102 ----FSALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
160-190 |
1.40e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 41.10 E-value: 1.40e-03
10 20 30
....*....|....*....|....*....|.
gi 928932812 160 SGGQKKRVALASALISPCDLLILDEPTNHMD 190
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
21-284 |
1.61e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 41.41 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 21 NISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVHMPSKMAIEYLSqnpefdpnatileqvfksdSQIMNVIRD 100
Cdd:PRK13545 42 NISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAIS-------------------SGLNGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 101 YENIleeisqnpddsTLQKKLLYLTDNmnaqdawEIENQVKTILTKLGIHNF-HQKIETLSGGQKKRVALA-SALISPcD 178
Cdd:PRK13545 103 IENI-----------ELKGLMMGLTKE-------KIKEIIPEIIEFADIGKFiYQPVKTYSSGMKSRLGFAiSVHINP-D 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 179 LLILDEPTNHMDHD-TIDWLEKY--LTNRTGSLLMITHDRYFLDRVVNKTLELDDGKIYSY------IGNYSQFIeKKLE 249
Cdd:PRK13545 164 ILVIDEALSVGDQTfTKKCLDKMneFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYgdikevVDHYDEFL-KKYN 242
|
250 260 270
....*....|....*....|....*....|....*
gi 928932812 250 RKTLESSIERKRERLYKKELEWIRAGAQARSTKQK 284
Cdd:PRK13545 243 QMSVEERKDFREEQISQFQHGLLQEDQTGRERKRK 277
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
347-391 |
1.88e-03 |
|
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: 41.27 E-value: 1.88e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 928932812 347 IGIIGKNGTGKSTLLNLITGKLTPDLGSI-------------DIGPTvkIGYFSQESE 391
Cdd:COG4618 361 LGVIGPSGSGKSTLARLLVGVWPPTAGSVrldgadlsqwdreELGRH--IGYLPQDVE 416
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
440-518 |
2.11e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 40.46 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 440 KLSGGERRRLYLLRILMDAPNVLILDEPTNDLDIDTLKVLENYIDDFNG--IVICVSHDRYFLDRICNKIFFFAgDGKII 517
Cdd:PRK14271 163 RLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHNLAQAARISDRAALFF-DGRLV 241
|
.
gi 928932812 518 E 518
Cdd:PRK14271 242 E 242
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
318-496 |
2.37e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 40.17 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 318 IIEINHISKSFEQNK--VIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPdlgsiDIGPTVKIGYfsqesEDMDI 395
Cdd:PRK13640 5 IVEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLP-----DDNPNSKITV-----DGITL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 396 NLRAIEYIKEKAEYI-----------TTEDGI-------KISASQMME------NFLFSKDLQWTYISKLSGGERRRLYL 451
Cdd:PRK13640 75 TAKTVWDIREKVGIVfqnpdnqfvgaTVGDDVafglenrAVPRPEMIKivrdvlADVGMLDYIDSEPANLSGGQKQRVAI 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 928932812 452 LRILMDAPNVLILDEPTNDLD----IDTLKVLENYIDDFNGIVICVSHD 496
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDpagkEQILKLIRKLKKKNNLTVISITHD 203
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
316-377 |
2.41e-03 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 40.16 E-value: 2.41e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 928932812 316 QKIIEINHISKSF---------EQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDI 377
Cdd:PRK15112 2 ETLLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLI 72
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
319-519 |
2.43e-03 |
|
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: 39.70 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 319 IEINHISKSFEQN--KVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIgptvkigyfsqesEDMDIN 396
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEI-------------DGIDIS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 397 LRAIEYIKEKAEYITTEDGI-------------KISASQMMENFLFSKDLqwtyiSKLSGGERRRLYLLRILMDAPNVLI 463
Cdd:cd03369 74 TIPLEDLRSSLTIIPQDPTLfsgtirsnldpfdEYSDEEIYGALRVSEGG-----LNLSQGQRQLLCLARALLKRPRVLV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 928932812 464 LDEPTNDLDIDTLKVLENYI-DDFNGIVICVSHDRyfLDRI--CNKIFFFAgDGKIIEH 519
Cdd:cd03369 149 LDEATASIDYATDALIQKTIrEEFTNSTILTIAHR--LRTIidYDKILVMD-AGEVKEY 204
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
19-174 |
2.52e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 40.37 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 19 FENISFSIGDTDKIG-LIGVNGTGKSSLLKIIA---GYDVADTGKVHmPSKMAIEYLSQNPE------FDPNATILEQVF 88
Cdd:COG3950 14 FEDLEIDFDNPPRLTvLVGENGSGKTTLLEAIAlalSGLLSRLDDVK-FRKLLIRNGEFGDSaklilyYGTSRLLLDGPL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 89 KSDSQIM-NVIRDYENILEEISQNPDDSTLQKKLLYLTDNMNAQDAWEIENQ---VKTILTKL----------------- 147
Cdd:COG3950 93 KKLERLKeEYFSRLDGYDSLLDEDSNLREFLEWLREYLEDLENKLSDELDEKleaVREALNKLlpdfkdiridrdpgrlv 172
|
170 180
....*....|....*....|....*....
gi 928932812 148 GIHNFHQKI--ETLSGGQKKRVALASALI 174
Cdd:COG3950 173 ILDKNGEELplNQLSDGERSLLALVGDLA 201
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
159-224 |
2.80e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 40.17 E-value: 2.80e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 159 LSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYLT----NRTGSLLMITHDRYFLDRVVNK 224
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTrlnqNNNTTILLISHDLQMLSQWADK 228
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
536-617 |
2.99e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 536 EIKEE-KNTKKSAPQKPKEKKLKFTYNEQR---EYETIDQEIENLENKLSTLEEEMKKYSTDFTKLQELMNEKDYIEEEL 611
Cdd:PRK12704 61 EAKEEiHKLRNEFEKELRERRNELQKLEKRllqKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQ 140
|
....*.
gi 928932812 612 LLKMER 617
Cdd:PRK12704 141 LQELER 146
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
349-479 |
3.75e-03 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 39.17 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 349 IIGKNGTGKSTLLNLITGKL--TPDLGSIDigptVKIGYFSQESEDMDiNLRAIEYIKEKAEYIttedgikiSASQMMEN 426
Cdd:COG2401 61 IVGASGSGKSTLLRLLAGALkgTPVAGCVD----VPDNQFGREASLID-AIGRKGDFKDAVELL--------NAVGLSDA 127
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 928932812 427 FLFSKdlqwTYiSKLSGGERRRLYLLRILMDAPNVLILDEPTNDLDIDTLKVL 479
Cdd:COG2401 128 VLWLR----RF-KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRV 175
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
316-497 |
3.90e-03 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 40.09 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 316 QKIIEINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIDIgptvkigyfsqESEDM-- 393
Cdd:PRK11432 4 KNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFI-----------DGEDVth 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 394 -DINLRAI-----EY-------IKEKAEYITTEDGI-KISASQMMENFLFSKDL---QWTYISKLSGGERRRLYLLRILM 456
Cdd:PRK11432 73 rSIQQRDIcmvfqSYalfphmsLGENVGYGLKMLGVpKEERKQRVKEALELVDLagfEDRYVDQISGGQQQRVALARALI 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 928932812 457 DAPNVLILDEPTNDLDIDTLKVLENYIDD----FNGIVICVSHDR 497
Cdd:PRK11432 153 LKPKVLLFDEPLSNLDANLRRSMREKIRElqqqFNITSLYVTHDQ 197
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
152-214 |
3.99e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 38.49 E-value: 3.99e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 152 FHQKIETLSGGQKKRVALASAL----ISPCDLLILDEPTNHMD-HDT--IDWLEKYLTNRTGSLLMITHD 214
Cdd:cd03227 71 LIFTRLQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDpRDGqaLAEAILEHLVKGAQVIVITHL 140
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
154-190 |
4.19e-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: 38.71 E-value: 4.19e-03
10 20 30
....*....|....*....|....*....|....*..
gi 928932812 154 QKIEtLSGGQKKRVALASALISPCDLLILDEPTNHMD 190
Cdd:cd03222 68 QYID-LSGGELQRVAIAAALLRNATFYLFDEPSAYLD 103
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
318-497 |
4.51e-03 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 38.93 E-value: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 318 IIEINHISKSFEQNKVIEDFSYIALKDDRIGIIGKNGTGKSTLLNLITGKLTPDLGSIdigptvkigYFsqesEDMDINL 397
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTL---------LF----EGEDIST 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 398 RAIEYIKEKAEYI---------TTEDGIKIS---ASQMMENFLFSKDLQW---------TYISKLSGGERRRLYLLRILM 456
Cdd:PRK10247 74 LKPEIYRQQVSYCaqtptlfgdTVYDNLIFPwqiRNQQPDPAIFLDDLERfalpdtiltKNIAELSGGEKQRISLIRNLQ 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 928932812 457 DAPNVLILDEPTNDLDIDTLK----VLENYIDDFNGIVICVSHDR 497
Cdd:PRK10247 154 FMPKVLLLDEITSALDESNKHnvneIIHRYVREQNIAVLWVTHDK 198
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
159-233 |
4.65e-03 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 39.94 E-value: 4.65e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 928932812 159 LSGGQKKRVALASALISPCDLLILDEPTNHMDHDT----IDWLEKYLTNRTgsLLMITHdRYFLDRVVNKTLELDDGKI 233
Cdd:PRK13657 472 LSGGERQRLAIARALLKDPPILILDEATSALDVETeakvKAALDELMKGRT--TFIIAH-RLSTVRNADRILVFDNGRV 547
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
391-495 |
5.43e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.01 E-value: 5.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 391 EDMDINLRAIEYIKEKAEYITTEDGIKISASQMMENFLFSKDLQWT-----YISKLSGGERRRLYLLRILMDAPNVLILD 465
Cdd:PTZ00265 1304 EPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDtnvgpYGKSLSGGQKQRIAIARALLREPKILLLD 1383
|
90 100 110
....*....|....*....|....*....|....
gi 928932812 466 EPTNDLDIDTLKVLENYI----DDFNGIVICVSH 495
Cdd:PTZ00265 1384 EATSSLDSNSEKLIEKTIvdikDKADKTIITIAH 1417
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
4-233 |
8.48e-03 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 38.86 E-value: 8.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 4 LSVENISKSYGEKILFENISFSIGDTDKIGLIGVNGTGKSSLLKIIAGYDVADTGKVhMPSKMAIEYLSQNPEFDPNATI 83
Cdd:PRK10070 29 LSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQV-LIDGVDIAKISDAELREVRRKK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 84 LEQVFKSDSQIMNV-IRDYENILEEISQNPDDSTLQKKLlyltdnmnaqDAweienqvktiLTKLGIHNF-HQKIETLSG 161
Cdd:PRK10070 108 IAMVFQSFALMPHMtVLDNTAFGMELAGINAEERREKAL----------DA----------LRQVGLENYaHSYPDELSG 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 928932812 162 GQKKRVALASALISPCDLLILDEPTNHMD----HDTIDWLEKYLTNRTGSLLMITHDRYFLDRVVNKTLELDDGKI 233
Cdd:PRK10070 168 GMRQRVGLARALAINPDILLMDEAFSALDplirTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
137-220 |
9.06e-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: 37.35 E-value: 9.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 137 ENQVKTILTKLGIHNFHQKIETLSGGQKKRVALASALISPCDLLILDEPTNHMDHDTIDWLEKYLTNRTG---------S 207
Cdd:smart00382 39 EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLlllkseknlT 118
|
90
....*....|...
gi 928932812 208 LLMITHDRYFLDR 220
Cdd:smart00382 119 VILTTNDEKDLGP 131
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
159-233 |
9.28e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 39.34 E-value: 9.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928932812 159 LSGGQKKRVALASALISPCDLLILDEPTNHMD-H------DTIdwLEKYLTNRTGSLlmITHDRYFLDRvVNKTLELDDG 231
Cdd:PLN03130 741 ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDaHvgrqvfDKC--IKDELRGKTRVL--VTNQLHFLSQ-VDRIILVHEG 815
|
..
gi 928932812 232 KI 233
Cdd:PLN03130 816 MI 817
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
459-512 |
9.91e-03 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 38.55 E-value: 9.91e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 928932812 459 PNVLILDEPTNDLD------IDTLkvLENYIDDFNGIVICVSHDRYFLDRICNKIF-FFAG 512
Cdd:PRK09473 180 PKLLIADEPTTALDvtvqaqIMTL--LNELKREFNTAIIMITHDLGVVAGICDKVLvMYAG 238
|
|
| |
