|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-633 |
0e+00 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 1104.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 1 MALLTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQQDLKVTRLEQDPPASSE 80
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPRNVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 81 ITVFDYAAEGLAGVGELLKQYHHVSHALAHDPSDANIRTMSQLQEQLDYQNGWQYETRINQVLTLLDLDPDVTLDSLSGG 160
Cdd:PRK11147 81 GTVYDFVAEGIEEQAEYLKRYHDISHLVETDPSEKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGLDPDAALSSLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 161 WLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITSWPGNYDE 240
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 241 YLQGKEEWLRVEELKNAEFDRKLAQEEVWVRQGIKARRTRNEGRVRALKAMRMERTQRRELQGKAKLQLDEAGRSGKLVF 320
Cdd:PRK11147 241 YLLEKEEALRVEELQNAEFDRKLAQEEVWIRQGIKARRTRNEGRVRALKALRRERSERREVMGTAKMQVEEASRSGKIVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRQGTNLEVAYFDQYREQLDPEKTV 400
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRAELDPEKTV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 401 VDNVGEGKQEVMVRGRSRHILGYLQDFLFEPKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLE 480
Cdd:PRK11147 401 MDNLAEGKQEVMVNGRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 481 ELLTDYPGTLLLVSHDRRFIDNTVTGCWLFEGDGRISDYVGGYADMMATRALQAAQQTAKPAPVKVAEPvASAAEPAKKT 560
Cdd:PRK11147 481 ELLDSYQGTVLLVSHDRQFVDNTVTECWIFEGNGKIGRYVGGYHDARQQQAQYLALKQPAVKKKEEAAA-PKAETVKRSS 559
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 657198994 561 RKLSYKLQLELDNLPARLEQLEMELDALQAEINHPGFFSLPAEQTQPKLDALNAAEAALEHAFSRWEELEALK 633
Cdd:PRK11147 560 KKLSYKLQRELEQLPQLLEDLEAEIEALQAQVADADFFSQPHEQTQKVLADLADAEQELEVAFERWEELEALK 632
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-528 |
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: 676.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 6 LHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQQDLKVTRLEQDPPASSEITVFD 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 86 YAAEGLAGVGELLKQYHHVSHALAHdpSDANIRTMSQLQEQLDYQNGWQYETRINQVLTLLDL---DPDVTLDSLSGGWL 162
Cdd:COG0488 81 TVLDGDAELRALEAELEELEAKLAE--PDEDLERLAELQEEFEALGGWEAEARAEEILSGLGFpeeDLDRPVSELSGGWR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 163 RKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITSWPGNYDEYL 242
Cdd:COG0488 159 RRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 243 QGKEEWLRVEELKNAEFDRKLAQEEVWVRQ-GIKARR-TRNEGRVRALKAMRMERTQRRElqGKAKLQLDEAGRSGKLVF 320
Cdd:COG0488 239 EQRAERLEQEAAAYAKQQKKIAKEEEFIRRfRAKARKaKQAQSRIKALEKLEREEPPRRD--KTVEIRFPPPERLGKKVL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRQGTNLEVAYFDQYREQLDPEKTV 400
Cdd:COG0488 317 ELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEELDPDKTV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 401 VDNVGEGKQEvmvrGRSRHILGYLQDFLFEPKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLE 480
Cdd:COG0488 397 LDELRDGAPG----GTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALE 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 657198994 481 ELLTDYPGTLLLVSHDRRFIDNTVTGCWLFEgDGRISDYVGGYADMMA 528
Cdd:COG0488 473 EALDDFPGTVLLVSHDRYFLDRVATRILEFE-DGGVREYPGGYDDYLE 519
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-545 |
1.27e-127 |
|
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: 387.37 E-value: 1.27e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 6 LHGASLSFsdFPlldhaeltierGERLCLVGRNGAGKSTLMKVIASelpLD---DGRLVLQQDLKVTRLEQDPPASSEIT 82
Cdd:TIGR03719 21 LKDISLSF--FP-----------GAKIGVLGLNGAGKSTLLRIMAG---VDkdfNGEARPQPGIKVGYLPQEPQLDPTKT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 83 VFDYAAEGLAGVGELLKQYHHVSHALAHDPSDAN--IRTMSQLQEQLDYQNGWQYETRINQVLTLLDLDP-DVTLDSLSG 159
Cdd:TIGR03719 85 VRENVEEGVAEIKDALDRFNEISAKYAEPDADFDklAAEQAELQEIIDAADAWDLDSQLEIAMDALRCPPwDADVTKLSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 160 GWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITSWPGNYD 239
Cdd:TIGR03719 165 GERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 240 EYLQGKEEWLRVEELKNAEFDRKLAQEEVWVRQGIKARRTRNEGRVRALKAMRMERTQRRElqGKAKLQLDEAGRSGKLV 319
Cdd:TIGR03719 245 SWLEQKQKRLEQEEKEESARQKTLKRELEWVRQSPKGRQAKSKARLARYEELLSQEFQKRN--ETAEIYIPPGPRLGDKV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 320 FETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRQGTNLEVAYFDQYREQLDPEKT 399
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRDALDPNKT 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 400 VVDNVGEGKQEVMVRGRSRHILGYLQDFLFEPKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLELL 479
Cdd:TIGR03719 403 VWEEISGGLDIIKLGKREIPSRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRAL 482
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 657198994 480 EELLTDYPGTLLLVSHDRRFIDNTVTGCWLFEGDGRISDYVGGYADMMATRALQAAQQTAKPAPVK 545
Cdd:TIGR03719 483 EEALLNFAGCAVVISHDRWFLDRIATHILAFEGDSHVEWFEGNFSEYEEDKKRRLGEDADQPHRIK 548
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
10-525 |
1.49e-124 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 379.46 E-value: 1.49e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 10 SLSFsdFPlldhaeltierGERLCLVGRNGAGKSTLMKVIASelpLD---DGRLVLQQDLKVTRLEQDPPASSEITVFDY 86
Cdd:PRK11819 27 SLSF--FP-----------GAKIGVLGLNGAGKSTLLRIMAG---VDkefEGEARPAPGIKVGYLPQEPQLDPEKTVREN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 87 AAEGLAGVGELLKQYHHVSHALAHDP--SDANIRTMSQLQEQLDYQNGWQYETRINQVLTLLDL-DPDVTLDSLSGGWLR 163
Cdd:PRK11819 91 VEEGVAEVKAALDRFNEIYAAYAEPDadFDALAAEQGELQEIIDAADAWDLDSQLEIAMDALRCpPWDAKVTKLSGGERR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 164 KVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITSWPGNYDEYLQ 243
Cdd:PRK11819 171 RVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 244 GKEEWLRVEELKNAEFDRKLAQEEVWVRQGIKARRTRNEGRVRALKAMRMERTQRRElqGKAKLQLDEAGRSGKLVFETE 323
Cdd:PRK11819 251 QKAKRLAQEEKQEAARQKALKRELEWVRQSPKARQAKSKARLARYEELLSEEYQKRN--ETNEIFIPPGPRLGDKVIEAE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 324 GLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRQGTNLEVAYFDQYREQLDPEKTVVDN 403
Cdd:PRK11819 329 NLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQSRDALDPNKTVWEE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 404 VGEGKQEVMVRGR---SRhilGYLQDFLFEPKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLE 480
Cdd:PRK11819 409 ISGGLDIIKVGNReipSR---AYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALE 485
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 657198994 481 ELLTDYPGTLLLVSHDRRFIDNTVTGCWLFEGDGRISDYVGGYAD 525
Cdd:PRK11819 486 EALLEFPGCAVVISHDRWFLDRIATHILAFEGDSQVEWFEGNFQE 530
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
29-533 |
1.04e-85 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 277.93 E-value: 1.04e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 29 GERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQQDLKVTRLEQDPPASSEITVFDYAaegLAGVGEL--LKQYHHVSH 106
Cdd:PRK15064 27 GNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFEEFTVLDTV---IMGHTELweVKQERDRIY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 107 ALAhDPSDANIRTMSQLQEQLDYQNGWQYETRINQVLTLLDLDPDV---TLDSLSGGWLRKVALARALACDPDLLLLDEP 183
Cdd:PRK15064 104 ALP-EMSEEDGMKVADLEVKFAEMDGYTAEARAGELLLGVGIPEEQhygLMSEVAPGWKLRVLLAQALFSNPDILLLDEP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 184 TNHLDIDAINWLEEFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITSWPGNYDEYL----QGKEEWLrveelknAEF 259
Cdd:PRK15064 183 TNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEYMtaatQARERLL-------ADN 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 260 DRKLAQ-EEVwvrQGIKARRTRNegrvrALKAMrmERTQR-RELQgkaKLQLDEAGRSGK---------------LVFET 322
Cdd:PRK15064 256 AKKKAQiAEL---QSFVSRFSAN-----ASKAK--QATSRaKQID---KIKLEEVKPSSRqnpfirfeqdkklhrNALEV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 323 EGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRQGTNLEVAYFDQ-YREQLDPEKTVV 401
Cdd:PRK15064 323 ENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQdHAYDFENDLTLF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 402 DNVGEGKQ----EVMVRGrsrhILGYLqdfLFEPKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLE 477
Cdd:PRK15064 403 DWMSQWRQegddEQAVRG----TLGRL---LFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIE 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 657198994 478 LLEELLTDYPGTLLLVSHDRRFIDNTVTGCWLFEGDGrISDYVGGYADMMATRALQ 533
Cdd:PRK15064 476 SLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDG-VVDFSGTYEEYLRSQGIE 530
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
18-593 |
7.40e-70 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 238.53 E-value: 7.40e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 18 LLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQQDLKVTRLEQDPPASsEITVFDYAAEGLAGVGEL 97
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPAL-PQPALEYVIDGDREYRQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 98 LKQYHHvshalAHDPSDANirTMSQLQEQLDYQNGWQYETRINQVLTLLDLDPDV---TLDSLSGGWLRKVALARALACD 174
Cdd:PRK10636 95 EAQLHD-----ANERNDGH--AIATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQlerPVSDFSGGWRMRLNLAQALICR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 175 PDLLLLDEPTNHLDIDAINWLEEFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITSWPGNYDEYlqgkeEWLRVEEL 254
Cdd:PRK10636 168 SDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSF-----EVQRATRL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 255 KNAEFDRKLAQEEVWVRQG----IKARRTR---NEGRVRALKamRMERTQRRELQGKAKLQLDEAGRSGKLVFETEGLGL 327
Cdd:PRK10636 243 AQQQAMYESQQERVAHLQSyidrFRAKATKakqAQSRIKMLE--RMELIAPAHVDNPFHFSFRAPESLPNPLLKMEKVSA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 328 DFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRQGTNLEVAYFDQYR-EQLDPEKTVVDNVGE 406
Cdd:PRK10636 321 GYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQlEFLRADESPLQHLAR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 407 GKQEVMvrgrSRHILGYLQDFLFEPKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEELLTDY 486
Cdd:PRK10636 401 LAPQEL----EQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 487 PGTLLLVSHDRRFIDNTVTGCWLFEgDGRISDYVGGYADMMATRALQAAQQTAKPAPVKvaEPVASAAEPAKKTRKLSYK 566
Cdd:PRK10636 477 EGALVVVSHDRHLLRSTTDDLYLVH-DGKVEPFDGDLEDYQQWLSDVQKQENQTDEAPK--ENNANSAQARKDQKRREAE 553
|
570 580
....*....|....*....|....*..
gi 657198994 567 LQLELDNLPARLEQLEMELDALQAEIN 593
Cdd:PRK10636 554 LRTQTQPLRKEIARLEKEMEKLNAQLA 580
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
10-525 |
1.14e-54 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 198.55 E-value: 1.14e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 10 SLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIA-----------------SELPLDDG---RLVLQQDLKVT 69
Cdd:PLN03073 184 SISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidgipkncqilhveQEVVGDDTtalQCVLNTDIERT 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 70 RL-EQDPPASSEITVFDYAAEGLAGVGELLkqyhhvshalAHDPSDANIRTMSQLQEQLDYQNGWQYETRINQVLTLLDL 148
Cdd:PLN03073 264 QLlEEEAQLVAQQRELEFETETGKGKGANK----------DGVDKDAVSQRLEEIYKRLELIDAYTAEARAASILAGLSF 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 149 DPDVTL---DSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRGAIVFISHDREFIHKLATRIID 225
Cdd:PLN03073 334 TPEMQVkatKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILH 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 226 LDRGVITSWPGNYDEYLQGKEEWLRVEELKNAEFDRKLAQEEVWV---RQGIKaRRTRNEGRVRALKamRMERTQRRELQ 302
Cdd:PLN03073 414 LHGQKLVTYKGDYDTFERTREEQLKNQQKAFESNERSRSHMQAFIdkfRYNAK-RASLVQSRIKALD--RLGHVDAVVND 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 303 GKAKLQL---DEAGRSGKLVFETEGLGLDfGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRQG 379
Cdd:PLN03073 491 PDYKFEFptpDDRPGPPIISFSDASFGYP-GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRS 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 380 TNLEVAYFDQYReqldpektvVDNVGEGKQEVMVRGR------SRHILGYLQDFLFEPKRARTPVKALSGGEKNRLLLAK 453
Cdd:PLN03073 570 AKVRMAVFSQHH---------VDGLDLSSNPLLYMMRcfpgvpEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAK 640
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 657198994 454 LFLKPSNLLILDEPTNDLDVETLELLEELLTDYPGTLLLVSHDRRFIDNTVTGCWLFEgDGRISDYVGGYAD 525
Cdd:PLN03073 641 ITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVS-EGKVTPFHGTFHD 711
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
322-539 |
1.50e-52 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 188.74 E-value: 1.50e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 322 TEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRQGTNLEVAYFDQyREQLDPEKTVV 401
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQ-EPPLDDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 402 DNVGEGKQEVM-VRGRSRHI-------------LGYLQDFL--------------------FEPKRARTPVKALSGGEKN 447
Cdd:COG0488 80 DTVLDGDAELRaLEAELEELeaklaepdedlerLAELQEEFealggweaearaeeilsglgFPEEDLDRPVSELSGGWRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 448 RLLLAKLFLKPSNLLILDEPTNDLDVETLELLEELLTDYPGTLLLVSHDRRFIDNTVTgcWLFE-GDGRISDYVGGYADM 526
Cdd:COG0488 160 RVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVAT--RILElDRGKLTLYPGNYSAY 237
|
250
....*....|...
gi 657198994 527 MATRALQAAQQTA 539
Cdd:COG0488 238 LEQRAERLEQEAA 250
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-243 |
1.66e-51 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 185.65 E-value: 1.66e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 3 LLTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQQDLKVTRLEQDPPA-SSEI 81
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEElDPDK 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 82 TVFDYAAEGLAGVGELlkqyhHVSHALAH---DPSDAnirtmsqlqeqldyqngwqyETRINqvltlldldpdvtldSLS 158
Cdd:COG0488 395 TVLDELRDGAPGGTEQ-----EVRGYLGRflfSGDDA--------------------FKPVG---------------VLS 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 159 GGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITSWPGNY 238
Cdd:COG0488 435 GGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGY 514
|
....*
gi 657198994 239 DEYLQ 243
Cdd:COG0488 515 DDYLE 519
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
323-514 |
2.79e-49 |
|
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: 168.40 E-value: 2.79e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 323 EGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRQGTNLEVAYFDQyreqldpektvvd 402
Cdd:cd03221 4 ENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 403 nvgegkqevmvrgrsrhilgylqdflfepkrartpvkaLSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEEL 482
Cdd:cd03221 71 --------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEA 112
|
170 180 190
....*....|....*....|....*....|..
gi 657198994 483 LTDYPGTLLLVSHDRRFIDNTVTGCWLFEGDG 514
Cdd:cd03221 113 LKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-229 |
4.08e-49 |
|
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: 168.01 E-value: 4.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 4 LTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQQDLKVTRLEQdppasseitv 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 84 fdyaaeglagvgellkqyhhvshalahdpsdanirtmsqlqeqldyqngwqyetrinqvltlldldpdvtldsLSGGWLR 163
Cdd:cd03221 71 -------------------------------------------------------------------------LSGGEKM 77
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 657198994 164 KVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRGAIVFISHDREFIHKLATRIIDLDRG 229
Cdd:cd03221 78 RLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-473 |
3.64e-43 |
|
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: 162.38 E-value: 3.64e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 2 ALLTLHGASLSF--SDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELP---------LDDGRLVLQQDLKVTR 70
Cdd:COG1123 3 PLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggrisgevLLDGRDLLELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 71 LE-----QDPPAS-SEITVFDYAAEGLAGVGellkqyhhVSHALAHDpsdanirtmsqlqeqldyqngwqyetRINQVLT 144
Cdd:COG1123 83 RRigmvfQDPMTQlNPVTVGDQIAEALENLG--------LSRAEARA--------------------------RVLELLE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 145 LLDLDP--DVTLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLD----IDAINWLEEFLKDFRGAIVFISHDREFIHK 218
Cdd:COG1123 129 AVGLERrlDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDvttqAEILDLLRELQRERGTTVLLITHDLGVVAE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 219 LATRIIDLDRGVItswpgnydeylqgkeewlrVEELKNAEFDRklaqeevwvrqgikarrtrnegRVRALKAmrmertqr 298
Cdd:COG1123 209 IADRVVVMDDGRI-------------------VEDGPPEEILA----------------------APQALAA-------- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 299 RELQGKAKLQLDEAGRSGKLVFETEGLGLDF-----GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASR 373
Cdd:COG1123 240 VPRLGAARGRAAPAAAAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTS 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 374 GSVR-QGTNLEVAYFDQYRE--------------QLDPEKTVVDNVGEGkqeVMVRG------RSRHILGYLQDFLFEPK 432
Cdd:COG1123 320 GSILfDGKDLTKLSRRSLRElrrrvqmvfqdpysSLNPRMTVGDIIAEP---LRLHGllsraeRRERVAELLERVGLPPD 396
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 657198994 433 RARTPVKALSGGEKNRLLLAK-LFLKPSnLLILDEPTNDLDV 473
Cdd:COG1123 397 LADRYPHELSGGQRQRVAIARaLALEPK-LLILDEPTSALDV 437
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-243 |
4.72e-36 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 135.60 E-value: 4.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 1 MALLTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRL-VLQQDLKVTR-----LEQD 74
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVrLFGKPPRRARrrigyVPQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 75 PPASSE--ITVFDYAAEGLAGVGELLKQYHHVSHAlahdpsdanirtmsqlqeqldyqngwqyetRINQVLTLLDLDP-- 150
Cdd:COG1121 84 AEVDWDfpITVRDVVLMGRYGRRGLFRRPSRADRE------------------------------AVDEALERVGLEDla 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 151 DVTLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRG---AIVFISHDREFIHKLATRIIDLD 227
Cdd:COG1121 134 DRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDLGAVREYFDRVLLLN 213
|
250
....*....|....*.
gi 657198994 228 RGVITSwpGNYDEYLQ 243
Cdd:COG1121 214 RGLVAH--GPPEEVLT 227
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-231 |
2.12e-35 |
|
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: 134.02 E-value: 2.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 3 LLTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQ-QDL----------KVTRL 71
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDgRDLaslsrrelarRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 72 EQDPPASSEITVFDYAAEGLagvgellkqYHHvshalahdpsdanIRTMSQLQEQlDYQngwqyetRINQVLTLLDLDP- 150
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGR---------YPH-------------LGLFGRPSAE-DRE-------AVEEALERTGLEHl 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 151 -DVTLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDI----DAINWLEEFLKDFRGAIVFISHDREFIHKLATRIID 225
Cdd:COG1120 131 aDRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLahqlEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVL 210
|
....*.
gi 657198994 226 LDRGVI 231
Cdd:COG1120 211 LKDGRI 216
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-231 |
2.58e-35 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 133.27 E-value: 2.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 4 LTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGR-LVLQQDLKVTRLE---------Q 73
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEvRVLGEDVARDPAEvrrrigyvpQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 74 DPPASSEITVFDYAaeglagvgELLKQYHHVSHALAhdpsdanirtmsqlqeqldyqngwqyETRINQVLTLLDLDP--D 151
Cdd:COG1131 81 EPALYPDLTVRENL--------RFFARLYGLPRKEA--------------------------RERIDELLELFGLTDaaD 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 152 VTLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDF--RGAIVFIS-HDREFIHKLATRIIDLDR 228
Cdd:COG1131 127 RKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELaaEGKTVLLStHYLEEAERLCDRVAIIDK 206
|
...
gi 657198994 229 GVI 231
Cdd:COG1131 207 GRI 209
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-258 |
4.05e-33 |
|
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: 127.28 E-value: 4.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 3 LLTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLD------DGRLVLQQDLKVTR----LE 72
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDsgsiliDGEDVRKEPREARRqigvLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 73 QDPPASSEITVFDYAaeglagvgellkQYhhvsHALAHDPSDANIrtmsqlqeqldyqngwqyETRINQVLTLLDLDP-- 150
Cdd:COG4555 81 DERGLYDRLTVRENI------------RY----FAELYGLFDEEL------------------KKRIEELIELLGLEEfl 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 151 DVTLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRG---AIVFISHDREFIHKLATRIIDLD 227
Cdd:COG4555 127 DRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKegkTVLFSSHIMQEVEALCDRVVILH 206
|
250 260 270
....*....|....*....|....*....|....
gi 657198994 228 RGVIT---SWPGNYDEYLQGKEEWLRVEELKNAE 258
Cdd:COG4555 207 KGKVVaqgSLDELREEIGEENLEDAFVALIGSEE 240
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2-228 |
4.82e-33 |
|
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: 126.05 E-value: 4.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 2 ALLTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQQdlkvTRLEQDPPAssei 81
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNG----EPIRDARED---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 82 tvfdyaaeglagvgellkqYHHVSHALAHDpsDANIRTMSqLQEQLDY----QNGWQYETRINQVLTLLDLDP--DVTLD 155
Cdd:COG4133 73 -------------------YRRRLAYLGHA--DGLKPELT-VRENLRFwaalYGLRADREAIDEALEAVGLAGlaDLPVR 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 657198994 156 SLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFR---GAIVFISHDREFIhkLATRIIDLDR 228
Cdd:COG4133 131 QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLargGAVLLTTHQPLEL--AAARVLDLGD 204
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-231 |
6.29e-33 |
|
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: 124.43 E-value: 6.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 4 LTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGrlvlqqdlkvtrleqdppassEITV 83
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSG---------------------EIKV 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 84 FDyaaeglagvgellkqyhhvshalaHDPSDANIRTMSQL----QEQLDYQNgwqyetrinqvLTLLDLdpdvtLDsLSG 159
Cdd:cd03230 60 LG------------------------KDIKKEPEEVKRRIgylpEEPSLYEN-----------LTVREN-----LK-LSG 98
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 657198994 160 GWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFR---GAIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:cd03230 99 GMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKkegKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
11-229 |
2.02e-32 |
|
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: 124.12 E-value: 2.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 11 LSFS----DFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGR-LVLQQDLKVTRLE----------QDP 75
Cdd:cd03225 5 LSFSypdgARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEvLVDGKDLTKLSLKelrrkvglvfQNP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 76 PAS-SEITVFDYAAEGLAGVGellkqyhhvshalaHDPSDAnirtmsqlqeqldyqngwqyETRINQVLTLLDLDP--DV 152
Cdd:cd03225 85 DDQfFGPTVEEEVAFGLENLG--------------LPEEEI--------------------EERVEEALELVGLEGlrDR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 153 TLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRGA---IVFISHDREFIHKLATRIIDLDRG 229
Cdd:cd03225 131 SPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEgktIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-231 |
4.88e-31 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 120.31 E-value: 4.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 4 LTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQQdlkVTRLEQDPPasseitv 83
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDG---KPLSAMPPP------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 84 fdyaaeglagvgELLKQyhhVSHaLAHDPS--DANIRTmsQLQEQLDYQNGWQYETRINQVLTLLDLDPDV---TLDSLS 158
Cdd:COG4619 71 ------------EWRRQ---VAY-VPQEPAlwGGTVRD--NLPFPFQLRERKFDRERALELLERLGLPPDIldkPVERLS 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 657198994 159 GGWLRKVALARALACDPDLLLLDEPTNHLDIDA----INWLEEFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:COG4619 133 GGERQRLALIRALLLQPDVLLLDEPTSALDPENtrrvEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-231 |
1.34e-30 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 119.18 E-value: 1.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 6 LHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRL-VLQQDLKVTR-----------LEQ 73
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIrVFGKPLEKERkrigyvpqrrsIDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 74 DPPasseITVFDYAAEGLagvgellkqYHHVSHalahdpsdanIRTMSQLQEQldyqngwqyetRINQVLTLLDLD--PD 151
Cdd:cd03235 82 DFP----ISVRDVVLMGL---------YGHKGL----------FRRLSKADKA-----------KVDEALERVGLSelAD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 152 VTLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRG---AIVFISHDREFIHKLATRIIDLDR 228
Cdd:cd03235 128 RQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRegmTILVVTHDLGLVLEYFDRVLLLNR 207
|
...
gi 657198994 229 GVI 231
Cdd:cd03235 208 TVV 210
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-246 |
2.37e-30 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 125.39 E-value: 2.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 4 LTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQQDLKVTRLEQDPPA--SSEI 81
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHAYdfENDL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 82 TVFDYaaeglagvgellkqyhhvshalahdpsdanirtMSQL-QEQLDyqngwqyETRINQVLTLL-----DLDPDVTld 155
Cdd:PRK15064 400 TLFDW---------------------------------MSQWrQEGDD-------EQAVRGTLGRLlfsqdDIKKSVK-- 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 156 SLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITSWP 235
Cdd:PRK15064 438 VLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFS 517
|
250
....*....|...
gi 657198994 236 GNYDEYL--QGKE 246
Cdd:PRK15064 518 GTYEEYLrsQGIE 530
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
11-231 |
8.15e-29 |
|
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: 114.74 E-value: 8.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 11 LSFS---DFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGR-LVLQQDLKVTRLE----------QDP- 75
Cdd:COG1122 6 LSFSypgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEvLVDGKDITKKNLRelrrkvglvfQNPd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 76 -----PasseiTVFDYAAEGLAgvgellkqyhhvshALAHDPSDAnirtmsqlqeqldyqngwqyETRINQVLTLLDLDP 150
Cdd:COG1122 86 dqlfaP-----TVEEDVAFGPE--------------NLGLPREEI--------------------RERVEEALELVGLEH 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 151 --DVTLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRGA---IVFISHDREFIHKLATRIID 225
Cdd:COG1122 127 laDRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEgktVIIVTHDLDLVAELADRVIV 206
|
....*.
gi 657198994 226 LDRGVI 231
Cdd:COG1122 207 LDDGRI 212
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
335-469 |
1.03e-28 |
|
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: 111.59 E-value: 1.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 335 FQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSV-----------RQGTNLEVAYFDQYrEQLDPEKTVVDN 403
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTIlldgqdltddeRKSLRKEIGYVFQD-PQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 657198994 404 VGEGKQEVMVRGRSR-----HILGYLQDFLFEPKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTN 469
Cdd:pfam00005 80 LRLGLLLKGLSKREKdaraeEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-473 |
1.48e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 119.74 E-value: 1.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 1 MALLTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLqqDLKVTRLeqDPPASS- 79
Cdd:COG1129 2 EPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILL--DGEPVRF--RSPRDAq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 80 ---------EITVFDY--AAEGLAgVGELLKQYHHVSHAlahdpsdaniRTMSQLQEQLDyqngwqyetRINqvltlLDL 148
Cdd:COG1129 78 aagiaiihqELNLVPNlsVAENIF-LGREPRRGGLIDWR----------AMRRRARELLA---------RLG-----LDI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 149 DPDVTLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRG---AIVFISHDREFIHKLAtriid 225
Cdd:COG1129 133 DPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAqgvAIIYISHRLDEVFEIA----- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 226 lDRGVItswpgnydeylqgkeewLR----VEELKNAEFDRklaqEEVwVRQ--GikarrtrnegrvRALKAMRMERTQrr 299
Cdd:COG1129 208 -DRVTV-----------------LRdgrlVGTGPVAELTE----DEL-VRLmvG------------RELEDLFPKRAA-- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 300 elqgkaklqldeagRSGKLVFETEGLGLdfgdRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRG----- 374
Cdd:COG1129 251 --------------APGEVVLEVEGLSV----GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGeirld 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 375 -------SVRQGTNLEVAYF--DQYREQLDPEKTVVDNVGEGKQEVMVRGR-------SRHILGYLQDFLFEPKRARTPV 438
Cdd:COG1129 313 gkpvrirSPRDAIRAGIAYVpeDRKGEGLVLDLSIRENITLASLDRLSRGGlldrrreRALAEEYIKRLRIKTPSPEQPV 392
|
490 500 510
....*....|....*....|....*....|....*.
gi 657198994 439 KALSGGEKNRLLLAK-LFLKPSnLLILDEPTNDLDV 473
Cdd:COG1129 393 GNLSGGNQQKVVLAKwLATDPK-VLILDEPTRGIDV 427
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-231 |
1.76e-28 |
|
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: 113.75 E-value: 1.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 3 LLTLHGASLSFSD----FPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVL---------QQDLKVT 69
Cdd:cd03257 1 LLEVKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFdgkdllklsRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 70 RLE-----QDPPASseitvfdyaaeglagvgelLKQYHHVSHALAhDPsdanirtmsqLQEQLDYQNGWQYETRINQVLT 144
Cdd:cd03257 81 RKEiqmvfQDPMSS-------------------LNPRMTIGEQIA-EP----------LRIHGKLSKKEARKEAVLLLLV 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 145 LLDLDPDVtLDS----LSGGWLRKVALARALACDPDLLLLDEPTNHLDIDA----INWLEEFLKDFRGAIVFISHDREFI 216
Cdd:cd03257 131 GVGLPEEV-LNRypheLSGGQRQRVAIARALALNPKLLIADEPTSALDVSVqaqiLDLLKKLQEELGLTLLFITHDLGVV 209
|
250
....*....|....*
gi 657198994 217 HKLATRIIDLDRGVI 231
Cdd:cd03257 210 AKIADRVAVMYAGKI 224
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-232 |
2.85e-28 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 113.74 E-value: 2.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 3 LLTLHGASLSFS----DFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQ-QDLKVTRLE----- 72
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDgRPVTRRRRKafrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 73 -----QDPPASSE--ITVFDYAAEGLAGVGELlkqyhhvshalahdpsdanirtmsqlqeqldyqngwQYETRINQVLTL 145
Cdd:COG1124 81 vqmvfQDPYASLHprHTVDRILAEPLRIHGLP------------------------------------DREERIAELLEQ 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 146 LDLDPDVtLD----SLSGGWLRKVALARALACDPDLLLLDEPTNHLDI----DAINWLEEFLKDFRGAIVFISHDREFIH 217
Cdd:COG1124 125 VGLPPSF-LDryphQLSGGQRQRVAIARALILEPELLLLDEPTSALDVsvqaEILNLLKDLREERGLTYLFVSHDLAVVA 203
|
250
....*....|....*
gi 657198994 218 KLATRIIDLDRGVIT 232
Cdd:COG1124 204 HLCDRVAVMQNGRIV 218
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-229 |
3.63e-28 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 110.41 E-value: 3.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 5 TLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLqqdlkvtrleqdppasseitvf 84
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILI---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 85 dyaaeglagvgellkqyhhvshalahDPSDANIRTMSQLQEQLDYqngwqyetrinqvltlldldpdvtLDSLSGGWLRK 164
Cdd:cd00267 59 --------------------------DGKDIAKLPLEELRRRIGY------------------------VPQLSGGQRQR 88
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 657198994 165 VALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRG---AIVFISHDREFIHKLATRIIDLDRG 229
Cdd:cd00267 89 VALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEegrTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-231 |
5.26e-28 |
|
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: 113.21 E-value: 5.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 1 MALLTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQ-QDlkVTRLeqdPPAS- 78
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDgRD--ITGL---PPHRi 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 79 ---------------SEITVFDYAAeglagVGELLKQYHHVSHALAHDPSDAniRTMSQLQEqldyqngwqyetRINQVL 143
Cdd:COG0411 77 arlgiartfqnprlfPELTVLENVL-----VAAHARLGRGLLAALLRLPRAR--REEREARE------------RAEELL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 144 TLLDLDP--DVTLDSLSGGWLRKVALARALACDPDLLLLDEPT---NHLDIDAINWLEEFLKDFRG-AIVFISHDREFIH 217
Cdd:COG0411 138 ERVGLADraDEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAaglNPEETEELAELIRRLRDERGiTILLIEHDMDLVM 217
|
250
....*....|....
gi 657198994 218 KLATRIIDLDRGVI 231
Cdd:COG0411 218 GLADRIVVLDFGRV 231
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
319-503 |
2.30e-27 |
|
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: 109.88 E-value: 2.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 319 VFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLEVAyFDQYREQL--- 394
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLwNGEPIRDA-REDYRRRLayl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 395 ------DPEKTVVDN---VGEGKQEVMVRGRSRHILGYLQdfLfePKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILD 465
Cdd:COG4133 81 ghadglKPELTVRENlrfWAALYGLRADREAIDEALEAVG--L--AGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 657198994 466 EPTNDLDVETLELLEELLTDYP---GTLLLVSHDRRFIDNT 503
Cdd:COG4133 157 EPFTALDAAGVALLAELIAAHLargGAVLLTTHQPLELAAA 197
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-231 |
2.33e-27 |
|
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: 109.92 E-value: 2.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 4 LTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQ-QDlkVTRLeqdPPASSEI- 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDgRD--VTGV---PPERRNIg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 82 TVF-DYAAeglagvgellkqYHHVShalAHDpsdaNI------RTMSQLQEQldyqngwqyeTRINQVLTLLDLDPDVTL 154
Cdd:cd03259 76 MVFqDYAL------------FPHLT---VAE----NIafglklRGVPKAEIR----------ARVRELLELVGLEGLLNR 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 155 --DSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDA----INWLEEFLKDFRGAIVFISHDREFIHKLATRIIDLDR 228
Cdd:cd03259 127 ypHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLreelREELKELQRELGITTIYVTHDQEEALALADRIAVMNE 206
|
...
gi 657198994 229 GVI 231
Cdd:cd03259 207 GRI 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-231 |
4.02e-27 |
|
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: 115.39 E-value: 4.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 3 LLTLHGASLSF-----SDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQ-QDLKVTRLE---- 72
Cdd:COG1123 260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDgKDLTKLSRRslre 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 73 ---------QDPPAS--SEITVFDYAAEGLagvgellKQYHHVSHALAHDpsdanirtmsqlqeqldyqngwqyetRINQ 141
Cdd:COG1123 340 lrrrvqmvfQDPYSSlnPRMTVGDIIAEPL-------RLHGLLSRAERRE--------------------------RVAE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 142 VLTLLDLDPDVtLD----SLSGGWLRKVALARALACDPDLLLLDEPTNHLDI----DAINWLEEFLKDFRGAIVFISHDR 213
Cdd:COG1123 387 LLERVGLPPDL-ADryphELSGGQRQRVAIARALALEPKLLILDEPTSALDVsvqaQILNLLRDLQRELGLTYLFISHDL 465
|
250
....*....|....*...
gi 657198994 214 EFIHKLATRIIDLDRGVI 231
Cdd:COG1123 466 AVVRYIADRVAVMYDGRI 483
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
320-501 |
9.91e-27 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 107.98 E-value: 9.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 320 FETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLEVAYFDQYREQL---- 394
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYlDGKPLSAMPPPEWRRQVayvp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 395 -DP---EKTVVDNVGEGKQEVMVRGRSRHILGYLQDFLFEPKRARTPVKALSGGEKNRLLLAK-LFLKPSNLLiLDEPTN 469
Cdd:COG4619 81 qEPalwGGTVRDNLPFPFQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRaLLLQPDVLL-LDEPTS 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 657198994 470 DLDVETLELLEELLTDYP----GTLLLVSHDRRFID 501
Cdd:COG4619 160 ALDPENTRRVEELLREYLaeegRAVLWVSHDPEQIE 195
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-233 |
1.10e-26 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 107.14 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 5 TLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGrlvlqqdlkvtrleqdppassEITVF 84
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSG---------------------EILLD 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 85 dyaaeglagvGELLKQYHHvsHALAhdpsdaniRTMSQLQeqldyqngwqyetrinQVLTLLDLDP--DVTLDSLSGGWL 162
Cdd:cd03214 60 ----------GKDLASLSP--KELA--------RKIAYVP----------------QALELLGLAHlaDRPFNELSGGER 103
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 657198994 163 RKVALARALACDPDLLLLDEPTNHLDI----DAINWLEEFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITS 233
Cdd:cd03214 104 QRVLLARALAQEPPILLLDEPTSHLDIahqiELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVA 178
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-231 |
1.55e-26 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 108.63 E-value: 1.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 1 MALLTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPlddgrlvlqqdlkvtrleqdPPASSE 80
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLP--------------------PTYGND 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 81 ITVFDyaaEGLAGVG--ELLKQYHHVSHALAHD-PSDANIRTM--------SQLQEQLDYQNgwqyETRINQVLTLLDLD 149
Cdd:COG1119 61 VRLFG---ERRGGEDvwELRKRIGLVSPALQLRfPRDETVLDVvlsgffdsIGLYREPTDEQ----RERARELLELLGLA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 150 P--DVTLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDA----INWLEEFLKDFRGAIVFISHDREFIHKLATRI 223
Cdd:COG1119 134 HlaDRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGArellLALLDKLAAEGAPTLVLVTHHVEEIPPGITHV 213
|
....*...
gi 657198994 224 IDLDRGVI 231
Cdd:COG1119 214 LLLKDGRV 221
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
16-231 |
2.97e-26 |
|
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: 106.81 E-value: 2.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 16 FPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLqqdlkvtrLEQDPPASSEITVFDYAAEGlagVG 95
Cdd:cd03255 17 VQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRV--------DGTDISKLSEKELAAFRRRH---IG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 96 ELLKQYHHVSHALAHDpsdaNIRtmsqLQEQLDYQNGWQYETRINQVLTLLDLD------PDvtldSLSGGWLRKVALAR 169
Cdd:cd03255 86 FVFQSFNLLPDLTALE----NVE----LPLLLAGVPKKERRERAEELLERVGLGdrlnhyPS----ELSGGQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 657198994 170 ALACDPDLLLLDEPTNHLDIDA----INWLEEFLKDFRGAIVFISHDREFIhKLATRIIDLDRGVI 231
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSETgkevMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
330-524 |
3.12e-26 |
|
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: 113.11 E-value: 3.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRQGTNLEVAYFDQyREQLDPEKTVVDNVGEGKQ 409
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQ-EPQLDPTKTVRENVEEGVA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 410 EVmvrgrsRHILGYLQ-------------DFLFEpKRAR------------------------------TPVKALSGGEK 446
Cdd:TIGR03719 95 EI------KDALDRFNeisakyaepdadfDKLAA-EQAElqeiidaadawdldsqleiamdalrcppwdADVTKLSGGER 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 657198994 447 NRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEELLTDYPGTLLLVSHDRRFIDNtVTGcWLFEGD-GRISDYVGGYA 524
Cdd:TIGR03719 168 RRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDN-VAG-WILELDrGRGIPWEGNYS 244
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-232 |
1.25e-25 |
|
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: 103.28 E-value: 1.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 4 LTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQQDlKVTRleqdppasseitv 83
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK-EVSF------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 84 fdyaaeglagvgellkqyhhvshalaHDPSDAN---IRTMSQlqeqldyqngwqyetrinqvltlldldpdvtldsLSGG 160
Cdd:cd03216 67 --------------------------ASPRDARragIAMVYQ----------------------------------LSVG 86
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 657198994 161 WLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRG---AIVFISHDREFIHKLATRIIDLDRGVIT 232
Cdd:cd03216 87 ERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAqgvAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-229 |
1.25e-25 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 105.60 E-value: 1.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 4 LTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQ-QDlkVTRLE---------- 72
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDgED--ITGLPpheiarlgig 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 73 ---QDPPASSEITVFDYAAEGLagvgellkQYHHVSHALahdpSDANIRTMSQLQEqldyqngwqyetRINQVLTLLDLD 149
Cdd:cd03219 79 rtfQIPRLFPELTVLENVMVAA--------QARTGSGLL----LARARREEREARE------------RAEELLERVGLA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 150 P--DVTLDSLSGGWLRKVALARALACDPDLLLLDEPT---NHLDIDAI-NWLEEfLKDFRGAIVFISHDREFIHKLATRI 223
Cdd:cd03219 135 DlaDRPAGELSYGQQRRLEIARALATDPKLLLLDEPAaglNPEETEELaELIRE-LRERGITVLLVEHDMDVVMSLADRV 213
|
....*.
gi 657198994 224 IDLDRG 229
Cdd:cd03219 214 TVLDQG 219
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
330-523 |
1.94e-25 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 110.98 E-value: 1.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRQGTNLEVAYFDQyrE-QLDPEKTVVDNVGEGK 408
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQ--EpQLDPEKTVRENVEEGV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 409 QEVM-VRGRSRHI-----------------LGYLQDFL-------FEPK--RA----RTP-----VKALSGGEKNRLLLA 452
Cdd:PRK11819 96 AEVKaALDRFNEIyaayaepdadfdalaaeQGELQEIIdaadawdLDSQleIAmdalRCPpwdakVTKLSGGERRRVALC 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 657198994 453 KLFLKPSNLLILDEPTNDLDVETLELLEELLTDYPGTLLLVSHDRRFIDNtVTGcWLFEGD-GRISDYVGGY 523
Cdd:PRK11819 176 RLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDN-VAG-WILELDrGRGIPWEGNY 245
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-518 |
3.88e-25 |
|
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: 109.51 E-value: 3.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 4 LTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVI--ASELPLDDGRLVLQqdlkVTRLEQ----DPPA 77
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIYH----VALCEKcgyvERPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 78 sseitvfdYAAEGLAGVGELLKQYHhVSHALAHDPSDANI---------RTMSQLQEQLDYQN--------GWQYETRIN 140
Cdd:TIGR03269 77 --------KVGEPCPVCGGTLEPEE-VDFWNLSDKLRRRIrkriaimlqRTFALYGDDTVLDNvlealeeiGYEGKEAVG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 141 QVLTLLDLdpdVTLD--------SLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINW----LEEFLKDFRGAIVF 208
Cdd:TIGR03269 148 RAVDLIEM---VQLShrithiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLvhnaLEEAVKASGISMVL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 209 ISHDREFIHKLATRIIDLDRGVITSwPGNYDE----YLQGKEEwlrVEELKNAEfdrkLAQEEVWVRQGIKARRTRNEGR 284
Cdd:TIGR03269 225 TSHWPEVIEDLSDKAIWLENGEIKE-EGTPDEvvavFMEGVSE---VEKECEVE----VGEPIIKVRNVSKRYISVDRGV 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 285 VRALkamrmertqrrelqgkaklqldeagrsgklvfeteglgldfgdrtlfQGLDLQVLRGDKIALVGPNGCGKSTLIKL 364
Cdd:TIGR03269 297 VKAV-----------------------------------------------DNVSLEVKEGEIFGIVGTSGAGKTTLSKI 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 365 LMGQLEASRGS--VRQG------TNLEVA-----------YFDQYreQLDPEKTVVDNVGEG-----KQEVMVRgRSRHI 420
Cdd:TIGR03269 330 IAGVLEPTSGEvnVRVGdewvdmTKPGPDgrgrakryigiLHQEY--DLYPHRTVLDNLTEAiglelPDELARM-KAVIT 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 421 LGYLQdflFEPKRARTPVK----ALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD----VETLELLEELLTDYPGTLLL 492
Cdd:TIGR03269 407 LKMVG---FDEEKAEEILDkypdELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkVDVTHSILKAREEMEQTFII 483
|
570 580
....*....|....*....|....*.
gi 657198994 493 VSHDRRFIDNTVTGCWLFEgDGRISD 518
Cdd:TIGR03269 484 VSHDMDFVLDVCDRAALMR-DGKIVK 508
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-231 |
6.06e-25 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 103.07 E-value: 6.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 4 LTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGrlvlqqdlKVTRLEQDppasseitv 83
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSG--------EITFDGKS--------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 84 FDYAAEGLAGVGELLKQYHHVSHALAHDpsdaNIRTmSQLQEQLDYQngwqyetRINQVLTLLDLD--PDVTLDSLSGGW 161
Cdd:cd03268 64 YQKNIEALRRIGALIEAPGFYPNLTARE----NLRL-LARLLGIRKK-------RIDEVLDVVGLKdsAKKKVKGFSLGM 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 657198994 162 LRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFR--GAIVFI-SHDREFIHKLATRIIDLDRGVI 231
Cdd:cd03268 132 KQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRdqGITVLIsSHLLSEIQKVADRIGIINKGKL 204
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-250 |
6.93e-25 |
|
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: 103.52 E-value: 6.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 2 ALLTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGR-LVLQQDLKVTRLEQDPPASSE 80
Cdd:COG1127 4 PMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEiLVDGQDITGLSEKELYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 81 I-------------TVFDyaaeglaGVGELLKQYHHVSHALAHDpsdanirtmsqlqeqldyqngwqyetRINQVLTLLD 147
Cdd:COG1127 84 IgmlfqggalfdslTVFE-------NVAFPLREHTDLSEAEIRE--------------------------LVLEKLELVG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 148 LDPDVTL--DSLSGGWLRKVALARALACDPDLLLLDEPTNHLDI---DAINWLEEFLKDFRGA-IVFISHDREFIHKLAT 221
Cdd:COG1127 131 LPGAADKmpSELSGGMRKRVALARALALDPEILLYDEPTAGLDPitsAVIDELIRELRDELGLtSVVVTHDLDSAFAIAD 210
|
250 260
....*....|....*....|....*....
gi 657198994 222 RIIDLDRGVITsWPGNYDEYLQGKEEWLR 250
Cdd:COG1127 211 RVAVLADGKII-AEGTPEELLASDDPWVR 238
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
319-504 |
8.68e-25 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 103.63 E-value: 8.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 319 VFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLE-----VAYFDQyRE 392
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRlFGKPPRrarrrIGYVPQ-RA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 393 QLDPEK--TVvdnvgegkQEVMVRGRSRHI--------------------LGyLQDFlfepkrARTPVKALSGGEKNRLL 450
Cdd:COG1121 85 EVDWDFpiTV--------RDVVLMGRYGRRglfrrpsradreavdealerVG-LEDL------ADRPIGELSGGQQQRVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 657198994 451 LAKLFLKPSNLLILDEPTNDLDVETLELLE---ELLTDYPGTLLLVSHD----RRFIDNTV 504
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATEEALYellRELRREGKTILVVTHDlgavREYFDRVL 210
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-185 |
9.23e-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: 100.41 E-value: 9.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 19 LDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLD------DGRLVLQQDLKVTR-----LEQDPPASSEITVFDYA 87
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTegtillDGQDLTDDERKSLRkeigyVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 88 AEGLAGvgellkqyhhvsHALAHDPSDAnirtmsqlqeqldyqngwqyetRINQVLTLLDLD------PDVTLDSLSGGW 161
Cdd:pfam00005 81 RLGLLL------------KGLSKREKDA----------------------RAEEALEKLGLGdladrpVGERPGTLSGGQ 126
|
170 180
....*....|....*....|....
gi 657198994 162 LRKVALARALACDPDLLLLDEPTN 185
Cdd:pfam00005 127 RQRVAIARALLTKPKLLLLDEPTA 150
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-233 |
3.70e-24 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 100.90 E-value: 3.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 4 LTLHGASLSFS-DFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGR-LVLQQDLkvTRLEqdppaSSEI 81
Cdd:COG2884 2 IRFENVSKRYPgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQvLVNGQDL--SRLK-----RREI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 82 --------TVF-DYaaeglagvgELLKQ---YHHVSHAL-AHDPSDANIRTmsqlqeqldyqngwqyetRINQVLTLLDL 148
Cdd:COG2884 75 pylrrrigVVFqDF---------RLLPDrtvYENVALPLrVTGKSRKEIRR------------------RVREVLDLVGL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 149 D------PDVtldsLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDF--RGAIVFI-SHDREFIHKL 219
Cdd:COG2884 128 SdkakalPHE----LSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEInrRGTTVLIaTHDLELVDRM 203
|
250
....*....|....
gi 657198994 220 ATRIIDLDRGVITS 233
Cdd:COG2884 204 PKRVLELEDGRLVR 217
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-229 |
4.28e-24 |
|
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: 99.57 E-value: 4.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 4 LTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIAselplddgrlvlqqdlkvtRLEqdPPASSEITV 83
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIA-------------------GLE--EPDSGSILI 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 84 FDyaaEGLAGVGELLKqyhhvshalahdPSDANIRTMSQlqeqlDYQngwqyetrINQVLTLLDldpDVTLdSLSGGWLR 163
Cdd:cd03229 60 DG---EDLTDLEDELP------------PLRRRIGMVFQ-----DFA--------LFPHLTVLE---NIAL-GLSGGQQQ 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 164 KVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRG----AIVFISHDREFIHKLATRIIDLDRG 229
Cdd:cd03229 108 RVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAqlgiTVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-231 |
4.54e-24 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 104.02 E-value: 4.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 1 MALLTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQ-QDlkVTRLeqdPPASS 79
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDgRD--VTGL---PPEKR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 80 EI-TVF-DYA-----------AEGLagvgellkqyhhvshalahdpsdaNIRTMSQlQEQldyqngwqyETRINQVLTLL 146
Cdd:COG3842 78 NVgMVFqDYAlfphltvaenvAFGL------------------------RMRGVPK-AEI---------RARVAELLELV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 147 DLD------PDvtldSLSGGWLRKVALARALACDPDLLLLDEPTNHLD----IDAINWLEEFLKDFRGAIVFISHDRE-- 214
Cdd:COG3842 124 GLEgladryPH----QLSGGQQQRVALARALAPEPRVLLLDEPLSALDaklrEEMREELRRLQRELGITFIYVTHDQEea 199
|
250
....*....|....*..
gi 657198994 215 FIhkLATRIIDLDRGVI 231
Cdd:COG3842 200 LA--LADRIAVMNDGRI 214
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
330-539 |
8.65e-24 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 106.02 E-value: 8.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRQGTNLEVAYFDQ-------------------Y 390
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQetpalpqpaleyvidgdreY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 391 ReQLDPEKTVVDNVGEGKQEVMVRG----------RSR-----HILGYLQDFLFEPkrartpVKALSGGEKNRLLLAKLF 455
Cdd:PRK10636 92 R-QLEAQLHDANERNDGHAIATIHGkldaidawtiRSRaasllHGLGFSNEQLERP------VSDFSGGWRMRLNLAQAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 456 LKPSNLLILDEPTNDLDVETLELLEELLTDYPGTLLLVSHDRRFIDNTVTGCWLFEGDgRISDYVGGYADMMATRALQAA 535
Cdd:PRK10636 165 ICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQ-SLFEYTGNYSSFEVQRATRLA 243
|
....
gi 657198994 536 QQTA 539
Cdd:PRK10636 244 QQQA 247
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-250 |
9.63e-24 |
|
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: 100.27 E-value: 9.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 6 LHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGR-LVLQQD--------LKVTRLE---- 72
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEvLIDGEDisglseaeLYRLRRRmgml 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 73 -QDPPASSEITVFDYAAEGLagvgellkqyhhvshalahdpsdaniRTMSQLQEqldyqngWQYETRINQVLTLLDLDPD 151
Cdd:cd03261 83 fQSGALFDSLTVFENVAFPL--------------------------REHTRLSE-------EEIREIVLEKLEAVGLRGA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 152 VTL--DSLSGGWLRKVALARALACDPDLLLLDEPTNHLD---IDAINWLEEFLKDFRGA-IVFISHDREFIHKLATRIID 225
Cdd:cd03261 130 EDLypAELSGGMKKRVALARALALDPELLLYDEPTAGLDpiaSGVIDDLIRSLKKELGLtSIMVTHDLDTAFAIADRIAV 209
|
250 260
....*....|....*....|....*
gi 657198994 226 LDRGVITsWPGNYDEYLQGKEEWLR 250
Cdd:cd03261 210 LYDGKIV-AEGTPEELRASDDPLVR 233
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-231 |
1.13e-23 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 102.92 E-value: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 4 LTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIAS-ELPlDDGRLVLQ-QDLKVTRleqdPPASSEI 81
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGlETP-DSGRIVLNgRDLFTNL----PPRERRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 82 -------------TVFDYAAEGLAgvgellkqyhhvshalAHDPSDANIRTmsqlqeqldyqngwqyetrinQVLTLLDL 148
Cdd:COG1118 78 gfvfqhyalfphmTVAENIAFGLR----------------VRPPSKAEIRA---------------------RVEELLEL 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 149 dpdVTLDS--------LSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAIN----WLEEFLKDFRGAIVFISHDREFI 216
Cdd:COG1118 121 ---VQLEGladrypsqLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKelrrWLRRLHDELGGTTVFVTHDQEEA 197
|
250
....*....|....*
gi 657198994 217 HKLATRIIDLDRGVI 231
Cdd:COG1118 198 LELADRVVVMNQGRI 212
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
321-502 |
1.60e-23 |
|
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: 97.32 E-value: 1.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRqgtnlevayFDqyreqldpektv 400
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL---------ID------------ 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 401 vdnvGEGKQEVMVRGRSRHILgylqdFLFEpkrartpvkaLSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLE 480
Cdd:cd00267 60 ----GKDIAKLPLEELRRRIG-----YVPQ----------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLL 120
|
170 180
....*....|....*....|....*
gi 657198994 481 ELLTDYPG---TLLLVSHDRRFIDN 502
Cdd:cd00267 121 ELLRELAEegrTVIIVTHDPELAEL 145
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
321-473 |
1.90e-23 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 99.37 E-value: 1.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLeVAYFDQYREQ------ 393
Cdd:COG1131 2 EVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvLGEDV-ARDPAEVRRRigyvpq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 394 ---LDPEKTVVDNV-------GEGKQEVMVRgrsrhILGYLQDFLFEPkRARTPVKALSGGEKNRLLLAKLFLKPSNLLI 463
Cdd:COG1131 81 epaLYPDLTVRENLrffarlyGLPRKEARER-----IDELLELFGLTD-AADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170
....*....|
gi 657198994 464 LDEPTNDLDV 473
Cdd:COG1131 155 LDEPTSGLDP 164
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
321-515 |
4.21e-23 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 97.54 E-value: 4.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 321 ETEGLGLDFGD--RTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLEVAYFDQYREQL--- 394
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLvDGKDLTKLSLKELRRKVglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 395 --DPE-----KTVVD-------NVGEGKQEVMVRgrsrhILGYLQDFLFEPKRARtPVKALSGGEKNRLLLAK-LFLKPs 459
Cdd:cd03225 81 fqNPDdqffgPTVEEevafgleNLGLPEEEIEER-----VEEALELVGLEGLRDR-SPFTLSGGQKQRVAIAGvLAMDP- 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 657198994 460 NLLILDEPTNDLDVETLELLEELLTDYPG---TLLLVSHDRRFIDNTVTGCWLFEgDGR 515
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLE-DGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
330-516 |
1.03e-22 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 97.02 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLEVAYFDQYREQL-----DPE-----K 398
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLvDGKDITKKNLRELRRKVglvfqNPDdqlfaP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 399 TVVDNV-------GEGKQEvmVRGRSRHILGY--LQDFlfepkrARTPVKALSGGEKNRLLLAK-LFLKPSnLLILDEPT 468
Cdd:COG1122 92 TVEEDVafgpenlGLPREE--IRERVEEALELvgLEHL------ADRPPHELSGGQKQRVAIAGvLAMEPE-VLVLDEPT 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 657198994 469 NDLDVETLELLEELLTDYPG---TLLLVSHDRRFIDNTVTGCWLFEgDGRI 516
Cdd:COG1122 163 AGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVLD-DGRI 212
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
321-473 |
1.12e-22 |
|
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: 95.16 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRqgtnlevayfdqyreqldpektv 400
Cdd:cd03230 2 EVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIK----------------------- 58
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 657198994 401 VDNVGEGKQEVMVRGRsrhiLGYL--QDFLFEPKRARTPVKaLSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:cd03230 59 VLGKDIKKEPEEVKRR----IGYLpeEPSLYENLTVRENLK-LSGGMKQRLALAQALLHDPELLILDEPTSGLDP 128
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
321-496 |
1.54e-22 |
|
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: 96.06 E-value: 1.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR------QGTNLEVAYFDQyREQL 394
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvfgkplEKERKRIGYVPQ-RRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 395 DPEK--TVVDNVGEGKqevmvRGRSRHILGYLQDflfEPKRART-------------PVKALSGGEKNRLLLAKLFLKPS 459
Cdd:cd03235 80 DRDFpiSVRDVVLMGL-----YGHKGLFRRLSKA---DKAKVDEalervglseladrQIGELSGGQQQRVLLARALVQDP 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 657198994 460 NLLILDEPTNDLDVETLELLEELLTDYPG---TLLLVSHD 496
Cdd:cd03235 152 DLLLLDEPFAGVDPKTQEDIYELLRELRRegmTILVVTHD 191
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-236 |
1.72e-22 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 97.47 E-value: 1.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 1 MALLTLHGASLSF----SDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRlVLQQDLKVTRleqdpp 76
Cdd:COG1116 5 APALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGE-VLVDGKPVTG------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 77 ASSEI-------------TVFDYAAEGLAGVGellkqyhhVSHAlahdpsdanirtmsqlqeqldyqngwQYETRINQVL 143
Cdd:COG1116 78 PGPDRgvvfqepallpwlTVLDNVALGLELRG--------VPKA--------------------------ERRERARELL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 144 TLLDLDPDvtLDS----LSGGWLRKVALARALACDPDLLLLDEPTNHLdiDAI------NWLEEFLKDFRGAIVFISHD- 212
Cdd:COG1116 124 ELVGLAGF--EDAyphqLSGGMRQRVAIARALANDPEVLLMDEPFGAL--DALtrerlqDELLRLWQETGKTVLFVTHDv 199
|
250 260
....*....|....*....|....
gi 657198994 213 REFIHkLATRIIdldrgVITSWPG 236
Cdd:COG1116 200 DEAVF-LADRVV-----VLSARPG 217
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
319-473 |
2.23e-22 |
|
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: 96.65 E-value: 2.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 319 VFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLE----------VAYF 387
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLlDGRDLAslsrrelarrIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 388 DQyREQLDPEKTVvdnvgegkQEVMVRGRSRHilgylQDFLFEPKR------------------ARTPVKALSGGEKNRL 449
Cdd:COG1120 81 PQ-EPPAPFGLTV--------RELVALGRYPH-----LGLFGRPSAedreaveealertglehlADRPVDELSGGERQRV 146
|
170 180
....*....|....*....|....
gi 657198994 450 LLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLDL 170
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
16-231 |
3.03e-22 |
|
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: 96.22 E-value: 3.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 16 FPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQ-QDLKvtrlEQDPPasseitvfdyaaeglagv 94
Cdd:cd03295 14 KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDgEDIR----EQDPV------------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 95 gELLKQYHHVSHA---LAHDPSDANIRTMSQLQeqldyqnGW---QYETRINQVLTLLDLDPDVTLD----SLSGGWLRK 164
Cdd:cd03295 72 -ELRRKIGYVIQQiglFPHMTVEENIALVPKLL-------KWpkeKIRERADELLALVGLDPAEFADryphELSGGQQQR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 657198994 165 VALARALACDPDLLLLDEPTNHLD-IDAINWLEEFLK---DFRGAIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:cd03295 144 VGVARALAADPPLLLMDEPFGALDpITRDQLQEEFKRlqqELGKTIVFVTHDIDEAFRLADRIAIMKNGEI 214
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
25-473 |
4.25e-22 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 100.65 E-value: 4.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 25 TIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRL----------------VLQQDLKvtRLeqdppASSEITV----- 83
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYeeepswdevlkrfrgtELQNYFK--KL-----YNGEIKVvhkpq 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 84 -FDYAAEGLAG-VGELLKQyhhvshalahdpsdANIRTMsqlqeqldyqngwqyetrINQVLTLLDLDP--DVTLDSLSG 159
Cdd:PRK13409 168 yVDLIPKVFKGkVRELLKK--------------VDERGK------------------LDEVVERLGLENilDRDISELSG 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 160 GWLRKVALARALACDPDLLLLDEPTNHLDID----AINWLEEFLKDfrGAIVFISHDrefihkLAtrIIDL--DR----- 228
Cdd:PRK13409 216 GELQRVAIAAALLRDADFYFFDEPTSYLDIRqrlnVARLIRELAEG--KYVLVVEHD------LA--VLDYlaDNvhiay 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 229 ------GVITSWPGN---YDEYLQG--KEEWLRV--EELknaEFDrklaqeevwvrqgikarrtrnegrvralkamrmER 295
Cdd:PRK13409 286 gepgayGVVSKPKGVrvgINEYLKGylPEENMRIrpEPI---EFE---------------------------------ER 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 296 TQRRELQGKAKLqldeagrsgklvfETEGLGLDFGDRTLF--QGldlQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASR 373
Cdd:PRK13409 330 PPRDESERETLV-------------EYPDLTKKLGDFSLEveGG---EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 374 GSVrqGTNLEVAYFDQYREQlDPEKTVVD---NVGEG------KQEVMVRgrsrhilgyLQ-DFLFEpkrarTPVKALSG 443
Cdd:PRK13409 394 GEV--DPELKISYKPQYIKP-DYDGTVEDllrSITDDlgssyyKSEIIKP---------LQlERLLD-----KNVKDLSG 456
|
490 500 510
....*....|....*....|....*....|
gi 657198994 444 GEKNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK13409 457 GELQRVAIAACLSRDADLYLLDEPSAHLDV 486
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
330-495 |
4.73e-22 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 93.60 E-value: 4.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLEVAYFDQYREQLdpekTVVDnvgegk 408
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILiDGVDLRDLDLESLRKNI----AYVP------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 409 QEVmvrgrsrhilgylqdFLFEpkrarTPVKA--LSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEELLTDY 486
Cdd:cd03228 83 QDP---------------FLFS-----GTIREniLSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRAL 142
|
170
....*....|.
gi 657198994 487 PG--TLLLVSH 495
Cdd:cd03228 143 AKgkTVIVIAH 153
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
321-473 |
5.16e-22 |
|
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: 93.65 E-value: 5.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLevayfdqyrEQLDPEKt 399
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILlDGKDL---------ASLSPKE- 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 657198994 400 vvdnvgegkqevmvrgRSRHIlGYLQDFL----FEPKRARtPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:cd03214 71 ----------------LARKI-AYVPQALellgLAHLADR-PFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDI 130
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-243 |
1.47e-21 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 99.52 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 4 LTLHGASLSFSDF--PLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVL------QQDLKVTR----- 70
Cdd:COG2274 474 IELENVSFRYPGDspPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIdgidlrQIDPASLRrqigv 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 71 LEQDPpassEI---TVFDyaaeglagvgellkqyhhvshalahdpsdaNIrTMSQlqEQLDYQngwqyetRINQVLTLLD 147
Cdd:COG2274 554 VLQDV----FLfsgTIRE------------------------------NI-TLGD--PDATDE-------EIIEAARLAG 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 148 LDPDV--------TL-----DSLSGGWLRKVALARALACDPDLLLLDEPTNHLDID---AINwleEFLKDFRG--AIVFI 209
Cdd:COG2274 590 LHDFIealpmgydTVvgeggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAEteaIIL---ENLRRLLKgrTVIII 666
|
250 260 270
....*....|....*....|....*....|....
gi 657198994 210 SHDREFIhKLATRIIDLDRGVITSwPGNYDEYLQ 243
Cdd:COG2274 667 AHRLSTI-RLADRIIVLDKGRIVE-DGTHEELLA 698
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
8-231 |
1.50e-21 |
|
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: 93.94 E-value: 1.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 8 GASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIAS-ELPlDDGRLVLQ---------QDLKVTRLEQDPPA 77
Cdd:cd03296 7 NVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGlERP-DSGTILFGgedatdvpvQERNVGFVFQHYAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 78 SSEITVFDYAAEGLagvgellkqyhHVSHAlAHDPSDANIRTmsqlqeqldyqngwqyetRINQVLTLLDLD--PDVTLD 155
Cdd:cd03296 86 FRHMTVFDNVAFGL-----------RVKPR-SERPPEAEIRA------------------KVHELLKLVQLDwlADRYPA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 156 SLSGGWLRKVALARALACDPDLLLLDEPTNHLDI----DAINWLEEFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:cd03296 136 QLSGGQRQRVALARALAVEPKVLLLDEPFGALDAkvrkELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-473 |
1.68e-21 |
|
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: 98.60 E-value: 1.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 1 MALLTLHGASLSF----SDFPLLDHAELTIERGERLCLVGRNGAGKStlmkVIAselplddgrlvlqqdLKVTRLEQDPP 76
Cdd:COG4172 4 MPLLSVEDLSVAFgqggGTVEAVKGVSFDIAAGETLALVGESGSGKS----VTA---------------LSILRLLPDPA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 77 A--SSEITvfdyaaegLAGVgELLKQyhhvshalahdpSDANIRT-------------MS----------QLQEQLDYQN 131
Cdd:COG4172 65 AhpSGSIL--------FDGQ-DLLGL------------SERELRRirgnriamifqepMTslnplhtigkQIAEVLRLHR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 132 GWQYETRINQVLTLLDL----DPDVTLDS----LSGGWLRKVALARALACDPDLLLLDEPTNHLD--IDA--INWLEEFL 199
Cdd:COG4172 124 GLSGAAARARALELLERvgipDPERRLDAyphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDvtVQAqiLDLLKDLQ 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 200 KDFRGAIVFISHDREFIHKLATRIIDLDRGVItswpgnydeylqgkeewlrVEelknaefdrklaqeevwvrqgikarrt 279
Cdd:COG4172 204 RELGMALLLITHDLGVVRRFADRVAVMRQGEI-------------------VE--------------------------- 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 280 rnEGRVRAL-KAMRMERTqRRELQGKAKLQLDEAGRSGKLVFETEGLGLDF-GDRTLFQ----------GLDLQVLRGDK 347
Cdd:COG4172 238 --QGPTAELfAAPQHPYT-RKLLAAEPRGDPRPVPPDAPPLLEARDLKVWFpIKRGLFRrtvghvkavdGVSLTLRRGET 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 348 IALVGPNGCGKSTLIKLLMGqLEASRGSVR-QGTNLEVAYFDQ---YREQ-----------LDPEKTVVDNVGEG----K 408
Cdd:COG4172 315 LGLVGESGSGKSTLGLALLR-LIPSEGEIRfDGQDLDGLSRRAlrpLRRRmqvvfqdpfgsLSPRMTVGQIIAEGlrvhG 393
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 657198994 409 QEVMVRGRSRHILGYLQDFLFEPK-RARTPvKALSGGEKNRLLLAK-LFLKPSnLLILDEPTNDLDV 473
Cdd:COG4172 394 PGLSAAERRARVAEALEEVGLDPAaRHRYP-HEFSGGQRQRIAIARaLILEPK-LLVLDEPTSALDV 458
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-473 |
1.75e-21 |
|
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: 98.70 E-value: 1.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 25 TIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRL----------------VLQQDLKvtRLeqdppASSEITV----- 83
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDYdeepswdevlkrfrgtELQDYFK--KL-----ANGEIKVahkpq 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 84 -FDYAAEGLAG-VGELLKQYhhvshalahDPSDAnirtMSQLQEQLDYQNgwqyetrinqvltLLDLDpdvtLDSLSGGW 161
Cdd:COG1245 168 yVDLIPKVFKGtVRELLEKV---------DERGK----LDELAEKLGLEN-------------ILDRD----ISELSGGE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 162 LRKVALARALACDPDLLLLDEPTNHLDI-------DAINwleEFLKDFRgAIVFISHDrefihkLAtrIIDL--DRGVIT 232
Cdd:COG1245 218 LQRVAIAAALLRDADFYFFDEPSSYLDIyqrlnvaRLIR---ELAEEGK-YVLVVEHD------LA--ILDYlaDYVHIL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 233 -SWPGNY-------------DEYLQGKeewlrveelknaefdrkLAQEEVWVRQgikarrtrnegrvralKAMRMERTQR 298
Cdd:COG1245 286 yGEPGVYgvvskpksvrvgiNQYLDGY-----------------LPEENVRIRD----------------EPIEFEVHAP 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 299 RELQGKAKLqldeagrsgklvFETEGLGLDFGDRTLF--QGldlQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSV 376
Cdd:COG1245 333 RREKEEETL------------VEYPDLTKSYGGFSLEveGG---EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 377 RqgTNLEVAYFDQYREQlDPEKTVvdnvgegkqEVMVRGRSRHILG--YLQDFLFEP----KRARTPVKALSGGEKNRLL 450
Cdd:COG1245 398 D--EDLKISYKPQYISP-DYDGTV---------EEFLRSANTDDFGssYYKTEIIKPlgleKLLDKNVKDLSGGELQRVA 465
|
490 500
....*....|....*....|...
gi 657198994 451 LAKLFLKPSNLLILDEPTNDLDV 473
Cdd:COG1245 466 IAACLSRDADLYLLDEPSAHLDV 488
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
330-473 |
2.65e-21 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 97.91 E-value: 2.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLEVAYFDQYREQL-----DP---EKTV 400
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILiNGVDLSDLDPASWRRQIawvpqNPylfAGTI 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 401 VDNVGEGKQEVmvrgrSRHIL------GYLQDFLFE-PKRARTPV----KALSGGEKNRLLLAKLFLKPSNLLILDEPTN 469
Cdd:COG4988 428 RENLRLGRPDA-----SDEELeaaleaAGLDEFVAAlPDGLDTPLgeggRGLSGGQAQRLALARALLRDAPLLLLDEPTA 502
|
....
gi 657198994 470 DLDV 473
Cdd:COG4988 503 HLDA 506
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-243 |
3.65e-21 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 97.53 E-value: 3.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 2 ALLTLHGASLSF--SDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVL---------QQDL--KV 68
Cdd:COG4987 332 PSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLggvdlrdldEDDLrrRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 69 TRLEQDPPasseitVFDyaaeglAGVGELLKqyhhvshaLA-HDPSDANIRtmsqlqeqldyqngwqyetrinQVLTLLD 147
Cdd:COG4987 412 AVVPQRPH------LFD------TTLRENLR--------LArPDATDEELW----------------------AALERVG 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 148 LDPDVT-----LDS--------LSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAInwlEEFLKDFRGA-----IVFI 209
Cdd:COG4987 450 LGDWLAalpdgLDTwlgeggrrLSGGERRRLALARALLRDAPILLLDEPTEGLDAATE---QALLADLLEAlagrtVLLI 526
|
250 260 270
....*....|....*....|....*....|....
gi 657198994 210 SHDREFIHKlATRIIDLDRGVITSwPGNYDEYLQ 243
Cdd:COG4987 527 THRLAGLER-MDRILVLEDGRIVE-QGTHEELLA 558
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-243 |
4.25e-21 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 97.52 E-value: 4.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 4 LTLHGASLSFSD-FPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVL-QQDL----------KVTRL 71
Cdd:COG4988 337 IELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILInGVDLsdldpaswrrQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 72 EQDP---------------PASSEITVfdYAAEGLAGVGELLKQyhhvshalahdpsdanirtmsqLQEQLDYQNGwqyE 136
Cdd:COG4988 417 PQNPylfagtirenlrlgrPDASDEEL--EAALEAAGLDEFVAA----------------------LPDGLDTPLG---E 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 137 TRINqvltlldldpdvtldsLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKD-FRGAIV-FISHDRE 214
Cdd:COG4988 470 GGRG----------------LSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRlAKGRTViLITHRLA 533
|
250 260
....*....|....*....|....*....
gi 657198994 215 FIhKLATRIIDLDRGVITSwPGNYDEYLQ 243
Cdd:COG4988 534 LL-AQADRILVLDDGRIVE-QGTHEELLA 560
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-236 |
5.21e-21 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 91.76 E-value: 5.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 4 LTLHGASLSFSD----FPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRlVLQQDLKVTRLE------- 72
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGE-VLVDGEPVTGPGpdrgyvf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 73 QDP---PAsseITVFDYAAEGLAGVGELLKQ-YHHVSHALAhdpsdanirtMSQLQeqlDYQNGWQYEtrinqvltlldl 148
Cdd:cd03293 80 QQDallPW---LTVLDNVALGLELQGVPKAEaRERAEELLE----------LVGLS---GFENAYPHQ------------ 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 149 dpdvtldsLSGGWLRKVALARALACDPDLLLLDEPTNHLD----IDAINWLEEFLKDFRGAIVFISHD-REFIHkLATRI 223
Cdd:cd03293 132 --------LSGGMRQRVALARALAVDPDVLLLDEPFSALDaltrEQLQEELLDIWRETGKTVLLVTHDiDEAVF-LADRV 202
|
250
....*....|...
gi 657198994 224 IdldrgVITSWPG 236
Cdd:cd03293 203 V-----VLSARPG 210
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-473 |
9.39e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 95.86 E-value: 9.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 3 LLTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQQDlkvtrlEQDPPASSEit 82
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGK------PVRIRSPRD-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 83 vfdyAAEglAGVGeLLKQyhhvsH-------------ALAHDPSDANIRTMSQLQEQL-----DYQngwqyetrinqvlt 144
Cdd:COG3845 77 ----AIA--LGIG-MVHQ-----HfmlvpnltvaeniVLGLEPTKGGRLDRKAARARIrelseRYG-------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 145 lLDLDPDVTLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRG---AIVFISHD-REfIHKLA 220
Cdd:COG3845 131 -LDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAegkSIIFITHKlRE-VMAIA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 221 TRIIDLDRGVItswpgnydeylqgkeewlrVEELKNAEFD-RKLAQEEVwvrqgikarrtrneGRVRALKAMRmertqrr 299
Cdd:COG3845 209 DRVTVLRRGKV-------------------VGTVDTAETSeEELAELMV--------------GREVLLRVEK------- 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 300 elqgkaklqldEAGRSGKLVFETEGLGL--DFGDRTLfQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR 377
Cdd:COG3845 249 -----------APAEPGEVVLEVENLSVrdDRGVPAL-KDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIR 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 378 -QGTNLE-----------VAYF--DQYREQLDPEKTVVDNV--GEGKQEVMVRG---RSRHILGYLQDfLFE-----PKR 433
Cdd:COG3845 317 lDGEDITglsprerrrlgVAYIpeDRLGRGLVPDMSVAENLilGRYRRPPFSRGgflDRKAIRAFAEE-LIEefdvrTPG 395
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 657198994 434 ARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:COG3845 396 PDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDV 435
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
17-226 |
2.38e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 89.22 E-value: 2.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 17 PLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQQDLKVTRLEQ--DPPASSEITVFDYAAEGLAGV 94
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQrsEVPDSLPLTVRDLVAMGRWAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 95 GELLKQYHHVSHALAHDPSDAnirtmsqlqeqldyqngwqyetrinqvLTLLDLDpDVTLDSLSGGWLRKVALARALACD 174
Cdd:NF040873 86 RGLWRRLTRDDRAAVDDALER---------------------------VGLADLA-GRQLGELSGGQRQRALLAQGLAQE 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 657198994 175 PDLLLLDEPTNHLDIDAINWLEEFLKDFRG---AIVFISHDREFIhKLATRIIDL 226
Cdd:NF040873 138 ADLLLLDEPTTGLDAESRERIIALLAEEHArgaTVVVVTHDLELV-RRADPCVLL 191
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
330-531 |
5.48e-20 |
|
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: 94.06 E-value: 5.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLE----------VAYFDQ--------Y 390
Cdd:COG4987 346 AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITlGGVDLRdldeddlrrrIAVVPQrphlfdttL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 391 REQL---DPEKT------VVDNVGegkqevmvrgrsrhilgyLQDFLFE-PKRARTPV----KALSGGEKNRLLLAKLFL 456
Cdd:COG4987 426 RENLrlaRPDATdeelwaALERVG------------------LGDWLAAlPDGLDTWLgeggRRLSGGERRRLALARALL 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 657198994 457 KPSNLLILDEPTNDLDVETLELLEELLTDYPG--TLLLVSHDRRFIDNTVTGCWLfeGDGRISDyVGGYADMMATRA 531
Cdd:COG4987 488 RDAPILLLDEPTEGLDAATEQALLADLLEALAgrTVLLITHRLAGLERMDRILVL--EDGRIVE-QGTHEELLAQNG 561
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-233 |
5.66e-20 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 88.95 E-value: 5.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 2 ALLTLHGASLSF----SDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGR-LVLQQDlkVTRLeqdpp 76
Cdd:COG1136 3 PLLELRNLTKSYgtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEvLIDGQD--ISSL----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 77 ASSEITVF--DYaaeglagVGELLKQYHHVSHALAHDpsdaNIRTMSQLQEQldyqNGWQYETRINQVLTLLDLD----- 149
Cdd:COG1136 76 SERELARLrrRH-------IGFVFQFFNLLPELTALE----NVALPLLLAGV----SRKERRERARELLERVGLGdrldh 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 150 -PDvtldSLSGGWLRKVALARALACDPDLLLLDEPTNHLD----IDAINWLEEFLKDFRGAIVFISHDREFIhKLATRII 224
Cdd:COG1136 141 rPS----QLSGGQQQRVAIARALVNRPKLILADEPTGNLDsktgEEVLELLRELNRELGTTIVMVTHDPELA-ARADRVI 215
|
....*....
gi 657198994 225 DLDRGVITS 233
Cdd:COG1136 216 RLRDGRIVS 224
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-231 |
7.02e-20 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 91.67 E-value: 7.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 1 MALLTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLqQDLKVTRLeqdPPASSE 80
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILI-GGRDVTDL---PPKDRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 81 IT-VF-DYA-------AEGLA-GvgelLKqyhhvshalahdpsdanIRTMSQlQEQldyqngwqyETRINQVLTLLDLDP 150
Cdd:COG3839 77 IAmVFqSYAlyphmtvYENIAfP----LK-----------------LRKVPK-AEI---------DRRVREAAELLGLED 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 151 dvTLD----SLSGGWLRKVALARALACDPDLLLLDEPTNHLD----IDAINWLEEFLKDFRGAIVFISHDREFIHKLATR 222
Cdd:COG3839 126 --LLDrkpkQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDaklrVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADR 203
|
....*....
gi 657198994 223 IIDLDRGVI 231
Cdd:COG3839 204 IAVMNDGRI 212
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
14-231 |
7.87e-20 |
|
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: 88.79 E-value: 7.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 14 SDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVI-ASELPlDDGRLVLQ-QDLKVTRLEQDPPASSEI-TVFDYAaeg 90
Cdd:cd03258 16 GKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCInGLERP-TSGSVLVDgTDLTLLSGKELRKARRRIgMIFQHF--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 91 lagvgELLKQ---YHHVSHALahdpsdanirtmsqlqeQLDYQNGWQYETRINQVLTLLDLD--PDVTLDSLSGGWLRKV 165
Cdd:cd03258 92 -----NLLSSrtvFENVALPL-----------------EIAGVPKAEIEERVLELLELVGLEdkADAYPAQLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 166 ALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKD----FRGAIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:cd03258 150 GIARALANNPKVLLCDEATSALDPETTQSILALLRDinreLGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
280-497 |
1.40e-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: 92.35 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 280 RNEGRVRALKAMRMERTQRRELQGKAKLqldEAGRSGKLVFEteGLGLDFGDRT-LFQGLDLQVLRGDKIALVGPNGCGK 358
Cdd:TIGR02857 287 RADGVAAAEALFAVLDAAPRPLAGKAPV---TAAPASSLEFS--GVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGK 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 359 STLIKLLMGQLEASRGSVR-QGTNLEVAYFDQYREQLD--------PEKTVVDNVGEGKQEV---MVRGRSRhiLGYLQD 426
Cdd:TIGR02857 362 STLLNLLLGFVDPTEGSIAvNGVPLADADADSWRDQIAwvpqhpflFAGTIAENIRLARPDAsdaEIREALE--RAGLDE 439
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 657198994 427 FLFE-PKRARTPV----KALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEELLTDYPG--TLLLVSHDR 497
Cdd:TIGR02857 440 FVAAlPQGLDTPIgeggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVTHRL 517
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-231 |
2.41e-19 |
|
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: 86.93 E-value: 2.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 4 LTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQqDLKVTRLeqdPPASSEI-- 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIG-GRDVTDL---PPKDRDIam 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 82 -----------TVFDYAAEGLAgvgellkqyhhvshaLAHDPSDANIRTMSQLQEQLdyqngwqyetrinQVLTLLDLDP 150
Cdd:cd03301 77 vfqnyalyphmTVYDNIAFGLK---------------LRKVPKDEIDERVREVAELL-------------QIEHLLDRKP 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 151 DvtldSLSGGWLRKVALARALACDPDLLLLDEPTNHLD----IDAINWLEEFLKDFRGAIVFISHDREFIHKLATRIIDL 226
Cdd:cd03301 129 K----QLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVM 204
|
....*
gi 657198994 227 DRGVI 231
Cdd:cd03301 205 NDGQI 209
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
19-231 |
2.70e-19 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 87.04 E-value: 2.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 19 LDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQQdlkvTRLEQDPPASSEITVFDYAAEGLagvgell 98
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG----FDVVKEPAEARRRLGFVSDSTGL------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 99 kqYHHVShalahdpsdanIRTMSQLQEQLDYQNGWQYETRINQVLTLLDLDP--DVTLDSLSGGWLRKVALARALACDPD 176
Cdd:cd03266 90 --YDRLT-----------ARENLEYFAGLYGLKGDELTARLEELADRLGMEEllDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 657198994 177 LLLLDEPTNHLDIDAINWLEEFLKDFRG---AIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQLRAlgkCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
323-467 |
4.35e-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: 87.45 E-value: 4.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 323 EGLGLDF----GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR------QGTNLEVAY-FDQYR 391
Cdd:COG1116 11 RGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLvdgkpvTGPGPDRGVvFQEPA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 392 eqLDPEKTVVDNV-------GEGKQEvmVRGRSRHIL---GyLQDFlfepkRARTPvKALSGGEKNRLLLAK-LFLKPSn 460
Cdd:COG1116 91 --LLPWLTVLDNValglelrGVPKAE--RRERARELLelvG-LAGF-----EDAYP-HQLSGGMRQRVAIARaLANDPE- 158
|
....*..
gi 657198994 461 LLILDEP 467
Cdd:COG1116 159 VLLMDEP 165
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
329-472 |
4.51e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 85.36 E-value: 4.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 329 FGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRQGTNLEVAYFDQyREQLDPE--KTVVDNVGE 406
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQ-RSEVPDSlpLTVRDLVAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 407 GK-QEvmvRGRSRHI--------------LGyLQDFlfepkrARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDL 471
Cdd:NF040873 81 GRwAR---RGLWRRLtrddraavddalerVG-LADL------AGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
.
gi 657198994 472 D 472
Cdd:NF040873 151 D 151
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
321-500 |
5.60e-19 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 85.77 E-value: 5.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 321 ETEGLGLDFGDRT-LFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-------QGTNLEVAYF---DQ 389
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILlngkpikAKERRKSIGYvmqDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 390 YReQLDpEKTVVDNVGEGKQEV-MVRGRSRHIlgyLQDF-LFEPKRaRTPvKALSGGEKNRLLLAKLFLKPSNLLILDEP 467
Cdd:cd03226 81 DY-QLF-TDSVREELLLGLKELdAGNEQAETV---LKDLdLYALKE-RHP-LSLSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
170 180 190
....*....|....*....|....*....|....*.
gi 657198994 468 TNDLDVETLELLEELLTDYPG---TLLLVSHDRRFI 500
Cdd:cd03226 154 TSGLDYKNMERVGELIRELAAqgkAVIVITHDYEFL 189
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
321-473 |
7.82e-19 |
|
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: 86.06 E-value: 7.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNL---------EVAYFDQY 390
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILiDGEDVrkeprearrQIGVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 391 REqLDPEKTVVDNV-------GEGKQEVMVRgrsrhILGYLQDFLFEPKRARtPVKALSGGEKNRLLLAKLFLKPSNLLI 463
Cdd:COG4555 83 RG-LYDRLTVRENIryfaelyGLFDEELKKR-----IEELIELLGLEEFLDR-RVGELSTGMKKKVALARALVHDPKVLL 155
|
170
....*....|
gi 657198994 464 LDEPTNDLDV 473
Cdd:COG4555 156 LDEPTNGLDV 165
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-235 |
1.01e-18 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 85.31 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 4 LTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIA------SELPLD-----DGRLVLQQDLKVTRLE 72
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNrlndliPGAPDEgevllDGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 73 -------QDP---PASseitVFDYAAEGLAGVGELLKqyhhvshalahdpsdanirtmsqlqEQLDYqngwqyetRINQV 142
Cdd:cd03260 81 rrvgmvfQKPnpfPGS----IYDNVAYGLRLHGIKLK-------------------------EELDE--------RVEEA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 143 LTLLDLDPDV----TLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRG--AIVFISHDREFI 216
Cdd:cd03260 124 LRKAALWDEVkdrlHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKeyTIVIVTHNMQQA 203
|
250 260
....*....|....*....|
gi 657198994 217 HKLATRIIDLDRG-VITSWP 235
Cdd:cd03260 204 ARVADRTAFLLNGrLVEFGP 223
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
323-496 |
1.47e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 85.88 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 323 EGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRQGTnlevAYFDQYRE---------Q 393
Cdd:PRK11247 16 NAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGT----APLAEAREdtrlmfqdaR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 394 LDPEKTVVDNVGEGkqevmVRGRSR-HILGYLQDFLFEPKRARTPVkALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:PRK11247 92 LLPWKKVIDNVGLG-----LKGQWRdAALQALAAVGLADRANEWPA-ALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
170 180
....*....|....*....|....*...
gi 657198994 473 ----VETLELLEELLTDYPGTLLLVSHD 496
Cdd:PRK11247 166 altrIEMQDLIESLWQQHGFTVLLVTHD 193
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
321-472 |
1.48e-18 |
|
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: 84.83 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 321 ETEGLGLDFGDR----TLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR------QGTNLEVAY-FDQ 389
Cdd:cd03293 2 EVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLvdgepvTGPGPDRGYvFQQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 390 YReqLDPEKTVVDNV-------GEGKQEvmVRGRSRHIL---GyLQDFlfepkRARTPvKALSGGEKNRLLLAKLFLKPS 459
Cdd:cd03293 82 DA--LLPWLTVLDNValglelqGVPKAE--ARERAEELLelvG-LSGF-----ENAYP-HQLSGGMRQRVALARALAVDP 150
|
170
....*....|...
gi 657198994 460 NLLILDEPTNDLD 472
Cdd:cd03293 151 DVLLLDEPFSALD 163
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
11-229 |
1.58e-18 |
|
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: 83.20 E-value: 1.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 11 LSFS----DFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGR-LVLQQDLKvtrleqdppassEITVFD 85
Cdd:cd03228 6 VSFSypgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEiLIDGVDLR------------DLDLES 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 86 YaaeglagvgellkqYHHVSHAlahdPSDANIRTMSqLQEQLdyqngwqyetrinqvltlldldpdvtldsLSGGWLRKV 165
Cdd:cd03228 74 L--------------RKNIAYV----PQDPFLFSGT-IRENI-----------------------------LSGGQRQRI 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 657198994 166 ALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRG--AIVFISHDREFIhKLATRIIDLDRG 229
Cdd:cd03228 106 AIARALLRDPPILILDEATSALDPETEALILEALRALAKgkTVIVIAHRLSTI-RDADRIIVLDDG 170
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
15-231 |
1.86e-18 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 84.38 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 15 DFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIAS-ELPLDDGRLVLQQDL------KVTRLE-------QDPPASSE 80
Cdd:cd03292 13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKeELPTSGTIRVNGQDVsdlrgrAIPYLRrkigvvfQDFRLLPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 81 ITVFDYAAEGLAGVGellkqyhhvshalaHDPSDANIRTMSqlqeqldyqngwqyetrinqVLTLLDLD--PDVTLDSLS 158
Cdd:cd03292 93 RNVYENVAFALEVTG--------------VPPREIRKRVPA--------------------ALELVGLShkHRALPAELS 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 657198994 159 GGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDF--RGAIVFIS-HDREFIHKLATRIIDLDRGVI 231
Cdd:cd03292 139 GGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKInkAGTTVVVAtHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-232 |
8.99e-18 |
|
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: 82.30 E-value: 8.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 5 TLHGASLSFSDFP-LLDHAELTIERGERLCLVGRNGAGKSTLMKVIASelplddgrlvLQQDLKVTRLEQDPPASSeitv 83
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAG----------LIKESSGSILLNGKPIKA---- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 84 fdyaaeglagvGELLKQYHHVSHalahDPSDanIRTMSQLQEQLDY--QNGWQYETRINQVLTLLDLD--PDVTLDSLSG 159
Cdd:cd03226 67 -----------KERRKSIGYVMQ----DVDY--QLFTDSVREELLLglKELDAGNEQAETVLKDLDLYalKERHPLSLSG 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 657198994 160 GWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRG---AIVFISHDREFIHKLATRIIDLDRGVIT 232
Cdd:cd03226 130 GQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAqgkAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
4-191 |
9.30e-18 |
|
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: 83.33 E-value: 9.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 4 LTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVL-----------QQDLKVTRLE 72
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLagvdlhglsrrARARRVALVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 73 QDPPASSEITVFDYAAeglagvgelLKQYHHVSHALAHDPSDANIrtmsqlqeqldyqngwqyetrINQVLTLLDLD--P 150
Cdd:TIGR03873 82 QDSDTAVPLTVRDVVA---------LGRIPHRSLWAGDSPHDAAV---------------------VDRALARTELShlA 131
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 657198994 151 DVTLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDA 191
Cdd:TIGR03873 132 DRDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDVRA 172
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-224 |
9.50e-18 |
|
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: 84.72 E-value: 9.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 3 LLTLHGASLSFS----DFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELP---LDDGRLVLQ-QDLkvtrLEQD 74
Cdd:COG0444 1 LLEVRNLKVYFPtrrgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDgEDL----LKLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 75 PPASSEIT------VFdyaaeglagvgellkQyhhvshalahDPSDA-N----IRTmsQLQEQLDYQNGWQYETRINQVL 143
Cdd:COG0444 77 EKELRKIRgreiqmIF---------------Q----------DPMTSlNpvmtVGD--QIAEPLRIHGGLSKAEARERAI 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 144 TLLDL----DPDVTLDS----LSGGWLRKVALARALACDPDLLLLDEPTNHLDI----DAINWLEEFLKDFRGAIVFISH 211
Cdd:COG0444 130 ELLERvglpDPERRLDRypheLSGGMRQRVMIARALALEPKLLIADEPTTALDVtiqaQILNLLKDLQRELGLAILFITH 209
|
250
....*....|...
gi 657198994 212 DREFIHKLATRII 224
Cdd:COG0444 210 DLGVVAEIADRVA 222
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-231 |
1.00e-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: 83.00 E-value: 1.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 4 LTLHGASLSF-SDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIaselplddGRLVlqqdlkvtrleqdPPASSEIT 82
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCL--------NGLV-------------EPTSGSVL 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 83 VFDYAAEGLAGvGELLKQYHHV-----SHALahdpsdanIRTMSQLQE----QLDYQNGWQ------YETRINQVLTLLD 147
Cdd:cd03256 60 IDGTDINKLKG-KALRQLRRQIgmifqQFNL--------IERLSVLENvlsgRLGRRSTWRslfglfPKEEKQRALAALE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 148 ---LDPDVTL--DSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDF---RGAIVFIS-HDREFIHK 218
Cdd:cd03256 131 rvgLLDKAYQraDQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInreEGITVIVSlHQVDLARE 210
|
250
....*....|...
gi 657198994 219 LATRIIDLDRGVI 231
Cdd:cd03256 211 YADRIVGLKDGRI 223
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-229 |
1.07e-17 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 82.24 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 4 LTLHGASLSFSDFPLLDHAELTIERGeRLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQ-QDLKVTR---------LEQ 73
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDgQDVLKQPqklrrrigyLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 74 DPPASSEITVFDyaaeglagvgellkqyhHVSH-ALAHDPSDANIRTmsqlqeqldyqngwqyetRINQVLTLLDLDP-- 150
Cdd:cd03264 80 EFGVYPNFTVRE-----------------FLDYiAWLKGIPSKEVKA------------------RVDEVLELVNLGDra 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 151 DVTLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDF-RGAIVFIS-HDREFIHKLATRIIDLDR 228
Cdd:cd03264 125 KKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELgEDRIVILStHIVEDVESLCNQVAVLNK 204
|
.
gi 657198994 229 G 229
Cdd:cd03264 205 G 205
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-225 |
1.14e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 85.66 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 1 MALLTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQQD-------LKVTRLEQ 73
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDdvealsaRAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 74 DPPASSEITvFDYAAEGLAGVGellkQYHHVSHALAHDPSDANIrtmsqlqeqldyqngwqYETRINQVLTLLDLDPDVT 153
Cdd:PRK09536 81 SVPQDTSLS-FEFDVRQVVEMG----RTPHRSRFDTWTETDRAA-----------------VERAMERTGVAQFADRPVT 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 657198994 154 ldSLSGGWLRKVALARALACDPDLLLLDEPTNHLDID-AINWLE---EFLKDFRGAIVFIsHDREfihkLATRIID 225
Cdd:PRK09536 139 --SLSGGERQRVLLARALAQATPVLLLDEPTASLDINhQVRTLElvrRLVDDGKTAVAAI-HDLD----LAARYCD 207
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
321-497 |
1.50e-17 |
|
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: 81.80 E-value: 1.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNL--------EVAY-FDQY 390
Cdd:cd03259 2 ELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILiDGRDVtgvpperrNIGMvFQDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 391 ReqLDPEKTVVDNVG-----EGKQEVMVRGRSRHILGYLQDFLFEPKRARTpvkaLSGGEKNRLLLAK-LFLKPSnLLIL 464
Cdd:cd03259 82 A--LFPHLTVAENIAfglklRGVPKAEIRARVRELLELVGLEGLLNRYPHE----LSGGQQQRVALARaLAREPS-LLLL 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 657198994 465 DEPTNDLDVETLELLEELLTDYPG----TLLLVSHDR 497
Cdd:cd03259 155 DEPLSALDAKLREELREELKELQRelgiTTIYVTHDQ 191
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
321-501 |
1.55e-17 |
|
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: 82.54 E-value: 1.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 321 ETEGLGLDFG----DRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLEVAY--------- 386
Cdd:COG1124 3 EVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTfDGRPVTRRRrkafrrrvq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 387 --FDQYREQLDPEKTVVDNVGE-----GKQEVMVR-GRSRHILGYLQDFLFepkraRTPvKALSGGEKNRLLLAK-LFLK 457
Cdd:COG1124 83 mvFQDPYASLHPRHTVDRILAEplrihGLPDREERiAELLEQVGLPPSFLD-----RYP-HQLSGGQRQRVAIARaLILE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 657198994 458 PSnLLILDEPTNDLDVETLEL----LEELLTDYPGTLLLVSHDRRFID 501
Cdd:COG1124 157 PE-LLLLDEPTSALDVSVQAEilnlLKDLREERGLTYLFVSHDLAVVA 203
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-249 |
1.77e-17 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 86.38 E-value: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 3 LLTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQQDLKVTRLEQdppasseit 82
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQ--------- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 83 vfdyaaeglagvgellkqyHHVSHALAHD-PSDANIRTMSQLQEQ--LDYQNGWQYETrinqvltllDLDPDVTlDSLSG 159
Cdd:PRK10636 383 -------------------HQLEFLRADEsPLQHLARLAPQELEQklRDYLGGFGFQG---------DKVTEET-RRFSG 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 160 GWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITSWPGNYD 239
Cdd:PRK10636 434 GEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLE 513
|
250
....*....|
gi 657198994 240 EYLQgkeeWL 249
Cdd:PRK10636 514 DYQQ----WL 519
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
13-232 |
2.24e-17 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 81.61 E-value: 2.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 13 FSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASelplddgrlVLQqdlkvtrleqdpPASSEITV-----FDYA 87
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSG---------LLQ------------PTSGEVRVaglvpWKRR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 88 AEGLAGVGELLKQYHHVSHALAHDPSDANIRTMSQLQEQldyqngwQYETRINQVLTLLDLDP--DVTLDSLSGGWLRKV 165
Cdd:cd03267 90 KKFLRRIGVVFGQKTQLWWDLPVIDSFYLLAAIYDLPPA-------RFKKRLDELSELLDLEEllDTPVRQLSLGQRMRA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 657198994 166 ALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDF---RGAIVFI-SHDREFIHKLATRIIDLDRGVIT 232
Cdd:cd03267 163 EIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnreRGTTVLLtSHYMKDIEALARRVLVIDKGRLL 233
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
321-495 |
2.49e-17 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 81.11 E-value: 2.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVrqgTNLEVAYFDQY---------- 390
Cdd:cd03268 2 KTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEI---TFDGKSYQKNIealrrigali 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 391 -REQLDPEKTVVDNVGEGKQEVMVRgRSRH--ILGY--LQDflfepkRARTPVKALSGGEKNRLLLAKLFLKPSNLLILD 465
Cdd:cd03268 79 eAPGFYPNLTARENLRLLARLLGIR-KKRIdeVLDVvgLKD------SAKKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190
....*....|....*....|....*....|...
gi 657198994 466 EPTNDLD---VETLELLEELLTDYPGTLLLVSH 495
Cdd:cd03268 152 EPTNGLDpdgIKELRELILSLRDQGITVLISSH 184
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
331-472 |
3.05e-17 |
|
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: 79.66 E-value: 3.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 331 DRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRQGTNLEVAYFDQYREQLdpekTVVDnvgegkQE 410
Cdd:cd03247 14 EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLI----SVLN------QR 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 657198994 411 VmvrgrsrhilgylqdFLFEPKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:cd03247 84 P---------------YLFDTTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLD 130
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
321-496 |
3.37e-17 |
|
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: 81.01 E-value: 3.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 321 ETEGLGLDFGDRTLF----QGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNL------------- 382
Cdd:cd03257 3 EVKNLSVSFPTGGGSvkalDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIfDGKDLlklsrrlrkirrk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 383 EVAY-FDQYREQLDPEKTVVDNVGEG--KQEVMVRGRSRHILGYLQDFLFEPKRA---RTPVkALSGGEKNRLLLAK-LF 455
Cdd:cd03257 83 EIQMvFQDPMSSLNPRMTIGEQIAEPlrIHGKLSKKEARKEAVLLLLVGVGLPEEvlnRYPH-ELSGGQRQRVAIARaLA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 657198994 456 LKPSnLLILDEPTNDLDVETLELLEELLTD----YPGTLLLVSHD 496
Cdd:cd03257 162 LNPK-LLIADEPTSALDVSVQAQILDLLKKlqeeLGLTLLFITHD 205
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-231 |
3.92e-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: 81.13 E-value: 3.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 4 LTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQqDLKVTRLeqdPPASSEI-T 82
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLD-GKDITNL---PPHKRPVnT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 83 VFDyaaeglagvgellkqyhhvSHAL-AHDPSDANIR---TMSQLQEQldyqngwQYETRINQVLTLLDLD--PDVTLDS 156
Cdd:cd03300 77 VFQ-------------------NYALfPHLTVFENIAfglRLKKLPKA-------EIKERVAEALDLVQLEgyANRKPSQ 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 657198994 157 LSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRGAI----VFISHDREFIHKLATRIIDLDRGVI 231
Cdd:cd03300 131 LSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELgitfVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
330-472 |
3.98e-17 |
|
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: 85.27 E-value: 3.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLevAYFD--QYREQL-----DPE---K 398
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILiDGIDL--RQIDpaSLRRQIgvvlqDVFlfsG 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 399 TVVDNVGEGK-----QEVMvrgRSRHILGyLQDFLFE-PKRARTPV----KALSGGEKNRLLLAKLFLKPSNLLILDEPT 468
Cdd:COG2274 564 TIRENITLGDpdatdEEII---EAARLAG-LHDFIEAlPMGYDTVVgeggSNLSGGQRQRLAIARALLRNPRILILDEAT 639
|
....
gi 657198994 469 NDLD 472
Cdd:COG2274 640 SALD 643
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
12-231 |
4.22e-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: 80.27 E-value: 4.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 12 SFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQqDLKVTrleQDPPASSEITvfdyaaegl 91
Cdd:cd03262 9 SFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIID-GLKLT---DDKKNINELR--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 92 AGVGELLKQYHHVSHALAHDpsdaNIrTMSQLQEQldyqnGWQYETRINQVLTLLDldpDVTLD--------SLSGGWLR 163
Cdd:cd03262 76 QKVGMVFQQFNLFPHLTVLE----NI-TLAPIKVK-----GMSKAEAEERALELLE---KVGLAdkadaypaQLSGGQQQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 657198994 164 KVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDF--RG-AIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:cd03262 143 RVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLaeEGmTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-473 |
5.33e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 84.33 E-value: 5.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 3 LLTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRL------------VLQQDLKVTR 70
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLeiggnpcarltpAKAHQLGIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 71 LEQDPPASSEITVFDYAAEGLAGvgellkqyhhvshalahdpSDANIRTMSQLQEQLDYQngwqyetrinqvltlldLDP 150
Cdd:PRK15439 91 VPQEPLLFPNLSVKENILFGLPK-------------------RQASMQKMKQLLAALGCQ-----------------LDL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 151 DVTLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRG---AIVFISHDREFIHKLATRIIDLD 227
Cdd:PRK15439 135 DSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAqgvGIVFISHKLPEIRQLADRISVMR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 228 RGVITswpgnydeyLQGKEEWLRVEELKNAefdrklaqeevwvrqgiKARRTRNEGRVRALKA-MRMERTQRRELQGKAK 306
Cdd:PRK15439 215 DGTIA---------LSGKTADLSTDDIIQA-----------------ITPAAREKSLSASQKLwLELPGNRRQQAAGAPV 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 307 LQLDEagrsgklvFETEGlgldfgdrtlFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMG------------QLEASRG 374
Cdd:PRK15439 269 LTVED--------LTGEG----------FRNISLEVRAGEILGLAGVVGAGRTELAETLYGlrparggrimlnGKEINAL 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 375 SVRQGTNLEVAYFDQYREQ----LDPEKT------VVDNVG---EGKQEVMVRGRSRHILGylqdflFEPKRARTPVKAL 441
Cdd:PRK15439 331 STAQRLARGLVYLPEDRQSsglyLDAPLAwnvcalTHNRRGfwiKPARENAVLERYRRALN------IKFNHAEQAARTL 404
|
490 500 510
....*....|....*....|....*....|..
gi 657198994 442 SGGEKNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK15439 405 SGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
29-229 |
5.74e-17 |
|
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: 80.03 E-value: 5.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 29 GERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQ-QDLKVTRLEQDPPASSEitvfdyaaeglaGVGELLKQYHHVSHA 107
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNgTVLFDSRKKINLPPQQR------------KIGLVFQQYALFPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 108 lahdpsdaNIRtmSQLQEQLDYQNGWQYETRINQVLTLLDLDP--DVTLDSLSGGWLRKVALARALACDPDLLLLDEPTN 185
Cdd:cd03297 91 --------NVR--ENLAFGLKRKRNREDRISVDELLDLLGLDHllNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 657198994 186 HLD----IDAINWLEEFLKDFRGAIVFISHDREFIHKLATRIIDLDRG 229
Cdd:cd03297 161 ALDralrLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDG 208
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
321-472 |
6.48e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 81.78 E-value: 6.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR----------QGTNLEVAYFDQY 390
Cdd:PRK13537 9 DFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISlcgepvpsraRHARQRVGVVPQF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 391 rEQLDPEKTVVDNVGE-GKQEVMVRGRSRHILGYLQDFLFEPKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTN 469
Cdd:PRK13537 89 -DNLDPDFTVRENLLVfGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTT 167
|
...
gi 657198994 470 DLD 472
Cdd:PRK13537 168 GLD 170
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
336-499 |
6.97e-17 |
|
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: 79.84 E-value: 6.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 336 QGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNL--------------EVAY-FDQYreQLDPEKT 399
Cdd:cd03255 21 KGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRvDGTDIsklsekelaafrrrHIGFvFQSF--NLLPDLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 400 VVDNV-------GEGKQEvmVRGRSRHILGYLQdfLfePKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:cd03255 99 ALENVelplllaGVPKKE--RRERAEELLERVG--L--GDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLD 172
|
170 180 190
....*....|....*....|....*....|.
gi 657198994 473 VETLEL----LEELLTDYPGTLLLVSHDRRF 499
Cdd:cd03255 173 SETGKEvmelLRELNKEAGTTIVVVTHDPEL 203
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
336-472 |
7.18e-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: 79.86 E-value: 7.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 336 QGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRG-------SVRQGTNL---EVAYFDQYReQLDPEKTVVDNVg 405
Cdd:cd03263 19 DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGtayingySIRTDRKAarqSLGYCPQFD-ALFDELTVREHL- 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 657198994 406 egKQEVMVRGRSRH-----ILGYLQDFLFEPKRARtPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:cd03263 97 --RFYARLKGLPKSeikeeVELLLRVLGLTDKANK-RARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLD 165
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
6-243 |
7.39e-17 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 80.52 E-value: 7.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 6 LHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGrlvlqqDLKVTRLEQDPPASSEITVFD 85
Cdd:PRK09493 4 FKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSG------DLIVDGLKVNDPKVDERLIRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 86 YAaeglagvGELLKQYHHVSH--AL---AHDPsdANIRTMSQLQEQldyqngwqyetriNQVLTLLDldpDVTLDS---- 156
Cdd:PRK09493 78 EA-------GMVFQQFYLFPHltALenvMFGP--LRVRGASKEEAE-------------KQARELLA---KVGLAErahh 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 157 ----LSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAinwLEEFLKDFRG------AIVFISHDREFIHKLATRIIDL 226
Cdd:PRK09493 133 ypseLSGGQQQRVAIARALAVKPKLMLFDEPTSALDPEL---RHEVLKVMQDlaeegmTMVIVTHEIGFAEKVASRLIFI 209
|
250
....*....|....*..
gi 657198994 227 DRGVITSwPGNYDEYLQ 243
Cdd:PRK09493 210 DKGRIAE-DGDPQVLIK 225
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
320-473 |
8.69e-17 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 78.41 E-value: 8.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 320 FETEGLGLDFGD--RTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLEVAYFDQYREQldp 396
Cdd:cd03246 1 LEVENVSFRYPGaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRlDGADISQWDPNELGDH--- 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 657198994 397 ektvvdnvgegkqevmvrgrsrhiLGYL-QDF-LFEPKRARTpvkALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:cd03246 78 ------------------------VGYLpQDDeLFSGSIAEN---ILSGGQRQRLGLARALYGNPRILVLDEPNSHLDV 129
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-189 |
9.05e-17 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 80.54 E-value: 9.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 3 LLTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQQdlkvTRLEQDPPA----- 77
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNG----RPLAAWSPWelarr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 78 ------SSEITvFDYAAEGLAGVGellkqyhhvshALAHDPSDANIRtmsqlqeqldyqngwqyeTRINQVLTLLDLDP- 150
Cdd:COG4559 77 ravlpqHSSLA-FPFTVEEVVALG-----------RAPHGSSAAQDR------------------QIVREALALVGLAHl 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 657198994 151 ---DVTldSLSGGWLRKVALARALA-----CDPD--LLLLDEPTNHLDI 189
Cdd:COG4559 127 agrSYQ--TLSGGEQQRVQLARVLAqlwepVDGGprWLFLDEPTSALDL 173
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-257 |
9.75e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 81.31 E-value: 9.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 4 LTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLvlqqdlkvtRLEQDPPASSEITV 83
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEV---------LWDGEPLDPEDRRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 84 FDYAAE--GL---AGVGELLK---QYHHVShalahdPSDAnirtmsqlQEQLDYqngWqyetrinqvLTLLDLDP--DVT 153
Cdd:COG4152 73 IGYLPEerGLypkMKVGEQLVylaRLKGLS------KAEA--------KRRADE---W---------LERLGLGDraNKK 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 154 LDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFR--GA-IVFISHDREFIHKLATRIIDLDRGV 230
Cdd:COG4152 127 VEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAakGTtVIFSSHQMELVEELCDRIVIINKGR 206
|
250 260
....*....|....*....|....*..
gi 657198994 231 ITswpgnydeyLQGKeewlrVEELKNA 257
Cdd:COG4152 207 KV---------LSGS-----VDEIRRQ 219
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
319-473 |
1.01e-16 |
|
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: 80.13 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 319 VFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSV-------RQGTNLE-----VAY 386
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDvrlfgerRGGEDVWelrkrIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 387 F-----DQYREQLDPEKTVV----DNVGEGKQ--EVMvRGRSRHILGYLQdflFEPKRARtPVKALSGGEKNRLLLAKLF 455
Cdd:COG1119 83 VspalqLRFPRDETVLDVVLsgffDSIGLYREptDEQ-RERARELLELLG---LAHLADR-PFGTLSQGEQRRVLIARAL 157
|
170
....*....|....*...
gi 657198994 456 LKPSNLLILDEPTNDLDV 473
Cdd:COG1119 158 VKDPELLILDEPTAGLDL 175
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
17-231 |
1.04e-16 |
|
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: 80.62 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 17 PLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASelplddgrlvlqqdlkvtrLEQdpPASSEITvfdYAAEGLAGV-G 95
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLG-------------------LEK--PAQGTVS---FRGQDLYQLdR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 96 ELLKQYHHVSHALAHD-PSDANIR-----TMSQLQEQLDYQNGWQYETRINQVLTLLDLDPDVtLD----SLSGGWLRKV 165
Cdd:TIGR02769 81 KQRRAFRRDVQLVFQDsPSAVNPRmtvrqIIGEPLRHLTSLDESEQKARIAELLDMVGLRSED-ADklprQLSGGQLQRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 166 ALARALACDPDLLLLDEPTNHLDI----DAINWLEEFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:TIGR02769 160 NIARALAVKPKLIVLDEAVSNLDMvlqaVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
17-231 |
2.16e-16 |
|
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: 78.40 E-value: 2.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 17 PLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVL------QQDLKVTR-----LEQDP---------- 75
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLdgtdirQLDPADLRrnigyVPQDVtlfygtlrdn 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 76 -----PASSEITVFDyAAEgLAGVGELLKQyhhvsHALAHDpsdanirtmSQLQEQldyqnGwqyetrinqvltlldldp 150
Cdd:cd03245 98 itlgaPLADDERILR-AAE-LAGVTDFVNK-----HPNGLD---------LQIGER-----G------------------ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 151 dvtlDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRG--AIVFISHdREFIHKLATRIIDLDR 228
Cdd:cd03245 139 ----RGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITH-RPSLLDLVDRIIVMDS 213
|
...
gi 657198994 229 GVI 231
Cdd:cd03245 214 GRI 216
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
315-472 |
2.62e-16 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 82.52 E-value: 2.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 315 SGKLVFEteglGLDF---GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNL-EVAYfDQ 389
Cdd:COG1132 337 RGEIEFE----NVSFsypGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILiDGVDIrDLTL-ES 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 390 YREQL-----DP---EKTVVDNVGEGKQEVmvrgrSR----------HILGYLQDFlfePKRARTPV----KALSGGEKN 447
Cdd:COG1132 412 LRRQIgvvpqDTflfSGTIRENIRYGRPDA-----TDeeveeaakaaQAHEFIEAL---PDGYDTVVgergVNLSGGQRQ 483
|
170 180
....*....|....*....|....*
gi 657198994 448 RLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:COG1132 484 RIAIARALLKDPPILILDEATSALD 508
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
321-468 |
2.80e-16 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 78.63 E-value: 2.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTnlEVAYFDQYR-------- 391
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLfDGE--DITGLPPHEiarlgigr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 392 ----EQLDPEKTVVDNV---------------GEGKQEVMVRGRSRHILgylqDFLFEPKRARTPVKALSGGEKNRLLLA 452
Cdd:cd03219 80 tfqiPRLFPELTVLENVmvaaqartgsglllaRARREEREARERAEELL----ERVGLADLADRPAGELSYGQQRRLEIA 155
|
170
....*....|....*..
gi 657198994 453 K-LFLKPSnLLILDEPT 468
Cdd:cd03219 156 RaLATDPK-LLLLDEPA 171
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
298-472 |
2.92e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 80.65 E-value: 2.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 298 RRELQGKAKLQLDEAGRSGKLVFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVr 377
Cdd:PRK13536 20 ERKHQGISEAKASIPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKI- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 378 qgTNLEVAYFDQYR------------EQLDPEKTVVDN-VGEGKQEVMVRGRSRHILGYLQDFLFEPKRARTPVKALSGG 444
Cdd:PRK13536 99 --TVLGVPVPARARlararigvvpqfDNLDLEFTVRENlLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGG 176
|
170 180
....*....|....*....|....*...
gi 657198994 445 EKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:PRK13536 177 MKRRLTLARALINDPQLLILDEPTTGLD 204
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
321-472 |
3.66e-16 |
|
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: 78.31 E-value: 3.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLEVAYFDQYRE------- 392
Cdd:cd03261 2 ELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLiDGEDISGLSEAELYRlrrrmgm 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 393 --Q---LDPEKTVVDNVG------EGKQEVMVRGRSRHILGYLQdflFEPKRARTPVKaLSGGEKNRLLLAK-LFLKPSn 460
Cdd:cd03261 82 lfQsgaLFDSLTVFENVAfplrehTRLSEEEIREIVLEKLEAVG---LRGAEDLYPAE-LSGGMKKRVALARaLALDPE- 156
|
170
....*....|..
gi 657198994 461 LLILDEPTNDLD 472
Cdd:cd03261 157 LLLYDEPTAGLD 168
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-501 |
5.86e-16 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 80.83 E-value: 5.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 1 MALLTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQQDlKVTRL--EQDPPAS 78
Cdd:PRK10938 1 MSSLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFS-HITRLsfEQLQKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 79 SEitvfdyaaeglagvgellkQYHHVSHALAHDPSDANIRTMSQLqeqldYQNGWQYETRINQVLTLLDLDP--DVTLDS 156
Cdd:PRK10938 80 SD-------------------EWQRNNTDMLSPGEDDTGRTTAEI-----IQDEVKDPARCEQLAQQFGITAllDRRFKY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 157 LSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRG---AIVFISHDREFIHKLATRIIDLDRGVITs 233
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQsgiTLVLVLNRFDEIPDFVQFAGVLADCTLA- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 234 wpgnydeyLQGKEEWLRVEELknaefdrklaqeevwVRQGIKARRTRNEgrvralkamrmertqrrELQGKAKLQLDEAG 313
Cdd:PRK10938 215 --------ETGEREEILQQAL---------------VAQLAHSEQLEGV-----------------QLPEPDEPSARHAL 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 314 RSGKLVFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEasrgsvrQGTNLEVAYFDQYR-- 391
Cdd:PRK10938 255 PANEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHP-------QGYSNDLTLFGRRRgs 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 392 ---------------EQLDPE-------KTVV-----DNVGEGKQevmVRGRSRHILGYLQDFLFEPKR-ARTPVKALSG 443
Cdd:PRK10938 328 getiwdikkhigyvsSSLHLDyrvstsvRNVIlsgffDSIGIYQA---VSDRQQKLAQQWLDILGIDKRtADAPFHSLSW 404
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 657198994 444 GEKNRLLLAKLFLKPSNLLILDEPTNDLDvetlelleelltdyPGTLLLVshdRRFID 501
Cdd:PRK10938 405 GQQRLALIVRALVKHPTLLILDEPLQGLD--------------PLNRQLV---RRFVD 445
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
12-231 |
5.99e-16 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 79.74 E-value: 5.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 12 SFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQ-QDlkVTRLE----------QDPPASSE 80
Cdd:PRK10851 11 SFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHgTD--VSRLHardrkvgfvfQHYALFRH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 81 ITVFDYAAEGLAgvgeLLKQYHHvshalahdPSDANIRT-MSQLQE--QLDYqngwqyetrinqvltLLDLDPDvtldSL 157
Cdd:PRK10851 89 MTVFDNIAFGLT----VLPRRER--------PNAAAIKAkVTQLLEmvQLAH---------------LADRYPA----QL 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 657198994 158 SGGWLRKVALARALACDPDLLLLDEPTNHLDI----DAINWLEEFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:PRK10851 138 SGGQKQRVALARALAVEPQILLLDEPFGALDAqvrkELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-231 |
6.17e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 78.19 E-value: 6.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 1 MALLTLHGASLSFSDFPL---------LDHAELTIERGERLCLVGRNGAGKSTLmkviaselplddGRLVLQqdlkvtrL 71
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGGLsgkhqhqtvLNNVSLSLKSGETVALLGRSGCGKSTL------------ARLLVG-------L 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 72 EQdpPASSEITVFDYAAEGLAGVGEllKQYHHVSHALAHD-PSDANIR-----TMSQLQEQLDYQNGWQYETRINQVLTL 145
Cdd:PRK10419 62 ES--PSQGNVSWRGEPLAKLNRAQR--KAFRRDIQMVFQDsISAVNPRktvreIIREPLRHLLSLDKAERLARASEMLRA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 146 LDLDPDVtLD----SLSGGWLRKVALARALACDPDLLLLDEPTNHLDI----DAINWLEEFLKDFRGAIVFISHDREFIH 217
Cdd:PRK10419 138 VDLDDSV-LDkrppQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHDLRLVE 216
|
250
....*....|....
gi 657198994 218 KLATRIIDLDRGVI 231
Cdd:PRK10419 217 RFCQRVMVMDNGQI 230
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
12-223 |
6.34e-16 |
|
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: 77.16 E-value: 6.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 12 SFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGR-LVLQQDLKVTRLEqdppASSEITV---FDYA 87
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTaYINGYSIRTDRKA----ARQSLGYcpqFDAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 88 AEGLAGVgELLKQY---HHVSHALAHDPSDANIRTMSqLQEQLDyqngwqyeTRINQvltlldldpdvtldsLSGGWLRK 164
Cdd:cd03263 87 FDELTVR-EHLRFYarlKGLPKSEIKEEVELLLRVLG-LTDKAN--------KRART---------------LSGGMKRK 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 657198994 165 VALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRG--AIVFISHDREFIHKLATRI 223
Cdd:cd03263 142 LSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKgrSIILTTHSMDEAEALCDRI 202
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
321-473 |
6.70e-16 |
|
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: 77.02 E-value: 6.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRqgtnleVAYFDQYREQLDPEKTV 400
Cdd:cd03265 2 EVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRAT------VAGHDVVREPREVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 401 --------VDNVGEGKQEVMVRGRsrhILGY-----------LQDFLFEPKRARTPVKALSGGEKNRLLLAKLFLKPSNL 461
Cdd:cd03265 76 givfqdlsVDDELTGWENLYIHAR---LYGVpgaerrerideLLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEV 152
|
170
....*....|..
gi 657198994 462 LILDEPTNDLDV 473
Cdd:cd03265 153 LFLDEPTIGLDP 164
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
12-231 |
7.65e-16 |
|
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: 77.02 E-value: 7.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 12 SFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRL------VLQQDLKVTR----LEQDPPASSEI 81
Cdd:cd03265 9 KYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRAtvaghdVVREPREVRRrigiVFQDLSVDDEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 82 TVFD--YAAEGLAGV-GELLKQyhhvshalahdpsdanirtmsqlqeqldyqngwqyetRINQVLTLLDL--DPDVTLDS 156
Cdd:cd03265 89 TGWEnlYIHARLYGVpGAERRE-------------------------------------RIDELLDFVGLleAADRLVKT 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 657198994 157 LSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAIN--W--LEEFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:cd03265 132 YSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAhvWeyIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
5-229 |
8.78e-16 |
|
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: 77.09 E-value: 8.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 5 TLH---GASLsfsdfPLLDHAELTIERGERLCLVGRNGAGKSTLMKVI-ASELPlDDGRLVLQQDLKVTRLEQDPPasSE 80
Cdd:COG4778 15 TLHlqgGKRL-----PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIyGNYLP-DSGSILVRHDGGWVDLAQASP--RE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 81 I---------------------TVFDYAAEGLAgvgellkqyhhvshALAHDPSDANIRTMSQLqeqldyqngwqyeTRI 139
Cdd:COG4778 87 IlalrrrtigyvsqflrviprvSALDVVAEPLL--------------ERGVDREEARARARELL-------------ARL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 140 NQVLTLLDLDPdVTLdslSGGWLRKVALARALACDPDLLLLDEPTNHLD-------IDAInwlEEfLKDfRG-AIVFISH 211
Cdd:COG4778 140 NLPERLWDLPP-ATF---SGGEQQRVNIARGFIADPPLLLLDEPTASLDaanravvVELI---EE-AKA-RGtAIIGIFH 210
|
250
....*....|....*...
gi 657198994 212 DREFIHKLATRIIDLDRG 229
Cdd:COG4778 211 DEEVREAVADRVVDVTPF 228
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
319-500 |
8.99e-16 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 77.39 E-value: 8.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 319 VFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNL------EVAyfdqyR 391
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILfDGRDItglpphRIA-----R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 392 E---------QLDPEKTVVDNV--------GEG------------KQEVMVRGRSRHILGY--LQDflfepkRARTPVKA 440
Cdd:COG0411 79 LgiartfqnpRLFPELTVLENVlvaaharlGRGllaallrlprarREEREARERAEELLERvgLAD------RADEPAGN 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 657198994 441 LSGGEKNRLLLAK-LFLKPSnLLILDEPT---NDLDVETLELLEELLTDYPG-TLLLVSHDRRFI 500
Cdd:COG0411 153 LSYGQQRRLEIARaLATEPK-LLLLDEPAaglNPEETEELAELIRRLRDERGiTILLIEHDMDLV 216
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
319-496 |
9.65e-16 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 80.33 E-value: 9.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 319 VFETEGLGLDF--GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEAS---RGSVR-QGTNL---------- 382
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLlDGRDLlelsealrgr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 383 EVAY-FDQYREQLDPEkTVVDNVGEGKQEVMVRGRSRH--ILGYLQDFLFEpKRARTPVKALSGGEKNRLLLA-KLFLKP 458
Cdd:COG1123 84 RIGMvFQDPMTQLNPV-TVGDQIAEALENLGLSRAEARarVLELLEAVGLE-RRLDRYPHQLSGGQRQRVAIAmALALDP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 657198994 459 SnLLILDEPTNDLDVET----LELLEELLTDYPGTLLLVSHD 496
Cdd:COG1123 162 D-LLIADEPTTALDVTTqaeiLDLLRELQRERGTTVLLITHD 202
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
19-212 |
9.84e-16 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 78.62 E-value: 9.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 19 LDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVL---------QQDLKVTRLE-----QDPPAS--SEIT 82
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFdgqditglsGRELRPLRRRmqmvfQDPYASlnPRMT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 83 VFDYAAEGLagvgellkqyhhvshaLAHDPSDANIRtmsqlqeqldyqngwqyETRINQVLTLLDLDPDVtLDS----LS 158
Cdd:COG4608 114 VGDIIAEPL----------------RIHGLASKAER-----------------RERVAELLELVGLRPEH-ADRypheFS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 657198994 159 GGWLRKVALARALACDPDLLLLDEPTNHLD--IDA--INWLEEFLKDFRGAIVFISHD 212
Cdd:COG4608 160 GGQRQRIGIARALALNPKLIVCDEPVSALDvsIQAqvLNLLEDLQDELGLTYLFISHD 217
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
319-473 |
9.95e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 76.07 E-value: 9.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 319 VFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRqgTNLEVAYFDQYREQ----- 393
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIK--LDGGDIDDPDVAEAchylg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 394 ----LDPEKTVVDNVgEGKQEVMvRGRSRHILGYLQDFLFEPKrARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTN 469
Cdd:PRK13539 80 hrnaMKPALTVAENL-EFWAAFL-GGEELDIAAALEAVGLAPL-AHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTA 156
|
....
gi 657198994 470 DLDV 473
Cdd:PRK13539 157 ALDA 160
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-189 |
1.32e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 77.05 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 5 TLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGR-LVLQQDLKVTR----------LEQ 73
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEvLVDGLDVATTPsrelakrlaiLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 74 DPPASSEITVFDyaaegLAGVGellkQY-HHVSHALAHDpsdanirtmsqlqeqldyqngwqyETRINQVLTLLDLDP-- 150
Cdd:COG4604 83 ENHINSRLTVRE-----LVAFG----RFpYSKGRLTAED------------------------REIIDEAIAYLDLEDla 129
|
170 180 190
....*....|....*....|....*....|....*....
gi 657198994 151 DVTLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDI 189
Cdd:COG4604 130 DRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDM 168
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
4-229 |
1.68e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 79.85 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 4 LTLHGASLSFSDF-PLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQQDLKVTRLEQDP--PASSE 80
Cdd:COG4178 363 LALEDLTLRTPDGrPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQRPylPLGTL 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 81 ITVFDYAAEglagvgellkqyhhvshalAHDPSDANIRT------MSQLQEQLDYQNGWQyetrinqvltlldldpdvtl 154
Cdd:COG4178 443 REALLYPAT-------------------AEAFSDAELREaleavgLGHLAERLDEEADWD-------------------- 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 657198994 155 DSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKD--FRGAIVFISHdREFIHKLATRIIDLDRG 229
Cdd:COG4178 484 QVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREelPGTTVISVGH-RSTLAAFHDRVLELTGD 559
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
323-473 |
2.25e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 76.31 E-value: 2.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 323 EGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRQGTNLEVAYFDQyREQLDPekTVVD 402
Cdd:PRK09544 8 ENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQ-KLYLDT--TLPL 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 657198994 403 NVgegKQEVMVRGRSRHilgylQDFLFEPKRART------PVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK09544 85 TV---NRFLRLRPGTKK-----EDILPALKRVQAghlidaPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDV 153
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
319-472 |
2.29e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 75.77 E-value: 2.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 319 VFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSvrqgtnlevAYFDQYREQLDPEK 398
Cdd:COG2401 30 VLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVA---------GCVDVPDNQFGREA 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 657198994 399 TVVDNVGEgKQEVMVRGRSRHILGYLQDFLFepkraRTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:COG2401 101 SLIDAIGR-KGDFKDAVELLNAVGLSDAVLW-----LRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
320-472 |
2.67e-15 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 75.68 E-value: 2.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 320 FETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRQGtnlEVAYFDQ--YREQLDPE 397
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEG---EVLLDGKdiYDLDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 398 -----------------KTVVDNV-------GEGKQEVMvRGRSRHILGylQDFLFEPKRARTPVKALSGGEKNRLLLAK 453
Cdd:cd03260 78 elrrrvgmvfqkpnpfpGSIYDNVayglrlhGIKLKEEL-DERVEEALR--KAALWDEVKDRLHALGLSGGQQQRLCLAR 154
|
170 180
....*....|....*....|
gi 657198994 454 -LFLKPSNLLiLDEPTNDLD 472
Cdd:cd03260 155 aLANEPEVLL-LDEPTSALD 173
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
283-473 |
2.86e-15 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 78.94 E-value: 2.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 283 GRVRAlKAMRMERTQRRELQGKAKLQ-LDEAGRSGKLVFETEGLGLDF-GDRTLFQGLDLQVLRGDKIALVGPNGCGKST 360
Cdd:TIGR02868 298 TRVRA-AAERIVEVLDAAGPVAEGSApAAGAVGLGKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKST 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 361 LIKLLMGQLEASRGSVRQgTNLEVAYFDQ----YREQLDPEK------TVVDNV----GEGKQEVMVRGRSRHILGYLQD 426
Cdd:TIGR02868 377 LLATLAGLLDPLQGEVTL-DGVPVSSLDQdevrRRVSVCAQDahlfdtTVRENLrlarPDATDEELWAALERVGLADWLR 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 657198994 427 FLfePKRARTPV----KALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:TIGR02868 456 AL--PDGLDTVLgeggARLSGGERQRLALARALLADAPILLLDEPTEHLDA 504
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
321-561 |
3.09e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 77.96 E-value: 3.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLEVAYFDQYREQLD--PE 397
Cdd:PRK09536 5 DVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLvAGDDVEALSARAASRRVAsvPQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 398 KTVVDNVGEGKQEVMVrGRSRHI-----LGYLQDFLFEPKRART--------PVKALSGGEKNRLLLAKLFLKPSNLLIL 464
Cdd:PRK09536 85 DTSLSFEFDVRQVVEM-GRTPHRsrfdtWTETDRAAVERAMERTgvaqfadrPVTSLSGGERQRVLLARALAQATPVLLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 465 DEPTNDLDVETL---ELLEELLTDYPGTLLLVSHD----RRFIDNTVtgcwlFEGDGRISDyVGGYADMMATRALQAA-- 535
Cdd:PRK09536 164 DEPTASLDINHQvrtLELVRRLVDDGKTAVAAIHDldlaARYCDELV-----LLADGRVRA-AGPPADVLTADTLRAAfd 237
|
250 260 270
....*....|....*....|....*....|..
gi 657198994 536 ------QQTAKPAPVKVAEPVASAAEPAKKTR 561
Cdd:PRK09536 238 artavgTDPATGAPTVTPLPDPDRTEAAADTR 269
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-226 |
3.37e-15 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 78.87 E-value: 3.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 4 LTLHGASLSFSD-FPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLqqdlkvtrleqdppASSEIT 82
Cdd:TIGR02857 322 LEFSGVSVAYPGrRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAV--------------NGVPLA 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 83 VFDyAAEGLAGVGELLKQYHHVSHALAhdpsdANIR------TMSQLQEQLDYQNGWQYETRINQVL-TLLDLDPDvtld 155
Cdd:TIGR02857 388 DAD-ADSWRDQIAWVPQHPFLFAGTIA-----ENIRlarpdaSDAEIREALERAGLDEFVAALPQGLdTPIGEGGA---- 457
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 657198994 156 SLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDF-RGAIVF-ISHDREFIHkLATRIIDL 226
Cdd:TIGR02857 458 GLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALaQGRTVLlVTHRLALAA-LADRIVVL 529
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-231 |
3.97e-15 |
|
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: 75.06 E-value: 3.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 4 LTLHGASLSFSDFPLLDhAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQ-QDlkVTRLeqdPPASSEI- 81
Cdd:cd03299 1 LKVENLSKDWKEFKLKN-VSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNgKD--ITNL---PPEKRDIs 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 82 ------------TVFDYAAEGLAGVGELLKQYHhvshalahdpsdaniRTMSQLQEQLDYQNgwqyetrinqvltLLDLD 149
Cdd:cd03299 75 yvpqnyalfphmTVYKNIAYGLKKRKVDKKEIE---------------RKVLEIAEMLGIDH-------------LLNRK 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 150 PDvtldSLSGGWLRKVALARALACDPDLLLLDEPTNHLDI----DAINWLEEFLKDFRGAIVFISHDREFIHKLATRIID 225
Cdd:cd03299 127 PE----TLSGGEQQRVAIARALVVNPKILLLDEPFSALDVrtkeKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAI 202
|
....*.
gi 657198994 226 LDRGVI 231
Cdd:cd03299 203 MLNGKL 208
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
320-500 |
4.02e-15 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 73.76 E-value: 4.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 320 FETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLE------------VAY 386
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILiDGEDLTdledelpplrrrIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 387 -FDQYreQLDPEKTVVDNVGEGkqevmvrgrsrhilgylqdflfepkrartpvkaLSGGEKNRLLLAK-LFLKPsNLLIL 464
Cdd:cd03229 81 vFQDF--ALFPHLTVLENIALG---------------------------------LSGGQQQRVALARaLAMDP-DVLLL 124
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 657198994 465 DEPTNDLDVETLELLEELLTD----YPGTLLLVSHDRRFI 500
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSlqaqLGITVVLVTHDLDEA 164
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-231 |
5.53e-15 |
|
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: 74.24 E-value: 5.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 4 LTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVlqqdlkvtrleqdppasseitv 83
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVL---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 84 FDYAAEGLAgvgellkqyhhVSHALAHDPSDANIRTMSQLQEQLDY------QNGWQYETRINQVLTLLDLDP--DVTLD 155
Cdd:cd03269 59 FDGKPLDIA-----------ARNRIGYLPEERGLYPKMKVIDQLVYlaqlkgLKKEEARRRIDEWLERLELSEyaNKRVE 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 657198994 156 SLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRGA---IVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:cd03269 128 ELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAgktVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
336-501 |
5.73e-15 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 74.55 E-value: 5.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 336 QGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLevayfdqyrEQLDPEK---------------- 398
Cdd:cd03245 21 DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLlDGTDI---------RQLDPADlrrnigyvpqdvtlfy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 399 -TVVDNVGEGK-----QEVMvrgRSRHILGYLQDFLFEPKRARTPV----KALSGGEKNRLLLAKLFLKPSNLLILDEPT 468
Cdd:cd03245 92 gTLRDNITLGApladdERIL---RAAELAGVTDFVNKHPNGLDLQIgergRGLSGGQRQAVALARALLNDPPILLLDEPT 168
|
170 180 190
....*....|....*....|....*....|....*
gi 657198994 469 NDLDVETLELLEELLTDYPG--TLLLVSHDRRFID 501
Cdd:cd03245 169 SAMDMNSEERLKERLRQLLGdkTLIIITHRPSLLD 203
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
17-231 |
6.45e-15 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 73.02 E-value: 6.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 17 PLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPlddgrlvlqqdlkvtrleqdpPASSEITVfDyaaeglagvGE 96
Cdd:cd03246 16 PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLR---------------------PTSGRVRL-D---------GA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 97 LLKQYHhvshalahdpsdanirtMSQLQEQLDYqngwqyetrinqvltlldLDPDVTLDS-------LSGGWLRKVALAR 169
Cdd:cd03246 65 DISQWD-----------------PNELGDHVGY------------------LPQDDELFSgsiaeniLSGGQRQRLGLAR 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 657198994 170 ALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRGA---IVFISHDREFIhKLATRIIDLDRGVI 231
Cdd:cd03246 110 ALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAgatRIVIAHRPETL-ASADRILVLEDGRV 173
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
321-473 |
6.76e-15 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 73.55 E-value: 6.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRQGTNLEVAYFDQYREQ------- 393
Cdd:TIGR01189 2 AARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENilylghl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 394 --LDPEKTVVDNVGegkqevmvrgRSRHILGYLQDFLFEP-------KRARTPVKALSGGEKNRLLLAKLFLKPSNLLIL 464
Cdd:TIGR01189 82 pgLKPELSALENLH----------FWAAIHGGAQRTIEDAlaavgltGFEDLPAAQLSAGQQRRLALARLWLSRRPLWIL 151
|
....*....
gi 657198994 465 DEPTNDLDV 473
Cdd:TIGR01189 152 DEPTTALDK 160
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
331-473 |
6.78e-15 |
|
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: 74.57 E-value: 6.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 331 DRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLEVAYFDQYREQLD--PEKTVV------ 401
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILiDGQDIREVTLDSLRRAIGvvPQDTVLfndtig 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 402 DNVGEGK-----QEVMVRGRSRHILGYLQDFlfePKRARTPVKA----LSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:cd03253 93 YNIRYGRpdatdEEVIEAAKAAQIHDKIMRF---PDGYDTIVGErglkLSGGEKQRVAIARAILKNPPILLLDEATSALD 169
|
.
gi 657198994 473 V 473
Cdd:cd03253 170 T 170
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-244 |
8.83e-15 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 74.02 E-value: 8.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 4 LTLHGASLSFSDFPLldHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQ-QDlkVTRLeqdPPASSEIT 82
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNgQD--LTAL---PPAERPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 83 VfdyaaeglagvgelLKQ----YHHVSH----ALAHDP----SDANIRTMSQLQEQLDYQNgwqyetrinqvltLLDLDP 150
Cdd:COG3840 75 M--------------LFQennlFPHLTVaqniGLGLRPglklTAEQRAQVEQALERVGLAG-------------LLDRLP 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 151 DvtldSLSGGWLRKVALARALACDPDLLLLDEPTNHLDI----DAINWLEEFLKDFRGAIVFISHDREFIHKLATRIIDL 226
Cdd:COG3840 128 G----QLSGGQRQRVALARCLVRKRPILLLDEPFSALDPalrqEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLV 203
|
250
....*....|....*...
gi 657198994 227 DRGVItSWPGNYDEYLQG 244
Cdd:COG3840 204 ADGRI-AADGPTAALLDG 220
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2-189 |
9.50e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 74.42 E-value: 9.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 2 ALLTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGR-LVLQQDLKvtrleqdppasse 80
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEvRLNGRPLA------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 81 itvfDYAAEGLAGVGELLKQYHHVSHA-LAHDpsdanIRTMSQLQEQLDYQNGwqyETRINQVLTLLDLDPDVTLD--SL 157
Cdd:PRK13548 68 ----DWSPAELARRRAVLPQHSSLSFPfTVEE-----VVAMGRAPHGLSRAED---DALVAAALAQVDLAHLAGRDypQL 135
|
170 180 190
....*....|....*....|....*....|....*...
gi 657198994 158 SGGWLRKVALARALA------CDPDLLLLDEPTNHLDI 189
Cdd:PRK13548 136 SGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDL 173
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
320-473 |
1.22e-14 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 71.69 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 320 FETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGsvrqgtnlevayfdqyreqldpekt 399
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSG------------------------- 55
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 657198994 400 vvdnvgegkqEVMVRGRSRHILGylqdflfePKRAR----TPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:cd03216 56 ----------EILVDGKEVSFAS--------PRDARragiAMVYQLSVGERQMVEIARALARNARLLILDEPTAALTP 115
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
329-472 |
1.33e-14 |
|
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: 72.95 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 329 FGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLEV--AYFDQYREQ---------LDP 396
Cdd:cd03262 10 FGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIiDGLKLTDdkKNINELRQKvgmvfqqfnLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 397 EKTVVDNVGEGkqEVMVRGRSR-----HILGYLQDFLFEPKRARTPVKaLSGGEKNRLLLAK-LFLKPSnLLILDEPTND 470
Cdd:cd03262 90 HLTVLENITLA--PIKVKGMSKaeaeeRALELLEKVGLADKADAYPAQ-LSGGQQQRVAIARaLAMNPK-VMLFDEPTSA 165
|
..
gi 657198994 471 LD 472
Cdd:cd03262 166 LD 167
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-224 |
1.42e-14 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 74.13 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 1 MALLTLHGASLSF----SDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQQDlKVTRleqdpP 76
Cdd:COG4525 1 MSMLTVRHVSVRYpgggQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGV-PVTG-----P 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 77 ASSEITVF------------DYAAEGL--AGVGellkqyHHVSHALAHdpsdanirtmsqlqeqldyqngwqyetrinQV 142
Cdd:COG4525 75 GADRGVVFqkdallpwlnvlDNVAFGLrlRGVP------KAERRARAE------------------------------EL 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 143 LTLLDLD--PDVTLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFL----KDFRGAIVFISHDREFI 216
Cdd:COG4525 119 LALVGLAdfARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLldvwQRTGKGVFLITHSVEEA 198
|
....*...
gi 657198994 217 HKLATRII 224
Cdd:COG4525 199 LFLATRLV 206
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
17-242 |
1.49e-14 |
|
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: 73.42 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 17 PLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQ----QDLKVTRL-------EQDPPASSEiTVFD 85
Cdd:cd03251 16 PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDghdvRDYTLASLrrqiglvSQDVFLFND-TVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 86 YAAEGLAGVGEllKQYHHVSH-ALAHDpsdaNIRTMSQlqeqldyqngwQYETRINQVLTlldldpdvtldSLSGGWLRK 164
Cdd:cd03251 95 NIAYGRPGATR--EEVEEAARaANAHE----FIMELPE-----------GYDTVIGERGV-----------KLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 165 VALARALACDPDLLLLDEPTNHLDI---DAI-NWLEEFLKDfRGAIVfISHDREFIhKLATRIIDLDRGVITSwPGNYDE 240
Cdd:cd03251 147 IAIARALLKDPPILILDEATSALDTeseRLVqAALERLMKN-RTTFV-IAHRLSTI-ENADRIVVLEDGKIVE-RGTHEE 222
|
..
gi 657198994 241 YL 242
Cdd:cd03251 223 LL 224
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
4-227 |
1.67e-14 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 71.42 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 4 LTLHGASLSFSD-FPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQQDLKVTRLEQDPpasseit 82
Cdd:cd03223 1 IELENLSLATPDgRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRP------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 83 vfdYAAEGLagvgellkqyhhvshalahdpsdanirtmsqLQEQLDYQngWQyetrinqvltlldldpdvtlDSLSGGWL 162
Cdd:cd03223 74 ---YLPLGT-------------------------------LREQLIYP--WD--------------------DVLSGGEQ 97
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 657198994 163 RKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRGAIVFISHdREFIHKLATRIIDLD 227
Cdd:cd03223 98 QRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVLDLD 161
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
25-224 |
1.68e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 76.77 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 25 TIERGERLCLVGRNGAGKSTLMKVIASELPLDDGrlVLQQDLKVTRLEQDPPASSEITVFDYaaegLAGVGEllkqyhhv 104
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEG--EVDPELKISYKPQYIKPDYDGTVEDL----LRSITD-------- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 105 shalahdpsdanirtmsqlqeqlDYQNGWqYETRINQVLTLLDLdPDVTLDSLSGGWLRKVALARALACDPDLLLLDEPT 184
Cdd:PRK13409 427 -----------------------DLGSSY-YKSEIIKPLQLERL-LDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPS 481
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 657198994 185 NHLDID-------AINwleEFLKDFRGAIVFISHDREFIHKLATRII 224
Cdd:PRK13409 482 AHLDVEqrlavakAIR---RIAEEREATALVVDHDIYMIDYISDRLM 525
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
337-503 |
1.81e-14 |
|
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: 72.83 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 337 GLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNL------EVAYFDQ-----YRE-QLDPEKTVVDN 403
Cdd:cd03292 19 GINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRvNGQDVsdlrgrAIPYLRRkigvvFQDfRLLPDRNVYEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 404 V-------GEGKQEvmVRGRSRHILgylqDFLFEPKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETL 476
Cdd:cd03292 99 VafalevtGVPPRE--IRKRVPAAL----ELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTT 172
|
170 180 190
....*....|....*....|....*....|
gi 657198994 477 ELLEELLTDY--PGTLLLVS-HDRRFIDNT 503
Cdd:cd03292 173 WEIMNLLKKInkAGTTVVVAtHAKELVDTT 202
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
12-224 |
2.06e-14 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 76.36 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 12 SFSDFPLlDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGrlVLQQDLKVTRLEQDPPASSEITVFDYAAEGL 91
Cdd:COG1245 350 SYGGFSL-EVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEG--EVDEDLKISYKPQYISPDYDGTVEEFLRSAN 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 92 AGvgellkqyhhvshalahdpsdanirtmsqlqeqlDYQNGWQYEtrinQVLTLLDLDP--DVTLDSLSGGWLRKVALAR 169
Cdd:COG1245 427 TD----------------------------------DFGSSYYKT----EIIKPLGLEKllDKNVKDLSGGELQRVAIAA 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 657198994 170 ALACDPDLLLLDEPTNHLDIdainwlEE------FLKDF---RGAIVF-ISHDREFIHKLATRII 224
Cdd:COG1245 469 CLSRDADLYLLDEPSAHLDV------EQrlavakAIRRFaenRGKTAMvVDHDIYLIDYISDRLM 527
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
319-472 |
2.25e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 73.27 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 319 VFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRqgtnlevaYFDQYREQLDPEK 398
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVR--------LNGRPLADWSPAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 399 ------------------TVvdnvgegkQEVMVRGRSRHILGYLQD-FLFEPKRART--------PVKALSGGEKNRLLL 451
Cdd:PRK13548 74 larrravlpqhsslsfpfTV--------EEVVAMGRAPHGLSRAEDdALVAAALAQVdlahlagrDYPQLSGGEQQRVQL 145
|
170 180
....*....|....*....|....*..
gi 657198994 452 AKLFL------KPSNLLILDEPTNDLD 472
Cdd:PRK13548 146 ARVLAqlwepdGPPRWLLLDEPTSALD 172
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-231 |
2.66e-14 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 75.88 E-value: 2.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 19 LDHAELTIERGERLCLVGRNGAGKSTL----MKVIASElplddGRLVL---------QQDLKVTRLE-----QDPPAS-- 78
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLglalLRLIPSE-----GEIRFdgqdldglsRRALRPLRRRmqvvfQDPFGSls 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 79 SEITVFDYAAEGLAgvgellkqyhhvshalAHDPsdanirtmsqlqeQLDYQngwQYETRINQVLTLLDLDPDvTLD--- 155
Cdd:COG4172 377 PRMTVGQIIAEGLR----------------VHGP-------------GLSAA---ERRARVAEALEEVGLDPA-ARHryp 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 156 -SLSGGWLRKVALARALACDPDLLLLDEPTNHLD--IDA--INWLEEFLKDFRGAIVFISHDREFIHKLATRIIDLDRGV 230
Cdd:COG4172 424 hEFSGGQRQRIAIARALILEPKLLVLDEPTSALDvsVQAqiLDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGK 503
|
.
gi 657198994 231 I 231
Cdd:COG4172 504 V 504
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
24-231 |
2.66e-14 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 72.74 E-value: 2.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 24 LTIERGERLCLVGRNGAGKSTLMKVI-ASELPlDDGRLVL---QQDLKvtrleqDPPASSEItvfdyaAEGLAGVGELLK 99
Cdd:PRK11124 23 LDCPQGETLVLLGPSGAGKSSLLRVLnLLEMP-RSGTLNIagnHFDFS------KTPSDKAI------RELRRNVGMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 100 QYH---H--VSHALAHDPsdANIRTMSQLQEQldyqngwqyeTRINQVLTLLDLDP--DVTLDSLSGGWLRKVALARALA 172
Cdd:PRK11124 90 QYNlwpHltVQQNLIEAP--CRVLGLSKDQAL----------ARAEKLLERLRLKPyaDRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 657198994 173 CDPDLLLLDEPTNHLDIDAINWLEEFLKDFRG-AI--VFISHDREFIHKLATRIIDLDRGVI 231
Cdd:PRK11124 158 MEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGItqVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-212 |
3.31e-14 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 75.47 E-value: 3.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 4 LTLHGASLSFSD-FPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQqDLKVTRLEQDPpasseit 82
Cdd:TIGR02868 335 LELRDLSAGYPGaPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLD-GVPVSSLDQDE------- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 83 vfdyaaegLAGVGELLKQYHHVSHA-------LAH-DPSDANIRTM---SQLQEQLDyqngwqyetrinqvlTLLD-LDP 150
Cdd:TIGR02868 407 --------VRRRVSVCAQDAHLFDTtvrenlrLARpDATDEELWAAlerVGLADWLR---------------ALPDgLDT 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 657198994 151 DVTLD--SLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAinwLEEFLKDFRGA-----IVFISHD 212
Cdd:TIGR02868 464 VLGEGgaRLSGGERQRLALARALLADAPILLLDEPTEHLDAET---ADELLEDLLAAlsgrtVVLITHH 529
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-231 |
3.94e-14 |
|
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: 72.08 E-value: 3.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 4 LTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQ-QDlkVTRLeqdppASSEIt 82
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDgRD--ITGL-----PPHER- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 83 vfdyAAEGLAGVGEllkqyhhvSHALAHDPS-DANIRTMSQLQEQLDyqngwqYETRINQVLTLLdldPDvtLD------ 155
Cdd:cd03224 73 ----ARAGIGYVPE--------GRRIFPELTvEENLLLGAYARRRAK------RKARLERVYELF---PR--LKerrkql 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 156 --SLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRG---AIVFISHDREFIHKLATRIIDLDRGV 230
Cdd:cd03224 130 agTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDegvTILLVEQNARFALEIADRAYVLERGR 209
|
.
gi 657198994 231 I 231
Cdd:cd03224 210 V 210
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
6-231 |
4.35e-14 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 72.35 E-value: 4.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 6 LHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVI-ASELPlDDGRLVLqqdlkvtrleqdppASSEitvF 84
Cdd:COG4161 5 LKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLnLLETP-DSGQLNI--------------AGHQ---F 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 85 DYAAEGLAG--------VGELLKQYHHVSHalahdpsdanIRTMSQLQE---QLDYQNGWQYETRINQVLTLLDLDP--D 151
Cdd:COG4161 67 DFSQKPSEKairllrqkVGMVFQQYNLWPH----------LTVMENLIEapcKVLGLSKEQAREKAMKLLARLRLTDkaD 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 152 VTLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRG-AI--VFISHDREFIHKLATRIIDLDR 228
Cdd:COG4161 137 RFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtGItqVIVTHEVEFARKVASQVVYMEK 216
|
...
gi 657198994 229 GVI 231
Cdd:COG4161 217 GRI 219
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
336-468 |
5.14e-14 |
|
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: 71.70 E-value: 5.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 336 QGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLE-----------VAYFDQYReQLDPEKTVVDN 403
Cdd:cd03224 17 FGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRfDGRDITglppheraragIGYVPEGR-RIFPELTVEEN 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 657198994 404 --VGEGKQEvmvRGRSRHILgylqDFLFE--PK---RARTPVKALSGGEKNRLLLAK-LFLKPSnLLILDEPT 468
Cdd:cd03224 96 llLGAYARR---RAKRKARL----ERVYElfPRlkeRRKQLAGTLSGGEQQMLAIARaLMSRPK-LLLLDEPS 160
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
11-241 |
5.26e-14 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 75.28 E-value: 5.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 11 LSFSD----FP----LLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPlddgrlvlqqdlkvtrleqdpPASSeiT 82
Cdd:PLN03073 509 ISFSDasfgYPggplLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQ---------------------PSSG--T 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 83 VFDYAAEGLAgvgeLLKQYHHVSHALAHDPSDANIRTMSQLQEQldyqngwqyetRINQVLTLLDLDPDVTLDS---LSG 159
Cdd:PLN03073 566 VFRSAKVRMA----VFSQHHVDGLDLSSNPLLYMMRCFPGVPEQ-----------KLRAHLGSFGVTGNLALQPmytLSG 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 160 GWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITSWPGNYD 239
Cdd:PLN03073 631 GQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFH 710
|
..
gi 657198994 240 EY 241
Cdd:PLN03073 711 DY 712
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
19-231 |
5.56e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 72.77 E-value: 5.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 19 LDHAELTIERGERLCLVGRNGAGKSTLMKVIaselpldDGRLvlqqdlkvtrleqdPPASSEITV--FDYAAEGLAgVGE 96
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHL-------NGLL--------------KPTSGKIIIdgVDITDKKVK-LSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 97 LLKQ----YHHVSHALAHDPSDANI----RTMSQLQEQLdyqngwqyETRINQVLTLLDLDPDVTLD----SLSGGWLRK 164
Cdd:PRK13637 81 IRKKvglvFQYPEYQLFEETIEKDIafgpINLGLSEEEI--------ENRVKRAMNIVGLDYEDYKDkspfELSGGQKRR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 657198994 165 VALARALACDPDLLLLDEPTNHLDI----DAINWLEEFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:PRK13637 153 VAIAGVVAMEPKILILDEPTAGLDPkgrdEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKC 223
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
321-473 |
5.97e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 71.97 E-value: 5.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRQGTNLEVAYFD-QYREQLD---- 395
Cdd:PRK11231 4 RTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSrQLARRLAllpq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 396 ----PEKTVVdnvgegkQEVMVRGRSRHI-----LGYLQDFLFEPKRART--------PVKALSGGEKNRLLLAKLFLKP 458
Cdd:PRK11231 84 hhltPEGITV-------RELVAYGRSPWLslwgrLSAEDNARVNQAMEQTrinhladrRLTDLSGGQRQRAFLAMVLAQD 156
|
170
....*....|....*
gi 657198994 459 SNLLILDEPTNDLDV 473
Cdd:PRK11231 157 TPVVLLDEPTTYLDI 171
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-184 |
6.00e-14 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 71.55 E-value: 6.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 1 MALLTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQ-QDLkvTRLeqdppASS 79
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDgEDI--TGL-----PPH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 80 EItvfdyAAEGLAgvgellkqyhHVshalahdPSDANI-----------------RTMSQLQEQLDyqngWQYET----- 137
Cdd:COG0410 74 RI-----ARLGIG----------YV-------PEGRRIfpsltveenlllgayarRDRAEVRADLE----RVYELfprlk 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 657198994 138 -RINQVLTlldldpdvtldSLSGGWLRKVALARALACDPDLLLLDEPT 184
Cdd:COG0410 128 eRRRQRAG-----------TLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
321-473 |
6.09e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 70.99 E-value: 6.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLEvAYFDQYREQL----- 394
Cdd:PRK13538 3 EARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLwQGEPIR-RQRDEYHQDLlylgh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 395 ----DPEKTVVDNV-------GEGKQEVMVRGRSRHILGylqdflfepKRARTPVKALSGGEKNRLLLAKLFLKPSNLLI 463
Cdd:PRK13538 82 qpgiKTELTALENLrfyqrlhGPGDDEALWEALAQVGLA---------GFEDVPVRQLSAGQQRRVALARLWLTRAPLWI 152
|
170
....*....|
gi 657198994 464 LDEPTNDLDV 473
Cdd:PRK13538 153 LDEPFTAIDK 162
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
323-472 |
6.65e-14 |
|
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: 71.55 E-value: 6.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 323 EGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRqgtnlevaYFDQYREQLDPEK---- 398
Cdd:COG1127 9 RNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEIL--------VDGQDITGLSEKElyel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 399 -----------------TVVDNVG------EGKQEVMVRGRSRHIL---GyLQDFlfepkRARTPvKALSGGEKNRLLLA 452
Cdd:COG1127 81 rrrigmlfqggalfdslTVFENVAfplrehTDLSEAEIRELVLEKLelvG-LPGA-----ADKMP-SELSGGMRKRVALA 153
|
170 180
....*....|....*....|.
gi 657198994 453 K-LFLKPSnLLILDEPTNDLD 472
Cdd:COG1127 154 RaLALDPE-ILLYDEPTAGLD 173
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
17-183 |
6.67e-14 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 71.42 E-value: 6.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 17 PLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRlVLQQDLKVTRLEQDPPASseitvfdyaaeglAGVGe 96
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGK-ILLDGQDITKLPMHKRAR-------------LGIG- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 97 llkqYhhvshaLAHDPS-------DANIRTMSQLQEQLDyqngWQYETRINQVLTLLDLDP--DVTLDSLSGGWLRKVAL 167
Cdd:cd03218 79 ----Y------LPQEASifrkltvEENILAVLEIRGLSK----KEREEKLEELLEEFHITHlrKSKASSLSGGERRRVEI 144
|
170
....*....|....*.
gi 657198994 168 ARALACDPDLLLLDEP 183
Cdd:cd03218 145 ARALATNPKFLLLDEP 160
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
338-472 |
7.41e-14 |
|
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: 71.49 E-value: 7.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 338 LDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLEVAYFDQYREQL-----DP---EKTVVDNVGEGK 408
Cdd:cd03251 21 ISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILiDGHDVRDYTLASLRRQIglvsqDVflfNDTVAENIAYGR 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 657198994 409 QEVM---VRGRSRhiLGYLQDFLFE-PKRARTPVK----ALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:cd03251 101 PGATreeVEEAAR--AANAHEFIMElPEGYDTVIGergvKLSGGQRQRIAIARALLKDPPILILDEATSALD 170
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
319-472 |
9.63e-14 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 70.84 E-value: 9.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 319 VFETEGLGLDFGD----RTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNL----------- 382
Cdd:COG1136 4 LLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLiDGQDIsslserelarl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 383 ---EVAY-FDQYreQLDPEKTVVDNV-------GEGKQEvmVRGRSRHILGYLQdfLfePKRARTPVKALSGGEKNRLLL 451
Cdd:COG1136 84 rrrHIGFvFQFF--NLLPELTALENValplllaGVSRKE--RRERARELLERVG--L--GDRLDHRPSQLSGGQQQRVAI 155
|
170 180
....*....|....*....|..
gi 657198994 452 AK-LFLKPSnLLILDEPTNDLD 472
Cdd:COG1136 156 ARaLVNRPK-LILADEPTGNLD 176
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
338-473 |
1.18e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 71.12 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 338 LDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASrGSVR-QGTNLEV----------AYFDQ------------YREQL 394
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGS-GSIQfAGQPLEAwsaaelarhrAYLSQqqtppfampvfqYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 395 DPEKTVVDNvgegkqevmvrgrSRHILGYLQDFL-FEPKRARtPVKALSGGEKNRLLLAKLFLK------P-SNLLILDE 466
Cdd:PRK03695 94 QPDKTRTEA-------------VASALNEVAEALgLDDKLGR-SVNQLSGGEWQRVRLAAVVLQvwpdinPaGQLLLLDE 159
|
....*..
gi 657198994 467 PTNDLDV 473
Cdd:PRK03695 160 PMNSLDV 166
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-229 |
1.54e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 72.56 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 3 LLTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQ-QDLKVTrleqdPPASSEI 81
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDgVDLSHV-----PPYQRPI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 82 TvfdyaaeglagvgeLLKQyhhvSHAL-AHDPSDANIrTMSQLQEQLDYQngwQYETRINQVLTLLDLDPDVTLD--SLS 158
Cdd:PRK11607 94 N--------------MMFQ----SYALfPHMTVEQNI-AFGLKQDKLPKA---EIASRVNEMLGLVHMQEFAKRKphQLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 159 GGWLRKVALARALACDPDLLLLDEPTNHLD--------IDAINWLEEFlkdfrGAI-VFISHDREFIHKLATRIIDLDRG 229
Cdd:PRK11607 152 GGQRQRVALARSLAKRPKLLLLDEPMGALDkklrdrmqLEVVDILERV-----GVTcVMVTHDQEEAMTMAGRIAIMNRG 226
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-227 |
1.63e-13 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 70.51 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 25 TIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQQDlKVTRLEQDPPASSEITVFDYAAEGLAGVGellkqyhhv 104
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELD-TVSYKPQYIKADYEGTVRDLLSSITKDFY--------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 105 SHAlahdpsdanirtmsqlqeqldyqngwQYETRINQVLTLLDLdPDVTLDSLSGGWLRKVALARALACDPDLLLLDEPT 184
Cdd:cd03237 91 THP--------------------------YFKTEIAKPLQIEQI-LDREVPELSGGELQRVAIAACLSKDADIYLLDEPS 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 657198994 185 NHLDID-------AINWLEEFLKdfRGAIVfISHDREFIHKLATRIIDLD 227
Cdd:cd03237 144 AYLDVEqrlmaskVIRRFAENNE--KTAFV-VEHDIIMIDYLADRLIVFE 190
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
321-473 |
1.64e-13 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 70.91 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRqgtnlevaYFDQYREQLDPEK-- 398
Cdd:COG4559 3 EAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVR--------LNGRPLAAWSPWEla 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 399 ----------------TVvdnvgegkQEVmVR-GRSRHILGYLQDflfePKRART-------------PVKALSGGEKNR 448
Cdd:COG4559 75 rrravlpqhsslafpfTV--------EEV-VAlGRAPHGSSAAQD----RQIVREalalvglahlagrSYQTLSGGEQQR 141
|
170 180 190
....*....|....*....|....*....|..
gi 657198994 449 LLLAKLFL-------KPSNLLILDEPTNDLDV 473
Cdd:COG4559 142 VQLARVLAqlwepvdGGPRWLFLDEPTSALDL 173
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
329-548 |
1.70e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 73.39 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 329 FGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRQGTNLEVAYFDQyrEQLDPEK-TVVDNVGEG 407
Cdd:PRK15064 11 FGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQ--DQFAFEEfTVLDTVIMG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 408 -------KQE------------------------------VMVRGRSRHIL---GYLQDFLFEPKRARTPvkalsgGEKN 447
Cdd:PRK15064 89 htelwevKQErdriyalpemseedgmkvadlevkfaemdgYTAEARAGELLlgvGIPEEQHYGLMSEVAP------GWKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 448 RLLLAK-LFLKPsNLLILDEPTNDLDVETLELLEELLTDYPGTLLLVSHDRRFIdNTVtgCW----LFEGDGRIsdYVGG 522
Cdd:PRK15064 163 RVLLAQaLFSNP-DILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFL-NSV--CThmadLDYGELRV--YPGN 236
|
250 260
....*....|....*....|....*...
gi 657198994 523 YADMMATRALQAAQQTAKPAPVK--VAE 548
Cdd:PRK15064 237 YDEYMTAATQARERLLADNAKKKaqIAE 264
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
321-495 |
1.79e-13 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 69.62 E-value: 1.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLEVA------YFDQYReQ 393
Cdd:cd03269 2 EVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLfDGKPLDIAarnrigYLPEER-G 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 394 LDPEKTVVDNV-------GEGKQEVmvrgrSRHILGYLQDFLFEPKRARtPVKALSGGEKNRLLLAKLFLKPSNLLILDE 466
Cdd:cd03269 81 LYPKMKVIDQLvylaqlkGLKKEEA-----RRRIDEWLERLELSEYANK-RVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190
....*....|....*....|....*....|..
gi 657198994 467 PTNDLDVETLELLEELLTDYPG---TLLLVSH 495
Cdd:cd03269 155 PFSGLDPVNVELLKDVIRELARagkTVILSTH 186
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-231 |
1.93e-13 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 72.03 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 4 LTLHGASLSFS----DFPLLDHAELTIERGERLCLVGRNGAGKSTLMkviaselplddgRLVlqqdlkvTRLEQdpPASS 79
Cdd:COG1135 2 IELENLSKTFPtkggPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLI------------RCI-------NLLER--PTSG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 80 EITVFDYAAEGLAGvGELLKQYHHVS----HAlahdpsdaNI---RTMsqlqeqldYQN--------GWQYETRINQVLT 144
Cdd:COG1135 61 SVLVDGVDLTALSE-RELRAARRKIGmifqHF--------NLlssRTV--------AENvalpleiaGVPKAEIRKRVAE 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 145 LLDLdpdVTL--------DSLSGGWLRKVALARALACDPDLLLLDEPTNHLD---IDAInwLeEFLKDFRG----AIVFI 209
Cdd:COG1135 124 LLEL---VGLsdkadaypSQLSGGQKQRVGIARALANNPKVLLCDEATSALDpetTRSI--L-DLLKDINRelglTIVLI 197
|
250 260
....*....|....*....|..
gi 657198994 210 SHDREFIHKLATRIIDLDRGVI 231
Cdd:COG1135 198 THEMDVVRRICDRVAVLENGRI 219
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
331-472 |
2.15e-13 |
|
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: 73.21 E-value: 2.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 331 DRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGS-VRQGTNLEVAYFDQYREQLDP--------EKTVV 401
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQiLLDGHDLADYTLASLRRQVALvsqdvvlfNDTIA 423
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 657198994 402 DNVGEGKQEVMVRGRSRHIL--GYLQDFLFE-PKRARTPVKA----LSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:TIGR02203 424 NNIAYGRTEQADRAEIERALaaAYAQDFVDKlPLGLDTPIGEngvlLSGGQRQRLAIARALLKDAPILILDEATSALD 501
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
15-232 |
2.83e-13 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 69.48 E-value: 2.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 15 DFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRlvlqqdlkVTRLEQDppaSSEITV---FDYAAEGL 91
Cdd:cd03220 34 EFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGT--------VTVRGRV---SSLLGLgggFNPELTGR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 92 agvgellkqyhhvshalahdpsdANIRTMSQLqeqldyqNGWQYE---TRINQVLTLLDLDPDVTL--DSLSGGWLRKVA 166
Cdd:cd03220 103 -----------------------ENIYLNGRL-------LGLSRKeidEKIDEIIEFSELGDFIDLpvKTYSSGMKARLA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 167 LARALACDPDLLLLDEPT----NHLDIDAINWLEEFLKDFRgAIVFISHDREFIHKLATRIIDLDRGVIT 232
Cdd:cd03220 153 FAIATALEPDILLIDEVLavgdAAFQEKCQRRLRELLKQGK-TVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
4-228 |
3.15e-13 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 69.05 E-value: 3.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 4 LTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLD---DGRLVL-QQDL--------KVTRL 71
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLnGRRLtalpaeqrRIGIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 72 EQDPPASSEITVfdyaAEGLAgvgellkqyhhvsHALAHDPSDANIRTmsqlqeqldyqngwqyetRINQVLTLLDL--- 148
Cdd:COG4136 82 FQDDLLFPHLSV----GENLA-------------FALPPTIGRAQRRA------------------RVEQALEEAGLagf 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 149 ---DPDvtldSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEF----LKDFRGAIVFISHDREFIhKLAT 221
Cdd:COG4136 127 adrDPA----TLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFvfeqIRQRGIPALLVTHDEEDA-PAAG 201
|
....*..
gi 657198994 222 RIIDLDR 228
Cdd:COG4136 202 RVLDLGN 208
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
323-472 |
3.18e-13 |
|
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: 69.14 E-value: 3.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 323 EGLGLDFGDRTLFQGLDLQVLRGdKIALVGPNGCGKSTLIKLLMGQLEASRGSVRqgtnlevayFDQYreqldpektvvd 402
Cdd:cd03264 4 ENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIR---------IDGQ------------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 403 NVGEGKQEVmvrgrsRHILGYL-QDFLFEPK------------------------------------RARTPVKALSGGE 445
Cdd:cd03264 62 DVLKQPQKL------RRRIGYLpQEFGVYPNftvrefldyiawlkgipskevkarvdevlelvnlgdRAKKKIGSLSGGM 135
|
170 180
....*....|....*....|....*..
gi 657198994 446 KNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:cd03264 136 RRRVGIAQALVGDPSILIVDEPTAGLD 162
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-224 |
3.49e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 70.93 E-value: 3.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 1 MALLTLHGASLSFSD----FPLLDHAELTIERGERLCLVGRNGAGKS----TLM-------KVIASELPLDdgrlvlQQD 65
Cdd:PRK11022 1 MALLNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSvsslAIMglidypgRVMAEKLEFN------GQD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 66 L-KVTRLEQDPPASSEIT-VFDYAAEGLagvgellkqyhhvshalahDPSdaniRTMS-QLQEQLDYQNGWQYETRINQV 142
Cdd:PRK11022 75 LqRISEKERRNLVGAEVAmIFQDPMTSL-------------------NPC----YTVGfQIMEAIKVHQGGNKKTRRQRA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 143 LTLLDL----DPDVTLD----SLSGGWLRKVALARALACDPDLLLLDEPTNHLD--IDA--INWLEEFLKDFRGAIVFIS 210
Cdd:PRK11022 132 IDLLNQvgipDPASRLDvyphQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDvtIQAqiIELLLELQQKENMALVLIT 211
|
250
....*....|....
gi 657198994 211 HDREFIHKLATRII 224
Cdd:PRK11022 212 HDLALVAEAAHKII 225
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
24-284 |
3.53e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 69.87 E-value: 3.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 24 LTIERGERLCLVGRNGAGKSTLMKVIASELP-----LDDGRLVLQ---QDLKVTR--LEQDPPASSEITVFDYAAEGLAG 93
Cdd:COG4138 17 AQVNAGELIHLIGPNGAGKSTLLARMAGLLPgqgeiLLNGRPLSDwsaAELARHRayLSQQQSPPFAMPVFQYLALHQPA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 94 VGellkqyhhvshalahdPSDANIRTMSQLQEQLDYQNgwQYETRINQvltlldldpdvtldsLSGG-WLRkVALARAL- 171
Cdd:COG4138 97 GA----------------SSEAVEQLLAQLAEALGLED--KLSRPLTQ---------------LSGGeWQR-VRLAAVLl 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 172 ----ACDPD--LLLLDEPTNHLDI------DaiNWLEEFlKDFRGAIVFISHDreFIHKL--ATRIIDLDRGVITSwpgn 237
Cdd:COG4138 143 qvwpTINPEgqLLLLDEPMNSLDVaqqaalD--RLLREL-CQQGITVVMSSHD--LNHTLrhADRVWLLKQGKLVA---- 213
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 657198994 238 ydeylQGK-EEWLRVEELKNAeFdrklaqeevwvrqGIKARRTRNEGR 284
Cdd:COG4138 214 -----SGEtAEVMTPENLSEV-F-------------GVKFRRLEVEGH 242
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-231 |
3.67e-13 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 69.64 E-value: 3.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 3 LLTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQqDLKVTRLEQDPPA-SSEI 81
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVD-GEDLTDSKKDINKlRRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 82 -------------TVFDYAAEGLAGVgellkqyHHVSHAlahdpsDANIRTMSQLQ-----EQLDyqngwQYetrinqvl 143
Cdd:COG1126 80 gmvfqqfnlfphlTVLENVTLAPIKV-------KKMSKA------EAEERAMELLErvglaDKAD-----AY-------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 144 tlldldPDvtldSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRGA---IVFISHDREFIHKLA 220
Cdd:COG1126 134 ------PA----QLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEgmtMVVVTHEMGFAREVA 203
|
250
....*....|.
gi 657198994 221 TRIIDLDRGVI 231
Cdd:COG1126 204 DRVVFMDGGRI 214
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
10-233 |
3.70e-13 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 71.30 E-value: 3.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 10 SLSFS----DFPLldHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLqqdlkvtrleqdppasSEITVFD 85
Cdd:TIGR02142 2 SARFSkrlgDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVL----------------NGRTLFD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 86 yAAEGLagvgELLKQYHHVSHALahdpSDANIRTMSQLQEQLDY----QNGWQYETRINQVLTLLDLDP--DVTLDSLSG 159
Cdd:TIGR02142 64 -SRKGI----FLPPEKRRIGYVF----QEARLFPHLSVRGNLRYgmkrARPSERRISFERVIELLGIGHllGRLPGRLSG 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 657198994 160 GWLRKVALARALACDPDLLLLDEPTNHLDI----DAINWLEEFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITS 233
Cdd:TIGR02142 135 GEKQRVAIGRALLSSPRLLLMDEPLAALDDprkyEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAA 212
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
3-231 |
5.71e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 69.47 E-value: 5.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 3 LLTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLD--------------DGRLVLQQD-LK 67
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvtgdvtlNGEPLAAIDaPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 68 VTRLEQDPPASSEiTVFDYAAEGLAgvgeLLKQYHHVSHALAHDPSDANIrtmsqlqeqldyqngwqyetrINQVLTLLD 147
Cdd:PRK13547 81 LARLRAVLPQAAQ-PAFAFSAREIV----LLGRYPHARRAGALTHRDGEI---------------------AWQALALAG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 148 LDP----DVTldSLSGGWLRKVALARALA---------CDPDLLLLDEPTNHLDIDAINWLEEFL----KDFRGAIVFIS 210
Cdd:PRK13547 135 ATAlvgrDVT--TLSGGELARVQFARVLAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVrrlaRDWNLGVLAIV 212
|
250 260
....*....|....*....|.
gi 657198994 211 HDREFIHKLATRIIDLDRGVI 231
Cdd:PRK13547 213 HDPNLAARHADRIAMLADGAI 233
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
320-472 |
5.91e-13 |
|
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: 68.75 E-value: 5.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 320 FETEGLGLDFGD-RTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSV----RQGTNLEVAYFDQYREQ- 393
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVlidgTDINKLKGKALRQLRRQi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 394 --------LDPEKTVVDNVGEGKQEVMVRGRS----------RHILGYLQDFLFEPKrARTPVKALSGGEKNRLLLAKLF 455
Cdd:cd03256 81 gmifqqfnLIERLSVLENVLSGRLGRRSTWRSlfglfpkeekQRALAALERVGLLDK-AYQRADQLSGGQQQRVAIARAL 159
|
170
....*....|....*..
gi 657198994 456 LKPSNLLILDEPTNDLD 472
Cdd:cd03256 160 MQQPKLILADEPVASLD 176
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
338-472 |
6.43e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 71.80 E-value: 6.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 338 LDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLeASRGSVR-QGTNLEVAYFDQYREQLD--------PEKTVVDNVGEGK 408
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKiNGIELRELDPESWRKHLSwvgqnpqlPHGTLRDNVLLGN 447
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 657198994 409 QEvMVRGRSRHIL--GYLQDFLFE-PKRARTPVK----ALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:PRK11174 448 PD-ASDEQLQQALenAWVSEFLPLlPQGLDTPIGdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
15-231 |
6.72e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 68.95 E-value: 6.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 15 DFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLV--------------LQQDL-------------K 67
Cdd:COG1134 38 EFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEvngrvsallelgagFHPELtgreniylngrllG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 68 VTRLEQDPpasseitVFDYAAEgLAGVGELLkqyhhvshalahdpsDANIRTMSqlqeqldyqngwqyetrinqvltlld 147
Cdd:COG1134 118 LSRKEIDE-------KFDEIVE-FAELGDFI---------------DQPVKTYS-------------------------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 148 ldpdvtldslSGGWLRkVALARALACDPDLLLLDEPTNHLDID----AINWLEEFLKDFRgAIVFISHDREFIHKLATRI 223
Cdd:COG1134 149 ----------SGMRAR-LAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIRELRESGR-TVIFVSHSMGAVRRLCDRA 216
|
....*...
gi 657198994 224 IDLDRGVI 231
Cdd:COG1134 217 IWLEKGRL 224
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
25-192 |
7.13e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 67.98 E-value: 7.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 25 TIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLqqdlkvtrleqdppASSEITVFDYAAeglagvgellkqyhhV 104
Cdd:PRK13539 24 TLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKL--------------DGGDIDDPDVAE---------------A 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 105 SHALAHdpSDANIRTMSqLQEQLDYqngW-----QYETRINQVLTLLDLDP--DVTLDSLSGGWLRKVALARALACDPDL 177
Cdd:PRK13539 75 CHYLGH--RNAMKPALT-VAENLEF---WaaflgGEELDIAAALEAVGLAPlaHLPFGYLSAGQKRRVALARLLVSNRPI 148
|
170
....*....|....*
gi 657198994 178 LLLDEPTNHLDIDAI 192
Cdd:PRK13539 149 WILDEPTAALDAAAV 163
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
328-473 |
7.68e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 68.71 E-value: 7.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 328 DFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGqLEASRGSVR-QGTNLEV----------AYFDQ------- 389
Cdd:COG4138 5 DVAVAGRLGPISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILlNGRPLSDwsaaelarhrAYLSQqqsppfa 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 390 -----YREQLDPEKTVVDNVgegKQEVMvrgrsrHILGYLQdflFEPKRARtPVKALSGGEKNRLLLAKLFLK------- 457
Cdd:COG4138 84 mpvfqYLALHQPAGASSEAV---EQLLA------QLAEALG---LEDKLSR-PLTQLSGGEWQRVRLAAVLLQvwptinp 150
|
170
....*....|....*.
gi 657198994 458 PSNLLILDEPTNDLDV 473
Cdd:COG4138 151 EGQLLLLDEPMNSLDV 166
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
11-232 |
7.69e-13 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 71.35 E-value: 7.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 11 LSFS---DFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGR-LVLQQDLKVTRLE----------QDPp 76
Cdd:COG1132 345 VSFSypgDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRiLIDGVDIRDLTLEslrrqigvvpQDT- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 77 asseiTVFD--------YAAEG--LAGVGELLKQyhhvshALAHDpsdaNIRTMSQlqeqldyqngwQYETRINQ--Vlt 144
Cdd:COG1132 424 -----FLFSgtirenirYGRPDatDEEVEEAAKA------AQAHE----FIEALPD-----------GYDTVVGErgV-- 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 145 lldldpdvtldSLSGGWLRKVALARALACDPDLLLLDEPTNHLD-------IDAinwLEEFLKDfRGAIVfIShdrefiH 217
Cdd:COG1132 476 -----------NLSGGQRQRIAIARALLKDPPILILDEATSALDtetealiQEA---LERLMKG-RTTIV-IA------H 533
|
250 260
....*....|....*....|
gi 657198994 218 KLAT-----RIIDLDRGVIT 232
Cdd:COG1132 534 RLSTirnadRILVLDDGRIV 553
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-229 |
7.87e-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: 68.26 E-value: 7.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 19 LDHAELTIERGERLCLVGRNGAGKSTLMKVIAS-ELPLDDGrlVLQQDLKVTRleqdpPASSEITVF-DYAAEGLAGVGE 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGlAQPTSGG--VILEGKQITE-----PGPDRMVVFqNYSLLPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 97 LLkqyhhvshALAHDpsdaniRTMSQLQEQldyqngwQYETRINQVLTLLDLD--PDVTLDSLSGGWLRKVALARALACD 174
Cdd:TIGR01184 74 NI--------ALAVD------RVLPDLSKS-------ERRAIVEEHIALVGLTeaADKRPGQLSGGMKQRVAIARALSIR 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 657198994 175 PDLLLLDEPTNHLD-IDAINWLEEFLK---DFRGAIVFISHDREFIHKLATRIIDLDRG 229
Cdd:TIGR01184 133 PKVLLLDEPFGALDaLTRGNLQEELMQiweEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
321-472 |
8.56e-13 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 68.23 E-value: 8.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 321 ETEGLGLDF-----GDRTL--FQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRqgtnlevayfdqYREQ 393
Cdd:COG4778 6 EVENLSKTFtlhlqGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIL------------VRHD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 394 ldpeKTVVDNVGEGKQEVM-VRgrsRHILGYLQDFL--------------------FEPKRARTPVKAL----------- 441
Cdd:COG4778 74 ----GGWVDLAQASPREILaLR---RRTIGYVSQFLrviprvsaldvvaepllergVDREEARARARELlarlnlperlw 146
|
170 180 190
....*....|....*....|....*....|....*...
gi 657198994 442 -------SGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:COG4778 147 dlppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLD 184
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
336-500 |
1.01e-12 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 68.13 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 336 QGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRqgtnleVAYFDQYREQldpeKTVVDNVGegkqeVMVRG 415
Cdd:cd03267 38 KGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVR------VAGLVPWKRR----KKFLRRIG-----VVFGQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 416 RS---------------RHILGyLQDFLFEPKRAR------------TPVKALSGGEKNRLLLAKLFLKPSNLLILDEPT 468
Cdd:cd03267 103 KTqlwwdlpvidsfyllAAIYD-LPPARFKKRLDElselldleelldTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
170 180 190
....*....|....*....|....*....|....*.
gi 657198994 469 NDLDVETLEL----LEELLTDYPGTLLLVSHDRRFI 500
Cdd:cd03267 182 IGLDVVAQENirnfLKEYNRERGTTVLLTSHYMKDI 217
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-604 |
1.01e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 71.04 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 3 LLTLHGASLSFSD----FPLLDHAELTIERGERLCLVGRNGAGKS----TLMKVI--ASELPLDDGRLVLQQDLKVTRL- 71
Cdd:PRK10261 12 VLAVENLNIAFMQeqqkIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGLVQCDKMLLRRRSRQVIELs 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 72 EQDPPASSEITVFDYA---AEGLAG------VGELLKQYHHVSHALAHDpsdaniRTMSQLQEQLDyqngwqyETRINQV 142
Cdd:PRK10261 92 EQSAAQMRHVRGADMAmifQEPMTSlnpvftVGEQIAESIRLHQGASRE------EAMVEAKRMLD-------QVRIPEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 143 LTLLDLDPDvtldSLSGGWLRKVALARALACDPDLLLLDEPTNHLDI----DAINWLEEFLKDFRGAIVFISHDREFIHK 218
Cdd:PRK10261 159 QTILSRYPH----QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVtiqaQILQLIKVLQKEMSMGVIFITHDMGVVAE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 219 LATRIIDLDRGVITswpgnydeylqgkeEWLRVEELKNAEfdrklaqEEVWVRQGIKArrtrnegrVRALKAMR------ 292
Cdd:PRK10261 235 IADRVLVMYQGEAV--------------ETGSVEQIFHAP-------QHPYTRALLAA--------VPQLGAMKgldypr 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 293 ------MERTQRRELQGKAKLQLDeagrsGKLVFETEGLGLDFGDRTlfqGLDLQVLR--------------GDKIALVG 352
Cdd:PRK10261 286 rfplisLEHPAKQEPPIEQDTVVD-----GEPILQVRNLVTRFPLRS---GLLNRVTRevhavekvsfdlwpGETLSLVG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 353 PNGCGKSTLIKLLMGQLEASRGSV-----RQGT-----------NLEVAYFDQYrEQLDPEKTVVDNVGEG-KQEVMVRG 415
Cdd:PRK10261 358 ESGSGKSTTGRALLRLVESQGGEIifngqRIDTlspgklqalrrDIQFIFQDPY-ASLDPRQTVGDSIMEPlRVHGLLPG 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 416 RS--RHILGYLQDFLFEPKRARTPVKALSGGEKNRLLLAK-LFLKPsNLLILDEPTNDLDVETLELLEELLTDYPGTL-- 490
Cdd:PRK10261 437 KAaaARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARaLALNP-KVIIADEAVSALDVSIRGQIINLLLDLQRDFgi 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 491 --LLVSHDRRFIDntvtgcwlfegdgRISD-----YVGGYADMMATRALQAAQQTAKPAPVKVAEPVASAAEPAKKTRKL 563
Cdd:PRK10261 516 ayLFISHDMAVVE-------------RISHrvavmYLGQIVEIGPRRAVFENPQHPYTRKLMAAVPVADPSRQRPQRVLL 582
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 657198994 564 SyklqlelDNLPARLEQLEMELDALQAEINHPGFFSLPAEQ 604
Cdd:PRK10261 583 S-------DDLPSNIHLRGEEVAAVSLQCVGPGHYVAQPQS 616
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
309-516 |
1.14e-12 |
|
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: 67.56 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 309 LDEAGRSGKLVFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSV-RQGT---NLEV 384
Cdd:cd03220 12 TYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVtVRGRvssLLGL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 385 AYFdqyreqLDPEKTVVDNV-------GEGKQEvmVRGRSRHILGY--LQDFLfepkraRTPVKALSGGEKNRLLLA-KL 454
Cdd:cd03220 92 GGG------FNPELTGRENIylngrllGLSRKE--IDEKIDEIIEFseLGDFI------DLPVKTYSSGMKARLAFAiAT 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 657198994 455 FLKPsNLLILDEPTNDLDVETL---ELLEELLTDYPGTLLLVSHDRRFIDNTVT-GCWLFegDGRI 516
Cdd:cd03220 158 ALEP-DILLIDEVLAVGDAAFQekcQRRLRELLKQGKTVILVSHDPSSIKRLCDrALVLE--KGKI 220
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-232 |
1.20e-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: 66.57 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 4 LTLHGASLSF--SDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIAselplddGRLVLQQdlkvtrleqdppassei 81
Cdd:cd03247 1 LSINNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLT-------GDLKPQQ----------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 82 tvfdyaaeglagvGELLKQYHHVShalahdpsdanirtmsQLQEQLDyqngwQYETRINQVLTLLDldpdVTLDS----- 156
Cdd:cd03247 57 -------------GEITLDGVPVS----------------DLEKALS-----SLISVLNQRPYLFD----TTLRNnlgrr 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 157 LSGGWLRKVALARALACDPDLLLLDEPTNHLD----IDAINWLEEFLKDfrGAIVFISHDREFIHKlATRIIDLDRGVIT 232
Cdd:cd03247 99 FSGGERQRLALARILLQDAPIVLLDEPTVGLDpiteRQLLSLIFEVLKD--KTLIWITHHLTGIEH-MDKILFLENGKII 175
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
10-229 |
1.25e-12 |
|
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: 69.74 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 10 SLSFSDFPLldHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRL-----VLQQDLKVTRLeqdPPASSEI-TV 83
Cdd:COG4148 8 RLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIrlggeVLQDSARGIFL---PPHRRRIgYV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 84 FDYAAeglagvgeLLkqyHHVShalahdpsdanirtmsqLQEQLDY--QNGWQYETRI--NQVLTLLDLDP--DVTLDSL 157
Cdd:COG4148 83 FQEAR--------LF---PHLS-----------------VRGNLLYgrKRAPRAERRIsfDEVVELLGIGHllDRRPATL 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 657198994 158 SGGWLRKVALARALACDPDLLLLDEPTNHLDIDA----INWLEEFLKDFRGAIVFISHDREFIHKLATRIIDLDRG 229
Cdd:COG4148 135 SGGERQRVAIGRALLSSPRLLLMDEPLAALDLARkaeiLPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQG 210
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
25-229 |
1.43e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.50 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 25 TIERGERLCLVGRNGAGKST----LMKVIASE-------LPLDdgRLVLQQDLKVTR----LEQDPPAS--SEITVFDYA 87
Cdd:PRK15134 308 TLRPGETLGLVGESGSGKSTtglaLLRLINSQgeiwfdgQPLH--NLNRRQLLPVRHriqvVFQDPNSSlnPRLNVLQII 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 88 AEGLagvgellkQYHHvshalahdpsdaniRTMSQLQEqldyqngwqyETRINQVLTLLDLDPDVTL---DSLSGGWLRK 164
Cdd:PRK15134 386 EEGL--------RVHQ--------------PTLSAAQR----------EQQVIAVMEEVGLDPETRHrypAEFSGGQRQR 433
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 657198994 165 VALARALACDPDLLLLDEPTNHLD--IDA--INWLEEFLKDFRGAIVFISHDREFIHKLATRIIDLDRG 229
Cdd:PRK15134 434 IAIARALILKPSLIILDEPTSSLDktVQAqiLALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQG 502
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-229 |
1.50e-12 |
|
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: 66.30 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 2 ALLTLHGASLSfsdfPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLqqdlkvtrleqdppASSEI 81
Cdd:cd03215 3 PVLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITL--------------DGKPV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 82 TVFDYAAEGLAGVGellkqyhHVS-----HALAHDpsdanirtMSqlqeqldyqngwqyeTRINQVLTLLdldpdvtlds 156
Cdd:cd03215 65 TRRSPRDAIRAGIA-------YVPedrkrEGLVLD--------LS---------------VAENIALSSL---------- 104
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 657198994 157 LSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFR---GAIVFISHDREFIHKLATRIIDLDRG 229
Cdd:cd03215 105 LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELAdagKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-233 |
1.90e-12 |
|
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: 67.07 E-value: 1.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 2 ALLTLHGASLSFSD----FPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIAS-ELPlDDGRLVLQ-QDLkvTRLEQDP 75
Cdd:COG4181 7 PIIELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGlDRP-TSGTVRLAgQDL--FALDEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 76 PA--------------------------------SSEITVFDYAAEGLAGVGellkqyhhVSHALAHDPSdanirtmsql 123
Cdd:COG4181 84 RArlrarhvgfvfqsfqllptltalenvmlplelAGRRDARARARALLERVG--------LGHRLDHYPA---------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 124 qeqldyqngwqyetrinqvltlldldpdvtldSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDA----INWLEEFL 199
Cdd:COG4181 146 --------------------------------QLSGGEQQRVALARAFATEPAILFADEPTGNLDAATgeqiIDLLFELN 193
|
250 260 270
....*....|....*....|....*....|....*..
gi 657198994 200 KDFRGAIVFISHDREfihkLAT---RIIDLDRGVITS 233
Cdd:COG4181 194 RERGTTLVLVTHDPA----LAArcdRVLRLRAGRLVE 226
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
335-531 |
1.94e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 67.41 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 335 FQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRqgTN------LEV-AYFdqyreqlDPEKTVVDNV--- 404
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE--VNgrvsalLELgAGF-------HPELTGRENIyln 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 405 ----GEGKQEvmVRGRSRHILGY--LQDFLfepkraRTPVKALSGGEKNRLLLA-KLFLKPsNLLILDEPT--------- 468
Cdd:COG1134 113 grllGLSRKE--IDEKFDEIVEFaeLGDFI------DQPVKTYSSGMRARLAFAvATAVDP-DILLVDEVLavgdaafqk 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 657198994 469 ------NDLdvetlelleellTDYPGTLLLVSHDRRFIDNTVT-GCWLFEG----DGRISDYVGGYADMMATRA 531
Cdd:COG1134 184 kclariREL------------RESGRTVIFVSHSMGAVRRLCDrAIWLEKGrlvmDGDPEEVIAAYEALLAGRE 245
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
325-496 |
2.08e-12 |
|
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: 66.93 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 325 LGLDFGDRTLFQGLDLQ-VLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSV----------RQGTNL-----EVAY-F 387
Cdd:cd03297 2 LCVDIEKRLPDFTLKIDfDLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngtvlfdsRKKINLppqqrKIGLvF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 388 DQYreQLDPEKTVVDNV--GEGKQEVMV-RGRSRHILGYLQ-DFLfepkrARTPVKALSGGEKNRLLLAKLFLKPSNLLI 463
Cdd:cd03297 82 QQY--ALFPHLNVRENLafGLKRKRNREdRISVDELLDLLGlDHL-----LNRYPAQLSGGEKQRVALARALAAQPELLL 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 657198994 464 LDEPTNDLDVETLELLEEL----LTDYPGTLLLVSHD 496
Cdd:cd03297 155 LDEPFSALDRALRLQLLPElkqiKKNLNIPVIFVTHD 191
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
321-473 |
2.17e-12 |
|
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: 66.98 E-value: 2.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 321 ETEGLGLDFGDRTLfQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QG---TNL-----EVAYFDQyR 391
Cdd:cd03299 2 KVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILlNGkdiTNLppekrDISYVPQ-N 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 392 EQLDPEKTVVDNVGEG--KQEVMVRGRSRHILGYLQDFLFEPKRARTPvKALSGGEKNRLLLAK-LFLKPSnLLILDEPT 468
Cdd:cd03299 80 YALFPHMTVYKNIAYGlkKRKVDKKEIERKVLEIAEMLGIDHLLNRKP-ETLSGGEQQRVAIARaLVVNPK-ILLLDEPF 157
|
....*
gi 657198994 469 NDLDV 473
Cdd:cd03299 158 SALDV 162
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
15-233 |
2.41e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 68.11 E-value: 2.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 15 DFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQqDLKVtrleqdPPASSEIT-VFDYAAEglAG 93
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVG-DYAI------PANLKKIKeVKRLRKE--IG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 94 VGELLKQYHHVSHALAHDPSDANIRTMSQLQEQldYQngwqyetRINQVLTLLDLDPDVTLDS---LSGGWLRKVALARA 170
Cdd:PRK13645 94 LVFQFPEYQLFQETIEKDIAFGPVNLGENKQEA--YK-------KVPELLKLVQLPEDYVKRSpfeLSGGQKRRVALAGI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 657198994 171 LACDPDLLLLDEPTNHLDI----DAINWLEEFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITS 233
Cdd:PRK13645 165 IAMDGNTLVLDEPTGGLDPkgeeDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVIS 231
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
15-231 |
2.44e-12 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 69.75 E-value: 2.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 15 DFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQ----QDLKVTRLE-QDPPASSEITVFD---- 85
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDghdlADYTLASLRrQVALVSQDVVLFNdtia 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 86 ----YAAEGLAGVGEllkqyhhVSHALAhdpsDANirtmsqLQEQLD-YQNGWQYETRINQVLtlldldpdvtldsLSGG 160
Cdd:TIGR02203 424 nniaYGRTEQADRAE-------IERALA----AAY------AQDFVDkLPLGLDTPIGENGVL-------------LSGG 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 657198994 161 WLRKVALARALACDPDLLLLDEPTNHLD------IDAInwLEEFLKDfRGAIVfISHDREFIHKlATRIIDLDRGVI 231
Cdd:TIGR02203 474 QRQRLAIARALLKDAPILILDEATSALDneserlVQAA--LERLMQG-RTTLV-IAHRLSTIEK-ADRIVVMDDGRI 545
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-212 |
2.56e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 67.23 E-value: 2.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 1 MALLTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQQDlkvtrleqdppassE 80
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDE--------------D 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 81 ITVFDYAAEGLAGVGELLKQYHHVSHALAHDpsdaNIRTMSQLQEQLDYQngwQYETRINQVLTLLDLD--PDVTLDSLS 158
Cdd:PRK10895 67 ISLLPLHARARRGIGYLPQEASIFRRLSVYD----NLMAVLQIRDDLSAE---QREDRANELMEEFHIEhlRDSMGQSLS 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 657198994 159 GGWLRKVALARALACDPDLLLLDEPTNHLD----IDaINWLEEFLKDFRGAIVFISHD 212
Cdd:PRK10895 140 GGERRRVEIARALAANPKFILLDEPFAGVDpisvID-IKRIIEHLRDSGLGVLITDHN 196
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-189 |
2.86e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 67.35 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 4 LTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIAselplddgRLVLQQDLKVTRLEQDppasseitV 83
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFA--------RLLTPQSGTVFLGDKP--------I 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 84 FDYAAEGLAGVGELLKQyHHVShalahdPSDANIRtmsQLQE--QLDYQNGW-----QYETRINQVL--TLLDLDPDVTL 154
Cdd:PRK11231 67 SMLSSRQLARRLALLPQ-HHLT------PEGITVR---ELVAygRSPWLSLWgrlsaEDNARVNQAMeqTRINHLADRRL 136
|
170 180 190
....*....|....*....|....*....|....*
gi 657198994 155 DSLSGGWLRKVALARALACDPDLLLLDEPTNHLDI 189
Cdd:PRK11231 137 TDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDI 171
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-231 |
2.97e-12 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 66.01 E-value: 2.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 4 LTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIA--SELPLDDGRLVLQ-QDLKvtrleqdppassE 80
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMghPKYEVTEGEILFKgEDIT------------D 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 81 ITVFDYAAEGLagvgellkqyhhvshalahdpsdanirTMSqlqeqldyqngWQYETRINQVlTLLDLDPDVTlDSLSGG 160
Cdd:cd03217 69 LPPEERARLGI---------------------------FLA-----------FQYPPEIPGV-KNADFLRYVN-EGFSGG 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 657198994 161 WLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRG---AIVFISHDREFI-HKLATRIIDLDRGVI 231
Cdd:cd03217 109 EKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREegkSVLIITHYQRLLdYIKPDRVHVLYDGRI 183
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-472 |
3.17e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 69.35 E-value: 3.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 1 MALLTLHGASLSFS----DFPLLDHAELTIERGERLCLVGRNGAGKStlmkVIAselplddgrlvlqqdLKVTRLEQDPP 76
Cdd:PRK15134 3 QPLLAIENLSVAFRqqqtVRTVVNDVSLQIEAGETLALVGESGSGKS----VTA---------------LSILRLLPSPP 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 77 ASSEITVFDYAAEGLAGVGE------------LLKQYHHVSHALAHdpsdaNIRtmSQLQEQLDYQNGWQYETRINQVLT 144
Cdd:PRK15134 64 VVYPSGDIRFHGESLLHASEqtlrgvrgnkiaMIFQEPMVSLNPLH-----TLE--KQLYEVLSLHRGMRREAARGEILN 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 145 LLDL----DPDVTLD----SLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRG----AIVFISHD 212
Cdd:PRK15134 137 CLDRvgirQAAKRLTdyphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelnmGLLFITHN 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 213 REFIHKLATRIIDLDRG----------------------VITSWPGNYDEYL-QGKEEWLRVEELKNAeFDrklaqeevw 269
Cdd:PRK15134 217 LSIVRKLADRVAVMQNGrcveqnraatlfsapthpytqkLLNSEPSGDPVPLpEPASPLLDVEQLQVA-FP--------- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 270 VRQGIKARRTrnegrvralkamrmertqrrelqgkaklqldeagrsgklvfeteglgldfGDRTLFQGLDLQVLRGDKIA 349
Cdd:PRK15134 287 IRKGILKRTV--------------------------------------------------DHNVVVKNISFTLRPGETLG 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 350 LVGPNGCGKST----LIKLLmgqleASRGSV------------RQ----GTNLEVAYFDQYrEQLDPEKTVVDNVGEGKQ 409
Cdd:PRK15134 317 LVGESGSGKSTtglaLLRLI-----NSQGEIwfdgqplhnlnrRQllpvRHRIQVVFQDPN-SSLNPRLNVLQIIEEGLR 390
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 657198994 410 ----EVMVRGRSRHILGYLQDFLFEPK-RARTPvKALSGGEKNRLLLAK-LFLKPSnLLILDEPTNDLD 472
Cdd:PRK15134 391 vhqpTLSAAQREQQVIAVMEEVGLDPEtRHRYP-AEFSGGQRQRIAIARaLILKPS-LIILDEPTSSLD 457
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-231 |
3.64e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 68.13 E-value: 3.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 1 MALLTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASelpLDDgrlVLQQDLKV--TRLEQDPPAS 78
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAG---LED---ITSGDLFIgeKRMNDVPPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 79 SEI-TVF-DYAAeglagvgellkqYHHVSHAlahdpsdaniRTMSqLQEQLDYQNGWQYETRINQVLTLLDLDPdvTLD- 155
Cdd:PRK11000 75 RGVgMVFqSYAL------------YPHLSVA----------ENMS-FGLKLAGAKKEEINQRVNQVAEVLQLAH--LLDr 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 156 ---SLSGGWLRKVALARALACDPDLLLLDEPTNHLD--------IDaINWLEeflKDFRGAIVFISHDREFIHKLATRII 224
Cdd:PRK11000 130 kpkALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaalrvqmrIE-ISRLH---KRLGRTMIYVTHDQVEAMTLADKIV 205
|
....*..
gi 657198994 225 DLDRGVI 231
Cdd:PRK11000 206 VLDAGRV 212
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
24-231 |
3.78e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 67.80 E-value: 3.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 24 LTIERGERLCLVGRNGAGKSTLMKVIAselplddGRLVlqqdlkvtrleqdpPASSEITVFDY----------------- 86
Cdd:COG4586 43 FTIEPGEIVGFIGPNGAGKSTTIKMLT-------GILV--------------PTSGEVRVLGYvpfkrrkefarrigvvf 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 87 -----------AAEGLagvgELLKQYHHVSHAlahdpsdanirtmsqlqeqldyqngwQYETRINQVLTLLDLDP--DVT 153
Cdd:COG4586 102 gqrsqlwwdlpAIDSF----RLLKAIYRIPDA--------------------------EYKKRLDELVELLDLGEllDTP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 154 LDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDF---RGAIVFI-SHDREFIHKLATRIIDLDRG 229
Cdd:COG4586 152 VRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnreRGTTILLtSHDMDDIEALCDRVIVIDHG 231
|
..
gi 657198994 230 VI 231
Cdd:COG4586 232 RI 233
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
6-230 |
4.46e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 67.93 E-value: 4.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 6 LHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGrlvlqqdlKVTRLEQDPPASseitvfd 85
Cdd:PRK13536 44 LAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAG--------KITVLGVPVPAR------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 86 yAAEGLAGVGeLLKQYhhvshalahDPSDANIRTMSQLqeqLDYQNGWQYETR-INQVL-TLLDL-----DPDVTLDSLS 158
Cdd:PRK13536 109 -ARLARARIG-VVPQF---------DNLDLEFTVRENL---LVFGRYFGMSTReIEAVIpSLLEFarlesKADARVSDLS 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 657198994 159 GGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDF--RG-AIVFISHDREFIHKLATRIIDLDRGV 230
Cdd:PRK13536 175 GGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLlaRGkTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-473 |
4.61e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 68.66 E-value: 4.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 3 LLTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASelplddgrlvlqqdlkvtrleQDPPASSEIT 82
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSG---------------------IHEPTKGTIT 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 83 VFDyaaeglagvgellKQYHHVSHALAHDPSDANI-RTMSQLQEQLDYQN-----------------GWQYETRINQVLT 144
Cdd:PRK09700 64 INN-------------INYNKLDHKLAAQLGIGIIyQELSVIDELTVLENlyigrhltkkvcgvniiDWREMRVRAAMML 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 145 L---LDLDPDVTLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRG---AIVFIShdrefiHK 218
Cdd:PRK09700 131 LrvgLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKegtAIVYIS------HK 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 219 LAT--RIIDldrgvitswpgnydeylqgkeewlRVEELKNAEFdrklaqeevwVRQGIKARRTrNEGRVRALKAmrmert 296
Cdd:PRK09700 205 LAEirRICD------------------------RYTVMKDGSS----------VCSGMVSDVS-NDDIVRLMVG------ 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 297 qrRELQGKAKLQLDEAGR-SGKLVFETEGLGLDfgDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGS 375
Cdd:PRK09700 244 --RELQNRFNAMKENVSNlAHETVFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGE 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 376 VR-QGTNLE-----------VAYFDQYREQ--LDPEKTVVDNVGEGKQevMVRGRSRHILGYLQDF----LFEPKRARTP 437
Cdd:PRK09700 320 IRlNGKDISprspldavkkgMAYITESRRDngFFPNFSIAQNMAISRS--LKDGGYKGAMGLFHEVdeqrTAENQRELLA 397
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 657198994 438 VKA---------LSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK09700 398 LKChsvnqniteLSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDV 442
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
330-472 |
5.24e-12 |
|
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: 65.14 E-value: 5.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSV-RQGTnlEVAY----FDQYREQL-----DPEK- 398
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVlIDGE--PLDYsrkgLLERRQRVglvfqDPDDq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 399 ----TVVDNVG-----EGKQEVMVRGRSRHILGYLQDFLFEPKrartPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTN 469
Cdd:TIGR01166 81 lfaaDVDQDVAfgplnLGLSEAEVERRVREALTAVGASGLRER----PTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTA 156
|
...
gi 657198994 470 DLD 472
Cdd:TIGR01166 157 GLD 159
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
329-472 |
5.57e-12 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 65.35 E-value: 5.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 329 FGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRQG----TNLEVA------YFDQYreQLDPEK 398
Cdd:cd03301 10 FGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGgrdvTDLPPKdrdiamVFQNY--ALYPHM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 399 TVVDNV-------GEGKQEVMVRGRSR----HILGYLQdflfepkraRTPvKALSGGEKNRLLLAKLFLKPSNLLILDEP 467
Cdd:cd03301 88 TVYDNIafglklrKVPKDEIDERVREVaellQIEHLLD---------RKP-KQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
....*
gi 657198994 468 TNDLD 472
Cdd:cd03301 158 LSNLD 162
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-473 |
5.79e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.40 E-value: 5.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 1 MALLTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVL---QQDLKVTR------- 70
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIdgqEMRFASTTaalaagv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 71 --LEQDPPASSEITVfdyaAEGLagvgeLLKQYHHVSHALahDPSDANIRTMSQLQEqLDyqngwqyetrinqvltlLDL 148
Cdd:PRK11288 82 aiIYQELHLVPEMTV----AENL-----YLGQLPHKGGIV--NRRLLNYEAREQLEH-LG-----------------VDI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 149 DPDVTLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRG---AIVFISHDREFIHKLATRIID 225
Cdd:PRK11288 133 DPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAegrVILYVSHRMEEIFALCDAITV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 226 LDRGvitswpgnydeylqgkeewLRVEELKN-AEFDR-KLAQEEVwvrqgikarrTRNEGRVRALKAmrmertqrRELqG 303
Cdd:PRK11288 213 FKDG-------------------RYVATFDDmAQVDRdQLVQAMV----------GREIGDIYGYRP--------RPL-G 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 304 KAKLQLDeagrsgklvfETEGLGLDfgdrtlfQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRqgtnle 383
Cdd:PRK11288 255 EVRLRLD----------GLKGPGLR-------EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVY------ 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 384 vayfdqyreqLDPEKTVVDNVGEG------------KQEVMVRGRS----------RHIL--GYLQDFLFEPKRA----- 434
Cdd:PRK11288 312 ----------LDGKPIDIRSPRDAiragimlcpedrKAEGIIPVHSvadninisarRHHLraGCLINNRWEAENAdrfir 381
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 657198994 435 ---------RTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK11288 382 slniktpsrEQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDV 429
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
322-472 |
5.86e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 66.57 E-value: 5.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 322 TEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLEVAY--FDQYREQL---- 394
Cdd:PRK13638 4 TSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLwQGKPLDYSKrgLLALRQQVatvf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 395 -DPEKTV------------VDNVGEGKQEVMVRGRSRHILGYLQDFlfepkrARTPVKALSGGEKNRLLLAKLFLKPSNL 461
Cdd:PRK13638 84 qDPEQQIfytdidsdiafsLRNLGVPEAEITRRVDEALTLVDAQHF------RHQPIQCLSHGQKKRVAIAGALVLQARY 157
|
170
....*....|.
gi 657198994 462 LILDEPTNDLD 472
Cdd:PRK13638 158 LLLDEPTAGLD 168
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
321-473 |
6.08e-12 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 65.21 E-value: 6.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLEVAYFDQYREQL----- 394
Cdd:cd03231 2 EADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLlNGGPLDFQRDSIARGLLylgha 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 395 DPEKT---VVDNV----GEGKQEVMVRGRSRHILGYLQDflfepkrarTPVKALSGGEKNRLLLAKLFLKPSNLLILDEP 467
Cdd:cd03231 82 PGIKTtlsVLENLrfwhADHSDEQVEEALARVGLNGFED---------RPVAQLSAGQQRRVALARLLLSGRPLWILDEP 152
|
....*.
gi 657198994 468 TNDLDV 473
Cdd:cd03231 153 TTALDK 158
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
344-520 |
6.76e-12 |
|
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: 65.89 E-value: 6.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 344 RGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVrqGTNLE-VAYFDQYREQlDPEKTV-------VDNVGEGKQ---EVM 412
Cdd:cd03237 24 ESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI--EIELDtVSYKPQYIKA-DYEGTVrdllssiTKDFYTHPYfktEIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 413 vrgrsrhilgylQDFLFEPKRARTpVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLelleelltdypgtLLL 492
Cdd:cd03237 101 ------------KPLQIEQILDRE-VPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQR-------------LMA 154
|
170 180
....*....|....*....|....*...
gi 657198994 493 VSHDRRFIDNTVTGCWLFEGDGRISDYV 520
Cdd:cd03237 155 SKVIRRFAENNEKTAFVVEHDIIMIDYL 182
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
323-472 |
6.89e-12 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 67.41 E-value: 6.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 323 EGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRQG----TNLE-----VAY-FDQYre 392
Cdd:COG3839 7 ENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGgrdvTDLPpkdrnIAMvFQSY-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 393 QLDPEKTVVDNV-------GEGKQEvmVRGRSRH---ILGyLQDFLfepkrARTPvKALSGGEKNRLLLA-------KLF 455
Cdd:COG3839 85 ALYPHMTVYENIafplklrKVPKAE--IDRRVREaaeLLG-LEDLL-----DRKP-KQLSGGQRQRVALGralvrepKVF 155
|
170
....*....|....*..
gi 657198994 456 LkpsnlliLDEPTNDLD 472
Cdd:COG3839 156 L-------LDEPLSNLD 165
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
316-473 |
7.12e-12 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 65.32 E-value: 7.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 316 GKLVFETEGLGLDFGDRTLfQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLEVAYFDQYREQL 394
Cdd:cd03254 1 GEIEFENVNFSYDEKKPVL-KDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILiDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 395 -----DP---EKTVVDNVGEGKQ-----EVMVRGRSRHILgylqDFL-FEPKRARTPV----KALSGGEKNRLLLAKLFL 456
Cdd:cd03254 80 gvvlqDTflfSGTIMENIRLGRPnatdeEVIEAAKEAGAH----DFImKLPNGYDTVLgengGNLSQGERQLLAIARAML 155
|
170
....*....|....*..
gi 657198994 457 KPSNLLILDEPTNDLDV 473
Cdd:cd03254 156 RDPKILILDEATSNIDT 172
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
25-233 |
9.51e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 65.34 E-value: 9.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 25 TIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQQDLKvtrleqdppasseitvfDYAAEGLAGVGELLKQYH-- 102
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQFAGQPLE-----------------AWSAAELARHRAYLSQQQtp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 103 ----HVSHALA-HDPSDANIRtmsqlqeqldyqngwQYETRINQVLTLLDLDPDVT--LDSLSGG-WLRkVALARA-LAC 173
Cdd:PRK03695 81 pfamPVFQYLTlHQPDKTRTE---------------AVASALNEVAEALGLDDKLGrsVNQLSGGeWQR-VRLAAVvLQV 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 657198994 174 DPD------LLLLDEPTNHLDIDAINWLEEFLKDF---RGAIVFISHDREFIHKLATRIIDLDRGVITS 233
Cdd:PRK03695 145 WPDinpagqLLLLDEPMNSLDVAQQAALDRLLSELcqqGIAVVMSSHDLNHTLRHADRVWLLKQGKLLA 213
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
331-472 |
1.14e-11 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 64.87 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 331 DRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLM-------GQLEASRGSVRQgTNLEvayfdQYREQL-----DP-- 396
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLErfydptsGEILLDGVDIRD-LNLR-----WLRSQIglvsqEPvl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 397 -EKTVVDNVGEGK---QEVMVRGRSRhiLGYLQDFLFE-PKRARTPVKA----LSGGEKNRLLLAKLFLKPSNLLILDEP 467
Cdd:cd03249 89 fDGTIAENIRYGKpdaTDEEVEEAAK--KANIHDFIMSlPDGYDTLVGErgsqLSGGQKQRIAIARALLRNPKILLLDEA 166
|
....*
gi 657198994 468 TNDLD 472
Cdd:cd03249 167 TSALD 171
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
20-224 |
1.23e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 66.27 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 20 DHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLV-LQQDL--------KVTRLE-----QDPPAS--SEITV 83
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAwLGKDLlgmkddewRAVRSDiqmifQDPLASlnPRMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 84 FDYAAEGLagvgellKQYHhvshalahdpsdanirtmSQLQEQldyqngwQYETRINQVLTLLDLDPDVT---LDSLSGG 160
Cdd:PRK15079 118 GEIIAEPL-------RTYH------------------PKLSRQ-------EVKDRVKAMMLKVGLLPNLInryPHEFSGG 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 657198994 161 WLRKVALARALACDPDLLLLDEPTNHLD--IDA--INWLEEFLKDFRGAIVFISHDREFIHKLATRII 224
Cdd:PRK15079 166 QCQRIGIARALILEPKLIICDEPVSALDvsIQAqvVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVL 233
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
12-220 |
1.27e-11 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 64.97 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 12 SFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASE--LPLDDGRLVLQ-QDLkvTRLEQDPPASSEITV-FDYA 87
Cdd:TIGR01978 9 SVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHpsYEVTSGTILFKgQDL--LELEPDERARAGLFLaFQYP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 88 AEgLAGVG--ELLKqyhhvshalahdpSDANIRTMSQLQEQLDYQngwQYETRINQVLTLLDLDPDVTLDSL----SGGW 161
Cdd:TIGR01978 87 EE-IPGVSnlEFLR-------------SALNARRSARGEEPLDLL---DFEKLLKEKLALLDMDEEFLNRSVnegfSGGE 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 657198994 162 LRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRG---AIVFISHDREFIHKLA 220
Cdd:TIGR01978 150 KKRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREpdrSFLIITHYQRLLNYIK 211
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
4-231 |
1.33e-11 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 64.44 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 4 LTLHGASLSFSDFPLldHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQQ---------DLKVTRLEQD 74
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvdvtaappaDRPVSMLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 75 PPASSEITVFDYAAEGLAGVGELLKQYHHVSHALAHDPSDANIrtMSQLQEQLdyqngwqyetrinqvltlldldpdvtl 154
Cdd:cd03298 79 NNLFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGL--EKRLPGEL--------------------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 155 dslSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRG----AIVFISHDREFIHKLATRIIDLDRGV 230
Cdd:cd03298 130 ---SGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAetkmTVLMVTHQPEDAKRLAQRVVFLDNGR 206
|
.
gi 657198994 231 I 231
Cdd:cd03298 207 I 207
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
323-473 |
1.36e-11 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 66.27 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 323 EGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRQG----TNLE-----VAY-FDQYre 392
Cdd:COG3842 9 ENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDgrdvTGLPpekrnVGMvFQDY-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 393 QLDPEKTVVDNVGEG-------KQEvmVRGRSRHILGY--LQDFlfepkrARTPVKALSGGEKNRLLLAK-LFLKPSnLL 462
Cdd:COG3842 87 ALFPHLTVAENVAFGlrmrgvpKAE--IRARVAELLELvgLEGL------ADRYPHQLSGGQQQRVALARaLAPEPR-VL 157
|
170
....*....|.
gi 657198994 463 ILDEPTNDLDV 473
Cdd:COG3842 158 LLDEPLSALDA 168
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
324-472 |
1.40e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 64.48 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 324 GLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR----QGTNLEVAYFDQYREQL---DP 396
Cdd:PRK13543 16 ALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQidgkTATRGDRSRFMAYLGHLpglKA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 397 EKTVVDNVG-----EGKQEVMVRGRSRHILGyLQDFlfepkrARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDL 471
Cdd:PRK13543 96 DLSTLENLHflcglHGRRAKQMPGSALAIVG-LAGY------EDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANL 168
|
.
gi 657198994 472 D 472
Cdd:PRK13543 169 D 169
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
335-472 |
1.51e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 67.16 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 335 FQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLevayfDQYRE-QLDPEKTVV----------- 401
Cdd:PRK11160 356 LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILlNGQPI-----ADYSEaALRQAISVVsqrvhlfsatl 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 402 -DNV----GEGKQEVMVRGRSRHILGYLQD-------FLFEPKRArtpvkaLSGGEKNRLLLAKLFLKPSNLLILDEPTN 469
Cdd:PRK11160 431 rDNLllaaPNASDEALIEVLQQVGLEKLLEddkglnaWLGEGGRQ------LSGGEQRRLGIARALLHDAPLLLLDEPTE 504
|
...
gi 657198994 470 DLD 472
Cdd:PRK11160 505 GLD 507
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-183 |
1.54e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 64.67 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 1 MALLTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQqDLKVTRLeqdpPasse 80
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLD-GEDITHL----P---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 81 itVFDYAAEGLAgvgellkqYhhvshaLAHDPS--------DaNIRTMSQLQEqLDYQngwQYETRINQVLTLLDLDP-- 150
Cdd:COG1137 72 --MHKRARLGIG--------Y------LPQEASifrkltveD-NILAVLELRK-LSKK---EREERLEELLEEFGITHlr 130
|
170 180 190
....*....|....*....|....*....|...
gi 657198994 151 DVTLDSLSGGWLRKVALARALACDPDLLLLDEP 183
Cdd:COG1137 131 KSKAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-473 |
2.00e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 66.77 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 3 LLTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLD--DGRLVLQ-QDLKVTRLEQDPPASS 79
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSgSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 80 EITVFDYAAEGLAGVGELLKQYHHVSHALAHDPSDANIRTMSQLQEQLDyqngwqyetrinqvltlLDLDPDV-TLDSLS 158
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQ-----------------LDADNVTrPVGDYG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 159 GGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRG---AIVFISH----------------DREFIHKL 219
Cdd:TIGR02633 144 GGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAhgvACVYISHklnevkavcdticvirDGQHVATK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 220 ATRIIDLDRgVITSWPGNYDEYLQGKEEwlrvEELKnaefDRKLAQEEVWVRQGIKARRTRNEGRVRALKamrmertqRR 299
Cdd:TIGR02633 224 DMSTMSEDD-IITMMVGREITSLYPHEP----HEIG----DVILEARNLTCWDVINPHRKRVDDVSFSLR--------RG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 300 ELQGKAKLQldEAGRsgklvfeTEGLGLDFGDRT-LFQGLDLqvLRGDKIALvgpNGCGKSTLIKLLMGQLEASR-GSVR 377
Cdd:TIGR02633 287 EILGVAGLV--GAGR-------TELVQALFGAYPgKFEGNVF--INGKPVDI---RNPAQAIRAGIAMVPEDRKRhGIVP 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 378 Q---GTNLEVAYFDQY--REQLDPEKTvVDNVGEGKQEVMVRGRSrhilgylqDFLfepkrartPVKALSGGEKNRLLLA 452
Cdd:TIGR02633 353 IlgvGKNITLSVLKSFcfKMRIDAAAE-LQIIGSAIQRLKVKTAS--------PFL--------PIGRLSGGNQQKAVLA 415
|
490 500
....*....|....*....|.
gi 657198994 453 KLFLKPSNLLILDEPTNDLDV 473
Cdd:TIGR02633 416 KMLLTNPRVLILDEPTRGVDV 436
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
338-472 |
2.27e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 66.01 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 338 LDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGS-VRQGTNLEVA---------YFDQYreQLDPEKTVVDNVGEG 407
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQiMLDGVDLSHVppyqrpinmMFQSY--ALFPHMTVEQNIAFG 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 657198994 408 -KQEVMVRG----RSRHILG--YLQDFlfepkRARTPvKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:PRK11607 116 lKQDKLPKAeiasRVNEMLGlvHMQEF-----AKRKP-HQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
323-473 |
2.85e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 64.24 E-value: 2.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 323 EGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVrqgtnlevaYFDQYREQLDPEKTVVD 402
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHV---------WLDGEHIQHYASKEVAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 403 NVG--------EGK---QEVMVRGRSRHILGYL------QDFLFEPKR-------ARTPVKALSGGEKNRLLLAKLFLKP 458
Cdd:PRK10253 82 RIGllaqnattPGDitvQELVARGRYPHQPLFTrwrkedEEAVTKAMQatgithlADQSVDTLSGGQRQRAWIAMVLAQE 161
|
170
....*....|....*
gi 657198994 459 SNLLILDEPTNDLDV 473
Cdd:PRK10253 162 TAIMLLDEPTTWLDI 176
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
4-209 |
2.89e-11 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 63.15 E-value: 2.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 4 LTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQQDlkvtrleqdppasseitv 83
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGT------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 84 fdyaaeglaGVGELLKQYHHVSHALAHDPSdanIRTMSQLQEQLD-YQNGWQYETR-INQVLTLLDLD--PDVTLDSLSG 159
Cdd:TIGR01189 63 ---------PLAEQRDEPHENILYLGHLPG---LKPELSALENLHfWAAIHGGAQRtIEDALAAVGLTgfEDLPAAQLSA 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 657198994 160 GWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDF--RGAIVFI 209
Cdd:TIGR01189 131 GQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHlaRGGIVLL 182
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
21-231 |
3.00e-11 |
|
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: 64.20 E-value: 3.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 21 HAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVL--QQDLKVTRLEQDPPASSEI-------------TVFD 85
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIdgQDIAAMSRKELRELRRKKIsmvfqsfallphrTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 86 YAAEGL--AGVGEllkqyhhvshalahdpsdaNIRtmsqlqeqldyqngwqyETRINQVLTLLDLDP--DVTLDSLSGGW 161
Cdd:cd03294 122 NVAFGLevQGVPR-------------------AER-----------------EERAAEALELVGLEGweHKYPDELSGGM 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 657198994 162 LRKVALARALACDPDLLLLDEPTNHLD----IDAINWLEEFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:cd03294 166 QQRVGLARALAVDPDILLMDEAFSALDplirREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-211 |
3.07e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.11 E-value: 3.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 1 MALLTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLD--DGRLVLQQDLKVTRleqdppas 78
Cdd:PRK13549 3 EYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQAS-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 79 seiTVFDYAAEGLAGVGELLKQYHHVSHA----LAHDPSDANIrtmsqlqeqLDYQNGWQYETRINQVLTlLDLDPDVTL 154
Cdd:PRK13549 75 ---NIRDTERAGIAIIHQELALVKELSVLenifLGNEITPGGI---------MDYDAMYLRAQKLLAQLK-LDINPATPV 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 155 DSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRG---AIVFISH 211
Cdd:PRK13549 142 GNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAhgiACIYISH 201
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
140-233 |
3.12e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 65.28 E-value: 3.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 140 NQVLTLLDLDPdvTLD----SLSGGWLRKVALARALACDPDLLLLDEPTNHLDI----DAINWLEEFLKDFRGAIVFISH 211
Cdd:PRK11144 110 DKIVALLGIEP--LLDrypgSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLprkrELLPYLERLAREINIPILYVSH 187
|
90 100
....*....|....*....|..
gi 657198994 212 DREFIHKLATRIIDLDRGVITS 233
Cdd:PRK11144 188 SLDEILRLADRVVVLEQGKVKA 209
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
11-262 |
3.37e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 64.24 E-value: 3.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 11 LSFS----DFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASEL-PLD-----DGRLVLQQDLKVTR-----LEQDP 75
Cdd:PRK13632 13 VSFSypnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLkPQSgeikiDGITISKENLKEIRkkigiIFQNP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 76 PAS-SEITVFDYAAEGLAGvgellKQYhhvshalahDPSDanirtMSQLQEQLDYQNGwqyetrinqVLTLLDLDPDvtl 154
Cdd:PRK13632 93 DNQfIGATVEDDIAFGLEN-----KKV---------PPKK-----MKDIIDDLAKKVG---------MEDYLDKEPQ--- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 155 dSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRG----AIVFISHDREFIhKLATRIIDLDRGV 230
Cdd:PRK13632 142 -NLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKtrkkTLISITHDMDEA-ILADKVIVFSEGK 219
|
250 260 270
....*....|....*....|....*....|..
gi 657198994 231 ITSwpgnydeylQGKEEwlrvEELKNAEFDRK 262
Cdd:PRK13632 220 LIA---------QGKPK----EILNNKEILEK 238
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
336-468 |
3.78e-11 |
|
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: 63.46 E-value: 3.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 336 QGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLE-----------VAYFDQYReQLDPEKTVVDN 403
Cdd:COG0410 20 HGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRfDGEDITglpphriarlgIGYVPEGR-RIFPSLTVEEN 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 657198994 404 --VGegkqevMVRGRSRHILGYLQDFLFE--PK---RARTPVKALSGGEKNRLLLAK-LFLKPSnLLILDEPT 468
Cdd:COG0410 99 llLG------AYARRDRAEVRADLERVYElfPRlkeRRRQRAGTLSGGEQQMLAIGRaLMSRPK-LLLLDEPS 164
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
18-242 |
4.53e-11 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 63.27 E-value: 4.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 18 LLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRL---------------------VLQQDLKVTR------ 70
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVlvdghdlaladpawlrrqvgvVLQENVLFNRsirdni 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 71 LEQDPPASSEITVfdyAAEGLAGvgellkqyhhvshalAHDpsdaNIRTMSQLQEQLDYQNGwqyetrinqvltlldldp 150
Cdd:cd03252 97 ALADPGMSMERVI---EAAKLAG---------------AHD----FISELPEGYDTIVGEQG------------------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 151 dvtlDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDF---RGAIVfISHDREFIhKLATRIIDLD 227
Cdd:cd03252 137 ----AGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDIcagRTVII-IAHRLSTV-KNADRIIVME 210
|
250
....*....|....*
gi 657198994 228 RGVITSwPGNYDEYL 242
Cdd:cd03252 211 KGRIVE-QGSHDELL 224
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-231 |
4.69e-11 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 63.06 E-value: 4.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 18 LLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDD---GRLVLqqDLKVTRLEQDPPASSEITVFDYAAEGLAgV 94
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILF--NGQPRKPDQFQKCVAYVRQDDILLPGLT-V 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 95 GELLkqyHHVSHALAHDPSDANIRTMSQLQEQLDYQNgwqyETRINQVLtlldldpdvtLDSLSGGWLRKVALARALACD 174
Cdd:cd03234 99 RETL---TYTAILRLPRKSSDAIRKKRVEDVLLRDLA----LTRIGGNL----------VKGISGGERRRVSIAVQLLWD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 657198994 175 PDLLLLDEPTNHLDIDAINWLEEFLKDF----RGAIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:cd03234 162 PKVLILDEPTSGLDSFTALNLVSTLSQLarrnRIVILTIHQPRSDLFRLFDRILLLSSGEI 222
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-245 |
4.93e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 63.06 E-value: 4.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 24 LTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQ-QDLKVTrleqdPPASSEITVfdyaaeglagvgeLLKQYH 102
Cdd:PRK10771 20 LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNgQDHTTT-----PPSRRPVSM-------------LFQENN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 103 HVSH-------ALAHDPsdaNIRTMSQLQEQLDyqngwqyetRINQVLTLLDLdpdvtLD----SLSGGWLRKVALARAL 171
Cdd:PRK10771 82 LFSHltvaqniGLGLNP---GLKLNAAQREKLH---------AIARQMGIEDL-----LArlpgQLSGGQRQRVALARCL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 657198994 172 ACDPDLLLLDEPTNHLD----IDAINWLEEFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVItSWPGNYDEYLQGK 245
Cdd:PRK10771 145 VREQPILLLDEPFSALDpalrQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRI-AWDGPTDELLSGK 221
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
329-472 |
5.60e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 63.98 E-value: 5.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 329 FGDRTLFQgLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRQG---------------TNLEVAYFDQYREQ 393
Cdd:PRK13643 17 FASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGdivvsstskqkeikpVRKKVGVVFQFPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 394 LDPEKTVVDNVGEGKQEV--------MVRGRSRHILGYLQDFLfepkrARTPVKaLSGGEKNRLLLAKLFLKPSNLLILD 465
Cdd:PRK13643 96 QLFEETVLKDVAFGPQNFgipkekaeKIAAEKLEMVGLADEFW-----EKSPFE-LSGGQMRRVAIAGILAMEPEVLVLD 169
|
....*..
gi 657198994 466 EPTNDLD 472
Cdd:PRK13643 170 EPTAGLD 176
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
321-473 |
5.64e-11 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 62.16 E-value: 5.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMG--QLEASRGSVR-QGTNLEvayfdqyreQLDPE 397
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILfKGEDIT---------DLPPE 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 657198994 398 KTVVDNVGEGKQE-VMVRGRSrhilgyLQDFLfepkraRTPVKALSGGEKNRL-LLAKLFLKPSnLLILDEPTNDLDV 473
Cdd:cd03217 73 ERARLGIFLAFQYpPEIPGVK------NADFL------RYVNEGFSGGEKKRNeILQLLLLEPD-LAILDEPDSGLDI 137
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
321-472 |
6.23e-11 |
|
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: 62.74 E-value: 6.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSV----RQGTNLEVA------YFDQY 390
Cdd:cd03296 4 EVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTIlfggEDATDVPVQernvgfVFQHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 391 reQLDPEKTVVDNVGEG---------KQEVMVRGRSRHILGYLQ-DFLFEpkraRTPVKaLSGGEKNRLLLAKLFLKPSN 460
Cdd:cd03296 84 --ALFRHMTVFDNVAFGlrvkprserPPEAEIRAKVHELLKLVQlDWLAD----RYPAQ-LSGGQRQRVALARALAVEPK 156
|
170
....*....|..
gi 657198994 461 LLILDEPTNDLD 472
Cdd:cd03296 157 VLLLDEPFGALD 168
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
416-537 |
6.33e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 65.65 E-value: 6.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 416 RSRHILGYLQdflFEPKRARTPVKALSGGEKNRLLLAK-LFLKPsNLLILDEPTNDLDVETLELLEELLTDYPGTLLLVS 494
Cdd:PLN03073 323 RAASILAGLS---FTPEMQVKATKTFSGGWRMRIALARaLFIEP-DLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVS 398
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 657198994 495 HDRRFIDNTVTGCWLFEGDgRISDYVGGYADMMATRALQAAQQ 537
Cdd:PLN03073 399 HAREFLNTVVTDILHLHGQ-KLVTYKGDYDTFERTREEQLKNQ 440
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-247 |
6.84e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 63.01 E-value: 6.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 1 MALLTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKV------------IASELPLDdGRLVLQQDL-- 66
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrlielypearVSGEVYLD-GQDIFKMDVie 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 67 ---KVTRLEQDPPASSEITVFDYAAEGLAgVGELLKQYHHVShalahdpsdanirtmSQLQEQLDYQNGWQyetrinQVL 143
Cdd:PRK14247 80 lrrRVQMVFQIPNPIPNLSIFENVALGLK-LNRLVKSKKELQ---------------ERVRWALEKAQLWD------EVK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 144 TLLDldpdVTLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRG--AIVFISHdrefIHKLAT 221
Cdd:PRK14247 138 DRLD----APAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKdmTIVLVTH----FPQQAA 209
|
250 260 270
....*....|....*....|....*....|
gi 657198994 222 RIID----LDRGVITSWPGNYDEYLQGKEE 247
Cdd:PRK14247 210 RISDyvafLYKGQIVEWGPTREVFTNPRHE 239
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-233 |
7.21e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 63.65 E-value: 7.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 19 LDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQqDLKVTRLEQDP---PASSEI-TVFDYAAEGLAgv 94
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVD-DITITHKTKDKyirPVRKRIgMVFQFPESQLF-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 95 gellkqYHHVSHALAHDPSDANIrtmsqlqeqldyqNGWQYETRINQVLTLLDLDPDVTLDS---LSGGWLRKVALARAL 171
Cdd:PRK13646 100 ------EDTVEREIIFGPKNFKM-------------NLDEVKNYAHRLLMDLGFSRDVMSQSpfqMSGGQMRKIAIVSIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 657198994 172 ACDPDLLLLDEPTNHLDIDAINWLEEFLKDFR----GAIVFISHDREFIHKLATRIIDLDRGVITS 233
Cdd:PRK13646 161 AMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdenKTIILVSHDMNEVARYADEVIVMKEGSIVS 226
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
329-472 |
8.79e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 63.97 E-value: 8.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 329 FGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRG------------SVRQGTNLEVayFDQYreQLDP 396
Cdd:PRK11432 16 FGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGqifidgedvthrSIQQRDICMV--FQSY--ALFP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 397 EKTVVDNVGEG-------KQEvmVRGRSRHILGYLQDFLFEPKRartpVKALSGGEKNRLLLAK-LFLKPSNLLiLDEPT 468
Cdd:PRK11432 92 HMSLGENVGYGlkmlgvpKEE--RKQRVKEALELVDLAGFEDRY----VDQISGGQQQRVALARaLILKPKVLL-FDEPL 164
|
....
gi 657198994 469 NDLD 472
Cdd:PRK11432 165 SNLD 168
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
321-472 |
9.05e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 62.46 E-value: 9.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRQGT---------NLEVAYFDQYR 391
Cdd:PRK11264 5 EVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDitidtarslSQQKGLIRQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 392 EQ---------LDPEKTVVDNVGEG--------KQEVMVRGRSrhilgYLQDFLFEPKRARTPvKALSGGEKNRLLLAKL 454
Cdd:PRK11264 85 QHvgfvfqnfnLFPHRTVLENIIEGpvivkgepKEEATARARE-----LLAKVGLAGKETSYP-RRLSGGQQQRVAIARA 158
|
170
....*....|....*...
gi 657198994 455 FLKPSNLLILDEPTNDLD 472
Cdd:PRK11264 159 LAMRPEVILFDEPTSALD 176
|
|
| ABC_tran_CTD |
pfam16326 |
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. ... |
562-631 |
1.01e-10 |
|
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: 57.86 E-value: 1.01e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 562 KLSYKLQLELDNLPARLEQLEMELDALQAEINHPGFFSlPAEQTQPKLDALNAAEAALEHAFSRWEELEA 631
Cdd:pfam16326 1 KLSYKEQRELEELEAEIEKLEEEIAELEAQLADPELYS-DYEKLQELSAELEELEAELEELYERWEELEE 69
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
317-472 |
1.04e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 62.55 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 317 KLVFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRQGtnlEVAYF--DQYREQL 394
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEG---EVRLFgrNIYSPDV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 395 D------------------PEKTVVDNVGEG-KQEVMVRGRS----RHILGYLQDFLFEPKRARTPVKA--LSGGEKNRL 449
Cdd:PRK14267 79 DpievrrevgmvfqypnpfPHLTIYDNVAIGvKLNGLVKSKKeldeRVEWALKKAALWDEVKDRLNDYPsnLSGGQRQRL 158
|
170 180
....*....|....*....|....
gi 657198994 450 LLAK-LFLKPsNLLILDEPTNDLD 472
Cdd:PRK14267 159 VIARaLAMKP-KILLMDEPTANID 181
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
14-231 |
1.19e-10 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 61.72 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 14 SDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQQD-----------LKVTRLEQDPPASSEiT 82
Cdd:cd03248 25 PDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpisqyehkylhSKVSLVGQEPVLFAR-S 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 83 VFDYAAEGLAGVG-ELLKQYHHVSHAlahdpsDANIRTMSQlqeqldyqngwQYETRINQVLTLldldpdvtldsLSGGW 161
Cdd:cd03248 104 LQDNIAYGLQSCSfECVKEAAQKAHA------HSFISELAS-----------GYDTEVGEKGSQ-----------LSGGQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 657198994 162 LRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDF--RGAIVFISHDREFIHKlATRIIDLDRGVI 231
Cdd:cd03248 156 KQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWpeRRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
306-472 |
1.19e-10 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 63.81 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 306 KLQLDEAGRSGKLVFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSV----RQGTN 381
Cdd:PRK09452 1 SKKLNKQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRImldgQDITH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 382 LEV------AYFDQYreQLDPEKTVVDNVGEG-------KQEV---------MVRgrsrhilgyLQDFlfepkrARTPVK 439
Cdd:PRK09452 81 VPAenrhvnTVFQSY--ALFPHMTVFENVAFGlrmqktpAAEItprvmealrMVQ---------LEEF------AQRKPH 143
|
170 180 190
....*....|....*....|....*....|...
gi 657198994 440 ALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:PRK09452 144 QLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
17-242 |
1.58e-10 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 64.38 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 17 PLLDHAELTIERGERLCLVGRNGAGKSTLMKVIA------------SELPLDD-GRLVLQQdlKVTRLEQDPPASSEiTV 83
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVgffqarsgeillNGFSLKDiDRHTLRQ--FINYLPQEPYIFSG-SI 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 84 FDYAaegLAGVGELLKQyHHVSHALAHDPSDANIRTMSQlqeqldyqngwQYETRINQVLTlldldpdvtldSLSGGWLR 163
Cdd:TIGR01193 565 LENL---LLGAKENVSQ-DEIWAACEIAEIKDDIENMPL-----------GYQTELSEEGS-----------SISGGQKQ 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 164 KVALARALACDPDLLLLDEPTNHLD-IDAINWLEEFLKDFRGAIVFISHdREFIHKLATRIIDLDRGVITSwPGNYDEYL 242
Cdd:TIGR01193 619 RIALARALLTDSKVLILDESTSNLDtITEKKIVNNLLNLQDKTIIFVAH-RLSVAKQSDKIIVLDHGKIIE-QGSHDELL 696
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-243 |
1.81e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 63.69 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 2 ALLTLHGASLSFSD--FPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVL-QQDLKvtrleqdppas 78
Cdd:PRK11160 337 VSLTLNNVSFTYPDqpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLnGQPIA----------- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 79 seitvfDYAAEGLAGVGELLKQYHHV-SHAL-------AHDPSDAnirtmsQLQEQLdyqngwqyetriNQV-LTLLdLD 149
Cdd:PRK11160 406 ------DYSEAALRQAISVVSQRVHLfSATLrdnlllaAPNASDE------ALIEVL------------QQVgLEKL-LE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 150 PDVTLDS--------LSGGWLRKVALARALACDPDLLLLDEPTNHLDIDA----INWLEEFLKDfrGAIVFISHDREFIH 217
Cdd:PRK11160 461 DDKGLNAwlgeggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETerqiLELLAEHAQN--KTVLMITHRLTGLE 538
|
250 260
....*....|....*....|....*..
gi 657198994 218 KLaTRIIDLDRG-VITSwpGNYDEYLQ 243
Cdd:PRK11160 539 QF-DRICVMDNGqIIEQ--GTHQELLA 562
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
18-226 |
1.81e-10 |
|
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: 60.97 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 18 LLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQQdlkvtrleqdppasseitvfdyaaeglAGVGEL 97
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG---------------------------GPLDFQ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 98 LKQYHHVSHALAHDPSdanIRTMSQLQEQLDYQNGWQYETRINQVLTLLDLD--PDVTLDSLSGGWLRKVALARALACDP 175
Cdd:cd03231 68 RDSIARGLLYLGHAPG---IKTTLSVLENLRFWHADHSDEQVEEALARVGLNgfEDRPVAQLSAGQQRRVALARLLLSGR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 657198994 176 DLLLLDEPTNHLDIDAINWLEEFLKDFR---GAIVFISHDREFIHKLATRIIDL 226
Cdd:cd03231 145 PLWILDEPTTALDKAGVARFAEAMAGHCargGMVVLTTHQDLGLSEAGARELDL 198
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
5-189 |
1.89e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 61.73 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 5 TLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQQDL-----------KVTRLEQ 73
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPleswsskafarKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 74 DPPasseitvfdyAAEGLAgVGELLkqyhhvshALAHDPSDANIRTMSQLQEQldyqngwqyetRINQVLTLLDLDP--D 151
Cdd:PRK10575 93 QLP----------AAEGMT-VRELV--------AIGRYPWHGALGRFGAADRE-----------KVEEAISLVGLKPlaH 142
|
170 180 190
....*....|....*....|....*....|....*...
gi 657198994 152 VTLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDI 189
Cdd:PRK10575 143 RLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI 180
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
284-472 |
1.95e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 63.67 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 284 RVRALkAMRMERTQRRElQGKAKLQLDEAGRsgklvFETEGLGLDFGD-RTLFQGLDLQVLRGDKIALVGPNGCGKSTLI 362
Cdd:COG4178 334 RLAGF-EEALEAADALP-EAASRIETSEDGA-----LALEDLTLRTPDgRPLLEDLSLSLKPGERLLITGPSGSGKSTLL 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 363 KLLMGQLEASRGSVRQGTNLEVAYFDQ--Y------REQL---DPEKTVVDnvgEGKQEVMVRGRsrhiLGYLQDFLFEP 431
Cdd:COG4178 407 RAIAGLWPYGSGRIARPAGARVLFLPQrpYlplgtlREALlypATAEAFSD---AELREALEAVG----LGHLAERLDEE 479
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 657198994 432 KR-ARTpvkaLSGGEKNRLLLAKLFL-KPSnLLILDEPTNDLD 472
Cdd:COG4178 480 ADwDQV----LSLGEQQRLAFARLLLhKPD-WLFLDEATSALD 517
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
338-516 |
2.03e-10 |
|
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: 60.97 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 338 LDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRQG----TNLEVA------YFDQyrEQLDPEKTVVDNVGEG 407
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINgvdvTAAPPAdrpvsmLFQE--NNLFAHLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 408 -----KQEVMVRGRSRHILGYLQDFLFEPKRARTpvkaLSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEEL 482
Cdd:cd03298 95 lspglKLTAEDRQAIEVALARVGLAGLEKRLPGE----LSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 657198994 483 LTDYPG----TLLLVSH---DRRFIDNTVtgcwLFEGDGRI 516
Cdd:cd03298 171 VLDLHAetkmTVLMVTHqpeDAKRLAQRV----VFLDNGRI 207
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
339-516 |
2.28e-10 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 60.92 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 339 DLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLEvayfdqyreQLDPEK----------------TVV 401
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILwNGQDLT---------ALPPAErpvsmlfqennlfphlTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 402 DNVGEG-----------KQEVmvrgrsRHILGY--LQDFLfepkrARTPvKALSGGEKNRLLLAKLFLKPSNLLILDEPT 468
Cdd:COG3840 90 QNIGLGlrpglkltaeqRAQV------EQALERvgLAGLL-----DRLP-GQLSGGQRQRVALARCLVRKRPILLLDEPF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 657198994 469 NDLD----------VetlellEELLTDYPGTLLLVSHD----RRFIDNTvtgcwLFEGDGRI 516
Cdd:COG3840 158 SALDpalrqemldlV------DELCRERGLTVLMVTHDpedaARIADRV-----LLVADGRI 208
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
311-521 |
2.31e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 61.60 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 311 EAGRSGKLVFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRqgTNLEVAYFDQY 390
Cdd:PRK14246 2 EAGKSAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIK--VDGKVLYFGKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 391 REQLD------------------PEKTVVDNVGEGKQEVMVRGRsRHILGYLQDFLFEP-------KRARTPVKALSGGE 445
Cdd:PRK14246 80 IFQIDaiklrkevgmvfqqpnpfPHLSIYDNIAYPLKSHGIKEK-REIKKIVEECLRKVglwkevyDRLNSPASQLSGGQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 657198994 446 KNRLLLAK-LFLKPSnLLILDEPTNDLDVETLELLEELLTDYPG--TLLLVSHDRRFIdntvtgcwlfegdGRISDYVG 521
Cdd:PRK14246 159 QQRLTIARaLALKPK-VLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQV-------------ARVADYVA 223
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
345-495 |
2.37e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 61.99 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 345 GDKIALVGPNGCGKSTLIKLLMGQLEASRGSV--------RQGTNL-----EVAYFDQYRE-QLDPEKTVVD------NV 404
Cdd:PRK13637 33 GEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIiidgvditDKKVKLsdirkKVGLVFQYPEyQLFEETIEKDiafgpiNL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 405 GEGKQEVMVR-GRSRHILGylqdFLFEPKRARTPVKaLSGGEKNRLLLAKLF-LKPSnLLILDEPTNDLDVETL----EL 478
Cdd:PRK13637 113 GLSEEEIENRvKRAMNIVG----LDYEDYKDKSPFE-LSGGQKRRVAIAGVVaMEPK-ILILDEPTAGLDPKGRdeilNK 186
|
170
....*....|....*..
gi 657198994 479 LEELLTDYPGTLLLVSH 495
Cdd:PRK13637 187 IKELHKEYNMTIILVSH 203
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
24-211 |
2.38e-10 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 61.24 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 24 LTIERGERLCLVGRNGAGKSTLMKVIA--SELPLDDGRLVLQ-QDLkvTRLE-------------QDPPASSEITVFDYa 87
Cdd:COG0396 21 LTIKPGEVHAIMGPNGSGKSTLAKVLMghPKYEVTSGSILLDgEDI--LELSpderaragiflafQYPVEIPGVSVSNF- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 88 aeglagvgellkqyhhvshalahdpsdanIRTM--SQLQEQLDYQngwQYETRINQVLTLLDLDPDVtLD-----SLSGG 160
Cdd:COG0396 98 -----------------------------LRTAlnARRGEELSAR---EFLKLLKEKMKELGLDEDF-LDryvneGFSGG 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 657198994 161 WLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRG---AIVFISH 211
Cdd:COG0396 145 EKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSpdrGILIITH 198
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
224-300 |
2.53e-10 |
|
ABC transporter; This domain is an extension of some members of pfam00005 and other ABC-transporter families.
Pssm-ID: 463731 [Multi-domain] Cd Length: 85 Bit Score: 57.20 E-value: 2.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 224 IDLDRGVITSWPGNYDEYLQGKEEWLRVEELKNAEFDRKLAQEEVWV-RQGIKARRTR-NEGRVRALKAM-RMERTQRRE 300
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIdRFRAKASKAKqAQSRIKALEKMeRIEKPERDK 80
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
3-231 |
2.60e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 61.54 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 3 LLTLHGASLSFSD-FPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVlqqdlkVTRLEQ-DPPASSE 80
Cdd:PRK13644 1 MIRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVL------VSGIDTgDFSKLQG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 81 I-----TVFDYAAEGLAGvgellkqyHHVSHALAHDPSDANIRTMsqlqeqldyqngwQYETRINQVLTLLDLDP--DVT 153
Cdd:PRK13644 75 IrklvgIVFQNPETQFVG--------RTVEEDLAFGPENLCLPPI-------------EIRKRVDRALAEIGLEKyrHRS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 154 LDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFR---GAIVFISHDREFIHkLATRIIDLDRGV 230
Cdd:PRK13644 134 PKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHekgKTIVYITHNLEELH-DADRIIVMDRGK 212
|
.
gi 657198994 231 I 231
Cdd:PRK13644 213 I 213
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
333-498 |
2.96e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 60.56 E-value: 2.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 333 TLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRQ-GTNLEvAYFDQYREQLD--------------PE 397
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLvGQPLH-QMDEEARAKLRakhvgfvfqsfmliPT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 398 KTVVDNVG-----EGKQEVMVRGRSRHILGYLQdflfEPKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:PRK10584 103 LNALENVElpallRGESSRQSRNGAKALLEQLG----LGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
170 180 190
....*....|....*....|....*....|
gi 657198994 473 VETLELLE----ELLTDYPGTLLLVSHDRR 498
Cdd:PRK10584 179 RQTGDKIAdllfSLNREHGTTLILVTHDLQ 208
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
337-473 |
3.29e-10 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 62.06 E-value: 3.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 337 GLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLEVAYFDQYREQ--------------LDPEKTVV 401
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILfDGQDITGLSGRELRPLrrrmqmvfqdpyasLNPRMTVG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 402 DNVGEG--------KQEvmVRGRSRHIL---GYLQDFLfepkrARTPvKALSGGEKNRLLLAK-LFLKPSnLLILDEPTN 469
Cdd:COG4608 116 DIIAEPlrihglasKAE--RRERVAELLelvGLRPEHA-----DRYP-HEFSGGQRQRIGIARaLALNPK-LIVCDEPVS 186
|
....
gi 657198994 470 DLDV 473
Cdd:COG4608 187 ALDV 190
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
329-473 |
3.67e-10 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 62.83 E-value: 3.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 329 FGDRTLfQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRQG----TNLEVAYFDQYREQLDPEK-----T 399
Cdd:TIGR01193 485 YGSNIL-SDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNgfslKDIDRHTLRQFINYLPQEPyifsgS 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 400 VVDNV------GEGKQEVMVRGRSRHI--------LGYLQDFLFEPKrartpvkALSGGEKNRLLLAKLFLKPSNLLILD 465
Cdd:TIGR01193 564 ILENLllgakeNVSQDEIWAACEIAEIkddienmpLGYQTELSEEGS-------SISGGQKQRIALARALLTDSKVLILD 636
|
....*...
gi 657198994 466 EPTNDLDV 473
Cdd:TIGR01193 637 ESTSNLDT 644
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3-231 |
3.90e-10 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 61.89 E-value: 3.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 3 LLTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQ-QDlkVTRLeqdPPASSEI 81
Cdd:PRK09452 14 LVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDgQD--ITHV---PAENRHV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 82 -------------TVFDYAAEGLagvgELLKQYHH-----VSHALAhdpsdanirtMSQLQEQLDyqngwqyeTRINQvl 143
Cdd:PRK09452 89 ntvfqsyalfphmTVFENVAFGL----RMQKTPAAeitprVMEALR----------MVQLEEFAQ--------RKPHQ-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 144 tlldldpdvtldsLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRGAI----VFISHDREFIHKL 219
Cdd:PRK09452 145 -------------LSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLgitfVFVTHDQEEALTM 211
|
250
....*....|..
gi 657198994 220 ATRIIDLDRGVI 231
Cdd:PRK09452 212 SDRIVVMRDGRI 223
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-243 |
4.01e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 60.87 E-value: 4.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 3 LLTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQQdlkvtRLEQDPPASSEI- 81
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG-----KPVEGPGAERGVv 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 82 ----------TVFDYAAEGL--AGVGELlkqyhhvshalahdpsdanirtmsqlqeqldyqngwQYETRINQVLTLLDLD 149
Cdd:PRK11248 76 fqnegllpwrNVQDNVAFGLqlAGVEKM------------------------------------QRLEIAHQMLKKVGLE 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 150 --PDVTLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFL----KDFRGAIVFISHDREFIHKLATRI 223
Cdd:PRK11248 120 gaEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLlklwQETGKQVLLITHDIEEAVFMATEL 199
|
250 260
....*....|....*....|
gi 657198994 224 IDLDRGvitswPGNYDEYLQ 243
Cdd:PRK11248 200 VLLSPG-----PGRVVERLP 214
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-231 |
4.28e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 60.87 E-value: 4.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 18 LLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQ-QDlkVTRLE------------QDPPA--SSEIT 82
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDgKD--VTKLPeykrakyigrvfQDPMMgtAPSMT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 83 VfdyaAEGLAgvgelLKQYHHVSHALAHDPSDANIRTMSQLQEQLDyqNGwqYETRINQVLTLldldpdvtldsLSGGWL 162
Cdd:COG1101 99 I----EENLA-----LAYRRGKRRGLRRGLTKKRRELFRELLATLG--LG--LENRLDTKVGL-----------LSGGQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 657198994 163 RKVALARALACDPDLLLLDEPTNHLD---IDAINWL-EEFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:COG1101 155 QALSLLMATLTKPKLLLLDEHTAALDpktAALVLELtEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
336-472 |
4.30e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 61.18 E-value: 4.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 336 QGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLEVAYFDQYREQL-----DPEK-----TVVDNV 404
Cdd:PRK13635 24 KDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITvGGMVLSEETVWDVRRQVgmvfqNPDNqfvgaTVQDDV 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 657198994 405 GEG------KQEVMVRgRSRHILG--YLQDFL-FEPKRartpvkaLSGGEKNRLLLAK-LFLKPSnLLILDEPTNDLD 472
Cdd:PRK13635 104 AFGlenigvPREEMVE-RVDQALRqvGMEDFLnREPHR-------LSGGQKQRVAIAGvLALQPD-IIILDEATSMLD 172
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
334-472 |
4.36e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 60.37 E-value: 4.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 334 LFQGL----DLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLEVAYFDQ------YREQ-LDPEKTVV 401
Cdd:PRK10771 10 LYHHLpmrfDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTlNGQDHTTTPPSRrpvsmlFQENnLFSHLTVA 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 657198994 402 DNVGEG-----KQEVMVRGRSRHILGY--LQDFLfepkrARTPvKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:PRK10771 90 QNIGLGlnpglKLNAAQREKLHAIARQmgIEDLL-----ARLP-GQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
321-473 |
4.56e-10 |
|
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: 60.33 E-value: 4.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRQGTNlEVAYFDQYREQ------- 393
Cdd:cd03300 2 ELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGK-DITNLPPHKRPvntvfqn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 394 --LDPEKTVVDNVG-----EGKQEVMVRGRSRHILGYLQdflFEPKRARTPvKALSGGEKNRLLLAK-LFLKPSnLLILD 465
Cdd:cd03300 81 yaLFPHLTVFENIAfglrlKKLPKAEIKERVAEALDLVQ---LEGYANRKP-SQLSGGQQQRVAIARaLVNEPK-VLLLD 155
|
....*...
gi 657198994 466 EPTNDLDV 473
Cdd:cd03300 156 EPLGALDL 163
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
17-233 |
4.67e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 60.80 E-value: 4.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 17 PLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGrlvlqqDLKVTRLEQDPPASSEI--------------- 81
Cdd:PRK13635 21 YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAG------TITVGGMVLSEETVWDVrrqvgmvfqnpdnqf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 82 ---TVFDYAAEGLAGVGEllkqyhhvshalahdPSDANIRTMSQLQEQLDYQNgwqyetrinqvltLLDLDPDvtldSLS 158
Cdd:PRK13635 95 vgaTVQDDVAFGLENIGV---------------PREEMVERVDQALRQVGMED-------------FLNREPH----RLS 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 657198994 159 GGWLRKVALARALACDPDLLLLDEPTNHLD-IDAINWLEEF--LKDFRGAIVF-ISHDREFIHKlATRIIDLDRGVITS 233
Cdd:PRK13635 143 GGQKQRVAIAGVLALQPDIIILDEATSMLDpRGRREVLETVrqLKEQKGITVLsITHDLDEAAQ-ADRVIVMNKGEILE 220
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
4-229 |
5.23e-10 |
|
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: 59.41 E-value: 5.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 4 LTLHGASLSFSD-----FPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLvlqqdlkvtrleqdppas 78
Cdd:cd03250 1 ISVEDASFTWDSgeqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 79 seitvfdyaaeglagvgellkqyhHVSHALAHDPSDANIRTMSqLQEqldyqN---GWQY-ETRINQVLTLLDLDPDVTL 154
Cdd:cd03250 63 ------------------------SVPGSIAYVSQEPWIQNGT-IRE-----NilfGKPFdEERYEKVIKACALEPDLEI 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 155 ----D---------SLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEE-----FLKDFRgAIVFISHDREFI 216
Cdd:cd03250 113 lpdgDlteigekgiNLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncilgLLLNNK-TRILVTHQLQLL 191
|
250
....*....|...
gi 657198994 217 HKlATRIIDLDRG 229
Cdd:cd03250 192 PH-ADQIVVLDNG 203
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
15-231 |
5.46e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 62.34 E-value: 5.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 15 DFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQ----QDLKVTRL-EQDPPASSEITVFD---- 85
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDghdlRDYTLASLrNQVALVSQNVHLFNdtia 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 86 ----YAAEGlagvgellkQYhhvshalahdpSDANIRTMSQLQEQLDY----QNGwqYETRI--NQVltlldldpdvtld 155
Cdd:PRK11176 435 nniaYARTE---------QY-----------SREQIEEAARMAYAMDFinkmDNG--LDTVIgeNGV------------- 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 156 SLSGGWLRKVALARALACDPDLLLLDEPTNHLDID---AIN-WLEEFLKDfRGAIVfISHDREFIHKlATRIIDLDRGVI 231
Cdd:PRK11176 480 LLSGGQRQRIAIARALLRDSPILILDEATSALDTEserAIQaALDELQKN-RTSLV-IAHRLSTIEK-ADEILVVEDGEI 556
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
317-472 |
5.71e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 59.73 E-value: 5.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 317 KLVFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLEVAYFDQYREQLD 395
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLfEGEDISTLKPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 396 -----PE---KTVVDNVGEGKQEVMVRGRSRHILGYLQDFLFEPKRARTPVKALSGGEKNRL-LLAKLFLKPSNLLiLDE 466
Cdd:PRK10247 85 ycaqtPTlfgDTVYDNLIFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRIsLIRNLQFMPKVLL-LDE 163
|
....*.
gi 657198994 467 PTNDLD 472
Cdd:PRK10247 164 ITSALD 169
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
336-472 |
5.71e-10 |
|
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: 59.79 E-value: 5.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 336 QGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLE------VAYFDQYreQLDPEKTVVDNVGEGK 408
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVIlEGKQITepgpdrMVVFQNY--SLLPWLTVRENIALAV 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 657198994 409 QEV---MVRGRSRHILGYLQDFLFEPKRARTPVKALSGGEKNRLLLAK-LFLKPSnLLILDEPTNDLD 472
Cdd:TIGR01184 80 DRVlpdLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARaLSIRPK-VLLLDEPFGALD 146
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
331-472 |
5.74e-10 |
|
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: 59.98 E-value: 5.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 331 DRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLE---ASRGSV--------RQGTNLEVAYFDQYrEQLDPEKT 399
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQIlfngqprkPDQFQKCVAYVRQD-DILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 400 VVDNV-------------GEGKQEVMVRGRSRHIlgylqdflfEPKRARTP-VKALSGGEKNRLLLAKLFLKPSNLLILD 465
Cdd:cd03234 98 VRETLtytailrlprkssDAIRKKRVEDVLLRDL---------ALTRIGGNlVKGISGGERRRVSIAVQLLWDPKVLILD 168
|
....*..
gi 657198994 466 EPTNDLD 472
Cdd:cd03234 169 EPTSGLD 175
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
320-542 |
6.76e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 60.09 E-value: 6.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 320 FETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLEVAYFDQYRE-----Q 393
Cdd:PRK10419 13 YAHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSwRGEPLAKLNRAQRKAfrrdiQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 394 L---------DPEKTVVDNVGEGKQEVMV---RGRSRHILGYLQDFLFEPKRARTPVKALSGGEKNRLLLAKLFLKPSNL 461
Cdd:PRK10419 93 MvfqdsisavNPRKTVREIIREPLRHLLSldkAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 462 LILDEPTNDLDVETLELLEELLTDYP---GT-LLLVSHDRRFIDNTVTGCWLFEGDGRISDYVGGYADMM---ATRALQA 534
Cdd:PRK10419 173 LILDEAVSNLDLVLQAGVIRLLKKLQqqfGTaCLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLTFsspAGRVLQN 252
|
....*...
gi 657198994 535 AQQTAKPA 542
Cdd:PRK10419 253 AVLPAFPV 260
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
316-472 |
7.27e-10 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 61.76 E-value: 7.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 316 GKLVFEteglGLDFG---DRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNL-EVAYfDQY 390
Cdd:COG5265 356 GEVRFE----NVSFGydpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILiDGQDIrDVTQ-ASL 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 391 REQLD--PEKTVV------DNVGEGK-----QEVMVRGRSRHILGYLQDFlfePKRARTPV-----KaLSGGEKNRLLLA 452
Cdd:COG5265 431 RAAIGivPQDTVLfndtiaYNIAYGRpdaseEEVEAAARAAQIHDFIESL---PDGYDTRVgerglK-LSGGEKQRVAIA 506
|
170 180
....*....|....*....|
gi 657198994 453 KLFLKPSNLLILDEPTNDLD 472
Cdd:COG5265 507 RTLLKNPPILIFDEATSALD 526
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
323-473 |
9.44e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 59.55 E-value: 9.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 323 EGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSV----RQGTNLEVA------------- 385
Cdd:PRK11701 10 RGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhyrmRDGQLRDLYalseaerrrllrt 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 386 ---YFDQY-REQLDPEKTVVDNVGEGKQEVMVR--GRSRHILG-YLQDFLFEPKRARTPVKALSGGEKNRLLLAKLFLKP 458
Cdd:PRK11701 90 ewgFVHQHpRDGLRMQVSAGGNIGERLMAVGARhyGDIRATAGdWLERVEIDAARIDDLPTTFSGGMQQRLQIARNLVTH 169
|
170
....*....|....*
gi 657198994 459 SNLLILDEPTNDLDV 473
Cdd:PRK11701 170 PRLVFMDEPTGGLDV 184
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-231 |
9.82e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 59.38 E-value: 9.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 1 MALLTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVI------------ASELPLDDGRLVLQQDLKV 68
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeagtirVGDITIDTARSLSQQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 69 TRLEQDppasseitvfdyaaeglagVGELLKQYHHVSHALAHDpsdaNIRTMSQLQEQLDYQngwQYETRINQVLTLLDL 148
Cdd:PRK11264 81 RQLRQH-------------------VGFVFQNFNLFPHRTVLE----NIIEGPVIVKGEPKE---EATARARELLAKVGL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 149 D--PDVTLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINwleEFLKDFRG------AIVFISHDREFIHKLA 220
Cdd:PRK11264 135 AgkETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVG---EVLNTIRQlaqekrTMVIVTHEMSFARDVA 211
|
250
....*....|.
gi 657198994 221 TRIIDLDRGVI 231
Cdd:PRK11264 212 DRAIFMDQGRI 222
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
330-472 |
1.05e-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: 58.33 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQL--EASRGSVR-QGTNLE-------VAYFDQyREQLDPEKT 399
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRtgLGVSGEVLiNGRPLDkrsfrkiIGYVPQ-DDILHPTLT 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 657198994 400 VVDNvgegkqevmvrgrsrhilgylqdFLFEPKrartpVKALSGGEKNRLLLA-KLFLKPSnLLILDEPTNDLD 472
Cdd:cd03213 99 VRET-----------------------LMFAAK-----LRGLSGGERKRVSIAlELVSNPS-LLFLDEPTSGLD 143
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
297-473 |
1.06e-09 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 61.52 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 297 QRRELQGKAKLQldeaGRSGKLVFETEGLGLDfGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSV 376
Cdd:PRK13657 318 DVRDPPGAIDLG----RVKGAVEFDDVSFSYD-NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRI 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 377 R-QGTNLEVAYFDQYREQL-----DP---EKTVVDNVGEGK----QEVMVRGRSRhilGYLQDFLF-EPKRARTPV---- 438
Cdd:PRK13657 393 LiDGTDIRTVTRASLRRNIavvfqDAglfNRSIEDNIRVGRpdatDEEMRAAAER---AQAHDFIErKPDGYDTVVgerg 469
|
170 180 190
....*....|....*....|....*....|....*
gi 657198994 439 KALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK13657 470 RQLSGGERQRLAIARALLKDPPILILDEATSALDV 504
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
334-467 |
1.20e-09 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 58.25 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 334 LFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRQGTNleVAYFDQY--------RE------QLDPE-- 397
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--IAYVSQEpwiqngtiREnilfgkPFDEEry 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 398 KTVV---------DNVGEGKQ-EVMVRGRSrhilgylqdflfepkrartpvkaLSGGEKNRLLLAKLFLKPSNLLILDEP 467
Cdd:cd03250 98 EKVIkacalepdlEILPDGDLtEIGEKGIN-----------------------LSGGQKQRISLARAVYSDADIYLLDDP 154
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
323-472 |
1.23e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 59.33 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 323 EGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR------QGTNLEVAYFDQyREQLDP 396
Cdd:PRK11248 5 SHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITldgkpvEGPGAERGVVFQ-NEGLLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 397 EKTVVDNVGEGKQEVMV-----RGRSRHILGYLQDFLFEPKRartpVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDL 471
Cdd:PRK11248 84 WRNVQDNVAFGLQLAGVekmqrLEIAHQMLKKVGLEGAEKRY----IWQLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
.
gi 657198994 472 D 472
Cdd:PRK11248 160 D 160
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
149-232 |
1.23e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 60.81 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 149 DPDVTLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFR---GAIVFISHDREFIHKLATRIID 225
Cdd:COG3845 395 GPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRdagAAVLLISEDLDEILALSDRIAV 474
|
....*..
gi 657198994 226 LDRGVIT 232
Cdd:COG3845 475 MYEGRIV 481
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
320-473 |
1.52e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 59.03 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 320 FETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSV-RQGTNL----------EVAYFD 388
Cdd:PRK10575 12 FALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIlLDAQPLeswsskafarKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 389 QyreQLDPEKtvvdnvGEGKQEVMVRGR-SRHilGYLQDFLFEPKR--------------ARTPVKALSGGEKNRLLLAK 453
Cdd:PRK10575 92 Q---QLPAAE------GMTVRELVAIGRyPWH--GALGRFGAADREkveeaislvglkplAHRLVDSLSGGERQRAWIAM 160
|
170 180
....*....|....*....|
gi 657198994 454 LFLKPSNLLILDEPTNDLDV 473
Cdd:PRK10575 161 LVAQDSRCLLLDEPTSALDI 180
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
331-495 |
1.55e-09 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 60.89 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 331 DRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLE----------VAYFDQyrEQLDPEKT 399
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLlDGVPLVqydhhylhrqVALVGQ--EPVLFSGS 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 400 VVDNVGEG-----KQEVMVRGRSRHILGYLQDFlfePKRARTPVKA----LSGGEKNRLLLAKLFLKPSNLLILDEPTND 470
Cdd:TIGR00958 571 VRENIAYGltdtpDEEIMAAAKAANAHDFIMEF---PNGYDTEVGEkgsqLSGGQKQRIAIARALVRKPRVLILDEATSA 647
|
170 180
....*....|....*....|....*
gi 657198994 471 LDVETLELLEELLTDYPGTLLLVSH 495
Cdd:TIGR00958 648 LDAECEQLLQESRSRASRTVLLIAH 672
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
14-231 |
1.73e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 58.99 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 14 SDFPL-LDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRL------VLQQDLKVTRLE-----QDPPAS--S 79
Cdd:PRK13648 19 SDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaITDDNFEKLRKHigivfQNPDNQfvG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 80 EITVFDYAAeGLagvgellkQYHHVSHALAHdpsdaniRTMSQLQEQLDYQNGWQYETRinqvltlldldpdvtldSLSG 159
Cdd:PRK13648 99 SIVKYDVAF-GL--------ENHAVPYDEMH-------RRVSEALKQVDMLERADYEPN-----------------ALSG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 657198994 160 GWLRKVALARALACDPDLLLLDEPTNHLDIDA----INWLEEFLKDFRGAIVFISHD-REFIHklATRIIDLDRGVI 231
Cdd:PRK13648 146 GQKQRVAIAGVLALNPSVIILDEATSMLDPDArqnlLDLVRKVKSEHNITIISITHDlSEAME--ADHVIVMNKGTV 220
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
326-472 |
1.87e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 58.99 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 326 GLDFGDRTLFqGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR--------QGTNLE-------VAYFDQY 390
Cdd:PRK13649 15 GTPFEGRALF-DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRvddtlitsTSKNKDikqirkkVGLVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 391 REQLDPEKTVVDNVGEGKQ-------EVMVRGRSRHILGYLQDFLFEpkraRTPVKaLSGGEKNRLLLAKLFLKPSNLLI 463
Cdd:PRK13649 94 PESQLFEETVLKDVAFGPQnfgvsqeEAEALAREKLALVGISESLFE----KNPFE-LSGGQMRRVAIAGILAMEPKILV 168
|
....*....
gi 657198994 464 LDEPTNDLD 472
Cdd:PRK13649 169 LDEPTAGLD 177
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
3-183 |
1.99e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 59.01 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 3 LLTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQQD--------------LKV 68
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEnipamsrsrlytvrKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 69 TRLEQDPPASSEITVFDYAAEGLagvgellkqyhhvshalahdpsdaniRTMSQLQEQLdyqngwqYETRINQVLTLLDL 148
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVAYPL--------------------------REHTQLPAPL-------LHSTVMMKLEAVGL 133
|
170 180 190
....*....|....*....|....*....|....*..
gi 657198994 149 DPDVTL--DSLSGGWLRKVALARALACDPDLLLLDEP 183
Cdd:PRK11831 134 RGAAKLmpSELSGGMARRAALARAIALEPDLIMFDEP 170
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
331-473 |
2.27e-09 |
|
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: 56.78 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 331 DRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRQGTNLEVAYFDQ--Yreqldpektvvdnvgegk 408
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQrpY------------------ 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 657198994 409 qevMVRGRSRHILGYLQDflfepkrartpvKALSGGEKNRLLLAKLFL-KPSnLLILDEPTNDLDV 473
Cdd:cd03223 75 ---LPLGTLREQLIYPWD------------DVLSGGEQQRLAFARLLLhKPK-FVFLDEATSALDE 124
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
3-212 |
2.34e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 58.59 E-value: 2.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 3 LLTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQQDLKV----TRLEQDPPAS 78
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIgyvpQKLYLDTTLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 79 SEITVFDYAAEGL--AGVGELLKQYHhVSHALahdpsdanirtmsqlqeqldyqngwqyetrinqvltlldldpDVTLDS 156
Cdd:PRK09544 84 LTVNRFLRLRPGTkkEDILPALKRVQ-AGHLI------------------------------------------DAPMQK 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 657198994 157 LSGGWLRKVALARALACDPDLLLLDEPTNHLDI-------DAINWLEeflKDFRGAIVFISHD 212
Cdd:PRK09544 121 LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVngqvalyDLIDQLR---RELDCAVLMVSHD 180
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
331-495 |
2.45e-09 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 57.87 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 331 DRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRQGTNLEVAYFDQY-REQL-----DP---EKTVV 401
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYlHSKVslvgqEPvlfARSLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 402 DNVGEGKQ-----EVMVRGRSRHILGYLQDFlfePKRARTPV----KALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:cd03248 106 DNIAYGLQscsfeCVKEAAQKAHAHSFISEL---ASGYDTEVgekgSQLSGGQKQRVAIARALIRNPQVLILDEATSALD 182
|
170 180
....*....|....*....|....*
gi 657198994 473 VETLELLEELLTDYPG--TLLLVSH 495
Cdd:cd03248 183 AESEQQVQQALYDWPErrTVLVIAH 207
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
345-472 |
2.69e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 58.10 E-value: 2.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 345 GDKIALVGPNGCGKSTLIKLL-------MGQLE--------ASRGSVRQGTNL--EVAY-FDQYreQLDPEKTVVDNV-- 404
Cdd:PRK11124 28 GETLVLLGPSGAGKSSLLRVLnllemprSGTLNiagnhfdfSKTPSDKAIRELrrNVGMvFQQY--NLWPHLTVQQNLie 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 657198994 405 ------GEGKQEVMvrGRSRHILGYLQdflFEPKRARTPVKaLSGGEKNRLLLAK-LFLKPSNLLiLDEPTNDLD 472
Cdd:PRK11124 106 apcrvlGLSKDQAL--ARAEKLLERLR---LKPYADRFPLH-LSGGQQQRVAIARaLMMEPQVLL-FDEPTAALD 173
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
330-472 |
2.83e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 60.34 E-value: 2.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTnleVAYFDQyrEQLDPEKTVVDNVGEGK 408
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHmKGS---VAYVPQ--QAWIQNDSLRENILFGK 723
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 657198994 409 QevMVRGRSRHIL---GYLQDFLFEPKRARTPVKA----LSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:TIGR00957 724 A--LNEKYYQQVLeacALLPDLEILPSGDRTEIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-229 |
2.94e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 58.66 E-value: 2.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 2 ALLTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLvlqqdlkvtRLEQDPpassei 81
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSI---------SLCGEP------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 82 tVFDYAAEGLAGVGeLLKQYHHVshalahDPsDANIRTMSQLQEQLDYQNGWQYETRINQVLTLLDLD--PDVTLDSLSG 159
Cdd:PRK13537 71 -VPSRARHARQRVG-VVPQFDNL------DP-DFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLEnkADAKVGELSG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 657198994 160 GWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDF--RG-AIVFISHDREFIHKLATRIIDLDRG 229
Cdd:PRK13537 142 GMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLlaRGkTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
330-501 |
3.06e-09 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 58.04 E-value: 3.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQ--LEASRGSVR-QG---TNLEV----------AYfdQYREQ 393
Cdd:TIGR01978 11 EDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHpsYEVTSGTILfKGqdlLELEPderaraglflAF--QYPEE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 394 LdPEKTVVDNVGEGKQEVmvrgRSRHILGYLQDFLFEpKRARTPVKAL---------------SGGEKNRL-LLAKLFLK 457
Cdd:TIGR01978 89 I-PGVSNLEFLRSALNAR----RSARGEEPLDLLDFE-KLLKEKLALLdmdeeflnrsvnegfSGGEKKRNeILQMALLE 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 657198994 458 PsNLLILDEPTNDLDVETLELLEELLTDY--PGT-LLLVSHDRRFID 501
Cdd:TIGR01978 163 P-KLAILDEIDSGLDIDALKIVAEGINRLrePDRsFLIITHYQRLLN 208
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
19-260 |
3.26e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 58.18 E-value: 3.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 19 LDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRlVLQQDLKVTRLE-------------QDPPASSEITVFD 85
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGK-VYVDGLDTSDEEnlwdirnkagmvfQNPDNQIVATIVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 86 ----YAAEGLaGVgellkqyhhvshalahDPSDanIRTmsQLQEQLDYQNGWQYEtrinqvltllDLDPDVtldsLSGGW 161
Cdd:PRK13633 105 edvaFGPENL-GI----------------PPEE--IRE--RVDESLKKVGMYEYR----------RHAPHL----LSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 162 LRKVALARALACDPDLLLLDEPTNHLD----IDAINWLEEFLKDFRGAIVFISHDREFIHKlATRIIDLDRGVITswpgn 237
Cdd:PRK13633 150 KQRVAIAGILAMRPECIIFDEPTAMLDpsgrREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVV----- 223
|
250 260
....*....|....*....|....*
gi 657198994 238 ydeyLQG--KEEWLRVEELKNAEFD 260
Cdd:PRK13633 224 ----MEGtpKEIFKEVEMMKKIGLD 244
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-473 |
3.45e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 59.63 E-value: 3.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 2 ALLTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQQdlKVTRLeQDPPASSEi 81
Cdd:PRK10762 3 ALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG--KEVTF-NGPKSSQE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 82 tvfdyaaeglAGVGELlkqyHHVSHALAHDPSDANI-------RTMSQLQEQLDYQNGWQYETRINqvltlLDLDPDVTL 154
Cdd:PRK10762 79 ----------AGIGII----HQELNLIPQLTIAENIflgrefvNRFGRIDWKKMYAEADKLLARLN-----LRFSSDKLV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 155 DSLSGGWLRKVALARALACDPDLLLLDEPTNHL-DIDA---INWLEEfLKDFRGAIVFISH----------------DRE 214
Cdd:PRK10762 140 GELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETeslFRVIRE-LKSQGRGIVYISHrlkeifeicddvtvfrDGQ 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 215 FIHKLATRIIDLDRGVitswpgnydEYLQGkeewlrveelknaefdRKLaqEEVWVRQGIKarrtrnegrvralkamrme 294
Cdd:PRK10762 219 FIAEREVADLTEDSLI---------EMMVG----------------RKL--EDQYPRLDKA------------------- 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 295 rtqrrelQGKAKLQldeagrsgklVFETEGLGLDFGDRTLFQGLDLQVlrgdkialVGPNGCGKSTLIKLLMGQLEASRG 374
Cdd:PRK10762 253 -------PGEVRLK----------VDNLSGPGVNDVSFTLRKGEILGV--------SGLMGAGRTELMKVLYGALPRTSG 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 375 SVR------------QGTNLEVAYF--DQYREQLDPEKTVVDNVG--------------EGKQEVMVRGrsrhilgylqD 426
Cdd:PRK10762 308 YVTldghevvtrspqDGLANGIVYIseDRKRDGLVLGMSVKENMSltalryfsraggslKHADEQQAVS----------D 377
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 657198994 427 F--LFEPKrarTP-----VKALSGGEKNRLLLAK-LFLKPsNLLILDEPTNDLDV 473
Cdd:PRK10762 378 FirLFNIK---TPsmeqaIGLLSGGNQQKVAIARgLMTRP-KVLILDEPTRGVDV 428
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-247 |
3.65e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 58.13 E-value: 3.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 11 LSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLvlQQDLKVTRLEQDppasseitVFDYAAEG 90
Cdd:PRK14246 18 LYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKI--KVDGKVLYFGKD--------IFQIDAIK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 91 L-AGVGELLKQ---------YHHVSHAL-AHDPSDAniRTMSQLQEQLDYQNGWQYET--RINQVLTlldldpdvtldSL 157
Cdd:PRK14246 88 LrKEVGMVFQQpnpfphlsiYDNIAYPLkSHGIKEK--REIKKIVEECLRKVGLWKEVydRLNSPAS-----------QL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 158 SGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRG--AIVFISHDREFIHKLATRIIDLDRGVITSWP 235
Cdd:PRK14246 155 SGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYVAFLYNGELVEWG 234
|
250
....*....|..
gi 657198994 236 GNYDEYLQGKEE 247
Cdd:PRK14246 235 SSNEIFTSPKNE 246
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
9-189 |
3.67e-09 |
|
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: 60.31 E-value: 3.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 9 ASLSFSDF-----PLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRlvLQQDLKVTRLEQDP---PAsse 80
Cdd:TIGR01271 427 DGLFFSNFslyvtPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGK--IKHSGRISFSPQTSwimPG--- 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 81 iTVFDYAAEGLAgvgelLKQYHHVShalahdpsdanIRTMSQLQEQLDyqngwQYETRINQVLtlldLDPDVTldsLSGG 160
Cdd:TIGR01271 502 -TIKDNIIFGLS-----YDEYRYTS-----------VIKACQLEEDIA-----LFPEKDKTVL----GEGGIT---LSGG 552
|
170 180
....*....|....*....|....*....
gi 657198994 161 WLRKVALARALACDPDLLLLDEPTNHLDI 189
Cdd:TIGR01271 553 QRARISLARAVYKDADLYLLDSPFTHLDV 581
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
325-497 |
3.76e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.88 E-value: 3.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 325 LGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSV---RQGTNLEVAYFDQ------YREQLD 395
Cdd:PRK13540 7 LDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEIlfeRQSIKKDLCTYQKqlcfvgHRSGIN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 396 PEKTVVDN------VGEGKQEV--MVRGRSrhiLGYLQDFlfepkrartPVKALSGGEKNRLLLAKLFLKPSNLLILDEP 467
Cdd:PRK13540 87 PYLTLRENclydihFSPGAVGIteLCRLFS---LEHLIDY---------PCGLLSSGQKRQVALLRLWMSKAKLWLLDEP 154
|
170 180 190
....*....|....*....|....*....|...
gi 657198994 468 TNDLDVETLELLEELLTDYP---GTLLLVSHDR 497
Cdd:PRK13540 155 LVALDELSLLTIITKIQEHRakgGAVLLTSHQD 187
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
320-541 |
3.83e-09 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 57.89 E-value: 3.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 320 FETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNL---------------E 383
Cdd:TIGR02769 12 YRTGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSfRGQDLyqldrkqrrafrrdvQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 384 VAYFDQYrEQLDPEKTVVDNVGEGKQEVM---VRGRSRHILGYLQDFLFEPKRARTPVKALSGGEKNRLLLAK-LFLKPs 459
Cdd:TIGR02769 92 LVFQDSP-SAVNPRMTVRQIIGEPLRHLTsldESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARaLAVKP- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 460 NLLILDEPTNDLDVETLELLEELLTDYP---GT-LLLVSHDRRFIDNTVTGCWLFEGDGRISDYVGGYADMM---ATRAL 532
Cdd:TIGR02769 170 KLIVLDEAVSNLDMVLQAVILELLRKLQqafGTaYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLSFkhpAGRNL 249
|
....*....
gi 657198994 533 QAAQQTAKP 541
Cdd:TIGR02769 250 QSAVLPEHP 258
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
336-473 |
3.84e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 58.56 E-value: 3.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 336 QGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRqgtnleVAYFDQYREqldpEKTVVDNVGegkqevMVRG 415
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR------VLGYVPFKR----RKEFARRIG------VVFG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 416 -RS---------------RHI-----------LGYL------QDFLfepkraRTPVKALSGGEKNRL-LLAKLFLKPSnL 461
Cdd:COG4586 103 qRSqlwwdlpaidsfrllKAIyripdaeykkrLDELvelldlGELL------DTPVRQLSLGQRMRCeLAAALLHRPK-I 175
|
170
....*....|..
gi 657198994 462 LILDEPTNDLDV 473
Cdd:COG4586 176 LFLDEPTIGLDV 187
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2-237 |
3.91e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 59.74 E-value: 3.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 2 ALLTLHGASLSF----SDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIAS-ELPLDDGRLVLQQDlkVTRLEQDPP 76
Cdd:PRK10535 3 ALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGClDKPTSGTYRVAGQD--VATLDADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 77 ASSEITVFdyaaeglagvGELLKQYHHVSH-ALAHDPSDANIRTMSQLQEQLDyqngwqyetRINQVLTLLDLDPDVTL- 154
Cdd:PRK10535 81 AQLRREHF----------GFIFQRYHLLSHlTAAQNVEVPAVYAGLERKQRLL---------RAQELLQRLGLEDRVEYq 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 155 -DSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFR--GAIVFI-SHDREfIHKLATRIIDLDRGV 230
Cdd:PRK10535 142 pSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRdrGHTVIIvTHDPQ-VAAQAERVIEIRDGE 220
|
....*..
gi 657198994 231 ITSWPGN 237
Cdd:PRK10535 221 IVRNPPA 227
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
316-473 |
4.09e-09 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 56.29 E-value: 4.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 316 GKLVFETEGLGLdfgdRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSV------------RQGTNLE 383
Cdd:cd03215 1 GEPVLEVRGLSV----KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEItldgkpvtrrspRDAIRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 384 VAYF--DQYREQLDPEKTVVDNVgegkqevmvrgrsrhILGYLqdflfepkrartpvkaLSGGEKNRLLLAKLFLKPSNL 461
Cdd:cd03215 77 IAYVpeDRKREGLVLDLSVAENI---------------ALSSL----------------LSGGNQQKVVLARWLARDPRV 125
|
170
....*....|..
gi 657198994 462 LILDEPTNDLDV 473
Cdd:cd03215 126 LILDEPTRGVDV 137
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
12-211 |
4.22e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 57.73 E-value: 4.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 12 SFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASElP---LDDGRLVLQQDlkvTRLEQDPPASSEITV---FD 85
Cdd:CHL00131 16 SVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH-PaykILEGDILFKGE---SILDLEPEERAHLGIflaFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 86 YAAEgLAGVG--ELLKqyhhvshaLAHdpsdaNIRTMSQLQEQLDYQNGWQYetrINQVLTLLDLDP-----DVTlDSLS 158
Cdd:CHL00131 92 YPIE-IPGVSnaDFLR--------LAY-----NSKRKFQGLPELDPLEFLEI---INEKLKLVGMDPsflsrNVN-EGFS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 657198994 159 GGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRG---AIVFISH 211
Cdd:CHL00131 154 GGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTsenSIILITH 209
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
329-472 |
4.30e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 57.41 E-value: 4.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 329 FGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIK------------LLMGQLEASRGSV-----RQGTNLevaYFDQYr 391
Cdd:PRK09493 11 FGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRcinkleeitsgdLIVDGLKVNDPKVderliRQEAGM---VFQQF- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 392 eQLDPEKTVVDNVGEGKqeVMVRGRSRHILGYLQDFLFE----PKRARTPVKALSGGEKNRLLLAK-LFLKPsNLLILDE 466
Cdd:PRK09493 87 -YLFPHLTALENVMFGP--LRVRGASKEEAEKQARELLAkvglAERAHHYPSELSGGQQQRVAIARaLAVKP-KLMLFDE 162
|
....*.
gi 657198994 467 PTNDLD 472
Cdd:PRK09493 163 PTSALD 168
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
329-472 |
5.09e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 58.50 E-value: 5.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 329 FGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRQGTNL--EVA--------YFDQYreQLDPEK 398
Cdd:PRK11000 13 YGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRmnDVPpaergvgmVFQSY--ALYPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 399 TVVDNV-------GEGKQEvmVRGRSRHILGYLQ-DFLFEpkraRTPvKALSGGEKNRLLLAKLFLKPSNLLILDEPTND 470
Cdd:PRK11000 91 SVAENMsfglklaGAKKEE--INQRVNQVAEVLQlAHLLD----RKP-KALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
|
..
gi 657198994 471 LD 472
Cdd:PRK11000 164 LD 165
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
149-232 |
5.56e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.91 E-value: 5.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 149 DPDVTLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRG---AIVFISHDREFIHKLATRIID 225
Cdd:PRK15439 396 HAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAqnvAVLFISSDLEEIEQMADRVLV 475
|
....*..
gi 657198994 226 LDRGVIT 232
Cdd:PRK15439 476 MHQGEIS 482
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-253 |
5.78e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 57.38 E-value: 5.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 29 GERLCLVGRNGAGKSTLMKVIASELPLDDGRLvlqqdlkvtrleQDPPASSEITVF-------DYAAEGLAGVGELLKQY 101
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKF------------DDPPDWDEILDEfrgselqNYFTKLLEGDVKVIVKP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 102 HHVSHAlahdPSDANIRTmSQLQEQLDYQNgwqyetRINQVLTLLDLDP--DVTLDSLSGGWLRKVALARALACDPDLLL 179
Cdd:cd03236 94 QYVDLI----PKAVKGKV-GELLKKKDERG------KLDELVDQLELRHvlDRNIDQLSGGELQRVAIAAALARDADFYF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 180 LDEPTNHLDI----DAINWLEEFLKDFRgAIVFISHDREFIHKLATRIIDL-----DRGVITSWPG---NYDEYLQG--K 245
Cdd:cd03236 163 FDEPSSYLDIkqrlNAARLIRELAEDDN-YVLVVEHDLAVLDYLSDYIHCLygepgAYGVVTLPKSvreGINEFLDGylP 241
|
....*...
gi 657198994 246 EEWLRVEE 253
Cdd:cd03236 242 TENMRFRE 249
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
332-472 |
8.75e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 57.02 E-value: 8.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 332 RTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNleVAYFDQYRE--------QlDPEK---- 398
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILiDGKD--VTKLPEYKRakyigrvfQ-DPMMgtap 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 399 --TVVDNV----GEGKQevmvRGRSRHILGYLQDFLFE---------PKRARTPVKALSGGEknR----LLLAKLflKPS 459
Cdd:COG1101 96 smTIEENLalayRRGKR----RGLRRGLTKKRRELFREllatlglglENRLDTKVGLLSGGQ--RqalsLLMATL--TKP 167
|
170
....*....|...
gi 657198994 460 NLLILDEPTNDLD 472
Cdd:COG1101 168 KLLLLDEHTAALD 180
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
337-473 |
8.94e-09 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 57.41 E-value: 8.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 337 GLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLEVAYFDQYRE--------------QLDPEKTVV 401
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAwLGKDLLGMKDDEWRAvrsdiqmifqdplaSLNPRMTIG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 402 DNVGE---------GKQEVMVRGRSRHI-LGYLQDFLfepkrARTPvKALSGGEKNRLLLAK-LFLKPsNLLILDEPTND 470
Cdd:PRK15079 119 EIIAEplrtyhpklSRQEVKDRVKAMMLkVGLLPNLI-----NRYP-HEFSGGQCQRIGIARaLILEP-KLIICDEPVSA 191
|
...
gi 657198994 471 LDV 473
Cdd:PRK15079 192 LDV 194
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-188 |
9.83e-09 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 57.42 E-value: 9.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 4 LTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIAS-ELPLDDGRLVLQQDLKVTRLEQdppasSEI- 81
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGlEKPTEGQIFIDGEDVTHRSIQQ-----RDIc 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 82 TVFDyaaeglagvgellkqyhhvSHAL-AHdpsdanirtMSqLQEQLDY------QNGWQYETRINQVLTLLDLD--PDV 152
Cdd:PRK11432 82 MVFQ-------------------SYALfPH---------MS-LGENVGYglkmlgVPKEERKQRVKEALELVDLAgfEDR 132
|
170 180 190
....*....|....*....|....*....|....*.
gi 657198994 153 TLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLD 188
Cdd:PRK11432 133 YVDQISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
337-473 |
1.06e-08 |
|
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: 56.99 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 337 GLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEA---SRGSVR-QGTNL--------------EVAY-FdqyreQ---- 393
Cdd:COG0444 23 GVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILfDGEDLlklsekelrkirgrEIQMiF-----Qdpmt 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 394 -LDPEKTVVDNVGE--------GKQEVmvRGRSRHILG---------YLQDFLFEpkrartpvkaLSGGEKNRLLLAK-L 454
Cdd:COG0444 98 sLNPVMTVGDQIAEplrihgglSKAEA--RERAIELLErvglpdperRLDRYPHE----------LSGGMRQRVMIARaL 165
|
170
....*....|....*....
gi 657198994 455 FLKPSnLLILDEPTNDLDV 473
Cdd:COG0444 166 ALEPK-LLIADEPTTALDV 183
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-226 |
1.12e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 55.88 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 2 ALLTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQQDlKVTRLeqdPPASSEI 81
Cdd:PRK10247 6 PLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGE-DISTL---KPEIYRQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 82 TVfDYAAEGLAGVGELLKQYHHVSHALAHDPSDanirtMSQLQEQLDyqngwqyetRINQVLTLLdldpDVTLDSLSGGW 161
Cdd:PRK10247 82 QV-SYCAQTPTLFGDTVYDNLIFPWQIRNQQPD-----PAIFLDDLE---------RFALPDTIL----TKNIAELSGGE 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 657198994 162 LRKVALARALACDPDLLLLDEPTNHLDIDAINWLEE----FLKDFRGAIVFISHDREFIhKLATRIIDL 226
Cdd:PRK10247 143 KQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEiihrYVREQNIAVLWVTHDKDEI-NHADKVITL 210
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
17-232 |
1.18e-08 |
|
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: 57.84 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 17 PLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELP-------LDD-----------GRLV--LQQDlkVT------- 69
Cdd:COG4618 346 PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPptagsvrLDGadlsqwdreelGRHIgyLPQD--VElfdgtia 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 70 ----RLEQDPPASseitVFDyAAEgLAGVgellkqyhhvsHALahdpsdanIRTMSQlqeqldyqnGwqYETRINQVLTl 145
Cdd:COG4618 424 eniaRFGDADPEK----VVA-AAK-LAGV-----------HEM--------ILRLPD---------G--YDTRIGEGGA- 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 146 ldldpdvtldSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFR---GAIVFISHDREFIhKLATR 222
Cdd:COG4618 467 ----------RLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKargATVVVITHRPSLL-AAVDK 535
|
250
....*....|
gi 657198994 223 IIDLDRGVIT 232
Cdd:COG4618 536 LLVLRDGRVQ 545
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
337-473 |
1.24e-08 |
|
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: 55.84 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 337 GLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVrqgtnlEVAYFDQYREQLDpektVVDNVG--EGKQEVMVR 414
Cdd:cd03266 23 GVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFA------TVDGFDVVKEPAE----ARRRLGfvSDSTGLYDR 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 657198994 415 GRSRHILGYLQDFL-------------------FEPKRARtPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:cd03266 93 LTARENLEYFAGLYglkgdeltarleeladrlgMEELLDR-RVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDV 169
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
19-212 |
1.53e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 56.90 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 19 LDHAELTIERGERLCLVGRNGAGKSTLmkviaselplddGRLVlqqdlkvTRLEqdPPASSEITvfdYAAEGLAGVG-EL 97
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTL------------ARLL-------TMIE--TPTGGELY---YQGQDLLKADpEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 98 LKQYHHVSHALAHDP-SDANIRTM--SQLQEQLDYQNGWQYETRINQVLTLLDLdpdVTLDS---------LSGGWLRKV 165
Cdd:PRK11308 87 QKLLRQKIQIVFQNPyGSLNPRKKvgQILEEPLLINTSLSAAERREKALAMMAK---VGLRPehydryphmFSGGQRQRI 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 657198994 166 ALARALACDPDLLLLDEPTNHLD--IDA--INWLEEFLKDFRGAIVFISHD 212
Cdd:PRK11308 164 AIARALMLDPDVVVADEPVSALDvsVQAqvLNLMMDLQQELGLSYVFISHD 214
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-229 |
1.63e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 56.38 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 19 LDHAELTIERGERLCLVGRNGAGKSTLMKVIaselpldDGRLVlqqdlkvtrleqdpPASSEITVFDYAAEGLAGVGELL 98
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHF-------NALLK--------------PSSGTITIAGYHITPETGNKNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 99 KQYHHVShaLAHDPSDANIRTMSQLQE-QLDYQN-GWQYETRINQVLTLLD---LDPDVTLDS---LSGGWLRKVALARA 170
Cdd:PRK13641 82 KLRKKVS--LVFQFPEAQLFENTVLKDvEFGPKNfGFSEDEAKEKALKWLKkvgLSEDLISKSpfeLSGGQMRRVAIAGV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 657198994 171 LACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRGA---IVFISHDREFIHKLATRIIDLDRG 229
Cdd:PRK13641 160 MAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAghtVILVTHNMDDVAEYADDVLVLEHG 221
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
25-212 |
1.66e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 56.66 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 25 TIERGERLCLVGRNGAGKS----TLMKVIASELPLD-----DGRLVL---QQDLKVTRLE------QDPPASseITVFDY 86
Cdd:PRK09473 38 SLRAGETLGIVGESGSGKSqtafALMGLLAANGRIGgsatfNGREILnlpEKELNKLRAEqismifQDPMTS--LNPYMR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 87 AAEGLAgvgELLKQYHHVSHALAHDPSdanIRTMS--QLQEQLDYQNGWQYEtrinqvltlldldpdvtldsLSGGWLRK 164
Cdd:PRK09473 116 VGEQLM---EVLMLHKGMSKAEAFEES---VRMLDavKMPEARKRMKMYPHE--------------------FSGGMRQR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 657198994 165 VALARALACDPDLLLLDEPTNHLDIDA----INWLEEFLKDFRGAIVFISHD 212
Cdd:PRK09473 170 VMIAMALLCRPKLLIADEPTTALDVTVqaqiMTLLNELKREFNTAIIMITHD 221
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-191 |
1.77e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 57.32 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 17 PLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQQDLKVTRLEQDPPAS-----SEitvfDYAAEGL 91
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANgivyiSE----DRKRDGL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 92 A---GVGE-----LLKQYHHVSHALAHDPSDA---------NIRTMSQLQeqldyqngwqyetrinqvltlldldpdvTL 154
Cdd:PRK10762 342 VlgmSVKEnmsltALRYFSRAGGSLKHADEQQavsdfirlfNIKTPSMEQ----------------------------AI 393
|
170 180 190
....*....|....*....|....*....|....*..
gi 657198994 155 DSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDA 191
Cdd:PRK10762 394 GLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGA 430
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
14-233 |
1.83e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 55.89 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 14 SDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQQDL-----------KVTRLEQDPPAS-SEI 81
Cdd:PRK13650 18 QEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLlteenvwdirhKIGMVFQNPDNQfVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 82 TVFDYAAEGLAGVGellkqyhhvshalahdpsdanirtmsqlqeqLDYQngwQYETRINQVLTLLDLD--PDVTLDSLSG 159
Cdd:PRK13650 98 TVEDDVAFGLENKG-------------------------------IPHE---EMKERVNEALELVGMQdfKEREPARLSG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 657198994 160 GWLRKVALARALACDPDLLLLDEPTNHLD----IDAINWLEEFLKDFRGAIVFISHDREFIhKLATRIIDLDRGVITS 233
Cdd:PRK13650 144 GQKQRVAIAGAVAMRPKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVES 220
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-468 |
1.87e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 57.83 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 6 LHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRL-VLQQDLKVTRLEQDppASSEITvf 84
Cdd:NF033858 4 LEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVeVLGGDMADARHRRA--VCPRIA-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 85 dYAAEGLagvGELLkqYHhvshalahdpsdanirTMSqLQEQLDY------QNGWQYETRINQVLTLLDLDPdvTLD--- 155
Cdd:NF033858 80 -YMPQGL---GKNL--YP----------------TLS-VFENLDFfgrlfgQDAAERRRRIDELLRATGLAP--FADrpa 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 156 -SLSGGWLRKVALARALACDPDLLLLDEPTNHLD----------IDAInwleeflkdfRGA------IVfishdrefihk 218
Cdd:NF033858 135 gKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDplsrrqfwelIDRI----------RAErpgmsvLV----------- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 219 lATriidldrgvitswpgnydEYLqgkeewlrvEElknAE-FDRKLAQeevwvrqgikarrtrNEGRVRALKAMR--MER 295
Cdd:NF033858 194 -AT------------------AYM---------EE---AErFDWLVAM---------------DAGRVLATGTPAelLAR 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 296 TQRREL-------------QGKAKLQLD--EAGRSGKLVFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKST 360
Cdd:NF033858 228 TGADTLeaafiallpeekrRGHQPVVIPprPADDDDEPAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKST 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 361 LIKLLMGQLEASRGSVR------QGTNLE----VAYFDQ----Y-----REQLD--------PEKTVVDNVGEgkqevMV 413
Cdd:NF033858 308 TMKMLTGLLPASEGEAWlfgqpvDAGDIAtrrrVGYMSQafslYgeltvRQNLElharlfhlPAAEIAARVAE-----ML 382
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 657198994 414 RgrsRHILGYLQDFLFEpkrartpvkALSGGEKNRLLLAKLFL-KPSnLLILDEPT 468
Cdd:NF033858 383 E---RFDLADVADALPD---------SLPLGIRQRLSLAVAVIhKPE-LLILDEPT 425
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
329-497 |
1.97e-08 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 56.69 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 329 FGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRQG-----TNLE-----VAY-FDQYreQLDPE 397
Cdd:COG1118 12 FGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNgrdlfTNLPprerrVGFvFQHY--ALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 398 KTVVDNVGEGKQevmVRGRSRH-----ILGYLQDFLFEPKRARTPvKALSGGEKNRLLLAK-LFLKPSnLLILDEPTNDL 471
Cdd:COG1118 90 MTVAENIAFGLR---VRPPSKAeirarVEELLELVQLEGLADRYP-SQLSGGQRQRVALARaLAVEPE-VLLLDEPFGAL 164
|
170 180 190
....*....|....*....|....*....|
gi 657198994 472 DVETLELL----EELLTDYPGTLLLVSHDR 497
Cdd:COG1118 165 DAKVRKELrrwlRRLHDELGGTTVFVTHDQ 194
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
149-232 |
2.10e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 56.95 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 149 DPDVTLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDA----INWLEEFLKdfRG-AIVFISHDREFIHKLATRI 223
Cdd:COG1129 387 SPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAkaeiYRLIRELAA--EGkAVIVISSELPELLGLSDRI 464
|
....*....
gi 657198994 224 IDLDRGVIT 232
Cdd:COG1129 465 LVMREGRIV 473
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
4-231 |
2.57e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 55.48 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 4 LTLHGASLSfSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELP----------LDDGRLVLQQDL---KVTR 70
Cdd:PRK10418 5 IELRNIALQ-AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPagvrqtagrvLLDGKPVAPCALrgrKIAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 71 LEQDPPASSE--ITVFDYAAEGLAGVGELlkqyhhvshalahdPSDAnirtmsQLQEQLDyqngwqyETRINQVLTLLDL 148
Cdd:PRK10418 84 IMQNPRSAFNplHTMHTHARETCLALGKP--------------ADDA------TLTAALE-------AVGLENAARVLKL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 149 DPDvtldSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDA----INWLEEFLKDFRGAIVFISHDREFIHKLATRII 224
Cdd:PRK10418 137 YPF----EMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAqariLDLLESIVQKRALGMLLVTHDMGVVARLADDVA 212
|
....*..
gi 657198994 225 DLDRGVI 231
Cdd:PRK10418 213 VMSHGRI 219
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
344-503 |
2.74e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 53.15 E-value: 2.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 344 RGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVrqgtnlevayfdqyreqldpektVVDNVGEGKQEVMVRGRSRHILGY 423
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV-----------------------IYIDGEDILEEVLDQLLLIIVGGK 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 424 lqdflfepkrartpVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEELLTDYPGTLLLVSHDRRFIDNT 503
Cdd:smart00382 58 --------------KASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTT 123
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1-216 |
2.78e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 54.58 E-value: 2.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 1 MALLTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELP--LDDGRLVLQQDL---KVTRLEQDP 75
Cdd:COG2401 28 AIVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQfgrEASLIDAIG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 76 PASSeitvFDYAAEGLAGVG-----ELLKQYHHVShalahdpsdanirtmsqlqeqldyqNGWQYetrinqvltlldldp 150
Cdd:COG2401 108 RKGD----FKDAVELLNAVGlsdavLWLRRFKELS-------------------------TGQKF--------------- 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 657198994 151 dvtldslsggwlrKVALARALACDPDLLLLDEPTNHLD-----IDAINWLeEFLKDFRGAIVFISHDREFI 216
Cdd:COG2401 144 -------------RFRLALLLAERPKLLVIDEFCSHLDrqtakRVARNLQ-KLARRAGITLVVATHHYDVI 200
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
157-231 |
2.92e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 55.36 E-value: 2.92e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 657198994 157 LSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFR---GAIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:PRK10619 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAeegKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
320-467 |
2.93e-08 |
|
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: 54.86 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 320 FETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRQG----TNLEV--------AYF 387
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDgqdiTKLPMhkrarlgiGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 388 DQ----YREQldpekTVVDN---VGEGkQEVMVRGRSRHILGYLQDFLFEPKRaRTPVKALSGGEKNRLLLAK-LFLKPS 459
Cdd:cd03218 81 PQeasiFRKL-----TVEENilaVLEI-RGLSKKEREEKLEELLEEFHITHLR-KSKASSLSGGERRRVEIARaLATNPK 153
|
....*...
gi 657198994 460 NLLiLDEP 467
Cdd:cd03218 154 FLL-LDEP 160
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
19-231 |
2.97e-08 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 55.96 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 19 LDHAELTIERGERLCLVGRNGAGKSTLMKVI-ASELPlDDGRLVLQ-QDLkvTRLEQDP--PASSEI------------- 81
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCInLLERP-TSGRVLVDgQDL--TALSEKElrKARRQIgmifqhfnllssr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 82 TVFDYAA---EgLAGVgellkqyhhvshalahdpSDANIrtmsqlqeqldyqngwqyETRINQVLTLLDLDP--DVTLDS 156
Cdd:PRK11153 98 TVFDNVAlplE-LAGT------------------PKAEI------------------KARVTELLELVGLSDkaDRYPAQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 657198994 157 LSGGWLRKVALARALACDPDLLLLDEPTNHLD---IDAI-NWLEEFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:PRK11153 141 LSGGQKQRVAIARALASNPKVLLCDEATSALDpatTRSIlELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
340-473 |
3.18e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 55.27 E-value: 3.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 340 LQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSV---RQGTNLE-----VAYFDQyREQLDPEKTVVdnvgegKQEV 411
Cdd:PRK15056 28 FTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKIsilGQPTRQAlqknlVAYVPQ-SEEVDWSFPVL------VEDV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 412 MVRGRSRHiLGYLQdflfEPK-RARTPVKA-----------------LSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:PRK15056 101 VMMGRYGH-MGWLR----RAKkRDRQIVTAalarvdmvefrhrqigeLSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
345-472 |
3.34e-08 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 54.63 E-value: 3.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 345 GDKIALVGPNGCGKSTLIKLL-------MGQLE--------ASRGSVRQGTNL--EVAY-FDQYreQLDPEKTVVDNV-- 404
Cdd:COG4161 28 GETLVLLGPSGAGKSSLLRVLnlletpdSGQLNiaghqfdfSQKPSEKAIRLLrqKVGMvFQQY--NLWPHLTVMENLie 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 657198994 405 ------GEGKQEVmvRGRSRHILGYLQdflFEPKRARTPVkALSGGEKNRLLLAK-LFLKPSNLLiLDEPTNDLD 472
Cdd:COG4161 106 apckvlGLSKEQA--REKAMKLLARLR---LTDKADRFPL-HLSGGQQQRVAIARaLMMEPQVLL-FDEPTAALD 173
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
330-472 |
3.38e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 55.19 E-value: 3.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLEVAYFDQYREQL-----DPEKTVVD- 402
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLiRGEPITKENIREVRKFVglvfqNPDDQIFSp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 403 -----------NVGEGKQEVMVRGRSR-HILGylqdflFEPKRARTPvKALSGGEKNRLLLAKLFLKPSNLLILDEPTND 470
Cdd:PRK13652 95 tveqdiafgpiNLGLDEETVAHRVSSAlHMLG------LEELRDRVP-HHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAG 167
|
..
gi 657198994 471 LD 472
Cdd:PRK13652 168 LD 169
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
17-227 |
3.62e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 54.04 E-value: 3.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 17 PLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQ-QDLKvtrlEQDPpasseitvfDYAAEGL---- 91
Cdd:PRK13538 15 ILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQgEPIR----RQRD---------EYHQDLLylgh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 92 -AGVGELLKQYHHV--SHALAHDPSDANIrtmsqlqeqldyqngWQYETRINqvltlLDLDPDVTLDSLSGGWLRKVALA 168
Cdd:PRK13538 82 qPGIKTELTALENLrfYQRLHGPGDDEAL---------------WEALAQVG-----LAGFEDVPVRQLSAGQQRRVALA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 657198994 169 RALACDPDLLLLDEPTNHLDIDAINWLEEFLKDF--RGAIV-FISHDREFIHKLATRIIDLD 227
Cdd:PRK13538 142 RLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHaeQGGMViLTTHQDLPVASDKVRKLRLG 203
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
321-472 |
3.92e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 55.11 E-value: 3.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLEVAYFDQ--YreqLdPE 397
Cdd:COG4152 3 ELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLwDGEPLDPEDRRRigY---L-PE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 398 -------KTVVDNV-------GEGKQEVMVRGrsrhilgylqDFLFE----PKRARTPVKALSGGEKNRL-LLAKLFLKP 458
Cdd:COG4152 79 erglypkMKVGEQLvylarlkGLSKAEAKRRA----------DEWLErlglGDRANKKVEELSKGNQQKVqLIAALLHDP 148
|
170
....*....|....
gi 657198994 459 SnLLILDEPTNDLD 472
Cdd:COG4152 149 E-LLILDEPFSGLD 161
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
18-222 |
3.92e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 54.40 E-value: 3.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 18 LLDHAELTIERGERLCLVGRNGAGKSTLMKVIASelpLDDGR----LVLQQDLKVTRLEQDppasseitvfdyAAEGLAG 93
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAG---LDDGSsgevSLVGQPLHQMDEEAR------------AKLRAKH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 94 VGELLKQYHHVshalahdPSdANIRTMSQLQEQLDYQNGWQYETRINQVLTLLDLDPDVTL--DSLSGGWLRKVALARAL 171
Cdd:PRK10584 90 VGFVFQSFMLI-------PT-LNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHlpAQLSGGEQQRVALARAF 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 657198994 172 ACDPDLLLLDEPTNHLDIDAINWLEEFL----KDFRGAIVFISHDREfihkLATR 222
Cdd:PRK10584 162 NGRPDVLFADEPTGNLDRQTGDKIADLLfslnREHGTTLILVTHDLQ----LAAR 212
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
2-226 |
4.21e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.08 E-value: 4.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 2 ALLTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLvlqqdlkvtRLEQDPPASSEI 81
Cdd:PRK13543 10 PLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQI---------QIDGKTATRGDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 82 TvfdyaaeglagvgellkqyHHVSHaLAHDPS-DANIRTMSQLQeQLDYQNGWQYETRINQVLTLLDLD--PDVTLDSLS 158
Cdd:PRK13543 81 S-------------------RFMAY-LGHLPGlKADLSTLENLH-FLCGLHGRRAKQMPGSALAIVGLAgyEDTLVRQLS 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 657198994 159 GGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDF---RGAIVFISHDREFIHKLATRIIDL 226
Cdd:PRK13543 140 AGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHlrgGGAALVTTHGAYAAPPVRTRMLTL 210
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
318-472 |
4.22e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 54.74 E-value: 4.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 318 LVFETEGLGLDFGDRT-LFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLEVAYFDQYREQL- 394
Cdd:PRK13647 3 NIIEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKvMGREVNAENEKWVRSKVg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 395 ----DPE-----KTVVD-------NVGEGKQEVMVRGRSRHILGYLQDFlfepkRARTPVKaLSGGEKNRLLLAKLFLKP 458
Cdd:PRK13647 83 lvfqDPDdqvfsSTVWDdvafgpvNMGLDKDEVERRVEEALKAVRMWDF-----RDKPPYH-LSYGQKKRVAIAGVLAMD 156
|
170
....*....|....
gi 657198994 459 SNLLILDEPTNDLD 472
Cdd:PRK13647 157 PDVIVLDEPMAYLD 170
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
321-472 |
4.26e-08 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 54.51 E-value: 4.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 321 ETEGLGLDFGDR----TLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGqLEA-SRGSVR-QGTNL------------ 382
Cdd:cd03258 3 ELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCING-LERpTSGSVLvDGTDLtllsgkelrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 383 -EVAY-FDQYreQLDPEKTVVDNV-------GEGKQEvmVRGRSRHILgylqDFL-FEPKRARTPvKALSGGEKNRLLLA 452
Cdd:cd03258 82 rRIGMiFQHF--NLLSSRTVFENValpleiaGVPKAE--IEERVLELL----ELVgLEDKADAYP-AQLSGGQKQRVGIA 152
|
170 180
....*....|....*....|.
gi 657198994 453 K-LFLKPSnLLILDEPTNDLD 472
Cdd:cd03258 153 RaLANNPK-VLLCDEATSALD 172
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
330-472 |
4.64e-08 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 54.23 E-value: 4.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNleVAYFDQ--------YREQ---LDPE 397
Cdd:cd03295 12 GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFiDGED--IREQDPvelrrkigYVIQqigLFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 398 KTVVDNVG-----EGKQEVMVRGRSRHILGYLQdflFEPK--RARTPvKALSGGEKNRLLLAKLFLKPSNLLILDEPTND 470
Cdd:cd03295 90 MTVEENIAlvpklLKWPKEKIRERADELLALVG---LDPAefADRYP-HELSGGQQQRVGVARALAADPPLLLMDEPFGA 165
|
..
gi 657198994 471 LD 472
Cdd:cd03295 166 LD 167
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
329-499 |
4.65e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 54.59 E-value: 4.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 329 FGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR---------QGTNLEVAYFDQYREQLDPEK- 398
Cdd:PRK10619 15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVvngqtinlvRDKDGQLKVADKNQLRLLRTRl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 399 -------------TVVDNVGEGKQEVM----VRGRSRHILGYLQDFLFEPKRARTPVKaLSGGEKNRLLLAKLFLKPSNL 461
Cdd:PRK10619 95 tmvfqhfnlwshmTVLENVMEAPIQVLglskQEARERAVKYLAKVGIDERAQGKYPVH-LSGGQQQRVSIARALAMEPEV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 657198994 462 LILDEPTNDLD---VETLELLEELLTDYPGTLLLVSHDRRF 499
Cdd:PRK10619 174 LLFDEPTSALDpelVGEVLRIMQQLAEEGKTMVVVTHEMGF 214
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
319-472 |
5.06e-08 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 54.27 E-value: 5.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 319 VFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLL--MGQLEAsrgSVR-QGtnlEVAYFDQ--YREQ 393
Cdd:COG1117 11 KIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMNDLIP---GARvEG---EILLDGEdiYDPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 394 LDPE-----------------KTVVDNVGEGkqeVMVRG-RSRHILgylqDFLFEP--KRA----------RTPVKALSG 443
Cdd:COG1117 85 VDVVelrrrvgmvfqkpnpfpKSIYDNVAYG---LRLHGiKSKSEL----DEIVEEslRKAalwdevkdrlKKSALGLSG 157
|
170 180 190
....*....|....*....|....*....|
gi 657198994 444 GEKNRLLLAK-LFLKPSNLLiLDEPTNDLD 472
Cdd:COG1117 158 GQQQRLCIARaLAVEPEVLL-MDEPTSALD 186
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
9-189 |
5.20e-08 |
|
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: 54.86 E-value: 5.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 9 ASLSFSDF-----PLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQQDLKVTrleqdpPASSEITV 83
Cdd:cd03291 38 NNLFFSNLclvgaPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFS------SQFSWIMP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 84 FDYAAEGLAGVGELLKQYHHVSHAlahdpsdanirtmSQLQEQLDyqngwQYETRINQVLTLLDLdpdvtldSLSGGWLR 163
Cdd:cd03291 112 GTIKENIIFGVSYDEYRYKSVVKA-------------CQLEEDIT-----KFPEKDNTVLGEGGI-------TLSGGQRA 166
|
170 180
....*....|....*....|....*.
gi 657198994 164 KVALARALACDPDLLLLDEPTNHLDI 189
Cdd:cd03291 167 RISLARAVYKDADLYLLDSPFGYLDV 192
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
11-188 |
5.29e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 56.01 E-value: 5.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 11 LSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLddgrlvlQQDLKVTRLEQdppasSEITVFDYAAEg 90
Cdd:PRK11174 358 LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-------QGSLKINGIEL-----RELDPESWRKH- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 91 LAGVGE---LLKQYHHVSHALA-HDPSDAnirtmsQLQEQLDyqngwqyETRINQVLTLLD--LDPDVTLDS--LSGGWL 162
Cdd:PRK11174 425 LSWVGQnpqLPHGTLRDNVLLGnPDASDE------QLQQALE-------NAWVSEFLPLLPqgLDTPIGDQAagLSVGQA 491
|
170 180
....*....|....*....|....*.
gi 657198994 163 RKVALARALACDPDLLLLDEPTNHLD 188
Cdd:PRK11174 492 QRLALARALLQPCQLLLLDEPTASLD 517
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
319-472 |
5.51e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 54.70 E-value: 5.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 319 VFETEGLGLDFGDRTL-FQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSV-----------------RQGT 380
Cdd:PRK13639 1 ILETRDLKYSYPDGTEaLKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVlikgepikydkksllevRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 381 NLevaYFDQYREQLDPEKTVVD------NVGEGKQEvmVRGRSRHILGYLQDFLFEPKrartPVKALSGGEKNRLLLAKL 454
Cdd:PRK13639 81 GI---VFQNPDDQLFAPTVEEDvafgplNLGLSKEE--VEKRVKEALKAVGMEGFENK----PPHHLSGGQKKRVAIAGI 151
|
170
....*....|....*...
gi 657198994 455 FLKPSNLLILDEPTNDLD 472
Cdd:PRK13639 152 LAMKPEIIVLDEPTSGLD 169
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-229 |
6.32e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 54.16 E-value: 6.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 1 MALLTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQQDLKVTRleqDPPASSE 80
Cdd:PRK11701 4 QPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLR---DLYALSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 81 IT-----------VFDYAAEGLAGvgellkqyhHVShalahdpSDANI--RTMSQlqeqldyqnGWQYETRINQV----L 143
Cdd:PRK11701 81 AErrrllrtewgfVHQHPRDGLRM---------QVS-------AGGNIgeRLMAV---------GARHYGDIRATagdwL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 144 TLLDLDPDVTLD---SLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDA----INWLEEFLKDFRGAIVFISHDREFI 216
Cdd:PRK11701 136 ERVEIDAARIDDlptTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVqarlLDLLRGLVRELGLAVVIVTHDLAVA 215
|
250
....*....|...
gi 657198994 217 HKLATRIIDLDRG 229
Cdd:PRK11701 216 RLLAHRLLVMKQG 228
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
321-473 |
6.82e-08 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 53.92 E-value: 6.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMG--QLEASRGSVR-QG---TNLEV---------- 384
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSILlDGediLELSPderaragifl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 385 AYfdQYreqldPE-----------KTVVDNVGEGKQEVM-----VRGRSRhILGYLQDFLfepKRartPVKA-LSGGEKN 447
Cdd:COG0396 82 AF--QY-----PVeipgvsvsnflRTALNARRGEELSAReflklLKEKMK-ELGLDEDFL---DR---YVNEgFSGGEKK 147
|
170 180
....*....|....*....|....*..
gi 657198994 448 RL-LLAKLFLKPSnLLILDEPTNDLDV 473
Cdd:COG0396 148 RNeILQMLLLEPK-LAILDETDSGLDI 173
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
14-233 |
8.02e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 54.04 E-value: 8.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 14 SDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPlddgrlvlqqdlkvtrleqdpPASSEITVfdyaaEGLAG 93
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILK---------------------PTSGSVLI-----RGEPI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 94 VGELLKQYHHVSHALAHDPSDaniRTMSQLQEQ----------LDYQNgwqYETRINQVLTLLDLDP--DVTLDSLSGGW 161
Cdd:PRK13652 69 TKENIREVRKFVGLVFQNPDD---QIFSPTVEQdiafgpinlgLDEET---VAHRVSSALHMLGLEElrDRVPHHLSGGE 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 657198994 162 LRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRG----AIVFISHDREFIHKLATRIIDLDRGVITS 233
Cdd:PRK13652 143 KKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtygmTVIFSTHQLDLVPEMADYIYVMDKGRIVA 218
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-184 |
8.35e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 53.73 E-value: 8.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 1 MALLTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASElplddgrlvlqqdlkvtrleqdPPASSE 80
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGD----------------------PRATSG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 81 ITVFDyaaeglagvGELLKQYHH---VSHALAHDPSDANIRTMSQLQEQLD----YQNGWQYETRINQVltlLDLDPDV- 152
Cdd:PRK11614 61 RIVFD---------GKDITDWQTakiMREAVAIVPEGRRVFSRMTVEENLAmggfFAERDQFQERIKWV---YELFPRLh 128
|
170 180 190
....*....|....*....|....*....|....*..
gi 657198994 153 -----TLDSLSGGWLRKVALARALACDPDLLLLDEPT 184
Cdd:PRK11614 129 erriqRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
14-216 |
8.44e-08 |
|
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: 53.10 E-value: 8.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 14 SDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQQDLKVTRLEQDPPASSEITVfDYAAEglag 93
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSV-AYAAQ---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 94 vgellKQYhhvshaLAHDPSDANIRTMSQLQEQldyqngwqyetRINQVLTLLDLDPDVTL-------------DSLSGG 160
Cdd:cd03290 87 -----KPW------LLNATVEENITFGSPFNKQ-----------RYKAVTDACSLQPDIDLlpfgdqteigergINLSGG 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 657198994 161 WLRKVALARALACDPDLLLLDEPTNHLDIDAINWLE-----EFLKDFRGAIVFISHDREFI 216
Cdd:cd03290 145 QRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMqegilKFLQDDKRTLVLVTHKLQYL 205
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
334-473 |
8.64e-08 |
|
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: 54.09 E-value: 8.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 334 LFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRQGTnlEVAYFDQYREQLdpEKTVVDNVGEGKQEVMV 413
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG--RISFSSQFSWIM--PGTIKENIIFGVSYDEY 127
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 657198994 414 RGRSRHILGYL-QDFLFEPKRARTPVK----ALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:cd03291 128 RYKSVVKACQLeEDITKFPEKDNTVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
334-473 |
9.64e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 55.69 E-value: 9.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 334 LFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRQGTnlEVAYFDQYREQLdpEKTVVDNVGEGKQEVMV 413
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG--RISFSPQTSWIM--PGTIKDNIIFGLSYDEY 516
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 657198994 414 RGRSrhILGYLQ---DFLFEPKRARTPVK----ALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:TIGR01271 517 RYTS--VIKACQleeDIALFPEKDKTVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
14-231 |
1.09e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 53.94 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 14 SDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRL--VLQQDLKVTRLEQDPPASSEITVFDYAAEGL 91
Cdd:PRK13651 18 TELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewIFKDEKNKKKTKEKEKVLEKLVIQKTRFKKI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 92 AGVGELLKQ----YHHVSHALAHDPSDANI----RTMSQLQEQLdyqngwqyETRINQVLTLLDLDPDVTLDS---LSGG 160
Cdd:PRK13651 98 KKIKEIRRRvgvvFQFAEYQLFEQTIEKDIifgpVSMGVSKEEA--------KKRAAKYIELVGLDESYLQRSpfeLSGG 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 657198994 161 WLRKVALARALACDPDLLLLDEPTNHLD----IDAINWLEEFLKDFRgAIVFISHDREFIHKLATRIIDLDRGVI 231
Cdd:PRK13651 170 QKRRVALAGILAMEPDFLVFDEPTAGLDpqgvKEILEIFDNLNKQGK-TIILVTHDLDNVLEWTKRTIFFKDGKI 243
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
319-472 |
1.22e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 53.38 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 319 VFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRQGTnlevAYFD---------- 388
Cdd:PRK14247 3 KIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGE----VYLDgqdifkmdvi 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 389 --QYREQL-------DPEKTVVDNVGEG-------KQEVMVRGRSRHILGYLQDFLFEPKRARTPVKALSGGEKNRLLLA 452
Cdd:PRK14247 79 elRRRVQMvfqipnpIPNLSIFENVALGlklnrlvKSKKELQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIA 158
|
170 180
....*....|....*....|
gi 657198994 453 KLFLKPSNLLILDEPTNDLD 472
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLD 178
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
329-472 |
1.29e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 52.95 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 329 FGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRQG-------TNLEVAYFdqyREQ-------- 393
Cdd:PRK10908 12 LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSghditrlKNREVPFL---RRQigmifqdh 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 394 -LDPEKTVVDNVGegkQEVMVRGRS-----RHILGYLQDFLFEPKRARTPVKaLSGGEKNRLLLAKLFLKPSNLLILDEP 467
Cdd:PRK10908 89 hLLMDRTVYDNVA---IPLIIAGASgddirRRVSAALDKVGLLDKAKNFPIQ-LSGGEQQRVGIARAVVNKPAVLLADEP 164
|
....*
gi 657198994 468 TNDLD 472
Cdd:PRK10908 165 TGNLD 169
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
345-473 |
1.38e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 53.14 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 345 GDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR------------QGTNLEvAYFDQYRE-QLDP----------EKTVV 401
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDdppdwdeildefRGSELQ-NYFTKLLEgDVKVivkpqyvdliPKAVK 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 657198994 402 DNVGegkqEVMVRGRSRHILGYLQDFL-FEPKRARTpVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:cd03236 105 GKVG----ELLKKKDERGKLDELVDQLeLRHVLDRN-IDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
19-231 |
1.62e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 53.20 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 19 LDHAELTIERGERLCLVGRNGAGKSTLM--------------KVIASELPLDDGRLVLQqdlKVTRLEQDPPA---SSei 81
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLlhlngiylpqrgrvKVMGREVNAENEKWVRS---KVGLVFQDPDDqvfSS-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 82 TVFDYAAEGLAGVGellkqyhhvshalaHDPSDANIRTmsqlQEQLDYQNGWQYETRINQvltlldldpdvtldSLSGGW 161
Cdd:PRK13647 96 TVWDDVAFGPVNMG--------------LDKDEVERRV----EEALKAVRMWDFRDKPPY--------------HLSYGQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 657198994 162 LRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDF--RGAIVFIS-HDREFIHKLATRIIDLDRGVI 231
Cdd:PRK13647 144 KKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLhnQGKTVIVAtHDVDLAAEWADQVIVLKEGRV 216
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
319-472 |
1.81e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 52.93 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 319 VFETEGLGLDFGDRT-LFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSV----------RQG-TNLEVA- 385
Cdd:PRK13636 5 ILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIlfdgkpidysRKGlMKLRESv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 386 --YFDQYREQLDPEKTVVD------NVGEGKQEVmvRGRSRHILGYLQdflFEPKRARtPVKALSGGEKNRLLLAKLFLK 457
Cdd:PRK13636 85 gmVFQDPDNQLFSASVYQDvsfgavNLKLPEDEV--RKRVDNALKRTG---IEHLKDK-PTHCLSFGQKKRVAIAGVLVM 158
|
170
....*....|....*
gi 657198994 458 PSNLLILDEPTNDLD 472
Cdd:PRK13636 159 EPKVLVLDEPTAGLD 173
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
136-231 |
2.06e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 53.10 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 136 ETRINQVLTLLDLDPDVTLDS---LSGGWLRKVALARALACDPDLLLLDEPTNHLD----IDAINWLEEFLKDFRGAIVF 208
Cdd:PRK13634 122 KQKAREMIELVGLPEELLARSpfeLSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDpkgrKEMMEMFYKLHKEKGLTTVL 201
|
90 100
....*....|....*....|...
gi 657198994 209 ISHDREFIHKLATRIIDLDRGVI 231
Cdd:PRK13634 202 VTHSMEDAARYADQIVVMHKGTV 224
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
315-472 |
2.07e-07 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 51.88 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 315 SGKLVFETEGLGLDfgDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEAS---RGSVRQGTNLEVAYFDQYR 391
Cdd:cd03233 5 SWRNISFTTGKGRS--KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 392 EQL---------DPEKTV---VDNVGEGKQEVMVRGrsrhilgylqdflfepkrartpvkaLSGGEKNRLLLAKLFLKPS 459
Cdd:cd03233 83 GEIiyvseedvhFPTLTVretLDFALRCKGNEFVRG-------------------------ISGGERKRVSIAEALVSRA 137
|
170
....*....|...
gi 657198994 460 NLLILDEPTNDLD 472
Cdd:cd03233 138 SVLCWDNSTRGLD 150
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
349-501 |
2.13e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 51.84 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 349 ALVGPNGCGKSTLIKLLmgqLEASRGSVRQGTNLEVAYFDQYREQldPEKTVVD---NVGEGKQEVMVRgrSRHIL---- 421
Cdd:cd03240 26 LIVGQNGAGKTTIIEAL---KYALTGELPPNSKGGAHDPKLIREG--EVRAQVKlafENANGKKYTITR--SLAILenvi 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 422 ----GYLQDFLFEPkrartpVKALSGGEKN------RLLLAKLFLKPSNLLILDEPTNDLDVETLELL-----EELLTDY 486
Cdd:cd03240 99 fchqGESNWPLLDM------RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESlaeiiEERKSQK 172
|
170
....*....|....*
gi 657198994 487 PGTLLLVSHDRRFID 501
Cdd:cd03240 173 NFQLIVITHDEELVD 187
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
3-211 |
2.73e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 52.10 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 3 LLTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIA--SELPLDDGRLVLQ-QDLkvtrLEQDPPass 79
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKgKDL----LELSPE--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 80 eitvfDYAAEGLAGVGELLKQYHHVSHALAHDPSDANIRTMSQlQEQLDYqngWQYETRINQVLTLLDLDPDVTLDSL-- 157
Cdd:PRK09580 74 -----DRAGEGIFMAFQYPVEIPGVSNQFFLQTALNAVRSYRG-QEPLDR---FDFQDLMEEKIALLKMPEDLLTRSVnv 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 657198994 158 --SGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEE---FLKDFRGAIVFISH 211
Cdd:PRK09580 145 gfSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADgvnSLRDGKRSFIIVTH 203
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
319-496 |
2.92e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 52.01 E-value: 2.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 319 VFETEGLGLDfGDRTLFQGLDLQVLRGDKIALVGPNGCGKS----TLIKLLMGQLEASRGSVR-QGTNLE--------VA 385
Cdd:PRK10418 4 QIELRNIALQ-AAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLlDGKPVApcalrgrkIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 386 YFDQY-REQLDPEKTVVDNVGEGKQEVMVRGRSRHILGYLQDF-LFEPKRA--RTPVKaLSGGEKNRLLLAKLFLKPSNL 461
Cdd:PRK10418 83 TIMQNpRSAFNPLHTMHTHARETCLALGKPADDATLTAALEAVgLENAARVlkLYPFE-MSGGMLQRMMIALALLCEAPF 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 657198994 462 LILDEPTNDLDVETLELLEELLTDY-----PGtLLLVSHD 496
Cdd:PRK10418 162 IIADEPTTDLDVVAQARILDLLESIvqkraLG-MLLVTHD 200
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
325-472 |
3.05e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 52.35 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 325 LGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLL--MGQLEasrGSVR-QGtnlEVAYFDQ--YREQLDPEK- 398
Cdd:PRK14258 13 LSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrMNELE---SEVRvEG---RVEFFNQniYERRVNLNRl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 399 ----------------TVVDNVGEGKQEVMVRGRSrHILGYLQ------DFLFEPK-RARTPVKALSGGEKNRLLLAK-L 454
Cdd:PRK14258 87 rrqvsmvhpkpnlfpmSVYDNVAYGVKIVGWRPKL-EIDDIVEsalkdaDLWDEIKhKIHKSALDLSGGQQQRLCIARaL 165
|
170
....*....|....*...
gi 657198994 455 FLKPsNLLILDEPTNDLD 472
Cdd:PRK14258 166 AVKP-KVLLMDEPCFGLD 182
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
22-242 |
3.27e-07 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 53.11 E-value: 3.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 22 AELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQ---------------QDLKVTRLEQDPPASSEITVFDY 86
Cdd:PRK10070 47 ASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDgvdiakisdaelrevRRKKIAMVFQSFALMPHMTVLDN 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 87 AAEG--LAGVGellkqyhhvshalAHDPSDANIRTMSQLQEQlDYQNGWQyetrinqvltlldldpdvtlDSLSGGWLRK 164
Cdd:PRK10070 127 TAFGmeLAGIN-------------AEERREKALDALRQVGLE-NYAHSYP--------------------DELSGGMRQR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 165 VALARALACDPDLLLLDEPTNHLD----IDAINWLEEFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITSwPGNYDE 240
Cdd:PRK10070 173 VGLARALAINPDILLMDEAFSALDplirTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQ-VGTPDE 251
|
..
gi 657198994 241 YL 242
Cdd:PRK10070 252 IL 253
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
17-245 |
3.58e-07 |
|
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: 51.46 E-value: 3.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 17 PLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLD------DGRLVLQQDLKVTR-----LEQDPPASSEiTVFD 85
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQkgqiliDGIDIRDISRKSLRsmigvVLQDTFLFSG-TIME 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 86 -------YAAEglAGVGELLKQYHhvshalAHDpsdanirtmsqLQEQLdyQNGwqYETRINQvltlldldpdvTLDSLS 158
Cdd:cd03254 96 nirlgrpNATD--EEVIEAAKEAG------AHD-----------FIMKL--PNG--YDTVLGE-----------NGGNLS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 159 GGWLRKVALARALACDPDLLLLDEPTNHLDIDAinwlEEFLKDfrgAIVFISHDREFI---HKLAT-----RIIDLDRGV 230
Cdd:cd03254 142 QGERQLLAIARAMLRDPKILILDEATSNIDTET----EKLIQE---ALEKLMKGRTSIiiaHRLSTiknadKILVLDDGK 214
|
250
....*....|....*
gi 657198994 231 ITSwPGNYDEYLQGK 245
Cdd:cd03254 215 IIE-EGTHDELLAKK 228
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
157-231 |
3.76e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 52.55 E-value: 3.76e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 657198994 157 LSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFR--GAIVF-ISHDREFIHKLATRIIDLDRGVI 231
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKanNKTVFvITHTMEHVLEVADEVIVMDKGKI 254
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
319-472 |
4.09e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 51.71 E-value: 4.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 319 VFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRQGtnlEVAYFDQ--YREQLDP 396
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEG---KVTFHGKnlYAPDVDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 397 -----------------EKTVVDNVGEGKQevmvrgrsrhILGYLQDF--LFEP--KRA----------RTPVKALSGGE 445
Cdd:PRK14243 87 vevrrrigmvfqkpnpfPKSIYDNIAYGAR----------INGYKGDMdeLVERslRQAalwdevkdklKQSGLSLSGGQ 156
|
170 180
....*....|....*....|....*..
gi 657198994 446 KNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:PRK14243 157 QQRLCIARAIAVQPEVILMDEPCSALD 183
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
10-229 |
4.63e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 51.55 E-value: 4.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 10 SLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMK-----VIASELPLDDGRLVLQQDLKVTRLEQDPPASSeitvf 84
Cdd:PRK09984 11 AKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsglITGDKSAGSHIELLGRTVQREGRLARDIRKSR----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 85 dyaaeglAGVGELLKQYHHVSH----------ALAHDPSdanIRTMSQLQEQLDYQNGWQYETRINQVLTLLDldpdvTL 154
Cdd:PRK09984 86 -------ANTGYIFQQFNLVNRlsvlenvligALGSTPF---WRTCFSWFTREQKQRALQALTRVGMVHFAHQ-----RV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 657198994 155 DSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFR---GAIVFIS-HDREFIHKLATRIIDLDRG 229
Cdd:PRK09984 151 STLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINqndGITVVVTlHQVDYALRYCERIVALRQG 229
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-188 |
4.84e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 51.60 E-value: 4.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 4 LTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIA-----SELPLDDGRLVLQQDLKVTRLE-QDPPA 77
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAgletpSAGELLAGTAPLAEAREDTRLMfQDARL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 78 SSEITVFDYAAEGLAGvgellkqyhhvshalahdpsdanirtmsqlqeqldyqnGWQYETRinQVLTLLDLDPDVT--LD 155
Cdd:PRK11247 93 LPWKKVIDNVGLGLKG--------------------------------------QWRDAAL--QALAAVGLADRANewPA 132
|
170 180 190
....*....|....*....|....*....|...
gi 657198994 156 SLSGGWLRKVALARALACDPDLLLLDEPTNHLD 188
Cdd:PRK11247 133 ALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
319-471 |
5.16e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 52.62 E-value: 5.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 319 VFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMG----------------QLEAS--RGSVRQGT 380
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvyphgtyegeiifegeELQASniRDTERAGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 381 NL---EVAyfdqyreqLDPEKTVVDNVGEGkQEVMVRGRSRHILGYL--QDFLFEPKRA---RTPVKALSGGEKNRLLLA 452
Cdd:PRK13549 85 AIihqELA--------LVKELSVLENIFLG-NEITPGGIMDYDAMYLraQKLLAQLKLDinpATPVGNLGLGQQQLVEIA 155
|
170
....*....|....*....
gi 657198994 453 KLFLKPSNLLILDEPTNDL 471
Cdd:PRK13549 156 KALNKQARLLILDEPTASL 174
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
332-472 |
5.81e-07 |
|
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: 50.95 E-value: 5.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 332 RTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLEVAYFDQYREQLDP--------EKTVVD 402
Cdd:cd03252 15 PVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLvDGHDLALADPAWLRRQVGVvlqenvlfNRSIRD 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 657198994 403 NVGEGKqEVMVRGRSRHI--LGYLQDFLFE-PKRARTPV----KALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:cd03252 95 NIALAD-PGMSMERVIEAakLAGAHDFISElPEGYDTIVgeqgAGLSGGQRQRIAIARALIHNPRILIFDEATSALD 170
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
323-472 |
5.95e-07 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 50.56 E-value: 5.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 323 EGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEA---SRGSVR-QGTNL--------EVAYFDQy 390
Cdd:COG4136 5 ENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLlNGRRLtalpaeqrRIGILFQ- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 391 REQLDPEKTVVDNVGEGKQEVMVRG-RSRHILGYLQDFLFEPKRARTPvKALSGGEKNRL-LLAKLFLKPSNLLiLDEPT 468
Cdd:COG4136 84 DDLLFPHLSVGENLAFALPPTIGRAqRRARVEQALEEAGLAGFADRDP-ATLSGGQRARVaLLRALLAEPRALL-LDEPF 161
|
....
gi 657198994 469 NDLD 472
Cdd:COG4136 162 SKLD 165
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
15-246 |
6.04e-07 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 51.00 E-value: 6.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 15 DFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVI-------ASELPLDdGRLVLQQDLKVTR-----LEQDPpasseiT 82
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLerfydptSGEILLD-GVDIRDLNLRWLRsqiglVSQEP------V 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 83 VFDYA-AEGLA-GvgellkqyhhvshalAHDPSDANIRTMSQLQEQLDYQNGW--QYETRINQVLTlldldpdvtldSLS 158
Cdd:cd03249 88 LFDGTiAENIRyG---------------KPDATDEEVEEAAKKANIHDFIMSLpdGYDTLVGERGS-----------QLS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 159 GGWLRKVALARALACDPDLLLLDEPTNHLDIDA----INWLEEFLKDfRGAIVfISHDREFIHKlATRIIDLDRGVITSw 234
Cdd:cd03249 142 GGQKQRIAIARALLRNPKILLLDEATSALDAESeklvQEALDRAMKG-RTTIV-IAHRLSTIRN-ADLIAVLQNGQVVE- 217
|
250
....*....|..
gi 657198994 235 PGNYDEYLQGKE 246
Cdd:cd03249 218 QGTHDELMAQKG 229
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
321-472 |
6.05e-07 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 52.01 E-value: 6.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNL--------EVAY-FDQY 390
Cdd:PRK10851 4 EIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRfHGTDVsrlhardrKVGFvFQHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 391 reQLDPEKTVVDNVGEG---------------KQEV-----MVRgrsrhiLGYLQDflfepkraRTPVKaLSGGEKNRLL 450
Cdd:PRK10851 84 --ALFRHMTVFDNIAFGltvlprrerpnaaaiKAKVtqlleMVQ------LAHLAD--------RYPAQ-LSGGQKQRVA 146
|
170 180
....*....|....*....|..
gi 657198994 451 LAKLFLKPSNLLILDEPTNDLD 472
Cdd:PRK10851 147 LARALAVEPQILLLDEPFGALD 168
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
28-224 |
6.19e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 49.29 E-value: 6.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 28 RGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLqqdlkvtrleqdppasseitvfdyaaeglagvgellkqyhhvsha 107
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY--------------------------------------------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 108 laHDPSDANIRTMSQLQEQLDYQNGWQYETRINQvltlldldpdvtldslsggwlrKVALARALACDPDLLLLDEPTNHL 187
Cdd:smart00382 36 --IDGEDILEEVLDQLLLIIVGGKKASGSGELRL----------------------RLALALARKLKPDVLILDEITSLL 91
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 657198994 188 DIDA---------INWLEEFLKDFRGAIVFISHDREFIHKLATRII 224
Cdd:smart00382 92 DAEQeallllleeLRLLLLLKSEKNLTVILTTNDEKDLGPALLRRR 137
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-214 |
6.33e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.32 E-value: 6.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 2 ALLTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPlddgrlvlqQDLkvtrleqdppaSSEI 81
Cdd:PRK10938 259 PRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHP---------QGY-----------SNDL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 82 TVFDYAaeglAGVGELL----KQYHHVSHALAHD----PSDANI------------RTMSQLQEQLdyqngwqyetrINQ 141
Cdd:PRK10938 319 TLFGRR----RGSGETIwdikKHIGYVSSSLHLDyrvsTSVRNVilsgffdsigiyQAVSDRQQKL-----------AQQ 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 142 VLTLLDLD---PDVTLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLdiDAIN------WLEEFLKDFRGAIVFISHD 212
Cdd:PRK10938 384 WLDILGIDkrtADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGL--DPLNrqlvrrFVDVLISEGETQLLFVSHH 461
|
..
gi 657198994 213 RE 214
Cdd:PRK10938 462 AE 463
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
23-219 |
6.59e-07 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 51.93 E-value: 6.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 23 ELTIERGERL-CLVGRNGAGKSTLMKVIASELPLDDGRLVLQQDLKVTRLEQDPPASSEITvFDYAAEGLAGVGELLKQY 101
Cdd:COG3593 16 DLSIELSDDLtVLVGENNSGKSSILEALRLLLGPSSSRKFDEEDFYLGDDPDLPEIEIELT-FGSLLSRLLRLLLKEEDK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 102 HHVSHALAHDPSDAN--IRTMSQLQEQLDYQNGWQYETRI-------NQVLTLLDL----DPDVTLDSLSGG--WLRKVA 166
Cdd:COG3593 95 EELEEALEELNEELKeaLKALNELLSEYLKELLDGLDLELelsldelEDLLKSLSLriedGKELPLDRLGSGfqRLILLA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 657198994 167 LARALA-----CDPDLLLLDEPTNHLDIDAINWLEEFLKDF--RGAIVFIS-HDREFIHKL 219
Cdd:COG3593 175 LLSALAelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELseKPNQVIITtHSPHLLSEV 235
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
14-231 |
6.63e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 51.34 E-value: 6.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 14 SDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIaselpldDGrLVLQQDLKVTRLEQDPPASSEITVFDYAAEglag 93
Cdd:PRK13640 18 SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLI-------NG-LLLPDDNPNSKITVDGITLTAKTVWDIREK---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 94 VGELLK----QYhhVSHALAHD----------PSDANIRTMSQLQEQ---LDYQngwqyetrinqvltllDLDPDvtldS 156
Cdd:PRK13640 86 VGIVFQnpdnQF--VGATVGDDvafglenravPRPEMIKIVRDVLADvgmLDYI----------------DSEPA----N 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 657198994 157 LSGGWLRKVALARALACDPDLLLLDEPTNHLDIDA----INWLEEFLKDFRGAIVFISHDREFIhKLATRIIDLDRGVI 231
Cdd:PRK13640 144 LSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGkeqiLKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKL 221
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
26-188 |
6.67e-07 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 52.36 E-value: 6.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 26 IERGERLCLVGRNGAGKSTLMKVIASELPLDdgrLVLQQDLKVTRLEQDPPASSEITVFDYAAEGLagVGELLKQYHHVS 105
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALAFRSPKG---VKGSGSVLLNGMPIDAKEMRAISAYVQQDDLF--IPTLTVREHLMF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 106 HALAHDPsdaniRTMSQLQEQLdyqngwqyetRINQVLTLLDL---------DPDvTLDSLSGGWLRKVALARALACDPD 176
Cdd:TIGR00955 123 QAHLRMP-----RRVTKKEKRE----------RVDEVLQALGLrkcantrigVPG-RVKGLSGGERKRLAFASELLTDPP 186
|
170
....*....|..
gi 657198994 177 LLLLDEPTNHLD 188
Cdd:TIGR00955 187 LLFCDEPTSGLD 198
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
10-233 |
6.95e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 51.14 E-value: 6.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 10 SLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQQDL-------KVTR----LEQDPPAS 78
Cdd:PRK10253 14 TLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHiqhyaskEVARriglLAQNATTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 79 SEITVFDYAAEGlagvgellkQYhhvshalAHDPSDANIRtmsqlQEQLDYQNGWQYETRINQVltlldldPDVTLDSLS 158
Cdd:PRK10253 94 GDITVQELVARG---------RY-------PHQPLFTRWR-----KEDEEAVTKAMQATGITHL-------ADQSVDTLS 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 657198994 159 GGWLRKVALARALACDPDLLLLDEPTNHLD----IDAINWLEEFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITS 233
Cdd:PRK10253 146 GGQRQRAWIAMVLAQETAIMLLDEPTTWLDishqIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVA 224
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
349-472 |
6.98e-07 |
|
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: 51.65 E-value: 6.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 349 ALVGPNGCGKSTLIKLLMGQLEASRG----------SVRQGTNL-----EVAY-FDQYReqLDPEKTVVDNVGEGKQEVM 412
Cdd:TIGR02142 27 AIFGRSGSGKTTLIRLIAGLTRPDEGeivlngrtlfDSRKGIFLppekrRIGYvFQEAR--LFPHLSVRGNLRYGMKRAR 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 413 VRGRSRHILGYLQDFLFEPKRARTPVKaLSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:TIGR02142 105 PSERRISFERVIELLGIGHLLGRLPGR-LSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
321-376 |
7.91e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 50.92 E-value: 7.91e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 657198994 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSV 376
Cdd:PRK11831 9 DMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEI 64
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
17-229 |
8.47e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 52.71 E-value: 8.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 17 PLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQQDLKVTRLEQDPPASSEITVFDYAAEGLAGvge 96
Cdd:TIGR01257 1953 PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTG--- 2029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 97 llKQYHHVSHALAHDPSdanirtmsqlqEQLDYQNGWQYETrinqvlTLLDLDPDVTLDSLSGGWLRKVALARALACDPD 176
Cdd:TIGR01257 2030 --REHLYLYARLRGVPA-----------EEIEKVANWSIQS------LGLSLYADRLAGTYSGGNKRKLSTAIALIGCPP 2090
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 657198994 177 LLLLDEPTNHLDIDA----INWLEEFLKDFRgAIVFISHDREFIHKLATRIIDLDRG 229
Cdd:TIGR01257 2091 LVLLDEPTTGMDPQArrmlWNTIVSIIREGR-AVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-188 |
9.33e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 51.38 E-value: 9.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 1 MALLTLHGASLSFS-DFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIAS-------ELPLDDGRlvlqqdlkVTRLE 72
Cdd:PRK11650 1 MAGLKLQAVRKSYDgKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGleritsgEIWIGGRV--------VNELE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 73 qdpPASSEIT-VF-DYAAeglagvgellkqYHHVS------HALahdpsdaNIRTMSQLQeqldyqngwqYETRINQVLT 144
Cdd:PRK11650 73 ---PADRDIAmVFqNYAL------------YPHMSvrenmaYGL-------KIRGMPKAE----------IEERVAEAAR 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 657198994 145 LLDLDPdvTLD----SLSGGWLRKVALARALACDPDLLLLDEPTNHLD 188
Cdd:PRK11650 121 ILELEP--LLDrkprELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
17-228 |
1.31e-06 |
|
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: 49.80 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 17 PLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVL-QQDLKVTRLE----------QDPpasseiTVFD 85
Cdd:cd03244 18 PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIdGVDISKIGLHdlrsrisiipQDP------VLFS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 86 yaaeglagvGEL------LKQYhhvshalahdpSDAnirtmsQLQEQLDYQNGWQYetrINQVLTLLDLDPDVTLDSLSG 159
Cdd:cd03244 92 ---------GTIrsnldpFGEY-----------SDE------ELWQALERVGLKEF---VESLPGGLDTVVEEGGENLSV 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 657198994 160 GWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKD-FRGAIVF-IShdrefiHKLATrIIDLDR 228
Cdd:cd03244 143 GQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREaFKDCTVLtIA------HRLDT-IIDSDR 206
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
337-473 |
1.43e-06 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 49.33 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 337 GLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLEVAYFDQYREQL-----DPE------KTVVDNV 404
Cdd:cd03369 26 NVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEiDGIDISTIPLEDLRSSLtiipqDPTlfsgtiRSNLDPF 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 657198994 405 GEgkqevmvrgrsrhilgYLQDFLFEPKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:cd03369 106 DE----------------YSDEEIYGALRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDY 158
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
156-211 |
1.66e-06 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 50.04 E-value: 1.66e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 657198994 156 SLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRG--AIVFISH 211
Cdd:COG1117 154 GLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKdyTIVIVTH 211
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
336-472 |
1.70e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 50.61 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 336 QGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGqLEA-SRGSVRQG----TNLEVA------YFDQYreQLDPEKTVVDNV 404
Cdd:PRK11650 21 KGIDLDVADGEFIVLVGPSGCGKSTLLRMVAG-LERiTSGEIWIGgrvvNELEPAdrdiamVFQNY--ALYPHMSVRENM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 405 GEG-------KQEVMVR-GRSRHILGyLQDFLfepkrARTPvKALSGGEKNRLLLA-------KLFLkpsnlliLDEPTN 469
Cdd:PRK11650 98 AYGlkirgmpKAEIEERvAEAARILE-LEPLL-----DRKP-RELSGGQRQRVAMGraivrepAVFL-------FDEPLS 163
|
...
gi 657198994 470 DLD 472
Cdd:PRK11650 164 NLD 166
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
339-472 |
1.74e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 50.01 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 339 DLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRQG-----TNL-----------EVAYFDQYRE-QLDPEKTVV 401
Cdd:PRK13645 31 SLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGdyaipANLkkikevkrlrkEIGLVFQFPEyQLFQETIEK 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 657198994 402 D------NVGEGKQEVMVRgrsrhiLGYLQDFLFEPKR--ARTPVKaLSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:PRK13645 111 DiafgpvNLGENKQEAYKK------VPELLKLVQLPEDyvKRSPFE-LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-223 |
1.86e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.94 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 19 LDHAELTIERGERLCLVGRNGAGKSTLMKVIASELP--------LDDGRLVLQQDLKvtrleqdppaSSEitvfdyaAEG 90
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPhgsyegeiLFDGEVCRFKDIR----------DSE-------ALG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 91 -------LAGVGELlkqyhhvSHA----LAHDPSDANI----RTMSQLQEQLDyqngwqyetRINqvltlLDLDPDVTLD 155
Cdd:NF040905 80 iviihqeLALIPYL-------SIAenifLGNERAKRGVidwnETNRRARELLA---------KVG-----LDESPDTLVT 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 657198994 156 SLSGGWLRKVALARALACDPDLLLLDEPTNHL-DIDAINWLeEFLKDFRG---AIVFISHDREFIHKLATRI 223
Cdd:NF040905 139 DIGVGKQQLVEIAKALSKDVKLLILDEPTAALnEEDSAALL-DLLLELKAqgiTSIIISHKLNEIRRVADSI 209
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-232 |
1.95e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 50.68 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 22 AELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLqqDLKVTRLEQDPPASSEITVF---DYAAEGLAGVgell 98
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYL--DGKPIDIRSPRDAIRAGIMLcpeDRKAEGIIPV---- 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 99 kqyHHVSHALahdpsdaNI---RTMSQLQEQLDyqNGWQYET--RINQVLTLLDLDPDVTLDSLSGGWLRKVALARALAC 173
Cdd:PRK11288 346 ---HSVADNI-------NIsarRHHLRAGCLIN--NRWEAENadRFIRSLNIKTPSREQLIMNLSGGNQQKAILGRWLSE 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 657198994 174 DPDLLLLDEPTNHLDIDAINWLEEFLKDF--RG-AIVFISHDREFIHKLATRIIDLDRGVIT 232
Cdd:PRK11288 414 DMKVILLDEPTRGIDVGAKHEIYNVIYELaaQGvAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
338-472 |
2.02e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.13 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 338 LDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGS--VRQGTnleVAYFDQYREQLDpeKTVVDNVGEG-KQEVMVR 414
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSsvVIRGS---VAYVPQVSWIFN--ATVRENILFGsDFESERY 710
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 657198994 415 GRSRHILGYLQDFLFEPKRARTPVKA----LSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:PLN03232 711 WRAIDVTALQHDLDLLPGRDLTEIGErgvnISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
8-229 |
2.04e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.50 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 8 GASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQQ---DLK---------VTRLEQDP 75
Cdd:PRK10982 3 NISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkeiDFKsskealengISMVHQEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 76 PASSEITVFD------YAAEGLagvgellkqyhHVSHALAHDPSDAnirtmsqLQEQLDyqngwqyetrinqvltlLDLD 149
Cdd:PRK10982 83 NLVLQRSVMDnmwlgrYPTKGM-----------FVDQDKMYRDTKA-------IFDELD-----------------IDID 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 150 PDVTLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEF---LKDFRGAIVFISHDREFIHKLATRIIDL 226
Cdd:PRK10982 128 PRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIirkLKERGCGIVYISHKMEEIFQLCDEITIL 207
|
...
gi 657198994 227 DRG 229
Cdd:PRK10982 208 RDG 210
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
319-472 |
2.06e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 49.71 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 319 VFETEGLGLDF---GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLEVAYFDQYREQL 394
Cdd:PRK13642 4 ILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKiDGELLTAENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 395 -----DPEK-----TVVDNVGEGKQ------EVMVRGRSRHILGY-LQDFlfepkRARTPVKaLSGGEKNRLLLAKLFLK 457
Cdd:PRK13642 84 gmvfqNPDNqfvgaTVEDDVAFGMEnqgiprEEMIKRVDEALLAVnMLDF-----KTREPAR-LSGGQKQRVAVAGIIAL 157
|
170
....*....|....*
gi 657198994 458 PSNLLILDEPTNDLD 472
Cdd:PRK13642 158 RPEIIILDESTSMLD 172
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
136-222 |
2.41e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 49.71 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 136 ETRINQVlTLLDLDPDVTLDS---LSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDF--RGAIVFIS 210
Cdd:PRK14271 141 QARLTEV-GLWDAVKDRLSDSpfrLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLadRLTVIIVT 219
|
90
....*....|..
gi 657198994 211 HDREFIHKLATR 222
Cdd:PRK14271 220 HNLAQAARISDR 231
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
156-243 |
2.43e-06 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 50.73 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 156 SLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAinwlEEFLKDfrgAIVFISHDR-EFI--HKLAT-----RIIDLD 227
Cdd:PRK13657 471 QLSGGERQRLAIARALLKDPPILILDEATSALDVET----EAKVKA---ALDELMKGRtTFIiaHRLSTvrnadRILVFD 543
|
90
....*....|....*..
gi 657198994 228 RG-VITSwpGNYDEYLQ 243
Cdd:PRK13657 544 NGrVVES--GSFDELVA 558
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
12-229 |
2.45e-06 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 50.88 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 12 SFS-----DFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVI-------ASELPLDDGRLV------LQQdlKVTRLEQ 73
Cdd:TIGR00958 485 SFSypnrpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLqnlyqptGGQVLLDGVPLVqydhhyLHR--QVALVGQ 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 74 DPPASSEiTVFDYAAEGLAgvgellkqyhhvshalahDPSDANIRTMSQLQEQLDYQNGWQ--YETRINQVLTLLdldpd 151
Cdd:TIGR00958 563 EPVLFSG-SVRENIAYGLT------------------DTPDEEIMAAAKAANAHDFIMEFPngYDTEVGEKGSQL----- 618
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 657198994 152 vtldslSGGWLRKVALARALACDPDLLLLDEPTNHLDIdAINWLEEFLKDFRG-AIVFISHDREFIHKlATRIIDLDRG 229
Cdd:TIGR00958 619 ------SGGQKQRIAIARALVRKPRVLILDEATSALDA-ECEQLLQESRSRASrTVLLIAHRLSTVER-ADQILVLKKG 689
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
344-472 |
2.65e-06 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 49.04 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 344 RGDKIALVGPNGCGKSTLIKLLMGQLEASRGSV-RQGTNL--------------EVAYFDQYREQLdPEKTVVDNVGE-- 406
Cdd:PRK11629 34 EGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDViFNGQPMsklssaakaelrnqKLGFIYQFHHLL-PDFTALENVAMpl 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 657198994 407 ---GKQEVMVRGRSRHILGYLQdflfEPKRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:PRK11629 113 ligKKKPAEINSRALEMLAAVG----LEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-236 |
3.40e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 49.24 E-value: 3.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 3 LLTLHGASLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQQDlkvtrleqdppasseit 82
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGK----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 83 VFDYAAEGLAGVGELLKQ-YHHVSHALAHDPSDANI----RTMSQLQEQLdyqngwqyETRINQVLTLLDLD--PDVTLD 155
Cdd:PRK13638 64 PLDYSKRGLLALRQQVATvFQDPEQQIFYTDIDSDIafslRNLGVPEAEI--------TRRVDEALTLVDAQhfRHQPIQ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 156 SLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRGA---IVFISHDREFIHKLATRIIDLDRGVIT 232
Cdd:PRK13638 136 CLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQgnhVIISSHDIDLIYEISDAVYVLRQGQIL 215
|
....*.
gi 657198994 233 SW--PG 236
Cdd:PRK13638 216 THgaPG 221
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-223 |
3.61e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 49.42 E-value: 3.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 1 MALLTLHGASLSF--SDFPL--LDHAELTIERGERLCLVGRNGAGKSTLMKVIASeLPLDDGRLVLQQ----DLKVTRLE 72
Cdd:PRK15093 1 MPLLDIRNLTIEFktSDGWVkaVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG-VTKDNWRVTADRmrfdDIDLLRLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 73 qdPPASSEItvfdyaaeglagVGellkqyHHVSHALAH-----DPSDANIRTMSQLQEQLDYQNGW--QYETRINQVLTL 145
Cdd:PRK15093 80 --PRERRKL------------VG------HNVSMIFQEpqsclDPSERVGRQLMQNIPGWTYKGRWwqRFGWRKRRAIEL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 146 LDL----DPDVTLDS----LSGGWLRKVALARALACDPDLLLLDEPTNHLD----IDAINWLEEFLKDFRGAIVFISHDR 213
Cdd:PRK15093 140 LHRvgikDHKDAMRSfpyeLTEGECQKVMIAIALANQPRLLIADEPTNAMEpttqAQIFRLLTRLNQNNNTTILLISHDL 219
|
250
....*....|
gi 657198994 214 EFIHKLATRI 223
Cdd:PRK15093 220 QMLSQWADKI 229
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
11-253 |
3.97e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.41 E-value: 3.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 11 LSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQQDLKVTRL--EQDPPASSEITV----- 83
Cdd:PTZ00265 1176 ISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIVFKNEHTNDMtnEQDYQGDEEQNVgmknv 1255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 84 --FDYAAEGlaGVGELLKQYHHVSHALAH--DPSDANIRTMSQL-----QEQL-----DYQN---GWQYETR-------- 138
Cdd:PTZ00265 1256 neFSLTKEG--GSGEDSTVFKNSGKILLDgvDICDYNLKDLRNLfsivsQEPMlfnmsIYENikfGKEDATRedvkrack 1333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 139 ---INQVLTLLDLDPDVTL----DSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRGaivfiSH 211
Cdd:PTZ00265 1334 faaIDEFIESLPNKYDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKD-----KA 1408
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 657198994 212 DREFI---HKLATrIIDLDRGVITSWPGNYDEYLQGK---EEWLRVEE 253
Cdd:PTZ00265 1409 DKTIItiaHRIAS-IKRSDKIVVFNNPDRTGSFVQAHgthEELLSVQD 1455
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
321-472 |
4.65e-06 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 48.54 E-value: 4.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLEVAYFDQYREQL----- 394
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLvDGLDVATTPSRELAKRLailrq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 395 ----DPEKTVVDNVGEGkqevmvR-----GR-----SRHI--------LGYLQD-FLFEpkrartpvkaLSGGEKNRLLL 451
Cdd:COG4604 83 enhiNSRLTVRELVAFG------RfpyskGRltaedREIIdeaiayldLEDLADrYLDE----------LSGGQRQRAFI 146
|
170 180
....*....|....*....|.
gi 657198994 452 AKLFLKPSNLLILDEPTNDLD 472
Cdd:COG4604 147 AMVLAQDTDYVLLDEPLNNLD 167
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
19-223 |
6.40e-06 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 48.75 E-value: 6.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 19 LDHAELTIERGERLCLVGRNGAGKSTLMKVIASelplddgrlVLQQDLKVT--RLEqdppasseitvfdyaaegLAGVgE 96
Cdd:COG4170 23 VDRVSLTLNEGEIRGLVGESGSGKSLIAKAICG---------ITKDNWHVTadRFR------------------WNGI-D 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 97 LLK-----QYHHVSHALA---HDPS---DANIRTMSQLQEQLDyqnGWQYE--------TRINQVLTLLDL----DPDVT 153
Cdd:COG4170 75 LLKlspreRRKIIGREIAmifQEPSsclDPSAKIGDQLIEAIP---SWTFKgkwwqrfkWRKKRAIELLHRvgikDHKDI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 657198994 154 LDS----LSGGWLRKVALARALACDPDLLLLDEPTNHLDI---DAINWLEEFLKDFRG-AIVFISHDREFIHKLATRI 223
Cdd:COG4170 152 MNSypheLTEGECQKVMIAMAIANQPRLLIADEPTNAMESttqAQIFRLLARLNQLQGtSILLISHDLESISQWADTI 229
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
331-472 |
6.74e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 49.33 E-value: 6.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 331 DRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLEVAYFDQYREQL-----DP---EKTVV 401
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRfHDIPLTKLQLDSWRSRLavvsqTPflfSDTVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 402 DNVGEGKQ-------EVMVRGRSRHilgylQDFLFEPKRARTPVKA----LSGGEKNRLLLAKLFLKPSNLLILDEPTND 470
Cdd:PRK10789 407 NNIALGRPdatqqeiEHVARLASVH-----DDILRLPQGYDTEVGErgvmLSGGQKQRISIARALLLNAEILILDDALSA 481
|
..
gi 657198994 471 LD 472
Cdd:PRK10789 482 VD 483
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
13-278 |
6.84e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 48.19 E-value: 6.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 13 FSDFPLLDhAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRlVLQQDLKVT---RLEQDPPASSEITVFDYAAE 89
Cdd:PRK13643 17 FASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGK-VTVGDIVVSstsKQKEIKPVRKKVGVVFQFPE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 90 GLAGVGELLKQyhhvshaLAHDPSDANIRTMsqlqeqldyqngwQYETRINQVLTLLDLDPDVTLDS---LSGGWLRKVA 166
Cdd:PRK13643 95 SQLFEETVLKD-------VAFGPQNFGIPKE-------------KAEKIAAEKLEMVGLADEFWEKSpfeLSGGQMRRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 167 LARALACDPDLLLLDEPTNHLDIDA---INWLEEFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITSWpGNYDEYLQ 243
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKArieMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISC-GTPSDVFQ 233
|
250 260 270
....*....|....*....|....*....|....*...
gi 657198994 244 gKEEWLRVEEL---KNAEFDRKLAQEEVWVRQGIKARR 278
Cdd:PRK13643 234 -EVDFLKAHELgvpKATHFADQLQKTGAVTFEKLPITR 270
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
24-237 |
7.99e-06 |
|
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: 49.03 E-value: 7.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 24 LTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQQDLkVTrlEQDPPASSEI--TVF-DYaaeglagvgellkq 100
Cdd:COG4615 353 LTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQP-VT--ADNREAYRQLfsAVFsDF-------------- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 101 yhHVSHALAHDPSDANirtmsqlqeqldyqngwqyETRINQVLTLLDLDPDVTLD-------SLSGGWLRKVALARALAC 173
Cdd:COG4615 416 --HLFDRLLGLDGEAD-------------------PARARELLERLELDHKVSVEdgrfsttDLSQGQRKRLALLVALLE 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 657198994 174 DPDLLLLDEptnhldidainW------------LEEFLKDFR--G-AIVFISHDREFIHkLATRIIDLDRGVITSWPGN 237
Cdd:COG4615 475 DRPILVFDE-----------WaadqdpefrrvfYTELLPELKarGkTVIAISHDDRYFD-LADRVLKMDYGKLVELTGP 541
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
302-472 |
8.12e-06 |
|
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: 48.02 E-value: 8.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 302 QGKAKLQLDEAGRSGKLVFETEGLGLDFGDrtlfqgLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGT 380
Cdd:cd03294 13 NPQKAFKLLAKGKSKEEILKKTGQTVGVND------VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLiDGQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 381 NLEVAYFDQYRE-------------QLDPEKTVVDNV-------GEGKQEvmvrgRSRHILGYLQDFLFEPKRARTPvKA 440
Cdd:cd03294 87 DIAAMSRKELRElrrkkismvfqsfALLPHRTVLENVafglevqGVPRAE-----REERAAEALELVGLEGWEHKYP-DE 160
|
170 180 190
....*....|....*....|....*....|...
gi 657198994 441 LSGGEKNRLLLAK-LFLKPSnLLILDEPTNDLD 472
Cdd:cd03294 161 LSGGMQQRVGLARaLAVDPD-ILLMDEAFSALD 192
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
19-203 |
8.17e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 47.96 E-value: 8.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 19 LDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRL-VLQQDLKvTRLEQD----PPASSEItvfDYAAEGLAG 93
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKIsILGQPTR-QALQKNlvayVPQSEEV---DWSFPVLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 94 VGELLKQYHHVshALAHDPSDANIRTMSQLQEQLDYQngwqyETRINQVltlldldpdvtlDSLSGGWLRKVALARALAC 173
Cdd:PRK15056 99 DVVMMGRYGHM--GWLRRAKKRDRQIVTAALARVDMV-----EFRHRQI------------GELSGGQKKRVFLARAIAQ 159
|
170 180 190
....*....|....*....|....*....|
gi 657198994 174 DPDLLLLDEPTNHLDIDAINWLEEFLKDFR 203
Cdd:PRK15056 160 QGQVILLDEPFTGVDVKTEARIISLLRELR 189
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
138-226 |
9.35e-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: 46.55 E-value: 9.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 138 RINQVLTLLD-----LDPDVTLDSLSGGWLRKVALARALACDPD--LLLLDEPTNHLDIDAINWLEEFLKDFRG---AIV 207
Cdd:cd03238 64 FIDQLQFLIDvglgyLTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDlgnTVI 143
|
90
....*....|....*....
gi 657198994 208 FISHDREFIhKLATRIIDL 226
Cdd:cd03238 144 LIEHNLDVL-SSADWIIDF 161
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
319-472 |
9.51e-06 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 47.70 E-value: 9.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 319 VFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASR--------------------GSVRQ 378
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellgrtvqregrlaRDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 379 GTNLEVAYFDQYreQLDPEKTVVDNVGEG-------------------KQEVMvRGRSRHILGYLqdflfepkrARTPVK 439
Cdd:PRK09984 84 SRANTGYIFQQF--NLVNRLSVLENVLIGalgstpfwrtcfswftreqKQRAL-QALTRVGMVHF---------AHQRVS 151
|
170 180 190
....*....|....*....|....*....|...
gi 657198994 440 ALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:PRK09984 152 TLSGGQQQRVAIARALMQQAKVILADEPIASLD 184
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
156-211 |
1.00e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 47.53 E-value: 1.00e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 657198994 156 SLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRG--AIVFISH 211
Cdd:PRK14267 149 NLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKeyTIVLVTH 206
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
15-188 |
1.23e-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: 46.84 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 15 DFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGR-LVLQQDLKVTRLE----------QDPPASSEiTV 83
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSiLIDGQDIREVTLDslrraigvvpQDTVLFND-TI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 84 FDYAAEGLAGVGELlKQYHHVSHALAHDpsdaNIRTMSQlqeqldyqngwQYETRINQVLTlldldpdvtldSLSGGWLR 163
Cdd:cd03253 92 GYNIRYGRPDATDE-EVIEAAKAAQIHD----KIMRFPD-----------GYDTIVGERGL-----------KLSGGEKQ 144
|
170 180
....*....|....*....|....*
gi 657198994 164 KVALARALACDPDLLLLDEPTNHLD 188
Cdd:cd03253 145 RVAIARAILKNPPILLLDEATSALD 169
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
337-473 |
1.28e-05 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 46.72 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 337 GLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLEVAYFDQYREQL-----DP---EKTVVDNV--- 404
Cdd:cd03244 22 NISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILiDGVDISKIGLHDLRSRIsiipqDPvlfSGTIRSNLdpf 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 657198994 405 GEGKQEVMVRGRSR-HILGYLQDFlfePKRARTPVKA----LSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:cd03244 102 GEYSDEELWQALERvGLKEFVESL---PGGLDTVVEEggenLSVGQRQLLCLARALLRKSKILVLDEATASVDP 172
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
341-472 |
1.32e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 47.42 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 341 QVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLEVAYFDQYREQL-----DPEK-----TVVDNVG---- 405
Cdd:PRK13650 29 HVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIiDGDLLTEENVWDIRHKIgmvfqNPDNqfvgaTVEDDVAfgle 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 406 -EGKQEVMVRGRSRHILGY--LQDFlfepkRARTPVKaLSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:PRK13650 109 nKGIPHEEMKERVNEALELvgMQDF-----KEREPAR-LSGGQKQRVAIAGAVAMRPKIIILDEATSMLD 172
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
321-550 |
1.46e-05 |
|
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: 47.87 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMG--QLEASRGSV-----------------RQGT- 380
Cdd:TIGR03269 2 EVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIiyhvalcekcgyverpsKVGEp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 381 ----------------NLEVAYFDQYREQ----------LDPEKTVVDNVGEGKQEVMVRGRSRhiLGYLQDFLFEPK-- 432
Cdd:TIGR03269 82 cpvcggtlepeevdfwNLSDKLRRRIRKRiaimlqrtfaLYGDDTVLDNVLEALEEIGYEGKEA--VGRAVDLIEMVQls 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 433 -RARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETL----ELLEELLTDYPGTLLLVSHDRRFIDNTVTGC 507
Cdd:TIGR03269 160 hRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAklvhNALEEAVKASGISMVLTSHWPEVIEDLSDKA 239
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 657198994 508 WLFEgDGRISDYvgGYADMMATRALQAAQQTAKPAPVKVAEPV 550
Cdd:TIGR03269 240 IWLE-NGEIKEE--GTPDEVVAVFMEGVSEVEKECEVEVGEPI 279
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
338-393 |
1.53e-05 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 47.87 E-value: 1.53e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 657198994 338 LDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLEVAYFDQYREQ 393
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILlDGQPVTADNREAYRQL 407
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
337-516 |
1.70e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 47.00 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 337 GLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-----QGTNLEVAYFDQYREQLDPEKTVVDNVGEGKQev 411
Cdd:PRK13651 25 NVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifkdEKNKKKTKEKEKVLEKLVIQKTRFKKIKKIKE-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 412 mVRGRSRHILGY----------LQDFLFEP-----------KRARTPVK--------------ALSGGEKNRLLLAKLFL 456
Cdd:PRK13651 103 -IRRRVGVVFQFaeyqlfeqtiEKDIIFGPvsmgvskeeakKRAAKYIElvgldesylqrspfELSGGQKRRVALAGILA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 657198994 457 KPSNLLILDEPTNDLD---VETLELLEELLTDYPGTLLLVSHDrrfIDNTV--TGCWLFEGDGRI 516
Cdd:PRK13651 182 MEPDFLVFDEPTAGLDpqgVKEILEIFDNLNKQGKTIILVTHD---LDNVLewTKRTIFFKDGKI 243
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
307-472 |
1.86e-05 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 47.71 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 307 LQLDEAGRSGKLVFETEGLGLDFGDRTL-FQGLDLQVLR--------GDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR 377
Cdd:PRK11176 322 LDLEQEKDEGKRVIERAKGDIEFRNVTFtYPGKEVPALRninfkipaGKTVALVGRSGSGKSTIANLLTRFYDIDEGEIL 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 378 -QGTNLEVAYFDQYREQL-----------DpekTVVDNVGEGKQEVMVRGRSRHI--LGYLQDFLFEPKRARTPV----- 438
Cdd:PRK11176 402 lDGHDLRDYTLASLRNQValvsqnvhlfnD---TIANNIAYARTEQYSREQIEEAarMAYAMDFINKMDNGLDTVigeng 478
|
170 180 190
....*....|....*....|....*....|....
gi 657198994 439 KALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:PRK11176 479 VLLSGGQRQRIAIARALLRDSPILILDEATSALD 512
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
17-241 |
1.86e-05 |
|
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: 46.25 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 17 PLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQ-QDLKVTRLEQdppASSEITVfdyaaeglagvg 95
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDgIDISTIPLED---LRSSLTI------------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 96 ellkqyhhvshaLAHDPS--DANIRTmsqlqeQLDYQNgwQYETRinQVLTLLDLDPDVtlDSLSGGWLRKVALARALAC 173
Cdd:cd03369 87 ------------IPQDPTlfSGTIRS------NLDPFD--EYSDE--EIYGALRVSEGG--LNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 657198994 174 DPDLLLLDEPTNHLDIDAINWLEEFL-KDFRGAIVFIshdreFIHKLATrIIDLDRGVITSwPGNYDEY 241
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIrEEFTNSTILT-----IAHRLRT-IIDYDKILVMD-AGEVKEY 204
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
319-472 |
1.97e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 46.69 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 319 VFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLL--MGQLEAS---RGSVR-QGTNLEVAYFD--QY 390
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVyNGHNIYSPRTDtvDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 391 R-------EQLDP-EKTVVDNV-------GEGKQEVM-------VRGRSrhILGYLQDFLFEPkrartpVKALSGGEKNR 448
Cdd:PRK14239 85 RkeigmvfQQPNPfPMSIYENVvyglrlkGIKDKQVLdeaveksLKGAS--IWDEVKDRLHDS------ALGLSGGQQQR 156
|
170 180
....*....|....*....|....
gi 657198994 449 LLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALD 180
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
10-188 |
1.97e-05 |
|
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: 45.62 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 10 SLSFSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIAselplddGRLVLQQ---DLKVTRLEQDPPASSEITVFdy 86
Cdd:cd03213 16 SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALA-------GRRTGLGvsgEVLINGRPLDKRSFRKIIGY-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 87 aaeglagVGEllKQYHHvshalahdpsdanirtmSQL--QEQLDYQngwqyetrinqvltlldldpdVTLDSLSGGWLRK 164
Cdd:cd03213 87 -------VPQ--DDILH-----------------PTLtvRETLMFA---------------------AKLRGLSGGERKR 119
|
170 180
....*....|....*....|....
gi 657198994 165 VALARALACDPDLLLLDEPTNHLD 188
Cdd:cd03213 120 VSIALELVSNPSLLFLDEPTSGLD 143
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
154-216 |
2.06e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 46.06 E-value: 2.06e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 657198994 154 LDSLSGGW-------LRkVALARALACDPDLLLLDEPTNHLDIDAINW-LEEFLKDFRGAIVF----ISHDREFI 216
Cdd:cd03240 113 RGRCSGGEkvlasliIR-LALAETFGSNCGILALDEPTTNLDEENIEEsLAEIIEERKSQKNFqlivITHDEELV 186
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
338-472 |
2.08e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 46.52 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 338 LDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLEVAYFDQYREQL-----DPEK-----TVVDNVGE 406
Cdd:PRK13632 28 VSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKiDGITISKENLKEIRKKIgiifqNPDNqfigaTVEDDIAF 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 657198994 407 GKQEVMV-RGRSRHILGYL------QDFL-FEPKRartpvkaLSGGEKNRLLLAK-LFLKPSnLLILDEPTNDLD 472
Cdd:PRK13632 108 GLENKKVpPKKMKDIIDDLakkvgmEDYLdKEPQN-------LSGGQKQRVAIASvLALNPE-IIIFDESTSMLD 174
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
336-501 |
2.08e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 45.39 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 336 QGLDLQVLRGDKIALVGPNGCGKSTLIKllmgQLEASRGSVRQGTNLEvAYFDQYREQLDPEKTVVDnVGegkqevmvrg 415
Cdd:cd03238 12 QNLDVSIPLNVLVVVTGVSGSGKSTLVN----EGLYASGKARLISFLP-KFSRNKLIFIDQLQFLID-VG---------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 416 rsrhiLGYLqdflfepkRARTPVKALSGGEKNRLLLAK-LFLKPSN-LLILDEPTNDL---DVETLELLEELLTDYPGTL 490
Cdd:cd03238 76 -----LGYL--------TLGQKLSTLSGGELQRVKLASeLFSEPPGtLFILDEPSTGLhqqDINQLLEVIKGLIDLGNTV 142
|
170
....*....|.
gi 657198994 491 LLVSHDRRFID 501
Cdd:cd03238 143 ILIEHNLDVLS 153
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
338-500 |
2.11e-05 |
|
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: 46.17 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 338 LDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRQGTNLE---------------VAYFDQYREQLDpeKTVVD 402
Cdd:cd03290 20 INIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNEsepsfeatrsrnrysVAYAAQKPWLLN--ATVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 403 NVGEGKQEVMVRGRSRHILGYLQ-DFLFEPKRARTPVKA----LSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLE 477
Cdd:cd03290 98 NITFGSPFNKQRYKAVTDACSLQpDIDLLPFGDQTEIGErginLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSD 177
|
170 180
....*....|....*....|....*...
gi 657198994 478 LLEEL-----LTDYPGTLLLVSHDRRFI 500
Cdd:cd03290 178 HLMQEgilkfLQDDKRTLVLVTHKLQYL 205
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
13-213 |
2.19e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 45.71 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 13 FSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELplddgrlvlqqdlkvtrleqdPPASSEITVFDYAAEglA 92
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLL---------------------NPEKGEILFERQSIK--K 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 93 GVGELLKQYHHVSHALAHDPsdaNIRTMSQLQEQLDYQNGwqyETRINQVLTLLDLDP--DVTLDSLSGGWLRKVALARA 170
Cdd:PRK13540 68 DLCTYQKQLCFVGHRSGINP---YLTLRENCLYDIHFSPG---AVGITELCRLFSLEHliDYPCGLLSSGQKRQVALLRL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 657198994 171 LACDPDLLLLDEPTNHLDIDAINWLEEFLKDFR---GAIVFISHDR 213
Cdd:PRK13540 142 WMSKAKLWLLDEPLVALDELSLLTIITKIQEHRakgGAVLLTSHQD 187
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
156-245 |
2.23e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 45.26 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 156 SLSGGWLRKVALARALACDPDLLLLDEPTNHLDID----AINWLEEFLKDFRGAIVFISHDREFIHKLATRIIdldrgVI 231
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlnAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIH-----VF 145
|
90
....*....|....
gi 657198994 232 TSWPGNYDEYLQGK 245
Cdd:cd03222 146 EGEPGVYGIASQPK 159
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
24-246 |
2.82e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 46.38 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 24 LTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLvlqqdlkvtrLEQDPPasseitvFDYAAEGL----AGVGELLK 99
Cdd:PRK13636 27 INIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRI----------LFDGKP-------IDYSRKGLmklrESVGMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 100 QYHH--VSHALAHDPSDANIRTmsQLQEQldyqngwQYETRINQVLTLLDLDP--DVTLDSLSGGWLRKVALARALACDP 175
Cdd:PRK13636 90 DPDNqlFSASVYQDVSFGAVNL--KLPED-------EVRKRVDNALKRTGIEHlkDKPTHCLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 657198994 176 DLLLLDEPTNHLDIDAIN----WLEEFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITsWPGNYDEYLQGKE 246
Cdd:PRK13636 161 KVLVLDEPTAGLDPMGVSeimkLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI-LQGNPKEVFAEKE 234
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
18-219 |
2.93e-05 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 45.96 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 18 LLDHAELTIERGERLCLVGRNGAGKSTLMKVIaselplddGRLvlqqdlkvtrleqDPPASSEI-------TVFDYAAEG 90
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLL--------GGL-------------DTPTSGDVifngqpmSKLSSAAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 91 LAGVGEL--LKQYHHvshaLAHDPSDANIRTMSQLqeqLDYQNGWQYETRINQVLTLLDLDPDVTLDS--LSGGWLRKVA 166
Cdd:PRK11629 83 ELRNQKLgfIYQFHH----LLPDFTALENVAMPLL---IGKKKPAEINSRALEMLAAVGLEHRANHRPseLSGGERQRVA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 657198994 167 LARALACDPDLLLLDEPTNHLDI---DAINWLEEFLKDFRG-AIVFISHDREFIHKL 219
Cdd:PRK11629 156 IARALVNNPRLVLADEPTGNLDArnaDSIFQLLGELNRLQGtAFLVVTHDLQLAKRM 212
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
330-472 |
2.93e-05 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 47.02 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLEVAYFDQYRE-----QLDP---EKTV 400
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRlDGRPLSSLSHSVLRQgvamvQQDPvvlADTF 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 401 VDNVGEGKQevMVRGRSRHILGYLQdfLFEPKRA-----RTPV----KALSGGEKNRLLLAKLFLKPSNLLILDEPTNDL 471
Cdd:PRK10790 432 LANVTLGRD--ISEEQVWQALETVQ--LAELARSlpdglYTPLgeqgNNLSVGQKQLLALARVLVQTPQILILDEATANI 507
|
.
gi 657198994 472 D 472
Cdd:PRK10790 508 D 508
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
335-467 |
2.96e-05 |
|
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: 46.63 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 335 FQGLDLQV---LRGDKI-ALVGPNGCGKSTLIKLLMGQLEASRGSVR----------QGTNL-----EVAY-FDQYReqL 394
Cdd:COG4148 11 RGGFTLDVdftLPGRGVtALFGPSGSGKTTLLRAIAGLERPDSGRIRlggevlqdsaRGIFLpphrrRIGYvFQEAR--L 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 657198994 395 DPEKTVVDNVGEGkQEVMVRGRSRHILGYLQDFL-FEPKRARTPVkALSGGEKNRLLLAKLFLKPSNLLILDEP 467
Cdd:COG4148 89 FPHLSVRGNLLYG-RKRAPRAERRISFDEVVELLgIGHLLDRRPA-TLSGGERQRVAIGRALLSSPRLLLMDEP 160
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-191 |
3.03e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 47.13 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 19 LDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLD-DGRLVLQQDLKVTRleqdppasseiTVFDYAAEGLAGVGEL 97
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIR-----------NPAQAIRAGIAMVPED 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 98 LKQYHHVSH-ALAHdpsdaNIrTMSQLQE-----QLDYQNGWQYETRINQVLTLLDLDPDVTLDSLSGGWLRKVALARAL 171
Cdd:TIGR02633 345 RKRHGIVPIlGVGK-----NI-TLSVLKSfcfkmRIDAAAELQIIGSAIQRLKVKTASPFLPIGRLSGGNQQKAVLAKML 418
|
170 180
....*....|....*....|
gi 657198994 172 ACDPDLLLLDEPTNHLDIDA 191
Cdd:TIGR02633 419 LTNPRVLILDEPTRGVDVGA 438
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
156-212 |
3.37e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 45.93 E-value: 3.37e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 657198994 156 SLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDF--RGAIVFISHD 212
Cdd:PRK14243 151 SLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELkeQYTIIIVTHN 209
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
156-225 |
3.78e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 45.54 E-value: 3.78e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 657198994 156 SLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRG--AIVFISHDREfihkLATRIID 225
Cdd:PRK14239 148 GLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDdyTMLLVTRSMQ----QASRISD 215
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
344-472 |
3.81e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 45.90 E-value: 3.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 344 RGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLEVAYFDQYREQL-----DPEK-----TVVDNVGEGKQEVM 412
Cdd:PRK13648 34 KGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFyNNQAITDDNFEKLRKHIgivfqNPDNqfvgsIVKYDVAFGLENHA 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 657198994 413 VRGRSRH--ILGYLQDFLFEPKRARTPvKALSGGEKNRLLLAK-LFLKPSnLLILDEPTNDLD 472
Cdd:PRK13648 114 VPYDEMHrrVSEALKQVDMLERADYEP-NALSGGQKQRVAIAGvLALNPS-VIILDEATSMLD 174
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
157-232 |
4.18e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 45.89 E-value: 4.18e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 657198994 157 LSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRGA---IVFISHDREFIHKLATRIIDLDRGVIT 232
Cdd:PRK13649 146 LSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSgmtIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
311-496 |
4.28e-05 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 46.18 E-value: 4.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 311 EAGRSGKLVFETEGLGLDFGDRTLfqgldlQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLEVAYFDQ 389
Cdd:PRK10070 26 EQGLSKEQILEKTGLSLGVKDASL------AIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLiDGVDIAKISDAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 390 YRE-------------QLDPEKTVVDNVGEGKQ--EVMVRGRSRHILGYLQDFLFEPKRARTPvKALSGGEKNRLLLAKL 454
Cdd:PRK10070 100 LREvrrkkiamvfqsfALMPHMTVLDNTAFGMElaGINAEERREKALDALRQVGLENYAHSYP-DELSGGMRQRVGLARA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 657198994 455 FLKPSNLLILDEPTNDLD----VETLELLEELLTDYPGTLLLVSHD 496
Cdd:PRK10070 179 LAINPDILLMDEAFSALDplirTEMQDELVKLQAKHQRTIVFISHD 224
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
344-513 |
6.04e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 44.10 E-value: 6.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 344 RGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRqgtnlevayFDQYREQLDPEKTvvdnvgegkqevmvrgrsrhilgy 423
Cdd:cd03222 24 EGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDE---------WDGITPVYKPQYI------------------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 424 lqdflfepkrartpvkALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEELLTDY----PGTLLLVSHDRRF 499
Cdd:cd03222 71 ----------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseegKKTALVVEHDLAV 134
|
170
....*....|....
gi 657198994 500 IDNTVTGCWLFEGD 513
Cdd:cd03222 135 LDYLSDRIHVFEGE 148
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
22-217 |
6.32e-05 |
|
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: 46.28 E-value: 6.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 22 AELTIE--RGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLQQDLKVTRLEQDPpasseitvfdyaaegLAGVGELLK 99
Cdd:TIGR00954 469 ESLSFEvpSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRP---------------YMTLGTLRD 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 100 QYhhvshalahdpsdanIRTMSQLQEQldyQNGWQyETRINQVLTLLDLDPDVT-----------LDSLSGGWLRKVALA 168
Cdd:TIGR00954 534 QI---------------IYPDSSEDMK---RRGLS-DKDLEQILDNVQLTHILEreggwsavqdwMDVLSGGEKQRIAMA 594
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 657198994 169 RALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRGAIVFISHDREFIH 217
Cdd:TIGR00954 595 RLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSHRKSLWK 643
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
157-226 |
6.35e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 45.03 E-value: 6.35e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 657198994 157 LSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDFR----GAIVFISHDrefIHKLaTRIIDL 226
Cdd:PRK14258 151 LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrseLTMVIVSHN---LHQV-SRLSDF 220
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
317-473 |
6.47e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 45.02 E-value: 6.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 317 KLVFETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQleasrgSVRQGTNLEVAYFDQYREQLDP 396
Cdd:CHL00131 5 KPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH------PAYKILEGDILFKGESILDLEP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 397 EKTVVDNVGEGKQ-EVMVRGRSRhilgylQDFL---------FEPKRARTPVKAL------------------------- 441
Cdd:CHL00131 79 EERAHLGIFLAFQyPIEIPGVSN------ADFLrlaynskrkFQGLPELDPLEFLeiineklklvgmdpsflsrnvnegf 152
|
170 180 190
....*....|....*....|....*....|..
gi 657198994 442 SGGEKNRLLLAKLFLKPSNLLILDEPTNDLDV 473
Cdd:CHL00131 153 SGGEKKRNEILQMALLDSELAILDETDSGLDI 184
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
337-473 |
7.00e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 45.34 E-value: 7.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 337 GLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLEVA---YFDQYREQ-----------LDPEKTVV 401
Cdd:PRK11308 33 GVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYyQGQDLLKAdpeAQKLLRQKiqivfqnpygsLNPRKKVG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 402 DNVGE--------GKQEvmvrgRSRHILGYLQDFLFEPKRA-RTPvKALSGGEKNRLLLAK-LFLKPsNLLILDEPTNDL 471
Cdd:PRK11308 113 QILEEpllintslSAAE-----RREKALAMMAKVGLRPEHYdRYP-HMFSGGQRQRIAIARaLMLDP-DVVVADEPVSAL 185
|
..
gi 657198994 472 DV 473
Cdd:PRK11308 186 DV 187
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
331-473 |
7.12e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 44.78 E-value: 7.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 331 DRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMG--QLEASRGSVR-QGTNLevayfdqyrEQLDPEktvvDNVGEG 407
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEfKGKDL---------LELSPE----DRAGEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 408 -----KQEVMVRGRSRHIL---------GY----------LQDFLFEPKR---------ARTPVKALSGGEKNRLLLAKL 454
Cdd:PRK09580 80 ifmafQYPVEIPGVSNQFFlqtalnavrSYrgqepldrfdFQDLMEEKIAllkmpedllTRSVNVGFSGGEKKRNDILQM 159
|
170
....*....|....*....
gi 657198994 455 FLKPSNLLILDEPTNDLDV 473
Cdd:PRK09580 160 AVLEPELCILDESDSGLDI 178
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
334-495 |
7.90e-05 |
|
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: 45.90 E-value: 7.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 334 LFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLmGQLEASRGSVRQGTNLEVAYFDQYREQLDpEKTVVDNV--GEGKQEV 411
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRIL-GELWPVYGGRLTKPAKGKLFYVPQRPYMT-LGTLRDQIiyPDSSEDM 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 412 MVRGRS----RHILGYLQ-DFLFEPKRARTPVK----ALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLDVETLELLEEL 482
Cdd:TIGR00954 545 KRRGLSdkdlEQILDNVQlTHILEREGGWSAVQdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRL 624
|
170
....*....|...
gi 657198994 483 LTDYPGTLLLVSH 495
Cdd:TIGR00954 625 CREFGITLFSVSH 637
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
349-472 |
8.87e-05 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 45.77 E-value: 8.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 349 ALVGPNGCGKSTLIKLLMGQLEASRGSVRQGTNLEVAYFDQYREQLD--PEKTVVDNVGEGKQEVM----VRGRSR---- 418
Cdd:TIGR01257 960 AFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGmcPQHNILFHHLTVAEHILfyaqLKGRSWeeaq 1039
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 657198994 419 -HILGYLQDFLFEPKRaRTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:TIGR01257 1040 lEMEAMLEDTGLHHKR-NEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVD 1093
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
29-229 |
9.05e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 44.10 E-value: 9.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 29 GERLCLVGRNGAGKSTLMKVIAS-ELPLDDGRLVLQQDlkVTRLEqdppaSSEITVFDYAaeglagVGELLKQYHHVSHA 107
Cdd:PRK10908 28 GEMAFLTGHSGAGKSTLLKLICGiERPSAGKIWFSGHD--ITRLK-----NREVPFLRRQ------IGMIFQDHHLLMDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 108 LAHD----------PSDANIRtmSQLQEQLDYqngwqyetrinqvLTLLDLDPDVTLdSLSGGWLRKVALARALACDPDL 177
Cdd:PRK10908 95 TVYDnvaipliiagASGDDIR--RRVSAALDK-------------VGLLDKAKNFPI-QLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 657198994 178 LLLDEPTNHLDiDAINwlEEFLKDFR-----GAIVFI-SHDREFIHKLATRIIDLDRG 229
Cdd:PRK10908 159 LLADEPTGNLD-DALS--EGILRLFEefnrvGVTVLMaTHDIGLISRRSYRMLTLSDG 213
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
149-210 |
9.76e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 45.31 E-value: 9.76e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 149 DPDVTLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDA-------INWLEEflkdfRG-AIVFIS 210
Cdd:PRK13549 398 SPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAkyeiyklINQLVQ-----QGvAIIVIS 462
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
157-231 |
1.04e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 44.68 E-value: 1.04e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 657198994 157 LSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEFLKDF--RGAIVFIS-HDREFIHKLATRIIDLDRGVI 231
Cdd:PRK13639 138 LSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLnkEGITIIIStHDVDLVPVYADKVYVMSDGKI 215
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
329-472 |
1.13e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 45.26 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 329 FGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEAS--RGSV-------------RQG--TNLEVAYFD-QY 390
Cdd:PLN03211 78 IQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTIlannrkptkqilkRTGfvTQDDILYPHlTV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 391 REQL-------------DPEKT-----VVDNVGEGKQEVMVRGRSRhilgylqdflfepkrartpVKALSGGEKNRLLLA 452
Cdd:PLN03211 158 RETLvfcsllrlpksltKQEKIlvaesVISELGLTKCENTIIGNSF-------------------IRGISGGERKRVSIA 218
|
170 180
....*....|....*....|.
gi 657198994 453 -KLFLKPSnLLILDEPTNDLD 472
Cdd:PLN03211 219 hEMLINPS-LLILDEPTSGLD 238
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
345-472 |
1.22e-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: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 345 GDKIALVGPNGCGKSTLIKLLMGQLEAsrGSVRQGT---NLEVAYFDQYRE------QLD---PEKTVVDNVgegKQEVM 412
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPK--GVKGSGSvllNGMPIDAKEMRAisayvqQDDlfiPTLTVREHL---MFQAH 125
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 657198994 413 VR-GRS------RHILGYLQDFLFEPKRART------PVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:TIGR00955 126 LRmPRRvtkkekRERVDEVLQALGLRKCANTrigvpgRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
331-473 |
1.23e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 45.08 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 331 DRTLFQGLDLQVLRGDKIALVGPNGCGKS----TLIKLL--------------MGQ--LEASRGSVRQGTNLEVAY-FDQ 389
Cdd:PRK15134 21 VRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLpsppvvypsgdirfHGEslLHASEQTLRGVRGNKIAMiFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 390 YREQLDPEKTVvdnvgeGKQ--EVMV--RGRSR-----HILGYLQDFLFE--PKRARTPVKALSGGEKNRLLLAKLFLKP 458
Cdd:PRK15134 101 PMVSLNPLHTL------EKQlyEVLSlhRGMRReaargEILNCLDRVGIRqaAKRLTDYPHQLSGGERQRVMIAMALLTR 174
|
170
....*....|....*
gi 657198994 459 SNLLILDEPTNDLDV 473
Cdd:PRK15134 175 PELLIADEPTTALDV 189
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
157-240 |
1.31e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 44.78 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 157 LSGGWLRKVALARALACDPDLLLLDEPTNHLDIDA---INWLEEFLKDFRGAIVFISHDREFIHKLATRIIDLDRGVITS 233
Cdd:PRK09700 410 LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAkaeIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
....*..
gi 657198994 234 WPGNYDE 240
Cdd:PRK09700 490 ILTNRDD 496
|
|
| RNA_helicase |
pfam00910 |
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ... |
350-413 |
1.44e-04 |
|
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding during viral RNA replication. Members of this family are found in a variety of single stranded RNA viruses.
Pssm-ID: 459992 Cd Length: 102 Bit Score: 41.44 E-value: 1.44e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 657198994 350 LVGPNGCGKSTLIKLLMGQLEASRGSVRQGT---NLEVAYFDQYREQldpEKTVVDNVGEGKQEVMV 413
Cdd:pfam00910 3 LYGPPGCGKSTLAKYLARALLKKLGLPKDSVysrNPDDDFWDGYTGQ---PVVIIDDFGQNPDGPDE 66
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
335-472 |
1.60e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 43.82 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 335 FQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSV------------RQGTNLEVAYFDQYREQLDPEKTVVD 402
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlvsgidtgdfskLQGIRKLVGIVFQNPETQFVGRTVEE 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 657198994 403 NVGEGKQE-----VMVRGRSRHILGYLQdflFEPKRARTPvKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:PRK13644 98 DLAFGPENlclppIEIRKRVDRALAEIG---LEKYRHRSP-KTLSGGQGQCVALAGILTMEPECLIFDEVTSMLD 168
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
10-203 |
1.75e-04 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 43.83 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 10 SLSFSDFPLLDHAELTIERGERL-CLVGRNGAGKSTLMKVIASELPLDDGRLVLQQDLKVT-RLEQDPPASSEITVFD-- 85
Cdd:COG3950 5 SLTIENFRGFEDLEIDFDNPPRLtVLVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLLiRNGEFGDSAKLILYYGts 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 86 --YAAEGLAGVGELLKQYHHVSHALAH-DPSDANIRT----MSQLQEQLDYQNGWQYETRINQVLTLL------------ 146
Cdd:COG3950 85 rlLLDGPLKKLERLKEEYFSRLDGYDSlLDEDSNLREflewLREYLEDLENKLSDELDEKLEAVREALnkllpdfkdiri 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 147 DLDP-----------DVTLDSLSGG------W----LRKVALARALACDPD----LLLLDEPTNHLDidaINWLEEFLKD 201
Cdd:COG3950 165 DRDPgrlvildkngeELPLNQLSDGersllaLvgdlARRLAELNPALENPLegegIVLIDEIDLHLH---PKWQRRILPD 241
|
..
gi 657198994 202 FR 203
Cdd:COG3950 242 LR 243
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
156-210 |
2.21e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.01 E-value: 2.21e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 657198994 156 SLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDA-------INWLEEFLKdfrgAIVFIS 210
Cdd:NF040905 404 NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAkyeiytiINELAAEGK----GVIVIS 461
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
332-473 |
2.60e-04 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 43.28 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 332 RTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRQGTNLEVAYFDQYREQLDPE-----KTVVDNVGE 406
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRGARVTGDVTLNGEPLAAIDAPrlarlRAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 407 -----GKQEVMVRGRSRHIL---------GYLQDFLFEPKRA----RTPVKALSGGEKNRL----LLAKLF-----LKPS 459
Cdd:PRK13547 94 pafafSAREIVLLGRYPHARragalthrdGEIAWQALALAGAtalvGRDVTTLSGGELARVqfarVLAQLWpphdaAQPP 173
|
170
....*....|....
gi 657198994 460 NLLILDEPTNDLDV 473
Cdd:PRK13547 174 RYLLLDEPTAALDL 187
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
13-195 |
2.64e-04 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 42.63 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 13 FSDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPlddGRLVLQQDLKVTRLEQDPPASseitvfdyaaegla 92
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTE---GNVSVEGDIHYNGIPYKEFAE-------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 93 gvgellkqyHHVSHALAHDPSDANIRTMSqLQEQLDYQ---NGWQYetrinqvltlldldpdvtLDSLSGGWLRKVALAR 169
Cdd:cd03233 80 ---------KYPGEIIYVSEEDVHFPTLT-VRETLDFAlrcKGNEF------------------VRGISGGERKRVSIAE 131
|
170 180
....*....|....*....|....*..
gi 657198994 170 ALACDPDLLLLDEPTNHLD-IDAINWL 195
Cdd:cd03233 132 ALVSRASVLCWDNSTRGLDsSTALEIL 158
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
24-232 |
3.71e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 43.42 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 24 LTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRLVLqQDLKVTRLEQDPPASSEITVFdyaaeglagvgellKQYHH 103
Cdd:PRK10522 344 LTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILL-DGKPVTAEQPEDYRKLFSAVF--------------TDFHL 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 104 VSHALAHDPSDANIRTMSQLQEQLDYQNGWQYETriNQVLTLldldpdvtldSLSGGWLRKVALARALACDPDLLLLDEP 183
Cdd:PRK10522 409 FDQLLGPEGKPANPALVEKWLERLKMAHKLELED--GRISNL----------KLSKGQKKRLALLLALAEERDILLLDEW 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 657198994 184 TNHLD--------IDAINWLEEFLKdfrgAIVFISHDRE-FIHklATRIIDLDRGVIT 232
Cdd:PRK10522 477 AADQDphfrrefyQVLLPLLQEMGK----TIFAISHDDHyFIH--ADRLLEMRNGQLS 528
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
330-473 |
6.70e-04 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 42.40 E-value: 6.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLeASRGSV--------RQGTNLEVAYFDQYR-EQL-----D 395
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLL-AANGRIggsatfngREILNLPEKELNKLRaEQIsmifqD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 396 PEKTVvdN----VGEGKQEVMVRGRsrhilGYLQDFLFEP--------------KRARTPVKALSGGEKNRLLLAKLFLK 457
Cdd:PRK09473 106 PMTSL--NpymrVGEQLMEVLMLHK-----GMSKAEAFEEsvrmldavkmpearKRMKMYPHEFSGGMRQRVMIAMALLC 178
|
170
....*....|....*.
gi 657198994 458 PSNLLILDEPTNDLDV 473
Cdd:PRK09473 179 RPKLLIADEPTTALDV 194
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
336-472 |
9.23e-04 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 42.40 E-value: 9.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 336 QGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLEVAYFDQY-------------REQLDPEKTVV 401
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRvAGQDVATLDADALaqlrrehfgfifqRYHLLSHLTAA 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 657198994 402 DNV-------GEGKQEVmvRGRSRHILGYLQdfLFEpkRARTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:PRK10535 105 QNVevpavyaGLERKQR--LLRAQELLQRLG--LED--RVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALD 176
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
140-216 |
1.38e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 41.22 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 140 NQVLTLLDLDPDVTLDSLSGGWLRKVALARALACD---PDLLLLDEPTNHLDIDAINWLEEFLKDF---RGAIVFISHDR 213
Cdd:pfam13304 220 GLILLENGGGGELPAFELSDGTKRLLALLAALLSAlpkGGLLLIDEPESGLHPKLLRRLLELLKELsrnGAQLILTTHSP 299
|
...
gi 657198994 214 EFI 216
Cdd:pfam13304 300 LLL 302
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
330-472 |
1.40e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 42.03 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 330 GDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGS--VRQGTnleVAYFDQYREQLDpeKTVVDNVGEG 407
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDAsvVIRGT---VAYVPQVSWIFN--ATVRDNILFG 702
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 408 KQEVMVR-GRSRHILGYLQDFLFEPKRARTPVKA----LSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:PLN03130 703 SPFDPERyERAIDVTALQHDLDLLPGGDLTEIGErgvnISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
140-229 |
1.45e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.12 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 140 NQVLTLLDL-----DPDVTLDSLSGGWLRKVALARALACDPD--LLLLDEPTNHL---DIDAINWLEEFLKDFRGAIVFI 209
Cdd:PRK00635 455 SRLSILIDLglpylTPERALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLhpqDTHKLINVIKKLRDQGNTVLLV 534
|
90 100
....*....|....*....|
gi 657198994 210 SHDREFIhKLATRIIDLDRG 229
Cdd:PRK00635 535 EHDEQMI-SLADRIIDIGPG 553
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
154-214 |
1.52e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.81 E-value: 1.52e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 657198994 154 LDSLSGG------WLRKVALARALACDPDLLLLDEPTNHLDIDAINWL----EEFLKDFRG--AIVFISHDRE 214
Cdd:PRK01156 799 IDSLSGGektavaFALRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLkdiiEYSLKDSSDipQVIMISHHRE 871
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
349-471 |
2.08e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.87 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 349 ALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLEvayFDQYREQLDP-------------EKTVVDNVGEGK------ 408
Cdd:PRK10982 28 ALMGENGAGKSTLLKCLFGIYQKDSGSILfQGKEID---FKSSKEALENgismvhqelnlvlQRSVMDNMWLGRyptkgm 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 657198994 409 ---QEVMVRgRSRHILGYLqDFLFEPkraRTPVKALSGGEKNRLLLAKLFLKPSNLLILDEPTNDL 471
Cdd:PRK10982 105 fvdQDKMYR-DTKAIFDEL-DIDIDP---RAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
336-379 |
2.15e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 40.69 E-value: 2.15e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 657198994 336 QGLDL--QVLRGDK-IALVGPNGCGKSTLIKLLMGQLEASRGSVRQG 379
Cdd:PRK01889 183 EGLDVlaAWLSGGKtVALLGSSGVGKSTLVNALLGEEVQKTGAVRED 229
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
336-381 |
2.27e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 39.69 E-value: 2.27e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 657198994 336 QGLD--LQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRQGTN 381
Cdd:cd01854 74 EGLDelRELLKGKTSVLVGQSGVGKSTLLNALLPELVLATGEISEKLG 121
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
332-558 |
2.28e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 41.30 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 332 RTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRQGTNleVAYFDQYREQLDpeKTVVDNVGEGKQEV 411
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERS--IAYVPQQAWIMN--ATVRGNILFFDEED 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 412 MVRgrsrhilgyLQDFL----FEPKRARTPVKA----------LSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD--VET 475
Cdd:PTZ00243 749 AAR---------LADAVrvsqLEADLAQLGGGLeteigekgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALDahVGE 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 476 LELLEELLTDYPG-TLLLVSHDRRFI---DNTVTgcwlfEGDGRIsDYVGGYADMMAT---RALQAAQQTAKPAPVKVAE 548
Cdd:PTZ00243 820 RVVEECFLGALAGkTRVLATHQVHVVpraDYVVA-----LGDGRV-EFSGSSADFMRTslyATLAAELKENKDSKEGDAD 893
|
250
....*....|
gi 657198994 549 PVASAAEPAK 558
Cdd:PTZ00243 894 AEVAEVDAAP 903
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
156-226 |
2.39e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.15 E-value: 2.39e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 657198994 156 SLSGGWLRKVALARAL---ACDPDLLLLDEPTNHLDIDAINWLEEFLKDFRGA---IVFISHDREFIhKLATRIIDL 226
Cdd:TIGR00630 829 TLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKgntVVVIEHNLDVI-KTADYIIDL 904
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
321-496 |
2.63e-03 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 39.97 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 321 ETEGLGLDFGDRTLFQGLDLQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVR-QGTNLE------------VAYF 387
Cdd:PRK11300 7 SVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILlRGQHIEglpghqiarmgvVRTF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 388 DQYReqLDPEKTVVDNvgegkqeVMVrGRSRHI-LGYLQDFLFEPKRARTPVKA-----------------------LSG 443
Cdd:PRK11300 87 QHVR--LFREMTVIEN-------LLV-AQHQQLkTGLFSGLLKTPAFRRAESEAldraatwlervgllehanrqagnLAY 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 657198994 444 GEKNRLLLAKLFLKPSNLLILDEP--------TNDLDvetlELLEELLTDYPGTLLLVSHD 496
Cdd:PRK11300 157 GQQRRLEIARCMVTQPEILMLDEPaaglnpkeTKELD----ELIAELRNEHNVTVLLIEHD 213
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
153-191 |
3.04e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.48 E-value: 3.04e-03
10 20 30
....*....|....*....|....*....|....*....
gi 657198994 153 TLDSLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDA 191
Cdd:PRK10982 388 QIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGA 426
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
336-381 |
3.35e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 38.68 E-value: 3.35e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 657198994 336 QGLD--LQVLRGDKIALVGPNGCGKSTLIKLLMGQLEASRGSVRQGTN 381
Cdd:pfam03193 95 EGIEalKELLKGKTTVLAGQSGVGKSTLLNALLPELDLRTGEISEKLG 142
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
14-188 |
3.74e-03 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 40.47 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 14 SDFPLLDHAELTIERGERLCLVGRNGAGKSTLMKVIASELPLDDGRlVLQQDLKVTRLEQDPPASSeitvfdyaaegLAG 93
Cdd:PRK10789 326 TDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGD-IRFHDIPLTKLQLDSWRSR-----------LAV 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 94 VGE---LLKQYHHVSHALAH-DPSDANIRTMSQL----QEQLDYQNGWQYETRINQVLtlldldpdvtldsLSGGWLRKV 165
Cdd:PRK10789 394 VSQtpfLFSDTVANNIALGRpDATQQEIEHVARLasvhDDILRLPQGYDTEVGERGVM-------------LSGGQKQRI 460
|
170 180
....*....|....*....|...
gi 657198994 166 ALARALACDPDLLLLDEPTNHLD 188
Cdd:PRK10789 461 SIARALLLNAEILILDDALSAVD 483
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
439-472 |
4.74e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.40 E-value: 4.74e-03
10 20 30
....*....|....*....|....*....|....
gi 657198994 439 KALSGGEKNRLLLAKLFLKPSNLLILDEPTNDLD 472
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLD 1390
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
437-471 |
4.77e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.00 E-value: 4.77e-03
10 20 30
....*....|....*....|....*....|....*...
gi 657198994 437 PVKALSGGEKNRLLLAKLFLKPSN---LLILDEPTNDL 471
Cdd:TIGR00630 826 PATTLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGL 863
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
152-228 |
5.08e-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: 38.11 E-value: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 152 VTLDSLSGGWLRKVALARALA---CDPD-LLLLDEPTNHLDIDAINWLEEFLKDFR--GAIV-FISHDREFIhKLATRII 224
Cdd:cd03227 73 FTRLQLSGGEKELSALALILAlasLKPRpLYILDEIDRGLDPRDGQALAEAILEHLvkGAQViVITHLPELA-ELADKLI 151
|
....
gi 657198994 225 DLDR 228
Cdd:cd03227 152 HIKK 155
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
350-467 |
5.25e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 39.18 E-value: 5.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 350 LVGPNGCGKSTLIKLLMGQLE-------ASRGSVRQGTNL------EVAYFDQY-----------REQLDPEKTVVDNVG 405
Cdd:COG4938 25 LIGPNGSGKSTLIQALLLLLQsnfiylpAERSGPARLYPSlvrelsDLGSRGEYtadflaelenlEILDDKSKELLEQVE 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 657198994 406 EGKQEVMVRGRSRHILGYLQDFLFEPKRARTPVKALSGGEKNR-----LLLAKLFLKPSNLLILDEP 467
Cdd:COG4938 105 EWLEKIFPGKVEVDASSDLVRLVFRPSGNGKRIPLSNVGSGVSellpiLLALLSAAKPGSLLIIEEP 171
|
|
| FlhF |
TIGR03499 |
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility] |
257-394 |
6.23e-03 |
|
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274609 [Multi-domain] Cd Length: 282 Bit Score: 38.86 E-value: 6.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 257 AEFDRKLAQEEVWVRQGIKARRTRNEgrVRALKAM------RMERTQRRELQGKAKLQLDEAGRSGKLVFETEGLGLDFG 330
Cdd:TIGR03499 87 APQEEPAAPAAQAAEPLLPEEELRKE--LEALRELlerllaGLAWLQRPPERAKLYERLLEAGVSEELARELLEKLPEDA 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 331 DRTLFQGLDLQVL---------------RGDKIALVGPNGCGKST-LIKLlmgqleASRGSVRQGtNLEVAY--FDQYR- 391
Cdd:TIGR03499 165 DAEDAWRWLREALegmlpvkpeedpileQGGVIALVGPTGVGKTTtLAKL------AARFALEHG-KKKVALitTDTYRi 237
|
....*.
gi 657198994 392 ---EQL 394
Cdd:TIGR03499 238 gavEQL 243
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
437-471 |
7.58e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 38.75 E-value: 7.58e-03
10 20 30
....*....|....*....|....*....|....*...
gi 657198994 437 PVKALSGGEKNRLLLAKLFLKPSN---LLILDEPTNDL 471
Cdd:cd03271 166 PATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGL 203
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
156-227 |
8.56e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 37.93 E-value: 8.56e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 657198994 156 SLSGGWLRKVALARALACDPDLLLLDEPTNHLDIDAINWLEEF--LKDFRGAIVFISHDREFIHKLAtRIIDLD 227
Cdd:PRK13541 123 SLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLivMKANSGGIVLLSSHLESSIKSA-QILQLD 195
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
157-231 |
9.52e-03 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 39.03 E-value: 9.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657198994 157 LSGGWLRKVALARALACDPDLLLLDEPTNHLDidaiNWLEeflKDFRGAIVFISHDREFI---HKLAT-----RIIDLDR 228
Cdd:COG5265 495 LSGGEKQRVAIARTLLKNPPILIFDEATSALD----SRTE---RAIQAALREVARGRTTLviaHRLSTivdadEILVLEA 567
|
...
gi 657198994 229 GVI 231
Cdd:COG5265 568 GRI 570
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
336-367 |
9.84e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.00 E-value: 9.84e-03
10 20 30
....*....|....*....|....*....|..
gi 657198994 336 QGLDLQVLRGDKIALVGPNGCGKSTLIKLLMG 367
Cdd:NF040905 18 DDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| |
