|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
6-570 |
2.19e-97 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 321.23 E-value: 2.19e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 6 WNNICYRDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRkktSSGNIACSSS----------------TSFCEQED 69
Cdd:TIGR00955 32 CRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFR---SPKGVKGSGSvllngmpidakemraiSAYVQQDD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 70 ALLGVMTVKETLKYSARLSVPHATSQVIE-ERVNAVIDGLGLHSVLNNRIGTPIQ-RGISGGQKRRVSIACSLVQFPDIL 147
Cdd:TIGR00955 109 LFIPTLTVREHLMFQAHLRMPRRVTKKEKrERVDEVLQALGLRKCANTRIGVPGRvKGLSGGERKRLAFASELLTDPPLL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 148 FLDEPTSGLDISTAHQVMTAIKRMAVTHNIAVVaTIHSPNWEIFTLFDKLLLLAKGETVFNSKIDQLVPYFEELGYNFPK 227
Cdd:TIGR00955 189 FCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIIC-TIHQPSSELFELFDKIILMAEGRVAYLGSPDQAVPFFSDLGHPCPE 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 228 FSNPVDVVMELINTDFEKQD------SKSIEEGTSSFNRLESLVTSWKSHEKFHVAVTNTSDTQicSSESLSDFVRRTYI 301
Cdd:TIGR00955 268 NYNPADFYVQVLAVIPGSENesreriEKICDSFAVSDIGRDMLVNTNLWSGKAGGLVKDSENME--GIGYNASWWTQFYA 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 302 LSERNLFNYSRNLLAYGVRMGMYVGLGVLLATIWVNLKQSDDRLNDRLSVHFFSVAFLSFMSVAG-IPSYLEERAVLRRE 380
Cdd:TIGR00955 346 LLKRSWLSVLRDPLLLKVRLIQTMMTAILIGLIYLGQGLTQKGVQNINGALFLFLTNMTFQNVFPvINVFTAELPVFLRE 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 381 RANGLYGPLSFTLAQTVMSLPFLFICVVIFTVICYFSIGLHPGASHFFKWMAILYLCILNAEFQSLLVASIFPVFVTSLA 460
Cdd:TIGR00955 426 TRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGATHFLTFLFLVTLVANVATSFGYLISCAFSSTSMALT 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 461 IAAFINGFFMCVQGYFIRAVNLPRFWyYWAHWIDYQTFGFAILTksdllglkfeCNGSIEDDSCQCSYPSTLisqGECAV 540
Cdd:TIGR00955 506 VGPPFVIPFLLFGGFFINSDSIPVYF-KWLSYLSWFRYGNEGLL----------INQWSDVDNIECTSANTT---GPCPS 571
|
570 580 590
....*....|....*....|....*....|
gi 1625600662 541 SGEDVLRQLDYDGISITLySFILLNIWFIG 570
Cdd:TIGR00955 572 SGEVILETLSFRNADLYL-DLIGLVILIFF 600
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
11-542 |
2.03e-66 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 245.02 E-value: 2.03e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 11 YRDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRR----KKTSSGNIACSSSTS------------FCEQEDALLGV 74
Cdd:TIGR00956 73 TFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNtdgfHIGVEGVITYDGITPeeikkhyrgdvvYNAETDVHFPH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 75 MTVKETLKYSARLSVPHATSQVI--EERVNAVID----GLGLHSVLNNRIGTPIQRGISGGQKRRVSIACSLVQFPDILF 148
Cdd:TIGR00956 153 LTVGETLDFAARCKTPQNRPDGVsrEEYAKHIADvymaTYGLSHTRNTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQC 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 149 LDEPTSGLDISTAHQVMTAIKRMAVTHNIAVVATIHSPNWEIFTLFDKLLLLAKGETVFNSKIDQLVPYFEELGYNFPKF 228
Cdd:TIGR00956 233 WDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAKQYFEKMGFKCPDR 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 229 SNPVDVVMEL-------INTDFEKQDSKSIEE------GTSSFNRLESLVTSW-------KSHEKF---HVAvTNTSDTQ 285
Cdd:TIGR00956 313 QTTADFLTSLtspaerqIKPGYEKKVPRTPQEfetywrNSPEYAQLMKEIDEYldrcsesDTKEAYresHVA-KQSKRTR 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 286 ICSSESLSDFVRRTYILsERNLFNYSRNLLAYGVRMGMYVGLGVLLATIWVNLKQSDDRLNDRLSVHFFSVAFLSFMSVA 365
Cdd:TIGR00956 392 PSSPYTVSFSMQVKYCL-ARNFLRMKGNPSFTLFMVFGNIIMALILSSVFYNLPKNTSDFYSRGGALFFAILFNAFSSLL 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 366 GIPSYLEERAVLRRERANGLYGPLSFTLAQTVMSLPFLFICVVIFTVICYFSIGLHPGASHFFKWMAILYLCIL--NAEF 443
Cdd:TIGR00956 471 EIASMYEARPIVEKHRKYALYHPSADAIASIISEIPFKIIESVVFNIILYFMVNFRRTAGRFFFYLLILFICTLamSHLF 550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 444 QSllVASIFPVFVTSLAIAA-FINGFFMcVQGYFIRAVNLPRfWYYWAHWIDYQTFGFAILTKSDLLGLKFECNGSIEDD 522
Cdd:TIGR00956 551 RS--IGAVTKTLSEAMTPAAiLLLALSI-YTGFAIPRPSMLG-WSKWIYYVNPLAYAFESLMVNEFHGRRFECSQYVPSG 626
|
570 580
....*....|....*....|
gi 1625600662 523 ScqcSYPSTLISQGECAVSG 542
Cdd:TIGR00956 627 G---GYDNLGVTNKVCTVVG 643
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
11-208 |
1.91e-55 |
|
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: 190.84 E-value: 1.91e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 11 YRDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTS--SGNI----------ACSSSTSFCEQEDALLGVMTVK 78
Cdd:cd03213 21 GKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVlingrpldkrSFRKIIGYVPQDDILHPTLTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 79 ETLKYSARLsvphatsqvieervnavidglglhsvlnnrigtpiqRGISGGQKRRVSIACSLVQFPDILFLDEPTSGLDI 158
Cdd:cd03213 101 ETLMFAAKL------------------------------------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1625600662 159 STAHQVMTAIKRMAVThNIAVVATIHSPNWEIFTLFDKLLLLAKGETVFN 208
Cdd:cd03213 145 SSALQVMSLLRRLADT-GRTIICSIHQPSSEIFELFDKLLLLSQGRVIYF 193
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
5-490 |
2.02e-55 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 210.74 E-value: 2.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 5 EWNNICY--------RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKT---------SSGNIACSS---STSF 64
Cdd:TIGR00956 761 HWRNLTYevkikkekRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgvitggdrlVNGRPLDSSfqrSIGY 840
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 65 CEQEDALLGVMTVKETLKYSARLSVPHATSqvIEER---VNAVIDGLGLHSVLNNRIGTPiQRGISGGQKRRVSIACSLV 141
Cdd:TIGR00956 841 VQQQDLHLPTSTVRESLRFSAYLRQPKSVS--KSEKmeyVEEVIKLLEMESYADAVVGVP-GEGLNVEQRKRLTIGVELV 917
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 142 QFPD-ILFLDEPTSGLDISTAHQVMTAIKRMAvTHNIAVVATIHSPNWEIFTLFDKLLLLAKG-ETVF------NSKidQ 213
Cdd:TIGR00956 918 AKPKlLLFLDEPTSGLDSQTAWSICKLMRKLA-DHGQAILCTIHQPSAILFEEFDRLLLLQKGgQTVYfgdlgeNSH--T 994
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 214 LVPYFEELG-YNFPKFSNPVDVVMELIN---TDFEKQDSKSIEEGTSSFNRLESLVtSWKSHEKFHVAVTNTSDTQICSS 289
Cdd:TIGR00956 995 IINYFEKHGaPKCPEDANPAEWMLEVIGaapGAHANQDYHEVWRNSSEYQAVKNEL-DRLEAELSKAEDDNDPDALSKYA 1073
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 290 ESLSDFVR----RTYILSERNL-FNYSRNLLAygVRMGMYVGLgvllaTIWVNLKQSDDRLNDRLSVHFFSVAFLSFMSv 364
Cdd:TIGR00956 1074 ASLWYQFKlvlwRTFQQYWRTPdYLYSKFFLT--IFAALFIGF-----TFFKVGTSLQGLQNQMFAVFMATVLFNPLIQ- 1145
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 365 AGIPSYLEERAVLR-RERANGLYGPLSFTLAQTVMSLPFLFICVVIFTVICYFSIGLHPGASH--------FFKWMAILY 435
Cdd:TIGR00956 1146 QYLPPFVAQRDLYEvRERPSRTFSWLAFIAAQITVEIPYNLVAGTIFFFIWYYPVGFYWNASKtgqvhergVLFWLLSTM 1225
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1625600662 436 LCILNAEFqSLLVASIFPVFVTSLAIAAFINGFFMCVQGYFIRAVNLPRFW--YYWA 490
Cdd:TIGR00956 1226 FFLYFSTL-GQMVISFNPNADNAAVLASLLFTMCLSFCGVLAPPSRMPGFWifMYRC 1281
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
5-207 |
2.58e-55 |
|
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: 191.72 E-value: 2.58e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 5 EWNNicYRDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRR---KKTSSGNIACS----------SSTSFCEQEDAL 71
Cdd:cd03234 15 NWNK--YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRvegGGTTSGQILFNgqprkpdqfqKCVAYVRQDDIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 72 LGVMTVKETLKYSARLSVPHATSQVIEERVNAVidgLGLHSVLNNRIGTPIQRGISGGQKRRVSIACSLVQFPDILFLDE 151
Cdd:cd03234 93 LPGLTVRETLTYTAILRLPRKSSDAIRKKRVED---VLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1625600662 152 PTSGLDISTAHQVMTAIKRMAVThNIAVVATIHSPNWEIFTLFDKLLLLAKGETVF 207
Cdd:cd03234 170 PTSGLDSFTALNLVSTLSQLARR-NRIVILTIHQPRSDLFRLFDRILLLSSGEIVY 224
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
12-439 |
1.07e-53 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 199.72 E-value: 1.07e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 12 RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSS--GNIACSSS---------TSFCEQEDALLGVMTVKET 80
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRkptkqilkrTGFVTQDDILYPHLTVRET 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 81 LKYSARLSVPHATSQVIEERV-NAVIDGLGLHSVLNNRIGTPIQRGISGGQKRRVSIACSLVQFPDILFLDEPTSGLDIS 159
Cdd:PLN03211 161 LVFCSLLRLPKSLTKQEKILVaESVISELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDAT 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 160 TAHQVMTAIKRMAvTHNIAVVATIHSPNWEIFTLFDKLLLLAKGETVFNSKIDQLVPYFEELGYNfPKFS-NPVDVVMEL 238
Cdd:PLN03211 241 AAYRLVLTLGSLA-QKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESVGFS-PSFPmNPADFLLDL 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 239 IN----TD-FEKQDSKSIEEG-TSSFNRLES-------LVTSWKSHEKFHVAVTNTSDTQICSSESLSDFVRRTYILSER 305
Cdd:PLN03211 319 ANgvcqTDgVSEREKPNVKQSlVASYNTLLApkvkaaiEMSHFPQANARFVGSASTKEHRSSDRISISTWFNQFSILLQR 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 306 NL---FNYSRNLLaygvRMGMYVGLGVLLATIWVNlkqSDDR-LNDRLSVHFFSVAFL----SFMSVAGIPsylEERAVL 377
Cdd:PLN03211 399 SLkerKHESFNTL----RVFQVIAAALLAGLMWWH---SDFRdVQDRLGLLFFISIFWgvfpSFNSVFVFP---QERAIF 468
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1625600662 378 RRERANGLYGPLSFTLAQTVMSLPFLFICVVIFTVICYFSIGLHPGASHFFKWMAILYLCIL 439
Cdd:PLN03211 469 VKERASGMYTLSSYFMARIVGDLPMELILPTIFLTVTYWMAGLKPELGAFLLTLLVLLGYVL 530
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
2-207 |
7.84e-47 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 165.88 E-value: 7.84e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 2 SPIEWNNICY--------RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTS--SGNIACSS---------ST 62
Cdd:cd03232 2 SVLTWKNLNYtvpvkggkRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGrpldknfqrST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 63 SFCEQEDALLGVMTVKETLKYSARLsvphatsqvieervnavidglglhsvlnnrigtpiqRGISGGQKRRVSIACSLVQ 142
Cdd:cd03232 82 GYVEQQDVHSPNLTVREALRFSALL------------------------------------RGLSVEQRKRLTIGVELAA 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1625600662 143 FPDILFLDEPTSGLDISTAHQVMTAIKRMAvTHNIAVVATIHSPNWEIFTLFDKLLLLAK-GETVF 207
Cdd:cd03232 126 KPSILFLDEPTSGLDSQAAYNIVRFLKKLA-DSGQAILCTIHQPSASIFEKFDRLLLLKRgGKTVY 190
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
14-493 |
1.30e-45 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 179.66 E-value: 1.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 14 ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTS--SGNIACSSS----------TSFCEQEDALLGVMTVKETL 81
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFpkkqetfariSGYCEQNDIHSPQVTVRESL 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 82 KYSARLSVPHATSQviEER---VNAVIDGLGLHSVLNNRIGTPIQRGISGGQKRRVSIACSLVQFPDILFLDEPTSGLDI 158
Cdd:PLN03140 975 IYSAFLRLPKEVSK--EEKmmfVDEVMELVELDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA 1052
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 159 STAHQVMTAIkRMAVTHNIAVVATIHSPNWEIFTLFDKLLLLAKGETVF-------NSKidQLVPYFEELgYNFPKFS-- 229
Cdd:PLN03140 1053 RAAAIVMRTV-RNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKRGGQVIysgplgrNSH--KIIEYFEAI-PGVPKIKek 1128
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 230 -NPVDVVMELINTDFEKQ---DSKSIEEGTSSFNRLESLVtswkshEKFHVAVTNTSDTQICSSESLSDFVRRTYILSeR 305
Cdd:PLN03140 1129 yNPATWMLEVSSLAAEVKlgiDFAEHYKSSSLYQRNKALV------KELSTPPPGASDLYFATQYSQSTWGQFKSCLW-K 1201
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 306 NLFNYSR----NLLAYGVRMGMYVGLGVLLATIWVNLKQSDDrLNDRLSVHFFSVAFLSFMSVAGI-PSYLEERAVLRRE 380
Cdd:PLN03140 1202 QWWTYWRspdyNLVRFFFTLAAALMVGTIFWKVGTKRSNAND-LTMVIGAMYAAVLFVGINNCSTVqPMVAVERTVFYRE 1280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 381 RANGLYGPLSFTLAQTVMSLPFLFICVVIFTVICYFSIGLHPGASHFFKWMAILYLCILNAEFQSLLVASIFPVFVTSLA 460
Cdd:PLN03140 1281 RAAGMYSALPYAIAQVVCEIPYVLIQTTYYTLIVYAMVAFEWTAAKFFWFYFISFFSFLYFTYYGMMTVSLTPNQQVAAI 1360
|
490 500 510
....*....|....*....|....*....|...
gi 1625600662 461 IAAFINGFFMCVQGYFIRAVNLPRfWYYWAHWI 493
Cdd:PLN03140 1361 FAAAFYGLFNLFSGFFIPRPKIPK-WWVWYYWI 1392
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
14-509 |
2.41e-38 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 156.16 E-value: 2.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 14 ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTS---SGNIACS----------SSTSFCEQEDALLGVMTVKET 80
Cdd:PLN03140 180 ILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNgyrlnefvprKTSAYISQNDVHVGVMTVKET 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 81 LKYSAR----------LS-----------VPHA------TSQVIEERVNAVIDG-----LGLHSVLNNRIGTPIQRGISG 128
Cdd:PLN03140 260 LDFSARcqgvgtrydlLSelarrekdagiFPEAevdlfmKATAMEGVKSSLITDytlkiLGLDICKDTIVGDEMIRGISG 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 129 GQKRRVSIACSLVQFPDILFLDEPTSGLDISTAHQVMTAIKRMAVTHNIAVVATIHSPNWEIFTLFDKLLLLAKGETVFN 208
Cdd:PLN03140 340 GQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQPAPETFDLFDDIILLSEGQIVYQ 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 209 SKIDQLVPYFEELGYNFPKFSNPVDVVMELINTDFEKQ---DSK------SIEEGTSSFNRL--------ESLVTSWKSh 271
Cdd:PLN03140 420 GPRDHILEFFESCGFKCPERKGTADFLQEVTSKKDQEQywaDRNkpyryiSVSEFAERFKSFhvgmqlenELSVPFDKS- 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 272 eKFHVAVTNTSDTQICSSESLSDFVRRTYILSERNLFNYsrnlLAYGVRMgmyVGLGVLLATIWVNLK-----QSDDRLn 346
Cdd:PLN03140 499 -QSHKAALVFSKYSVPKMELLKACWDKEWLLMKRNAFVY----VFKTVQI---IIVAAIASTVFLRTEmhtrnEEDGAL- 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 347 dRLSVHFFSVAFLSFMSVAGIPSYLEERAVLRRERANGLYGPLSFTLAQTVMSLPFLFICVVIFTVICYFSIGLHPGASH 426
Cdd:PLN03140 570 -YIGALLFSMIINMFNGFAELALMIQRLPVFYKQRDLLFHPPWTFTLPTFLLGIPISIIESVVWVVITYYSIGFAPEASR 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 427 FFKWMAILYLCILNAEFQSLLVASIFPVFVTSLAIAAFINGFFMCVQGYFIRAVNLPRfWYYWAHWIDYQTFGFAILTKS 506
Cdd:PLN03140 649 FFKQLLLVFLIQQMAAGIFRLIASVCRTMIIANTGGALVLLLVFLLGGFILPKGEIPN-WWEWAYWVSPLSYGFNALAVN 727
|
...
gi 1625600662 507 DLL 509
Cdd:PLN03140 728 EMF 730
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-214 |
3.47e-38 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 142.90 E-value: 3.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 4 IEWNNIC--YRD--ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI------------ACSSSTSFCEQ 67
Cdd:COG1131 1 IEVRGLTkrYGDktALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVrvlgedvardpaEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 68 EDALLGVMTVKETLKYSARLSvpHATSQVIEERVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDIL 147
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLY--GLPRKEARERIDELLELFGLTDAADRKVGT-----LSGGMKQRLGLALALLHDPELL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1625600662 148 FLDEPTSGLDISTAHQVMTAIKRMAvTHNIAVVATIHSPNwEIFTLFDKLLLLAKGETVFNSKIDQL 214
Cdd:COG1131 154 ILDEPTSGLDPEARRELWELLRELA-AEGKTVLLSTHYLE-EAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
10-214 |
5.63e-38 |
|
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: 141.49 E-value: 5.63e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 10 CYRDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI------------ACSSSTSFCEQEDALLGVMTV 77
Cdd:cd03263 13 GTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAyingysirtdrkAARQSLGYCPQFDALFDELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 78 KETLKYSARL-SVPHATsqvIEERVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLDEPTSGL 156
Cdd:cd03263 93 REHLRFYARLkGLPKSE---IKEEVELLLRVLGLTDKANKRART-----LSGGMKRKLSLAIALIGGPSVLLLDEPTSGL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1625600662 157 DISTAHQVMTAIKRMavTHNIAVVATIHSPNwEIFTLFDKLLLLAKGETVFNSKIDQL 214
Cdd:cd03263 165 DPASRRAIWDLILEV--RKGRSIILTTHSMD-EAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
12-206 |
9.36e-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: 133.63 E-value: 9.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 12 RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACS----SSTSFCE---------QEDALLGVMTVK 78
Cdd:COG1120 14 RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDgrdlASLSRRElarriayvpQEPPAPFGLTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 79 ETLKYsARLsvPHAT-----SQVIEERVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLDEPT 153
Cdd:COG1120 94 ELVAL-GRY--PHLGlfgrpSAEDREAVEEALERTGLEHLADRPVDE-----LSGGERQRVLIARALAQEPPLLLLDEPT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1625600662 154 SGLDISTAHQVMTAIKRMAVTHNIAVVATIHSPNWeIFTLFDKLLLLAKGETV 206
Cdd:COG1120 166 SHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNL-AARYADRLVLLKDGRIV 217
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1-207 |
2.03e-34 |
|
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: 130.85 E-value: 2.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 1 MSPIEWNNICYR--------DILKQISGDVKPAEILAVMGPSGSGKTTLLECISRR---KKTSSGNI------------A 57
Cdd:cd03233 1 ASTLSWRNISFTtgkgrskiPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegNVSVEGDIhyngipykefaeK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 58 CSSSTSFCEQEDALLGVMTVKETLKYSARLsvphatsqvieeRVNAVIdglglhsvlnnrigtpiqRGISGGQKRRVSIA 137
Cdd:cd03233 81 YPGEIIYVSEEDVHFPTLTVRETLDFALRC------------KGNEFV------------------RGISGGERKRVSIA 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 138 CSLVQFPDILFLDEPTSGLDISTAHQVMTAIKRMAVTHNIAVVATIHSPNWEIFTLFDKLLLLAKGETVF 207
Cdd:cd03233 131 EALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIY 200
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
12-206 |
6.12e-34 |
|
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: 128.71 E-value: 6.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 12 RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIacssstSFCEQEdalLGVMTVKETLKysaRLSVph 91
Cdd:cd03214 12 RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEI------LLDGKD---LASLSPKELAR---KIAY-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 92 aTSQVIEErvnavidgLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTAHQVMTAIKRM 171
Cdd:cd03214 78 -VPQALEL--------LGLAHLADRPFNE-----LSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRL 143
|
170 180 190
....*....|....*....|....*....|....*
gi 1625600662 172 AVTHNIAVVATIHSPNWeIFTLFDKLLLLAKGETV 206
Cdd:cd03214 144 ARERGKTVVMVLHDLNL-AARYADRVILLKDGRIV 177
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
302-503 |
6.78e-34 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 129.32 E-value: 6.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 302 LSERNLFNYSRNLLAYGVRMGMYVGLGVLLATIWVNLKQSDDRLNdRLSVHFFSVAFLSFMSVAGI-PSYLEERAVLRRE 380
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLGNQQGGLN-RPGLLFFSILFNAFSALSGIsPVFEKERGVLYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 381 RANGLYGPLSFTLAQTVMSLPFLFICVVIFTVICYFSIGLHPGASHFFKWMAILYLCILNAEFQSLLVASIFPVFVTSLA 460
Cdd:pfam01061 80 LASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDASQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1625600662 461 IAAFINGFFMCVQGYFIRAVNLPRFWyYWAHWIDYQTFGFAIL 503
Cdd:pfam01061 160 LGPLVLLPLLLLSGFFIPIDSMPVWW-QWIYYLNPLTYAIEAL 201
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-204 |
7.56e-34 |
|
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: 129.51 E-value: 7.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 7 NNICYR------DILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACS----SSTSFCE---------Q 67
Cdd:cd03225 3 KNLSFSypdgarPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDgkdlTKLSLKElrrkvglvfQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 68 --EDALLGvMTVKETLKYSAR-LSVPHATsqvIEERVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFP 144
Cdd:cd03225 83 npDDQFFG-PTVEEEVAFGLEnLGLPEEE---IEERVEEALELVGLEGLRDRSPFT-----LSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 145 DILFLDEPTSGLDISTAHQVMTAIKRMAVTHNIAVVATiHSPNWeIFTLFDKLLLLAKGE 204
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVT-HDLDL-LLELADRVIVLEDGK 211
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
14-214 |
3.18e-32 |
|
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: 125.74 E-value: 3.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 14 ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIA---CSSST---------SFCEQEDALLGVMTVKETL 81
Cdd:COG4555 16 ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILidgEDVRKeprearrqiGVLPDERGLYDRLTVRENI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 82 KYSARLSvpHATSQVIEERVNAVIDGLGLHSVLNNRIGtpiqrGISGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTA 161
Cdd:COG4555 96 RYFAELY--GLFDEELKKRIEELIELLGLEEFLDRRVG-----ELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMAR 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1625600662 162 HQVMTAIKRMAvTHNIAVVATIHSPNwEIFTLFDKLLLLAKGETVFNSKIDQL 214
Cdd:COG4555 169 RLLREILRALK-KEGKTVLFSSHIMQ-EVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
9-204 |
4.29e-32 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 124.16 E-value: 4.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 9 ICYRDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI-----ACSSST--------SFCEQEDALLGvM 75
Cdd:COG4619 10 VGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIyldgkPLSAMPppewrrqvAYVPQEPALWG-G 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 76 TVKETLKYSARLSVPHATsqviEERVNAVIDGLGL-HSVLNnrigTPIQRgISGGQKRRVSIACSLVQFPDILFLDEPTS 154
Cdd:COG4619 89 TVRDNLPFPFQLRERKFD----RERALELLERLGLpPDILD----KPVER-LSGGERQRLALIRALLLQPDVLLLDEPTS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1625600662 155 GLDISTAHQVMTAIKRMAVTHNIAVVATIHSPNWeIFTLFDKLLLLAKGE 204
Cdd:COG4619 160 ALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQ-IERVADRVLTLEAGR 208
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-206 |
1.89e-31 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 123.23 E-value: 1.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 1 MSP-IEWNNIC--YRD------ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIacssstSFCEQ---- 67
Cdd:COG1136 1 MSPlLELRNLTksYGTgegevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEV------LIDGQdiss 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 68 --EDA-----------------LLGVMTVKETLKYSARLSvpHATSQVIEERVNAVIDGLGLHSVLNNRIGTpiqrgISG 128
Cdd:COG1136 75 lsERElarlrrrhigfvfqffnLLPELTALENVALPLLLA--GVSRKERRERARELLERVGLGDRLDHRPSQ-----LSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1625600662 129 GQKRRVSIACSLVQFPDILFLDEPTSGLDISTAHQVMTAIKRMAVTHNIAVVATIHSPnwEIFTLFDKLLLLAKGETV 206
Cdd:COG1136 148 GQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP--ELAARADRVIRLRDGRIV 223
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-214 |
5.93e-31 |
|
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: 121.84 E-value: 5.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 4 IEWNNICY----RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI--------ACSSS--------TS 63
Cdd:cd03261 1 IELRGLTKsfggRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVlidgedisGLSEAelyrlrrrMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 64 FCEQEDALLGVMTVKET----LKYSARLSvphatSQVIEERVNAVIDGLGLHSVLNNRigtPIQrgISGGQKRRVSIACS 139
Cdd:cd03261 81 MLFQSGALFDSLTVFENvafpLREHTRLS-----EEEIREIVLEKLEAVGLRGAEDLY---PAE--LSGGMKKRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1625600662 140 LVQFPDILFLDEPTSGLDISTAHQVMTAIKRMAVTHNIAVVATIHSPNwEIFTLFDKLLLLAKGETVFNSKIDQL 214
Cdd:cd03261 151 LALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLD-TAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
15-154 |
8.84e-31 |
|
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: 118.52 E-value: 8.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 15 LKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIAC-------------SSSTSFCEQEDALLGVMTVKETL 81
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLdgqdltdderkslRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1625600662 82 KYSARLsvPHATSQVIEERVNAVIDGLGLHSVLNNRIGTPIqRGISGGQKRRVSIACSLVQFPDILFLDEPTS 154
Cdd:pfam00005 81 RLGLLL--KGLSKREKDARAEEALEKLGLGDLADRPVGERP-GTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
12-204 |
1.36e-30 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 118.12 E-value: 1.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 12 RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIacssstsfceqedallgvmtvketlkysarlsvph 91
Cdd:cd00267 12 RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEI----------------------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 92 atsqvieervnaVIDGLGLHSVLNNRIGTPIQR--GISGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTAHQVMTAIK 169
Cdd:cd00267 57 ------------LIDGKDIAKLPLEELRRRIGYvpQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLR 124
|
170 180 190
....*....|....*....|....*....|....*
gi 1625600662 170 RMAVTHNIAVVATiHSPNWEIFtLFDKLLLLAKGE 204
Cdd:cd00267 125 ELAEEGRTVIIVT-HDPELAEL-AADRVIVLKDGK 157
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
14-204 |
1.49e-30 |
|
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: 120.29 E-value: 1.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 14 ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSG-------NIACSSST----------SFCEQEDALLGVMT 76
Cdd:cd03255 19 ALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGevrvdgtDISKLSEKelaafrrrhiGFVFQSFNLLPDLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 77 VKETLKYSARLSvpHATSQVIEERVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLDEPTSGL 156
Cdd:cd03255 99 ALENVELPLLLA--GVPKKERRERAEELLERVGLGDRLNHYPSE-----LSGGQQQRVAIARALANDPKIILADEPTGNL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1625600662 157 DISTAHQVMTAIKRMAVTHNIAVVATIHSPnwEIFTLFDKLLLLAKGE 204
Cdd:cd03255 172 DSETGKEVMELLRELNKEAGTTIVVVTHDP--ELAEYADRIIELRDGK 217
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
12-214 |
1.73e-30 |
|
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: 120.75 E-value: 1.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 12 RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI----------------ACSSSTSFCEQEDALLGVM 75
Cdd:cd03256 14 KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVlidgtdinklkgkalrQLRRQIGMIFQQFNLIERL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 76 TVKETLkYSARLSVpHATSQVI------EERVNAV--IDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDIL 147
Cdd:cd03256 94 SVLENV-LSGRLGR-RSTWRSLfglfpkEEKQRALaaLERVGLLDKAYQRADQ-----LSGGQQQRVAIARALMQQPKLI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1625600662 148 FLDEPTSGLDISTAHQVMTAIKRMAVTHNIAVVATIHSPnwEIFTLF-DKLLLLAKGETVFNSKIDQL 214
Cdd:cd03256 167 LADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQV--DLAREYaDRIVGLKDGRIVFDGPPAEL 232
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
12-214 |
2.61e-30 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 120.55 E-value: 2.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 12 RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACS----------------SSTSFCEQEDALLGVM 75
Cdd:COG3638 16 TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDgqdvtalrgralrrlrRRIGMIFQQFNLVPRL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 76 TVKE-----TLkysARLSVPHATSQVI--EERVNA--VIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDI 146
Cdd:COG3638 96 SVLTnvlagRL---GRTSTWRSLLGLFppEDRERAleALERVGLADKAYQRADQ-----LSGGQQQRVAIARALVQEPKL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1625600662 147 LFLDEPTSGLDISTAHQVMTAIKRMAVTHNIAVVATIHSPNWeIFTLFDKLLLLAKGETVFNSKIDQL 214
Cdd:COG3638 168 ILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDL-ARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
14-183 |
8.78e-30 |
|
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: 118.38 E-value: 8.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 14 ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIacssstSFCEQEDALLG-------------------- 73
Cdd:cd03257 20 ALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSI------IFDGKDLLKLSrrlrkirrkeiqmvfqdpms 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 74 ----VMTVKETLKYSARLSVPHATSQVIEERVNAVIDGLGLHS-VLNNRigtPIQrgISGGQKRRVSIACSLVQFPDILF 148
Cdd:cd03257 94 slnpRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEeVLNRY---PHE--LSGGQRQRVAIARALALNPKLLI 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1625600662 149 LDEPTSGLDISTAHQVMTAIKRMA---------VTHNIAVVATI 183
Cdd:cd03257 169 ADEPTSALDVSVQAQILDLLKKLQeelgltllfITHDLGVVAKI 212
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
12-214 |
1.36e-29 |
|
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: 118.16 E-value: 1.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 12 RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI--------ACSSST----------SFceQEDALLG 73
Cdd:COG1127 18 RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEIlvdgqditGLSEKElyelrrrigmLF--QGGALFD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 74 VMTVKE----TLKYSARLSvphatSQVIEERVNAVIDGLGLHSVLNNRigtPIQrgISGGQKRRVSIACSLVQFPDILFL 149
Cdd:COG1127 96 SLTVFEnvafPLREHTDLS-----EAEIRELVLEKLELVGLPGAADKM---PSE--LSGGMRKRVALARALALDPEILLY 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1625600662 150 DEPTSGLDISTAHQVMTAIKRMAVTHNIAVVATIHSPNwEIFTLFDKLLLLAKGETVFNSKIDQL 214
Cdd:COG1127 166 DEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLD-SAFAIADRVAVLADGKIIAEGTPEEL 229
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
13-206 |
2.81e-29 |
|
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: 116.46 E-value: 2.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 13 DILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI-----------ACSSSTSFCEQEDALLGVMTVKETL 81
Cdd:cd03259 14 RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEIlidgrdvtgvpPERRNIGMVFQDYALFPHLTVAENI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 82 KYSARLS-VPHATsqvIEERVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLDIST 160
Cdd:cd03259 94 AFGLKLRgVPKAE---IRARVRELLELVGLEGLLNRYPHE-----LSGGQQQRVALARALAREPSLLLLDEPLSALDAKL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1625600662 161 AHQVMTAIKRMAVTHNIAVVATIHSPNwEIFTLFDKLLLLAKGETV 206
Cdd:cd03259 166 REELREELKELQRELGITTIYVTHDQE-EALALADRIAVMNEGRIV 210
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-221 |
5.93e-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: 115.89 E-value: 5.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 4 IEWNNICY-----RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSG-------NIACSSSTSFCEQ---- 67
Cdd:COG1122 1 IELENLSFsypggTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGevlvdgkDITKKNLRELRRKvglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 68 ----EDALLGvMTVKETLKYSAR-LSVPHATsqvIEERVNAVIDGLGLHSVLNnrigTPIQRgISGGQKRRVSIACSLVQ 142
Cdd:COG1122 81 fqnpDDQLFA-PTVEEDVAFGPEnLGLPREE---IRERVEEALELVGLEHLAD----RPPHE-LSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1625600662 143 FPDILFLDEPTSGLDISTAHQVMTAIKRMAVTHNIAVVATiHSPNwEIFTLFDKLLLLAKGETVFNSKIDQLVPYFEEL 221
Cdd:COG1122 152 EPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVT-HDLD-LVAELADRVIVLDDGRIVADGTPREVFSDYELL 228
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-204 |
1.38e-28 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 113.05 E-value: 1.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 4 IEWNNICYR----DILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSstsfceqedallgvmtvkE 79
Cdd:cd03229 1 LELKNVSKRygqkTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDG------------------E 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 80 TLKYSARLSVPHatsqviEERVNAVIDGLGL--H-SVLNNrigtpIQRGISGGQKRRVSIACSLVQFPDILFLDEPTSGL 156
Cdd:cd03229 63 DLTDLEDELPPL------RRRIGMVFQDFALfpHlTVLEN-----IALGLSGGQQQRVALARALAMDPDVLLLDEPTSAL 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1625600662 157 DISTAHQVMTAIKRMAVTHNIAVVATIHSPNwEIFTLFDKLLLLAKGE 204
Cdd:cd03229 132 DPITRREVRALLKSLQAQLGITVVLVTHDLD-EAARLADRVVVLRDGK 178
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
14-214 |
1.82e-28 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 115.09 E-value: 1.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 14 ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACS----------------SSTSFCEQEDALLGVMTV 77
Cdd:TIGR02315 17 ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEgtditklrgkklrklrRRIGMIFQHYNLIERLTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 78 KETLkYSARLSVpHATSQVI------EERVNAV--IDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFL 149
Cdd:TIGR02315 97 LENV-LHGRLGY-KPTWRSLlgrfseEDKERALsaLERVGLADKAYQRADQ-----LSGGQQQRVAIARALAQQPDLILA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1625600662 150 DEPTSGLDISTAHQVMTAIKRMAVTHNIAVVATIHspNWEIFTLF-DKLLLLAKGETVFNSKIDQL 214
Cdd:TIGR02315 170 DEPIASLDPKTSKQVMDYLKRINKEDGITVIINLH--QVDLAKKYaDRIVGLKAGEIVFDGAPSEL 233
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-204 |
2.42e-28 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 112.11 E-value: 2.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 4 IEWNNIC--YRD--ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI------------ACSSSTSFCEQ 67
Cdd:cd03230 1 IEVRNLSkrYGKktALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIkvlgkdikkepeEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 68 EDALLGVMTVKETLKYSarlsvphatsqvieervnavidglglhsvlnnrigtpiqrgisGGQKRRVSIACSLVQFPDIL 147
Cdd:cd03230 81 EPSLYENLTVRENLKLS-------------------------------------------GGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1625600662 148 FLDEPTSGLDISTAHQVMTAIKRMAvTHNIAVVATIHSPNwEIFTLFDKLLLLAKGE 204
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRELK-KEGKTILLSSHILE-EAERLCDRVAILNNGR 172
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-209 |
2.85e-28 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 114.42 E-value: 2.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 1 MSPIEWNNICY----RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSSTSfcEQEDALLG-V- 74
Cdd:COG1121 4 MPAIELENLTVsyggRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP--RRARRRIGyVp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 75 ----------MTVKETLK--YSARLSVPHATSQVIEERVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQ 142
Cdd:COG1121 82 qraevdwdfpITVRDVVLmgRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGE-----LSGGQQQRVLLARALAQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 143 FPDILFLDEPTSGLDISTAHQVMTAIKRMA--------VTHNIAVVAtihspnweifTLFDKLLLLAKG-------ETVF 207
Cdd:COG1121 157 DPDLLLLDEPFAGVDAATEEALYELLRELRregktilvVTHDLGAVR----------EYFDRVLLLNRGlvahgppEEVL 226
|
..
gi 1625600662 208 NS 209
Cdd:COG1121 227 TP 228
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-204 |
8.73e-27 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 116.40 E-value: 8.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 2 SPIEWNNICY-----RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACS-------SSTSFCE--- 66
Cdd:COG4988 335 PSIELEDVSFsypggRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINgvdlsdlDPASWRRqia 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 67 ---QEDALLGvMTVKETLkysaRLSVPHATsqviEERVNAVIDGLGLHSV---LNNRIGTPIQ---RGISGGQKRRVSIA 137
Cdd:COG4988 415 wvpQNPYLFA-GTIRENL----RLGRPDAS----DEELEAALEAAGLDEFvaaLPDGLDTPLGeggRGLSGGQAQRLALA 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1625600662 138 CSLVQFPDILFLDEPTSGLDISTAHQVMTAIKRMAVTHnIAVVATiHSPNWEifTLFDKLLLLAKGE 204
Cdd:COG4988 486 RALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR-TVILIT-HRLALL--AQADRILVLDDGR 548
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
24-207 |
1.27e-26 |
|
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: 108.92 E-value: 1.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 24 PAEILAVMGPSGSGKTTLLECISRRKKTSSGNIA-------------CSSST----SFCEQEDALLGVMTVKETLKYSAR 86
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVlngtvlfdsrkkiNLPPQqrkiGLVFQQYALFPHLNVRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 87 LSVPhatsQVIEERVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTAHQVMT 166
Cdd:cd03297 102 RKRN----REDRISVDELLDLLGLDHLLNRYPAQ-----LSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1625600662 167 AIKRMAVTHNIAVVATIHSPNwEIFTLFDKLLLLAKGETVF 207
Cdd:cd03297 173 ELKQIKKNLNIPVIFVTHDLS-EAEYLADRIVVMEDGRLQY 212
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
12-183 |
8.21e-26 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 106.88 E-value: 8.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 12 RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISR-----RKKTSSGNIACSSSTSFCEQEDALL-----GV------- 74
Cdd:cd03260 13 KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDIYDLDVDVLElrrrvGMvfqkpnp 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 75 --MTVKETLKYSARLsvpH--ATSQVIEERVNAVIDGLGLHSVLNNRIGTpiqRGISGGQKRRVSIACSLVQFPDILFLD 150
Cdd:cd03260 93 fpGSIYDNVAYGLRL---HgiKLKEELDERVEEALRKAALWDEVKDRLHA---LGLSGGQQQRLCLARALANEPEVLLLD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1625600662 151 EPTSGLDISTAHQVMTAIKRMA-------VTHNIAVVATI 183
Cdd:cd03260 167 EPTSALDPISTAKIEELIAELKkeytiviVTHNMQQAARV 206
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-221 |
2.26e-25 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 112.17 E-value: 2.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 4 IEWNNICYR------DILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIAC-------------SSSTSF 64
Cdd:COG4987 334 LELEDVSFRypgagrPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLggvdlrdldeddlRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 65 CEQEDALLGvMTVKETLkysaRLSVPHATsqviEERVNAVIDGLGLHSVLNNRIG---TPIQ---RGISGGQKRRVSIAC 138
Cdd:COG4987 414 VPQRPHLFD-TTLRENL----RLARPDAT----DEELWAALERVGLGDWLAALPDgldTWLGeggRRLSGGERRRLALAR 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 139 SLVQFPDILFLDEPTSGLDISTAHQVMTAIKRMA-------VTHNIAVVAtihspnweiftLFDKLLLLAKGETVFNSKI 211
Cdd:COG4987 485 ALLRDAPILLLDEPTEGLDAATEQALLADLLEALagrtvllITHRLAGLE-----------RMDRILVLEDGRIVEQGTH 553
|
250
....*....|...
gi 1625600662 212 DQLV---PYFEEL 221
Cdd:COG4987 554 EELLaqnGRYRQL 566
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
12-186 |
2.50e-25 |
|
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: 104.87 E-value: 2.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 12 RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI------------ACSSSTSFCEQEDALLGVMTVKE 79
Cdd:COG4133 15 RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVlwngepirdareDYRRRLAYLGHADGLKPELTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 80 TLKYSARLSVPHATsqviEERVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLDIS 159
Cdd:COG4133 95 NLRFWAALYGLRAD----REAIDEALEAVGLAGLADLPVRQ-----LSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA 165
|
170 180
....*....|....*....|....*..
gi 1625600662 160 TAHQVMTAIKRMAVTHNIAVVATiHSP 186
Cdd:COG4133 166 GVALLAELIAAHLARGGAVLLTT-HQP 191
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
14-183 |
3.35e-25 |
|
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: 111.15 E-value: 3.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 14 ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSG-------NIACSSSTSFCEQ-----------EDALLGVM 75
Cdd:COG1123 280 AVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGsilfdgkDLTKLSRRSLRELrrrvqmvfqdpYSSLNPRM 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 76 TVKETLKYSARLSvPHATSQVIEERVNAVIDGLGLH-SVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLDEPTS 154
Cdd:COG1123 360 TVGDIIAEPLRLH-GLLSRAERRERVAELLERVGLPpDLADRYPHE-----LSGGQRQRVAIARALALEPKLLILDEPTS 433
|
170 180 190
....*....|....*....|....*....|....*...
gi 1625600662 155 GLDISTAHQVMTAIKRMA---------VTHNIAVVATI 183
Cdd:COG1123 434 ALDVSVQAQILNLLRDLQrelgltylfISHDLAVVRYI 471
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-224 |
5.02e-25 |
|
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: 104.73 E-value: 5.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 4 IEWNNIC--YRDI-LKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSS-----------TSFCEQED 69
Cdd:cd03299 1 LKVENLSkdWKEFkLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppekrdISYVPQNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 70 ALLGVMTVKETLKYSARL-SVPHATsqvIEERVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILF 148
Cdd:cd03299 81 ALFPHMTVYKNIAYGLKKrKVDKKE---IERKVLEIAEMLGIDHLLNRKPET-----LSGGEQQRVAIARALVVNPKILL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 149 LDEPTSGLDISTAHQVMTAIKRMAVTHNIAVVATIHSPNwEIFTLFDKLLLLAKG--------ETVFNSKIDQLVPYFee 220
Cdd:cd03299 153 LDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFE-EAWALADKVAIMLNGkliqvgkpEEVFKKPKNEFVAEF-- 229
|
....
gi 1625600662 221 LGYN 224
Cdd:cd03299 230 LGFN 233
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-215 |
8.05e-25 |
|
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: 111.08 E-value: 8.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 4 IEWNNICYR------DILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI-------------ACSSSTSF 64
Cdd:COG2274 474 IELENVSFRypgdspPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIlidgidlrqidpaSLRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 65 CEQEDALLGvMTVKETLkysaRLSVPHATsqviEERVNAVIDGLGLHSVLNNR---IGTPIQ---RGISGGQKRRVSIAC 138
Cdd:COG2274 554 VLQDVFLFS-GTIRENI----TLGDPDAT----DEEIIEAARLAGLHDFIEALpmgYDTVVGeggSNLSGGQRQRLAIAR 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 139 SLVQFPDILFLDEPTSGLDISTAHQVMTAIKRMA-------VTHNIAVVAtihspnweiftLFDKLLLLAKGETVFNSKI 211
Cdd:COG2274 625 ALLRNPRILILDEATSALDAETEAIILENLRRLLkgrtviiIAHRLSTIR-----------LADRIIVLDKGRIVEDGTH 693
|
....
gi 1625600662 212 DQLV 215
Cdd:COG2274 694 EELL 697
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
12-206 |
1.35e-24 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 104.11 E-value: 1.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 12 RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIAC-------SSSTSFCEQ--------EDALLGVMT 76
Cdd:COG1124 18 VPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFdgrpvtrRRRKAFRRRvqmvfqdpYASLHPRHT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 77 VKETLKYSARlsvpHATSQVIEERVNAVIDGLGLHSVLNNRigTPIQrgISGGQKRRVSIACSLVQFPDILFLDEPTSGL 156
Cdd:COG1124 98 VDRILAEPLR----IHGLPDREERIAELLEQVGLPPSFLDR--YPHQ--LSGGQRQRVAIARALILEPELLLLDEPTSAL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1625600662 157 DISTAHQVMTAIKRM---------AVTHNIAVVAtiHspnweiftLFDKLLLLAKGETV 206
Cdd:COG1124 170 DVSVQAEILNLLKDLreergltylFVSHDLAVVA--H--------LCDRVAVMQNGRIV 218
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
14-202 |
1.47e-24 |
|
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: 102.94 E-value: 1.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 14 ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI--------ACSSSTSFCEQEDALLGVMTVKETLKYSA 85
Cdd:cd03293 19 ALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVlvdgepvtGPGPDRGYVFQQDALLPWLTVLDNVALGL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 86 RLsVPHATSQvIEERVNAVIDGLGLHSVLNNRigtPIQrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTAHQVM 165
Cdd:cd03293 99 EL-QGVPKAE-ARERAEELLELVGLSGFENAY---PHQ--LSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQ 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1625600662 166 TAIKRMA---------VTHNIAvvatihspnwEIFTLFDKLLLLAK 202
Cdd:cd03293 172 EELLDIWretgktvllVTHDID----------EAVFLADRVVVLSA 207
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
14-203 |
1.78e-24 |
|
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: 102.61 E-value: 1.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 14 ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI-------------------ACSSSTSFCeqedallgv 74
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIrvfgkplekerkrigyvpqRRSIDRDFP--------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 75 MTVKETLKYS--ARLSVPHATSQVIEERVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLDEP 152
Cdd:cd03235 85 ISVRDVVLMGlyGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGE-----LSGGQQQRVLLARALVQDPDLLLLDEP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1625600662 153 TSGLDISTAHQVMTAIKRMAvTHNIAVVATIHSPNwEIFTLFDKLLLLAKG 203
Cdd:cd03235 160 FAGVDPKTQEDIYELLRELR-REGMTILVVTHDLG-LVLEYFDRVLLLNRT 208
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-204 |
9.40e-24 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 98.99 E-value: 9.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 4 IEWNNICYR------DILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI-------------ACSSSTSF 64
Cdd:cd03228 1 IEFKNVSFSypgrpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEIlidgvdlrdldleSLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 65 CEQEDALLGvMTVKETLkysarlsvphatsqvieervnavidglglhsvlnnrigtpiqrgISGGQKRRVSIACSLVQFP 144
Cdd:cd03228 81 VPQDPFLFS-GTIRENI--------------------------------------------LSGGQRQRIAIARALLRDP 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 145 DILFLDEPTSGLDISTAHQVMTAIKRMAVTHNIAVVAtiHSPNWEIftLFDKLLLLAKGE 204
Cdd:cd03228 116 PILILDEATSALDPETEALILEALRALAKGKTVIVIA--HRLSTIR--DADRIIVLDDGR 171
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-214 |
9.44e-24 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 106.53 E-value: 9.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 1 MSP-IEWNNICYR------DILKQISGDVKPAEILAVMGPSGSGKTTLLECISR---RKKTSSGNI-------------- 56
Cdd:COG1123 1 MTPlLEVRDLSVRypggdvPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVlldgrdllelseal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 57 -ACSSSTSFCEQEDALLGVmTVKETLKYSARLSVphATSQVIEERVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVS 135
Cdd:COG1123 81 rGRRIGMVFQDPMTQLNPV-TVGDQIAEALENLG--LSRAEARARVLELLEAVGLERRLDRYPHQ-----LSGGQRQRVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1625600662 136 IACSLVQFPDILFLDEPTSGLDISTAHQVMTAIKRMAVTHNIAVVATIHSPNwEIFTLFDKLLLLAKGETVFNSKIDQL 214
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLG-VVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-206 |
1.02e-23 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 101.73 E-value: 1.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 4 IEWNNICY----RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACS--SSTSFCEQEDA-LLGVM- 75
Cdd:COG4559 2 LEAENLSVrlggRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNgrPLAAWSPWELArRRAVLp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 76 ---------TVKE--TLKYSARLSVPHATSQVIEERVNAV-IDGLGLHSVlnnrigtpiqRGISGGQKRRVSIACSLVQ- 142
Cdd:COG4559 82 qhsslafpfTVEEvvALGRAPHGSSAAQDRQIVREALALVgLAHLAGRSY----------QTLSGGEQQRVQLARVLAQl 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1625600662 143 ------FPDILFLDEPTSGLDISTAHQVMTAIKRMAvTHNIAVVATIHSPNweIFTLF-DKLLLLAKGETV 206
Cdd:COG4559 152 wepvdgGPRWLFLDEPTSALDLAHQHAVLRLARQLA-RRGGGVVAVLHDLN--LAAQYaDRILLLHQGRLV 219
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
24-208 |
3.72e-23 |
|
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: 98.80 E-value: 3.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 24 PAEILAVMGPSGSGKTTLLECISRRKKTSSGNIA-CSSSTS-----------FCEQEDALLGVMTVKETLKYSARLS-VP 90
Cdd:cd03264 24 GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRiDGQDVLkqpqklrrrigYLPQEFGVYPNFTVREFLDYIAWLKgIP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 91 HATSqviEERVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTAHQVMTAIKR 170
Cdd:cd03264 104 SKEV---KARVDEVLELVNLGDRAKKKIGS-----LSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSE 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 1625600662 171 MAVTHnIAVVAT-IHSpnwEIFTLFDKLLLLAKGETVFN 208
Cdd:cd03264 176 LGEDR-IVILSThIVE---DVESLCNQVAVLNKGKLVFE 210
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
15-184 |
4.18e-23 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 98.98 E-value: 4.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 15 LKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSG-------NIACSS-----STSFCEQEDALLGVMTVKETLK 82
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGratvaghDVVREPrevrrRIGIVFQDLSVDDELTGWENLY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 83 YSARL-SVPhatSQVIEERVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTA 161
Cdd:cd03265 96 IHARLyGVP---GAERRERIDELLDFVGLLEAADRLVKT-----YSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTR 167
|
170 180
....*....|....*....|...
gi 1625600662 162 HQVMTAIKRMAVTHNIAVVATIH 184
Cdd:cd03265 168 AHVWEYIEKLKEEFGMTILLTTH 190
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
15-183 |
1.61e-22 |
|
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: 97.51 E-value: 1.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 15 LKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIacssstSFCEQED--------ALLGV------------ 74
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSV------LFDGEDItglppheiARLGIgrtfqiprlfpe 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 75 MTVKETLKYSARLSVPHATSQV--------IEERVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDI 146
Cdd:cd03219 90 LTVLENVMVAAQARTGSGLLLArarreereARERAEELLERVGLADLADRPAGE-----LSYGQQRRLEIARALATDPKL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1625600662 147 LFLDEPTSGLDISTAHQVMTAIKRMA--------VTHNIAVVATI 183
Cdd:cd03219 165 LLLDEPAAGLNPEETEELAELIRELRergitvllVEHDMDVVMSL 209
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-206 |
1.92e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 97.92 E-value: 1.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 4 IEWNNICY----RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACS----SSTSFCEQEdALLGVM 75
Cdd:PRK13548 3 LEARNLSVrlggRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNgrplADWSPAELA-RRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 76 TVKETLKYSarLSV---------PHATSQVIEER-VNAVIDGLGLHSvLNNRigtPIQRgISGGQKRRVSIACSLVQ--- 142
Cdd:PRK13548 82 PQHSSLSFP--FTVeevvamgraPHGLSRAEDDAlVAAALAQVDLAH-LAGR---DYPQ-LSGGEQQRVQLARVLAQlwe 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1625600662 143 ---FPDILFLDEPTSGLDISTAHQVMTAIKRMAVTHNIAVVATIHSPNweIFTLF-DKLLLLAKGETV 206
Cdd:PRK13548 155 pdgPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLN--LAARYaDRIVLLHQGRLV 220
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
12-214 |
1.97e-22 |
|
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: 97.85 E-value: 1.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 12 RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGN--------------------IACSSStsfcEQEDAL 71
Cdd:COG1119 16 KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvrlfgerrggedvwelrkrIGLVSP----ALQLRF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 72 LGVMTVKETL---KYSArLSVPHATSQVIEERVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILF 148
Cdd:COG1119 92 PRDETVLDVVlsgFFDS-IGLYREPTDEQRERARELLELLGLAHLADRPFGT-----LSQGEQRRVLIARALVKDPELLI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1625600662 149 LDEPTSGLDISTAHQVMTAIKRMAVTHNIAVVATIHSPnWEIFTLFDKLLLLAKGETVFNSKIDQL 214
Cdd:COG1119 166 LDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHV-EEIPPGITHVLLLKDGRVVAAGPKEEV 230
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
17-206 |
3.79e-22 |
|
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: 99.40 E-value: 3.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 17 QISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIAC------SSSTSFCE-----------QEDALLGVMTVKE 79
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLggevlqDSARGIFLpphrrrigyvfQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 80 TLKYSARLSvPHATSQVieeRVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLDIS 159
Cdd:COG4148 97 NLLYGRKRA-PRAERRI---SFDEVVELLGIGHLLDRRPAT-----LSGGERQRVAIGRALLSSPRLLLMDEPLAALDLA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1625600662 160 TAHQVMTAIKRMAVTHNIAVVATIHSPNwEIFTLFDKLLLLAKGETV 206
Cdd:COG4148 168 RKAEILPYLERLRDELDIPILYVSHSLD-EVARLADHVVLLEQGRVV 213
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
12-206 |
6.62e-22 |
|
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: 95.02 E-value: 6.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 12 RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI----------ACSSSTSFCEQE-DALLGVMTVKET 80
Cdd:cd03226 13 TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSIllngkpikakERRKSIGYVMQDvDYQLFTDSVREE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 81 LKYSARLsvPHATSQVIEErvnaVIDGLGLHSvLNNRigTPiqRGISGGQKRRVSIACSLVQFPDILFLDEPTSGLDIST 160
Cdd:cd03226 93 LLLGLKE--LDAGNEQAET----VLKDLDLYA-LKER--HP--LSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKN 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1625600662 161 AHQVMTAIKRMAVTHNIAVVATiHSPNWeIFTLFDKLLLLAKGETV 206
Cdd:cd03226 162 MERVGELIRELAAQGKAVIVIT-HDYEF-LAKVCDRVLLLANGAIV 205
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
4-206 |
1.27e-21 |
|
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: 94.99 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 4 IEWNNICY-----RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACS-------SSTSFCEQedal 71
Cdd:cd03253 1 IEFENVTFaydpgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDgqdirevTLDSLRRA---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 72 LGVM---TV--KETLKYSARLSVPHATS-QVIEERVNAVIDG--LGLHSVLNNRIGtpiQRG--ISGGQKRRVSIACSLV 141
Cdd:cd03253 77 IGVVpqdTVlfNDTIGYNIRYGRPDATDeEVIEAAKAAQIHDkiMRFPDGYDTIVG---ERGlkLSGGEKQRVAIARAIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1625600662 142 QFPDILFLDEPTSGLDISTAHQVMTAIKRMA-------VTHNIAVVATIhspnweiftlfDKLLLLAKGETV 206
Cdd:cd03253 154 KNPPILLLDEATSALDTHTEREIQAALRDVSkgrttivIAHRLSTIVNA-----------DKIIVLKDGRIV 214
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
14-178 |
1.62e-21 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 94.13 E-value: 1.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 14 ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIA---------------CSSSTSFCEQEDALLGVMTVK 78
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIidglkltddkknineLRQKVGMVFQQFNLFPHLTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 79 ETLKYsARLSVPHATSQVIEERVNAVIDGLGLHSVLNNRigtPIQrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLDI 158
Cdd:cd03262 95 ENITL-APIKVKGMSKAEAEERALELLEKVGLADKADAY---PAQ--LSGGQQQRVAIARALAMNPKVMLFDEPTSALDP 168
|
170 180
....*....|....*....|....*...
gi 1625600662 159 STAHQVMTAIKRMA--------VTHNIA 178
Cdd:cd03262 169 ELVGEVLDVMKDLAeegmtmvvVTHEMG 196
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
15-231 |
1.85e-21 |
|
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: 94.57 E-value: 1.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 15 LKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACS----SSTSFCEQEDA------------LLGVMTVK 78
Cdd:cd03258 21 LKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDgtdlTLLSGKELRKArrrigmifqhfnLLSSRTVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 79 ETLKYSarLSVPHATSQVIEERVNAVIDGLGLHSVLNNRigtPIQrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLDI 158
Cdd:cd03258 101 ENVALP--LEIAGVPKAEIEERVLELLELVGLEDKADAY---PAQ--LSGGQKQRVGIARALANNPKVLLCDEATSALDP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 159 STAHQVMTAIKRM---------AVTHNIAVVATIhspnweiftlFDKLLLLAKGETVfnskidqlvpyfeELGYNFPKFS 229
Cdd:cd03258 174 ETTQSILALLRDInrelgltivLITHEMEVVKRI----------CDRVAVMEKGEVV-------------EEGTVEEVFA 230
|
..
gi 1625600662 230 NP 231
Cdd:cd03258 231 NP 232
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
15-207 |
2.94e-21 |
|
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: 93.59 E-value: 2.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 15 LKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI------------ACSSSTSFCEQEDALLGVMTVKETLK 82
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFAtvdgfdvvkepaEARRRLGFVSDSTGLYDRLTARENLE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 83 YSARLsvpHATS-QVIEERVNAVIDGLGLHSVLNNRIGtpiqrGISGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTA 161
Cdd:cd03266 101 YFAGL---YGLKgDELTARLEELADRLGMEELLDRRVG-----GFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMAT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1625600662 162 HQVMTAIKRM-AVTHNIAVVATIHSpnwEIFTLFDKLLLLAKGETVF 207
Cdd:cd03266 173 RALREFIRQLrALGKCILFSTHIMQ---EVERLCDRVVVLHRGRVVY 216
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-181 |
4.08e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 92.30 E-value: 4.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 12 RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI--ACSSSTSFCEQEDALLGVM--TVKETLKYS--A 85
Cdd:NF040873 5 RPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVrrAGGARVAYVPQRSEVPDSLplTVRDLVAMGrwA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 86 RLSVPHATSQVIEERVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTAHQVM 165
Cdd:NF040873 85 RRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGE-----LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERII 159
|
170 180
....*....|....*....|....
gi 1625600662 166 TAIKR--------MAVTHNIAVVA 181
Cdd:NF040873 160 ALLAEehargatvVVVTHDLELVR 183
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-206 |
6.88e-21 |
|
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: 92.68 E-value: 6.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 4 IEWNNICYR------DILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIaCSSSTSFCE----------- 66
Cdd:cd03251 1 VEFKNVTFRypgdgpPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRI-LIDGHDVRDytlaslrrqig 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 67 --QEDALLGVMTVKETLKYSArlsvPHATSQVIEERVNAV-----IDGL--GLHSVlnnrIGtpiQRGI--SGGQKRRVS 135
Cdd:cd03251 80 lvSQDVFLFNDTVAENIAYGR----PGATREEVEEAARAAnahefIMELpeGYDTV----IG---ERGVklSGGQRQRIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1625600662 136 IACSLVQFPDILFLDEPTSGLDISTAHQVMTAIKRMAVTHNIAVVA----TIHSPnweiftlfDKLLLLAKGETV 206
Cdd:cd03251 149 IARALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAhrlsTIENA--------DRIVVLEDGKIV 215
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
12-157 |
9.02e-21 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 91.51 E-value: 9.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 12 RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSSTSFCEQED-----------ALLGVMTVKET 80
Cdd:cd03268 13 KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAlrrigalieapGFYPNLTAREN 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1625600662 81 LKYSARLSvphatsQVIEERVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLD 157
Cdd:cd03268 93 LRLLARLL------GIRKKRIDEVLDVVGLKDSAKKKVKG-----FSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
26-223 |
1.26e-20 |
|
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: 94.79 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 26 EILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSST-----------------SFCEQEDALLGVMTVKETLKYSARLS 88
Cdd:TIGR02142 24 GVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTlfdsrkgiflppekrriGYVFQEARLFPHLSVRGNLRYGMKRA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 89 VPhATSQVIEERVnavIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTAHQVMTAI 168
Cdd:TIGR02142 104 RP-SERRISFERV---IELLGIGHLLGRLPGR-----LSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1625600662 169 KRMAVTHNIAVVATIHSPNwEIFTLFDKLLLLAKGETVFNSKIDQL-----VPY--FEELGY 223
Cdd:TIGR02142 175 ERLHAEFGIPILYVSHSLQ-EVLRLADRVVVLEDGRVAAAGPIAEVwaspdLPWlaREDQGS 235
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
14-179 |
1.30e-20 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 92.46 E-value: 1.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 14 ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIAC--------SSSTSFCEQEDALLGVMTVKETLKYSA 85
Cdd:COG1116 26 ALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVdgkpvtgpGPDRGVVFQEPALLPWLTVLDNVALGL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 86 RLSvpHATSQVIEERVNAVIDGLGLHSVLNNRigtPIQrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTAHQVM 165
Cdd:COG1116 106 ELR--GVPKAERRERARELLELVGLAGFEDAY---PHQ--LSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQ 178
|
170 180
....*....|....*....|....*
gi 1625600662 166 TAIKRMA---------VTHNI--AV 179
Cdd:COG1116 179 DELLRLWqetgktvlfVTHDVdeAV 203
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
14-180 |
2.34e-20 |
|
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: 90.22 E-value: 2.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 14 ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSSTSFCEQEDALLGvMTVKETLKYSARLSvphat 93
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQN-GTIRENILFGKPFD----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 94 sqviEERVNAVIDGLGLH---SVLNNRIGTPI-QRGI--SGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTAHQVMT- 166
Cdd:cd03250 94 ----EERYEKVIKACALEpdlEILPDGDLTEIgEKGInlSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEn 169
|
170 180
....*....|....*....|..
gi 1625600662 167 AIK--------RMAVTHNIAVV 180
Cdd:cd03250 170 CILglllnnktRILVTHQLQLL 191
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-200 |
2.48e-20 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 96.20 E-value: 2.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 2 SPIEWNNICYRD-----ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSSTSFCEQEDALLGVMT 76
Cdd:TIGR02857 320 SSLEFSGVSVAYpgrrpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 77 --------VKETLKYSARLSVPHATSQVIEERVNAVidglGLHSVLNNR---IGTPIQ---RGISGGQKRRVSIACSLVQ 142
Cdd:TIGR02857 400 wvpqhpflFAGTIAENIRLARPDASDAEIREALERA----GLDEFVAALpqgLDTPIGeggAGLSGGQAQRLALARAFLR 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1625600662 143 FPDILFLDEPTSGLDISTAHQVMTAIKRMAVTHNIAVVAtiHSPNWeiFTLFDKLLLL 200
Cdd:TIGR02857 476 DAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVT--HRLAL--AALADRIVVL 529
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
15-206 |
2.83e-20 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 92.84 E-value: 2.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 15 LKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSS------------STSFCEQEDALLGVMTVKETLK 82
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGydvvreprkvrrSIGIVPQYASVDEDLTGRENLE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 83 YSARL-SVPHAtsqVIEERVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTA 161
Cdd:TIGR01188 89 MMGRLyGLPKD---EAEERAEELLELFELGEAADRPVGT-----YSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1625600662 162 HQVMTAIKRMaVTHNIAVVATIHSPNwEIFTLFDKLLLLAKGETV 206
Cdd:TIGR01188 161 RAIWDYIRAL-KEEGVTILLTTHYME-EADKLCDRIAIIDHGRII 203
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
14-203 |
3.30e-20 |
|
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: 90.01 E-value: 3.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 14 ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI-----------ACSSSTSFCEQEDALLGVMTVKETLK 82
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIyiggrdvtdlpPKDRDIAMVFQNYALYPHMTVYDNIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 83 YSarLSVPHATSQVIEERVNAVIDGLGLHSVLNNRigtPIQrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTAH 162
Cdd:cd03301 95 FG--LKLRKVPKDEIDERVREVAELLQIEHLLDRK---PKQ--LSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRV 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1625600662 163 QVMTAIKRMAVTHNIAVVATIHSPNwEIFTLFDKLLLLAKG 203
Cdd:cd03301 168 QMRAELKRLQQRLGTTTIYVTHDQV-EAMTMADRIAVMNDG 207
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
12-186 |
8.05e-20 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 89.34 E-value: 8.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 12 RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIacssstSFCEQE------DAL------LGV----- 74
Cdd:COG2884 15 REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQV------LVNGQDlsrlkrREIpylrrrIGVvfqdf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 75 -----MTVKETLKYSarLSVPHATSQVIEERVNAVIDGLGLHSVLNNRigtPIQrgISGGQKRRVSIACSLVQFPDILFL 149
Cdd:COG2884 89 rllpdRTVYENVALP--LRVTGKSRKEIRRRVREVLDLVGLSDKAKAL---PHE--LSGGEQQRVAIARALVNRPELLLA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1625600662 150 DEPTSGLDISTAHQVMTAIKR---------MAvTHNIAVVATIHSP 186
Cdd:COG2884 162 DEPTGNLDPETSWEIMELLEEinrrgttvlIA-THDLELVDRMPKR 206
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
14-186 |
8.92e-20 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 94.35 E-value: 8.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 14 ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI------ACSSST-------SFCEQeDALLGVMTVKET 80
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVtldgvpVSSLDQdevrrrvSVCAQ-DAHLFDTTVREN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 81 LkysaRLSVPHATsqviEERVNAVIDGLGLHSVLNNR---IGTPIQRG---ISGGQKRRVSIACSLVQFPDILFLDEPTS 154
Cdd:TIGR02868 429 L----RLARPDAT----DEELWAALERVGLADWLRALpdgLDTVLGEGgarLSGGERQRLALARALLADAPILLLDEPTE 500
|
170 180 190
....*....|....*....|....*....|..
gi 1625600662 155 GLDISTAHQVMTAIkrMAVTHNIAVVATIHSP 186
Cdd:TIGR02868 501 HLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
12-215 |
3.44e-19 |
|
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: 87.60 E-value: 3.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 12 RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIA---CSSST-----------SFCEQEDALLGVMTV 77
Cdd:cd03218 13 RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILldgQDITKlpmhkrarlgiGYLPQEASIFRKLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 78 KETLkySARLSVPHATSQVIEERVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLD 157
Cdd:cd03218 93 EENI--LAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASS-----LSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1625600662 158 ISTAHQVMTAIKRMAvTHNIAVVATIHSPNwEIFTLFDKLLLLAKGETVFNSKIDQLV 215
Cdd:cd03218 166 PIAVQDIQKIIKILK-DRGIGVLITDHNVR-ETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
13-182 |
4.14e-19 |
|
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: 86.32 E-value: 4.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 13 DILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSS-----------------TSFCEQEDALLGVm 75
Cdd:TIGR01166 6 EVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEpldysrkgllerrqrvgLVFQDPDDQLFAA- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 76 TVKETLKYSAR-LSVPHATsqvIEERVNAVIDGLGLhSVLNNRigtPIQRgISGGQKRRVSIACSLVQFPDILFLDEPTS 154
Cdd:TIGR01166 85 DVDQDVAFGPLnLGLSEAE---VERRVREALTAVGA-SGLRER---PTHC-LSGGEKKRVAIAGAVAMRPDVLLLDEPTA 156
|
170 180
....*....|....*....|....*...
gi 1625600662 155 GLDISTAHQVMTAIKRMAVTHNIAVVAT 182
Cdd:TIGR01166 157 GLDPAGREQMLAILRRLRAEGMTVVIST 184
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
14-214 |
4.21e-19 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 87.10 E-value: 4.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 14 ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIA--------------CSSSTSFCEQEDALLGVMTVKE 79
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRfdgrditglppherARAGIGYVPEGRRIFPELTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 80 TLKYSARLSVPHATSQVIEE------RvnavidglgLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLDEPT 153
Cdd:cd03224 95 NLLLGAYARRRAKRKARLERvyelfpR---------LKERRKQLAGT-----LSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1625600662 154 SGLDISTAHQVMTAIKRMA--------VTHNIAVVATIHspnweiftlfDKLLLLAKGETVFNSKIDQL 214
Cdd:cd03224 161 EGLAPKIVEEIFEAIRELRdegvtillVEQNARFALEIA----------DRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
15-182 |
4.73e-19 |
|
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: 87.08 E-value: 4.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 15 LKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSS----------------STSFCEQEDALLGVMTVK 78
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqdvsdlrgraipylrrKIGVVFQDFRLLPDRNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 79 ETLKYSARLS-VPHatsQVIEERVNAVIDGLGLHSVLNNrigtpIQRGISGGQKRRVSIACSLVQFPDILFLDEPTSGLD 157
Cdd:cd03292 97 ENVAFALEVTgVPP---REIRKRVPAALELVGLSHKHRA-----LPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLD 168
|
170 180
....*....|....*....|....*
gi 1625600662 158 ISTAHQVMTAIKRMAVTHNIAVVAT 182
Cdd:cd03292 169 PDTTWEIMNLLKKINKAGTTVVVAT 193
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
14-204 |
5.78e-19 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 89.77 E-value: 5.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 14 ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSS-------------STSFceQEDALLGVMTVKET 80
Cdd:COG3842 20 ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGrdvtglppekrnvGMVF--QDYALFPHLTVAEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 81 LKYSarLSVPHATSQVIEERVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLDIST 160
Cdd:COG3842 98 VAFG--LRMRGVPKAEIRARVAELLELVGLEGLADRYPHQ-----LSGGQQQRVALARALAPEPRVLLLDEPLSALDAKL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1625600662 161 AHQVMTAIKRMAVTHNI-AVVATiHSPNwEIFTLFDKLLLLAKGE 204
Cdd:COG3842 171 REEMREELRRLQRELGItFIYVT-HDQE-EALALADRIAVMNDGR 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
14-227 |
6.40e-19 |
|
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: 86.91 E-value: 6.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 14 ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACS-------------SSTSFceQEDALLGVMTVKET 80
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDgkditnlpphkrpVNTVF--QNYALFPHLTVFEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 81 LKYSARLS-VPHATsqvIEERVNAVIDGLGLHSVLNNRIgtpiqRGISGGQKRRVSIACSLVQFPDILFLDEPTSGLDIS 159
Cdd:cd03300 93 IAFGLRLKkLPKAE---IKERVAEALDLVQLEGYANRKP-----SQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1625600662 160 TAHQVMTAIKRMAVTHNIAVVATIHSPNwEIFTLFDKLLLLAKGetvfnsKIDQL-VPyfEELgYNFPK 227
Cdd:cd03300 165 LRKDMQLELKRLQKELGITFVFVTHDQE-EALTMSDRIAVMNKG------KIQQIgTP--EEI-YEEPA 223
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-206 |
8.47e-19 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 91.38 E-value: 8.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 4 IEWNNICY-----RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI-------------ACSSSTSFC 65
Cdd:COG1132 340 IEFENVSFsypgdRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIlidgvdirdltleSLRRQIGVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 66 EQEDALLGvMTVKETLKYSArlsvPHATSQVIEE---RVNA--VIDGL--GLHSVLNnrigtpiQRGI--SGGQKRRVSI 136
Cdd:COG1132 420 PQDTFLFS-GTIRENIRYGR----PDATDEEVEEaakAAQAheFIEALpdGYDTVVG-------ERGVnlSGGQRQRIAI 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1625600662 137 ACSLVQFPDILFLDEPTSGLDISTAHQVMTAIKRM-------AVTHNIavvATIHSpnweiftlFDKLLLLAKGETV 206
Cdd:COG1132 488 ARALLKDPPILILDEATSALDTETEALIQEALERLmkgrttiVIAHRL---STIRN--------ADRILVLDDGRIV 553
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-204 |
9.85e-19 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 84.58 E-value: 9.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 4 IEWNNICYR------DILKQISGDVKPAEILAVMGPSGSGKTTLLECIsrrkktssgniacssstsfceqedalLGVMTV 77
Cdd:cd03246 1 LEVENVSFRypgaepPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLI--------------------------LGLLRP 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 78 ketlkysarlsvphaTSQVIeervnaVIDGLGLHSV----LNNRIGTPIQRGI-----------SGGQKRRVSIACSLVQ 142
Cdd:cd03246 55 ---------------TSGRV------RLDGADISQWdpneLGDHVGYLPQDDElfsgsiaenilSGGQRQRLGLARALYG 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1625600662 143 FPDILFLDEPTSGLDISTAHQVMTAIKRMAVTHNIAVVATiHSPnwEIFTLFDKLLLLAKGE 204
Cdd:cd03246 114 NPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIA-HRP--ETLASADRILVLEDGR 172
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
15-157 |
1.36e-18 |
|
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: 86.93 E-value: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 15 LKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSG-------NIACSSSTSFCE----------QEDALLGVMTV 77
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGkvlidgqDIAAMSRKELRElrrkkismvfQSFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 78 KETLKYSarLSVPHATSQVIEERVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLD 157
Cdd:cd03294 120 LENVAFG--LEVQGVPRAEREERAAEALELVGLEGWEHKYPDE-----LSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
4-206 |
1.50e-18 |
|
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: 85.72 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 4 IEWNNICY------RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI-------------ACSSSTSF 64
Cdd:cd03245 3 IEFRNVSFsypnqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVlldgtdirqldpaDLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 65 CEQEdallgVMTVKETLKYSARLSVPHATsqviEERVNAVIDGLGLHSVLNNR---IGTPIQ---RGISGGQKRRVSIAC 138
Cdd:cd03245 83 VPQD-----VTLFYGTLRDNITLGAPLAD----DERILRAAELAGVTDFVNKHpngLDLQIGergRGLSGGQRQAVALAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1625600662 139 SLVQFPDILFLDEPTSGLDISTAHQVMTAIKRMAVtHNIAVVATiHSPNweIFTLFDKLLLLAKGETV 206
Cdd:cd03245 154 ALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG-DKTLIIIT-HRPS--LLDLVDRIIVMDSGRIV 217
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
10-186 |
1.87e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 84.93 E-value: 1.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 10 CYRD---ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIA----------CSSSTSFCEQEDALLGVMT 76
Cdd:PRK13539 10 CVRGgrvLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKldggdiddpdVAEACHYLGHRNAMKPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 77 VKETLKYSARLsvpHATSqviEERVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLDEPTSGL 156
Cdd:PRK13539 90 VAENLEFWAAF---LGGE---ELDIAAALEAVGLAPLAHLPFGY-----LSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170 180 190
....*....|....*....|....*....|
gi 1625600662 157 DISTAHQVMTAIKRMAVTHNIAVVATiHSP 186
Cdd:PRK13539 159 DAAAVALFAELIRAHLAQGGIVIAAT-HIP 187
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-178 |
2.03e-18 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 85.91 E-value: 2.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 4 IEWNNICYR----DILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI------ACSSSTSFCE------- 66
Cdd:PRK09493 2 IEFKNVSKHfgptQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLivdglkVNDPKVDERLirqeagm 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 67 --QEDALLGVMTVKETLKYSARlSVPHATSQVIEERVNAVIDGLGLHSVLNNrigTPIQrgISGGQKRRVSIACSLVQFP 144
Cdd:PRK09493 82 vfQQFYLFPHLTALENVMFGPL-RVRGASKEEAEKQARELLAKVGLAERAHH---YPSE--LSGGQQQRVAIARALAVKP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1625600662 145 DILFLDEPTSGLDISTAHQVMTAIKRMA--------VTHNIA 178
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQDLAeegmtmviVTHEIG 197
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-170 |
2.67e-18 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 87.83 E-value: 2.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 1 MSpIEWNNIC----YRDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI-----------ACSSSTSFC 65
Cdd:PRK10851 1 MS-IEIANIKksfgRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIrfhgtdvsrlhARDRKVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 66 EQEDALLGVMTVKETLKYSarLSV----PHATSQVIEERVNAVIDGLGLhSVLNNRIgtPIQrgISGGQKRRVSIACSLV 141
Cdd:PRK10851 80 FQHYALFRHMTVFDNIAFG--LTVlprrERPNAAAIKAKVTQLLEMVQL-AHLADRY--PAQ--LSGGQKQRVALARALA 152
|
170 180
....*....|....*....|....*....
gi 1625600662 142 QFPDILFLDEPTSGLDIstahQVMTAIKR 170
Cdd:PRK10851 153 VEPQILLLDEPFGALDA----QVRKELRR 177
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
11-209 |
3.61e-18 |
|
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: 85.08 E-value: 3.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 11 YRDI--LKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSSTSFcEQEDALLG----VMTVKETLKY- 83
Cdd:cd03267 31 YREVeaLKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPW-KRRKKFLRrigvVFGQKTQLWWd 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 84 -SAR--LSVPHATSQV----IEERVNAVIDGLGLHSVLNnrigTPIqRGISGGQKRRVSIACSLVQFPDILFLDEPTSGL 156
Cdd:cd03267 110 lPVIdsFYLLAAIYDLpparFKKRLDELSELLDLEELLD----TPV-RQLSLGQRMRAEIAAALLHEPEILFLDEPTIGL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1625600662 157 DISTAHQVMTAIKRMAVTHNIAVVATIHSPNwEIFTLFDKLLLLAKGETVFNS 209
Cdd:cd03267 185 DVVAQENIRNFLKEYNRERGTTVLLTSHYMK-DIEALARRVLVIDKGRLLYDG 236
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-175 |
5.54e-18 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 86.67 E-value: 5.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 1 MSPIEWNNICYR----DILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSG-----------------NIAcs 59
Cdd:COG3839 1 MASLELENVSKSyggvEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGeiliggrdvtdlppkdrNIA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 60 ssTSFceQEDALLGVMTVKETLKYSARLS-VPHATsqvIEERVNAVIDGLGLHSVLNNRigtPiqRGISGGQKRRVSIAC 138
Cdd:COG3839 79 --MVF--QSYALYPHMTVYENIAFPLKLRkVPKAE---IDRRVREAAELLGLEDLLDRK---P--KQLSGGQRQRVALGR 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1625600662 139 SLVQFPDILFLDEPTSGLDISTAHQVMTAIKRMA---------VTH 175
Cdd:COG3839 147 ALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHrrlgtttiyVTH 192
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-214 |
7.28e-18 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 84.04 E-value: 7.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 4 IEWNNICYR--DILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSS-------------STSFceQE 68
Cdd:COG3840 2 LRLDDLTYRygDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGqdltalppaerpvSMLF--QE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 69 DALLGVMTVKE--------TLKYSA--RLSVPHATSQVieervnavidglGLHSVLNNRIGTpiqrgISGGQKRRVSIAC 138
Cdd:COG3840 80 NNLFPHLTVAQniglglrpGLKLTAeqRAQVEQALERV------------GLAGLLDRLPGQ-----LSGGQRQRVALAR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1625600662 139 SLVQFPDILFLDEPTSGLDISTAHQVMTAIKRMAVTHNIAVVATIHSPNwEIFTLFDKLLLLAKGETVFNSKIDQL 214
Cdd:COG3840 143 CLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPE-DAARIADRVLLVADGRIAADGPTAAL 217
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-204 |
8.65e-18 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 84.03 E-value: 8.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 1 MSPIEWNNICYR----DILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSS-----GNIACSSSTSFCEQEdAL 71
Cdd:PRK11264 1 MSAIEVKNLVKKfhgqTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAgtirvGDITIDTARSLSQQK-GL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 72 LGVMTVKETLKYSARLSVPHATS--QVIEERVnaVIDG------LGLHSVLNNRIG-----TPIQRGISGGQKRRVSIAC 138
Cdd:PRK11264 80 IRQLRQHVGFVFQNFNLFPHRTVleNIIEGPV--IVKGepkeeaTARARELLAKVGlagkeTSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1625600662 139 SLVQFPDILFLDEPTSGLDISTAHQVMTAIKRMA--------VTHNIAVVATIhsPNWEIFtlFDKLLLLAKGE 204
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAqekrtmviVTHEMSFARDV--ADRAIF--MDQGRIVEQGP 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-160 |
9.16e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.81 E-value: 9.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 7 NNICY----RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSST--SFCEQEDALLGVMTVKET 80
Cdd:COG0488 2 ENLSKsfggRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLriGYLPQEPPLDDDLTVLDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 81 L---------------KYSARLSVPHATSQVIEE---------------RVNAVIDGLGLHSV-LNNRIGTpiqrgISGG 129
Cdd:COG0488 82 VldgdaelraleaeleELEAKLAEPDEDLERLAElqeefealggweaeaRAEEILSGLGFPEEdLDRPVSE-----LSGG 156
|
170 180 190
....*....|....*....|....*....|.
gi 1625600662 130 QKRRVSIACSLVQFPDILFLDEPTSGLDIST 160
Cdd:COG0488 157 WRRRVALARALLSEPDLLLLDEPTNHLDLES 187
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
15-183 |
9.86e-18 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 85.90 E-value: 9.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 15 LKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI--------ACSSS----------TSFceQEDALLGVMT 76
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVlvdgvdltALSERelraarrkigMIF--QHFNLLSSRT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 77 VKETLKYSARLS-VPHATsqvIEERVNAVIDGLGLHSVLNNRigtPIQrgISGGQKRRVSIACSLVQFPDILFLDEPTSG 155
Cdd:COG1135 99 VAENVALPLEIAgVPKAE---IRKRVAELLELVGLSDKADAY---PSQ--LSGGQKQRVGIARALANNPKVLLCDEATSA 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 1625600662 156 LDISTAHQVMTAIKR---------MAVTHNIAVVATI 183
Cdd:COG1135 171 LDPETTRSILDLLKDinrelgltiVLITHEMDVVRRI 207
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
14-175 |
1.05e-17 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 83.50 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 14 ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIacssstSFCEQEdallgvMTVKETLKYSARLSV---- 89
Cdd:COG1126 16 VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTI------TVDGED------LTDSKKDINKLRRKVgmvf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 90 ------PHATsqVIEervNaVIdgLGLHSVLN--------------NRIGT-------PIQrgISGGQKRRVSIACSLVQ 142
Cdd:COG1126 84 qqfnlfPHLT--VLE---N-VT--LAPIKVKKmskaeaeeramellERVGLadkadayPAQ--LSGGQQQRVAIARALAM 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1625600662 143 FPDILFLDEPTSGLDISTAHQVMTAIKRMA--------VTH 175
Cdd:COG1126 154 EPKVMLFDEPTSALDPELVGEVLDVMRDLAkegmtmvvVTH 194
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
14-207 |
1.36e-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: 81.59 E-value: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 14 ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSstsfceqedallgvmtvKETLKYSARLSvpHAT 93
Cdd:cd03247 17 VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDG-----------------VPVSDLEKALS--SLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 94 SqVIEERVNaVIDGlglhSVLNNrIGTPIqrgiSGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTAHQVMTAIKRMA- 172
Cdd:cd03247 78 S-VLNQRPY-LFDT----TLRNN-LGRRF----SGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLk 146
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1625600662 173 ------VTHNIAVVATihspnweiftlFDKLLLLAKGETVF 207
Cdd:cd03247 147 dktliwITHHLTGIEH-----------MDKILFLENGKIIM 176
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
30-206 |
1.37e-17 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 85.24 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 30 VMGPSGSGKTTLLECISRRKKTSSGNIACSS-------------STSFceQEDALLGVMTVKETLKYSARL-SVPHATsq 95
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGedvtnvpphlrhiNMVF--QSYALFPHMTVEENVAFGLKMrKVPRAE-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 96 vIEERVNAVIDGLGLHSVLNNRigtPIQrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTAHQVMTAIKRMAVTH 175
Cdd:TIGR01187 77 -IKPRVLEALRLVQLEEFADRK---PHQ--LSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQL 150
|
170 180 190
....*....|....*....|....*....|.
gi 1625600662 176 NIAVVATIHSPNwEIFTLFDKLLLLAKGETV 206
Cdd:TIGR01187 151 GITFVFVTHDQE-EAMTMSDRIAIMRKGKIA 180
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
11-215 |
1.83e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 84.75 E-value: 1.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 11 YRDI--LKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSSTSFcEQEDALL---GV----------- 74
Cdd:COG4586 32 YREVeaVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPF-KRRKEFArriGVvfgqrsqlwwd 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 75 MTVKETLKYSARL-SVPHAtsqVIEERVNAVIDGLGLHSVLNnrigTPIqRGISGGQKRRVSIACSLVQFPDILFLDEPT 153
Cdd:COG4586 111 LPAIDSFRLLKAIyRIPDA---EYKKRLDELVELLDLGELLD----TPV-RQLSLGQRMRCELAAALLHRPKILFLDEPT 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1625600662 154 SGLDISTAHQVMTAIKRMAVTHNIAVVATIHSPNwEIFTLFDKLLLLAKGETVFNSKIDQLV 215
Cdd:COG4586 183 IGLDVVSKEAIREFLKEYNRERGTTILLTSHDMD-DIEALCDRVIVIDHGRIIYDGSLEELK 243
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
14-206 |
4.14e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 82.37 E-value: 4.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 14 ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGN-------IACSSSTSFCEQEdALL--------GVmTVK 78
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTvflgdkpISMLSSRQLARRL-ALLpqhhltpeGI-TVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 79 ETLKY--SARLSVPHATSQVIEERVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLDEPTSGL 156
Cdd:PRK11231 95 ELVAYgrSPWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTD-----LSGGQRQRAFLAMVLAQDTPVVLLDEPTTYL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1625600662 157 DIStaHQV--MTAIKRMAvTHNIAVVATIHSPNwEIFTLFDKLLLLAKGETV 206
Cdd:PRK11231 170 DIN--HQVelMRLMRELN-TQGKTVVTVLHDLN-QASRYCDHLVVLANGHVM 217
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
13-182 |
4.95e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 82.32 E-value: 4.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 13 DILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSST-SFCEQEDALLGVMTVKETLKYSARLSV-- 89
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTiNLVRDKDGQLKVADKNQLRLLRTRLTMvf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 90 ------PHATsqVIEERVNAVIDGLGLHSVLN--------NRIG-TPIQRG-----ISGGQKRRVSIACSLVQFPDILFL 149
Cdd:PRK10619 99 qhfnlwSHMT--VLENVMEAPIQVLGLSKQEAreravkylAKVGiDERAQGkypvhLSGGQQQRVSIARALAMEPEVLLF 176
|
170 180 190
....*....|....*....|....*....|...
gi 1625600662 150 DEPTSGLDISTAHQVMTAIKRMAVTHNIAVVAT 182
Cdd:PRK10619 177 DEPTSALDPELVGEVLRIMQQLAEEGKTMVVVT 209
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-176 |
5.11e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 85.65 E-value: 5.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 4 IEWNNICYR------DILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACS--SSTSFCEQedALLGVM 75
Cdd:PRK11160 339 LTLNNVSFTypdqpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNgqPIADYSEA--ALRQAI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 76 TV--------KETLKYSARLSVPHATsqviEERVNAVIDGLGLHSVLNNRIGTPI-----QRGISGGQKRRVSIACSLVQ 142
Cdd:PRK11160 417 SVvsqrvhlfSATLRDNLLLAAPNAS----DEALIEVLQQVGLEKLLEDDKGLNAwlgegGRQLSGGEQRRLGIARALLH 492
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1625600662 143 FPDILFLDEPTSGLDISTAHQVMTAIKRMA-------VTHN 176
Cdd:PRK11160 493 DAPLLLLDEPTEGLDAETERQILELLAEHAqnktvlmITHR 533
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
14-206 |
6.34e-17 |
|
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: 80.40 E-value: 6.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 14 ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI---------ACSSSTSFCEQEDALLGVMTVKETLKYS 84
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVlfdgkpldiAARNRIGYLPEERGLYPKMKVIDQLVYL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 85 ARL-SVPHatsQVIEERVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTAHQ 163
Cdd:cd03269 95 AQLkGLKK---EEARRRIDEWLERLELSEYANKRVEE-----LSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVEL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1625600662 164 VMTAIKRMA--------VTHNIAVVAtihspnweifTLFDKLLLLAKGETV 206
Cdd:cd03269 167 LKDVIRELAragktvilSTHQMELVE----------ELCDRVLLLNKGRAV 207
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
18-183 |
2.65e-16 |
|
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: 81.25 E-value: 2.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 18 ISGDVKPAEILAVMGPSGSGKTTLLECISR---RKKTSSGNIacssstSFCEQEdaLLG--------------------- 73
Cdd:COG0444 24 VSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEI------LFDGED--LLKlsekelrkirgreiqmifqdp 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 74 ------VMTVK----ETLKYSARLSVPHATSQVIE--ERVnavidglGLH---SVLNNRigtPIQrgISGGQKRRVSIAC 138
Cdd:COG0444 96 mtslnpVMTVGdqiaEPLRIHGGLSKAEARERAIEllERV-------GLPdpeRRLDRY---PHE--LSGGMRQRVMIAR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1625600662 139 SLVQFPDILFLDEPTSGLDISTAHQVMTAIKR------MAV---THNIAVVATI 183
Cdd:COG0444 164 ALALEPKLLIADEPTTALDVTIQAQILNLLKDlqrelgLAIlfiTHDLGVVAEI 217
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-184 |
2.69e-16 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 79.74 E-value: 2.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 4 IEWNNICYR----DILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIacssstsfceqedaLLGVMTVKE 79
Cdd:COG4604 2 IEIKNVSKRyggkVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEV--------------LVDGLDVAT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 80 T-----------LKYS----ARLSV---------PHA----TSQViEERVNAVIDGLGLHSVLNNRIGTpiqrgISGGQK 131
Cdd:COG4604 68 TpsrelakrlaiLRQEnhinSRLTVrelvafgrfPYSkgrlTAED-REIIDEAIAYLDLEDLADRYLDE-----LSGGQR 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1625600662 132 RRVSIACSLVQFPDILFLDEPTSGLDISTAHQVMTAIKRMAVTHNIAVVATIH 184
Cdd:COG4604 142 QRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLH 194
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
11-205 |
3.72e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 82.93 E-value: 3.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 11 YRDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIAcssstsFCEQEDAL---------LGvmTVKETL 81
Cdd:COG4178 375 GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA------RPAGARVLflpqrpylpLG--TLREAL 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 82 KYsarlsvPHATSQVIEERVNAVIDGLGLHSvLNNRIGT--PIQRGISGGQKRRVSIACSLVQFPDILFLDEPTSGLDIS 159
Cdd:COG4178 447 LY------PATAEAFSDAELREALEAVGLGH-LAERLDEeaDWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEE 519
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1625600662 160 TAHQVMTAIKRMavTHNIAVVATIHSPnwEIFTLFDKLLLLAKGET 205
Cdd:COG4178 520 NEAALYQLLREE--LPGTTVISVGHRS--TLAAFHDRVLELTGDGS 561
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-213 |
3.92e-16 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 78.92 E-value: 3.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 1 MSpIEWNNICYR----DILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIAC----SSSTS-------FC 65
Cdd:cd03296 1 MS-IEVRNVSKRfgdfVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFggedATDVPvqernvgFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 66 EQEDALLGVMTVKET----LKYSARLSVPHATSqvIEERVNAVIDGLGLhSVLNNRIgtPIQrgISGGQKRRVSIACSLV 141
Cdd:cd03296 80 FQHYALFRHMTVFDNvafgLRVKPRSERPPEAE--IRAKVHELLKLVQL-DWLADRY--PAQ--LSGGQRQRVALARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1625600662 142 QFPDILFLDEPTSGLDISTAHQVMTAIKRMAVTHNIAVVATIHSPNwEIFTLFDKLLLLAKGetvfnsKIDQ 213
Cdd:cd03296 153 VEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQE-EALEVADRVVVMNKG------RIEQ 217
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
4-215 |
4.53e-16 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 78.68 E-value: 4.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 4 IEWNNICYR------DILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSG-------NIACSSSTSFCEQeda 70
Cdd:cd03252 1 ITFEHVRFRykpdgpVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGrvlvdghDLALADPAWLRRQ--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 71 lLGVMTVKETL-KYSARLSVPHATSQVIEERVNAVIDGLGLHSVLN------NRIGTPIQRGISGGQKRRVSIACSLVQF 143
Cdd:cd03252 78 -VGVVLQENVLfNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISelpegyDTIVGEQGAGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1625600662 144 PDILFLDEPTSGLDISTAHQVMTAIKRMAVTHNIAVVA----TIHSPnweiftlfDKLLLLAKGETVFNSKIDQLV 215
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAhrlsTVKNA--------DRIIVMEKGRIVEQGSHDELL 224
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
15-227 |
5.87e-16 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 79.42 E-value: 5.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 15 LKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSSTSFCEQEDAL------LGV-----------MTV 77
Cdd:TIGR04521 21 LDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLkdlrkkVGLvfqfpehqlfeETV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 78 KETLKYSAR-LSVPHATsqvIEERVNAVIDGLGLHSVLNNRigTPIQrgISGGQKRRVSIACSLVQFPDILFLDEPTSGL 156
Cdd:TIGR04521 101 YKDIAFGPKnLGLSEEE---AEERVKEALELVGLDEEYLER--SPFE--LSGGQMRRVAIAGVLAMEPEVLILDEPTAGL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 157 DISTAHQVMTAIKRMAVTHNIAVVATIHSPNwEIFTLFDKLLLLAKG--------ETVFNS------------KIDQLVP 216
Cdd:TIGR04521 174 DPKGRKEILDLFKRLHKEKGLTVILVTHSME-DVAEYADRVIVMHKGkivldgtpREVFSDvdelekigldvpEITELAR 252
|
250
....*....|.
gi 1625600662 217 YFEELGYNFPK 227
Cdd:TIGR04521 253 KLKEKGLPVPK 263
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
14-180 |
7.01e-16 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 77.95 E-value: 7.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 14 ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSS--TSFCEQEDALLGV------------MTVKE 79
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEdiTKLPPHERARAGIayvpqgreifprLTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 80 TLK--YSARlsvPHATSQVIEErvnavIDGL--GLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLDEPTSG 155
Cdd:TIGR03410 95 NLLtgLAAL---PRRSRKIPDE-----IYELfpVLKEMLGRRGGD-----LSGGQQQQLAIARALVTRPKLLLLDEPTEG 161
|
170 180
....*....|....*....|....*
gi 1625600662 156 LDISTAHQVMTAIKRMAVTHNIAVV 180
Cdd:TIGR03410 162 IQPSIIKDIGRVIRRLRAEGGMAIL 186
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
14-214 |
7.24e-16 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 80.76 E-value: 7.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 14 ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSS-------------STSFceQEDALLGVMTVKET 80
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGqdithvpaenrhvNTVF--QSYALFPHMTVFEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 81 LKYSARLS-VPHATsqvIEERVNAVIDGLGLHSVLNNRigtPIQrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLDIS 159
Cdd:PRK09452 107 VAFGLRMQkTPAAE---ITPRVMEALRMVQLEEFAQRK---PHQ--LSGGQQQRVAIARAVVNKPKVLLLDESLSALDYK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1625600662 160 TAHQVMTAIKRMAVTHNIAVVATIHSPNwEIFTLFDKLLLLAKGetvfnsKIDQL 214
Cdd:PRK09452 179 LRKQMQNELKALQRKLGITFVFVTHDQE-EALTMSDRIVVMRDG------RIEQD 226
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
12-171 |
7.61e-16 |
|
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: 82.07 E-value: 7.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 12 RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI------------AC-SSSTSFCEQeDALLGVMTVK 78
Cdd:TIGR02203 345 RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQIlldghdladytlASlRRQVALVSQ-DVVLFNDTIA 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 79 ETLKYSARLSVPHATSQVIEERVNA--VIDGL--GLHsvlnnrigTPI-QRG--ISGGQKRRVSIACSLVQFPDILFLDE 151
Cdd:TIGR02203 424 NNIAYGRTEQADRAEIERALAAAYAqdFVDKLplGLD--------TPIgENGvlLSGGQRQRLAIARALLKDAPILILDE 495
|
170 180
....*....|....*....|
gi 1625600662 152 PTSGLDISTAHQVMTAIKRM 171
Cdd:TIGR02203 496 ATSALDNESERLVQAALERL 515
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
15-203 |
1.18e-15 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 77.51 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 15 LKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSS----------TSFceQEDALLGVMTVKETLKYS 84
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKqitepgpdrmVVF--QNYSLLPWLTVRENIALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 85 ARLSVPHATSQVIEERVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTAHQV 164
Cdd:TIGR01184 79 VDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQ-----LSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 1625600662 165 MTAIKRMAVTHNIAVVATIHSPNwEIFTLFDKLLLLAKG 203
Cdd:TIGR01184 154 QEELMQIWEEHRVTVLMVTHDVD-EALLLSDRVVMLTNG 191
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
14-178 |
1.21e-15 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 76.75 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 14 ILKQISGDVKPAEILAVMGPSGSGKTTLLECISrrkKTSSGNIACSSSTSFCEQE----------------DALL-GVMT 76
Cdd:COG4136 16 LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIA---GTLSPAFSASGEVLLNGRRltalpaeqrrigilfqDDLLfPHLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 77 VKETLKYSARLSVPHATSQvieERVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLDEPTSGL 156
Cdd:COG4136 93 VGENLAFALPPTIGRAQRR---ARVEQALEEAGLAGFADRDPAT-----LSGGQRARVALLRALLAEPRALLLDEPFSKL 164
|
170 180 190
....*....|....*....|....*....|.
gi 1625600662 157 D----ISTAHQVMTAIKRMA-----VTHNIA 178
Cdd:COG4136 165 DaalrAQFREFVFEQIRQRGipallVTHDEE 195
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
22-206 |
1.30e-15 |
|
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: 76.76 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 22 VKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIA-----------CSSSTSFCEQEDALLGVMTVKET--LKYSARLS 88
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLingvdvtaappADRPVSMLFQENNLFAHLTVEQNvgLGLSPGLK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 89 VphatSQVIEERVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTAHQVMTAI 168
Cdd:cd03298 101 L----TAEDRQAIEVALARVGLAGLEKRLPGE-----LSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190
....*....|....*....|....*....|....*...
gi 1625600662 169 KRMAVTHNIAVVATIHSPNwEIFTLFDKLLLLAKGETV 206
Cdd:cd03298 172 LDLHAETKMTVLMVTHQPE-DAKRLAQRVVFLDNGRIA 208
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
15-164 |
1.52e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 77.51 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 15 LKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKK-----TSSGNIACSSSTSFCEQEDAL-----LGV---------M 75
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYSPRTDTVdlrkeIGMvfqqpnpfpM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 76 TVKETLKYSARLSVPHaTSQVIEERVNAVIDGLGLHSVLNNRIGTPiQRGISGGQKRRVSIACSLVQFPDILFLDEPTSG 155
Cdd:PRK14239 101 SIYENVVYGLRLKGIK-DKQVLDEAVEKSLKGASIWDEVKDRLHDS-ALGLSGGQQQRVCIARVLATSPKIILLDEPTSA 178
|
....*....
gi 1625600662 156 LDISTAHQV 164
Cdd:PRK14239 179 LDPISAGKI 187
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
13-186 |
1.80e-15 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 77.09 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 13 DILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSSTSFCEQEDA-----------------LLGVM 75
Cdd:COG4181 26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDArarlrarhvgfvfqsfqLLPTL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 76 TVKETLKYSARL-SVPHATSQVIE--ERVnavidGLGlhsvlnNRIG-TPIQrgISGGQKRRVSIACSLVQFPDILFLDE 151
Cdd:COG4181 106 TALENVMLPLELaGRRDARARARAllERV-----GLG------HRLDhYPAQ--LSGGEQQRVALARAFATEPAILFADE 172
|
170 180 190
....*....|....*....|....*....|....*
gi 1625600662 152 PTSGLDISTAHQVMTAIKRMAVTHNIAVVATIHSP 186
Cdd:COG4181 173 PTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDP 207
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
18-213 |
2.22e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 77.19 E-value: 2.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 18 ISGDVKPAEILAVMGPSGSGKTTLLECISRRKkTSSGNIACS----SSTSFCE---------QEDALLGVMTVKETLkys 84
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNgrplSDWSAAElarhraylsQQQSPPFAMPVFQYL--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 85 aRLSVP-HATSQVIEERVNAVIDGLGLhsvlNNRIGTPIQRgISGGQKRRVSIACSLVQ-FPDI------LFLDEPTSGL 156
Cdd:COG4138 91 -ALHQPaGASSEAVEQLLAQLAEALGL----EDKLSRPLTQ-LSGGEWQRVRLAAVLLQvWPTInpegqlLLLDEPMNSL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1625600662 157 DIstAHQVM--TAIKRMAvTHNIAVVATIHSPNweiFTLF--DKLLLLAKGETVFNSKIDQ 213
Cdd:COG4138 165 DV--AQQAAldRLLRELC-QQGITVVMSSHDLN---HTLRhaDRVWLLKQGKLVASGETAE 219
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-204 |
2.26e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 79.30 E-value: 2.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 1 MSPIEWNNIC--YRD--ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI-----------ACSSSTSFC 65
Cdd:PRK11000 1 MASVTLRNVTkaYGDvvISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLfigekrmndvpPAERGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 66 EQEDALLGVMTVKETLKYSARLSvpHATSQVIEERVNAVIDGLGLHSVLNNRigtPiqRGISGGQKRRVSIACSLVQFPD 145
Cdd:PRK11000 81 FQSYALYPHLSVAENMSFGLKLA--GAKKEEINQRVNQVAEVLQLAHLLDRK---P--KALSGGQRQRVAIGRTLVAEPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1625600662 146 ILFLDEPTSGLDISTAHQVMTAIKRMA---------VTHNiavvatihspNWEIFTLFDKLLLLAKGE 204
Cdd:PRK11000 154 VFLLDEPLSNLDAALRVQMRIEISRLHkrlgrtmiyVTHD----------QVEAMTLADKIVVLDAGR 211
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
15-214 |
2.36e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 77.84 E-value: 2.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 15 LKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIacssstSFCEQ---------------EDALLGVMTVKE 79
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEV------LWDGEpldpedrrrigylpeERGLYPKMKVGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 80 TLKYSARLsvpH-ATSQVIEERVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLDI 158
Cdd:COG4152 91 QLVYLARL---KgLSKAEAKRRADEWLERLGLGDRANKKVEE-----LSKGNQQKVQLIAALLHDPELLILDEPFSGLDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1625600662 159 STAHQVMTAIKRMA--------VTHNIAVVatihspnwEifTLFDKLLLLAKGETVFNSKIDQL 214
Cdd:COG4152 163 VNVELLKDVIRELAakgttvifSSHQMELV--------E--ELCDRIVIINKGRKVLSGSVDEI 216
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
14-172 |
3.23e-15 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 76.17 E-value: 3.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 14 ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIacssstSFCEQE-DAL-------LGV----------- 74
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSI------RFDGEDiTGLpphriarLGIgyvpegrrifp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 75 -MTVKETLKYSARLSVPHATSQVIEERVnavidgLGLHSVLNNRIGtpiQRG--ISGGQKRRVSIACSLVQFPDILFLDE 151
Cdd:COG0410 92 sLTVEENLLLGAYARRDRAEVRADLERV------YELFPRLKERRR---QRAgtLSGGEQQMLAIGRALMSRPKLLLLDE 162
|
170 180
....*....|....*....|.
gi 1625600662 152 PTSGLDISTAHQVMTAIKRMA 172
Cdd:COG0410 163 PSLGLAPLIVEEIFEIIRRLN 183
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
22-204 |
4.18e-15 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 75.28 E-value: 4.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 22 VKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSST-----------SFCEQEDALLGVMTVKETLKYSARLSVP 90
Cdd:TIGR01277 21 VADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQShtglapyqrpvSMLFQENNLFAHLTVRQNIGLGLHPGLK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 91 HATSQviEERVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTAHQVMTAIKR 170
Cdd:TIGR01277 101 LNAEQ--QEKVVDAAQQVGIADYLDRLPEQ-----LSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQ 173
|
170 180 190
....*....|....*....|....*....|....
gi 1625600662 171 MAVTHNIAVVATIHSPNwEIFTLFDKLLLLAKGE 204
Cdd:TIGR01277 174 LCSERQRTLLMVTHHLS-DARAIASQIAVVSQGK 206
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
22-203 |
5.60e-15 |
|
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: 80.44 E-value: 5.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 22 VKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACS------------SSTSFCEQEDALLGVMTVKETLKYSARL-S 88
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAgksiltnisdvhQNMGYCPQFDAIDDLLTGREHLYLYARLrG 2041
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 89 VPhatSQVIEERVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTAHQVMTAI 168
Cdd:TIGR01257 2042 VP---AEEIEKVANWSIQSLGLSLYADRLAGT-----YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTI 2113
|
170 180 190
....*....|....*....|....*....|....*
gi 1625600662 169 KRMaVTHNIAVVATIHSPNwEIFTLFDKLLLLAKG 203
Cdd:TIGR01257 2114 VSI-IREGRAVVLTSHSME-ECEALCTRLAIMVKG 2146
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
12-204 |
5.87e-15 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 75.45 E-value: 5.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 12 RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIacssstsFCEQED---------ALLGV-------- 74
Cdd:COG1137 16 RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRI-------FLDGEDithlpmhkrARLGIgylpqeas 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 75 ----MTVKETLKysARLSVPHATSQVIEERVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLD 150
Cdd:COG1137 89 ifrkLTVEDNIL--AVLELRKLSKKEREERLEELLEEFGITHLRKSKAYS-----LSGGERRRVEIARALATNPKFILLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 151 EPTSGLD-ISTAHqvmtaIKRMaVTH----NIAVVATIHspN-WEIFTLFDKLLLLAKGE 204
Cdd:COG1137 162 EPFAGVDpIAVAD-----IQKI-IRHlkerGIGVLITDH--NvRETLGICDRAYIISEGK 213
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
14-164 |
8.25e-15 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 75.67 E-value: 8.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 14 ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI--------ACSSSTSFCEQEDALLGVMTVKETLKYSA 85
Cdd:COG4525 22 ALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEItldgvpvtGPGADRGVVFQKDALLPWLNVLDNVAFGL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 86 RLS-VPHATSQvieERVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTAHQV 164
Cdd:COG4525 102 RLRgVPKAERR---ARAEELLALVGLADFARRRIWQ-----LSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQM 173
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
14-181 |
9.89e-15 |
|
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: 74.88 E-value: 9.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 14 ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI-------------ACSSSTSFCEQEDALLGvMTVKET 80
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEIlldgvdirdlnlrWLRSQIGLVSQEPVLFD-GTIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 81 LKYSArlsvPHATSQVIEERVNAVidglGLHSV---LNNRIGTPI-QRG--ISGGQKRRVSIACSLVQFPDILFLDEPTS 154
Cdd:cd03249 97 IRYGK----PDATDEEVEEAAKKA----NIHDFimsLPDGYDTLVgERGsqLSGGQKQRIAIARALLRNPKILLLDEATS 168
|
170 180
....*....|....*....|....*..
gi 1625600662 155 GLDISTAHQVMTAIKRMAVTHNIAVVA 181
Cdd:cd03249 169 ALDAESEKLVQEALDRAMKGRTTIVIA 195
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
12-158 |
1.20e-14 |
|
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: 72.10 E-value: 1.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 12 RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSSTSFCeqedallgvmtvketlkYSARLSvph 91
Cdd:cd03221 13 KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIG-----------------YFEQLS--- 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1625600662 92 atsqvieervnavidglglhsvlnnrigtpiqrgisGGQKRRVSIACSLVQFPDILFLDEPTSGLDI 158
Cdd:cd03221 73 ------------------------------------GGEKMRLALAKLLLENPNLLLLDEPTNHLDL 103
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
18-180 |
1.23e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 74.96 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 18 ISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIacssstSFCEQEDALLGVMTVKEtlkysARLSVPHATS--- 94
Cdd:PRK11701 25 VSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV------HYRMRDGQLRDLYALSE-----AERRRLLRTEwgf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 95 -----------QV-----IEERVNAV------------IDGLGLHSVLNNRIG-TPiqRGISGGQKRRVSIACSLVQFPD 145
Cdd:PRK11701 94 vhqhprdglrmQVsaggnIGERLMAVgarhygdirataGDWLERVEIDAARIDdLP--TTFSGGMQQRLQIARNLVTHPR 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1625600662 146 ILFLDEPTSGLDISTAHQVMTAIKRMA---------VTHNIAVV 180
Cdd:PRK11701 172 LVFMDEPTGGLDVSVQARLLDLLRGLVrelglavviVTHDLAVA 215
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
14-230 |
1.24e-14 |
|
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: 75.66 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 14 ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSSTSFCEQEDALLGvMTVKETLKYSARLSvphat 93
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMP-GTIKENIIFGVSYD----- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 94 sqviEERVNAVIDGLGLH---SVLNNRIGTPIQRG---ISGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTAHQVMTA 167
Cdd:cd03291 126 ----EYRYKSVVKACQLEediTKFPEKDNTVLGEGgitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFES 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1625600662 168 --IKRMAVTHNIAVVATIhspnwEIFTLFDKLLLLAKGETVFNSKidqlvpyFEELGYNFPKFSN 230
Cdd:cd03291 202 cvCKLMANKTRILVTSKM-----EHLKKADKILILHEGSSYFYGT-------FSELQSLRPDFSS 254
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
4-170 |
1.64e-14 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 74.18 E-value: 1.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 4 IEWNNICY-----RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI-------------ACSSSTSFC 65
Cdd:cd03254 3 IEFENVNFsydekKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQIlidgidirdisrkSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 66 EQEDALLGvMTVKETLKYSArlsvPHATSQVIEERVNAV-----IDGL--GLHSVLNNRIGTpiqrgISGGQKRRVSIAC 138
Cdd:cd03254 83 LQDTFLFS-GTIMENIRLGR----PNATDEEVIEAAKEAgahdfIMKLpnGYDTVLGENGGN-----LSQGERQLLAIAR 152
|
170 180 190
....*....|....*....|....*....|..
gi 1625600662 139 SLVQFPDILFLDEPTSGLDISTAHQVMTAIKR 170
Cdd:cd03254 153 AMLRDPKILILDEATSNIDTETEKLIQEALEK 184
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
15-179 |
1.68e-14 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 77.98 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 15 LKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI-------------ACSSSTSFCEQEDALL-GvmTVKET 80
Cdd:TIGR03375 481 LDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVlldgvdirqidpaDLRRNIGYVPQDPRLFyG--TLRDN 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 81 LKYSArlsvPHATSQVIeerVNAVIDGlGLHSVLN---NRIGTPIQ---RGISGGQKRRVSIACSLVQFPDILFLDEPTS 154
Cdd:TIGR03375 559 IALGA----PYADDEEI---LRAAELA-GVTEFVRrhpDGLDMQIGergRSLSGGQRQAVALARALLRDPPILLLDEPTS 630
|
170 180 190
....*....|....*....|....*....|..
gi 1625600662 155 GLDISTAHQVMTAIKRMA-------VTHNIAV 179
Cdd:TIGR03375 631 AMDNRSEERFKDRLKRWLagktlvlVTHRTSL 662
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
14-254 |
3.56e-14 |
|
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: 76.38 E-value: 3.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 14 ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRK--KTSSGNI---------------------ACSSSTSFCEQEDA 70
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIiyhvalcekcgyverpskvgePCPVCGGTLEPEEV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 71 LLGVMTVKETLKYSARLSVP-------HATSQVIEERVNAV--IDGLGLHSV-----------LNNRIgTPIQRGISGGQ 130
Cdd:TIGR03269 95 DFWNLSDKLRRRIRKRIAIMlqrtfalYGDDTVLDNVLEALeeIGYEGKEAVgravdliemvqLSHRI-THIARDLSGGE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 131 KRRVSIACSLVQFPDILFLDEPTSGLDISTAHQVMTAIKRMAVTHNIAVVATIHSPNwEIFTLFDKLLLLAKGETVFNSK 210
Cdd:TIGR03269 174 KQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPE-VIEDLSDKAIWLENGEIKEEGT 252
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1625600662 211 IDQLVPYFEELGYNFPKFSNpVDVVMELINTDFEKQDSKSIEEG 254
Cdd:TIGR03269 253 PDEVVAVFMEGVSEVEKECE-VEVGEPIIKVRNVSKRYISVDRG 295
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
10-185 |
3.62e-14 |
|
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: 72.53 E-value: 3.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 10 CYRD---ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI------------ACSSSTSFCEQEDALLGV 74
Cdd:cd03231 8 CERDgraLFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVllnggpldfqrdSIARGLLYLGHAPGIKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 75 MTVKETLKYSARLsvpHATSQVIEervnaVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLDEPTS 154
Cdd:cd03231 88 LSVLENLRFWHAD---HSDEQVEE-----ALARVGLNGFEDRPVAQ-----LSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170 180 190
....*....|....*....|....*....|.
gi 1625600662 155 GLDISTAHQVMTAIKRMAVTHNIAVVATIHS 185
Cdd:cd03231 155 ALDKAGVARFAEAMAGHCARGGMVVLTTHQD 185
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
14-190 |
3.94e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 72.82 E-value: 3.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 14 ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI-------------ACSSSTSFCEQEDALLGvMTVKET 80
Cdd:PRK10247 22 ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLlfegedistlkpeIYRQQVSYCAQTPTLFG-DTVYDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 81 LK--YSARLSVPHatsqviEERVNAVIDGLGL-HSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLD 157
Cdd:PRK10247 101 LIfpWQIRNQQPD------PAIFLDDLERFALpDTILTKNIAE-----LSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
170 180 190
....*....|....*....|....*....|...
gi 1625600662 158 ISTAHQVMTAIKRMAVTHNIAVVATIHSPNwEI 190
Cdd:PRK10247 170 ESNKHNVNEIIHRYVREQNIAVLWVTHDKD-EI 201
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
24-203 |
4.63e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 74.91 E-value: 4.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 24 PAE-ILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSSTSF-CEQ---------------EDA-LLGVMTVKETLKYSA 85
Cdd:PRK11144 22 PAQgITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFdAEKgiclppekrrigyvfQDArLFPHYKVRGNLRYGM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 86 RLSVPhatsqvieERVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTAHQVM 165
Cdd:PRK11144 102 AKSMV--------AQFDKIVALLGIEPLLDRYPGS-----LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELL 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 1625600662 166 TAIKRMAVTHNIAVVATIHSPNwEIFTLFDKLLLLAKG 203
Cdd:PRK11144 169 PYLERLAREINIPILYVSHSLD-EILRLADRVVVLEQG 205
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-185 |
5.89e-14 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 72.74 E-value: 5.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 1 MSpIEWNNICY----RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSST-SFCEqedallgvm 75
Cdd:COG4161 1 MS-IQLKNINCfygsHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfDFSQ--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 76 TVKETLKYSARLSV----------PHATsqVIEERVNAVIDGLGLHS--------VLNNRIGT-------PIQrgISGGQ 130
Cdd:COG4161 71 KPSEKAIRLLRQKVgmvfqqynlwPHLT--VMENLIEAPCKVLGLSKeqarekamKLLARLRLtdkadrfPLH--LSGGQ 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1625600662 131 KRRVSIACSLVQFPDILFLDEPTSGLDISTAHQVM--------TAIKRMAVTHNIAVVATIHS 185
Cdd:COG4161 147 QQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVeiirelsqTGITQVIVTHEVEFARKVAS 209
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
12-170 |
6.04e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 75.90 E-value: 6.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 12 RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSSTSFCEQEDALLGVMTV--------KETLKY 83
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVvsqtpflfSDTVAN 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 84 SARLSVPHATSQVIEE--RVNAVIDG-LGLHSVLNNRIGtpiQRGI--SGGQKRRVSIACSLVQFPDILFLDEPTSGLDI 158
Cdd:PRK10789 408 NIALGRPDATQQEIEHvaRLASVHDDiLRLPQGYDTEVG---ERGVmlSGGQKQRISIARALLLNAEILILDDALSAVDG 484
|
170
....*....|..
gi 1625600662 159 STAHQVMTAIKR 170
Cdd:PRK10789 485 RTEHQILHNLRQ 496
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
15-208 |
6.36e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 73.12 E-value: 6.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 15 LKQISGDVKPAEILAVMGPSGSGKTTLLECIS--------------------RRKKTSSGNIACS-SSTSFCEQEDALLG 73
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSglitgdksagshiellgrtvQREGRLARDIRKSrANTGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 74 VMTVKETLKYSARLSVP------HATSQVIEERVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDIL 147
Cdd:PRK09984 100 RLSVLENVLIGALGSTPfwrtcfSWFTREQKQRALQALTRVGMVHFAHQRVST-----LSGGQQQRVAIARALMQQAKVI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1625600662 148 FLDEPTSGLDISTAHQVMTAIKRMAVTHNIAVVATIHSPNWEIfTLFDKLLLLAKGETVFN 208
Cdd:PRK09984 175 LADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYAL-RYCERIVALRQGHVFYD 234
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
15-227 |
6.37e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 73.54 E-value: 6.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 15 LKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIAC--------SSSTSFCEQEDAL--------LGVMTVK 78
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIdgvditdkKVKLSDIRKKVGLvfqypeyqLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 79 ETLKYSAR---LSvphatSQVIEERVNAVIDGLGL-HSVLNNRigTPIQrgISGGQKRRVSIACSLVQFPDILFLDEPTS 154
Cdd:PRK13637 103 KDIAFGPInlgLS-----EEEIENRVKRAMNIVGLdYEDYKDK--SPFE--LSGGQKRRVAIAGVVAMEPKILILDEPTA 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1625600662 155 GLDISTAHQVMTAIKRMAVTHNIAVVATIHSPNwEIFTLFDKLLLLAKGETVFNSKIDQL---VPYFEELGYNFPK 227
Cdd:PRK13637 174 GLDPKGRDEILNKIKELHKEYNMTIILVSHSME-DVAKLADRIIVMNKGKCELQGTPREVfkeVETLESIGLAVPQ 248
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
12-203 |
6.68e-14 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 75.85 E-value: 6.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 12 RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSS-------------STSFCEQeDALLGVMTVK 78
Cdd:TIGR01842 331 KPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGadlkqwdretfgkHIGYLPQ-DVELFPGTVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 79 ETLkysARLSVPHATSQVIEERVNAvidglGLHSV---LNNRIGTPIQRG---ISGGQKRRVSIACSLVQFPDILFLDEP 152
Cdd:TIGR01842 410 ENI---ARFGENADPEKIIEAAKLA-----GVHELilrLPDGYDTVIGPGgatLSGGQRQRIALARALYGDPKLVVLDEP 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1625600662 153 TSGLDISTAHQVMTAIKRMAVTHNIAVVATiHSPNweIFTLFDKLLLLAKG 203
Cdd:TIGR01842 482 NSNLDEEGEQALANAIKALKARGITVVVIT-HRPS--LLGCVDKILVLQDG 529
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-157 |
1.10e-13 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 73.64 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 1 MSpIEWNNICYR----DILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI------------ACSSSTSF 64
Cdd:COG1118 1 MS-IEVRNISKRfgsfTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIvlngrdlftnlpPRERRVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 65 CEQEDALLGVMTVKETLKYSarLSVPHATSQVIEERVNAVIDGLGLHSvLNNRigTPIQrgISGGQKRRVSIACSLVQFP 144
Cdd:COG1118 80 VFQHYALFPHMTVAENIAFG--LRVRPPSKAEIRARVEELLELVQLEG-LADR--YPSQ--LSGGQRQRVALARALAVEP 152
|
170
....*....|...
gi 1625600662 145 DILFLDEPTSGLD 157
Cdd:COG1118 153 EVLLLDEPFGALD 165
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
12-181 |
1.32e-13 |
|
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: 74.86 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 12 RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI--------ACSsstsfceQED--ALLGVM---TV- 77
Cdd:COG5265 371 RPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRIlidgqdirDVT-------QASlrAAIGIVpqdTVl 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 78 -KETLKYSARLSVPHATsqviEERVNAVIDGLGLH---SVLNNRIGTPI-QRG--ISGGQKRRVSIACSLVQFPDILFLD 150
Cdd:COG5265 444 fNDTIAYNIAYGRPDAS----EEEVEAAARAAQIHdfiESLPDGYDTRVgERGlkLSGGEKQRVAIARTLLKNPPILIFD 519
|
170 180 190
....*....|....*....|....*....|.
gi 1625600662 151 EPTSGLDISTAHQVMTAIKRMAVTHNIAVVA 181
Cdd:COG5265 520 EATSALDSRTERAIQAALREVARGRTTLVIA 550
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
12-195 |
1.33e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 71.06 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 12 RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI---------ACSSSTSFCE-------QEDALLGVM 75
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsghditrLKNREVPFLRrqigmifQDHHLLMDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 76 TVKETLkySARLSVPHATSQVIEERVNAVIDGLGLhsvLNNRIGTPIQrgISGGQKRRVSIACSLVQFPDILFLDEPTSG 155
Cdd:PRK10908 95 TVYDNV--AIPLIIAGASGDDIRRRVSAALDKVGL---LDKAKNFPIQ--LSGGEQQRVGIARAVVNKPAVLLADEPTGN 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1625600662 156 LDISTAHQVM--------TAIKRMAVTHNIAVVAtihSPNWEIFTLFD 195
Cdd:PRK10908 168 LDDALSEGILrlfeefnrVGVTVLMATHDIGLIS---RRSYRMLTLSD 212
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
12-187 |
1.35e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 72.13 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 12 RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACS-------SSTSFC-------EQEDALLGvMTV 77
Cdd:PRK10575 24 RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDaqpleswSSKAFArkvaylpQQLPAAEG-MTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 78 KETL---KYS-----ARLSVPHatsqviEERVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFL 149
Cdd:PRK10575 103 RELVaigRYPwhgalGRFGAAD------REKVEEAISLVGLKPLAHRLVDS-----LSGGERQRAWIAMLVAQDSRCLLL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1625600662 150 DEPTSGLDIstAHQ--VMTAIKRMAVTHNIAVVATIHSPN 187
Cdd:PRK10575 172 DEPTSALDI--AHQvdVLALVHRLSQERGLTVIAVLHDIN 209
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
15-206 |
1.42e-13 |
|
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: 71.56 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 15 LKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI-------------ACSSSTSFCEQEDALLGVMTVKETL 81
Cdd:cd03295 17 VNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIfidgedireqdpvELRRKIGYVIQQIGLFPHMTVEENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 82 kySARLSVPHATSQVIEERVNAVIDGLGLHSV-LNNRIgtPIQrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLDIST 160
Cdd:cd03295 97 --ALVPKLLKWPKEKIRERADELLALVGLDPAeFADRY--PHE--LSGGQQQRVGVARALAADPPLLLMDEPFGALDPIT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1625600662 161 AHQVMTAIKRMA---------VTHNIAvvatihspnwEIFTLFDKLLLLAKGETV 206
Cdd:cd03295 171 RDQLQEEFKRLQqelgktivfVTHDID----------EAFRLADRIAIMKNGEIV 215
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-233 |
1.47e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 71.99 E-value: 1.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 4 IEWNNICY----RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSsGNIACSSSTSFCEQE----------- 68
Cdd:PRK14258 8 IKVNNLSFyydtQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGRVEFFNQNiyerrvnlnrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 69 ---------DALLGVMTVKETLKYSARLSVPHATSQvIEERVNAVIDGLGLHSVLNNRIGTPIQRgISGGQKRRVSIACS 139
Cdd:PRK14258 87 rrqvsmvhpKPNLFPMSVYDNVAYGVKIVGWRPKLE-IDDIVESALKDADLWDEIKHKIHKSALD-LSGGQQQRLCIARA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 140 LVQFPDILFLDEPTSGLDISTAHQVMTAIKRMAVTHNIAVVATIHSPNwEIFTLFDKLLLLAKGEtvfnSKIDQLVpyfe 219
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLH-QVSRLSDFTAFFKGNE----NRIGQLV---- 235
|
250
....*....|....
gi 1625600662 220 ELGYNFPKFSNPVD 233
Cdd:PRK14258 236 EFGLTKKIFNSPHD 249
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
12-177 |
1.55e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 71.65 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 12 RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIAC--------SSSTSFCEQEDALLGVMTVKETLKY 83
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLdgkpvegpGAERGVVFQNEGLLPWRNVQDNVAF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 84 SARLS-VPHATSQVIEERVNAVIDGLGLHsvlnnrigtpiQRGI---SGGQKRRVSIACSLVQFPDILFLDEPTSGLDIS 159
Cdd:PRK11248 94 GLQLAgVEKMQRLEIAHQMLKKVGLEGAE-----------KRYIwqlSGGQRQRVGIARALAANPQLLLLDEPFGALDAF 162
|
170 180
....*....|....*....|....*..
gi 1625600662 160 TAHQVMTAIKRM---------AVTHNI 177
Cdd:PRK11248 163 TREQMQTLLLKLwqetgkqvlLITHDI 189
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
12-181 |
1.71e-13 |
|
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: 70.96 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 12 RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACS-------------SSTSFCEQEDALLGvMTVK 78
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDgkpisqyehkylhSKVSLVGQEPVLFA-RSLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 79 ETLKYsarlsvphATSQVIEERVNAVIDGLGLH---SVLNNRIGTPI-QRG--ISGGQKRRVSIACSLVQFPDILFLDEP 152
Cdd:cd03248 106 DNIAY--------GLQSCSFECVKEAAQKAHAHsfiSELASGYDTEVgEKGsqLSGGQKQRVAIARALIRNPQVLILDEA 177
|
170 180
....*....|....*....|....*....
gi 1625600662 153 TSGLDISTAHQVMTAIKRMAVTHNIAVVA 181
Cdd:cd03248 178 TSALDAESEQQVQQALYDWPERRTVLVIA 206
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
14-230 |
2.24e-13 |
|
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: 74.95 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 14 ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSSTSFCEQEDALLGvMTVKETLKYSARLSvphat 93
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMP-GTIKDNIIFGLSYD----- 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 94 sqviEERVNAVIDGLGLH---SVLNNRIGTPIQRG---ISGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTAHQVMTA 167
Cdd:TIGR01271 515 ----EYRYTSVIKACQLEediALFPEKDKTVLGEGgitLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFES 590
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1625600662 168 --IKRMAVTHNIAVVATIhspnwEIFTLFDKLLLLAKGETVFNSKidqlvpyFEELGYNFPKFSN 230
Cdd:TIGR01271 591 clCKLMSNKTRILVTSKL-----EHLKKADKILLLHEGVCYFYGT-------FSELQAKRPDFSS 643
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
11-178 |
2.42e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 73.97 E-value: 2.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 11 YRDILKQISGDVKPAEILAVMGPSGSGKTT----LLECISrrkktSSGNIACSSS------------------TSFCEQE 68
Cdd:PRK15134 298 HNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQplhnlnrrqllpvrhriqVVFQDPN 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 69 DALLGVMTVKETLKYSARLSVPHATSQVIEERVNAVIDGLGLHSVLNNRIGTPIqrgiSGGQKRRVSIACSLVQFPDILF 148
Cdd:PRK15134 373 SSLNPRLNVLQIIEEGLRVHQPTLSAAQREQQVIAVMEEVGLDPETRHRYPAEF----SGGQRQRIAIARALILKPSLII 448
|
170 180 190
....*....|....*....|....*....|
gi 1625600662 149 LDEPTSGLDISTAHQVMTAIKRMAVTHNIA 178
Cdd:PRK15134 449 LDEPTSSLDKTVQAQILALLKSLQQKHQLA 478
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
12-191 |
2.83e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 70.37 E-value: 2.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 12 RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSSTSFCEQEDALLgvmtvkETLkySARLSVPH 91
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGREASLI------DAI--GRKGDFKD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 92 ATsqvieERVNAVidglGLHSVLNNRigTPIqRGISGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTAHQVMTAIKRM 171
Cdd:COG2401 115 AV-----ELLNAV----GLSDAVLWL--RRF-KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKL 182
|
170 180
....*....|....*....|....*...
gi 1625600662 172 AVTHNI-AVVATIH-------SPNWEIF 191
Cdd:COG2401 183 ARRAGItLVVATHHydviddlQPDLLIF 210
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
15-180 |
3.17e-13 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 72.14 E-value: 3.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 15 LKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSS--TSFCEQEDA--------------LLGVMTVK 78
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQdlTALSEKELRkarrqigmifqhfnLLSSRTVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 79 ETLKYSARLS-VPHATsqvIEERVNAVIDGLGLhSVLNNRIgtPIQrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLD 157
Cdd:PRK11153 101 DNVALPLELAgTPKAE---IKARVTELLELVGL-SDKADRY--PAQ--LSGGQKQRVAIARALASNPKVLLCDEATSALD 172
|
170 180 190
....*....|....*....|....*....|..
gi 1625600662 158 ISTAHQVMTAIKR---------MAVTHNIAVV 180
Cdd:PRK11153 173 PATTRSILELLKDinrelgltiVLITHEMDVV 204
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
21-183 |
3.36e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 70.38 E-value: 3.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 21 DVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSST-----------SFCEQEDALLGVMTVKET----LKYSA 85
Cdd:PRK10771 21 TVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDhtttppsrrpvSMLFQENNLFSHLTVAQNiglgLNPGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 86 RLSVP-HATSQVIEERVnavidglGLHSVLNnRIgtPIQrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTAHQV 164
Cdd:PRK10771 101 KLNAAqREKLHAIARQM-------GIEDLLA-RL--PGQ--LSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEM 168
|
170 180
....*....|....*....|....*...
gi 1625600662 165 MTAIKR---------MAVTHNIAVVATI 183
Cdd:PRK10771 169 LTLVSQvcqerqltlLMVSHSLEDAARI 196
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
9-182 |
3.57e-13 |
|
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: 69.31 E-value: 3.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 9 ICYRD---ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSSTSFCEQE------------DALLG 73
Cdd:TIGR01189 7 ACSRGermLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDephenilylghlPGLKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 74 VMTVKETLKYSARLSVPHatSQVIEERVNAVidGLGLHSVLnnrigtpIQRGISGGQKRRVSIACSLVQFPDILFLDEPT 153
Cdd:TIGR01189 87 ELSALENLHFWAAIHGGA--QRTIEDALAAV--GLTGFEDL-------PAAQLSAGQQRRLALARLWLSRRPLWILDEPT 155
|
170 180
....*....|....*....|....*....
gi 1625600662 154 SGLDISTAHQVMTAIKRMAVTHNIAVVAT 182
Cdd:TIGR01189 156 TALDKAGVALLAGLLRAHLARGGIVLLTT 184
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
12-203 |
4.28e-13 |
|
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: 73.24 E-value: 4.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 12 RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSG-------NIACSSSTSFCE------QEDALL-GvmTV 77
Cdd:COG4618 345 RPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGsvrldgaDLSQWDREELGRhigylpQDVELFdG--TI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 78 KETLkysARLsvPHATSQVIEE-----RVNAVIDGL--GLHSvlnnRIGtPIQRGISGGQKRRVSIACSLVQFPDILFLD 150
Cdd:COG4618 423 AENI---ARF--GDADPEKVVAaaklaGVHEMILRLpdGYDT----RIG-EGGARLSGGQRQRIGLARALYGDPRLVVLD 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1625600662 151 EPTSGLDiSTAHQ-VMTAIKRMAvTHNIAVVATIHSPNweIFTLFDKLLLLAKG 203
Cdd:COG4618 493 EPNSNLD-DEGEAaLAAAIRALK-ARGATVVVITHRPS--LLAAVDKLLVLRDG 542
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
18-206 |
6.48e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.58 E-value: 6.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 18 ISGDVKPAEILAVMGPSGSGKTTLLECISRrKKTSSGNI----ACSSSTSFCE---------QEDALLGVMTVKETLKys 84
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIqfagQPLEAWSAAElarhraylsQQQTPPFAMPVFQYLT-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 85 arLSVP-HATSQVIEERVNAVIDGLGLHSVLnnriGTPIQRgISGGQKRRVSIACSLVQ-FPDI------LFLDEPTSGL 156
Cdd:PRK03695 92 --LHQPdKTRTEAVASALNEVAEALGLDDKL----GRSVNQ-LSGGEWQRVRLAAVVLQvWPDInpagqlLLLDEPMNSL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1625600662 157 DIstAHQVM--TAIKRMAvTHNIAVVATIHSPNweiFTL--FDKLLLLAKGETV 206
Cdd:PRK03695 165 DV--AQQAAldRLLSELC-QQGIAVVMSSHDLN---HTLrhADRVWLLKQGKLL 212
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
12-176 |
8.90e-13 |
|
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: 68.32 E-value: 8.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 12 RDILKQISGDVKPAEILAVMGPSGSGKTTLLECIS--RRKKTSSGNIacssstsFCEQEDALlgVMTVKEtlkySARLSV 89
Cdd:cd03217 13 KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMghPKYEVTEGEI-------LFKGEDIT--DLPPEE----RARLGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 90 PHAtSQVIEErvnavIDGLGLHSVLNNrigtpIQRGISGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTAHQVMTAIK 169
Cdd:cd03217 80 FLA-FQYPPE-----IPGVKNADFLRY-----VNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVIN 148
|
170
....*....|....*
gi 1625600662 170 RMA--------VTHN 176
Cdd:cd03217 149 KLReegksvliITHY 163
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
15-209 |
1.04e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 69.81 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 15 LKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSSTSFCEQEDALLgvmtvkETLKYSARLSVPHATS 94
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYI------RPVRKRIGMVFQFPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 95 QVIEERVNAVID------GLGLHSVLNNRIGTPIQRG------------ISGGQKRRVSIACSLVQFPDILFLDEPTSGL 156
Cdd:PRK13646 97 QLFEDTVEREIIfgpknfKMNLDEVKNYAHRLLMDLGfsrdvmsqspfqMSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1625600662 157 DISTAHQVMTAIKRMAVTHNIAVVATIHSPNwEIFTLFDKLLLLAKGETVFNS 209
Cdd:PRK13646 177 DPQSKRQVMRLLKSLQTDENKTIILVSHDMN-EVARYADEVIVMKEGSIVSQT 228
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
14-221 |
1.06e-12 |
|
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: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 14 ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSSTSfceqedALLGV-------MTVKETLKYSAR 86
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVS------ALLELgagfhpeLTGRENIYLNGR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 87 LsvpH-ATSQVIEERVNAVID--GLGLHsvlnnrIGTPIQRgISGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTAHQ 163
Cdd:COG1134 115 L---LgLSRKEIDEKFDEIVEfaELGDF------IDQPVKT-YSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKK 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1625600662 164 VMTAIKRMA--------VTHNIAVVAtihspnweifTLFDKLLLLAKGETVFNSKIDQLVPYFEEL 221
Cdd:COG1134 185 CLARIRELResgrtvifVSHSMGAVR----------RLCDRAIWLEKGRLVMDGDPEEVIAAYEAL 240
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
8-178 |
1.16e-12 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 69.30 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 8 NICYRD--ILKQISGDVKPAEILAVMGPSGSGKTTLLECISR-----RKKTSSGNIAcssstsfceqedaLLGV------ 74
Cdd:COG1117 18 NVYYGDkqALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRmndliPGARVEGEIL-------------LDGEdiydpd 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 75 ---------------------MTVKETLKYSARLsvpH--ATSQVIEERVNAVIDGLGLHSVLNNRIGTPiQRGISGGQK 131
Cdd:COG1117 85 vdvvelrrrvgmvfqkpnpfpKSIYDNVAYGLRL---HgiKSKSELDEIVEESLRKAALWDEVKDRLKKS-ALGLSGGQQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1625600662 132 RRVSIACSL-VQfPDILFLDEPTSGLD-ISTAH--QVMTAIKR----MAVTHNIA 178
Cdd:COG1117 161 QRLCIARALaVE-PEVLLMDEPTSALDpISTAKieELILELKKdytiVIVTHNMQ 214
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
7-184 |
1.27e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 68.69 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 7 NNICYR--------DILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACS-------SSTS-------- 63
Cdd:PRK11629 9 DNLCKRyqegsvqtDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNgqpmsklSSAAkaelrnqk 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 64 --FCEQEDALLGVMTVKETLkySARLSVPHATSQVIEERVNAVIDGLGLHSVLNNRigtpiQRGISGGQKRRVSIACSLV 141
Cdd:PRK11629 89 lgFIYQFHHLLPDFTALENV--AMPLLIGKKKPAEINSRALEMLAAVGLEHRANHR-----PSELSGGERQRVAIARALV 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1625600662 142 QFPDILFLDEPTSGLDISTAHQVMTAIKRMAVTHNIAVVATIH 184
Cdd:PRK11629 162 NNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTH 204
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-206 |
1.31e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 68.92 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 12 RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSSTSFCEQEDALLGVMTVKET----------- 80
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDAIKLRKEvgmvfqqpnpf 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 81 --LKYSARLSVPHATSQVIEER-----VNAVIDGLGLHSVLNNRIGTPIQRgISGGQKRRVSIACSLVQFPDILFLDEPT 153
Cdd:PRK14246 103 phLSIYDNIAYPLKSHGIKEKReikkiVEECLRKVGLWKEVYDRLNSPASQ-LSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1625600662 154 SGLDISTAHQVMTAIKRMavTHNIAVVATIHSPNwEIFTLFDKLLLLAKGETV 206
Cdd:PRK14246 182 SMIDIVNSQAIEKLITEL--KNEIAIVIVSHNPQ-QVARVADYVAFLYNGELV 231
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
8-204 |
1.33e-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: 67.07 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 8 NICYRDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIAcssstsfceqedaLLGVMTVKETLKYSARL 87
Cdd:cd03215 9 GLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEIT-------------LDGKPVTRRSPRDAIRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 88 SVPHatsqVIEERVNaviDGLGL-HSVLNNRIgtpIQRGISGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTAHQVMT 166
Cdd:cd03215 76 GIAY----VPEDRKR---EGLVLdLSVAENIA---LSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYR 145
|
170 180 190
....*....|....*....|....*....|....*...
gi 1625600662 167 AIKRMAvTHNIAVVaTIHSPNWEIFTLFDKLLLLAKGE 204
Cdd:cd03215 146 LIRELA-DAGKAVL-LISSELDELLGLCDRILVMYEGR 181
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
15-183 |
1.52e-12 |
|
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: 71.25 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 15 LKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKtSSGNIAcssstsFCEQEdalLGVMTVKETLKY----------- 83
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIR------FDGQD---LDGLSRRALRPLrrrmqvvfqdp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 84 ----SARLSV------------PHATSQVIEERVNAVIDGLGLHSVLNNRIgtPIQrgISGGQKRRVSIACSLVQFPDIL 147
Cdd:COG4172 372 fgslSPRMTVgqiiaeglrvhgPGLSAAERRARVAEALEEVGLDPAARHRY--PHE--FSGGQRQRIAIARALILEPKLL 447
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1625600662 148 FLDEPTSGLDISTAHQVMTAIKR------MA---VTHNIAVVATI 183
Cdd:COG4172 448 VLDEPTSALDVSVQAQILDLLRDlqrehgLAylfISHDLAVVRAL 492
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
12-160 |
2.28e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 70.86 E-value: 2.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 12 RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSST--SFCEQE-DALLGVMTVKETLKYSARls 88
Cdd:COG0488 328 KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVkiGYFDQHqEELDPDKTVLDELRDGAP-- 405
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1625600662 89 vphatsQVIEERVNAVIDGLGLHSvlnNRIGTPIqRGISGGQKRRVSIACSLVQFPDILFLDEPTSGLDIST 160
Cdd:COG0488 406 ------GGTEQEVRGYLGRFLFSG---DDAFKPV-GVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIET 467
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
14-177 |
2.85e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 68.19 E-value: 2.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 14 ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI---------------ACSSSTSFceqEDALLGV---M 75
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSIlidgkdvtklpeykrAKYIGRVF---QDPMMGTapsM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 76 TVKETL--------KYSARLSVPHATSQVIEERVNAVidGLGLhsvlNNRIGTPIqrG-ISGGQKRRVS-IACSLVQfPD 145
Cdd:COG1101 98 TIEENLalayrrgkRRGLRRGLTKKRRELFRELLATL--GLGL----ENRLDTKV--GlLSGGQRQALSlLMATLTK-PK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1625600662 146 ILFLDEPTSGLDISTAHQVMTAIKR---------MAVTHNI 177
Cdd:COG1101 169 LLLLDEHTAALDPKTAALVLELTEKiveennlttLMVTHNM 209
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-183 |
3.07e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 68.20 E-value: 3.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 12 RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGniacssstsFCEQEDALLG---VMTVKETLKYSARLS 88
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG---------YRYSGDVLLGgrsIFNYRDVLEFRRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 89 V----PHATSQVIEERV-------------------NAVIDGLGLHSVLNNRIGTPIQRgISGGQKRRVSIACSLVQFPD 145
Cdd:PRK14271 105 MlfqrPNPFPMSIMDNVlagvrahklvprkefrgvaQARLTEVGLWDAVKDRLSDSPFR-LSGGQQQLLCLARTLAVNPE 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1625600662 146 ILFLDEPTSGLDISTAHQVMTAIKRMA-------VTHNIAVVATI 183
Cdd:PRK14271 184 VLLLDEPTSALDPTTTEKIEEFIRSLAdrltviiVTHNLAQAARI 228
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
19-183 |
3.27e-12 |
|
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: 70.58 E-value: 3.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 19 SGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSSTSFCEQEDALLGVMTVKETLKYSARLSVPhaTSQVIE 98
Cdd:COG1245 360 GGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYKPQYISPDYDGTVEEFLRSANTDDFG--SSYYKT 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 99 ErvnaVIDGLGLHSVLNNRIgtpiqRGISGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTAHQVMTAIKRMA------ 172
Cdd:COG1245 438 E----IIKPLGLEKLLDKNV-----KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAenrgkt 508
|
170
....*....|....
gi 1625600662 173 ---VTHNIAVVATI 183
Cdd:COG1245 509 amvVDHDIYLIDYI 522
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-206 |
3.29e-12 |
|
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: 67.13 E-value: 3.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 4 IEWNNIC--YRD----ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIA-----CS--------SSTSF 64
Cdd:cd03244 3 IEFKNVSlrYRPnlppVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILidgvdISkiglhdlrSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 65 CEQEDALL-GvmTVKETL----KYSarlsvphatsqviEERVNAVIDGLGLHSVLNNRIG---TPIQRG---ISGGQKRR 133
Cdd:cd03244 83 IPQDPVLFsG--TIRSNLdpfgEYS-------------DEELWQALERVGLKEFVESLPGgldTVVEEGgenLSVGQRQL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1625600662 134 VSIACSLVQFPDILFLDEPTSGLDISTAHQVMTAIKRMAVTHNIAVVA----TIHSpnweiftlFDKLLLLAKGETV 206
Cdd:cd03244 148 LCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAhrldTIID--------SDRILVLDKGRVV 216
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
21-184 |
3.30e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 67.71 E-value: 3.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 21 DVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIAC--SSSTSFCEQEDALLGV------------MTVKETLK---- 82
Cdd:PRK11300 27 EVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLrgQHIEGLPGHQIARMGVvrtfqhvrlfreMTVIENLLvaqh 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 83 -------YSARLSVP---HATSQVIEeRVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLDEP 152
Cdd:PRK11300 107 qqlktglFSGLLKTPafrRAESEALD-RAATWLERVGLLEHANRQAGN-----LAYGQQRRLEIARCMVTQPEILMLDEP 180
|
170 180 190
....*....|....*....|....*....|..
gi 1625600662 153 TSGLDISTAHQVMTAIKRMAVTHNIAVVATIH 184
Cdd:PRK11300 181 AAGLNPKETKELDELIAELRNEHNVTVLLIEH 212
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-214 |
3.74e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 68.34 E-value: 3.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 4 IEWNNICYR-----DILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI---------------ACSSSTS 63
Cdd:PRK13636 6 LKVEELNYNysdgtHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIlfdgkpidysrkglmKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 64 FCEQE-DALLGVMTVKETLKYSA-RLSVPhatSQVIEERVNAVIDGLGLhSVLNNRigtPIQrGISGGQKRRVSIACSLV 141
Cdd:PRK13636 86 MVFQDpDNQLFSASVYQDVSFGAvNLKLP---EDEVRKRVDNALKRTGI-EHLKDK---PTH-CLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1625600662 142 QFPDILFLDEPTSGLDISTAHQVMTAIKRMAVTHNIAVVATIHspNWEIFTLF-DKLLLLAKGETVFNSKIDQL 214
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATH--DIDIVPLYcDNVFVMKEGRVILQGNPKEV 229
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
15-180 |
3.91e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 67.45 E-value: 3.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 15 LKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSS--TSFCEQEDALLGV------------MTVKET 80
Cdd:COG4674 26 LNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTdlTGLDEHEIARLGIgrkfqkptvfeeLTVFEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 81 L------KYSARLSVPHATSQVIEERVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLDEPTS 154
Cdd:COG4674 106 LelalkgDRGVFASLFARLTAEERDRIEEVLETIGLTDKADRLAGL-----LSHGQKQWLEIGMLLAQDPKLLLLDEPVA 180
|
170 180
....*....|....*....|....*....
gi 1625600662 155 GLdisTAHQVM-TA--IKRMAVTHNIAVV 180
Cdd:COG4674 181 GM---TDAETErTAelLKSLAGKHSVVVV 206
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
14-202 |
3.92e-12 |
|
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: 65.64 E-value: 3.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 14 ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIacssstSFCEQEDAL-------LGVMTVKETLKYsar 86
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI------GMPEGEDLLflpqrpyLPLGTLREQLIY--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 87 lsvphatsqvieervnavidglglhsvlnnrigtPIQRGISGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTAHQVMt 166
Cdd:cd03223 87 ----------------------------------PWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLY- 131
|
170 180 190
....*....|....*....|....*....|....*.
gi 1625600662 167 aikRMAVTHNIAVVATIHSPnwEIFTLFDKLLLLAK 202
Cdd:cd03223 132 ---QLLKELGITVISVGHRP--SLWKFHDRVLDLDG 162
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
14-203 |
4.77e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 69.10 E-value: 4.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 14 ILKQISGDVKPAEILAVMGPSGSGKTTLLECISrrkktssGNIACSSSTSFCEQEDAllGVMTVKETLKYSArlSVPHAT 93
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAIN-------GTLTPTAGTVLVAGDDV--EALSARAASRRVA--SVPQDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 94 SQVIEERVNAVIDgLGLHSVLN-----------------NRIGT------PIQRgISGGQKRRVSIACSLVQFPDILFLD 150
Cdd:PRK09536 87 SLSFEFDVRQVVE-MGRTPHRSrfdtwtetdraaveramERTGVaqfadrPVTS-LSGGERQRVLLARALAQATPVLLLD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1625600662 151 EPTSGLDIStaHQVMT-AIKRMAVTHNIAVVATIHSPNWEIfTLFDKLLLLAKG 203
Cdd:PRK09536 165 EPTASLDIN--HQVRTlELVRRLVDDGKTAVAAIHDLDLAA-RYCDELVLLADG 215
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
20-176 |
6.19e-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: 66.66 E-value: 6.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 20 GDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSST-SFCEQEDALLGVMTVKETLkySARLSVPHATSQVIE 98
Cdd:cd03237 20 GSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTvSYKPQYIKADYEGTVRDLL--SSITKDFYTHPYFKT 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1625600662 99 ErvnaVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTAHQVMTAIKRMAVTHN 176
Cdd:cd03237 98 E----IAKPLQIEQILDREVPE-----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNE 166
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
13-181 |
6.74e-12 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 69.75 E-value: 6.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 13 DILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSG-------NIACSSSTS----------FCEQEDALLGVM 75
Cdd:PRK10535 22 EVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGtyrvagqDVATLDADAlaqlrrehfgFIFQRYHLLSHL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 76 TVKETLKYSARLS-VPHATSQvieERVNAVIDGLGLHSVLNNRigtPIQrgISGGQKRRVSIACSLVQFPDILFLDEPTS 154
Cdd:PRK10535 102 TAAQNVEVPAVYAgLERKQRL---LRAQELLQRLGLEDRVEYQ---PSQ--LSGGQQQRVSIARALMNGGQVILADEPTG 173
|
170 180 190
....*....|....*....|....*....|....*
gi 1625600662 155 GLDISTAHQVMTAIKRMA--------VTHNIAVVA 181
Cdd:PRK10535 174 ALDSHSGEEVMAILHQLRdrghtviiVTHDPQVAA 208
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
11-215 |
7.15e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 67.93 E-value: 7.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 11 YRD--ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI------------ACSSSTSFCEQEDALLGVMT 76
Cdd:PRK13536 51 YGDkaVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItvlgvpvpararLARARIGVVPQFDNLDLEFT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 77 VKETLKYSARLSVPHAtsqvieERVNAVIDGLGLHSVLNNRIGTPIQRgISGGQKRRVSIACSLVQFPDILFLDEPTSGL 156
Cdd:PRK13536 131 VRENLLVFGRYFGMST------REIEAVIPSLLEFARLESKADARVSD-LSGGMKRRLTLARALINDPQLLILDEPTTGL 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1625600662 157 DISTAHQVMTAIkRMAVTHNIAVVATIHSPNwEIFTLFDKLLLLAKGETVFNSKIDQLV 215
Cdd:PRK13536 204 DPHARHLIWERL-RSLLARGKTILLTTHFME-EAERLCDRLCVLEAGRKIAEGRPHALI 260
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
4-215 |
8.87e-12 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 69.22 E-value: 8.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 4 IEWNNICY-----RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIAC---------------SSSTS 63
Cdd:PRK13657 335 VEFDDVSFsydnsRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIdgtdirtvtraslrrNIAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 64 FceqEDALLGVMTVKETLkysaRLSVPHATSQVIE---ERVNAV------IDGLglhsvlNNRIGtpiQRG--ISGGQKR 132
Cdd:PRK13657 415 F---QDAGLFNRSIEDNI----RVGRPDATDEEMRaaaERAQAHdfierkPDGY------DTVVG---ERGrqLSGGERQ 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 133 RVSIACSLVQFPDILFLDEPTSGLDISTAHQVMTAIKrmAVTHN-----IA-VVATIHSPnweiftlfDKLLLLAKGETV 206
Cdd:PRK13657 479 RLAIARALLKDPPILILDEATSALDVETEAKVKAALD--ELMKGrttfiIAhRLSTVRNA--------DRILVFDNGRVV 548
|
....*....
gi 1625600662 207 FNSKIDQLV 215
Cdd:PRK13657 549 ESGSFDELV 557
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
26-183 |
1.21e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 67.42 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 26 EILAVMGPSGSGKTTLLECISRRKKTSSGNIAC--SSSTSFCEQE-------------DALLGV---MTVKETLKYSARL 87
Cdd:PRK15079 48 ETLGVVGESGCGKSTFARAIIGLVKATDGEVAWlgKDLLGMKDDEwravrsdiqmifqDPLASLnprMTIGEIIAEPLRT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 88 SVPHATSQVIEERVNAVIDGLGLHSVLNNRIgtPIQrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTAHQVMTA 167
Cdd:PRK15079 128 YHPKLSRQEVKDRVKAMMLKVGLLPNLINRY--PHE--FSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNL 203
|
170 180
....*....|....*....|....*
gi 1625600662 168 IKRMA---------VTHNIAVVATI 183
Cdd:PRK15079 204 LQQLQremglslifIAHDLAVVKHI 228
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-206 |
1.33e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 66.09 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 13 DILKQISGDVKPAEILAVMGPSGSGKTTLLECISR-----RKKTSSGNIACSSSTSFCEQEDAL-------------LGV 74
Cdd:PRK14247 17 EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielyPEARVSGEVYLDGQDIFKMDVIELrrrvqmvfqipnpIPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 75 MTVKETLKYSARLSVPHATSQVIEERVNAVIDGLGLHSVLNNRIGTPIQRgISGGQKRRVSIACSLVQFPDILFLDEPTS 154
Cdd:PRK14247 97 LSIFENVALGLKLNRLVKSKKELQERVRWALEKAQLWDEVKDRLDAPAGK-LSGGQQQRLCIARALAFQPEVLLADEPTA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1625600662 155 GLD-ISTA--HQVMTAIKRmavthNIAVVATIHSPNwEIFTLFDKLLLLAKGETV 206
Cdd:PRK14247 176 NLDpENTAkiESLFLELKK-----DMTIVLVTHFPQ-QAARISDYVAFLYKGQIV 224
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-206 |
1.38e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 66.25 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 4 IEWNNICYR-----DILKQISGDVKPAEILAVMGPSGSGKTTLL------------------ECISRRKKtssGNIACSS 60
Cdd:PRK13639 2 LETRDLKYSypdgtEALKGINFKAEKGEMVALLGPNGAGKSTLFlhfngilkptsgevlikgEPIKYDKK---SLLEVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 61 STSFCEQE-DALLGVMTVKETLKYSA-RLSVPHatsQVIEERVNAVIDGLGLHSVLNnrigTPIQRgISGGQKRRVSIAC 138
Cdd:PRK13639 79 TVGIVFQNpDDQLFAPTVEEDVAFGPlNLGLSK---EEVEKRVKEALKAVGMEGFEN----KPPHH-LSGGQKKRVAIAG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1625600662 139 SLVQFPDILFLDEPTSGLDISTAHQVMTAIKRMAvTHNIAVVATIHSPNWeIFTLFDKLLLLAKGETV 206
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLN-KEGITIIISTHDVDL-VPVYADKVYVMSDGKII 216
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-182 |
1.52e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 65.42 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 1 MSpIEWNNI-CY---RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSG--NIACSS---STSFCEQEDAL 71
Cdd:PRK11124 1 MS-IQLNGInCFygaHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGtlNIAGNHfdfSKTPSDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 72 L----GV----------MTVKETLkYSARLSVPHATSQVIEERVNAVIDGLGLhSVLNNRIgtPIQrgISGGQKRRVSIA 137
Cdd:PRK11124 80 LrrnvGMvfqqynlwphLTVQQNL-IEAPCRVLGLSKDQALARAEKLLERLRL-KPYADRF--PLH--LSGGQQQRVAIA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1625600662 138 CSLVQFPDILFLDEPTSGLDISTAHQVMTAIKRMAVTHNIAVVAT 182
Cdd:PRK11124 154 RALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVT 198
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
29-187 |
1.67e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 65.78 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 29 AVMGPSGSGKTTLLECISRRKKTSSGNIACSSS--TSFCEQEDA----LL-------GVMTVKETLkysARLSVPHAT-- 93
Cdd:PRK10253 37 AIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEhiQHYASKEVArrigLLaqnattpGDITVQELV---ARGRYPHQPlf 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 94 ---SQVIEERVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTAHQVMTAIKR 170
Cdd:PRK10253 114 trwRKEDEEAVTKAMQATGITHLADQSVDT-----LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSE 188
|
170
....*....|....*..
gi 1625600662 171 MAVTHNIAVVATIHSPN 187
Cdd:PRK10253 189 LNREKGYTLAAVLHDLN 205
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-162 |
1.78e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 66.37 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 2 SPIEWNNI--CYRD--ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIA-CSSS-----------TSFC 65
Cdd:PRK13537 6 APIDFRNVekRYGDklVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISlCGEPvpsrarharqrVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 66 EQEDALLGVMTVKETLKYSAR---LSvphatSQVIEERVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQ 142
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLVFGRyfgLS-----AAAARALVPPLLEFAKLENKADAKVGE-----LSGGMKRRLTLARALVN 155
|
170 180
....*....|....*....|
gi 1625600662 143 FPDILFLDEPTSGLDISTAH 162
Cdd:PRK13537 156 DPDVLVLDEPTTGLDPQARH 175
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
14-221 |
1.82e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 67.95 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 14 ILKQISGDVKPAEILAVMGPSGSGKTTLLECISrrkktssGNIACSSS-----TSFCE--------------QEDALLgv 74
Cdd:PRK11174 365 LAGPLNFTLPAGQRIALVGPSGAGKTSLLNALL-------GFLPYQGSlkingIELREldpeswrkhlswvgQNPQLP-- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 75 mtvKETLKYSARLSVPHATsqviEERVNAVIDGLGLH---SVLNNRIGTPIQ---RGISGGQKRRVSIACSLVQFPDILF 148
Cdd:PRK11174 436 ---HGTLRDNVLLGNPDAS----DEQLQQALENAWVSeflPLLPQGLDTPIGdqaAGLSVGQAQRLALARALLQPCQLLL 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 149 LDEPTSGLDISTAHQVMTAIKRMA-------VTHNIavvatihspnwEIFTLFDKLLLLAKGETVFNSKIDQLV---PYF 218
Cdd:PRK11174 509 LDEPTASLDAHSEQLVMQALNAASrrqttlmVTHQL-----------EDLAQWDQIWVMQDGQIVQQGDYAELSqagGLF 577
|
...
gi 1625600662 219 EEL 221
Cdd:PRK11174 578 ATL 580
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
12-157 |
2.12e-11 |
|
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: 67.65 E-value: 2.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 12 RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSSTS--FCEQEDAL-----------LGVMTVK 78
Cdd:TIGR03719 18 KEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKvgYLPQEPQLdptktvrenveEGVAEIK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 79 ETLK----YSARLSVPHAT-SQVIEE--RVNAVIDGLGLHSvLNNRI------------GTPIQRgISGGQKRRVSIACS 139
Cdd:TIGR03719 98 DALDrfneISAKYAEPDADfDKLAAEqaELQEIIDAADAWD-LDSQLeiamdalrcppwDADVTK-LSGGERRRVALCRL 175
|
170
....*....|....*...
gi 1625600662 140 LVQFPDILFLDEPTSGLD 157
Cdd:TIGR03719 176 LLSKPDMLLLDEPTNHLD 193
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
19-183 |
2.38e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 67.53 E-value: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 19 SGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSSTSFCEQEdalLGV---MTVKETL-KYSARLSvphaTS 94
Cdd:PRK13409 359 GGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQY---IKPdydGTVEDLLrSITDDLG----SS 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 95 QVIEErvnaVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTAHQVMTAIKRMA-- 172
Cdd:PRK13409 432 YYKSE----IIKPLQLERLLDKNVKD-----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAee 502
|
170
....*....|....*...
gi 1625600662 173 -------VTHNIAVVATI 183
Cdd:PRK13409 503 reatalvVDHDIYMIDYI 520
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-206 |
3.46e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 65.21 E-value: 3.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 1 MSPIEWNNICY-----RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSST------------- 62
Cdd:PRK13652 1 MHLIETRDLCYsysgsKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPitkenirevrkfv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 63 --SFCEQEDALLGVmTVKETLKYS-ARLSVPHATsqvIEERVNAVIDGLGLHSVLnnrigTPIQRGISGGQKRRVSIACS 139
Cdd:PRK13652 81 glVFQNPDDQIFSP-TVEQDIAFGpINLGLDEET---VAHRVSSALHMLGLEELR-----DRVPHHLSGGEKKRVAIAGV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1625600662 140 LVQFPDILFLDEPTSGLDISTAHQVMTAIKRMAVTHNIAVVATIHSPNWeIFTLFDKLLLLAKGETV 206
Cdd:PRK13652 152 IAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDL-VPEMADYIYVMDKGRIV 217
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
12-176 |
3.70e-11 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 64.32 E-value: 3.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 12 RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKK--TSSGNIacssstsFCEQED---------ALLGV------ 74
Cdd:COG0396 13 KEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSI-------LLDGEDilelspderARAGIflafqy 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 75 ------MTVKETLK--YSARLSVPHATSQVIEErVNAVIDGLGLHSVLNNRigtPIQRGISGGQKRRVSIACSLVQFPDI 146
Cdd:COG0396 86 pveipgVSVSNFLRtaLNARRGEELSAREFLKL-LKEKMKELGLDEDFLDR---YVNEGFSGGEKKRNEILQMLLLEPKL 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 1625600662 147 LFLDEPTSGLDISTAHQVMTAIKRMA--------VTHN 176
Cdd:COG0396 162 AILDETDSGLDIDALRIVAEGVNKLRspdrgiliITHY 199
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
15-204 |
4.14e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 65.04 E-value: 4.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 15 LKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI-----ACSSST----------SFCEQEDALLGVmTVKE 79
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTItvggmVLSEETvwdvrrqvgmVFQNPDNQFVGA-TVQD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 80 TLKYS-ARLSVPHATSQvieERVNAVIDGLGLHSVLNNRigtPIQrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLDI 158
Cdd:PRK13635 102 DVAFGlENIGVPREEMV---ERVDQALRQVGMEDFLNRE---PHR--LSGGQKQRVAIAGVLALQPDIIILDEATSMLDP 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1625600662 159 STAHQVMTAIKRMAVTHNIAVVATIHSPNWEIFTlfDKLLLLAKGE 204
Cdd:PRK13635 174 RGRREVLETVRQLKEQKGITVLSITHDLDEAAQA--DRVIVMNKGE 217
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
14-207 |
4.20e-11 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 63.71 E-value: 4.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 14 ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSSTSfceqedALLGV-------MTVKETLKYSAR 86
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS------SLLGLgggfnpeLTGRENIYLNGR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 87 LSvpHATSQVIEERVNAVIDglglHSVLNNRIGTPIqRGISGGQKRRVSIACSLVQFPDILFLDEPTSGLDIST---AHQ 163
Cdd:cd03220 111 LL--GLSRKEIDEKIDEIIE----FSELGDFIDLPV-KTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFqekCQR 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1625600662 164 VMTAIKRMAVThniAVVATiHSPNwEIFTLFDKLLLLAKGETVF 207
Cdd:cd03220 184 RLRELLKQGKT---VILVS-HDPS-SIKRLCDRALVLEKGKIRF 222
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
12-226 |
4.51e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 64.85 E-value: 4.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 12 RDILKQISGDVKPAEILAVMGPSGSGKTTLL--------ECISRRKKTSSGNIACSSSTSFCEQEDALLGVMTV-----K 78
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLkalagdltGGGAPRGARVTGDVTLNGEPLAAIDAPRLARLRAVlpqaaQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 79 ETLKYSARLSV-----PHA-----TSQVIEERVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQF----- 143
Cdd:PRK13547 94 PAFAFSAREIVllgryPHArragaLTHRDGEIAWQALALAGATALVGRDVTT-----LSGGELARVQFARVLAQLwpphd 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 144 ----PDILFLDEPTSGLDISTAHQVMTAIKRMAVTHNIAVVATIHSPNWEIfTLFDKLLLLAKGETVFN-SKIDQLVPYF 218
Cdd:PRK13547 169 aaqpPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAA-RHADRIAMLADGAIVAHgAPADVLTPAH 247
|
....*...
gi 1625600662 219 EELGYNFP 226
Cdd:PRK13547 248 IARCYGFA 255
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
12-204 |
5.81e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 64.31 E-value: 5.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 12 RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSSTSFCEQEDALLgvmtvketLKYSARLsVPH 91
Cdd:PRK11247 25 RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRL--------MFQDARL-LPW 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 92 ATsqvieervnaVID--GLGL------------HSV-LNNRIGT-PIqrGISGGQKRRVSIACSLVQFPDILFLDEPTSG 155
Cdd:PRK11247 96 KK----------VIDnvGLGLkgqwrdaalqalAAVgLADRANEwPA--ALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1625600662 156 LDISTAHQVMTAIKRMAVTHNIAVVATIHSPNwEIFTLFDKLLLLAKGE 204
Cdd:PRK11247 164 LDALTRIEMQDLIESLWQQHGFTVLLVTHDVS-EAVAMADRVLLIEEGK 211
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
125-260 |
6.13e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 64.87 E-value: 6.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 125 GISGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTAHQVMTAIKRmAVTHNIAVVATIHSPNwEIFTLFDKLLLLAKGE 204
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTME-HVLEVADEVIVMDKGK 253
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1625600662 205 TVFNSKidqlvPY---FEELGYNFPKFSNP--VDVVMELINTD--FEK---QDSKSIEEGTSSFNR 260
Cdd:PRK13631 254 ILKTGT-----PYeifTDQHIINSTSIQVPrvIQVINDLIKKDpkYKKlyqKQPRTIEQLADAINE 314
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
14-181 |
7.33e-11 |
|
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: 65.86 E-value: 7.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 14 ILKQISGDVKPAEILAVMGPSGSGKT-T------LLecisrrkktSSGNIACSSSTSFCEQ------EDALLGV------ 74
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSvTalsilrLL---------PDPAAHPSGSILFDGQdllglsERELRRIrgnria 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 75 ------MT-----------VKETLKYSARLSVPHATSQVIE--ERVnavidglGLHSVlNNRIGT-PIQrgISGGQKRRV 134
Cdd:COG4172 96 mifqepMTslnplhtigkqIAEVLRLHRGLSGAAARARALEllERV-------GIPDP-ERRLDAyPHQ--LSGGQRQRV 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1625600662 135 SIACSLVQFPDILFLDEPTSGLDISTAHQVMTAIKR------MAV---THNIAVVA 181
Cdd:COG4172 166 MIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDlqrelgMALlliTHDLGVVR 221
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
15-206 |
1.14e-10 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 64.67 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 15 LKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSG-------NIACSSSTSFCE----------QEDALLGVMTV 77
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGqvlidgvDIAKISDAELREvrrkkiamvfQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 78 KETLKYSARLSVPHAtsqviEERVNAVIDGLGLHSVLNNRIGTPIQrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLD 157
Cdd:PRK10070 124 LDNTAFGMELAGINA-----EERREKALDALRQVGLENYAHSYPDE--LSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1625600662 158 ISTAHQVMTAIKRMAVTHNIAVVATIHSPNwEIFTLFDKLLLLAKGETV 206
Cdd:PRK10070 197 PLIRTEMQDELVKLQAKHQRTIVFISHDLD-EAMRIGDRIAIMQNGEVV 244
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
4-253 |
1.17e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 63.60 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 4 IEWNNICYR-------DILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSS---------------S 61
Cdd:PRK13650 5 IEVKNLTFKykedqekYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGdllteenvwdirhkiG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 62 TSFCEQEDALLGVmTVKETLKYS-ARLSVPHatsQVIEERVNAVIDGLGLhSVLNNRigTPIQrgISGGQKRRVSIACSL 140
Cdd:PRK13650 85 MVFQNPDNQFVGA-TVEDDVAFGlENKGIPH---EEMKERVNEALELVGM-QDFKER--EPAR--LSGGQKQRVAIAGAV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 141 VQFPDILFLDEPTSGLDISTAHQVMTAIKRMAVTHNIAVVATIHspNWEIFTLFDKLLLLAKGETVFNSKIDQLVPYFEE 220
Cdd:PRK13650 156 AMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITH--DLDEVALSDRVLVMKNGQVESTSTPRELFSRGND 233
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1625600662 221 L---GYNFPkFSNpvDVVMELINTDFEKQDS----KSIEE 253
Cdd:PRK13650 234 LlqlGLDIP-FTT--SLVQSLRQNGYDLPEGylteKELEE 270
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
11-206 |
1.29e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 63.49 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 11 YRD--ILKQISGDVKPAEILAVMGPSGSGKTTLLECIS---RRKK------------TSSGNIACSSSTSFCEQE-DALL 72
Cdd:PRK13638 11 YQDepVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSgllRPQKgavlwqgkpldySKRGLLALRQQVATVFQDpEQQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 73 GVMTVKETLKYSAR-LSVPHATsqvIEERVNaviDGLGLHSVLNNRiGTPIQrGISGGQKRRVSIACSLVQFPDILFLDE 151
Cdd:PRK13638 91 FYTDIDSDIAFSLRnLGVPEAE---ITRRVD---EALTLVDAQHFR-HQPIQ-CLSHGQKKRVAIAGALVLQARYLLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1625600662 152 PTSGLDISTAHQVMTAIKRMAVTHNIAVVATiHSPNWeIFTLFDKLLLLAKGETV 206
Cdd:PRK13638 163 PTAGLDPAGRTQMIAIIRRIVAQGNHVIISS-HDIDL-IYEISDAVYVLRQGQIL 215
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
14-164 |
2.03e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 62.10 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 14 ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIAC-----------------SSSTSFCEQEDALLGVMT 76
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLvgqplhqmdeearaklrAKHVGFVFQSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 77 VKETLKYSARLSvpHATSQVIEERVNAVIDGLGLHSVLNNrigTPIQrgISGGQKRRVSIACSLVQFPDILFLDEPTSGL 156
Cdd:PRK10584 105 ALENVELPALLR--GESSRQSRNGAKALLEQLGLGKRLDH---LPAQ--LSGGEQQRVALARAFNGRPDVLFADEPTGNL 177
|
....*...
gi 1625600662 157 DISTAHQV 164
Cdd:PRK10584 178 DRQTGDKI 185
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
13-157 |
2.50e-10 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 62.13 E-value: 2.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 13 DILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSST-SFCEQEDALLGVMTVKETLKYSARLSV-- 89
Cdd:COG4598 22 EVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEiRLKPDRDGELVPADRRQLQRIRTRLGMvf 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 90 ------PHAT--SQVIE--------------ERVNAVIDGLGLHSVlnnRIGTPIQrgISGGQKRRVSIACSLVQFPDIL 147
Cdd:COG4598 102 qsfnlwSHMTvlENVIEapvhvlgrpkaeaiERAEALLAKVGLADK---RDAYPAH--LSGGQQQRAAIARALAMEPEVM 176
|
170
....*....|
gi 1625600662 148 FLDEPTSGLD 157
Cdd:COG4598 177 LFDEPTSALD 186
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-216 |
2.61e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 63.20 E-value: 2.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 4 IEWNNICYR----DILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIacssstsFCEQED---------- 69
Cdd:PRK11432 7 VVLKNITKRfgsnTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQI-------FIDGEDvthrsiqqrd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 70 --------ALLGVMTVKETLKYSAR-LSVPHATsqvIEERVN---AVIDGLGLHSVLNNRigtpiqrgISGGQKRRVSIA 137
Cdd:PRK11432 80 icmvfqsyALFPHMSLGENVGYGLKmLGVPKEE---RKQRVKealELVDLAGFEDRYVDQ--------ISGGQQQRVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1625600662 138 CSLVQFPDILFLDEPTSGLDISTAHQVMTAIKRMAVTHNIAVVATIHSPNwEIFTLFDKLLLLAKGetvfnsKIDQLVP 216
Cdd:PRK11432 149 RALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQS-EAFAVSDTVIVMNKG------KIMQIGS 220
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
12-185 |
3.43e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 62.34 E-value: 3.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 12 RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSSTSFCEQEDALLGVMTVK------------- 78
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKPLRKKvgivfqfpehqlf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 79 -ET-LKYSA----RLSVPHATSqviEERVNAVIDGLGL-HSVLNNrigTPIQrgISGGQKRRVSIACSLVQFPDILFLDE 151
Cdd:PRK13634 100 eETvEKDICfgpmNFGVSEEDA---KQKAREMIELVGLpEELLAR---SPFE--LSGGQMRRVAIAGVLAMEPEVLVLDE 171
|
170 180 190
....*....|....*....|....*....|....
gi 1625600662 152 PTSGLDISTAHQVMTAIKRMAVTHNIAVVATIHS 185
Cdd:PRK13634 172 PTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHS 205
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-207 |
4.11e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 61.40 E-value: 4.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 14 ILKQISGDVKPAEILAVMGPSGSGKTTLLECISR-----RKKTSSGNIACSSSTSFCEQEDAL-----LGV--------- 74
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRllelnEEARVEGEVRLFGRNIYSPDVDPIevrreVGMvfqypnpfp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 75 -MTVKETLKYSARLSVPHATSQVIEERVNAVIDGLGLHSVLNNRIGT-PIQrgISGGQKRRVSIACSLVQFPDILFLDEP 152
Cdd:PRK14267 99 hLTIYDNVAIGVKLNGLVKSKKELDERVEWALKKAALWDEVKDRLNDyPSN--LSGGQRQRLVIARALAMKPKILLMDEP 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1625600662 153 TSGLDISTAHQVMTAIKRMAVTHNIAVVAtiHSP-------NWEIFTLFDKLLLLAKGETVF 207
Cdd:PRK14267 177 TANIDPVGTAKIEELLFELKKEYTIVLVT--HSPaqaarvsDYVAFLYLGKLIEVGPTRKVF 236
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
13-227 |
5.49e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 63.34 E-value: 5.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 13 DILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSS---------STSFCEQEDA------------- 70
Cdd:PRK10261 30 AAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqVIELSEQSAAqmrhvrgadmami 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 71 -------LLGVMTVKETLKYSARLsvpHATSQVIEERVNA--VIDGLGL---HSVLNNrigTPIQrgISGGQKRRVSIAC 138
Cdd:PRK10261 110 fqepmtsLNPVFTVGEQIAESIRL---HQGASREEAMVEAkrMLDQVRIpeaQTILSR---YPHQ--LSGGMRQRVMIAM 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 139 SLVQFPDILFLDEPTSGLDISTAHQVMTAIK------RMAV---THNIAVVATIHspnweiftlfDKLLLLAKGETVFNS 209
Cdd:PRK10261 182 ALSCRPAVLIADEPTTALDVTIQAQILQLIKvlqkemSMGVifiTHDMGVVAEIA----------DRVLVMYQGEAVETG 251
|
250 260
....*....|....*....|...
gi 1625600662 210 KIDQLV-----PYFEELGYNFPK 227
Cdd:PRK10261 252 SVEQIFhapqhPYTRALLAAVPQ 274
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
15-181 |
5.99e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 61.38 E-value: 5.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 15 LKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSG--NIACSSSTS-------------------FCEQEdalLG 73
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGtiTIAGYHITPetgnknlkklrkkvslvfqFPEAQ---LF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 74 VMTVKETLKYSARLSvpHATSQVIEERVNAVIDGLGLHSVLNNRigTPIQrgISGGQKRRVSIACSLVQFPDILFLDEPT 153
Cdd:PRK13641 100 ENTVLKDVEFGPKNF--GFSEDEAKEKALKWLKKVGLSEDLISK--SPFE--LSGGQMRRVAIAGVMAYEPEILCLDEPA 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 1625600662 154 SGLDISTAHQVMTAIKR--------MAVTHNIAVVA 181
Cdd:PRK13641 174 AGLDPEGRKEMMQLFKDyqkaghtvILVTHNMDDVA 209
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
9-203 |
6.74e-10 |
|
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: 63.49 E-value: 6.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 9 ICYRDILKQISGDVKPA-----------EILAVMGPSGSGKTTLLECISRRKKTSSGNI------------ACSSSTSFC 65
Cdd:TIGR01257 929 VCVKNLVKIFEPSGRPAvdrlnitfyenQITAFLGHNGAGKTTTLSILTGLLPPTSGTVlvggkdietnldAVRQSLGMC 1008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 66 EQEDALLGVMTVKETLKYSARLSVPHATSQVIEerVNAVIDGLGLHSVLNNRigtpiQRGISGGQKRRVSIACSLVQFPD 145
Cdd:TIGR01257 1009 PQHNILFHHLTVAEHILFYAQLKGRSWEEAQLE--MEAMLEDTGLHHKRNEE-----AQDLSGGMQRKLSVAIAFVGDAK 1081
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1625600662 146 ILFLDEPTSGLDISTAHQVMTAIKRMAVTHNIaVVATIHSPNWEIftLFDKLLLLAKG 203
Cdd:TIGR01257 1082 VVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTI-IMSTHHMDEADL--LGDRIAIISQG 1136
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
15-184 |
7.53e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 60.92 E-value: 7.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 15 LKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI----ACSSSTSFCEQEDALLGVMT------VKETLKYS 84
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnQAITDDNFEKLRKHIGIVFQnpdnqfVGSIVKYD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 85 ARL-----SVPHATSQvieERVNAVIDGLGLhsvLNNRIGTPiqRGISGGQKRRVSIACSLVQFPDILFLDEPTSGLDIS 159
Cdd:PRK13648 105 VAFglenhAVPYDEMH---RRVSEALKQVDM---LERADYEP--NALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPD 176
|
170 180
....*....|....*....|....*
gi 1625600662 160 TAHQVMTAIKRMAVTHNIAVVATIH 184
Cdd:PRK13648 177 ARQNLLDLVRKVKSEHNITIISITH 201
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
15-183 |
7.58e-10 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 60.14 E-value: 7.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 15 LKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSSTSFCE----QEDALLGVMtvKETLKY------- 83
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDlaqaSPREILALR--RRTIGYvsqflrv 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 84 ----SAR---------LSVPHATSqviEERVNAVIDGLGLHSVL-NNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFL 149
Cdd:COG4778 105 iprvSALdvvaeplleRGVDREEA---RARARELLARLNLPERLwDLPPAT-----FSGGEQQRVNIARGFIADPPLLLL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1625600662 150 DEPTSGLDISTAHQVM----------TAIkrMAVTHNIAVVATI 183
Cdd:COG4778 177 DEPTASLDAANRAVVVelieeakargTAI--IGIFHDEEVREAV 218
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
15-206 |
7.82e-10 |
|
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: 58.59 E-value: 7.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 15 LKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIacssstSFCEQEdallgvmtvketlkySARLSVPHAts 94
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEI------LVDGKE---------------VSFASPRDA-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 95 qvieervnavidglglhsvLNNRIGTPIQrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTAHQVMTAIKRMA-- 172
Cdd:cd03216 73 -------------------RRAGIAMVYQ--LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRaq 131
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1625600662 173 ------VTHNIAvvatihspnwEIFTLFDKLLLLAKGETV 206
Cdd:cd03216 132 gvavifISHRLD----------EVFEIADRVTVLRDGRVV 161
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
26-174 |
2.03e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 60.62 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 26 EILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSS-----------TSFCEQEDALLGVMTVKETLKYSARLS-VPHAT 93
Cdd:PRK11607 46 EIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVdlshvppyqrpINMMFQSYALFPHMTVEQNIAFGLKQDkLPKAE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 94 sqvIEERVNAVidgLGLHSVLNNRIGTPIQrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLDIS----TAHQVMTAIK 169
Cdd:PRK11607 126 ---IASRVNEM---LGLVHMQEFAKRKPHQ--LSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKlrdrMQLEVVDILE 197
|
....*
gi 1625600662 170 RMAVT 174
Cdd:PRK11607 198 RVGVT 202
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
4-242 |
2.58e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 59.33 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 4 IEWNNICYRDI----------LKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSS-STSFCEQ----- 67
Cdd:PRK13633 5 IKCKNVSYKYEsneesteklaLDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGlDTSDEENlwdir 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 68 ---------EDALLGVMTVKETLKYSAR-LSVPhatSQVIEERVNAVIDGLGLHSVlnnRIGTPiqRGISGGQKRRVSIA 137
Cdd:PRK13633 85 nkagmvfqnPDNQIVATIVEEDVAFGPEnLGIP---PEEIRERVDESLKKVGMYEY---RRHAP--HLLSGGQKQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 138 CSLVQFPDILFLDEPTSGLDISTAHQVMTAIKRMAVTHNIAVVATIHSpnWEIFTLFDKLLLLAKGETVFN--------- 208
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHY--MEEAVEADRIIVMDSGKVVMEgtpkeifke 234
|
250 260 270
....*....|....*....|....*....|....*...
gi 1625600662 209 ----SKIDQLVPYFEELGYNFPKfsNPVDVVMELINTD 242
Cdd:PRK13633 235 vemmKKIGLDVPQVTELAYELKK--EGVDIPSDILTID 270
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
15-206 |
3.19e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 60.57 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 15 LKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI--------------ACSSSTSFCEQEDALLGVMTVKET 80
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTItinninynkldhklAAQLGIGIIYQELSVIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 81 LkYSARL------SVPHATSQVIEERVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLDEPTS 154
Cdd:PRK09700 101 L-YIGRHltkkvcGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVAN-----LSISHKQMLEIAKTLMLDAKVIIMDEPTS 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1625600662 155 GLDISTAHQVMtAIKRMAVTHNIAVVATIHSPNwEIFTLFDKLLLLAKGETV 206
Cdd:PRK09700 175 SLTNKEVDYLF-LIMNQLRKEGTAIVYISHKLA-EIRRICDRYTVMKDGSSV 224
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-226 |
3.78e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 58.85 E-value: 3.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 1 MSPIEWNNICYRD---ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI------ACSSST--------- 62
Cdd:PRK13644 1 MIRLENVSYSYPDgtpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlvsgidTGDFSKlqgirklvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 63 -SFCEQEDALLGvMTVKETLKYSAR-LSVPHATsqvIEERVNAVIDGLGLHSVlnnRIGTPiqRGISGGQKRRVSIACSL 140
Cdd:PRK13644 81 iVFQNPETQFVG-RTVEEDLAFGPEnLCLPPIE---IRKRVDRALAEIGLEKY---RHRSP--KTLSGGQGQCVALAGIL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 141 VQFPDILFLDEPTSGLDISTAHQVMTAIKRMAvTHNIAVVATIHspNWEIFTLFDKLLLLAKGETVFNSKIDQLV--PYF 218
Cdd:PRK13644 152 TMEPECLIFDEVTSMLDPDSGIAVLERIKKLH-EKGKTIVYITH--NLEELHDADRIIVMDRGKIVLEGEPENVLsdVSL 228
|
....*...
gi 1625600662 219 EELGYNFP 226
Cdd:PRK13644 229 QTLGLTPP 236
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
12-184 |
4.14e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 58.59 E-value: 4.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 12 RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIacssstsfcEQEDAL-LGVMTVKETLKYSARLSV- 89
Cdd:PRK09544 17 RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI---------KRNGKLrIGYVPQKLYLDTTLPLTVn 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 90 ------PHATSQVIE---ERVNAvidglglhsvlNNRIGTPIQRgISGGQKRRVSIACSLVQFPDILFLDEPTSGLDIST 160
Cdd:PRK09544 88 rflrlrPGTKKEDILpalKRVQA-----------GHLIDAPMQK-LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNG 155
|
170 180
....*....|....*....|....
gi 1625600662 161 AHQVMTAIKRMAVTHNIAVVATIH 184
Cdd:PRK09544 156 QVALYDLIDQLRRELDCAVLMVSH 179
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
15-157 |
4.17e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 59.33 E-value: 4.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 15 LKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSSTSFCEQEDALLGVMTVKETLKYSARLSVPHATS 94
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEKVLEKLVIQKTRFKKIKKIKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 95 qvIEERVNAVID----GLGLHSVLNNRIGTPIQRGI------------------------------SGGQKRRVSIACSL 140
Cdd:PRK13651 103 --IRRRVGVVFQfaeyQLFEQTIEKDIIFGPVSMGVskeeakkraakyielvgldesylqrspfelSGGQKRRVALAGIL 180
|
170
....*....|....*..
gi 1625600662 141 VQFPDILFLDEPTSGLD 157
Cdd:PRK13651 181 AMEPDFLVFDEPTAGLD 197
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
15-167 |
4.57e-09 |
|
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: 57.73 E-value: 4.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 15 LKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSS-----------------STSFCEQEDALLGVmTV 77
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNknesepsfeatrsrnrySVAYAAQKPWLLNA-TV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 78 KETLKYSARLSvphatsqviEERVNAVIDGLGLHSVLN-------NRIGtpiQRGI--SGGQKRRVSIACSLVQFPDILF 148
Cdd:cd03290 96 EENITFGSPFN---------KQRYKAVTDACSLQPDIDllpfgdqTEIG---ERGInlSGGQRQRICVARALYQNTNIVF 163
|
170
....*....|....*....
gi 1625600662 149 LDEPTSGLDISTAHQVMTA 167
Cdd:cd03290 164 LDDPFSALDIHLSDHLMQE 182
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
16-204 |
5.39e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.06 E-value: 5.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 16 KQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIAcssstsFCEQEdalLGVMTVKETLK------------Y 83
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIM------LNGKE---INALSTAQRLArglvylpedrqsS 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 84 SARLSVPHA--TSQVI---------EERVNAVIDGLglHSVLNNRIGTPIQ--RGISGGQKRRVSIACSLVQFPDILFLD 150
Cdd:PRK15439 351 GLYLDAPLAwnVCALThnrrgfwikPARENAVLERY--RRALNIKFNHAEQaaRTLSGGNQQKVLIAKCLEASPQLLIVD 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1625600662 151 EPTSGLDISTAHQVMTAIKRMAvTHNIAVVaTIHSPNWEIFTLFDKLLLLAKGE 204
Cdd:PRK15439 429 EPTRGVDVSARNDIYQLIRSIA-AQNVAVL-FISSDLEEIEQMADRVLVMHQGE 480
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
12-157 |
8.55e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 57.21 E-value: 8.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 12 RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSS--TSFCEQEDALLGVMTVKETLKYSARLSV 89
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdiSLLPLHARARRGIGYLPQEASIFRRLSV 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1625600662 90 -----------PHATSQVIEERVNAVIDGLGLhSVLNNRIGtpiqRGISGGQKRRVSIACSLVQFPDILFLDEPTSGLD 157
Cdd:PRK10895 96 ydnlmavlqirDDLSAEQREDRANELMEEFHI-EHLRDSMG----QSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
6-203 |
8.82e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.99 E-value: 8.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 6 WNNICYRDILKQISGDVKPAEILAVMGPSGSGKTTLLEC-ISRRKKTSSGNIACSSSTSFCEQEDALLGVmTVKETLKYS 84
Cdd:PLN03232 624 WDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAmLGELSHAETSSVVIRGSVAYVPQVSWIFNA-TVRENILFG 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 85 ARLSvphatsqviEERVNAVIDGLGLHSVLN---NRIGTPI-QRG--ISGGQKRRVSIACSLVQFPDILFLDEPTSGLDI 158
Cdd:PLN03232 703 SDFE---------SERYWRAIDVTALQHDLDllpGRDLTEIgERGvnISGGQKQRVSMARAVYSNSDIYIFDDPLSALDA 773
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1625600662 159 STAHQVMTAIKRMAVTHNIAVVAT--IHspnweIFTLFDKLLLLAKG 203
Cdd:PLN03232 774 HVAHQVFDSCMKDELKGKTRVLVTnqLH-----FLPLMDRIILVSEG 815
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
12-158 |
1.03e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 57.11 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 12 RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRK--KTSSGNIACSSS--TSFCEQEDALLGVMtvketLKYSARL 87
Cdd:PRK09580 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKdlLELSPEDRAGEGIF-----MAFQYPV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 88 SVPHATSQV-IEERVNAV--------IDGLGLHSVLNNRIG----------TPIQRGISGGQKRRVSIACSLVQFPDILF 148
Cdd:PRK09580 89 EIPGVSNQFfLQTALNAVrsyrgqepLDRFDFQDLMEEKIAllkmpedlltRSVNVGFSGGEKKRNDILQMAVLEPELCI 168
|
170
....*....|
gi 1625600662 149 LDEPTSGLDI 158
Cdd:PRK09580 169 LDESDSGLDI 178
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
24-190 |
1.10e-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: 55.07 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 24 PAEILAVMGPSGSGKTTLLECIsrrkktssgniacssstsfceqedallgvmtvketlkysARLSVPHATSQVIeerVNA 103
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARAL---------------------------------------ARELGPPGGGVIY---IDG 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 104 VIDGLGLHSVLNNRIGTPIQRGISGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTAHQVM-----TAIKRMAVTHNIA 178
Cdd:smart00382 39 EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelRLLLLLKSEKNLT 118
|
170
....*....|..
gi 1625600662 179 VVATIHSPNWEI 190
Cdd:smart00382 119 VILTTNDEKDLG 130
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
12-182 |
1.11e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 57.34 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 12 RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTS--SGNIAC--SSSTSFCEQEDALLGV------------M 75
Cdd:CHL00131 20 NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFkgESILDLEPEERAHLGIflafqypieipgV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 76 TVKETLK--YSARLSV-------PHATSQVIEERVNAVidglGLHSVLNNRigtPIQRGISGGQKRRVSIACSLVQFPDI 146
Cdd:CHL00131 100 SNADFLRlaYNSKRKFqglpeldPLEFLEIINEKLKLV----GMDPSFLSR---NVNEGFSGGEKKRNEILQMALLDSEL 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 1625600662 147 LFLDEPTSGLDISTAHQVMTAIKRMAVTHNIAVVAT 182
Cdd:CHL00131 173 AILDETDSGLDIDALKIIAEGINKLMTSENSIILIT 208
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
12-157 |
1.15e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.98 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 12 RDILKQISGDVKP-AEIlAVMGPSGSGKTTLLECISRRKKTSSGNIACSSSTS--FCEQEDAL-----------LGVMTV 77
Cdd:PRK11819 20 KQILKDISLSFFPgAKI-GVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKvgYLPQEPQLdpektvrenveEGVAEV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 78 KETLK----YSARLSVPHATSQ-VIEE--RVNAVIDGLGLHSvLNNRI------------GTPIQRgISGGQKRRVSIAC 138
Cdd:PRK11819 99 KAALDrfneIYAAYAEPDADFDaLAAEqgELQEIIDAADAWD-LDSQLeiamdalrcppwDAKVTK-LSGGERRRVALCR 176
|
170
....*....|....*....
gi 1625600662 139 SLVQFPDILFLDEPTSGLD 157
Cdd:PRK11819 177 LLLEKPDMLLLDEPTNHLD 195
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
14-157 |
1.40e-08 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 57.93 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 14 ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSS-------------STSFceQEDALLGVMTVKET 80
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGrvvnelepadrdiAMVF--QNYALYPHMSVREN 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1625600662 81 LKYSARL-SVPHATsqvIEERVNAVIDGLGLHSVLNNRigtPiqRGISGGQKRRVSIACSLVQFPDILFLDEPTSGLD 157
Cdd:PRK11650 97 MAYGLKIrGMPKAE---IEERVAEAARILELEPLLDRK---P--RELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
15-230 |
1.85e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 57.03 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 15 LKQISGDVKPAEILAVMGPSGSGKTTLLECI---------------SRRKKTSSGNIACSSSTSFCEQEDALLGVmTVKE 79
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIdglfeefegkvkidgELLTAENVWNLRRKIGMVFQNPDNQFVGA-TVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 80 TLKYSAR-LSVPHatsqviEERVNAVIDGLGLHSVLNNRIGTPIQrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLDI 158
Cdd:PRK13642 102 DVAFGMEnQGIPR------EEMIKRVDEALLAVNMLDFKTREPAR--LSGGQKQRVAVAGIIALRPEIIILDESTSMLDP 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1625600662 159 STAHQVMTAIKRMAVTHNIAVVATIHSPNWEIFTlfDKLLLLAKGETVFNSKIDQLVPYFE---ELGYNFPKFSN 230
Cdd:PRK13642 174 TGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASS--DRILVMKAGEIIKEAAPSELFATSEdmvEIGLDVPFSSN 246
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
12-157 |
1.86e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 56.70 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 12 RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI--------ACSSS--------TSFCEQEDALLGVM 75
Cdd:PRK11831 20 RCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEIlfdgenipAMSRSrlytvrkrMSMLFQSGALFTDM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 76 TVKETLKYSARLSVpHATSQVIEERVNAVIDGLGLHSVLNNRigtPIQrgISGGQKRRVSIACSLVQFPDILFLDEPTSG 155
Cdd:PRK11831 100 NVFDNVAYPLREHT-QLPAPLLHSTVMMKLEAVGLRGAAKLM---PSE--LSGGMARRAALARAIALEPDLIMFDEPFVG 173
|
..
gi 1625600662 156 LD 157
Cdd:PRK11831 174 QD 175
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
6-228 |
3.14e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.21 E-value: 3.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 6 WNNICYRDILKQISGDVKPAEILAVMGPSGSGKTTLLEC-ISRRKKTSSGNIACSSSTSFCEQEDALLGVmTVKETLKYS 84
Cdd:PLN03130 624 WDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAmLGELPPRSDASVVIRGTVAYVPQVSWIFNA-TVRDNILFG 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 85 ARLSvphatsqviEERVNAVIDGLGLHSVLNNRIG---TPI-QRG--ISGGQKRRVSIACSLVQFPDILFLDEPTSGLDI 158
Cdd:PLN03130 703 SPFD---------PERYERAIDVTALQHDLDLLPGgdlTEIgERGvnISGGQKQRVSMARAVYSNSDVYIFDDPLSALDA 773
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1625600662 159 STAHQVMTAIKRMAVTHNIAVVAT--IHspnweIFTLFDKLLLLAKGETVFNSKidqlvpyFEELGYNFPKF 228
Cdd:PLN03130 774 HVGRQVFDKCIKDELRGKTRVLVTnqLH-----FLSQVDRIILVHEGMIKEEGT-------YEELSNNGPLF 833
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
126-227 |
3.18e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 56.29 E-value: 3.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 126 ISGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTAHQVMTAIKRM--------AVTHNIAVVAtihspNWEiftlfDKL 197
Cdd:PRK13649 146 LSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLhqsgmtivLVTHLMDDVA-----NYA-----DFV 215
|
90 100 110
....*....|....*....|....*....|...
gi 1625600662 198 LLLAKGETVFNSK---IDQLVPYFEELGYNFPK 227
Cdd:PRK13649 216 YVLEKGKLVLSGKpkdIFQDVDFLEEKQLGVPK 248
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
15-171 |
3.45e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 55.66 E-value: 3.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 15 LKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSS------TSFCEQEDA--------LLGVMTVKET 80
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKditdwqTAKIMREAVaivpegrrVFSRMTVEEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 81 LKYSARLsvphATSQVIEERVNAVIDGLG-LHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLDIS 159
Cdd:PRK11614 101 LAMGGFF----AERDQFQERIKWVYELFPrLHERRIQRAGT-----MSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPI 171
|
170
....*....|..
gi 1625600662 160 TAHQVMTAIKRM 171
Cdd:PRK11614 172 IIQQIFDTIEQL 183
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
4-206 |
3.70e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 55.77 E-value: 3.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 4 IEWNNICYR------DILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIAcssstsfceqedaLLGVMTV 77
Cdd:PRK13632 8 IKVENVSFSypnsenNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIK-------------IDGITIS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 78 KETLKYsARLSV----PHATSQVIEERVNAVID-GLGLHSVLNNRIGTPI-----QRGI-----------SGGQKRRVSI 136
Cdd:PRK13632 75 KENLKE-IRKKIgiifQNPDNQFIGATVEDDIAfGLENKKVPPKKMKDIIddlakKVGMedyldkepqnlSGGQKQRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 137 ACSLVQFPDILFLDEPTSGLDISTAHQVMTAIKRMAVTHNIAVVATIHspNWEIFTLFDKLLLLAKGETV 206
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITH--DMDEAILADKVIVFSEGKLI 221
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
14-214 |
3.88e-08 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 57.42 E-value: 3.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 14 ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACS-------------SSTSFCEQEDALLGvMTVKET 80
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDgvplvqydhhylhRQVALVGQEPVLFS-GSVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 81 LKYSARlsvphatsQVIEERVNAVIDGLGLH---SVLNNRIGTPI-QRG--ISGGQKRRVSIACSLVQFPDILFLDEPTS 154
Cdd:TIGR00958 575 IAYGLT--------DTPDEEIMAAAKAANAHdfiMEFPNGYDTEVgEKGsqLSGGQKQRIAIARALVRKPRVLILDEATS 646
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1625600662 155 GLDISTAHQVMTAIKR-----MAVTHNIAVVATIHspnweiftlfdKLLLLAKGETVFNSKIDQL 214
Cdd:TIGR00958 647 ALDAECEQLLQESRSRasrtvLLIAHRLSTVERAD-----------QILVLKKGSVVEMGTHKQL 700
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
18-180 |
4.17e-08 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 56.28 E-value: 4.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 18 ISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIacssstsFCEQED-------ALLGV---------------- 74
Cdd:COG4608 37 VSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEI-------LFDGQDitglsgrELRPLrrrmqmvfqdpyasln 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 75 --MTVKETLkySARLSVpH--ATSQVIEERVNAVIDGLGLHSVLNNRIgtPIQrgISGGQKRRVSIACSLVQFPDILFLD 150
Cdd:COG4608 110 prMTVGDII--AEPLRI-HglASKAERRERVAELLELVGLRPEHADRY--PHE--FSGGQRQRIGIARALALNPKLIVCD 182
|
170 180 190
....*....|....*....|....*....|....*....
gi 1625600662 151 EPTSGLDISTAHQVMTAI----KRMAVT-----HNIAVV 180
Cdd:COG4608 183 EPVSALDVSIQAQVLNLLedlqDELGLTylfisHDLSVV 221
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
15-245 |
4.28e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 55.90 E-value: 4.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 15 LKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSS--STSFCEQEDallgVMTVKEtlKYSARLSVPHa 92
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivVSSTSKQKE----IKPVRK--KVGVVFQFPE- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 93 tSQVIEERVNAVI----DGLGLHSVLNNRIG----------------TPIQrgISGGQKRRVSIACSLVQFPDILFLDEP 152
Cdd:PRK13643 95 -SQLFEETVLKDVafgpQNFGIPKEKAEKIAaeklemvgladefwekSPFE--LSGGQMRRVAIAGILAMEPEVLVLDEP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 153 TSGLDISTAHQVMTAIKRMAVTHNIAVVATiHSPNwEIFTLFDKLLLLAKGETV---FNSKIDQLVPYFEELGYNFPKFS 229
Cdd:PRK13643 172 TAGLDPKARIEMMQLFESIHQSGQTVVLVT-HLMD-DVADYADYVYLLEKGHIIscgTPSDVFQEVDFLKAHELGVPKAT 249
|
250
....*....|....*.
gi 1625600662 230 NPVDVVMELINTDFEK 245
Cdd:PRK13643 250 HFADQLQKTGAVTFEK 265
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
8-172 |
4.35e-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: 4.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 8 NICYRDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI-----ACSSST---------SFC-E--QEDA 70
Cdd:COG1129 261 GLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIrldgkPVRIRSprdairagiAYVpEdrKGEG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 71 LLGVMTVKE--TL----KYSARLSVPHATsqvIEERVNAVIDGLGLHSvlnNRIGTPIqRGISGG--QKrrVSIACSLVQ 142
Cdd:COG1129 341 LVLDLSIREniTLasldRLSRGGLLDRRR---ERALAEEYIKRLRIKT---PSPEQPV-GNLSGGnqQK--VVLAKWLAT 411
|
170 180 190
....*....|....*....|....*....|
gi 1625600662 143 FPDILFLDEPTSGLDISTAHQVMTAIKRMA 172
Cdd:COG1129 412 DPKVLILDEPTRGIDVGAKAEIYRLIRELA 441
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
14-214 |
4.62e-08 |
|
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: 55.58 E-value: 4.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 14 ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIAC----------SSSTSFCEQ-----EDALLGV---M 75
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFrgqdlyqldrKQRRAFRRDvqlvfQDSPSAVnprM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 76 TVK----ETLKYSARLSvphATSQviEERVNAVIDGLGLHSVLNNRIgtPIQrgISGGQKRRVSIACSLVQFPDILFLDE 151
Cdd:TIGR02769 106 TVRqiigEPLRHLTSLD---ESEQ--KARIAELLDMVGLRSEDADKL--PRQ--LSGGQLQRINIARALAVKPKLIVLDE 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1625600662 152 PTSGLDISTAHQVMTAIKRMA---------VTHNIAVVATIHspnweiftlfDKLLLLAKGETVFNSKIDQL 214
Cdd:TIGR02769 177 AVSNLDMVLQAVILELLRKLQqafgtaylfITHDLRLVQSFC----------QRVAVMDKGQIVEECDVAQL 238
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
127-205 |
6.19e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 55.89 E-value: 6.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 127 SGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTAHQVMT---AIKR------MAVTHNIAVVATIhspnweiftlFDKL 197
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTllnELKRefntaiIMITHDLGVVAGI----------CDKV 232
|
....*...
gi 1625600662 198 LLLAKGET 205
Cdd:PRK09473 233 LVMYAGRT 240
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
15-209 |
6.74e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 55.27 E-value: 6.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 15 LKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSSTSFCEQEDALLGVMTVKETLKYS---------- 84
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQSEEVDWSfpvlvedvvm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 85 -------ARLSVPHATSQvieERVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLD 157
Cdd:PRK15056 103 mgryghmGWLRRAKKRDR---QIVTAALARVDMVEFRHRQIGE-----LSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1625600662 158 ISTAHQVMTAI-------KRMAV-THNIAVVATIHSpnweiFTLFDKLLLLAKG--ETVFNS 209
Cdd:PRK15056 175 VKTEARIISLLrelrdegKTMLVsTHNLGSVTEFCD-----YTVMVKGTVLASGptETTFTA 231
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
127-214 |
6.95e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 55.90 E-value: 6.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 127 SGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTAHQVMTAIKRMAVTHNIAVVATIHSPNWEifTLFDKLLLLAKGETV 206
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAE--QLAHELTVIDRGRVI 223
|
....*...
gi 1625600662 207 FNSKIDQL 214
Cdd:NF000106 224 ADGKVDEL 231
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
4-165 |
1.03e-07 |
|
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: 56.29 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 4 IEWNNICY-----RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI-------------ACSSSTSFC 65
Cdd:TIGR01193 474 IVINDVSYsygygSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEIllngfslkdidrhTLRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 66 EQEDALLGvMTVKETLKYSARlsvPHATSQVIEERVN-AVIDG------LGLHSVLNNRIGTpiqrgISGGQKRRVSIAC 138
Cdd:TIGR01193 554 PQEPYIFS-GSILENLLLGAK---ENVSQDEIWAACEiAEIKDdienmpLGYQTELSEEGSS-----ISGGQKQRIALAR 624
|
170 180
....*....|....*....|....*..
gi 1625600662 139 SLVQFPDILFLDEPTSGLDISTAHQVM 165
Cdd:TIGR01193 625 ALLTDSKVLILDESTSNLDTITEKKIV 651
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
126-241 |
1.12e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 54.42 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 126 ISGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTAHQVMTAIKRMAVTHNIAVVATIHSPNWEifTLFDKLLLLAKGET 205
Cdd:PRK13640 144 LSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA--NMADQVLVLDDGKL 221
|
90 100 110
....*....|....*....|....*....|....*....
gi 1625600662 206 VFNS---KIDQLVPYFEELGYNFPKFSNpvdVVMELINT 241
Cdd:PRK13640 222 LAQGspvEIFSKVEMLKEIGLDIPFVYK---LKNKLKEK 257
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
8-177 |
1.26e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 54.02 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 8 NICYRDIL--KQISGDVKPAEILAVMGPSGSGKTTLLECISRRKK-----TSSGNIACSSSTSFCEQEDAL-----LGVM 75
Cdd:PRK14243 17 NVYYGSFLavKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLYAPDVDPVevrrrIGMV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 76 ---------TVKETLKYSARLSvphATSQVIEERVNAVIDGLGLHSVLNNRIGTPIQrGISGGQKRRVSIACSLVQFPDI 146
Cdd:PRK14243 97 fqkpnpfpkSIYDNIAYGARIN---GYKGDMDELVERSLRQAALWDEVKDKLKQSGL-SLSGGQQQRLCIARAIAVQPEV 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 1625600662 147 LFLDEPTSGLD-IST--AHQVMTAIKR----MAVTHNI 177
Cdd:PRK14243 173 ILMDEPCSALDpISTlrIEELMHELKEqytiIIVTHNM 210
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
14-207 |
1.29e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.94 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 14 ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSSTSFCEQEdALLGVMTVKETLKY-----SARLS 88
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSIAYVPQQ-AWIMNATVRGNILFfdeedAARLA 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 89 VPHATSQvIEERVNAVIDGLglhsvlNNRIGtpiQRGI--SGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTAHQVMT 166
Cdd:PTZ00243 754 DAVRVSQ-LEADLAQLGGGL------ETEIG---EKGVnlSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVE 823
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1625600662 167 AIKRMAVTHNIAVVAT--IHspnweIFTLFDKLLLLAKGETVF 207
Cdd:PTZ00243 824 ECFLGALAGKTRVLAThqVH-----VVPRADYVVALGDGRVEF 861
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
14-180 |
2.06e-07 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 53.54 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 14 ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIAC----------SSSTSFCEQ-----EDALLGV---M 75
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWrgeplaklnrAQRKAFRRDiqmvfQDSISAVnprK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 76 TVKETLKYSARlsvpHATS---QVIEERVNAVIDGLGLHSVLNNRIgtPIQrgISGGQKRRVSIACSLVQFPDILFLDEP 152
Cdd:PRK10419 107 TVREIIREPLR----HLLSldkAERLARASEMLRAVDLDDSVLDKR--PPQ--LSGGQLQRVCLARALAVEPKLLILDEA 178
|
170 180 190
....*....|....*....|....*....|....*..
gi 1625600662 153 TSGLDISTAHQVMTAIKRMA---------VTHNIAVV 180
Cdd:PRK10419 179 VSNLDLVLQAGVIRLLKKLQqqfgtaclfITHDLRLV 215
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
15-228 |
2.10e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 55.34 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 15 LKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSSTSFCEQEdALLGVMTVKETLKYSARLSvphats 94
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQ-AWIQNDSLRENILFGKALN------ 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 95 qviEERVNAVIDGLGLHSVLN-------NRIGtpiQRGI--SGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTAHQVM 165
Cdd:TIGR00957 727 ---EKYYQQVLEACALLPDLEilpsgdrTEIG---EKGVnlSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIF 800
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1625600662 166 TAI----------KRMAVTHNIAVVATIhspnweiftlfDKLLLLAKGetvfnsKIDQLVPYFEELGYN--FPKF 228
Cdd:TIGR00957 801 EHVigpegvlknkTRILVTHGISYLPQV-----------DVIIVMSGG------KISEMGSYQELLQRDgaFAEF 858
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
10-206 |
2.41e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 53.59 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 10 CYRD---ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI-----ACSSSTS----------FCEQEDAL 71
Cdd:PRK13647 13 RYKDgtkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVkvmgrEVNAENEkwvrskvglvFQDPDDQV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 72 LGvMTVKETLKYSAR-LSVphaTSQVIEERVNAVIDGLGLHSVlnnRIGTPIQrgISGGQKRRVSIACSLVQFPDILFLD 150
Cdd:PRK13647 93 FS-STVWDDVAFGPVnMGL---DKDEVERRVEEALKAVRMWDF---RDKPPYH--LSYGQKKRVAIAGVLAMDPDVIVLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1625600662 151 EPTSGLDISTAHQVMTAIKRMAVTHNIAVVATiHSPNWEIfTLFDKLLLLAKGETV 206
Cdd:PRK13647 164 EPMAYLDPRGQETLMEILDRLHNQGKTVIVAT-HDVDLAA-EWADQVIVLKEGRVL 217
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
22-179 |
5.72e-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: 51.98 E-value: 5.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 22 VKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNiacssstsFCEQE--DALLGVMTVKETLKYSARL------------ 87
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGK--------FDDPPdwDEILDEFRGSELQNYFTKLlegdvkvivkpq 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 88 -------SVPHATSQVIE-----ERVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLDEPTSG 155
Cdd:cd03236 95 yvdlipkAVKGKVGELLKkkderGKLDELVDQLELRHVLDRNIDQ-----LSGGELQRVAIAAALARDADFYFFDEPSSY 169
|
170 180 190
....*....|....*....|....*....|..
gi 1625600662 156 LDISTAHQVMTAIKRMA--------VTHNIAV 179
Cdd:cd03236 170 LDIKQRLNAARLIRELAeddnyvlvVEHDLAV 201
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
104-179 |
8.00e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.89 E-value: 8.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 104 VIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTAHQVMTAIKRMA-------VTHN 176
Cdd:PRK13409 196 VVERLGLENILDRDISE-----LSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAegkyvlvVEHD 270
|
...
gi 1625600662 177 IAV 179
Cdd:PRK13409 271 LAV 273
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-180 |
8.24e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.79 E-value: 8.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 12 RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTS-----SGNIACSSSTSFCEQEDALLGV------MTVKET 80
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHASEQTLRGVrgnkiaMIFQEP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 81 LkysARLSVPHAtsqvIEERVNAVidgLGLH----------SVLN--NRIGT----------PIQrgISGGQKRRVSIAC 138
Cdd:PRK15134 102 M---VSLNPLHT----LEKQLYEV---LSLHrgmrreaargEILNclDRVGIrqaakrltdyPHQ--LSGGERQRVMIAM 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1625600662 139 SLVQFPDILFLDEPTSGLDISTAHQVMTAIKRMA---------VTHNIAVV 180
Cdd:PRK15134 170 ALLTRPELLIADEPTTALDVSVQAQILQLLRELQqelnmgllfITHNLSIV 220
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
127-183 |
9.51e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 51.89 E-value: 9.51e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1625600662 127 SGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTAHQV----MTAIKRMA-----VTHNIAVVATI 183
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVlnlmMDLQQELGlsyvfISHDLSVVEHI 221
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
13-184 |
9.76e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.11 E-value: 9.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 13 DILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSSTSFCE-------------QEDALLGVMTVKE 79
Cdd:PTZ00265 399 EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDinlkwwrskigvvSQDPLLFSNSIKN 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 80 TLKYSA-RLSVPHATSQVIEERVNAVIDGLGLHSV--------LNNRIGTPIQRGI------------------------ 126
Cdd:PTZ00265 479 NIKYSLySLKDLEALSNYYNEDGNDSQENKNKRNScrakcagdLNDMSNTTDSNELiemrknyqtikdsevvdvskkvli 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 127 ----------------------SGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTAHQVMTAIKRMAVTHNIAVVATIH 184
Cdd:PTZ00265 559 hdfvsalpdkyetlvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAH 638
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
98-160 |
1.08e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 52.65 E-value: 1.08e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1625600662 98 EERVNAVIDGLGL--HSVLNNrigtpiqrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLDIST 160
Cdd:PRK11147 136 ENRINEVLAQLGLdpDAALSS---------LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET 191
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
15-175 |
1.19e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 52.34 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 15 LKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI-------ACSSSTsfceqeDAL-LGV------------ 74
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEIlidgkpvRIRSPR------DAIaLGIgmvhqhfmlvpn 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 75 MTVKE----TLKYSARLSVPHATsqvIEERVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLD 150
Cdd:COG3845 95 LTVAEnivlGLEPTKGGRLDRKA---ARARIRELSERYGLDVDPDAKVED-----LSVGEQQRVEILKALYRGARILILD 166
|
170 180 190
....*....|....*....|....*....|...
gi 1625600662 151 EPTSGLDISTAHQVMTAIKRMA--------VTH 175
Cdd:COG3845 167 EPTAVLTPQEADELFEILRRLAaegksiifITH 199
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
15-207 |
1.36e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.22 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 15 LKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSS-STSFCEQEDALL-GV------------MTVKET 80
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGqEMRFASTTAALAaGVaiiyqelhlvpeMTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 81 LkYSARLsvPHATSQVIE----ERVNAVIDGLGLHsvlnnrI--GTPIQRgISGGQKRRVSIACSLVQFPDILFLDEPTS 154
Cdd:PRK11288 100 L-YLGQL--PHKGGIVNRrllnYEAREQLEHLGVD------IdpDTPLKY-LSIGQRQMVEIAKALARNARVIAFDEPTS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1625600662 155 GLDISTAHQVMTAIKRMA--------VTHNIAvvatihspnwEIFTLFDKLlllakgeTVF 207
Cdd:PRK11288 170 SLSAREIEQLFRVIRELRaegrvilyVSHRME----------EIFALCDAI-------TVF 213
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
3-157 |
1.44e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.94 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 3 PIEWNN--ICYRD--ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNiacsSSTSFCEQEDALLGVMTVK 78
Cdd:PRK10938 260 RIVLNNgvVSYNDrpILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGYSN----DLTLFGRRRGSGETIWDIK 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 79 ETLKY-SARLsvpHatsqvIEERVNA----VI-----DGLGLHSV-----------------LNNRIGTPIQRGISGGQK 131
Cdd:PRK10938 336 KHIGYvSSSL---H-----LDYRVSTsvrnVIlsgffDSIGIYQAvsdrqqklaqqwldilgIDKRTADAPFHSLSWGQQ 407
|
170 180
....*....|....*....|....*.
gi 1625600662 132 RRVSIACSLVQFPDILFLDEPTSGLD 157
Cdd:PRK10938 408 RLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
15-158 |
1.57e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.93 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 15 LKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSST--SFCEQE---------------DALLGVMTV 77
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEvvTRSPQDglangivyisedrkrDGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 78 KETLKYSARLSVPHATSQVI-EERVNAVIDGLGLHSV----LNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLDEP 152
Cdd:PRK10762 348 KENMSLTALRYFSRAGGSLKhADEQQAVSDFIRLFNIktpsMEQAIGL-----LSGGNQQKVAIARGLMTRPKVLILDEP 422
|
....*.
gi 1625600662 153 TSGLDI 158
Cdd:PRK10762 423 TRGVDV 428
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
104-179 |
2.38e-06 |
|
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: 51.71 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 104 VIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTAHQVMTAIKRMA--------VTH 175
Cdd:COG1245 196 LAEKLGLENILDRDISE-----LSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAeegkyvlvVEH 270
|
....
gi 1625600662 176 NIAV 179
Cdd:COG1245 271 DLAI 274
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
12-158 |
3.26e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 51.32 E-value: 3.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 12 RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSSTS---FCEQEdalLGVMTVKET-LKYSARL 87
Cdd:PRK10636 325 RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKlgyFAQHQ---LEFLRADESpLQHLARL 401
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1625600662 88 SvphatSQVIEERVNAVIDGLGLHSvlnNRIGTPIQRgISGGQKRRVSIACSLVQFPDILFLDEPTSGLDI 158
Cdd:PRK10636 402 A-----PQELEQKLRDYLGGFGFQG---DKVTEETRR-FSGGEKARLVLALIVWQRPNLLLLDEPTNHLDL 463
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
15-206 |
3.31e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 50.01 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 15 LKQISGDVKPAEILAVMGPSGSGKTTLLE-----CISRRKKTSSGNIACSSSTSFCEQEDAL---LGVM-------TVKE 79
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQltnglIISETGQTIVGDYAIPANLKKIKEVKRLrkeIGLVfqfpeyqLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 80 TLKYSARLSVPH--ATSQVIEERVNAVIDGLGLHSVLNNRigTPIQrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLD 157
Cdd:PRK13645 107 TIEKDIAFGPVNlgENKQEAYKKVPELLKLVQLPEDYVKR--SPFE--LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1625600662 158 ISTAHQVMTAIKRMAVTHNIAVVATIHSPNwEIFTLFDKLLLLAKGETV 206
Cdd:PRK13645 183 PKGEEDFINLFERLNKEYKKRIIMVTHNMD-QVLRIADEVIVMHEGKVI 230
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
12-177 |
3.87e-06 |
|
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: 50.96 E-value: 3.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 12 RDILKQISG---DVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIA--------------------CSSSTSFCEQE 68
Cdd:TIGR03269 294 RGVVKAVDNvslEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewvdmtkpgpdgrgrAKRYIGILHQE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 69 DALLGVMTVKETLKYSARLSVPH--ATSQVIEERVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDI 146
Cdd:TIGR03269 374 YDLYPHRTVLDNLTEAIGLELPDelARMKAVITLKMVGFDEEKAEEILDKYPDE-----LSEGERHRVALAQVLIKEPRI 448
|
170 180 190
....*....|....*....|....*....|.
gi 1625600662 147 LFLDEPTSGLDistahqvmtAIKRMAVTHNI 177
Cdd:TIGR03269 449 VILDEPTGTMD---------PITKVDVTHSI 470
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
11-214 |
4.30e-06 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 50.87 E-value: 4.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 11 YRD---ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI-------------ACSSSTSFCEQEDALL-G 73
Cdd:PRK10790 350 YRDdnlVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIrldgrplsslshsVLRQGVAMVQQDPVVLaD 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 74 VMTVKETLkysARLSVPHATSQVIEE-RVNAVIDGL--GLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLD 150
Cdd:PRK10790 430 TFLANVTL---GRDISEEQVWQALETvQLAELARSLpdGLYTPLGEQGNN-----LSVGQKQLLALARVLVQTPQILILD 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1625600662 151 EPTSGLDISTAHQVMTAIKrmAVTHNIAVVATIHspnwEIFTLF--DKLLLLAKGETVFNSKIDQL 214
Cdd:PRK10790 502 EATANIDSGTEQAIQQALA--AVREHTTLVVIAH----RLSTIVeaDTILVLHRGQAVEQGTHQQL 561
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
15-183 |
5.18e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 50.62 E-value: 5.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 15 LKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSstsfcEQEDALLG--VMTVKETLKY-----SARL 87
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNG-----QRIDTLSPgkLQALRRDIQFifqdpYASL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 88 SVPHATSQVIEE--RVNAVIDGLGLH---SVLNNRIGTPIQRG------ISGGQKRRVSIACSLVQFPDILFLDEPTSGL 156
Cdd:PRK10261 415 DPRQTVGDSIMEplRVHGLLPGKAAAarvAWLLERVGLLPEHAwrypheFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180 190
....*....|....*....|....*....|....*.
gi 1625600662 157 DISTAHQVMT---------AIKRMAVTHNIAVVATI 183
Cdd:PRK10261 495 DVSIRGQIINllldlqrdfGIAYLFISHDMAVVERI 530
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-204 |
5.41e-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: 48.56 E-value: 5.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 4 IEWNNICYR------DILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI-------------ACSSSTSF 64
Cdd:cd03369 7 IEVENLSVRyapdlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIeidgidistipleDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 65 CEQEDALLgVMTVKETL----KYSarlsvphatsqviEERVNAV--IDGLGLHsvlnnrigtpiqrgISGGQKRRVSIAC 138
Cdd:cd03369 87 IPQDPTLF-SGTIRSNLdpfdEYS-------------DEEIYGAlrVSEGGLN--------------LSQGQRQLLCLAR 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1625600662 139 SLVQFPDILFLDEPTSGLDISTAHQVMTAIKRMAVTHNIAVVAtiHspnwEIFTL--FDKLLLLAKGE 204
Cdd:cd03369 139 ALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIA--H----RLRTIidYDKILVMDAGE 200
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
71-157 |
8.76e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.12 E-value: 8.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 71 LLGVMTVKETLKYSARL-SVPHATsqvIEERVNAVIDGLGLHSVLNNRIGT-PIqrgisgGQKRRVSIACSLVQFPDILF 148
Cdd:NF033858 350 LYGELTVRQNLELHARLfHLPAAE---IAARVAEMLERFDLADVADALPDSlPL------GIRQRLSLAVAVIHKPELLI 420
|
....*....
gi 1625600662 149 LDEPTSGLD 157
Cdd:NF033858 421 LDEPTSGVD 429
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
24-198 |
1.21e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 46.58 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 24 PAEILAVMGPSGSGKTTLLECIsrrkktssgniacssstsfceqedaLLGVmtvkeTLKYSARLSVPHATSQVIEERVNA 103
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDAI-------------------------GLAL-----GGAQSATRRRSGVKAGCIVAAVSA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 104 VIdglglhsvlnnrIGTPIQrgISGGQKRRVSIACSL----VQFPDILFLDEPTSGLDISTAHQVMTAIKRMAVTHNIAV 179
Cdd:cd03227 70 EL------------IFTRLQ--LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVI 135
|
170
....*....|....*....
gi 1625600662 180 VATiHSPnwEIFTLFDKLL 198
Cdd:cd03227 136 VIT-HLP--ELAELADKLI 151
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
18-204 |
1.28e-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: 49.05 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 18 ISGDVKPAEILAVMGPSGSGKTTLLECI-------------SRRKKTSSGNIACSSSTSFC-----EQEDALLGVMTVKE 79
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALfgaypgkfegnvfINGKPVDIRNPAQAIRAGIAmvpedRKRHGIVPILGVGK 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 80 TLKYSARLSVPHATSQVIEERVNAVIDGLGLHSVLNNRIGTPIQRgISGGQKRRVSIACSLVQFPDILFLDEPTSGLDIS 159
Cdd:TIGR02633 359 NITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIGR-LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVG 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1625600662 160 TAHQVMTAIKRMAvTHNIAVVaTIHSPNWEIFTLFDKLLLLAKGE 204
Cdd:TIGR02633 438 AKYEIYKLINQLA-QEGVAII-VVSSELAEVLGLSDRVLVIGEGK 480
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
15-168 |
1.94e-05 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 48.48 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 15 LKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSS-------TSFCEQ-----EDALLGVMTVKETLK 82
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHdlrdytlASLRNQvalvsQNVHLFNDTIANNIA 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 83 YSARlsvPHATSQVIEERVNAV-----IDGL--GLHSVlnnrIGtpiQRGI--SGGQKRRVSIACSLVQFPDILFLDEPT 153
Cdd:PRK11176 439 YART---EQYSREQIEEAARMAyamdfINKMdnGLDTV----IG---ENGVllSGGQRQRIAIARALLRDSPILILDEAT 508
|
170
....*....|....*
gi 1625600662 154 SGLDISTAHQVMTAI 168
Cdd:PRK11176 509 SALDTESERAIQAAL 523
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
10-157 |
2.92e-05 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 46.34 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 10 CYRD---ILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIaCSSSTSFCEQEDAL------LG------- 73
Cdd:PRK13538 9 CERDeriLFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEV-LWQGEPIRRQRDEYhqdllyLGhqpgikt 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 74 VMTVKETLKYSARLSvphatSQVIEERVNAVIDGLGLHSVLNnrigTPIqRGISGGQKRRVSIACSLVQFPDILFLDEPT 153
Cdd:PRK13538 88 ELTALENLRFYQRLH-----GPGDDEALWEALAQVGLAGFED----VPV-RQLSAGQQRRVALARLWLTRAPLWILDEPF 157
|
....
gi 1625600662 154 SGLD 157
Cdd:PRK13538 158 TAID 161
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-204 |
3.15e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 47.86 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 5 EWNNICYRDI--LKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI--------------ACSSSTSFCEQ- 67
Cdd:PRK09700 267 EVRNVTSRDRkkVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIrlngkdisprspldAVKKGMAYITEs 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 68 --EDALLGVMTVKETLKYSARLS----------VPHATSQVIEERVNAVIDgLGLHSVlNNRIGTpiqrgISGGQKRRVS 135
Cdd:PRK09700 347 rrDNGFFPNFSIAQNMAISRSLKdggykgamglFHEVDEQRTAENQRELLA-LKCHSV-NQNITE-----LSGGNQQKVL 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1625600662 136 IACSLVQFPDILFLDEPTSGLDISTAHQVMTAIKRMAVTHNIAVVATIHSPnwEIFTLFDKLLLLAKGE 204
Cdd:PRK09700 420 ISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELP--EIITVCDRIAVFCEGR 486
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
20-180 |
3.38e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 45.64 E-value: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 20 GDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIacssstsfceqedallgvmtvketlkysarlSVPHATSQVIEE 99
Cdd:cd03222 20 GVVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDND-------------------------------EWDGITPVYKPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 100 RVNavidglglhsvlnnrigtpiqrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTAHQVMTAIKRMA------- 172
Cdd:cd03222 69 YID-----------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSeegkkta 125
|
170
....*....|
gi 1625600662 173 --VTHNIAVV 180
Cdd:cd03222 126 lvVEHDLAVL 135
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
63-157 |
4.58e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.72 E-value: 4.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 63 SFCEQEDALLGvMTVKETLKYSARlsvpHATSQVIEERVN-AVIDGL--GLHSVLNNRIGtPIQRGISGGQKRRVSIACS 139
Cdd:PTZ00265 1299 SIVSQEPMLFN-MSIYENIKFGKE----DATREDVKRACKfAAIDEFieSLPNKYDTNVG-PYGKSLSGGQKQRIAIARA 1372
|
90
....*....|....*...
gi 1625600662 140 LVQFPDILFLDEPTSGLD 157
Cdd:PTZ00265 1373 LLREPKILLLDEATSSLD 1390
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
15-203 |
5.74e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.03 E-value: 5.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 15 LKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIAcssstsfceqedaLLGvmtvKETLKYSARLSVPHATS 94
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTIT-------------LHG----KKINNHNANEAINHGFA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 95 QVIEERVNAVIDG---LGLHSVLNN---------------------------RIGTPIQR----GISGGQKRRVSIACSL 140
Cdd:PRK10982 327 LVTEERRSTGIYAyldIGFNSLISNirnyknkvglldnsrmksdtqwvidsmRVKTPGHRtqigSLSGGNQQKVIIGRWL 406
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1625600662 141 VQFPDILFLDEPTSGLDISTAHQVMTAIKRMAVTHNIAVVATIHSPnwEIFTLFDKLLLLAKG 203
Cdd:PRK10982 407 LTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMP--ELLGITDRILVMSNG 467
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
9-214 |
5.77e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 46.97 E-value: 5.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 9 ICYRDILKQISG---------DVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNI-----ACSSSTS---------FC 65
Cdd:PRK15439 12 LCARSISKQYSGvevlkgidfTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLeiggnPCARLTPakahqlgiyLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 66 EQEDALLGVMTVKETLKYsaRLsvphATSQVIEERVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPD 145
Cdd:PRK15439 92 PQEPLLFPNLSVKENILF--GL----PKRQASMQKMKQLLAALGCQLDLDSSAGS-----LEVADRQIVEILRGLMRDSR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 146 ILFLDEPTSGLDISTAHQVMTAIkRMAVTHNIAVVATIHS-PnwEIFTLFDKLLLLAKGETVFNSKIDQL 214
Cdd:PRK15439 161 ILILDEPTASLTPAETERLFSRI-RELLAQGVGIVFISHKlP--EIRQLADRISVMRDGTIALSGKTADL 227
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
12-204 |
6.64e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 46.85 E-value: 6.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 12 RDILKQISGDVKPAEILAVMGPSGSGKTTLLECI-SRRKKTSSGNIACSS---STSFCEQ----------ED----ALLG 73
Cdd:PRK13549 275 IKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLfGAYPGRWEGEIFIDGkpvKIRNPQQaiaqgiamvpEDrkrdGIVP 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 74 VMTVKE--TL----KYSARLSVPHATSQ-VIEERVNAvidglglhsvLNNRIGTPIQR--GISGGQKRRVSIACSLVQFP 144
Cdd:PRK13549 355 VMGVGKniTLaaldRFTGGSRIDDAAELkTILESIQR----------LKVKTASPELAiaRLSGGNQQKAVLAKCLLLNP 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 145 DILFLDEPTSGLDISTAHQVMTAIKRMaVTHNIAVVaTIHSPNWEIFTLFDKLLLLAKGE 204
Cdd:PRK13549 425 KILILDEPTRGIDVGAKYEIYKLINQL-VQQGVAII-VISSELPEVLGLSDRVLVMHEGK 482
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
12-158 |
8.90e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.32 E-value: 8.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 12 RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSS--STSFCEQEDALLGVMTV-------KETLK 82
Cdd:PRK10636 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwQLAWVNQETPALPQPALeyvidgdREYRQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 83 YSARLSVP------HATSQV-----------IEERVNAVIDGLGLHsvlNNRIGTPIqRGISGGQKRRVSIACSLVQFPD 145
Cdd:PRK10636 94 LEAQLHDAnerndgHAIATIhgkldaidawtIRSRAASLLHGLGFS---NEQLERPV-SDFSGGWRMRLNLAQALICRSD 169
|
170
....*....|...
gi 1625600662 146 ILFLDEPTSGLDI 158
Cdd:PRK10636 170 LLLLDEPTNHLDL 182
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
12-170 |
1.07e-04 |
|
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: 46.44 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 12 RDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTsSGNI---ACSSSTSFCEQEDALLGVMTVKE-TLKYSARL 87
Cdd:TIGR01271 1232 RAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST-EGEIqidGVSWNSVTLQTWRKAFGVIPQKVfIFSGTFRK 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 88 SV-PHAtsQVIEERVNAVIDGLGLHSVLN---NRIGTPIQRG---ISGGQKRRVSIACSLVQFPDILFLDEPTSGLDIST 160
Cdd:TIGR01271 1311 NLdPYE--QWSDEEIWKVAEEVGLKSVIEqfpDKLDFVLVDGgyvLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVT 1388
|
170
....*....|
gi 1625600662 161 AHQVMTAIKR 170
Cdd:TIGR01271 1389 LQIIRKTLKQ 1398
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
126-181 |
1.77e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 44.73 E-value: 1.77e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1625600662 126 ISGGQKRRVSIACSLVQFPDILFLDEPTSGLDISTAHQVMTAI------KRMA---VTHNIAVVA 181
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLlelqqkENMAlvlITHDLALVA 218
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
127-157 |
3.29e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 44.73 E-value: 3.29e-04
10 20 30
....*....|....*....|....*....|.
gi 1625600662 127 SGGQKRRVSIACSLVQFPDILFLDEPTSGLD 157
Cdd:NF033858 138 SGGMKQKLGLCCALIHDPDLLILDEPTTGVD 168
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
11-154 |
5.23e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 44.11 E-value: 5.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 11 YRDILKQISGDVKPAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSSTSFCEQEDALLGVMTVKETLKYSARLSvp 90
Cdd:PRK13545 36 YHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGIENIELKGLMM-- 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1625600662 91 HATSQVIEERVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLDEPTS 154
Cdd:PRK13545 114 GLTKEKIKEIIPEIIEFADIGKFIYQPVKT-----YSSGMKSRLGFAISVHINPDILVIDEALS 172
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
26-171 |
9.26e-04 |
|
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: 41.15 E-value: 9.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 26 EILAVMGPSGSGKTTLL-ECISRRKKtssgniacssstsfceqedallgvmtvketLKYSARLSVPHATSQVIEERVNAV 104
Cdd:cd03238 22 VLVVVTGVSGSGKSTLVnEGLYASGK------------------------------ARLISFLPKFSRNKLIFIDQLQFL 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 105 ID-GLGLHSvLNNRIGTpiqrgISGGQKRRVSIACSLVQ--FPDILFLDEPTSGLDISTAHQVMTAIKRM 171
Cdd:cd03238 72 IDvGLGYLT-LGQKLST-----LSGGELQRVKLASELFSepPGTLFILDEPSTGLHQQDINQLLEVIKGL 135
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
126-160 |
1.01e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.96 E-value: 1.01e-03
10 20 30
....*....|....*....|....*....|....*
gi 1625600662 126 ISGGQKRRVSIACSLVQFPDILFLDEPTSGLDIST 160
Cdd:PRK15064 156 VAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINT 190
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
129-232 |
1.71e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 41.71 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 129 GQKRRVSIACSLVQFPDILFLDEPTSGLDISTAHQVMTAIKRMAVTHNIAVVATIHSPNWeIFTLFDKLLLLAKGETVFN 208
Cdd:PRK15093 162 GECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQM-LSQWADKINVLYCGQTVET 240
|
90 100
....*....|....*....|....*....
gi 1625600662 209 SKIDQLV-----PYFEELGYNFPKFSNPV 232
Cdd:PRK15093 241 APSKELVttphhPYTQALIRAIPDFGSAM 269
|
|
| ABC2_membrane_7 |
pfam19055 |
ABC-2 type transporter; |
184-233 |
1.85e-03 |
|
ABC-2 type transporter;
Pssm-ID: 465963 [Multi-domain] Cd Length: 409 Bit Score: 41.82 E-value: 1.85e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1625600662 184 HSPNWEIFTLFDKLLLLAK-GETVFNSKIDQLVPYFEELGYNFPKFSNPVD 233
Cdd:pfam19055 1 HQPSYTLFKMFDDLILLAKgGLTVYHGPVKKVEEYFAGLGINVPERVNPPD 51
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
98-165 |
6.39e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.61 E-value: 6.39e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1625600662 98 EERVNAVIDGLGLHSVLNNRIgtpiQRGISGGQKRRVSIACSLVQFPDILFLDEPTSGLDIstaHQVM 165
Cdd:PLN03073 321 EARAASILAGLSFTPEMQVKA----TKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL---HAVL 381
|
|
| MobB |
COG1763 |
Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; ... |
27-43 |
7.48e-03 |
|
Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 441369 [Multi-domain] Cd Length: 162 Bit Score: 38.24 E-value: 7.48e-03
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
24-157 |
7.64e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 38.70 E-value: 7.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625600662 24 PAEILAVMGPSGSGKTTLLECISRRKKTSSGNIACSSSTS------FCEQEDALLGV---MTVKETLKYSARLSVPHATs 94
Cdd:PRK13541 25 PSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNInniakpYCTYIGHNLGLkleMTVFENLKFWSEIYNSAET- 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1625600662 95 qvieerVNAVIDGLGLHSVLNNRIGTpiqrgISGGQKRRVSIACSLVQFPDILFLDEPTSGLD 157
Cdd:PRK13541 104 ------LYAAIHYFKLHDLLDEKCYS-----LSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
|
|
| |
