|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
112-748 |
0e+00 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 588.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 112 FTGFAMPPEEISDSKPFSDDemiPEDIeagkkkPKFQAEPTLPIFLKFRDVTYKVVIKKLTSS----------------- 174
Cdd:PLN03211 4 FDGVENQNDGPDRSKPPSQD---SRDL------PSLLLSSCYPITLKFMDVCYRVKFENMKNKgsnikrilghkpkisde 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 175 ----VEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSSTGGSVTYNDKPYSKYLKSKIGFVTQDDVLFPH 250
Cdd:PLN03211 75 trqiQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQILKRTGFVTQDDILYPH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 251 LTVKETLTYAARLRLPKTLTREQKKQRALDVIQELGLERCQDTMIGGAFVRGVSGGERKRVSIGNEIIINPSLLLLDEPT 330
Cdd:PLN03211 155 LTVRETLVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 331 SGLDSTTALRTILMLHDIAEAGKTVITTIHQPSSRLFHRFDKLILLGRGSLLYFGKSSEALDYFSSIGCSPLIAMNPAEF 410
Cdd:PLN03211 235 SGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESVGFSPSFPMNPADF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 411 LLDLANGnindisvPSELDdrvqvGNSGREtqtgKPSpaaVHEYLVEAYETRVAEQEKKKLLDPVPLDEEAKAKSTRLKR 490
Cdd:PLN03211 315 LLDLANG-------VCQTD-----GVSERE----KPN---VKQSLVASYNTLLAPKVKAAIEMSHFPQANARFVGSASTK 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 491 QWGTC-------WWEQYCILFCRGLKERRHEYFSWLRVTQVLSTAVILGLLWWQSDIRTpmgLQDQAGLLFFIAVFWGFF 563
Cdd:PLN03211 376 EHRSSdrisistWFNQFSILLQRSLKERKHESFNTLRVFQVIAAALLAGLMWWHSDFRD---VQDRLGLLFFISIFWGVF 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 564 PVFTAIFAFPQERAMLNKERAADMYRLSAYFLARTTSDLPLDFILPSLFLLVVYFMTGLRISPYPFFLSMLTVFLCIIAA 643
Cdd:PLN03211 453 PSFNSVFVFPQERAIFVKERASGMYTLSSYFMARIVGDLPMELILPTIFLTVTYWMAGLKPELGAFLLTLLVLLGYVLVS 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 644 QGLGLAIGAILMDLKKATTLASVTVMTFMLAGGFFVKKVPVFISWIRYLSFNYHTYKLLLKVQYQDFA--VSINGMRIDN 721
Cdd:PLN03211 533 QGLGLALGAAIMDAKKASTIVTVTMLAFVLTGGFYVHKLPSCMAWIKYISTTFYSYRLLINVQYGEGKriSSLLGCSLPH 612
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 79597808 722 GLTE-------------------VAALVVMIFGYRLLAYLSLRQMK 748
Cdd:PLN03211 613 GSDRasckfveedvagqispatsVSVLIFMFVGYRLLAYLALRRIK 658
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
153-745 |
2.44e-139 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 423.69 E-value: 2.44e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 153 LPIFLKFRDVTYKVVIKKLTSSV------EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSSTG-GSVTY 225
Cdd:TIGR00955 8 SDVFGRVAQDGSWKQLVSRLRGCfcrerpRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGsGSVLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 226 NDKPYSKYLKSKI-GFVTQDDVLFPHLTVKETLTYAARLRLPKTLTREQKKQRALDVIQELGLERCQDTMIG-GAFVRGV 303
Cdd:TIGR00955 88 NGMPIDAKEMRAIsAYVQQDDLFIPTLTVREHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGvPGRVKGL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 304 SGGERKRVSIGNEIIINPSLLLLDEPTSGLDSTTALRTILMLHDIAEAGKTVITTIHQPSSRLFHRFDKLILLGRGSLLY 383
Cdd:TIGR00955 168 SGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAY 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 384 FGKSSEALDYFSSIG--CSPliAMNPAEFLLDLANGNINDISVPSE----LDDRVQVGNSGRETQTgkpspaavheylve 457
Cdd:TIGR00955 248 LGSPDQAVPFFSDLGhpCPE--NYNPADFYVQVLAVIPGSENESREriekICDSFAVSDIGRDMLV-------------- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 458 ayETRVAEQEKKKLLDPVPLDEEAKAKSTrlkrqwgtcWWEQYCILFCRG-LKERRHEYFSWLRVTQVLSTAVILGLLWW 536
Cdd:TIGR00955 312 --NTNLWSGKAGGLVKDSENMEGIGYNAS---------WWTQFYALLKRSwLSVLRDPLLLKVRLIQTMMTAILIGLIYL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 537 QSDIrTPMGLQDQAGLLFFIAVFWGFFPVFTAIFAFPQERAMLNKERAADMYRLSAYFLARTTSDLPLDFILPSLFLLVV 616
Cdd:TIGR00955 381 GQGL-TQKGVQNINGALFLFLTNMTFQNVFPVINVFTAELPVFLRETRSGLYRVSAYFLAKTIAELPLFIILPALFTSIT 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 617 YFMTGLRISPYPFFLSMLTVFLCIIAAQGLGLAIGAILMDLKKATTLASVTVMTFMLAGGFFVK--KVPVFISWIRYLSF 694
Cdd:TIGR00955 460 YWMIGLRSGATHFLTFLFLVTLVANVATSFGYLISCAFSSTSMALTVGPPFVIPFLLFGGFFINsdSIPVYFKWLSYLSW 539
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79597808 695 NYHTYKLLLKVQYQD------FAVSING--------------MRIDNGLTEVAALVVMIFGYRLLAYLSLR 745
Cdd:TIGR00955 540 FRYGNEGLLINQWSDvdniecTSANTTGpcpssgeviletlsFRNADLYLDLIGLVILIFFFRLLAYFALR 610
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
149-703 |
5.76e-78 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 273.91 E-value: 5.76e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 149 AEPTLP-IFLKFrdvtYKVVIKKL---TSSVEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSSTG--GS 222
Cdd:TIGR00956 46 YQPTFPnALLKI----LTRGFRKLkkfRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGveGV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 223 VTYNDKP---YSKYLKSKIGFVTQDDVLFPHLTVKETLTYAARLRLPKT----LTREQKKQRALDVIQE-LGLERCQDTM 294
Cdd:TIGR00956 122 ITYDGITpeeIKKHYRGDVVYNAETDVHFPHLTVGETLDFAARCKTPQNrpdgVSREEYAKHIADVYMAtYGLSHTRNTK 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 295 IGGAFVRGVSGGERKRVSIGNEIIINPSLLLLDEPTSGLDSTTALRTILMLHDIA-EAGKTVITTIHQPSSRLFHRFDKL 373
Cdd:TIGR00956 202 VGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSAnILDTTPLVAIYQCSQDAYELFDKV 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 374 ILLGRGSLLYFGKSSEALDYFSSIG--CSPLIAMnpAEFLLDLANGNINDISVPSEldDRVQVGNSGRETQTGKPSPAAV 451
Cdd:TIGR00956 282 IVLYEGYQIYFGPADKAKQYFEKMGfkCPDRQTT--ADFLTSLTSPAERQIKPGYE--KKVPRTPQEFETYWRNSPEYAQ 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 452 HEYLVEAYETRVAEQEKKKLLDPVPLDEeaKAKSTRLKRQWGTCWWEQYCILFCRG-LKERRHEYFSWLRVTQVLSTAVI 530
Cdd:TIGR00956 358 LMKEIDEYLDRCSESDTKEAYRESHVAK--QSKRTRPSSPYTVSFSMQVKYCLARNfLRMKGNPSFTLFMVFGNIIMALI 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 531 LGLLWWqsdiRTPMGLQD---QAGLLFFiAVFWGFFPVFTAIFAFPQERAMLNKERAADMYRLSAYFLARTTSDLPLDFI 607
Cdd:TIGR00956 436 LSSVFY----NLPKNTSDfysRGGALFF-AILFNAFSSLLEIASMYEARPIVEKHRKYALYHPSADAIASIISEIPFKII 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 608 LPSLFLLVVYFMTGLRISPYPFFLSMLTVFLCIIAAQGLGLAIGAILMDLKKATTLASVTVMTFMLAGGFFV--KKVPVF 685
Cdd:TIGR00956 511 ESVVFNIILYFMVNFRRTAGRFFFYLLILFICTLAMSHLFRSIGAVTKTLSEAMTPAAILLLALSIYTGFAIprPSMLGW 590
|
570
....*....|....*...
gi 79597808 686 ISWIRYLSFNYHTYKLLL 703
Cdd:TIGR00956 591 SKWIYYVNPLAYAFESLM 608
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
176-385 |
6.74e-77 |
|
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: 247.18 E-value: 6.74e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRI-SQSSTGGSVTYNDKPYSKYL-KSKIGFVTQDDVLFPHLTV 253
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeGGGTTSGQILFNGQPRKPDQfQKCVAYVRQDDILLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 254 KETLTYAARLRLPKTLTREQKKQRALDViqelGLERCQDTMIGGAFVRGVSGGERKRVSIGNEIIINPSLLLLDEPTSGL 333
Cdd:cd03234 99 RETLTYTAILRLPRKSSDAIRKKRVEDV----LLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 79597808 334 DSTTALRTILMLHDIAEAGKTVITTIHQPSSRLFHRFDKLILLGRGSLLYFG 385
Cdd:cd03234 175 DSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
154-385 |
4.25e-76 |
|
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: 243.61 E-value: 4.25e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 154 PIFLKFRDVTYKVviKKLTSSVEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSSTGGSVTYNDKP-YSK 232
Cdd:cd03213 1 GVTLSFRNLTVTV--KSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGVSGEVLINGRPlDKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 233 YLKSKIGFVTQDDVLFPHLTVKETLTYAARLRlpktltreqkkqraldviqelglercqdtmiggafvrGVSGGERKRVS 312
Cdd:cd03213 79 SFRKIIGYVPQDDILHPTLTVRETLMFAAKLR-------------------------------------GLSGGERKRVS 121
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79597808 313 IGNEIIINPSLLLLDEPTSGLDSTTALRTILMLHDIAEAGKTVITTIHQPSSRLFHRFDKLILLGRGSLLYFG 385
Cdd:cd03213 122 IALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
127-724 |
9.65e-67 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 240.78 E-value: 9.65e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 127 PFSDDEMIPEDIEAGKKKPKFQAEPtlpIFLkFRDVTYKVVIKKltssVEKEILTGISGSVNPGEVLALMGPSGSGKTTL 206
Cdd:TIGR00956 734 GSTDLTDESDDVNDEKDMEKESGED---IFH-WRNLTYEVKIKK----EKRVILNNVDGWVKPGTLTALMGASGAGKTTL 805
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 207 LSLLAGRISQSS-TGGSVTYNDKPYSKYLKSKIGFVTQDDVLFPHLTVKETLTYAARLRLPKTLTREQKKQRALDVIQEL 285
Cdd:TIGR00956 806 LNVLAERVTTGViTGGDRLVNGRPLDSSFQRSIGYVQQQDLHLPTSTVRESLRFSAYLRQPKSVSKSEKMEYVEEVIKLL 885
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 286 GLERCQDTMIGGAFVrGVSGGERKRVSIGNEIIINPSLLL-LDEPTSGLDSTTALRTILMLHDIAEAGKTVITTIHQPSS 364
Cdd:TIGR00956 886 EMESYADAVVGVPGE-GLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSA 964
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 365 RLFHRFDKLILLGRGS-LLYFGK----SSEALDYFSSIGCSPLIA-MNPAEFLLdlangnindisvpselddrvQVGNSG 438
Cdd:TIGR00956 965 ILFEEFDRLLLLQKGGqTVYFGDlgenSHTIINYFEKHGAPKCPEdANPAEWML--------------------EVIGAA 1024
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 439 RETQTGKPspaaVHEYLVEAYETRVAEQEKKKLLDPVPLDEEAKAKSTRLKrqWGTCWWEQYCILFCRGLKE--RRHEYF 516
Cdd:TIGR00956 1025 PGAHANQD----YHEVWRNSSEYQAVKNELDRLEAELSKAEDDNDPDALSK--YAASLWYQFKLVLWRTFQQywRTPDYL 1098
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 517 sWLRVTQVLSTAVILGLLWWQSDiRTPMGLQDQAGLLFFIAVFWG-----FFPVFTAifafpQERAMLNKERAADMYRLS 591
Cdd:TIGR00956 1099 -YSKFFLTIFAALFIGFTFFKVG-TSLQGLQNQMFAVFMATVLFNpliqqYLPPFVA-----QRDLYEVRERPSRTFSWL 1171
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 592 AYFLARTTSDLPLDFILPSLFLLVVYFMTGL--RISPYP-----FFLSMLTVFLCIIAAQGLGLAIGAILMDLKKATTLA 664
Cdd:TIGR00956 1172 AFIAAQITVEIPYNLVAGTIFFFIWYYPVGFywNASKTGqvherGVLFWLLSTMFFLYFSTLGQMVISFNPNADNAAVLA 1251
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79597808 665 SVTVMTFMLAGGFFVKK--VPVFisWIRYLSFNYHTYKL--LLKVQYQDFAVSI-----NGMRIDNGLT 724
Cdd:TIGR00956 1252 SLLFTMCLSFCGVLAPPsrMPGF--WIFMYRCSPFTYLVqaLLSTGLADVPVTCkvkelLTFNPPSGQT 1318
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
157-385 |
1.00e-59 |
|
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: 200.16 E-value: 1.00e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 157 LKFRDVTYKVVIKKltssVEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSSTGGSVTYNDKPYSKYLKS 236
Cdd:cd03232 4 LTWKNLNYTVPVKG----GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGVITGEILINGRPLDKNFQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 237 KIGFVTQDDVLFPHLTVKETLTYAARLRlpktltreqkkqraldviqelglercqdtmiggafvrGVSGGERKRVSIGNE 316
Cdd:cd03232 80 STGYVEQQDVHSPNLTVREALRFSALLR-------------------------------------GLSVEQRKRLTIGVE 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 317 IIINPSLLLLDEPTSGLDSTTALRTILMLHDIAEAGKTVITTIHQPSSRLFHRFDKLILLGR-GSLLYFG 385
Cdd:cd03232 123 LAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRgGKTVYFG 192
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
151-724 |
4.73e-57 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 211.63 E-value: 4.73e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 151 PTLPIFLKFRDVTYKVVI-----KKLTSSVEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSSTGGSVTY 225
Cdd:PLN03140 862 PFTPLAMSFDDVNYFVDMpaemkEQGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIEGDIRI 941
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 226 NDKPYSKYLKSKI-GFVTQDDVLFPHLTVKETLTYAARLRLPKTLTREQKKQRALDVIQELGLERCQDTMIGGAFVRGVS 304
Cdd:PLN03140 942 SGFPKKQETFARIsGYCEQNDIHSPQVTVRESLIYSAFLRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPGVTGLS 1021
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 305 GGERKRVSIGNEIIINPSLLLLDEPTSGLDSTTALRTILMLHDIAEAGKTVITTIHQPSSRLFHRFDKLILLGR-GSLLY 383
Cdd:PLN03140 1022 TEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKRgGQVIY 1101
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 384 FG----KSSEALDYFSSIGCSPLIA--MNPAEFLLDLAngnindiSVPSELD---DRVQVGNSGRETQTGK--------P 446
Cdd:PLN03140 1102 SGplgrNSHKIIEYFEAIPGVPKIKekYNPATWMLEVS-------SLAAEVKlgiDFAEHYKSSSLYQRNKalvkelstP 1174
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 447 SPAAVHEYLVEAYETRVAEQEKKKLLdpvpldeeakakstrlkRQWGTCWweqycilfcrglkerRHEYFSWLRVTQVLS 526
Cdd:PLN03140 1175 PPGASDLYFATQYSQSTWGQFKSCLW-----------------KQWWTYW---------------RSPDYNLVRFFFTLA 1222
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 527 TAVILGLLWWQSDIR--TPMGLQDQAGLLFFIAVFWGFFPVFTAIFAFPQERAMLNKERAADMYRLSAYFLARTTSDLPL 604
Cdd:PLN03140 1223 AALMVGTIFWKVGTKrsNANDLTMVIGAMYAAVLFVGINNCSTVQPMVAVERTVFYRERAAGMYSALPYAIAQVVCEIPY 1302
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 605 DFILPSLFLLVVYFMTGLRISPYPFFLSMLTVFLCIIAAQGLGLAIGAILMDLKKATTLASVTVMTFMLAGGFFV--KKV 682
Cdd:PLN03140 1303 VLIQTTYYTLIVYAMVAFEWTAAKFFWFYFISFFSFLYFTYYGMMTVSLTPNQQVAAIFAAAFYGLFNLFSGFFIprPKI 1382
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 79597808 683 PVFISWIRYLSFNYHTYKLLLKVQYQDFAVSINGMRIDNGLT 724
Cdd:PLN03140 1383 PKWWVWYYWICPVAWTVYGLIVSQYGDVEDTIKVPGGAPDPT 1424
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
155-385 |
2.26e-49 |
|
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: 172.06 E-value: 2.26e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 155 IFLKFRDVTYKvvIKKLTSsvEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQS-STGGSVTYNDKPY--- 230
Cdd:cd03233 2 STLSWRNISFT--TGKGRS--KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvSVEGDIHYNGIPYkef 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 231 SKYLKSKIGFVTQDDVLFPHLTVKETLTYAARLRlpktltreqkkqraldviqelglercqdtmiGGAFVRGVSGGERKR 310
Cdd:cd03233 78 AEKYPGEIIYVSEEDVHFPTLTVRETLDFALRCK-------------------------------GNEFVRGISGGERKR 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79597808 311 VSIGNEIIINPSLLLLDEPTSGLDSTTALRTILMLHDIAEA-GKTVITTIHQPSSRLFHRFDKLILLGRGSLLYFG 385
Cdd:cd03233 127 VSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVlKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
177-394 |
2.37e-47 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 167.93 E-value: 2.37e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 177 KEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYSKY---LKSKIGFVTQDDVLFPHLTV 253
Cdd:COG1131 13 KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTS--GEVRVLGEDVARDpaeVRRRIGYVPQEPALYPDLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 254 KETLTYAARLRlpkTLTREQKKQRALDVIQELGLERCQDTMiggafVRGVSGGERKRVSIGNEIIINPSLLLLDEPTSGL 333
Cdd:COG1131 91 RENLRFFARLY---GLPRKEARERIDELLELFGLTDAADRK-----VGTLSGGMKQRLGLALALLHDPELLILDEPTSGL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79597808 334 DSTTALRTILMLHDIAEAGKTVITTIHQPS--SRLFHRfdkLILLGRGSLLYFGKSSEALDYF 394
Cdd:COG1131 163 DPEARRELWELLRELAAEGKTVLLSTHYLEeaERLCDR---VAIIDKGRIVADGTPDELKARL 222
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
503-705 |
1.28e-44 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 158.98 E-value: 1.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 503 LFCRGLKER-RHEYFSWLRVTQVLSTAVILGLLWWQSDirTPMGLQDQAGLLFFIAVFWGFFPVFTAIFAFPQERAMLNK 581
Cdd:pfam01061 1 LLKREFLRRwRDPSLGLWRLIQPILMALIFGTLFGNLG--NQQGGLNRPGLLFFSILFNAFSALSGISPVFEKERGVLYR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 582 ERAADMYRLSAYFLARTTSDLPLDFILPSLFLLVVYFMTGLRISPYPFFLSMLTVFLCIIAAQGLGLAIGAILMDLKKAT 661
Cdd:pfam01061 79 ELASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDAS 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 79597808 662 TLASVTVMTFMLAGGFFV--KKVPVFISWIRYLSFNYHTYKLLLKV 705
Cdd:pfam01061 159 QLGPLVLLPLLLLSGFFIpiDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
168-383 |
1.20e-41 |
|
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: 151.93 E-value: 1.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 168 IKKLTSSV-EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYSKY---LKSKIGFVTQ 243
Cdd:COG4555 4 VENLSKKYgKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDS--GSILIDGEDVRKEpreARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 244 DDVLFPHLTVKETLTYAARLRLpktLTREQKKQRALDVIQELGLERCQDTMiggafVRGVSGGERKRVSIGNEIIINPSL 323
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELYG---LFDEELKKRIEELIELLGLEEFLDRR-----VGELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79597808 324 LLLDEPTSGLD--STTALRTILMLHdiAEAGKTVITTIHQPS--SRLfhrFDKLILLGRGSLLY 383
Cdd:COG4555 154 LLLDEPTNGLDvmARRLLREILRAL--KKEGKTVLFSSHIMQevEAL---CDRVVILHKGKVVA 212
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
157-381 |
4.92e-41 |
|
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: 149.56 E-value: 4.92e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 157 LKFRDV--TYKvvikklTSSVEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRisQSSTGGSVTYNDKPYSK-- 232
Cdd:cd03255 1 IELKNLskTYG------GGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGL--DRPTSGEVRVDGTDISKls 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 233 ------YLKSKIGFVTQDDVLFPHLTVKETLTYAARLRlpkTLTREQKKQRALDVIQELGLERCQDtmiggAFVRGVSGG 306
Cdd:cd03255 73 ekelaaFRRRHIGFVFQSFNLLPDLTALENVELPLLLA---GVPKKERRERAEELLERVGLGDRLN-----HYPSELSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79597808 307 ERKRVSIGNEIIINPSLLLLDEPTSGLDSTTALRTILMLHDIA-EAGKTVITTIHQPssRLFHRFDKLILLGRGSL 381
Cdd:cd03255 145 QQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNkEAGTTIVVVTHDP--ELAEYADRIIELRDGKI 218
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
170-693 |
2.53e-40 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 160.40 E-value: 2.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 170 KLTSSVEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQS-STGGSVTYNDKPYSKYLKSKI-GFVTQDDVL 247
Cdd:PLN03140 171 NLAKKTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlKVSGEITYNGYRLNEFVPRKTsAYISQNDVH 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 248 FPHLTVKETLTYAARLR-------LPKTLTREQK--------------KQRALDVIQE----------LGLERCQDTMIG 296
Cdd:PLN03140 251 VGVMTVKETLDFSARCQgvgtrydLLSELARREKdagifpeaevdlfmKATAMEGVKSslitdytlkiLGLDICKDTIVG 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 297 GAFVRGVSGGERKRVSIGnEIIINPS-LLLLDEPTSGLDSTTALRTILMLHDI---AEAgkTVITTIHQPSSRLFHRFDK 372
Cdd:PLN03140 331 DEMIRGISGGQKKRVTTG-EMIVGPTkTLFMDEISTGLDSSTTYQIVKCLQQIvhlTEA--TVLMSLLQPAPETFDLFDD 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 373 LILLGRGSLLYFGKSSEALDYFSSIGCSPLIAMNPAEFLLDlangnindisVPSELDDRVQVGNSGRETQTgkpspAAVH 452
Cdd:PLN03140 408 IILLSEGQIVYQGPRDHILEFFESCGFKCPERKGTADFLQE----------VTSKKDQEQYWADRNKPYRY-----ISVS 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 453 EYLVEAYETRVAEQEKKKLLdpVPLDEEAKAKSTRLKRQWG--------TCWWEQYCILfcrglkeRRHEYFSWLRVTQV 524
Cdd:PLN03140 473 EFAERFKSFHVGMQLENELS--VPFDKSQSHKAALVFSKYSvpkmellkACWDKEWLLM-------KRNAFVYVFKTVQI 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 525 LSTAVILGLLWwqsdIRTPMGLQDQA------GLLFF---IAVFWGFFPVFTAIFAFPqeraMLNKERAADMYRLSAYFL 595
Cdd:PLN03140 544 IIVAAIASTVF----LRTEMHTRNEEdgalyiGALLFsmiINMFNGFAELALMIQRLP----VFYKQRDLLFHPPWTFTL 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 596 ARTTSDLPLDFILPSLFLLVVYFMTGLRISPYPFFLSMLTVFLCIIAAQGLGLAIGAILMDLKKATTLASVTVMTFMLAG 675
Cdd:PLN03140 616 PTFLLGIPISIIESVVWVVITYYSIGFAPEASRFFKQLLLVFLIQQMAAGIFRLIASVCRTMIIANTGGALVLLLVFLLG 695
|
570 580
....*....|....*....|
gi 79597808 676 GFFVKK--VPVFISWIRYLS 693
Cdd:PLN03140 696 GFILPKgeIPNWWEWAYWVS 715
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
180-331 |
1.00e-39 |
|
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: 143.56 E-value: 1.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 180 LTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRIsqSSTGGSVTYNDKPYS----KYLKSKIGFVTQDDVLFPHLTVKE 255
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLL--SPTEGTILLDGQDLTdderKSLRKEIGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79597808 256 TLTYAARLrlpKTLTREQKKQRALDVIQELGLERCQDTMIgGAFVRGVSGGERKRVSIGNEIIINPSLLLLDEPTS 331
Cdd:pfam00005 79 NLRLGLLL---KGLSKREKDARAEEALEKLGLGDLADRPV-GERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
157-376 |
1.87e-39 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 145.19 E-value: 1.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 157 LKFRDVT--YKvvikklTSSVEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYS--- 231
Cdd:COG1136 5 LELRNLTksYG------TGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTS--GEVLIDGQDISsls 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 232 -----KYLKSKIGFVTQDDVLFPHLTVKETLTYAARLRlpkTLTREQKKQRALDVIQELGLERCQDtmiggAFVRGVSGG 306
Cdd:COG1136 77 erelaRLRRRHIGFVFQFFNLLPELTALENVALPLLLA---GVSRKERRERARELLERVGLGDRLD-----HRPSQLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79597808 307 ERKRVSIGNEIIINPSLLLLDEPTSGLDSTTALRTILMLHDIA-EAGKTVITTIHQPssRLFHRFDKLILL 376
Cdd:COG1136 149 QQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNrELGTTIVMVTHDP--ELAARADRVIRL 217
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
166-389 |
1.96e-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: 142.26 E-value: 1.96e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 166 VVIKKLT---SSVEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRIsqSSTGGSVT---YNDKPYSKYLKSKIG 239
Cdd:cd03263 1 LQIRNLTktyKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGEL--RPTSGTAYingYSIRTDRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 240 FVTQDDVLFPHLTVKETLTYAARLrlpKTLTREQKKQRALDVIQELGLERCQDTmiggaFVRGVSGGERKRVSIGNEIII 319
Cdd:cd03263 79 YCPQFDALFDELTVREHLRFYARL---KGLPKSEIKEEVELLLRVLGLTDKANK-----RARTLSGGMKRKLSLAIALIG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79597808 320 NPSLLLLDEPTSGLDSTTalRTIL--MLHDIAEaGKTVITTIHQP--SSRLFHRfdkLILLGRGSLLYFGKSSE 389
Cdd:cd03263 151 GPSVLLLDEPTSGLDPAS--RRAIwdLILEVRK-GRSIILTTHSMdeAEALCDR---IAIMSDGKLRCIGSPQE 218
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
158-379 |
2.01e-38 |
|
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: 141.84 E-value: 2.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 158 KFRDVTYKVvikkltSSVEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYSKY---- 233
Cdd:cd03225 1 ELKNLSFSY------PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTS--GEVLVDGKDLTKLslke 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 234 LKSKIGFVTQD-DVLFPHLTVKETLTYAARLRlpkTLTREQKKQRALDVIQELGLERCQDTMIggafvRGVSGGERKRVS 312
Cdd:cd03225 73 LRRKVGLVFQNpDDQFFGPTVEEEVAFGLENL---GLPEEEIEERVEEALELVGLEGLRDRSP-----FTLSGGQKQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 79597808 313 IGNEIIINPSLLLLDEPTSGLDSTTALRTILMLHDIAEAGKTVITTIHQPsSRLFHRFDKLILLGRG 379
Cdd:cd03225 145 IAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDL-DLLLELADRVIVLEDG 210
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
154-351 |
2.94e-38 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 142.92 E-value: 2.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 154 PIFLKFRDV--TYKvvikklTSSVEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYS 231
Cdd:COG1116 5 APALELRGVskRFP------TGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTS--GEVLVDGKPVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 232 KyLKSKIGFVTQDDVLFPHLTVKETLTYAARLRlpkTLTREQKKQRALDVIQELGLERCQDtmiggAFVRGVSGGERKRV 311
Cdd:COG1116 77 G-PGPDRGVVFQEPALLPWLTVLDNVALGLELR---GVPKAERRERARELLELVGLAGFED-----AYPHQLSGGMRQRV 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 79597808 312 SIGNEIIINPSLLLLDEPTSGLDSTTALR--------------TILML-HDIAEA 351
Cdd:COG1116 148 AIARALANDPEVLLMDEPFGALDALTRERlqdellrlwqetgkTVLFVtHDVDEA 202
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
157-351 |
5.40e-38 |
|
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: 141.07 E-value: 5.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 157 LKFRDVT--YKvvikklTSSVEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYSKyL 234
Cdd:cd03293 1 LEVRNVSktYG------GGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTS--GEVLVDGEPVTG-P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 235 KSKIGFVTQDDVLFPHLTVKETLTYAARLRLpktLTREQKKQRALDVIQELGLERCQDtmiggAFVRGVSGGERKRVSIG 314
Cdd:cd03293 72 GPDRGYVFQQDALLPWLTVLDNVALGLELQG---VPKAEARERAEELLELVGLSGFEN-----AYPHQLSGGMRQRVALA 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 79597808 315 NEIIINPSLLLLDEPTSGLDSTTAL--------------RTILML-HDIAEA 351
Cdd:cd03293 144 RALAVDPDVLLLDEPFSALDALTREqlqeelldiwretgKTVLLVtHDIDEA 195
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
176-392 |
2.09e-37 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 140.22 E-value: 2.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYSKyLKSKIGFVTQD---DVLFPhLT 252
Cdd:COG1121 18 GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTS--GTVRLFGKPPRR-ARRRIGYVPQRaevDWDFP-IT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 253 VKET--LTYAARLRLPKTLTREQkKQRALDVIQELGLERCQDTMIGgafvrGVSGGERKRVSIGNEIIINPSLLLLDEPT 330
Cdd:COG1121 94 VRDVvlMGRYGRRGLFRRPSRAD-REAVDEALERVGLEDLADRPIG-----ELSGGQQQRVLLARALAQDPDLLLLDEPF 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79597808 331 SGLDSTTAlRTIL-MLHDIAEAGKTVITTIHQPSSrLFHRFDKLILLGRGsLLYFGKSSEALD 392
Cdd:COG1121 168 AGVDAATE-EALYeLLRELRREGKTILVVTHDLGA-VREYFDRVLLLNRG-LVAHGPPEEVLT 227
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
157-391 |
3.60e-37 |
|
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: 139.00 E-value: 3.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 157 LKFRDVTYKVvikkltsSVEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYSKY--- 233
Cdd:COG1122 1 IELENLSFSY-------PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTS--GEVLVDGKDITKKnlr 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 234 -LKSKIGFVTQ--DDVLFpHLTVKETLTYAAR-LRLPktltREQKKQRALDVIQELGLERCQDtmiggafvRGV---SGG 306
Cdd:COG1122 72 eLRRKVGLVFQnpDDQLF-APTVEEDVAFGPEnLGLP----REEIRERVEEALELVGLEHLAD--------RPPhelSGG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 307 ERKRVSIGNEIIINPSLLLLDEPTSGLDSTTALRTILMLHDIAEAGKTVITTIHQPSSrLFHRFDKLILLGRGSLLYFGK 386
Cdd:COG1122 139 QKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDL-VAELADRVIVLDDGRIVADGT 217
|
....*
gi 79597808 387 SSEAL 391
Cdd:COG1122 218 PREVF 222
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
176-385 |
1.04e-36 |
|
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: 137.27 E-value: 1.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRIsqSSTGGSVTYNDKPYSKYLKSK--IGFVTQDDVLFPHLTV 253
Cdd:cd03259 12 SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLE--RPDSGEILIDGRDVTGVPPERrnIGMVFQDYALFPHLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 254 KETLTYAARLRLPKtltREQKKQRALDVIQELGLERcqdtmIGGAFVRGVSGGERKRVSIGNEIIINPSLLLLDEPTSGL 333
Cdd:cd03259 90 AENIAFGLKLRGVP---KAEIRARVRELLELVGLEG-----LLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSAL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 79597808 334 D--STTALRTiLMLHDIAEAGKTVITTIHQPSSRLfhRF-DKLILLGRGSLLYFG 385
Cdd:cd03259 162 DakLREELRE-ELKELQRELGITTIYVTHDQEEAL--ALaDRIAVMNEGRIVQVG 213
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
157-375 |
1.59e-36 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 136.72 E-value: 1.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 157 LKFRDVTYKVvikkltsSVEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYSK---- 232
Cdd:COG2884 2 IRFENVSKRY-------PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTS--GQVLVNGQDLSRlkrr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 233 ---YLKSKIGFVTQDDVLFPHLTVKETLTYAARLRlpkTLTREQKKQRALDVIQELGLERcqdtmIGGAFVRGVSGGERK 309
Cdd:COG2884 73 eipYLRRRIGVVFQDFRLLPDRTVYENVALPLRVT---GKSRKEIRRRVREVLDLVGLSD-----KAKALPHELSGGEQQ 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79597808 310 RVSIGNEIIINPSLLLLDEPTSGLDSTTALRTILMLHDIAEAGKTVITTIHQPSsrLFHRFDKLIL 375
Cdd:COG2884 145 RVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLE--LVDRMPKRVL 208
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
177-357 |
2.34e-35 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 133.38 E-value: 2.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 177 KEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQS-STGGSVTYNDKPYSKY--LKSKIGFVTQDDVLFPHLTV 253
Cdd:COG4136 14 RPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfSASGEVLLNGRRLTALpaEQRRIGILFQDDLLFPHLSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 254 KETLTYAarlrLPKTLTREQKKQRALDVIQELGLercqdtmiGGAFVRGV---SGGERKRVSIGNEIIINPSLLLLDEPT 330
Cdd:COG4136 94 GENLAFA----LPPTIGRAQRRARVEQALEEAGL--------AGFADRDPatlSGGQRARVALLRALLAEPRALLLDEPF 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 79597808 331 SGLDstTALR-----------------TILMLHDI--AEAGKTVIT 357
Cdd:COG4136 162 SKLD--AALRaqfrefvfeqirqrgipALLVTHDEedAPAAGRVLD 205
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
157-381 |
3.40e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 132.63 E-value: 3.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 157 LKFRDVTYKVVikkltssvEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQssTGGSVTYNDKPYSKY--- 233
Cdd:COG4619 1 LELEGLSFRVG--------GKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPP--TSGEIYLDGKPLSAMppp 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 234 -LKSKIGFVTQDDVLFPHlTVKETLTYAARLRlpktlTREQKKQRALDVIQELGLErcQDTMigGAFVRGVSGGERKRVS 312
Cdd:COG4619 71 eWRRQVAYVPQEPALWGG-TVRDNLPFPFQLR-----ERKFDRERALELLERLGLP--PDIL--DKPVERLSGGERQRLA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79597808 313 IGNEIIINPSLLLLDEPTSGLDSTTALRTILMLHD-IAEAGKTVITTIHQPssRLFHRF-DKLILLGRGSL 381
Cdd:COG4619 141 LIRALLLQPDVLLLDEPTSALDPENTRRVEELLREyLAEEGRAVLWVSHDP--EQIERVaDRVLTLEAGRL 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
166-381 |
4.60e-35 |
|
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: 130.98 E-value: 4.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 166 VVIKKLTSSV-EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYSKY---LKSKIGFV 241
Cdd:cd03230 1 IEVRNLSKRYgKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDS--GEIKVLGKDIKKEpeeVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 242 TQDDVLFPHLTVKETLTYaarlrlpktltreqkkqraldviqelglercqdtmiggafvrgvSGGERKRVSIGNEIIINP 321
Cdd:cd03230 79 PEEPSLYENLTVRENLKL--------------------------------------------SGGMKQRLALAQALLHDP 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79597808 322 SLLLLDEPTSGLDSTTALRTILMLHDIAEAGKTVITTIHQPS--SRLfhrFDKLILLGRGSL 381
Cdd:cd03230 115 ELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEeaERL---CDRVAILNNGRI 173
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
166-392 |
5.23e-35 |
|
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: 133.18 E-value: 5.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 166 VVIKKLTSSV-EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYSKY-------LKSK 237
Cdd:COG1127 6 IEVRNLTKSFgDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDS--GEILVDGQDITGLsekelyeLRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 238 IGFVTQDDVLFPHLTVKETLtyAARLRLPKTLTREQKKQRALDVIQELGLERCQDTMIGgafvrGVSGGERKRVSIGNEI 317
Cdd:COG1127 84 IGMLFQGGALFDSLTVFENV--AFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPS-----ELSGGMRKRVALARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79597808 318 IINPSLLLLDEPTSGLDSTTALRTILMLHDIAEA-GKTVITTIHQPSSrLFHRFDKLILLGRGSLLYFGKSSEALD 392
Cdd:COG1127 157 ALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDS-AFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
176-392 |
1.21e-34 |
|
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: 132.47 E-value: 1.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYSKY----LKSKIGFVTQDDVLFPHL 251
Cdd:COG1120 13 GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSS--GEVLLDGRDLASLsrreLARRIAYVPQEPPAPFGL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 252 TVKETLTYAarlRLP--KTLTREQKK--QRALDVIQELGLERCQDtmiggafvRGV---SGGERKRVSIGNEIIINPSLL 324
Cdd:COG1120 91 TVRELVALG---RYPhlGLFGRPSAEdrEAVEEALERTGLEHLAD--------RPVdelSGGERQRVLIARALAQEPPLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 325 LLDEPTSGLDSTTALRTILMLHDIA-EAGKTVITTIHQPSsrLFHRF-DKLILLGRGSLLYFGKSSEALD 392
Cdd:COG1120 160 LLDEPTSHLDLAHQLEVLELLRRLArERGRTVVMVLHDLN--LAARYaDRLVLLKDGRIVAQGPPEEVLT 227
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
180-381 |
2.36e-33 |
|
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: 127.52 E-value: 2.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 180 LTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYSK-------YLKSKIGFVTQDDVLFPHLT 252
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTS--GTIRVNGQDVSDlrgraipYLRRKIGVVFQDFRLLPDRN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 253 VKETLTYAarLRLPKTLTREQKKqRALDVIQELGLERCQDTMiggafVRGVSGGERKRVSIGNEIIINPSLLLLDEPTSG 332
Cdd:cd03292 95 VYENVAFA--LEVTGVPPREIRK-RVPAALELVGLSHKHRAL-----PAELSGGEQQRVAIARAIVNSPTILIADEPTGN 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 79597808 333 LDSTTALRTILMLHDIAEAGKTVITTIHqpSSRLFHRFDK-LILLGRGSL 381
Cdd:cd03292 167 LDPDTTWEIMNLLKKINKAGTTVVVATH--AKELVDTTRHrVIALERGKL 214
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
168-385 |
5.26e-33 |
|
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: 127.23 E-value: 5.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 168 IKKLTSSV-EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYSKY-------LKSKIG 239
Cdd:cd03261 3 LRGLTKSFgGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDS--GEVLIDGEDISGLseaelyrLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 240 FVTQDDVLFPHLTVKETLtyAARLRLPKTLTREQKKQRALDVIQELGLERCQDTMIGgafvrGVSGGERKRVSIGNEIII 319
Cdd:cd03261 81 MLFQSGALFDSLTVFENV--AFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPA-----ELSGGMKKRVALARALAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79597808 320 NPSLLLLDEPTSGLD---STTALRTILMLHDiaEAGKTVITTIHQPSSrLFHRFDKLILLGRGSLLYFG 385
Cdd:cd03261 154 DPELLLYDEPTAGLDpiaSGVIDDLIRSLKK--ELGLTSIMVTHDLDT-AFAIADRIAVLYDGKIVAEG 219
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
176-378 |
5.87e-33 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 126.05 E-value: 5.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYSK---YLKSKIGFVTQDDVLFPHLT 252
Cdd:COG4133 14 ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSA--GEVLWNGEPIRDareDYRRRLAYLGHADGLKPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 253 VKETLTYAARLRlPKTLTREqkkqRALDVIQELGLERCQDTmiggaFVRGVSGGERKRVSIGNEIIINPSLLLLDEPTSG 332
Cdd:COG4133 92 VRENLRFWAALY-GLRADRE----AIDEALEAVGLAGLADL-----PVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 79597808 333 LD--STTALRTILMLHdiAEAGKTVITTIHQPssrLFHRFDKLILLGR 378
Cdd:COG4133 162 LDaaGVALLAELIAAH--LARGGAVLLTTHQP---LELAAARVLDLGD 204
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
189-385 |
8.01e-33 |
|
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: 126.26 E-value: 8.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 189 PGEVLALMGPSGSGKTTLLSLLAGRISqsSTGGSVTYNDKPY---SKYL-----KSKIGFVTQDDVLFPHLTVKETLTYA 260
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEK--PDGGTIVLNGTVLfdsRKKInlppqQRKIGLVFQQYALFPHLNVRENLAFG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 261 ARLRLPKtltreQKKQRALDVIQELGLERcqdtmIGGAFVRGVSGGERKRVSIGNEIIINPSLLLLDEPTSGLDstTALR 340
Cdd:cd03297 100 LKRKRNR-----EDRISVDELLDLLGLDH-----LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALD--RALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 79597808 341 TILM--LHDI-AEAGKTVITTIHQPsSRLFHRFDKLILLGRGSLLYFG 385
Cdd:cd03297 168 LQLLpeLKQIkKNLNIPVIFVTHDL-SEAEYLADRIVVMEDGRLQYIG 214
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
132-391 |
8.55e-33 |
|
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: 134.12 E-value: 8.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 132 EMIPEDIEAGKKKPKFQAEPTLpiflKFRDVTYkvvikklTSSVEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLA 211
Cdd:COG4988 316 DAPEPAAPAGTAPLPAAGPPSI----ELEDVSF-------SYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 212 GRISQSStgGSVTYNDKPYSKY----LKSKIGFVTQDDVLFpHLTVKETLTYAARlrlpkTLTREQ-----KKQRALDVI 282
Cdd:COG4988 385 GFLPPYS--GSILINGVDLSDLdpasWRRQIAWVPQNPYLF-AGTIRENLRLGRP-----DASDEEleaalEAAGLDEFV 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 283 QEL--GLercqDTMIG-GAfvRGVSGGERKRVSIGNEIIINPSLLLLDEPTSGLDSTTALRTILMLHDIAeAGKTVITTI 359
Cdd:COG4988 457 AALpdGL----DTPLGeGG--RGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILIT 529
|
250 260 270
....*....|....*....|....*....|..
gi 79597808 360 HQPSSRlfHRFDKLILLGRGSLLYFGKSSEAL 391
Cdd:COG4988 530 HRLALL--AQADRILVLDDGRIVEQGTHEELL 559
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
177-385 |
9.06e-33 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 125.72 E-value: 9.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 177 KEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYSKYLKsKIGFVTQD---DVLFPhLTV 253
Cdd:cd03235 12 HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTS--GSIRVFGKPLEKERK-RIGYVPQRrsiDRDFP-ISV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 254 KET--LTYAARLRLPKTLTREQKkQRALDVIQELGLERCQDTMIGGAfvrgvSGGERKRVSIGNEIIINPSLLLLDEPTS 331
Cdd:cd03235 88 RDVvlMGLYGHKGLFRRLSKADK-AKVDEALERVGLSELADRQIGEL-----SGGQQQRVLLARALVQDPDLLLLDEPFA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 79597808 332 GLDSTTALRTILMLHDIAEAGKTVITTIHQPSSrLFHRFDKLILLGRGsLLYFG 385
Cdd:cd03235 162 GVDPKTQEDIYELLRELRREGMTILVVTHDLGL-VLEYFDRVLLLNRT-VVASG 213
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
157-379 |
8.47e-32 |
|
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: 121.72 E-value: 8.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 157 LKFRDVTYKvvikklTSSVEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYSKY--- 233
Cdd:cd03228 1 IEFKNVSFS------YPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTS--GEILIDGVDLRDLdle 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 234 -LKSKIGFVTQDDVLFpHLTVKETLtyaarlrlpktltreqkkqraldviqelglercqdtmiggafvrgVSGGERKRVS 312
Cdd:cd03228 73 sLRKNIAYVPQDPFLF-SGTIRENI---------------------------------------------LSGGQRQRIA 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 79597808 313 IGNEIIINPSLLLLDEPTSGLDSTTALRTILMLHDIAEaGKTVITTIHQPSSrlFHRFDKLILLGRG 379
Cdd:cd03228 107 IARALLRDPPILILDEATSALDPETEALILEALRALAK-GKTVIVIAHRLST--IRDADRIIVLDDG 170
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
176-361 |
9.26e-32 |
|
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: 123.02 E-value: 9.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLL-------AGRIsqsSTGGSVTYNDKPYSKYLKSKIGFVTQDDVLF 248
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCInlleepdSGTI---IIDGLKLTDDKKNINELRQKVGMVFQQFNLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 249 PHLTVKETLTYAarLRLPKTLTREQKKQRALDVIQELGLERCQDtmiggAFVRGVSGGERKRVSIGNEIIINPSLLLLDE 328
Cdd:cd03262 89 PHLTVLENITLA--PIKVKGMSKAEAEERALELLEKVGLADKAD-----AYPAQLSGGQQQRVAIARALAMNPKVMLFDE 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 79597808 329 PTSGLDSTTA---LRTILmlhDIAEAGKTVITTIHQ 361
Cdd:cd03262 162 PTSALDPELVgevLDVMK---DLAEEGMTMVVVTHE 194
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
166-385 |
1.09e-31 |
|
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: 122.69 E-value: 1.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 166 VVIKKLTSSV-EKEILTGISGSVNPGeVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYSKY---LKSKIGFV 241
Cdd:cd03264 1 LQLENLTKRYgKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSS--GTIRIDGQDVLKQpqkLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 242 TQDDVLFPHLTVKETLTYAARLrlpKTLTREQKKQRALDVIQELGLERCQDTMIGGafvrgVSGGERKRVSIGNEIIINP 321
Cdd:cd03264 78 PQEFGVYPNFTVREFLDYIAWL---KGIPSKEVKARVDEVLELVNLGDRAKKKIGS-----LSGGMRRRVGIAQALVGDP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79597808 322 SLLLLDEPTSGLDSTTALRTILMLHDIAEaGKTVITTIHQPSSRLFHrFDKLILLGRGSLLYFG 385
Cdd:cd03264 150 SILIVDEPTAGLDPEERIRFRNLLSELGE-DRIVILSTHIVEDVESL-CNQVAVLNKGKLVFEG 211
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
179-360 |
1.49e-31 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 126.37 E-value: 1.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 179 ILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDK------PYskylKSKIGFVTQDDVLFPHLT 252
Cdd:COG3842 20 ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDS--GRILLDGRdvtglpPE----KRNVGMVFQDYALFPHLT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 253 VKETLTYAARLRlpkTLTREQKKQRALDVIQELGLERcqdtmIGGAFVRGVSGGERKRVSIGNEIIINPSLLLLDEPTSG 332
Cdd:COG3842 94 VAENVAFGLRMR---GVPKAEIRARVAELLELVGLEG-----LADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSA 165
|
170 180
....*....|....*....|....*....
gi 79597808 333 LDSTTALRTILMLHDI-AEAGktvITTIH 360
Cdd:COG3842 166 LDAKLREEMREELRRLqRELG---ITFIY 191
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
154-391 |
1.64e-31 |
|
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: 123.27 E-value: 1.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 154 PIFLKFRDVTykvVIKKltssvEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStGGSVTYNDKPYSKY 233
Cdd:COG1119 1 DPLLELRNVT---VRRG-----GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTY-GNDVRLFGERRGGE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 234 ----LKSKIGFVTQD--DVLFPHLTVKET-LT--YAArLRLPKTLTREQkKQRALDVIQELGLERCQDTMIGgafvrGVS 304
Cdd:COG1119 72 dvweLRKRIGLVSPAlqLRFPRDETVLDVvLSgfFDS-IGLYREPTDEQ-RERARELLELLGLAHLADRPFG-----TLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 305 GGERKRVSIGNEIIINPSLLLLDEPTSGLDSTTALRTILMLHDIAEAGKTVITTI-HQ----PSSrlfhrFDKLILLGRG 379
Cdd:COG1119 145 QGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVtHHveeiPPG-----ITHVLLLKDG 219
|
250
....*....|..
gi 79597808 380 SLLYFGKSSEAL 391
Cdd:COG1119 220 RVVAAGPKEEVL 231
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
177-389 |
1.73e-31 |
|
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: 123.06 E-value: 1.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 177 KEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRIsqSSTGGSVTYNDKPYSKY-------LKSKIGFVTQDDVLFP 249
Cdd:cd03256 14 KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLV--EPTSGSVLIDGTDINKLkgkalrqLRRQIGMIFQQFNLIE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 250 HLTVKET-----LTYAARLR-LPKTLTREQkKQRALDVIQELGLE-----RCqDTMiggafvrgvSGGERKRVSIGNEII 318
Cdd:cd03256 92 RLSVLENvlsgrLGRRSTWRsLFGLFPKEE-KQRALAALERVGLLdkayqRA-DQL---------SGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79597808 319 INPSLLLLDEPTSGLDSTTALRTILMLHDIA-EAGKTVITTIHQPSsrLFHRF-DKLILLGRGSLLYFGKSSE 389
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINrEEGITVIVSLHQVD--LAREYaDRIVGLKDGRIVFDGPPAE 231
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
142-356 |
3.21e-31 |
|
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: 128.48 E-value: 3.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 142 KKKPKFQAEPTLPIFLKFRDVT--YKVVIKKltssvEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSSt 219
Cdd:COG1123 246 ARGRAAPAAAAAEPLLEVRNLSkrYPVRGKG-----GVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTS- 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 220 gGSVTYNDKPYSKY-------LKSKIGFVTQD--DVLFPHLTVKETLTYAARLRlpKTLTREQKKQRALDVIQELGLERc 290
Cdd:COG1123 320 -GSILFDGKDLTKLsrrslreLRRRVQMVFQDpySSLNPRMTVGDIIAEPLRLH--GLLSRAERRERVAELLERVGLPP- 395
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 79597808 291 qDTMigGAFVRGVSGGERKRVSIGNEIIINPSLLLLDEPTSGLDSTTALRTILMLHDI-AEAGKTVI 356
Cdd:COG1123 396 -DLA--DRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLqRELGLTYL 459
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
176-379 |
3.23e-31 |
|
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: 120.37 E-value: 3.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRIsqSSTGGSVTYNDKPYSKY------LKSKIGFVTQDDVLFP 249
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLE--EPDSGSILIDGEDLTDLedelppLRRRIGMVFQDFALFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 250 HLTVKETLTYaarlrlpktltreqkkqraldviqelglercqdtmiggafvrGVSGGERKRVSIGNEIIINPSLLLLDEP 329
Cdd:cd03229 90 HLTVLENIAL------------------------------------------GLSGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 79597808 330 TSGLDSTTALRTILMLHDI-AEAGKTVITTIHQPSSrLFHRFDKLILLGRG 379
Cdd:cd03229 128 TSALDPITRREVRALLKSLqAQLGITVVLVTHDLDE-AARLADRVVVLRDG 177
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
157-356 |
3.71e-31 |
|
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: 121.84 E-value: 3.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 157 LKFRDVTYKVVIKKLTssveKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQssTGGSVTYNDKPYS----- 231
Cdd:cd03257 2 LEVKNLSVSFPTGGGS----VKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKP--TSGSIIFDGKDLLklsrr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 232 --KYLKSKIGFVTQD--DVLFPHLTVKETLTYAARLRLPKTlTREQKKQRALDVIQELGL-ERCQDtmiggAFVRGVSGG 306
Cdd:cd03257 76 lrKIRRKEIQMVFQDpmSSLNPRMTIGEQIAEPLRIHGKLS-KKEARKEAVLLLLVGVGLpEEVLN-----RYPHELSGG 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 79597808 307 ERKRVSIGNEIIINPSLLLLDEPTSGLDSTTALRTILMLHDIAEA-GKTVI 356
Cdd:cd03257 150 QRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLL 200
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
180-391 |
5.11e-31 |
|
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: 121.67 E-value: 5.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 180 LTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSS-----TGGSVTyNDKPyskyLKSKIGFVTQDDVLFPHLTVK 254
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSgkillNGKDIT-NLPP----EKRDISYVPQNYALFPHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 255 ETLTYAARLRLPKtltREQKKQRALDVIQELGLERCQDTmiggaFVRGVSGGERKRVSIGNEIIINPSLLLLDEPTSGLD 334
Cdd:cd03299 90 KNIAYGLKKRKVD---KKEIERKVLEIAEMLGIDHLLNR-----KPETLSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79597808 335 STTALRTILMLHDIAEAGKTviTTIHqpssrLFHRF-------DKLILLGRGSLLYFGKSSEAL 391
Cdd:cd03299 162 VRTKEKLREELKKIRKEFGV--TVLH-----VTHDFeeawalaDKVAIMLNGKLIQVGKPEEVF 218
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
157-364 |
9.75e-31 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 127.97 E-value: 9.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 157 LKFRDVTYkvvikklTSSVEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAG--RIsqssTGGSVTYNDKPYSKY- 233
Cdd:COG1132 340 IEFENVSF-------SYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRfyDP----TSGRILIDGVDIRDLt 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 234 ---LKSKIGFVTQDDVLFpHLTVKETLTYAArlrlpKTLTREQ-----KKQRALDVIQEL--GLercqDTMIGGafvRGV 303
Cdd:COG1132 409 lesLRRQIGVVPQDTFLF-SGTIRENIRYGR-----PDATDEEveeaaKAAQAHEFIEALpdGY----DTVVGE---RGV 475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79597808 304 --SGGERKRVSIGNEIIINPSLLLLDEPTSGLDSTT------ALRTILmlhdiaeAGKTVITTIHQPSS 364
Cdd:COG1132 476 nlSGGQRQRIAIARALLKDPPILILDEATSALDTETealiqeALERLM-------KGRTTIVIAHRLST 537
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
176-385 |
1.93e-30 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 117.92 E-value: 1.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYSKY----LKSKIGFVTQddVLfphl 251
Cdd:cd03214 11 GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSS--GEILLDGKDLASLspkeLARKIAYVPQ--AL---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 252 tvketltyaARLRLpktltrEQKKQRaldVIQELglercqdtmiggafvrgvSGGERKRVSIGNEIIINPSLLLLDEPTS 331
Cdd:cd03214 83 ---------ELLGL------AHLADR---PFNEL------------------SGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 79597808 332 GLDSTTALRTILMLHDIA-EAGKTVITTIHQPSsrLFHRF-DKLILLGRGSLLYFG 385
Cdd:cd03214 127 HLDIAHQIELLELLRRLArERGKTVVMVLHDLN--LAARYaDRVILLKDGRIVAQG 180
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
157-381 |
7.49e-30 |
|
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: 125.26 E-value: 7.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 157 LKFRDVTYKvvikklTSSVEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRIsqSSTGGSVTYNDKPYSKY--- 233
Cdd:COG4987 334 LELEDVSFR------YPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFL--DPQSGSITLGGVDLRDLded 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 234 -LKSKIGFVTQDDVLFpHLTVKETLTYAArlrlpKTLTREQKKQrAL------DVIQEL--GLercqDTMIG--GafvRG 302
Cdd:COG4987 406 dLRRRIAVVPQRPHLF-DTTLRENLRLAR-----PDATDEELWA-ALervglgDWLAALpdGL----DTWLGegG---RR 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 303 VSGGERKRVSIGNEIIINPSLLLLDEPTSGLDSTTALRtilMLHDIAEA--GKTVITTIHQPSsrLFHRFDKLILLGRGS 380
Cdd:COG4987 472 LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQA---LLADLLEAlaGRTVLLITHRLA--GLERMDRILVLEDGR 546
|
.
gi 79597808 381 L 381
Cdd:COG4987 547 I 547
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
157-391 |
1.98e-29 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 124.95 E-value: 1.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 157 LKFRDVTYKVvikkltSSVEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYSKY--- 233
Cdd:COG2274 474 IELENVSFRY------PGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTS--GRILIDGIDLRQIdpa 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 234 -LKSKIGFVTQDDVLFpHLTVKETLTYAArlrlpKTLTREQ-----KKQRALDVIQEL--GLercqDTMIG--GAfvrGV 303
Cdd:COG2274 546 sLRRQIGVVLQDVFLF-SGTIRENITLGD-----PDATDEEiieaaRLAGLHDFIEALpmGY----DTVVGegGS---NL 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 304 SGGERKRVSIGNEIIINPSLLLLDEPTSGLDSTTALRTILMLHDIAeAGKTVITTIHQPSsrLFHRFDKLILLGRGSLLY 383
Cdd:COG2274 613 SGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLS--TIRLADRIIVLDKGRIVE 689
|
....*...
gi 79597808 384 FGKSSEAL 391
Cdd:COG2274 690 DGTHEELL 697
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
176-409 |
2.07e-29 |
|
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: 123.09 E-value: 2.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSST-GGSVTYNDKPYSKY----LKSKIGFVTQD--DVLF 248
Cdd:COG1123 18 DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRiSGEVLLDGRDLLELsealRGRRIGMVFQDpmTQLN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 249 PhLTVKETLTYAARLRLpktLTREQKKQRALDVIQELGLERcqdtmIGGAFVRGVSGGERKRVSIGNEIIINPSLLLLDE 328
Cdd:COG1123 98 P-VTVGDQIAEALENLG---LSRAEARARVLELLEAVGLER-----RLDRYPHQLSGGQRQRVAIAMALALDPDLLIADE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 329 PTSGLDSTTALRTILMLHDI-AEAGKTVITTIHQPsSRLFHRFDKLILLGRGSLLYFGKSSEALDYFSSIGCSPLIAMNP 407
Cdd:COG1123 169 PTTALDVTTQAEILDLLRELqRERGTTVLLITHDL-GVVAEIADRVVVMDDGRIVEDGPPEEILAAPQALAAVPRLGAAR 247
|
..
gi 79597808 408 AE 409
Cdd:COG1123 248 GR 249
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
176-356 |
2.07e-29 |
|
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: 117.21 E-value: 2.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYS----KYLKSKIGFVTQD--DVLFP 249
Cdd:COG1124 17 RVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWS--GEVTFDGRPVTrrrrKAFRRRVQMVFQDpyASLHP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 250 HLTVKETLTYAARLrlpktLTREQKKQRALDVIQELGL-----ERcqdtmiggaFVRGVSGGERKRVSIGNEIIINPSLL 324
Cdd:COG1124 95 RHTVDRILAEPLRI-----HGLPDREERIAELLEQVGLppsflDR---------YPHQLSGGQRQRVAIARALILEPELL 160
|
170 180 190
....*....|....*....|....*....|....*
gi 79597808 325 LLDEPTSGLD-STTALrtIL-MLHDI-AEAGKTVI 356
Cdd:COG1124 161 LLDEPTSALDvSVQAE--ILnLLKDLrEERGLTYL 193
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
176-379 |
2.68e-29 |
|
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: 113.88 E-value: 2.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISqsSTGGSVTYNDKPYSKY----LKSKIGFVTQddvlfphl 251
Cdd:cd00267 11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLK--PTSGEILIDGKDIAKLpleeLRRRIGYVPQ-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 252 tvketltyaarlrlpktltreqkkqraldviqelglercqdtmiggafvrgVSGGERKRVSIGNEIIINPSLLLLDEPTS 331
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 79597808 332 GLDSTTALRTILMLHDIAEAGKTVITTIHQPSSrLFHRFDKLILLGRG 379
Cdd:cd00267 110 GLDPASRERLLELLRELAEEGRTVIIVTHDPEL-AELAADRVIVLKDG 156
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
176-334 |
5.35e-29 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 115.86 E-value: 5.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAG--RIsqssTGGSVTYNDKPYS------KYLKSKIGFVTQDDVL 247
Cdd:COG1126 13 DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLleEP----DSGTITVDGEDLTdskkdiNKLRRKVGMVFQQFNL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 248 FPHLTVKETLTYAarLRLPKTLTREQKKQRALDVIQELGL-ERCQdtmiggAFVRGVSGGERKRVSIGNEIIINPSLLLL 326
Cdd:COG1126 89 FPHLTVLENVTLA--PIKVKKMSKAEAEERAMELLERVGLaDKAD------AYPAQLSGGQQQRVAIARALAMEPKVMLF 160
|
....*...
gi 79597808 327 DEPTSGLD 334
Cdd:COG1126 161 DEPTSALD 168
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
176-379 |
1.15e-28 |
|
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: 113.91 E-value: 1.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGrISQSSTgGSVTYNDKPYSKYLKSKIGFVTQDDVLFPHLTVKE 255
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILG-IILPDS-GEVLFDGKPLDIAARNRIGYLPEERGLYPKMKVID 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 256 TLTYAARLrlpKTLTREQKKQRALDVIQELGLERCQDTMiggafVRGVSGGERKRVSIGNEIIINPSLLLLDEPTSGLD- 334
Cdd:cd03269 90 QLVYLAQL---KGLKKEEARRRIDEWLERLELSEYANKR-----VEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDp 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 79597808 335 -STTALRTILMlhDIAEAGKTVITTIHQpsSRLFHRF-DKLILLGRG 379
Cdd:cd03269 162 vNVELLKDVIR--ELARAGKTVILSTHQ--MELVEELcDRVLLLNKG 204
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
159-392 |
1.24e-28 |
|
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: 114.63 E-value: 1.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 159 FRDVTYKVvikkltsSVEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAgRISQSStGGSVTYNDKPYSKY----L 234
Cdd:cd03253 3 FENVTFAY-------DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLF-RFYDVS-SGSILIDGQDIREVtldsL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 235 KSKIGFVTQDDVLFpHLTVKETLTYAarlRLpkTLTREQ-----KKQRALDVIqeLGLERCQDTMIGGafvRGV--SGGE 307
Cdd:cd03253 74 RRAIGVVPQDTVLF-NDTIGYNIRYG---RP--DATDEEvieaaKAAQIHDKI--MRFPDGYDTIVGE---RGLklSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 308 RKRVSIGNEIIINPSLLLLDEPTSGLDSTT------ALRTILmlhdiaeAGKTVITTIHQPSSrlFHRFDKLILLGRGSL 381
Cdd:cd03253 143 KQRVAIARAILKNPPILLLDEATSALDTHTereiqaALRDVS-------KGRTTIVIAHRLST--IVNADKIIVLKDGRI 213
|
250
....*....|.
gi 79597808 382 LYFGKSSEALD 392
Cdd:cd03253 214 VERGTHEELLA 224
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
173-334 |
2.26e-28 |
|
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: 113.87 E-value: 2.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 173 SSVEKE-----ILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGriSQSSTGGSVTYNDKPYSKYL--KSKIGFVTQDD 245
Cdd:cd03300 4 ENVSKFyggfvALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAG--FETPTSGEILLDGKDITNLPphKRPVNTVFQNY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 246 VLFPHLTVKETLTYAARLR-LPKTLTREQKKqRALDVIQELGLERcqdtmiggAFVRGVSGGERKRVSIGNEIIINPSLL 324
Cdd:cd03300 82 ALFPHLTVFENIAFGLRLKkLPKAEIKERVA-EALDLVQLEGYAN--------RKPSQLSGGQQQRVAIARALVNEPKVL 152
|
170
....*....|
gi 79597808 325 LLDEPTSGLD 334
Cdd:cd03300 153 LLDEPLGALD 162
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
180-356 |
4.36e-28 |
|
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: 113.30 E-value: 4.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 180 LTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKP---YSKYLKSKIGFV-T-QDDVLFPHLTVK 254
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTS--GSVLFDGEDitgLPPHEIARLGIGrTfQIPRLFPELTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 255 ETLTYAARLRLPKTL-------TREQKKQRALDVIQELGLERCQDTMIGGafvrgVSGGERKRVSIGNEIIINPSLLLLD 327
Cdd:cd03219 94 ENVMVAAQARTGSGLllararrEEREARERAEELLERVGLADLADRPAGE-----LSYGQQRRLEIARALATDPKLLLLD 168
|
170 180
....*....|....*....|....*....
gi 79597808 328 EPTSGLDSTTALRTILMLHDIAEAGKTVI 356
Cdd:cd03219 169 EPAAGLNPEETEELAELIRELRERGITVL 197
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
180-385 |
7.43e-28 |
|
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: 112.08 E-value: 7.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 180 LTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYSK---YLKSKIGFVTQDDVLFPHLTVKET 256
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDA--GFATVDGFDVVKepaEARRRLGFVSDSTGLYDRLTAREN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 257 LTYAARLRlpkTLTREQKKQRALDVIQELGLERCQDTMIGGafvrgVSGGERKRVSIGNEIIINPSLLLLDEPTSGLD-- 334
Cdd:cd03266 99 LEYFAGLY---GLKGDELTARLEELADRLGMEELLDRRVGG-----FSTGMRQKVAIARALVHDPPVLLLDEPTTGLDvm 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 79597808 335 STTALRTIlmLHDIAEAGKTVITTIH--QPSSRLfhrFDKLILLGRGSLLYFG 385
Cdd:cd03266 171 ATRALREF--IRQLRALGKCILFSTHimQEVERL---CDRVVVLHRGRVVYEG 218
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
180-356 |
8.38e-28 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 115.24 E-value: 8.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 180 LTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYSKYL---KSKIGFVTQDDVLFPHLTVKET 256
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDS--GRIVLNGRDLFTNLpprERRVGFVFQHYALFPHMTVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 257 LTYAARLRLPktlTREQKKQRALDVIQELGLERcqdtmIGGAFVRGVSGGERKRVSIGNEIIINPSLLLLDEPTSGLDS- 335
Cdd:COG1118 96 IAFGLRVRPP---SKAEIRARVEELLELVQLEG-----LADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAk 167
|
170 180
....*....|....*....|...
gi 79597808 336 -TTALRTILM-LHDiaEAGKTVI 356
Cdd:COG1118 168 vRKELRRWLRrLHD--ELGGTTV 188
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
149-381 |
9.73e-28 |
|
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: 112.14 E-value: 9.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 149 AEPTLPIfLKFRDVTYKVVikklTSSVEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRisQSSTGGSVTYNDK 228
Cdd:COG4181 2 SSSSAPI-IELRGLTKTVG----TGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGL--DRPTSGTVRLAGQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 229 PYS--------KYLKSKIGFVTQDDVLFPHLTVKETLTyaarlrLPKTLTRE-QKKQRALDVIQELGL-ERCqdtmigGA 298
Cdd:COG4181 75 DLFaldedaraRLRARHVGFVFQSFQLLPTLTALENVM------LPLELAGRrDARARARALLERVGLgHRL------DH 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 299 FVRGVSGGERKRVSIGNEIIINPSLLLLDEPTSGLDSTTALRTILMLHDI-AEAGKTVITTIHQPssRLFHRFDKLILLG 377
Cdd:COG4181 143 YPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELnRERGTTLVLVTHDP--ALAARCDRVLRLR 220
|
....
gi 79597808 378 RGSL 381
Cdd:COG4181 221 AGRL 224
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
166-356 |
1.08e-27 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 115.17 E-value: 1.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 166 VVIKKLTSSV-EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAG--RIsqssTGGSVTYNDKPYSKyLKSK---IG 239
Cdd:COG3839 4 LELENVSKSYgGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGleDP----TSGEILIGGRDVTD-LPPKdrnIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 240 FVTQDDVLFPHLTVKETLTYAARLR-LPKTlTREQKKQRALDV--IQELgLERcqdtmiggaFVRGVSGGERKRVSIGNE 316
Cdd:COG3839 79 MVFQSYALYPHMTVYENIAFPLKLRkVPKA-EIDRRVREAAELlgLEDL-LDR---------KPKQLSGGQRQRVALGRA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 79597808 317 IIINPSLLLLDEPTSGLD--STTALRTILM-LHdiAEAGKTVI 356
Cdd:COG3839 148 LVREPKVFLLDEPLSNLDakLRVEMRAEIKrLH--RRLGTTTI 188
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
168-334 |
5.86e-27 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 110.16 E-value: 5.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 168 IKKLTSSVE-KEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSSTGGSVTYNDKPYSKYL-----KSKIGFV 241
Cdd:COG0396 3 IKNLHVSVEgKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKYEVTSGSILLDGEDILELSpderaRAGIFLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 242 TQDDVLFPHLTVKETLTYAARLRLPKTLTREQKKQRALDVIQELGLERcqdtmiggAFV-RGV----SGGERKRvsigNE 316
Cdd:COG0396 83 FQYPVEIPGVSVSNFLRTALNARRGEELSAREFLKLLKEKMKELGLDE--------DFLdRYVnegfSGGEKKR----NE 150
|
170 180
....*....|....*....|..
gi 79597808 317 I----IINPSLLLLDEPTSGLD 334
Cdd:COG0396 151 IlqmlLLEPKLAILDETDSGLD 172
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
166-383 |
7.79e-27 |
|
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: 108.84 E-value: 7.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 166 VVIKKLTSSV-EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYSKYLK--SKIGFVT 242
Cdd:cd03268 1 LKTNDLTKTYgKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDS--GEITFDGKSYQKNIEalRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 243 QDDVLFPHLTVKETLTYAARLrlpkTLTREQKKQRALDVIqelGLERcqdtmIGGAFVRGVSGGERKRVSIGNEIIINPS 322
Cdd:cd03268 79 EAPGFYPNLTARENLRLLARL----LGIRKKRIDEVLDVV---GLKD-----SAKKKVKGFSLGMKQRLGIALALLGNPD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79597808 323 LLLLDEPTSGLD--STTALRTILMLHdiAEAGKTVITTIHQpSSRLFHRFDKLILLGRGSLLY 383
Cdd:cd03268 147 LLILDEPTNGLDpdGIKELRELILSL--RDQGITVLISSHL-LSEIQKVADRIGIINKGKLIE 206
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
176-351 |
9.01e-27 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 109.95 E-value: 9.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYSKyLKSKIGFVTQDDVLFPHLTVKE 255
Cdd:COG4525 19 PQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSS--GEITLDGVPVTG-PGADRGVVFQKDALLPWLNVLD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 256 TLTYAARLRlpkTLTREQKKQRALDVIQELGLERcqdtmIGGAFVRGVSGGERKRVSIGNEIIINPSLLLLDEPTSGLDS 335
Cdd:COG4525 96 NVAFGLRLR---GVPKAERRARAEELLALVGLAD-----FARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDA 167
|
170 180 190
....*....|....*....|....*....|.
gi 79597808 336 TT-----AL---------RTILML-HDIAEA 351
Cdd:COG4525 168 LTreqmqELlldvwqrtgKGVFLItHSVEEA 198
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
176-389 |
9.65e-27 |
|
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: 108.81 E-value: 9.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAG---RISQSSTGGSVTYNDKPYSKY------LKSKIGFVTQDDV 246
Cdd:cd03260 12 DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndLIPGAPDEGEVLLDGKDIYDLdvdvleLRRRVGMVFQKPN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 247 LFPhLTVKETLTYAARLrlpktltREQKKQRALDVIQELGLERCQ--DTMIGGAFVRGVSGGERKRVSIGNEIIINPSLL 324
Cdd:cd03260 92 PFP-GSIYDNVAYGLRL-------HGIKLKEELDERVEEALRKAAlwDEVKDRLHALGLSGGQQQRLCLARALANEPEVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 79597808 325 LLDEPTSGLDSTTALRTILMLHDIAEAGKTVITT--IHQpSSRLfhrFDKLILLGRGSLLYFGKSSE 389
Cdd:cd03260 164 LLDEPTSALDPISTAKIEELIAELKKEYTIVIVThnMQQ-AARV---ADRTAFLLNGRLVEFGPTEQ 226
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
186-334 |
1.07e-26 |
|
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: 112.12 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 186 SVNPGEVLALMGPSGSGKTTLLSLLAG-------RIS------QSSTGGsvtYNDKPYskylKSKIGFVTQDDVLFPHLT 252
Cdd:COG4148 21 TLPGRGVTALFGPSGSGKTTLLRAIAGlerpdsgRIRlggevlQDSARG---IFLPPH----RRRIGYVFQEARLFPHLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 253 VKETLTYAARlRLPKTLTREQkkqraLD-VIQELG----LERcqdtmiggaFVRGVSGGERKRVSIGNEIIINPSLLLLD 327
Cdd:COG4148 94 VRGNLLYGRK-RAPRAERRIS-----FDeVVELLGighlLDR---------RPATLSGGERQRVAIGRALLSSPRLLLMD 158
|
....*..
gi 79597808 328 EPTSGLD 334
Cdd:COG4148 159 EPLAALD 165
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
178-392 |
1.44e-26 |
|
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: 108.29 E-value: 1.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 178 EILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYSKY-----LKSKIGFVTQDDVLFPHLT 252
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRS--GSIRFDGRDITGLppherARAGIGYVPEGRRIFPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 253 VKETLTYAARLRlpktltREQKKQRALDVIQEL--GLERCQDTMiGGAFvrgvSGGERKRVSIGNEIIINPSLLLLDEPT 330
Cdd:cd03224 92 VEENLLLGAYAR------RRAKRKARLERVYELfpRLKERRKQL-AGTL----SGGEQQMLAIARALMSRPKLLLLDEPS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79597808 331 SGLdSTTALRTIL-MLHDIAEAGKTVItTIHQPSSRLFHRFDKLILLGRGSLLYFGKSSEALD 392
Cdd:cd03224 161 EGL-APKIVEEIFeAIRELRDEGVTIL-LVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
186-392 |
2.10e-26 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 108.30 E-value: 2.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 186 SVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYSKYLKSK--IGFVTQDDVLFPHLTVKET--LTYAA 261
Cdd:COG3840 21 TIAAGERVAILGPSGAGKSTLLNLIAGFLPPDS--GRILWNGQDLTALPPAErpVSMLFQENNLFPHLTVAQNigLGLRP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 262 RLRlpktLTREQKKQRAlDVIQELGLERCQDTMIGgafvrGVSGGERKRVSIGNEIIINPSLLLLDEPTSGLDSttALRT 341
Cdd:COG3840 99 GLK----LTAEQRAQVE-QALERVGLAGLLDRLPG-----QLSGGQRQRVALARCLVRKRPILLLDEPFSALDP--ALRQ 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 79597808 342 --ILMLHDIA-EAGKTVITTIHQPS--SRLfhrFDKLILLGRGSLLYFGKSSEALD 392
Cdd:COG3840 167 emLDLVDELCrERGLTVLMVTHDPEdaARI---ADRVLLVADGRIAADGPTAALLD 219
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
177-334 |
2.53e-26 |
|
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: 108.01 E-value: 2.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 177 KEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYSKYLKSK-----IGFVTQDDVLFPHL 251
Cdd:cd03218 13 RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDS--GKILLDGQDITKLPMHKrarlgIGYLPQEASIFRKL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 252 TVKETLTYAARLRlpkTLTREQKKQRALDVIQELGLERCQDTMiGGAfvrgVSGGERKRVSIGNEIIINPSLLLLDEPTS 331
Cdd:cd03218 91 TVEENILAVLEIR---GLSKKEREEKLEELLEEFHITHLRKSK-ASS----LSGGERRRVEIARALATNPKFLLLDEPFA 162
|
...
gi 79597808 332 GLD 334
Cdd:cd03218 163 GVD 165
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
176-334 |
3.60e-26 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 107.75 E-value: 3.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYSK---YLKSK--IGFVTQDDVLFPH 250
Cdd:TIGR04406 13 KRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDA--GKILIDGQDITHlpmHERARlgIGYLPQEASIFRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 251 LTVKETLTyaARLRLPKTLTREQKKQRALDVIQELGLERCQDTMIGGafvrgVSGGERKRVSIGNEIIINPSLLLLDEPT 330
Cdd:TIGR04406 91 LTVEENIM--AVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMS-----LSGGERRRVEIARALATNPKFILLDEPF 163
|
....
gi 79597808 331 SGLD 334
Cdd:TIGR04406 164 AGVD 167
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
157-393 |
4.56e-26 |
|
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: 107.32 E-value: 4.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 157 LKFRDVTYKVvikkltSSVEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYSKY--- 233
Cdd:cd03251 1 VEFKNVTFRY------PGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDS--GRILIDGHDVRDYtla 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 234 -LKSKIGFVTQDDVLFpHLTVKETLTYAARLRLPKTLTREQKKQRALDVIQEL--GLercqDTMIGgafVRGV--SGGER 308
Cdd:cd03251 73 sLRRQIGLVSQDVFLF-NDTVAENIAYGRPGATREEVEEAARAANAHEFIMELpeGY----DTVIG---ERGVklSGGQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 309 KRVSIGNEIIINPSLLLLDEPTSGLDSTT------ALRTiLMlhdiaeAGKTVITTIHQPSSrlFHRFDKLILLGRGSLL 382
Cdd:cd03251 145 QRIAIARALLKDPPILILDEATSALDTESerlvqaALER-LM------KNRTTFVIAHRLST--IENADRIVVLEDGKIV 215
|
250
....*....|.
gi 79597808 383 YFGKSSEALDY 393
Cdd:cd03251 216 ERGTHEELLAQ 226
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
166-363 |
5.62e-26 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 107.53 E-value: 5.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 166 VVIKKLTSSVE-KEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLagRISQSSTGGSVTYND------KPYSK------ 232
Cdd:PRK11264 4 IEVKNLVKKFHgQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCI--NLLEQPEAGTIRVGDitidtaRSLSQqkglir 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 233 YLKSKIGFVTQDDVLFPHLTVKETLTYAArlRLPKTLTREQKKQRALDVIQELGLERCQDtmiggAFVRGVSGGERKRVS 312
Cdd:PRK11264 82 QLRQHVGFVFQNFNLFPHRTVLENIIEGP--VIVKGEPKEEATARARELLAKVGLAGKET-----SYPRRLSGGQQQRVA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 79597808 313 IGNEIIINPSLLLLDEPTSGLDSTTALRTILMLHDIAEAGKTVITTIHQPS 363
Cdd:PRK11264 155 IARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMS 205
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
176-360 |
7.18e-26 |
|
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: 105.20 E-value: 7.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGriSQSSTGGSVTYNDKP--YSKY----LKSKIGFVTQ--DDVL 247
Cdd:TIGR01166 4 GPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNG--LLRPQSGAVLIDGEPldYSRKglleRRQRVGLVFQdpDDQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 248 FpHLTVKETLTYAAR-LRLPKTLTREQKKQrALDVIQELGLERCQDTMIggafvrgvSGGERKRVSIGNEIIINPSLLLL 326
Cdd:TIGR01166 82 F-AADVDQDVAFGPLnLGLSEAEVERRVRE-ALTAVGASGLRERPTHCL--------SGGEKKRVAIAGAVAMRPDVLLL 151
|
170 180 190
....*....|....*....|....*....|....
gi 79597808 327 DEPTSGLDSTTALRTILMLHDIAEAGKTVITTIH 360
Cdd:TIGR01166 152 DEPTAGLDPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
177-334 |
1.10e-25 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 106.27 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 177 KEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISqsSTGGSVTYNDKPYSK---YLKSK--IGFVTQDDVLFPHL 251
Cdd:COG1137 16 RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVK--PDSGRIFLDGEDITHlpmHKRARlgIGYLPQEASIFRKL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 252 TVKETLTYAARLRlpkTLTREQKKQRALDVIQELGLERCQDTMiGGAfvrgVSGGERKRVSIGNEIIINPSLLLLDEPTS 331
Cdd:COG1137 94 TVEDNILAVLELR---KLSKKEREERLEELLEEFGITHLRKSK-AYS----LSGGERRRVEIARALATNPKFILLDEPFA 165
|
...
gi 79597808 332 GLD 334
Cdd:COG1137 166 GVD 168
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
157-381 |
1.42e-25 |
|
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: 105.36 E-value: 1.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 157 LKFRDVTYKVvikkltSSVEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISqsSTGGSVTYNDKPYSKY--- 233
Cdd:cd03245 3 IEFRNVSFSY------PNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYK--PTSGSVLLDGTDIRQLdpa 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 234 -LKSKIGFVTQDDVLFpHLTVKETLTYAARlrlpktltrEQKKQRALDVIQELGLE-------RCQDTMIG--GafvRGV 303
Cdd:cd03245 75 dLRRNIGYVPQDVTLF-YGTLRDNITLGAP---------LADDERILRAAELAGVTdfvnkhpNGLDLQIGerG---RGL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79597808 304 SGGERKRVSIGNEIIINPSLLLLDEPTSGLDSTTALRTILMLHDIAeAGKTVITTIHQPSsrLFHRFDKLILLGRGSL 381
Cdd:cd03245 142 SGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPS--LLDLVDRIIVMDSGRI 216
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
180-392 |
2.00e-25 |
|
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: 105.50 E-value: 2.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 180 LTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRisQSSTGGSVTYNDKPYSKY--LKSKIGFVTQDDVLFPHLTVKETL 257
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGL--ERPDSGTILFGGEDATDVpvQERNVGFVFQHYALFRHMTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 258 TYAARLRLPKTLTRE-QKKQRALDVIQELGLERCQDTmiggaFVRGVSGGERKRVSIGNEIIINPSLLLLDEPTSGLDST 336
Cdd:cd03296 96 AFGLRVKPRSERPPEaEIRAKVHELLKLVQLDWLADR-----YPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAK 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 79597808 337 T--ALRTILM-LHDiaEAGKTVITTIHQPSSRLfHRFDKLILLGRGSLLYFGKSSEALD 392
Cdd:cd03296 171 VrkELRRWLRrLHD--ELHVTTVFVTHDQEEAL-EVADRVVVMNKGRIEQVGTPDEVYD 226
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
177-391 |
2.75e-25 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 105.58 E-value: 2.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 177 KEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYSKY----LKSKIGFVTQDDVL-FPhL 251
Cdd:COG4559 14 RTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSS--GEVRLNGRPLAAWspweLARRRAVLPQHSSLaFP-F 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 252 TVKETltyaARL-RLPKTLTREQKKQRALDVIQELGLErcqdtMIGGAFVRGVSGGERKRVS-------IGNEIIINPSL 323
Cdd:COG4559 91 TVEEV----VALgRAPHGSSAAQDRQIVREALALVGLA-----HLAGRSYQTLSGGEQQRVQlarvlaqLWEPVDGGPRW 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79597808 324 LLLDEPTSGLDSTTALRTILMLHDIAEAGKTVITTIHQPSsrLFHRF-DKLILLGRGSLLYFGKSSEAL 391
Cdd:COG4559 162 LFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLN--LAAQYaDRILLLHQGRLVAQGTPEEVL 228
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
157-381 |
4.27e-25 |
|
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: 102.78 E-value: 4.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 157 LKFRDVTYKVVIKkltssvEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYSKY--- 233
Cdd:cd03247 1 LSINNVSFSYPEQ------EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQ--GEITLDGVPVSDLeka 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 234 LKSKIGFVTQDdvlfPHLtvketltYAARLRlpktltreqkkqraldviQELGlercqdtmiggafvRGVSGGERKRVSI 313
Cdd:cd03247 73 LSSLISVLNQR----PYL-------FDTTLR------------------NNLG--------------RRFSGGERQRLAL 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79597808 314 GNEIIINPSLLLLDEPTSGLDSTTALRTILMLHDIAEaGKTVITTIHQPSSrlFHRFDKLILLGRGSL 381
Cdd:cd03247 110 ARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLK-DKTLIWITHHLTG--IEHMDKILFLENGKI 174
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
172-381 |
4.58e-25 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 103.97 E-value: 4.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 172 TSSVEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRisQSSTGGSVTYNDKPYSK-------YLKSK-IGFVTQ 243
Cdd:TIGR02211 13 EGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGL--DNPTSGEVLFNGQSLSKlssneraKLRNKkLGFIYQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 244 DDVLFPHLTVKETLTYAArlrLPKTLTREQKKQRALDVIQELGLERCQDTMIGGafvrgVSGGERKRVSIGNEIIINPSL 323
Cdd:TIGR02211 91 FHHLLPDFTALENVAMPL---LIGKKSVKEAKERAYEMLEKVGLEHRINHRPSE-----LSGGERQRVAIARALVNQPSL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 324 LLLDEPTSGLDSTTAlRTI--LMLHDIAEAGKTVITTIHQPssRLFHRFDKLILLGRGSL 381
Cdd:TIGR02211 163 VLADEPTGNLDNNNA-KIIfdLMLELNRELNTSFLVVTHDL--ELAKKLDRVLEMKDGQL 219
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
180-356 |
7.14e-25 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 104.35 E-value: 7.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 180 LTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISqsSTGGSVTYNDKPYSKyLK----SKIG----F-VTQddvLFPH 250
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYR--PTSGRILFDGRDITG-LPphriARLGiartFqNPR---LFPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 251 LTVKETL-----------TYAARLRLPKTLTREQK-KQRALDVIQELGLERCQDTMiggafVRGVSGGERKRVSIGNEII 318
Cdd:COG0411 94 LTVLENVlvaaharlgrgLLAALLRLPRARREEREaRERAEELLERVGLADRADEP-----AGNLSYGQQRRLEIARALA 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 79597808 319 INPSLLLLDEPTSGLDSTTALRTILMLHDI-AEAGKTVI 356
Cdd:COG0411 169 TEPKLLLLDEPAAGLNPEETEELAELIRRLrDERGITIL 207
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
168-360 |
7.38e-25 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 102.72 E-value: 7.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 168 IKKLTSSVEK--EILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYS-KYLKSKIGFVTQD 244
Cdd:cd03226 2 IENISFSYKKgtEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESS--GSILLNGKPIKaKERRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 245 --DVLFPHlTVKETLTYAARLrLPKtltreqKKQRALDVIQELGLERCQDtmiggAFVRGVSGGERKRVSIGNEIIINPS 322
Cdd:cd03226 80 vdYQLFTD-SVREELLLGLKE-LDA------GNEQAETVLKDLDLYALKE-----RHPLSLSGGQKQRLAIAAALLSGKD 146
|
170 180 190
....*....|....*....|....*....|....*...
gi 79597808 323 LLLLDEPTSGLDSTTALRTILMLHDIAEAGKTVITTIH 360
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITH 184
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
157-391 |
8.73e-25 |
|
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: 103.92 E-value: 8.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 157 LKFRDVTykvvikKLTSSVEKeILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYSKY--- 233
Cdd:cd03295 1 IEFENVT------KRYGGGKK-AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTS--GEIFIDGEDIREQdpv 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 234 -LKSKIGFVTQDDVLFPHLTVKETLTYaarlrLPKTL--TREQKKQRALDVIQELGLERCQdtmIGGAFVRGVSGGERKR 310
Cdd:cd03295 72 eLRRKIGYVIQQIGLFPHMTVEENIAL-----VPKLLkwPKEKIRERADELLALVGLDPAE---FADRYPHELSGGQQQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 311 VSIGNEIIINPSLLLLDEPTSGLDSTTalRTIL---MLHDIAEAGKTVITTIH--QPSSRLfhrFDKLILLGRGSLLYFG 385
Cdd:cd03295 144 VGVARALAADPPLLLMDEPFGALDPIT--RDQLqeeFKRLQQELGKTIVFVTHdiDEAFRL---ADRIAIMKNGEIVQVG 218
|
....*.
gi 79597808 386 KSSEAL 391
Cdd:cd03295 219 TPDEIL 224
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
180-362 |
1.75e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 101.54 E-value: 1.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 180 LTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTyndkpysKYLKSKIGFVTQ---DDVLFPhLTVKET 256
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTS--GTVR-------RAGGARVAYVPQrseVPDSLP-LTVRDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 257 LTYA--ARLRLPKTLTREQKKqRALDVIQELGLERcqdtmIGGAFVRGVSGGERKRVSIGNEIIINPSLLLLDEPTSGLD 334
Cdd:NF040873 78 VAMGrwARRGLWRRLTRDDRA-AVDDALERVGLAD-----LAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180
....*....|....*....|....*...
gi 79597808 335 STTALRTILMLHDIAEAGKTVITTIHQP 362
Cdd:NF040873 152 AESRERIIALLAEEHARGATVVVVTHDL 179
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
156-392 |
1.80e-24 |
|
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: 102.30 E-value: 1.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 156 FLKFRDVTYkvvikkltSSVEKE-ILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRIsqSSTGGSVTYNDKPYSKY- 233
Cdd:cd03254 2 EIEFENVNF--------SYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFY--DPQKGQILIDGIDIRDIs 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 234 ---LKSKIGFVTQDDVLFPHlTVKETLTYaARLRLPKTLTREQKKQ-RALDVIQEL--GLercqDTMIG--GAfvrGVSG 305
Cdd:cd03254 72 rksLRSMIGVVLQDTFLFSG-TIMENIRL-GRPNATDEEVIEAAKEaGAHDFIMKLpnGY----DTVLGenGG---NLSQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 306 GERKRVSIGNEIIINPSLLLLDEPTSGLDSTT------ALRTILmlhdiaeAGKTVITTIHQPSSRLFHrfDKLILLGRG 379
Cdd:cd03254 143 GERQLLAIARAMLRDPKILILDEATSNIDTETekliqeALEKLM-------KGRTSIIIAHRLSTIKNA--DKILVLDDG 213
|
250
....*....|...
gi 79597808 380 SLLYFGKSSEALD 392
Cdd:cd03254 214 KIIEEGTHDELLA 226
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
120-362 |
3.15e-24 |
|
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: 107.45 E-value: 3.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 120 EEISDSKPFSDDEMIPEDIEAGKKKPKfqaeptlpifLKFRDVTYKvvikkltSSVEKEILTGISGSVNPGEVLALMGPS 199
Cdd:TIGR02868 308 VEVLDAAGPVAEGSAPAAGAVGLGKPT----------LELRDLSAG-------YPGAPPVLDGVSLDLPPGERVAILGPS 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 200 GSGKTTLLSLLAGRISQSstGGSVTYNDKPYSKY----LKSKIGFVTQDDVLFpHLTVKETLTYAARLRLPKTLTREQKK 275
Cdd:TIGR02868 371 GSGKSTLLATLAGLLDPL--QGEVTLDGVPVSSLdqdeVRRRVSVCAQDAHLF-DTTVRENLRLARPDATDEELWAALER 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 276 QRALDVIQEL--GLercqDTMIGGAFVRgVSGGERKRVSIGNEIIINPSLLLLDEPTSGLDSTTALRtilMLHDI--AEA 351
Cdd:TIGR02868 448 VGLADWLRALpdGL----DTVLGEGGAR-LSGGERQRLALARALLADAPILLLDEPTEHLDAETADE---LLEDLlaALS 519
|
250
....*....|.
gi 79597808 352 GKTVITTIHQP 362
Cdd:TIGR02868 520 GRTVVLITHHL 530
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
177-391 |
3.55e-24 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 101.89 E-value: 3.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 177 KEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDK-----PYSKYLKSKIGFVTQDDVLFPHL 251
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDA--GNIIIDDEdisllPLHARARRGIGYLPQEASIFRRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 252 TVKETLTyaARLRLPKTLTREQKKQRALDVIQELGLERCQDTMiggafVRGVSGGERKRVSIGNEIIINPSLLLLDEPTS 331
Cdd:PRK10895 94 SVYDNLM--AVLQIRDDLSAEQREDRANELMEEFHIEHLRDSM-----GQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 332 GLDSTTALRTILMLHDIAEAGKTVITTIHQPSSRLfHRFDKLILLGRGSLLYFGKSSEAL 391
Cdd:PRK10895 167 GVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETL-AVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
177-351 |
3.90e-24 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 102.47 E-value: 3.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 177 KEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYSKYLKSKiGFVTQDDVLFPHLTVKET 256
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQH--GSITLDGKPVEGPGAER-GVVFQNEGLLPWRNVQDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 257 LTYAARLRlpkTLTREQKKQRALDVIQELGLERcqdtmIGGAFVRGVSGGERKRVSIGNEIIINPSLLLLDEPTSGLDS- 335
Cdd:PRK11248 91 VAFGLQLA---GVEKMQRLEIAHQMLKKVGLEG-----AEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAf 162
|
170 180 190
....*....|....*....|....*....|
gi 79597808 336 --------------TTALRTILMLHDIAEA 351
Cdd:PRK11248 163 treqmqtlllklwqETGKQVLLITHDIEEA 192
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
143-392 |
5.44e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 107.50 E-value: 5.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 143 KKPKFQAEPTL-PIFL----KFRDVTYKVVIKKltssvEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAgRISQs 217
Cdd:TIGR00958 460 RKPNIPLTGTLaPLNLegliEFQDVSFSYPNRP-----DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQ-NLYQ- 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 218 STGGSVTYNDKPYS----KYLKSKIGFVTQDDVLFPHlTVKETLTYAARLRLPKTLTREQKKQRALDVIQElgLERCQDT 293
Cdd:TIGR00958 533 PTGGQVLLDGVPLVqydhHYLHRQVALVGQEPVLFSG-SVRENIAYGLTDTPDEEIMAAAKAANAHDFIME--FPNGYDT 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 294 MIGGAFVRgVSGGERKRVSIGNEIIINPSLLLLDEPTSGLDsttALRTILMLHDIAEAGKTVITTIHQPSsrLFHRFDKL 373
Cdd:TIGR00958 610 EVGEKGSQ-LSGGQKQRIAIARALVRKPRVLILDEATSALD---AECEQLLQESRSRASRTVLLIAHRLS--TVERADQI 683
|
250
....*....|....*....
gi 79597808 374 ILLGRGSLLYFGKSSEALD 392
Cdd:TIGR00958 684 LVLKKGSVVEMGTHKQLME 702
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
176-389 |
7.72e-24 |
|
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: 101.08 E-value: 7.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLagrisQ---SSTGGSVTYNDKPYSKY----LKSKIGFVTQDDVLF 248
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLL-----ErfyDPTSGEILLDGVDIRDLnlrwLRSQIGLVSQEPVLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 249 PhLTVKETLTYAARLRLPKTLTREQKKQRALDVIQEL--GLercqDTMIGGafvRGV--SGGERKRVSIGNEIIINPSLL 324
Cdd:cd03249 90 D-GTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLpdGY----DTLVGE---RGSqlSGGQKQRIAIARALLRNPKIL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79597808 325 LLDEPTSGLDSTT------ALrtilmlhDIAEAGKTVITTIHQPSSrlFHRFDKLILLGRGSLLYFGKSSE 389
Cdd:cd03249 162 LLDEATSALDAESeklvqeAL-------DRAMKGRTTIVIAHRLST--IRNADLIAVLQNGQVVEQGTHDE 223
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
176-392 |
1.70e-23 |
|
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: 99.87 E-value: 1.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSSTGGSVTYNDKPY--SKYLKSKIGFVTQDDVLFpHLTV 253
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALadPAWLRRQVGVVLQENVLF-NRSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 254 KETLTYAARLRLPKTLTREQKKQRALDVIQELGLErcQDTMIG--GAfvrGVSGGERKRVSIGNEIIINPSLLLLDEPTS 331
Cdd:cd03252 93 RDNIALADPGMSMERVIEAAKLAGAHDFISELPEG--YDTIVGeqGA---GLSGGQRQRIAIARALIHNPRILIFDEATS 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79597808 332 GLDSTTALRTILMLHDIAeAGKTVITTIHQPSSrlFHRFDKLILLGRGSLLYFGKSSEALD 392
Cdd:cd03252 168 ALDYESEHAIMRNMHDIC-AGRTVIIIAHRLST--VKNADRIIVMEKGRIVEQGSHDELLA 225
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
157-381 |
3.06e-23 |
|
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: 98.70 E-value: 3.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 157 LKFRDVTYKVVIKKltssvEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAgRISQsSTGGSVTYNDKPYS----K 232
Cdd:cd03248 12 VKFQNVTFAYPTRP-----DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLE-NFYQ-PQGGQVLLDGKPISqyehK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 233 YLKSKIGFVTQDDVLFPHlTVKETLTYAARLRLPKTLTREQKKQRALDVIQELGLERCQDTMIGGAFvrgVSGGERKRVS 312
Cdd:cd03248 85 YLHSKVSLVGQEPVLFAR-SLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQ---LSGGQKQRVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79597808 313 IGNEIIINPSLLLLDEPTSGLDSTTALRTILMLHDIAEAgKTVITTIHQPSsrLFHRFDKLILLGRGSL 381
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAESEQQVQQALYDWPER-RTVLVIAHRLS--TVERADQILVLDGGRI 226
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
176-360 |
3.17e-23 |
|
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: 98.48 E-value: 3.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISqsSTGGSVTYNDK------PYskylKSKIGFVTQDDVLFP 249
Cdd:cd03301 12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEE--PTSGRIYIGGRdvtdlpPK----DRDIAMVFQNYALYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 250 HLTVKETLTYAARLRlpkTLTREQKKQRALDVIQELGLERCQDTmiggaFVRGVSGGERKRVSIGNEIIINPSLLLLDEP 329
Cdd:cd03301 86 HMTVYDNIAFGLKLR---KVPKDEIDERVREVAELLQIEHLLDR-----KPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190
....*....|....*....|....*....|....
gi 79597808 330 TSGLDST--TALRT-ILMLHdiAEAGKTVITTIH 360
Cdd:cd03301 158 LSNLDAKlrVQMRAeLKRLQ--QRLGTTTIYVTH 189
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
176-379 |
3.82e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 100.57 E-value: 3.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYSKYLKSKIGFVTQDDVLFPHLTVKE 255
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDS--GEVLWDGEPLDPEDRRRIGYLPEERGLYPKMKVGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 256 TLTYAARLrlpKTLTREQKKQRALDVIQELGL-ERCQDTmiggafVRGVSGGERKRVSIGNEIIINPSLLLLDEPTSGLD 334
Cdd:COG4152 91 QLVYLARL---KGLSKAEAKRRADEWLERLGLgDRANKK------VEELSKGNQQKVQLIAALLHDPELLILDEPFSGLD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 79597808 335 --STTALRTILMlhDIAEAGKTVITTIHQPSS--RLfhrFDKLILLGRG 379
Cdd:COG4152 162 pvNVELLKDVIR--ELAAKGTTVIFSSHQMELveEL---CDRIVIINKG 205
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
190-385 |
4.51e-23 |
|
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: 97.95 E-value: 4.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 190 GEVLALMGPSGSGKTTLLSLLAGriSQSSTGGSVTYN--DKPYSKYLKSKIGFVTQDDVLFPHLTVKET--LTYAARLRL 265
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIAG--FETPQSGRVLINgvDVTAAPPADRPVSMLFQENNLFAHLTVEQNvgLGLSPGLKL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 266 pktltREQKKQRALDVIQELGLE----RCQDTMiggafvrgvSGGERKRVSIGNEIIINPSLLLLDEPTSGLDSttALR- 340
Cdd:cd03298 102 -----TAEDRQAIEVALARVGLAglekRLPGEL---------SGGERQRVALARVLVRDKPVLLLDEPFAALDP--ALRa 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 79597808 341 --TILMLHDIAEAGKTVITTIHQPSSRLfHRFDKLILLGRGSLLYFG 385
Cdd:cd03298 166 emLDLVLDLHAETKMTVLMVTHQPEDAK-RLAQRVVFLDNGRIAAQG 211
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
168-360 |
5.54e-23 |
|
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: 97.21 E-value: 5.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 168 IKKLTSSV-EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSSTGGSVTYNDK------PYSKYLKSkIGF 240
Cdd:cd03217 3 IKDLHVSVgGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVTEGEILFKGEditdlpPEERARLG-IFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 241 VTQDDVLFPHLTVKETLtyaarlrlpktltreqkkqRALDViqelglercqdtmiggafvrGVSGGERKRVSIGNEIIIN 320
Cdd:cd03217 82 AFQYPPEIPGVKNADFL-------------------RYVNE--------------------GFSGGEKKRNEILQLLLLE 122
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 79597808 321 PSLLLLDEPTSGLDsTTALRTILM-LHDIAEAGKTVITTIH 360
Cdd:cd03217 123 PDLAILDEPDSGLD-IDALRLVAEvINKLREEGKSVLIITH 162
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
180-376 |
6.30e-23 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 103.52 E-value: 6.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 180 LTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRIsqSSTGGSVTYNDKPYS----KYLKSKIGFVTQDDVLFPHlTVKE 255
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFV--DPTEGSIAVNGVPLAdadaDSWRDQIAWVPQHPFLFAG-TIAE 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 256 TLTYAARLRLPKTLTREQKKQRALDVIQELGLErcQDTMIGGAfVRGVSGGERKRVSIGNEIIINPSLLLLDEPTSGLDS 335
Cdd:TIGR02857 415 NIRLARPDASDAEIREALERAGLDEFVAALPQG--LDTPIGEG-GAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDA 491
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 79597808 336 TTALRTILMLHDIAEaGKTVITTIHQPSSRlfHRFDKLILL 376
Cdd:TIGR02857 492 ETEAEVLEALRALAQ-GRTVLLVTHRLALA--ALADRIVVL 529
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
179-458 |
6.80e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 101.84 E-value: 6.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 179 ILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISqsSTGGSVTYNDKPY----SKYLKSKIGFVTQDDVLFPHLTVK 254
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLT--PTAGTVLVAGDDVealsARAASRRVASVPQDTSLSFEFDVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 255 ETLTYAarlRLPKtLTREQKKQRALDVIQELGLERCQDTMIGGAFVRGVSGGERKRVSIGNEIIINPSLLLLDEPTSGLD 334
Cdd:PRK09536 96 QVVEMG---RTPH-RSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 335 STTALRTILMLHDIAEAGKTVITTIHQPSsrLFHRF-DKLILLGRGSLLYFGKSSEAL------DYFssiGCSPLIAMNP 407
Cdd:PRK09536 172 INHQVRTLELVRRLVDDGKTAVAAIHDLD--LAARYcDELVLLADGRVRAAGPPADVLtadtlrAAF---DARTAVGTDP 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 79597808 408 aeflldlANGNINDISVPSELDDRVQVGNSGRETQTGKPSPAAVHEyLVEA 458
Cdd:PRK09536 247 -------ATGAPTVTPLPDPDRTEAAADTRVHVVGGGQPAARAVSR-LVAA 289
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
178-335 |
6.91e-23 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 100.93 E-value: 6.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 178 EILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYSKY--LKSKIGFVTQDDVLFPHLTVKE 255
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTS--GHIRFHGTDVSRLhaRDRKVGFVFQHYALFRHMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 256 T----LTYAARLRLPKTLTREQKKQRALDVIQelgLERCQDTmiggaFVRGVSGGERKRVSIGNEIIINPSLLLLDEPTS 331
Cdd:PRK10851 94 NiafgLTVLPRRERPNAAAIKAKVTQLLEMVQ---LAHLADR-----YPAQLSGGQKQRVALARALAVEPQILLLDEPFG 165
|
....
gi 79597808 332 GLDS 335
Cdd:PRK10851 166 ALDA 169
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
183-391 |
7.98e-23 |
|
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: 98.87 E-value: 7.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 183 ISGSVNPGEVLALMGPSGSGKTTLLSLLAGRIsqSSTGGSVTYNDKPYSKYLKS--------KIGFVTQDDVLFPHLTVK 254
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLI--EPTSGKVLIDGQDIAAMSRKelrelrrkKISMVFQSFALLPHRTVL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 255 ETLTYAARLRlpkTLTREQKKQRALDVIQELGLERCQDTMIGgafvrGVSGGERKRVSIGNEIIINPSLLLLDEPTSGLD 334
Cdd:cd03294 121 ENVAFGLEVQ---GVPRAEREERAAEALELVGLEGWEHKYPD-----ELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79597808 335 ST--TALRTILM-LHdiAEAGKTVITTIHQPSS--RLFHRfdkLILLGRGSLLYFGKSSEAL 391
Cdd:cd03294 193 PLirREMQDELLrLQ--AELQKTIVFITHDLDEalRLGDR---IAIMKDGRLVQVGTPEEIL 249
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
174-338 |
8.53e-23 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 97.96 E-value: 8.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 174 SVEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRisQSSTGGSVTYNDKPYSKYLKS--------KIGFVTQDD 245
Cdd:PRK11629 19 SVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGL--DTPTSGDVIFNGQPMSKLSSAakaelrnqKLGFIYQFH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 246 VLFPHLTVKETltyAARLRLPKTLTREQKKQRALDVIQELGLERcqdtmiggafvRG------VSGGERKRVSIGNEIII 319
Cdd:PRK11629 97 HLLPDFTALEN---VAMPLLIGKKKPAEINSRALEMLAAVGLEH-----------RAnhrpseLSGGERQRVAIARALVN 162
|
170
....*....|....*....
gi 79597808 320 NPSLLLLDEPTSGLDSTTA 338
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNA 181
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
189-414 |
9.53e-23 |
|
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: 100.57 E-value: 9.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 189 PG-EVLALMGPSGSGKTTLLSLLAGRI----SQSSTGGsVTYNDKPYSKYL---KSKIGFVTQDDVLFPHLTVKETLTYA 260
Cdd:TIGR02142 21 PGqGVTAIFGRSGSGKTTLIRLIAGLTrpdeGEIVLNG-RTLFDSRKGIFLppeKRRIGYVFQEARLFPHLSVRGNLRYG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 261 -ARLRLPKTLTREQKkqraldVIQELGLERcqdtmIGGAFVRGVSGGERKRVSIGNEIIINPSLLLLDEPTSGLDSTTAL 339
Cdd:TIGR02142 100 mKRARPSERRISFER------VIELLGIGH-----LLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79597808 340 RTILMLHDI-AEAGKTVITTIHQPSSRLfHRFDKLILLGRGSLLYFGKSSEALdyfsSIGCSPLIAMNPAEFLLDL 414
Cdd:TIGR02142 169 EILPYLERLhAEFGIPILYVSHSLQEVL-RLADRVVVLEDGRVAAAGPIAEVW----ASPDLPWLAREDQGSLIEG 239
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
176-361 |
1.03e-22 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 98.12 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLL-------AGRISQSS--------TGGSVTYNDKPYSKYLKSKIGF 240
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCInflekpsEGSIVVNGqtinlvrdKDGQLKVADKNQLRLLRTRLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 241 VTQDDVLFPHLTVKETLTYAARLRLpkTLTREQKKQRALDVIQELGL-ERCQdtmigGAFVRGVSGGERKRVSIGNEIII 319
Cdd:PRK10619 97 VFQHFNLWSHMTVLENVMEAPIQVL--GLSKQEARERAVKYLAKVGIdERAQ-----GKYPVHLSGGQQQRVSIARALAM 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 79597808 320 NPSLLLLDEPTSGLDSTTALRTILMLHDIAEAGKTVITTIHQ 361
Cdd:PRK10619 170 EPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
178-358 |
1.08e-22 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 97.78 E-value: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 178 EILTGISGSVNPGEVLALMGPSGSGKTTLLSLL-------AGRISQSstGGSVTYNDKPYSK---YLKSKIGFVTQDDVL 247
Cdd:COG4161 16 QALFDINLECPSGETLVLLGPSGAGKSSLLRVLnlletpdSGQLNIA--GHQFDFSQKPSEKairLLRQKVGMVFQQYNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 248 FPHLTVKETLTyAARLRLPKtLTREQKKQRAldviQELgLERCQDTMIGGAFVRGVSGGERKRVSIGNEIIINPSLLLLD 327
Cdd:COG4161 94 WPHLTVMENLI-EAPCKVLG-LSKEQAREKA----MKL-LARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFD 166
|
170 180 190
....*....|....*....|....*....|..
gi 79597808 328 EPTSGLDSTTALRTILMLHDIAEAGKT-VITT 358
Cdd:COG4161 167 EPTAALDPEITAQVVEIIRELSQTGITqVIVT 198
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
168-342 |
1.14e-22 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 97.72 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 168 IKKLTSSVE-KEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSSTGGSVTYNDKPYSK---YLKSKIG-FVT 242
Cdd:TIGR01978 3 IKDLHVSVEdKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSYEVTSGTILFKGQDLLElepDERARAGlFLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 243 -QDDVLFPHLTVKETLTYAARLRlpktltREQKKQRALDVIQ--ELGLERCQDTMIGGAFVR-----GVSGGERKRvsig 314
Cdd:TIGR01978 83 fQYPEEIPGVSNLEFLRSALNAR------RSARGEEPLDLLDfeKLLKEKLALLDMDEEFLNrsvneGFSGGEKKR---- 152
|
170 180 190
....*....|....*....|....*....|..
gi 79597808 315 NEI----IINPSLLLLDEPTSGLDsTTALRTI 342
Cdd:TIGR01978 153 NEIlqmaLLEPKLAILDEIDSGLD-IDALKIV 183
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
178-333 |
1.58e-22 |
|
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: 96.97 E-value: 1.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 178 EILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYSKyLKSK------IGFVTQDDVLFPHL 251
Cdd:COG0410 17 HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRS--GSIRFDGEDITG-LPPHriarlgIGYVPEGRRIFPSL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 252 TVKETLTYAARLRLPKTlTREQKKQRALDVIQELGlERcQDTMiGGAfvrgVSGGERKRVSIGNEIIINPSLLLLDEPTS 331
Cdd:COG0410 94 TVEENLLLGAYARRDRA-EVRADLERVYELFPRLK-ER-RRQR-AGT----LSGGEQQMLAIGRALMSRPKLLLLDEPSL 165
|
..
gi 79597808 332 GL 333
Cdd:COG0410 166 GL 167
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
178-360 |
2.28e-22 |
|
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: 96.28 E-value: 2.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 178 EILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSSTGGSVT-YNDKPYSKYLKSKIGFVTQDDVLFPHLTVKET 256
Cdd:cd03265 14 EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAgHDVVREPREVRRRIGIVFQDLSVDDELTGWEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 257 LTYAARLrlpKTLTREQKKQRALDVIQELGLERCQDTMiggafVRGVSGGERKRVSIGNEIIINPSLLLLDEPTSGLDST 336
Cdd:cd03265 94 LYIHARL---YGVPGAERRERIDELLDFVGLLEAADRL-----VKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQ 165
|
170 180
....*....|....*....|....*
gi 79597808 337 TALRTILMLHDI-AEAGKTVITTIH 360
Cdd:cd03265 166 TRAHVWEYIEKLkEEFGMTILLTTH 190
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
177-391 |
2.41e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 97.15 E-value: 2.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 177 KEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYSKY----LKSKIGFVTQDDVL-FPhL 251
Cdd:PRK13548 15 RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDS--GEVRLNGRPLADWspaeLARRRAVLPQHSSLsFP-F 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 252 TVKETLtyaaRL-RLPKTLTREQKKQRALDVIQELGLercqdTMIGGAFVRGVSGGERKRV---------SIGNEIiinP 321
Cdd:PRK13548 92 TVEEVV----AMgRAPHGLSRAEDDALVAAALAQVDL-----AHLAGRDYPQLSGGEQQRVqlarvlaqlWEPDGP---P 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79597808 322 SLLLLDEPTSGLDSTTALRTILMLHDIA-EAGKTVITTIHQPSsrLFHRF-DKLILLGRGSLLYFGKSSEAL 391
Cdd:PRK13548 160 RWLLLDEPTSALDLAHQHHVLRLARQLAhERGLAVIVVLHDLN--LAARYaDRIVLLHQGRLVADGTPAEVL 229
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
176-399 |
2.97e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 97.95 E-value: 2.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKP---YSKYLKSKIGFVTQDDVLFPHLT 252
Cdd:PRK13537 19 DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDA--GSISLCGEPvpsRARHARQRVGVVPQFDNLDPDFT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 253 VKETLTYAARLRlpkTLTREQKKQRALDVIQELGLERCQDtmiggAFVRGVSGGERKRVSIGNEIIINPSLLLLDEPTSG 332
Cdd:PRK13537 97 VRENLLVFGRYF---GLSAAAARALVPPLLEFAKLENKAD-----AKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTG 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79597808 333 LDSTTALRTILMLHDIAEAGKTVITTIH--QPSSRLFHRfdkLILLGRGSLLYFGKSSEALDyfSSIGC 399
Cdd:PRK13537 169 LDPQARHLMWERLRSLLARGKTILLTTHfmEEAERLCDR---LCVIEEGRKIAEGAPHALIE--SEIGC 232
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
179-391 |
5.11e-22 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 100.59 E-value: 5.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 179 ILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGriSQSSTGGSVTYNDKPYSKY----LKSKIGFVTQDDVLFPHlTVK 254
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVG--VWPPTAGSVRLDGADLSQWdreeLGRHIGYLPQDVELFDG-TIA 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 255 ETLtyaARLRLPktlTREQ-----KKQRALDVIQEL--GLercqDTMIG--GAfvrGVSGGERKRVSI-----GneiiiN 320
Cdd:COG4618 424 ENI---ARFGDA---DPEKvvaaaKLAGVHEMILRLpdGY----DTRIGegGA---RLSGGQRQRIGLaralyG-----D 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79597808 321 PSLLLLDEPTSGLDST--TALRTILMlhDIAEAGKTVITTIHQPSsrLFHRFDKLILLGRGSLLYFGKSSEAL 391
Cdd:COG4618 486 PRLVVLDEPNSNLDDEgeAALAAAIR--ALKARGATVVVITHRPS--LLAAVDKLLVLRDGRVQAFGPRDEVL 554
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
162-361 |
6.09e-22 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 95.54 E-value: 6.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 162 VTYKVVIKKLTSSvekEILTGISGSVNPGEVLALMGPSGSGKTTLL------------SLLAGriSQSSTGGSVTyndkp 229
Cdd:PRK09493 2 IEFKNVSKHFGPT---QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLrcinkleeitsgDLIVD--GLKVNDPKVD----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 230 ySKYLKSKIGFVTQDDVLFPHLTVKETLTYAA-RLRlpkTLTREQKKQRALDVIQELGL-ERcqdtmiGGAFVRGVSGGE 307
Cdd:PRK09493 72 -ERLIRQEAGMVFQQFYLFPHLTALENVMFGPlRVR---GASKEEAEKQARELLAKVGLaER------AHHYPSELSGGQ 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 79597808 308 RKRVSIGNEIIINPSLLLLDEPTSGLDSTTALRTILMLHDIAEAGKTVITTIHQ 361
Cdd:PRK09493 142 QQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHE 195
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
178-358 |
7.11e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 95.47 E-value: 7.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 178 EILTGISGSVNPGEVLALMGPSGSGKTTLLSLL-------AGR--ISQSSTGGSVTYNDKPYSKyLKSKIGFVTQDDVLF 248
Cdd:PRK11124 16 QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprSGTlnIAGNHFDFSKTPSDKAIRE-LRRNVGMVFQQYNLW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 249 PHLTVKETLTYAARLRLpkTLTREQKKQRALDVIQELGLERCQDtmiggAFVRGVSGGERKRVSIGNEIIINPSLLLLDE 328
Cdd:PRK11124 95 PHLTVQQNLIEAPCRVL--GLSKDQALARAEKLLERLRLKPYAD-----RFPLHLSGGQQQRVAIARALMMEPQVLLFDE 167
|
170 180 190
....*....|....*....|....*....|.
gi 79597808 329 PTSGLDSTTALRTILMLHDIAEAGKT-VITT 358
Cdd:PRK11124 168 PTAALDPEITAQIVSIIRELAETGITqVIVT 198
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
176-336 |
7.67e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 100.16 E-value: 7.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGK-TTLLSLLagRISQSStgGSVTYNDKPYSKY-------LKSKIGFVTQD--D 245
Cdd:PRK15134 298 HNVVVKNISFTLRPGETLGLVGESGSGKsTTGLALL--RLINSQ--GEIWFDGQPLHNLnrrqllpVRHRIQVVFQDpnS 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 246 VLFPHLTVKETLTYAARLRLPkTLTREQKKQRALDVIQELGLERCQDTMIGGAFvrgvSGGERKRVSIGNEIIINPSLLL 325
Cdd:PRK15134 374 SLNPRLNVLQIIEEGLRVHQP-TLSAAQREQQVIAVMEEVGLDPETRHRYPAEF----SGGQRQRIAIARALILKPSLII 448
|
170
....*....|.
gi 79597808 326 LDEPTSGLDST 336
Cdd:PRK15134 449 LDEPTSSLDKT 459
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
180-360 |
8.80e-22 |
|
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: 96.69 E-value: 8.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 180 LTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSSTGGSVT-YNDKPYSKYLKSKIGFVTQDDVLFPHLTVKETLT 258
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAgYDVVREPRKVRRSIGIVPQYASVDEDLTGRENLE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 259 YAARLR-LPKTLTREQkkqraldvIQELgLERCQDTMIGGAFVRGVSGGERKRVSIGNEIIINPSLLLLDEPTSGLDSTT 337
Cdd:TIGR01188 89 MMGRLYgLPKDEAEER--------AEEL-LELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRT 159
|
170 180
....*....|....*....|...
gi 79597808 338 ALRTILMLHDIAEAGKTVITTIH 360
Cdd:TIGR01188 160 RRAIWDYIRALKEEGVTILLTTH 182
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
178-360 |
1.01e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 95.91 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 178 EILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKP--YSKY----LKSKIGFVTQ--DDVLF- 248
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTS--GEVLIKGEPikYDKKslleVRKTVGIVFQnpDDQLFa 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 249 PhlTVKETLTYAA-RLRLPKtltrEQKKQRALDVIQELGLERCQDTMiggafVRGVSGGERKRVSIGNEIIINPSLLLLD 327
Cdd:PRK13639 94 P--TVEEDVAFGPlNLGLSK----EEVEKRVKEALKAVGMEGFENKP-----PHHLSGGQKKRVAIAGILAMKPEIIVLD 162
|
170 180 190
....*....|....*....|....*....|...
gi 79597808 328 EPTSGLDSTTALRTILMLHDIAEAGKTVITTIH 360
Cdd:PRK13639 163 EPTSGLDPMGASQIMKLLYDLNKEGITIIISTH 195
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
186-353 |
1.49e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 94.26 E-value: 1.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 186 SVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYSKYLKSK--IGFVTQDDVLFPHLTVKET--LTYAA 261
Cdd:PRK10771 21 TVERGERVAILGPSGAGKSTLLNLIAGFLTPAS--GSLTLNGQDHTTTPPSRrpVSMLFQENNLFSHLTVAQNigLGLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 262 RLRlpktLTREQKKQRAlDVIQELGLERCQDTMIGgafvrGVSGGERKRVSIGNEIIINPSLLLLDEPTSGLDSttALR- 340
Cdd:PRK10771 99 GLK----LNAAQREKLH-AIARQMGIEDLLARLPG-----QLSGGQRQRVALARCLVREQPILLLDEPFSALDP--ALRq 166
|
170 180
....*....|....*....|....*....
gi 79597808 341 ---------------TILML-HDIAEAGK 353
Cdd:PRK10771 167 emltlvsqvcqerqlTLLMVsHSLEDAAR 195
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
179-381 |
1.73e-21 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 93.69 E-value: 1.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 179 ILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSS-----TGGSVTYNDKPYSKYLKSK-IGFVTQDDVLFPHLT 252
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSgevslVGQPLHQMDEEARAKLRAKhVGFVFQSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 253 VKETLTYAARLRlpkTLTREQKKQRALDVIQELGLERCQDTMIGgafvrGVSGGERKRVSIGNEIIINPSLLLLDEPTSG 332
Cdd:PRK10584 105 ALENVELPALLR---GESSRQSRNGAKALLEQLGLGKRLDHLPA-----QLSGGEQQRVALARAFNGRPDVLFADEPTGN 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 79597808 333 LDSTTALRTILMLHDI-AEAGKTVITTIHQPssRLFHRFDKLILLGRGSL 381
Cdd:PRK10584 177 LDRQTGDKIADLLFSLnREHGTTLILVTHDL--QLAARCDRRLRLVNGQL 224
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
175-385 |
3.87e-21 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 93.17 E-value: 3.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 175 VEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDK-PYS--KYLKSKIGFVT-QDDVLFPH 250
Cdd:cd03267 32 REVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTS--GEVRVAGLvPWKrrKKFLRRIGVVFgQKTQLWWD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 251 LTVKETLTYAARL-RLPKtltrEQKKQRALDVIQELGLERCQDTMiggafVRGVSGGERKRVSIGNEIIINPSLLLLDEP 329
Cdd:cd03267 110 LPVIDSFYLLAAIyDLPP----ARFKKRLDELSELLDLEELLDTP-----VRQLSLGQRMRAEIAAALLHEPEILFLDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 79597808 330 TSGLDSTTALRTILMLHDI-AEAGKTVITTIH--QPSSRLfhrFDKLILLGRGSLLYFG 385
Cdd:cd03267 181 TIGLDVVAQENIRNFLKEYnRERGTTVLLTSHymKDIEAL---ARRVLVIDKGRLLYDG 236
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
177-334 |
9.63e-21 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 95.01 E-value: 9.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 177 KEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGriSQSSTGGSVTYNDKPYSKYLKSK--IGFVTQDDVLFPHLTVK 254
Cdd:PRK09452 27 KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAG--FETPDSGRIMLDGQDITHVPAENrhVNTVFQSYALFPHMTVF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 255 ETLTYAarLRLPKTLTREQKKqRALDVIQELGLERcqdtmIGGAFVRGVSGGERKRVSIGNEIIINPSLLLLDEPTSGLD 334
Cdd:PRK09452 105 ENVAFG--LRMQKTPAAEITP-RVMEALRMVQLEE-----FAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
165-391 |
1.19e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 92.00 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 165 KVVIKKLTSSV-EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAgRISQSSTgGSVTYNDKPYSKY----LKSKIG 239
Cdd:PRK11231 2 TLRTENLTVGYgTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFA-RLLTPQS-GTVFLGDKPISMLssrqLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 240 FVTQDDVLFPHLTVKETLTY--AARLRLPKTLTREQKK--QRALDVIQELGL-ERCqdtmiggafVRGVSGGERKRVSIG 314
Cdd:PRK11231 80 LLPQHHLTPEGITVRELVAYgrSPWLSLWGRLSAEDNArvNQAMEQTRINHLaDRR---------LTDLSGGQRQRAFLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 315 NEIIINPSLLLLDEPTSGLDSTTALRTILMLHDIAEAGKTVITTIH---QPSsrlfhRF-DKLILLGRGSLLYFGKSSEA 390
Cdd:PRK11231 151 MVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHdlnQAS-----RYcDHLVVLANGHVMAQGTPEEV 225
|
.
gi 79597808 391 L 391
Cdd:PRK11231 226 M 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
176-334 |
1.48e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.90 E-value: 1.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRIsqSSTGGSVTYNDkpyskylKSKIGFVTQDDVLFPHLTVKE 255
Cdd:COG0488 10 GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGEL--EPDSGEVSIPK-------GLRIGYLPQEPPLDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 256 TL------------TYAARLRLPKTLTREQKKQ-----------------RALDVIQELGLercqDTMIGGAFVRGVSGG 306
Cdd:COG0488 81 TVldgdaelraleaELEELEAKLAEPDEDLERLaelqeefealggweaeaRAEEILSGLGF----PEEDLDRPVSELSGG 156
|
170 180
....*....|....*....|....*...
gi 79597808 307 ERKRVSIGNEIIINPSLLLLDEPTSGLD 334
Cdd:COG0488 157 WRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
180-386 |
1.51e-20 |
|
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: 90.99 E-value: 1.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 180 LTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGrISQSSTGGsVTYNDKPYSKYLKSKIgFVTQDDVLFPHLTVKETLTY 259
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISG-LAQPTSGG-VILEGKQITEPGPDRM-VVFQNYSLLPWLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 260 AARLRLPkTLTREQKKQRALDVIQELGLERCQDTMIGGafvrgVSGGERKRVSIGNEIIINPSLLLLDEPTSGLDSTT-- 337
Cdd:TIGR01184 78 AVDRVLP-DLSKSERRAIVEEHIALVGLTEAADKRPGQ-----LSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTrg 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 79597808 338 ALRTILMlhDIA-EAGKTVITTIHQPSSRLFHRfDKLILLGRGSLLYFGK 386
Cdd:TIGR01184 152 NLQEELM--QIWeEHRVTVLMVTHDVDEALLLS-DRVVMLTNGPAANIGQ 198
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
180-391 |
1.76e-20 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 91.53 E-value: 1.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 180 LTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSstgGSVTYNDKPYSKYLKSKI----GFVTQDDVLFPHLTVKE 255
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGS---GSIQFAGQPLEAWSAAELarhrAYLSQQQTPPFAMPVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 256 TLTyaarLRLPkTLTREQKKQRAL-DVIQELGLERCQDTMIGgafvrGVSGGERKRVSIGNEII-----INPS--LLLLD 327
Cdd:PRK03695 89 YLT----LHQP-DKTRTEAVASALnEVAEALGLDDKLGRSVN-----QLSGGEWQRVRLAAVVLqvwpdINPAgqLLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79597808 328 EPTSGLDST--TALRTIlmLHDIAEAGKTVITTIHQpSSRLFHRFDKLILLGRGSLLYFGKSSEAL 391
Cdd:PRK03695 159 EPMNSLDVAqqAALDRL--LSELCQQGIAVVMSSHD-LNHTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
178-362 |
1.94e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 96.33 E-value: 1.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 178 EILTGISGSVNPGEVLALMGPSGSGKTTLLSLLaGRISQSSTG-------GSVTYNDKPYSKYLKSKIGFVTQDDVLFPH 250
Cdd:PRK10535 22 EVLKGISLDIYAGEMVAIVGASGSGKSTLMNIL-GCLDKPTSGtyrvagqDVATLDADALAQLRREHFGFIFQRYHLLSH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 251 LTVKETL----TYAArlrlpktLTREQKKQRALDVIQELGLERCQDTMIGGafvrgVSGGERKRVSIGNEIIINPSLLLL 326
Cdd:PRK10535 101 LTAAQNVevpaVYAG-------LERKQRLLRAQELLQRLGLEDRVEYQPSQ-----LSGGQQQRVSIARALMNGGQVILA 168
|
170 180 190
....*....|....*....|....*....|....*.
gi 79597808 327 DEPTSGLDSTTALRTILMLHDIAEAGKTVITTIHQP 362
Cdd:PRK10535 169 DEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDP 204
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
179-391 |
2.16e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 95.66 E-value: 2.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 179 ILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAgRISQSSTGgSVTYNDKPYSKY----LKSKIGFVTQDDVLFPHlTVK 254
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLT-RAWDPQQG-EILLNGQPIADYseaaLRQAISVVSQRVHLFSA-TLR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 255 ETLTYAArlrlpKTLTREQkkqrALDVIQELGLERCQDTMIG-----GAFVRGVSGGERKRVSIGNEIIINPSLLLLDEP 329
Cdd:PRK11160 432 DNLLLAA-----PNASDEA----LIEVLQQVGLEKLLEDDKGlnawlGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEP 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79597808 330 TSGLDSTTAlRTIL-MLHDIAeAGKTVITTIHqpssRLF--HRFDKLILLGRGSLLYFGKSSEAL 391
Cdd:PRK11160 503 TEGLDAETE-RQILeLLAEHA-QNKTVLMITH----RLTglEQFDRICVMDNGQIIEQGTHQELL 561
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
182-356 |
2.22e-20 |
|
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: 92.81 E-value: 2.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 182 GISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSS-TGGSVTYNDKP--------YSKYLKSKIGFVTQD--DVLFPH 250
Cdd:COG0444 23 GVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGiTSGEILFDGEDllklsekeLRKIRGREIQMIFQDpmTSLNPV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 251 LTVKETLTYAarLRLPKTLTREQKKQRALDVIQELGLERCQDTMigGAFVRGVSGGERKRVSIGNEIIINPSLLLLDEPT 330
Cdd:COG0444 103 MTVGDQIAEP--LRIHGGLSKAEARERAIELLERVGLPDPERRL--DRYPHELSGGMRQRVMIARALALEPKLLIADEPT 178
|
170 180
....*....|....*....|....*..
gi 79597808 331 SGLDSTTALRTILMLHDI-AEAGKTVI 356
Cdd:COG0444 179 TALDVTIQAQILNLLKDLqRELGLAIL 205
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
168-392 |
3.76e-20 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 90.84 E-value: 3.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 168 IKKLTSSVEK-EILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSST--------GGSVTYNDKPYSKYLKSK- 237
Cdd:PRK09984 7 VEKLAKTFNQhQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSagshiellGRTVQREGRLARDIRKSRa 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 238 -IGFVTQDDVLFPHLTVKETLTYAARLRLP------KTLTREQkKQRALDVIQELGLERcqdtmIGGAFVRGVSGGERKR 310
Cdd:PRK09984 87 nTGYIFQQFNLVNRLSVLENVLIGALGSTPfwrtcfSWFTREQ-KQRALQALTRVGMVH-----FAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 311 VSIGNEIIINPSLLLLDEPTSGLDSTTALRTILMLHDIAEA-GKTVITTIHQPSSRLfhRF-DKLILLGRGSLLYFGkSS 388
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYAL--RYcERIVALRQGHVFYDG-SS 237
|
....
gi 79597808 389 EALD 392
Cdd:PRK09984 238 QQFD 241
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
157-361 |
3.78e-20 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 89.95 E-value: 3.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 157 LKFRDVTykvviKKLTSSVEK-EILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRisQSSTGGSVTYNDKPYSKY-- 233
Cdd:cd03258 2 IELKNVS-----KVFGDTGGKvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGL--ERPTSGSVLVDGTDLTLLsg 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 234 -----LKSKIGFVTQDDVLFPHLTVKETLTYAarLRLPKTlTREQKKQRALDVIQELGLERCQDtmiggAFVRGVSGGER 308
Cdd:cd03258 75 kelrkARRRIGMIFQHFNLLSSRTVFENVALP--LEIAGV-PKAEIEERVLELLELVGLEDKAD-----AYPAQLSGGQK 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 79597808 309 KRVSIGNEIIINPSLLLLDEPTSGLDSTTAlRTIL-MLHDI-AEAGKTVITTIHQ 361
Cdd:cd03258 147 QRVGIARALANNPKVLLCDEATSALDPETT-QSILaLLRDInRELGLTIVLITHE 200
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
161-360 |
6.06e-20 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 92.40 E-value: 6.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 161 DVTYKVVIKkltSSVEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGrISQSSTG----GSVTYNDKPYSKylkS 236
Cdd:PRK11000 3 SVTLRNVTK---AYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAG-LEDITSGdlfiGEKRMNDVPPAE---R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 237 KIGFVTQDDVLFPHLTVKETLTYAARLRLPKTLTREQKKQRALDVIQeLG--LERCQdtmiggafvRGVSGGERKRVSIG 314
Cdd:PRK11000 76 GVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQ-LAhlLDRKP---------KALSGGQRQRVAIG 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 79597808 315 NEIIINPSLLLLDEPTSGLDSttALRT-----ILMLHDiaEAGKTVITTIH 360
Cdd:PRK11000 146 RTLVAEPSVFLLDEPLSNLDA--ALRVqmrieISRLHK--RLGRTMIYVTH 192
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
177-400 |
7.33e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 91.82 E-value: 7.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 177 KEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPY---SKYLKSKIGFVTQDDVLFPHLTV 253
Cdd:PRK13536 54 KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDA--GKITVLGVPVparARLARARIGVVPQFDNLDLEFTV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 254 KETLTYAARLRLPKTLTREQKKQRALDVIQelgLERCQDTMiggafVRGVSGGERKRVSIGNEIIINPSLLLLDEPTSGL 333
Cdd:PRK13536 132 RENLLVFGRYFGMSTREIEAVIPSLLEFAR---LESKADAR-----VSDLSGGMKRRLTLARALINDPQLLILDEPTTGL 203
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79597808 334 DSTT------ALRTILMLhdiaeaGKTVITTIH--QPSSRLfhrFDKLILLGRGSLLYFGKSSEALDyfSSIGCS 400
Cdd:PRK13536 204 DPHArhliweRLRSLLAR------GKTILLTTHfmEEAERL---CDRLCVLEAGRKIAEGRPHALID--EHIGCQ 267
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
176-408 |
1.32e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 89.06 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLL---AGRISQSSTGGSVTYNDKP-YSKY-----LKSKIGFVTQDDV 246
Cdd:PRK14239 17 KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmNDLNPEVTITGSIVYNGHNiYSPRtdtvdLRKEIGMVFQQPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 247 LFPhLTVKETLTYAARLRlpktltrEQKKQRALDVIQELGL------ERCQDTMIGGAFvrGVSGGERKRVSIGNEIIIN 320
Cdd:PRK14239 97 PFP-MSIYENVVYGLRLK-------GIKDKQVLDEAVEKSLkgasiwDEVKDRLHDSAL--GLSGGQQQRVCIARVLATS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 321 PSLLLLDEPTSGLDSTTALR---TILMLHDiaeaGKTVITTIH--QPSSRLfhrFDKLILLGRGSLLYFGKSSEaldyfs 395
Cdd:PRK14239 167 PKIILLDEPTSALDPISAGKieeTLLGLKD----DYTMLLVTRsmQQASRI---SDRTGFFLDGDLIEYNDTKQ------ 233
|
250
....*....|...
gi 79597808 396 sigcsplIAMNPA 408
Cdd:PRK14239 234 -------MFMNPK 239
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
157-392 |
2.69e-19 |
|
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: 92.09 E-value: 2.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 157 LKFRDVTYKVvikkltSSVEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAgRISQSsTGGSVTYNDKPYSKY--- 233
Cdd:TIGR02203 331 VEFRNVTFRY------PGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIP-RFYEP-DSGQILLDGHDLADYtla 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 234 -LKSKIGFVTQDDVLFPHlTVKETLTYAARLRLPKTLTREQ-KKQRALDVIQEL--GLercqDTMIGGAFVRgVSGGERK 309
Cdd:TIGR02203 403 sLRRQVALVSQDVVLFND-TIANNIAYGRTEQADRAEIERAlAAAYAQDFVDKLplGL----DTPIGENGVL-LSGGQRQ 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 310 RVSIGNEIIINPSLLLLDEPTSGLDSTTAlRTILMLHDIAEAGKTVITTIHQPSSrlFHRFDKLILLGRGSLLYFGKSSE 389
Cdd:TIGR02203 477 RLAIARALLKDAPILILDEATSALDNESE-RLVQAALERLMQGRTTLVIAHRLST--IEKADRIVVMDDGRIVERGTHNE 553
|
...
gi 79597808 390 ALD 392
Cdd:TIGR02203 554 LLA 556
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
176-379 |
3.86e-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: 85.35 E-value: 3.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRIsqSSTGGSVTYNDKPYSKYLKSK----IGFVTQDDVLFPHl 251
Cdd:cd03246 14 EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLL--RPTSGRVRLDGADISQWDPNElgdhVGYLPQDDELFSG- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 252 TVKETLtyaarlrlpktltreqkkqraldviqelglercqdtmiggafvrgVSGGERKRVSIGNEIIINPSLLLLDEPTS 331
Cdd:cd03246 91 SIAENI---------------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNS 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 79597808 332 GLDSTTALRTILMLHDIAEAGKTVITTIHQPSsrLFHRFDKLILLGRG 379
Cdd:cd03246 126 HLDVEGERALNQAIAALKAAGATRIVIAHRPE--TLASADRILVLEDG 171
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
176-362 |
4.37e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 86.08 E-value: 4.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRisQSSTGGSVTYNDKP--YSKYlKSKIGFVTQDDVLFPHLTV 253
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGL--LPPAAGTIKLDGGDidDPDV-AEACHYLGHRNAMKPALTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 254 KETLTYAARLrlpktltREQKKQRALDVIQELGLERCQDTMIGgafvrGVSGGERKRVSIGNEIIINPSLLLLDEPTSGL 333
Cdd:PRK13539 91 AENLEFWAAF-------LGGEELDIAAALEAVGLAPLAHLPFG-----YLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170 180 190
....*....|....*....|....*....|
gi 79597808 334 DSTT-ALRTILMLHDIAEAGKTVITTiHQP 362
Cdd:PRK13539 159 DAAAvALFAELIRAHLAQGGIVIAAT-HIP 187
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
168-360 |
4.57e-19 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 87.39 E-value: 4.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 168 IKKLTSSV-EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSSTGGSVTYNDKPYSKY---LKSKIG-FVT 242
Cdd:CHL00131 10 IKNLHASVnENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKILEGDILFKGESILDLepeERAHLGiFLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 243 -QDDVLFPhltvkeTLTYAARLRLPKTLTREQKKQRALDVIQELGLERCQDTMIG--GAFV-----RGVSGGERKRVSIG 314
Cdd:CHL00131 90 fQYPIEIP------GVSNADFLRLAYNSKRKFQGLPELDPLEFLEIINEKLKLVGmdPSFLsrnvnEGFSGGEKKRNEIL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 79597808 315 NEIIINPSLLLLDEPTSGLDsTTALRTILM-LHDIAEAGKTVITTIH 360
Cdd:CHL00131 164 QMALLDSELAILDETDSGLD-IDALKIIAEgINKLMTSENSIILITH 209
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
163-396 |
5.68e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 88.61 E-value: 5.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 163 TYKVVIKK--LTSSV---------EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDK-PY 230
Cdd:COG4586 10 TYRVYEKEpgLKGALkglfrreyrEVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTS--GEVRVLGYvPF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 231 --SKYLKSKIGFV----TQddvLFPHLTVKETLTYAARL-RLPKtltrEQKKQRALDVIQELGLERCQDTMiggafVRGV 303
Cdd:COG4586 88 krRKEFARRIGVVfgqrSQ---LWWDLPAIDSFRLLKAIyRIPD----AEYKKRLDELVELLDLGELLDTP-----VRQL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 304 SGGERKRVSIGNEIIINPSLLLLDEPTSGLD--STTALRTilMLHDI-AEAGKTVITTIH------QPSSRlfhrfdkLI 374
Cdd:COG4586 156 SLGQRMRCELAAALLHRPKILFLDEPTIGLDvvSKEAIRE--FLKEYnRERGTTILLTSHdmddieALCDR-------VI 226
|
250 260
....*....|....*....|..
gi 79597808 375 LLGRGSLLYFGKSSEALDYFSS 396
Cdd:COG4586 227 VIDHGRIIYDGSLEELKERFGP 248
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
176-362 |
6.90e-19 |
|
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: 85.49 E-value: 6.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRisQSSTGGSVTYNDKPYSK---YLKSKIGFVTQDDVLFPHLT 252
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGL--LRPDSGEVRWNGTPLAEqrdEPHENILYLGHLPGLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 253 VKETLTYAARLRLPKTLTREQkkqrALDVIQELGLERcqdtmiggAFVRGVSGGERKRVSIGNEIIINPSLLLLDEPTSG 332
Cdd:TIGR01189 90 ALENLHFWAAIHGGAQRTIED----ALAAVGLTGFED--------LPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170 180 190
....*....|....*....|....*....|.
gi 79597808 333 LD-STTALRTILMLHDIAEAGKTVITTiHQP 362
Cdd:TIGR01189 158 LDkAGVALLAGLLRAHLARGGIVLLTT-HQD 187
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
180-365 |
8.49e-19 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 85.95 E-value: 8.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 180 LTGISGSVNPGEVLALMGPSGSGKTTLLSLL-------AGRISQSSTGGSVTYNDKPYSKYL---KSKIGFVTQddvlfp 249
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIygnylpdSGSILVRHDGGWVDLAQASPREILalrRRTIGYVSQ------ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 250 HLTV---KETLTYAARLRLPKTLTREQKKQRALDVIQELGL-ERCQD----TmiggaFvrgvSGGERKRVSIGNEIIINP 321
Cdd:COG4778 101 FLRViprVSALDVVAEPLLERGVDREEARARARELLARLNLpERLWDlppaT-----F----SGGEQQRVNIARGFIADP 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 79597808 322 SLLLLDEPTSGLDSTTALRTILMLHDIAEAGKTVITTIHQPSSR 365
Cdd:COG4778 172 PLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVR 215
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
131-339 |
1.10e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.12 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 131 DEMIPEDIEAGKKKPKFQAEPTLPIFlkfRDVtykVVIKKLTSSV-EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSL 209
Cdd:COG0488 287 EKLEREEPPRRDKTVEIRFPPPERLG---KKV---LELEGLSKSYgDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 210 LAGRISQSStgGSVTYNDkpyskylKSKIGFVTQD-DVLFPHLTVKETLTYAArlrlpktltREQKKQRALDVIQELGL- 287
Cdd:COG0488 361 LAGELEPDS--GTVKLGE-------TVKIGYFDQHqEELDPDKTVLDELRDGA---------PGGTEQEVRGYLGRFLFs 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 79597808 288 -ERcQDTmiggaFVRGVSGGERKRVSIGNEIIINPSLLLLDEPTSGLD--STTAL 339
Cdd:COG0488 423 gDD-AFK-----PVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDieTLEAL 471
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
176-360 |
4.02e-18 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 88.72 E-value: 4.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLL-------AGRI----------SQSStggsvtyndkpyskyLKSKI 238
Cdd:COG5265 370 ERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLfrfydvtSGRIlidgqdirdvTQAS---------------LRAAI 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 239 GFVTQDDVLFphltvKETLTY----------------AARL--------RLPKtltreqkkqraldviqelGLercqDTM 294
Cdd:COG5265 435 GIVPQDTVLF-----NDTIAYniaygrpdaseeeveaAARAaqihdfieSLPD------------------GY----DTR 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79597808 295 IGGafvRGV--SGGERKRVSIGNEIIINPSLLLLDEPTSGLDSTTAlRTILM-LHDIAEaGKTVITTIH 360
Cdd:COG5265 488 VGE---RGLklSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTE-RAIQAaLREVAR-GRTTLVIAH 551
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
182-336 |
4.69e-18 |
|
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: 88.20 E-value: 4.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 182 GISGSVNPGEVLALMGPSGSGKTTL-LSLLagRISQSStgGSVTYNDKPYSKY-------LKSKIGFVTQDDV--LFPHL 251
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTLgLALL--RLIPSE--GEIRFDGQDLDGLsrralrpLRRRMQVVFQDPFgsLSPRM 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 252 TVKETLTYAARLRLPKtLTREQKKQRALDVIQELGLERcqDTMigGAFVRGVSGGERKRVSIGNEIIINPSLLLLDEPTS 331
Cdd:COG4172 380 TVGQIIAEGLRVHGPG-LSAAERRARVAEALEEVGLDP--AAR--HRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTS 454
|
....*
gi 79597808 332 GLDST 336
Cdd:COG4172 455 ALDVS 459
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
168-420 |
5.27e-18 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 86.81 E-value: 5.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 168 IKKLTSSVE-KEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGriSQSSTGGSVTYNDK------PYSKylksKIGF 240
Cdd:PRK11607 22 IRNLTKSFDgQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAG--FEQPTAGQIMLDGVdlshvpPYQR----PINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 241 VTQDDVLFPHLTVKETLTYAARL-RLPKtltrEQKKQRaldVIQELGLERCQDtmIGGAFVRGVSGGERKRVSIGNEIII 319
Cdd:PRK11607 96 MFQSYALFPHMTVEQNIAFGLKQdKLPK----AEIASR---VNEMLGLVHMQE--FAKRKPHQLSGGQRQRVALARSLAK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 320 NPSLLLLDEPTSGLDSTTALRTILMLHDIAE-AGKTVITTIHQPSsrlfhrfDKLILLGRGSLLYFGKssealdyFSSIG 398
Cdd:PRK11607 167 RPKLLLLDEPMGALDKKLRDRMQLEVVDILErVGVTCVMVTHDQE-------EAMTMAGRIAIMNRGK-------FVQIG 232
|
250 260
....*....|....*....|....*..
gi 79597808 399 CSPLIAMNP-----AEFLldlanGNIN 420
Cdd:PRK11607 233 EPEEIYEHPttrysAEFI-----GSVN 254
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
157-391 |
5.83e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 85.14 E-value: 5.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 157 LKFRDVTyKVVIKKLtsSVEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYN---------- 226
Cdd:PRK13651 3 IKVKNIV-KIFNKKL--PTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDT--GTIEWIfkdeknkkkt 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 227 ------------DKPYSKYLKS------KIGFVTQ--DDVLFPHlTVKETLTYAAR-LRLPKtltrEQKKQRALDVIQEL 285
Cdd:PRK13651 78 kekekvleklviQKTRFKKIKKikeirrRVGVVFQfaEYQLFEQ-TIEKDIIFGPVsMGVSK----EEAKKRAAKYIELV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 286 GLErcQDTMIGGAFvrGVSGGERKRVSIGNEIIINPSLLLLDEPTSGLDSTTALRTILMLHDIAEAGKTVITTIHQPSSR 365
Cdd:PRK13651 153 GLD--ESYLQRSPF--ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNV 228
|
250 260
....*....|....*....|....*.
gi 79597808 366 LfHRFDKLILLGRGSLLYFGKSSEAL 391
Cdd:PRK13651 229 L-EWTKRTIFFKDGKIIKDGDTYDIL 253
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
192-334 |
7.55e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 85.70 E-value: 7.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 192 VLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYSK-----YL---KSKIGFVTQDDVLFPHLTVKETLTYAarl 263
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQK--GRIVLNGRVLFDaekgiCLppeKRRIGYVFQDARLFPHYKVRGNLRYG--- 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79597808 264 rlpktlTREQKKQRALDVIQELGLERCQDTmiggaFVRGVSGGERKRVSIGNEIIINPSLLLLDEPTSGLD 334
Cdd:PRK11144 101 ------MAKSMVAQFDKIVALLGIEPLLDR-----YPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
157-360 |
8.61e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 84.45 E-value: 8.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 157 LKFRDVTYkvvIKKLTSSVEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISqsSTGGSVTYND-----KPYS 231
Cdd:PRK13646 3 IRFDNVSY---TYQKGTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLK--PTTGTVTVDDitithKTKD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 232 KYLK---SKIGFVTQddvlFPHLTVKETLTYAARLRLPKT--LTREQKKQRALDVIQELGLERcqDTMIGGAFvrGVSGG 306
Cdd:PRK13646 78 KYIRpvrKRIGMVFQ----FPESQLFEDTVEREIIFGPKNfkMNLDEVKNYAHRLLMDLGFSR--DVMSQSPF--QMSGG 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 79597808 307 ERKRVSIGNEIIINPSLLLLDEPTSGLDSTTALRTILMLHDI-AEAGKTVITTIH 360
Cdd:PRK13646 150 QMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLqTDENKTIILVSH 204
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
180-356 |
9.88e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 87.00 E-value: 9.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 180 LTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGriSQSSTGGSVTYNDKPYSKY-----LKSKIGFVTQDDVLFPHLTVK 254
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSG--VYQPDSGEILLDGEPVRFRsprdaQAAGIAIIHQELNLVPNLSVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 255 ETLTYAARLRLPKTLTREQKKQRALDVIQELGLERCQDTMiggafVRGVSGGERKRVSIGNEIIINPSLLLLDEPTSGLD 334
Cdd:COG1129 98 ENIFLGREPRRGGLIDWRAMRRRARELLARLGLDIDPDTP-----VGDLSVAQQQLVEIARALSRDARVLILDEPTASLT 172
|
170 180
....*....|....*....|....
gi 79597808 335 S--TTALRTIlmLHDIAEAGKTVI 356
Cdd:COG1129 173 EreVERLFRI--IRRLKAQGVAII 194
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
157-380 |
1.07e-17 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 82.13 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 157 LKFRDVTYKVVIKKLTSSVekeILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNdkpyskylkS 236
Cdd:cd03250 1 ISVEDASFTWDSGEQETSF---TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLS--GSVSVP---------G 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 237 KIGFVTQddvlFPHL---TVKETLTYAARLRlpktltreqkKQRALDVIQELGLERcqD---------TMIGgafVRGV- 303
Cdd:cd03250 67 SIAYVSQ----EPWIqngTIRENILFGKPFD----------EERYEKVIKACALEP--DleilpdgdlTEIG---EKGIn 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 304 -SGGERKRVSIGNEIIINPSLLLLDEPTSGLDSTTA-------LRTILMLhdiaeaGKTVITTIHQPSsrLFHRFDKLIL 375
Cdd:cd03250 128 lSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGrhifencILGLLLN------NKTRILVTHQLQ--LLPHADQIVV 199
|
....*
gi 79597808 376 LGRGS 380
Cdd:cd03250 200 LDNGR 204
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
157-360 |
1.14e-17 |
|
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: 86.78 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 157 LKFRDVtykvviKKLTSSVEKEILT---GISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSSTGGSVTYND------ 227
Cdd:TIGR03269 280 IKVRNV------SKRYISVDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDewvdmt 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 228 ----------KPYskylkskIGFVTQDDVLFPHLTVKETLTYAARLRLPKTLTReqkkQRALDVIQELGLERCQDTMIGG 297
Cdd:TIGR03269 354 kpgpdgrgraKRY-------IGILHQEYDLYPHRTVLDNLTEAIGLELPDELAR----MKAVITLKMVGFDEEKAEEILD 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79597808 298 AFVRGVSGGERKRVSIGNEIIINPSLLLLDEPTSGLDSTTALR-TILMLHDIAEAGKTVITTIH 360
Cdd:TIGR03269 423 KYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDvTHSILKAREEMEQTFIIVSH 486
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
180-361 |
2.02e-17 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 84.36 E-value: 2.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 180 LTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRisQSSTGGSVTYNDKPYSKY-------LKSKIGFVTQDDVLFPHLT 252
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLL--ERPTSGSVLVDGVDLTALserelraARRKIGMIFQHFNLLSSRT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 253 VKETLTYAarLRLPKTlTREQKKQRALDVIQELGLE-RcqdtmiGGAFVRGVSGGERKRVSIGNEIIINPSLLLLDEPTS 331
Cdd:COG1135 99 VAENVALP--LEIAGV-PKAEIRKRVAELLELVGLSdK------ADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATS 169
|
170 180 190
....*....|....*....|....*....|....
gi 79597808 332 GLDSTTAlRTIL-MLHDI-AEAGKTV--ITtiHQ 361
Cdd:COG1135 170 ALDPETT-RSILdLLKDInRELGLTIvlIT--HE 200
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
176-362 |
2.03e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 81.39 E-value: 2.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGrISQsSTGGSVTYNDKPYSK----YLkskigfvtqDDVLF--- 248
Cdd:PRK13538 13 ERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAG-LAR-PDAGEVLWQGEPIRRqrdeYH---------QDLLYlgh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 249 -----PHLTVKETLTYAARLRlpktltREQKKQRALDVIQELGLERCQDtmiggAFVRGVSGGERKRVSIGNEIIINPSL 323
Cdd:PRK13538 82 qpgikTELTALENLRFYQRLH------GPGDDEALWEALAQVGLAGFED-----VPVRQLSAGQQRRVALARLWLTRAPL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 79597808 324 LLLDEPTSGLD--STTALRTILMLHdiAEAGKTVITTIHQP 362
Cdd:PRK13538 151 WILDEPFTAIDkqGVARLEALLAQH--AEQGGMVILTTHQD 189
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
159-337 |
2.65e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 86.17 E-value: 2.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 159 FRDVTYKVVIKKltssvekEILTGISGSVNPGEVLALMGPSGSGKTTLLSLL-------AGRISQSSTG-GSVTYndkpy 230
Cdd:PRK13657 337 FDDVSFSYDNSR-------QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLqrvfdpqSGRILIDGTDiRTVTR----- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 231 sKYLKSKIGFVTQDDVLFPHltvketlTYAARLRLPKT------LTREQKKQRALDVI--QELGLercqDTMIGGafvRG 302
Cdd:PRK13657 405 -ASLRRNIAVVFQDAGLFNR-------SIEDNIRVGRPdatdeeMRAAAERAQAHDFIerKPDGY----DTVVGE---RG 469
|
170 180 190
....*....|....*....|....*....|....*..
gi 79597808 303 --VSGGERKRVSIGNEIIINPSLLLLDEPTSGLDSTT 337
Cdd:PRK13657 470 rqLSGGERQRLAIARALLKDPPILILDEATSALDVET 506
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
178-334 |
3.91e-17 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 83.74 E-value: 3.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 178 EILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAG--RIsqssTGGSVTYNDKPYSKyLKSK---IGFVTQDDVLFPHLT 252
Cdd:PRK11650 18 QVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGleRI----TSGEIWIGGRVVNE-LEPAdrdIAMVFQNYALYPHMS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 253 VKETLTYAARLR-LPKTlTREQKKQRALDvIQELG--LERCQdtmiggafvRGVSGGERKRVSIGNEIIINPSLLLLDEP 329
Cdd:PRK11650 93 VRENMAYGLKIRgMPKA-EIEERVAEAAR-ILELEplLDRKP---------RELSGGQRQRVAMGRAIVREPAVFLFDEP 161
|
....*
gi 79597808 330 TSGLD 334
Cdd:PRK11650 162 LSNLD 166
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
166-335 |
4.50e-17 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 83.62 E-value: 4.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 166 VVIKKLTSSVEKE-ILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRisQSSTGGSVTYN--DKPYSKYLKSKIGFVT 242
Cdd:PRK11432 7 VVLKNITKRFGSNtVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGL--EKPTEGQIFIDgeDVTHRSIQQRDICMVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 243 QDDVLFPHLTVKETLTYAAR-LRLPKtltrEQKKQRALDVIQELGLERCQDTmiggaFVRGVSGGERKRVSIGNEIIINP 321
Cdd:PRK11432 85 QSYALFPHMSLGENVGYGLKmLGVPK----EERKQRVKEALELVDLAGFEDR-----YVDQISGGQQQRVALARALILKP 155
|
170
....*....|....
gi 79597808 322 SLLLLDEPTSGLDS 335
Cdd:PRK11432 156 KVLLFDEPLSNLDA 169
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
168-334 |
4.59e-17 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 81.38 E-value: 4.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 168 IKKLTSSVE-KEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSSTGGSVTYNDKPYSKYLKSK-----IGFV 241
Cdd:PRK09580 4 IKDLHVSVEdKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGTVEFKGKDLLELSPEDragegIFMA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 242 TQDDVLFPHLTVKETLTYAArlrlpkTLTREQKKQRAL------DVIQE-LGLERCQDTMIGGAFVRGVSGGERKRVSIG 314
Cdd:PRK09580 84 FQYPVEIPGVSNQFFLQTAL------NAVRSYRGQEPLdrfdfqDLMEEkIALLKMPEDLLTRSVNVGFSGGEKKRNDIL 157
|
170 180
....*....|....*....|
gi 79597808 315 NEIIINPSLLLLDEPTSGLD 334
Cdd:PRK09580 158 QMAVLEPELCILDESDSGLD 177
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
180-356 |
5.68e-17 |
|
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: 79.40 E-value: 5.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 180 LTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPY-----SKYLKSKIGFVTQD---DVLFPHL 251
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPAS--GEITLDGKPVtrrspRDAIRAGIAYVPEDrkrEGLVLDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 252 TVKETLTYAARLrlpktltreqkkqraldviqelglercqdtmiggafvrgvSGGERKRVSIGNEIIINPSLLLLDEPTS 331
Cdd:cd03215 94 SVAENIALSSLL----------------------------------------SGGNQQKVVLARWLARDPRVLILDEPTR 133
|
170 180
....*....|....*....|....*
gi 79597808 332 GLDSTTALRTILMLHDIAEAGKTVI 356
Cdd:cd03215 134 GVDVGAKAEIYRLIRELADAGKAVL 158
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
180-389 |
6.42e-17 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 84.75 E-value: 6.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 180 LTGISGSVNPGEVLALMGPSGSGKTTLLSLL-------AGRIsqsSTGGSVTYNDKPysKYLKSKIGFVTQDDVLFPHlT 252
Cdd:TIGR02204 356 LDGLNLTVRPGETVALVGPSGAGKSTLFQLLlrfydpqSGRI---LLDGVDLRQLDP--AELRARMALVPQDPVLFAA-S 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 253 VKETLTYAArlrlPKTlTREQ-----KKQRALDVIqeLGLERCQDTMIGGafvRGV--SGGERKRVSIGNEIIINPSLLL 325
Cdd:TIGR02204 430 VMENIRYGR----PDA-TDEEveaaaRAAHAHEFI--SALPEGYDTYLGE---RGVtlSGGQRQRIAIARAILKDAPILL 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79597808 326 LDEPTSGLD--STTALRTILmlhDIAEAGKTVITTIHQPSSRLfhRFDKLILLGRGSLLYFGKSSE 389
Cdd:TIGR02204 500 LDEATSALDaeSEQLVQQAL---ETLMKGRTTLIIAHRLATVL--KADRIVVMDQGRIVAQGTHAE 560
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
157-380 |
8.83e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 84.47 E-value: 8.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 157 LKFRDVTykvvikkLTSSVEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGrISQSSTGgsvtyndkpyskylks 236
Cdd:COG4178 363 LALEDLT-------LRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-LWPYGSG---------------- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 237 KIGFVTQDDVLF-------PHLTVKETLTYAARlrlPKTLTREQkkqrALDVIQELGLERCQDTM-IGGAFVRGVSGGER 308
Cdd:COG4178 419 RIARPAGARVLFlpqrpylPLGTLREALLYPAT---AEAFSDAE----LREALEAVGLGHLAERLdEEADWDQVLSLGEQ 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79597808 309 KRVSIGNEIIINPSLLLLDEPTSGLDSTTALRTILMLHDiAEAGKTVITTIHQPSSRLFHRfDKLILLGRGS 380
Cdd:COG4178 492 QRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGHRSTLAAFHD-RVLELTGDGS 561
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
157-360 |
1.78e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 80.64 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 157 LKFRDVTYkvvIKKLTSSVEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSS-----TGGSVTYNDKPYS 231
Cdd:PRK13641 3 IKFENVDY---IYSPGTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSgtitiAGYHITPETGNKN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 232 -KYLKSKIGFVTQ--DDVLFPHlTVKETLTYAarlrlPKTL--TREQKKQRALDVIQELGLErcQDTMIGGAFvrGVSGG 306
Cdd:PRK13641 80 lKKLRKKVSLVFQfpEAQLFEN-TVLKDVEFG-----PKNFgfSEDEAKEKALKWLKKVGLS--EDLISKSPF--ELSGG 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 79597808 307 ERKRVSIGNEIIINPSLLLLDEPTSGLDSTTALRTILMLHDIAEAGKTVITTIH 360
Cdd:PRK13641 150 QMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTH 203
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
182-351 |
3.03e-16 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 79.20 E-value: 3.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 182 GISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDK---PYSKY----------LKSKIGFVTQD--DV 246
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDA--GEVHYRMRdgqLRDLYalseaerrrlLRTEWGFVHQHprDG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 247 LFPHLT----VKETLT-----YAARLRlpktltreqkkQRALDVIQ--ELGLERCQDTmiGGAFvrgvSGGERKRVSIGN 315
Cdd:PRK11701 102 LRMQVSaggnIGERLMavgarHYGDIR-----------ATAGDWLErvEIDAARIDDL--PTTF----SGGMQQRLQIAR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 79597808 316 EIIINPSLLLLDEPTSGLD-STTA-----LRT---------ILMLHDIAEA 351
Cdd:PRK11701 165 NLVTHPRLVFMDEPTGGLDvSVQArlldlLRGlvrelglavVIVTHDLAVA 215
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
182-334 |
3.26e-16 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 80.55 E-value: 3.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 182 GISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISqsSTGGSVTYNDKPYSKY-------LKSKIGFVTQD--DVLFPHLT 252
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEE--PTSGEILFDGQDITGLsgrelrpLRRRMQMVFQDpyASLNPRMT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 253 VKETLtyAARLRLPKTLTREQKKQRALDVIQELGLERcqDTMigGAFVRGVSGGERKRVSIGNEIIINPSLLLLDEPTSG 332
Cdd:COG4608 114 VGDII--AEPLRIHGLASKAERRERVAELLELVGLRP--EHA--DRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSA 187
|
..
gi 79597808 333 LD 334
Cdd:COG4608 188 LD 189
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
176-336 |
3.99e-16 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 78.93 E-value: 3.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLaGR----ISQSSTGGSVTYNDKP-YSK-----YLKSKIGFVTQDD 245
Cdd:COG1117 23 DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCL-NRmndlIPGARVEGEILLDGEDiYDPdvdvvELRRRVGMVFQKP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 246 VLFPHlTVKETLTYAARLrlpktltREQKKQRALDVIQELGLERC------QDtmiggafvR------GVSGGERKRVSI 313
Cdd:COG1117 102 NPFPK-SIYDNVAYGLRL-------HGIKSKSELDEIVEESLRKAalwdevKD--------RlkksalGLSGGQQQRLCI 165
|
170 180
....*....|....*....|....*
gi 79597808 314 GNEIIINPSLLLLDEPTSGLD--ST 336
Cdd:COG1117 166 ARALAVEPEVLLMDEPTSALDpiST 190
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
168-394 |
5.08e-16 |
|
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: 81.77 E-value: 5.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 168 IKKLTSSVE-KEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSSTGGSVTYN-------------------- 226
Cdd:TIGR03269 3 VKNLTKKFDgKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSGRIIYHvalcekcgyverpskvgepc 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 227 -----------------DKPYSKYLKSKIGFVTQ--------DDVLFPHLTVKETLTYAArlrlpktltrEQKKQRALDV 281
Cdd:TIGR03269 83 pvcggtlepeevdfwnlSDKLRRRIRKRIAIMLQrtfalygdDTVLDNVLEALEEIGYEG----------KEAVGRAVDL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 282 IQELGLERcQDTMIGgafvRGVSGGERKRVSIGNEIIINPSLLLLDEPTSGLDSTTA-LRTILMLHDIAEAGKTVITTIH 360
Cdd:TIGR03269 153 IEMVQLSH-RITHIA----RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAkLVHNALEEAVKASGISMVLTSH 227
|
250 260 270
....*....|....*....|....*....|....
gi 79597808 361 QPSSrLFHRFDKLILLGRGSLLYFGKSSEALDYF 394
Cdd:TIGR03269 228 WPEV-IEDLSDKAIWLENGEIKEEGTPDEVVAVF 260
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
158-391 |
5.13e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 78.88 E-value: 5.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 158 KFRDVTYKVvikkltSSVEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISqsSTGGSVTYNDKPYSK----Y 233
Cdd:PRK13632 9 KVENVSFSY------PNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLK--PQSGEIKIDGITISKenlkE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 234 LKSKIGFVTQD-DVLFPHLTVKETLTYAARlrlPKTLTREQKKQRALDVIQELGLERCQDTMiggafVRGVSGGERKRVS 312
Cdd:PRK13632 81 IRKKIGIIFQNpDNQFIGATVEDDIAFGLE---NKKVPPKKMKDIIDDLAKKVGMEDYLDKE-----PQNLSGGQKQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 313 IGNEIIINPSLLLLDEPTSGLDSTTALRTILMLHDIAEAG-KTVITTIHQPSSRLfhRFDKLILLGRGSLLYFGKSSEAL 391
Cdd:PRK13632 153 IASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHDMDEAI--LADKVIVFSEGKLIAQGKPKEIL 230
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
178-355 |
6.61e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 78.00 E-value: 6.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 178 EILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGriSQSSTGGSVTYNDK-----PYSKYLKSKIGFVTQDDVLFPHLT 252
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCG--DPRATSGRIVFDGKditdwQTAKIMREAVAIVPEGRRVFSRMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 253 VKETLT----YAARLRLpktltrEQKKQRALDVIQELGLERCQ--DTMiggafvrgvSGGERKRVSIGNEIIINPSLLLL 326
Cdd:PRK11614 97 VEENLAmggfFAERDQF------QERIKWVYELFPRLHERRIQraGTM---------SGGEQQMLAIGRALMSQPRLLLL 161
|
170 180
....*....|....*....|....*....
gi 79597808 327 DEPTSGLDSTTALRTILMLHDIAEAGKTV 355
Cdd:PRK11614 162 DEPSLGLAPIIIQQIFDTIEQLREQGMTI 190
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
177-356 |
8.54e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 80.83 E-value: 8.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 177 KEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRisQSSTGGSVTYNDKPYS-----KYLKSKIGFVTQD---DVLF 248
Cdd:COG1129 265 GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGA--DPADSGEIRLDGKPVRirsprDAIRAGIAYVPEDrkgEGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 249 PHLTVKETLTYAARLRLPKT--LTREQKKQRALDVIQELGLeRCQDTmigGAFVRGVSGGERKRVSIGNEIIINPSLLLL 326
Cdd:COG1129 343 LDLSIRENITLASLDRLSRGglLDRRRERALAEEYIKRLRI-KTPSP---EQPVGNLSGGNQQKVVLAKWLATDPKVLIL 418
|
170 180 190
....*....|....*....|....*....|..
gi 79597808 327 DEPTSGLD--STTALRTIlmLHDIAEAGKTVI 356
Cdd:COG1129 419 DEPTRGIDvgAKAEIYRL--IRELAAEGKAVI 448
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
168-333 |
1.02e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.87 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 168 IKKLTSSVEkeILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYSKYLKSK-----IGFVT 242
Cdd:PRK15439 17 ISKQYSGVE--VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDS--GTLEIGGNPCARLTPAKahqlgIYLVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 243 QDDVLFPHLTVKETLTYaarlRLPKTLTREQKKQralDVIQELGlerCQDTMIGGAFVRGVSggERKRVSIGNEIIINPS 322
Cdd:PRK15439 93 QEPLLFPNLSVKENILF----GLPKRQASMQKMK---QLLAALG---CQLDLDSSAGSLEVA--DRQIVEILRGLMRDSR 160
|
170
....*....|.
gi 79597808 323 LLLLDEPTSGL 333
Cdd:PRK15439 161 ILILDEPTASL 171
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
177-408 |
1.24e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 77.80 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 177 KEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRisQSSTGGSVTYNDKPYSKYLKSK-------IGFVTQDDV--L 247
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGL--ESPSQGNVSWRGEPLAKLNRAQrkafrrdIQMVFQDSIsaV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 248 FPHLTVKETLtyAARLRLPKTLTREQKKQRALDVIQELGLercqDTMIGGAFVRGVSGGERKRVSIGNEIIINPSLLLLD 327
Cdd:PRK10419 103 NPRKTVREII--REPLRHLLSLDKAERLARASEMLRAVDL----DDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 328 EPTSGLDSTTALRTILMLHDIAEAGKTVITTI-HqpSSRLFHRF-DKLILLGRGSLLYFGKSSEALDYFSSIGCSPLIAM 405
Cdd:PRK10419 177 EAVSNLDLVLQAGVIRLLKKLQQQFGTACLFItH--DLRLVERFcQRVMVMDNGQIVETQPVGDKLTFSSPAGRVLQNAV 254
|
...
gi 79597808 406 NPA 408
Cdd:PRK10419 255 LPA 257
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
176-385 |
2.08e-15 |
|
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: 75.99 E-value: 2.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTL-LSLLagRISQsSTGGSVTYNDKPYSKY----LKSKIGFVTQDDVLFPH 250
Cdd:cd03244 16 LPPVLKNISFSIKPGEKVGIVGRTGSGKSSLlLALF--RLVE-LSSGSILIDGVDISKIglhdLRSRISIIPQDPVLFSG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 251 lTVKETL---TYAARLRLPKTLTREQKKQRALDviQELGLercqDTMI--GGAFvrgVSGGERKRVSIGNEIIINPSLLL 325
Cdd:cd03244 93 -TIRSNLdpfGEYSDEELWQALERVGLKEFVES--LPGGL----DTVVeeGGEN---LSVGQRQLLCLARALLRKSKILV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79597808 326 LDEPTSGLDSTTA--LRTILMLHDiaeAGKTVITTIHqpssRL--FHRFDKLILLGRGSLLYFG 385
Cdd:cd03244 163 LDEATASVDPETDalIQKTIREAF---KDCTVLTIAH----RLdtIIDSDRILVLDKGRVVEFD 219
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
177-382 |
2.72e-15 |
|
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: 76.77 E-value: 2.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 177 KEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRisQSSTGGSVTYNDKPYSKY-------LKSKIGFVTQD--DVL 247
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGL--EKPAQGTVSFRGQDLYQLdrkqrraFRRDVQLVFQDspSAV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 248 FPHLTVKETLtyAARLRLPKTLTREQKKQRALDVIQELGLercqDTMIGGAFVRGVSGGERKRVSIGNEIIINPSLLLLD 327
Cdd:TIGR02769 102 NPRMTVRQII--GEPLRHLTSLDESEQKARIAELLDMVGL----RSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 79597808 328 EPTSGLDSTTALRTILMLHDIAEAGKTVITTIHQpSSRLFHRF-DKLILLGRGSLL 382
Cdd:TIGR02769 176 EAVSNLDMVLQAVILELLRKLQQAFGTAYLFITH-DLRLVQSFcQRVAVMDKGQIV 230
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
178-360 |
2.98e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 76.81 E-value: 2.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 178 EILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKP--YSKY----LKSKIGFVTQ--DDVLFP 249
Cdd:PRK13636 20 HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSS--GRILFDGKPidYSRKglmkLRESVGMVFQdpDNQLFS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 250 hLTVKETLTYAA-RLRLPKTLTREqkkqRALDVIQELGLERCQDTMiggafVRGVSGGERKRVSIGNEIIINPSLLLLDE 328
Cdd:PRK13636 98 -ASVYQDVSFGAvNLKLPEDEVRK----RVDNALKRTGIEHLKDKP-----THCLSFGQKKRVAIAGVLVMEPKVLVLDE 167
|
170 180 190
....*....|....*....|....*....|...
gi 79597808 329 PTSGLDSTTALRTILMLHDIA-EAGKTVITTIH 360
Cdd:PRK13636 168 PTAGLDPMGVSEIMKLLVEMQkELGLTIIIATH 200
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
176-345 |
3.19e-15 |
|
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: 79.34 E-value: 3.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKT----TLLSLLAGriSQSSTGGSVTYNDKPyskYLK-----------SKIGF 240
Cdd:COG4172 22 TVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPD--PAAHPSGSILFDGQD---LLGlserelrrirgNRIAM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 241 VTQDDV--LFPHLTVKETLtyAARLRLPKTLTREQKKQRALDVIQELGL---ERCQDtmiggAFVRGVSGGERKRVSIGN 315
Cdd:COG4172 97 IFQEPMtsLNPLHTIGKQI--AEVLRLHRGLSGAAARARALELLERVGIpdpERRLD-----AYPHQLSGGQRQRVMIAM 169
|
170 180 190
....*....|....*....|....*....|
gi 79597808 316 EIIINPSLLLLDEPTSGLDSTTAlRTILML 345
Cdd:COG4172 170 ALANEPDLLIADEPTTALDVTVQ-AQILDL 198
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
182-356 |
3.59e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.92 E-value: 3.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 182 GISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYS-----KYLKSKIGFVTQDDVLFPHLTVKET 256
Cdd:COG3845 23 DVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDS--GEILIDGKPVRirsprDAIALGIGMVHQHFMLVPNLTVAEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 257 LTYAARLRLPKTLTREQKKQRALDVIQELGLErcqdtmIG-GAFVRGVSGGERKRVsignEII----INPSLLLLDEPTS 331
Cdd:COG3845 101 IVLGLEPTKGGRLDRKAARARIRELSERYGLD------VDpDAKVEDLSVGEQQRV----EILkalyRGARILILDEPTA 170
|
170 180
....*....|....*....|....*..
gi 79597808 332 GLdsTTALRTILM--LHDIAEAGKTVI 356
Cdd:COG3845 171 VL--TPQEADELFeiLRRLAAEGKSII 195
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
176-362 |
4.80e-15 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 74.45 E-value: 4.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRisQSSTGGSVTYNDKPYSKY---LKSKIGFVTQDDVLFPHLT 252
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGL--SPPLAGRVLLNGGPLDFQrdsIARGLLYLGHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 253 VKETLTYAARLRlpktlTREQKKQrALDVIQELGLERcqdtmiggAFVRGVSGGERKRVSIGNEIIINPSLLLLDEPTSG 332
Cdd:cd03231 90 VLENLRFWHADH-----SDEQVEE-ALARVGLNGFED--------RPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
170 180 190
....*....|....*....|....*....|
gi 79597808 333 LDSTTALRTILMLHDIAEAGKTVITTIHQP 362
Cdd:cd03231 156 LDKAGVARFAEAMAGHCARGGMVVLTTHQD 185
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
176-389 |
6.01e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 75.47 E-value: 6.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRI----SQSSTGGSVTYNDKPYSKY----LKSKIGFVTQDDVL 247
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIeiydSKIKVDGKVLYFGKDIFQIdaikLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 248 FPHLTVKETLTYAarLRLPKTLTREQKKQRALDVIQELGL-ERCQDTMIGGAfvRGVSGGERKRVSIGNEIIINPSLLLL 326
Cdd:PRK14246 102 FPHLSIYDNIAYP--LKSHGIKEKREIKKIVEECLRKVGLwKEVYDRLNSPA--SQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79597808 327 DEPTSGLDSTTALRTILMLHDIAEAGKTVITTiHQPsSRLFHRFDKLILLGRGSLLYFGKSSE 389
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELKNEIAIVIVS-HNP-QQVARVADYVAFLYNGELVEWGSSNE 238
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
157-364 |
6.78e-15 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 78.52 E-value: 6.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 157 LKFRDVTYKVVIKkltssvEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAgR---ISQsstgGSVT---YNDKPY 230
Cdd:PRK11176 342 IEFRNVTFTYPGK------EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLT-RfydIDE----GEILldgHDLRDY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 231 S-KYLKSKIGFVTQDDVLFpHLTVKETLTYAARlrlpKTLTREQ-----KKQRALDVIQEL--GLercqDTMIG--GAFV 300
Cdd:PRK11176 411 TlASLRNQVALVSQNVHLF-NDTIANNIAYART----EQYSREQieeaaRMAYAMDFINKMdnGL----DTVIGenGVLL 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79597808 301 rgvSGGERKRVSIGNEIIINPSLLLLDEPTSGLDsTTALRTILMLHDIAEAGKTVITTIHQPSS 364
Cdd:PRK11176 482 ---SGGQRQRIAIARALLRDSPILILDEATSALD-TESERAIQAALDELQKNRTSLVIAHRLST 541
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
180-334 |
7.76e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 76.16 E-value: 7.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 180 LTGISGSVNPGEVLALMGPSGSGKTTLLSLLAgrISQSSTGGSVTYN-------DKPYSKYLKSKIGFVTQDDV--LFPH 250
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLT--MIETPTGGELYYQgqdllkaDPEAQKLLRQKIQIVFQNPYgsLNPR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 251 LTVKETLtyAARLRLPKTLTREQKKQRALDVIQELGL--ERCQ--DTMIggafvrgvSGGERKRVSIGNEIIINPSLLLL 326
Cdd:PRK11308 109 KKVGQIL--EEPLLINTSLSAAERREKALAMMAKVGLrpEHYDryPHMF--------SGGQRQRIAIARALMLDPDVVVA 178
|
....*...
gi 79597808 327 DEPTSGLD 334
Cdd:PRK11308 179 DEPVSALD 186
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
168-385 |
1.25e-14 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 73.72 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 168 IKKLTSSVEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPySKYLKSKIGFVtqddvl 247
Cdd:cd03220 26 LGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDS--GTVTVRGRV-SSLLGLGGGFN------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 248 fPHLTVKETLTYAARLrlpKTLTREQKKQRALDVIQELGLERCQDTMiggafVRGVSGGERKRVSIGNEIIINPSLLLLD 327
Cdd:cd03220 97 -PELTGRENIYLNGRL---LGLSRKEIDEKIDEIIEFSELGDFIDLP-----VKTYSSGMKARLAFAIATALEPDILLID 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 79597808 328 EPTSGLDSTTALRTILMLHDIAEAGKTVITTIHQPSSrlFHRF-DKLILLGRGSLLYFG 385
Cdd:cd03220 168 EVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSS--IKRLcDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
157-361 |
1.60e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 74.45 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 157 LKFRDVTYkvvikklTSSVEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYSKY--- 233
Cdd:PRK13652 4 IETRDLCY-------SYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTS--GSVLIRGEPITKEnir 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 234 -LKSKIGFVTQ--DDVLFPHlTVKETLTYAArlrLPKTLTREQKKQRALDVIQELGLERCQDTMiggafVRGVSGGERKR 310
Cdd:PRK13652 75 eVRKFVGLVFQnpDDQIFSP-TVEQDIAFGP---INLGLDEETVAHRVSSALHMLGLEELRDRV-----PHHLSGGEKKR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 79597808 311 VSIGNEIIINPSLLLLDEPTSGLDSTTALRTILMLHDIAEA-GKTVITTIHQ 361
Cdd:PRK13652 146 VAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQ 197
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
175-382 |
1.87e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 73.07 E-value: 1.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 175 VEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSSTGGSVTYNDKPYSkylkskigfvtQDDVLFPHLTVK 254
Cdd:COG2401 41 VERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFG-----------REASLIDAIGRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 255 ETLTYAARLrlpktltreqkkqraldviqelgLERCQdtmIGGAF-----VRGVSGGERKRVSIGNEIIINPSLLLLDEP 329
Cdd:COG2401 110 GDFKDAVEL-----------------------LNAVG---LSDAVlwlrrFKELSTGQKFRFRLALLLAERPKLLVIDEF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 79597808 330 TSGLDSTTALRTILMLHDIA-EAGKTVITTIHQPSSRLFHRFDKLILLGRGSLL 382
Cdd:COG2401 164 CSHLDRQTAKRVARNLQKLArRAGITLVVATHHYDVIDDLQPDLLIFVGYGGVP 217
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
184-334 |
2.34e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 75.84 E-value: 2.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 184 SGSVNPGEVLALMGPSGSGKTTLLSLLaGRISQSSTGGSV-------TYNDKPYSKYLKSKIGFVTQDDVLFPHLTVKET 256
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLL-NRLIEPTRGQVLidgvdiaKISDAELREVRRKKIAMVFQSFALMPHMTVLDN 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79597808 257 LTYAARLrlpKTLTREQKKQRALDVIQELGLERcqdtmIGGAFVRGVSGGERKRVSIGNEIIINPSLLLLDEPTSGLD 334
Cdd:PRK10070 127 TAFGMEL---AGINAEERREKALDALRQVGLEN-----YAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
176-334 |
3.93e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 72.44 E-value: 3.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYSKY----LKSKIGFVTQDDVLFPHl 251
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTS--GTLLFEGEDISTLkpeiYRQQVSYCAQTPTLFGD- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 252 TVKETLTYAARLRlpktlTREQKKQRALDVIQELGLErcqDTMIGGAfVRGVSGGERKRVSIGNEIIINPSLLLLDEPTS 331
Cdd:PRK10247 96 TVYDNLIFPWQIR-----NQQPDPAIFLDDLERFALP---DTILTKN-IAELSGGEKQRISLIRNLQFMPKVLLLDEITS 166
|
...
gi 79597808 332 GLD 334
Cdd:PRK10247 167 ALD 169
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
179-360 |
4.31e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 72.90 E-value: 4.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 179 ILTGISGSVNPGEVLALMGPSGSGKTTLLSLLaGRiSQSSTGGSVTYNDKPY----SKYLKSKIGFVTQDDVLFPHLTVK 254
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-GR-HQPPSEGEILLDAQPLeswsSKAFARKVAYLPQQLPAAEGMTVR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 255 EtLTYAARLRLPKTLTR--EQKKQRALDVIQELGLercqdTMIGGAFVRGVSGGERKRVSIGNEIIINPSLLLLDEPTSG 332
Cdd:PRK10575 104 E-LVAIGRYPWHGALGRfgAADREKVEEAISLVGL-----KPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSA 177
|
170 180
....*....|....*....|....*....
gi 79597808 333 LDSTTALRTILMLHDIA-EAGKTVITTIH 360
Cdd:PRK10575 178 LDIAHQVDVLALVHRLSqERGLTVIAVLH 206
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
165-389 |
4.69e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 72.64 E-value: 4.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 165 KVVIKKLTSSV-EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRIS---QSSTGGSVTYNDKPYSKY----LKS 236
Cdd:PRK14247 3 KIEIRDLKVSFgQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypEARVSGEVYLDGQDIFKMdvieLRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 237 KIGFVTQDDVLFPHLTVKETLTYAARL-RLPKtlTREQKKQRALDVIQELGL-ERCQDTMigGAFVRGVSGGERKRVSIG 314
Cdd:PRK14247 83 RVQMVFQIPNPIPNLSIFENVALGLKLnRLVK--SKKELQERVRWALEKAQLwDEVKDRL--DAPAGKLSGGQQQRLCIA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79597808 315 NEIIINPSLLLLDEPTSGLD-STTALRTILMLHDIAEAGKTVITTIHQPSSRLfhrFDKLILLGRGSLLYFGKSSE 389
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDpENTAKIESLFLELKKDMTIVLVTHFPQQAARI---SDYVAFLYKGQIVEWGPTRE 231
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
166-351 |
9.47e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 72.02 E-value: 9.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 166 VVIKKLTSSV-EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRisQSSTGGSVTYNDKPYSKyLKSKIGFVTQD 244
Cdd:PRK11247 13 LLLNAVSKRYgERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGL--ETPSAGELLAGTAPLAE-AREDTRLMFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 245 DVLFPHLTVKETLTyaarLRLpktltREQKKQRALDVIQELGL-ERCQDtmiggaFVRGVSGGERKRVSIGNEIIINPSL 323
Cdd:PRK11247 90 ARLLPWKKVIDNVG----LGL-----KGQWRDAALQALAAVGLaDRANE------WPAALSGGQKQRVALARALIHRPGL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 79597808 324 LLLDEPTSGLDSTTALR--------------TILML-HDIAEA 351
Cdd:PRK11247 155 LLLDEPLGALDALTRIEmqdlieslwqqhgfTVLLVtHDVSEA 197
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
166-337 |
1.02e-13 |
|
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: 69.01 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 166 VVIKKLTSSVE-KEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDkpyskylKSKIGFVTQd 244
Cdd:cd03221 1 IELENLSKTYGgKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDE--GIVTWGS-------TVKIGYFEQ- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 245 dvlfphltvketltyaarlrlpktltreqkkqraldviqelglercqdtmiggafvrgVSGGERKRVSIGNEIIINPSLL 324
Cdd:cd03221 71 ----------------------------------------------------------LSGGEKMRLALAKLLLENPNLL 92
|
170
....*....|...
gi 79597808 325 LLDEPTSGLDSTT 337
Cdd:cd03221 93 LLDEPTNHLDLES 105
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
176-398 |
1.09e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 72.39 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYND------KPYSKYLKSKIGFVTQ--DDVL 247
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTS--GKIIIDGvditdkKVKLSDIRKKVGLVFQypEYQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 248 FPHlTVKETLTYAarlrlPKTL--TREQKKQRALDVIQELGLERcQDTMIGGAFvrGVSGGERKRVSIGNEIIINPSLLL 325
Cdd:PRK13637 97 FEE-TIEKDIAFG-----PINLglSEEEIENRVKRAMNIVGLDY-EDYKDKSPF--ELSGGQKRRVAIAGVVAMEPKILI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 326 LDEPTSGLDSTT---ALRTILMLHDiaEAGKTVITTIHqpSSRLFHRF-DKLILLGRGSLLYFGKSSEA---LDYFSSIG 398
Cdd:PRK13637 168 LDEPTAGLDPKGrdeILNKIKELHK--EYNMTIILVSH--SMEDVAKLaDRIIVMNKGKCELQGTPREVfkeVETLESIG 243
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
176-389 |
1.53e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 71.58 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYSKY----LKSKIGFVTQD-DVLFPH 250
Cdd:PRK13635 19 ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEA--GTITVGGMVLSEEtvwdVRRQVGMVFQNpDNQFVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 251 LTVKETLTYAARLR-LPktltREQKKQRALDVIQELGLErcqdtmiggAFVR----GVSGGERKRVSIGNEIIINPSLLL 325
Cdd:PRK13635 97 ATVQDDVAFGLENIgVP----REEMVERVDQALRQVGME---------DFLNrephRLSGGQKQRVAIAGVLALQPDIII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 79597808 326 LDEPTSGLD---STTALRTILMLHDiaEAGKTVITTIHQPSSRLfhRFDKLILLGRGSLLYFGKSSE 389
Cdd:PRK13635 164 LDEATSMLDprgRREVLETVRQLKE--QKGITVLSITHDLDEAA--QADRVIVMNKGEILEEGTPEE 226
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
174-381 |
1.73e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 73.73 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 174 SVEKEILTG-ISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSstgGSVTYNDKPYS----KYLKSKIGFVTQDDVLF 248
Cdd:PRK11174 359 SPDGKTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ---GSLKINGIELReldpESWRKHLSWVGQNPQLP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 249 pHLTVKETLTYAArlrlpKTLTREQ-----KKQRALDVI--QELGLercqDTMIG--GAfvrGVSGGERKRVSIGNEIII 319
Cdd:PRK11174 436 -HGTLRDNVLLGN-----PDASDEQlqqalENAWVSEFLplLPQGL----DTPIGdqAA---GLSVGQAQRLALARALLQ 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79597808 320 NPSLLLLDEPTSGLDSTTALRTILMLHDiAEAGKTVITTIHQPSSrlFHRFDKLILLGRGSL 381
Cdd:PRK11174 503 PCQLLLLDEPTASLDAHSEQLVMQALNA-ASRRQTTLMVTHQLED--LAQWDQIWVMQDGQI 561
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
176-389 |
2.28e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 71.19 E-value: 2.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKP--YSKY----LKSKIGFVTQD-DVLF 248
Cdd:PRK13638 13 DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQK--GAVLWQGKPldYSKRgllaLRQQVATVFQDpEQQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 249 PHLTVKETLTYAAR-LRLPKtltrEQKKQRALDVIQELGLERCQDTMIggafvRGVSGGERKRVSIGNEIIINPSLLLLD 327
Cdd:PRK13638 91 FYTDIDSDIAFSLRnLGVPE----AEITRRVDEALTLVDAQHFRHQPI-----QCLSHGQKKRVAIAGALVLQARYLLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79597808 328 EPTSGLDSTTALRTILMLHDIAEAGKTVITTIHQpSSRLFHRFDKLILLGRGSLLYFGKSSE 389
Cdd:PRK13638 162 EPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHD-IDLIYEISDAVYVLRQGQILTHGAPGE 222
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
180-335 |
2.56e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 73.02 E-value: 2.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 180 LTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGriSQSSTGGSVTYNDKPYsKY------LKSKIGFVTQDDVLFPHLTV 253
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSG--NYQPDAGSILIDGQEM-RFasttaaLAAGVAIIYQELHLVPEMTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 254 KETLTYAarlRLPKT---LTREQKKQRALDVIQELGLERCQDTMiggafVRGVSGGERKRVSIGNEIIINPSLLLLDEPT 330
Cdd:PRK11288 97 AENLYLG---QLPHKggiVNRRLLNYEAREQLEHLGVDIDPDTP-----LKYLSIGQRQMVEIAKALARNARVIAFDEPT 168
|
....*
gi 79597808 331 SGLDS 335
Cdd:PRK11288 169 SSLSA 173
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
157-391 |
2.56e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 71.30 E-value: 2.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 157 LKFRDVTYKVvikKLTSSVEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISqsSTGGSVTYND--------K 228
Cdd:PRK13643 2 IKFEKVNYTY---QPNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQ--PTEGKVTVGDivvsstskQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 229 PYSKYLKSKIGFVTQddvlFPHLTVKETLTYAARLRLPKT--LTREQKKQRALDVIQELGLERcqDTMIGGAFvrGVSGG 306
Cdd:PRK13643 77 KEIKPVRKKVGVVFQ----FPESQLFEETVLKDVAFGPQNfgIPKEKAEKIAAEKLEMVGLAD--EFWEKSPF--ELSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 307 ERKRVSIGNEIIINPSLLLLDEPTSGLDSTTALRTILMLHDIAEAGKTVITTIHQPSSrLFHRFDKLILLGRGSLLYFGK 386
Cdd:PRK13643 149 QMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDD-VADYADYVYLLEKGHIISCGT 227
|
....*
gi 79597808 387 SSEAL 391
Cdd:PRK13643 228 PSDVF 232
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
176-334 |
3.06e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 70.14 E-value: 3.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDkpyskylKSKIGFVTQD---DVLFPhLT 252
Cdd:PRK09544 16 QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDE--GVIKRNG-------KLRIGYVPQKlylDTTLP-LT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 253 VKETLtyaaRLRlPKTltreqKKQRALDViqelgLERCQDTMIGGAFVRGVSGGERKRVSIGNEIIINPSLLLLDEPTSG 332
Cdd:PRK09544 86 VNRFL----RLR-PGT-----KKEDILPA-----LKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQG 150
|
..
gi 79597808 333 LD 334
Cdd:PRK09544 151 VD 152
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
187-360 |
4.43e-13 |
|
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: 73.51 E-value: 4.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 187 VNPGEVLALMGPSGSGKTTLLSLLAGriSQSSTGGSVTYNDKPYSKYLK---SKIGFVTQDDVLFPHLTVKETLTYAARL 263
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTG--DTTVTSGDATVAGKSILTNISdvhQNMGYCPQFDAIDDLLTGREHLYLYARL 2039
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 264 RlpkTLTREQKKQRALDVIQELGLERCQDTMIGGafvrgVSGGERKRVSIGNEIIINPSLLLLDEPTSGLDSTTALRTIL 343
Cdd:TIGR01257 2040 R---GVPAEEIEKVANWSIQSLGLSLYADRLAGT-----YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWN 2111
|
170
....*....|....*..
gi 79597808 344 MLHDIAEAGKTVITTIH 360
Cdd:TIGR01257 2112 TIVSIIREGRAVVLTSH 2128
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
191-361 |
4.55e-13 |
|
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: 73.51 E-value: 4.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 191 EVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYSKYL---KSKIGFVTQDDVLFPHLTVKETLTYAARLrlpK 267
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTS--GTVLVGGKDIETNLdavRQSLGMCPQHNILFHHLTVAEHILFYAQL---K 1031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 268 TLTREQKKQRALDVIQELGLERCQDTMiggafVRGVSGGERKRVSIGNEIIINPSLLLLDEPTSGLDSTTAlRTILMLHD 347
Cdd:TIGR01257 1032 GRSWEEAQLEMEAMLEDTGLHHKRNEE-----AQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSR-RSIWDLLL 1105
|
170
....*....|....
gi 79597808 348 IAEAGKTVITTIHQ 361
Cdd:TIGR01257 1106 KYRSGRTIIMSTHH 1119
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
177-353 |
4.69e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 70.12 E-value: 4.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 177 KEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLA---GRISQSSTGGSVTYNDKPYSKY-----LKSKIGFVTQDDVLF 248
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNrmnDKVSGYRYSGDVLLGGRSIFNYrdvleFRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 249 PHLTVKETLtyaARLRLPKTLTREQKKQRALDVIQELGL-ERCQDTMIGGAFvrGVSGGERKRVSIGNEIIINPSLLLLD 327
Cdd:PRK14271 114 PMSIMDNVL---AGVRAHKLVPRKEFRGVAQARLTEVGLwDAVKDRLSDSPF--RLSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190
....*....|....*....|....*....|....*....
gi 79597808 328 EPTSGLDSTTA-------------LRTILMLHDIAEAGK 353
Cdd:PRK14271 189 EPTSALDPTTTekieefirsladrLTVIIVTHNLAQAAR 227
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
185-335 |
4.79e-13 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 69.74 E-value: 4.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 185 GSVNPGEVLALMGPSGSGKTTLLSLLAGRISQS-----STGGSVTYndKPysKYLKSKIGfVTQDDVLFPHLTVKETLTY 259
Cdd:cd03237 20 GSISESEVIGILGPNGIGKTTFIKMLAGVLKPDegdieIELDTVSY--KP--QYIKADYE-GTVRDLLSSITKDFYTHPY 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79597808 260 AarlrlpKTltreqkkqralDVIQELGLERCQDTMiggafVRGVSGGERKRVSIGNEIIINPSLLLLDEPTSGLDS 335
Cdd:cd03237 95 F------KT-----------EIAKPLQIEQILDRE-----VPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
180-365 |
5.29e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 69.81 E-value: 5.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 180 LTGISGSVNPGEVLALMGPSGSGKTTLL---SLLAGRISQSSTGGSVTYNDKP-YSKY-----LKSKIGFVTQDDVLFPH 250
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILrcfNRLNDLIPGFRVEGKVTFHGKNlYAPDvdpveVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 251 lTVKETLTYAARLRLPK----TLTREQKKQRAL-----DVIQELGLercqdtmiggafvrGVSGGERKRVSIGNEIIINP 321
Cdd:PRK14243 106 -SIYDNIAYGARINGYKgdmdELVERSLRQAALwdevkDKLKQSGL--------------SLSGGQQQRLCIARAIAVQP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 79597808 322 SLLLLDEPTSGLDSTTALRTILMLHDIAEAGKTVITTiH--QPSSR 365
Cdd:PRK14243 171 EVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVT-HnmQQAAR 215
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
157-361 |
5.46e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 70.05 E-value: 5.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 157 LKFRDVTYKVVIKkltSSVEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISqsSTGGSVTYNDKPYS----- 231
Cdd:PRK13634 3 ITFQKVEHRYQYK---TPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQ--PTSGTVTIGERVITagkkn 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 232 ---KYLKSKIGFVTQddvlFPHL-----TVKETLTYAarlrlPKT--LTREQKKQRALDVIQELGLErcQDTMIGGAFvr 301
Cdd:PRK13634 78 kklKPLRKKVGIVFQ----FPEHqlfeeTVEKDICFG-----PMNfgVSEEDAKQKAREMIELVGLP--EELLARSPF-- 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79597808 302 GVSGGERKRVSIGNEIIINPSLLLLDEPTSGLDSTTALRTILM---LHDiaEAGKTVITTIHQ 361
Cdd:PRK13634 145 ELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMfykLHK--EKGLTTVLVTHS 205
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
177-334 |
6.30e-13 |
|
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: 71.89 E-value: 6.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 177 KEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGrISQSSTGGSvtyndKPYSKYlksKIGFVTQDDVLFPHLTVKET 256
Cdd:TIGR03719 18 KEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-VDKDFNGEA-----RPQPGI---KVGYLPQEPQLDPTKTVREN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 257 LTYAARlRLPKTLTR-EQ----------------KKQRAL-DVIQELG-------LE------RCQDtmiGGAFVRGVSG 305
Cdd:TIGR03719 89 VEEGVA-EIKDALDRfNEisakyaepdadfdklaAEQAELqEIIDAADawdldsqLEiamdalRCPP---WDADVTKLSG 164
|
170 180
....*....|....*....|....*....
gi 79597808 306 GERKRVSIGNEIIINPSLLLLDEPTSGLD 334
Cdd:TIGR03719 165 GERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
180-356 |
7.60e-13 |
|
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: 67.07 E-value: 7.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 180 LTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQssTGGSVTYNDKPYSKY-----LKSKIGFVTQddvlfphltvk 254
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKP--DSGEILVDGKEVSFAsprdaRRAGIAMVYQ----------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 255 etltyaarlrlpktltreqkkqraldviqelglercqdtmiggafvrgVSGGERKRVSIGNEIIINPSLLLLDEPTSGLD 334
Cdd:cd03216 83 ------------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALT 114
|
170 180
....*....|....*....|..
gi 79597808 335 STTALRTILMLHDIAEAGKTVI 356
Cdd:cd03216 115 PAEVERLFKVIRRLRAQGVAVI 136
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
176-364 |
8.03e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 71.67 E-value: 8.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRIsqSSTGGSVTYNDKPYSKY----LKSKIGFVTQDDVLFPHl 251
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHF--DVSEGDIRFHDIPLTKLqldsWRSRLAVVSQTPFLFSD- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 252 tvketlTYAARLRLPK-TLTREQKKQRA-LDVIQE--LGLERCQDTMIGGafvRGV--SGGERKRVSIGNEIIINPSLLL 325
Cdd:PRK10789 404 ------TVANNIALGRpDATQQEIEHVArLASVHDdiLRLPQGYDTEVGE---RGVmlSGGQKQRISIARALLLNAEILI 474
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 79597808 326 LDEPTSGLDSTTALRtilMLHDIAE--AGKTVITTIHQPSS 364
Cdd:PRK10789 475 LDDALSAVDGRTEHQ---ILHNLRQwgEGRTVIISAHRLSA 512
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
180-361 |
9.67e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 71.35 E-value: 9.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 180 LTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGriSQSSTGGSVTYNDKPYSKyLKSK------IGFVTQDDVLFPHLTV 253
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSG--IHEPTKGTITINNINYNK-LDHKlaaqlgIGIIYQELSVIDELTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 254 KETLtYAARLRLPKTL-----TREQKKQRALDVIQELGLERCQDTmiggaFVRGVSGGERKRVSIGNEIIINPSLLLLDE 328
Cdd:PRK09700 98 LENL-YIGRHLTKKVCgvniiDWREMRVRAAMMLLRVGLKVDLDE-----KVANLSISHKQMLEIAKTLMLDAKVIIMDE 171
|
170 180 190
....*....|....*....|....*....|...
gi 79597808 329 PTSGLDSTTALRTILMLHDIAEAGKTVITTIHQ 361
Cdd:PRK09700 172 PTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHK 204
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
186-364 |
1.22e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 68.76 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 186 SVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYSKYLKSK-IGFVTQD---DVLFPHLTvkETLTYAA 261
Cdd:PRK15056 29 TVPGGSIAALVGVNGSGKSTLFKALMGFVRLAS--GKISILGQPTRQALQKNlVAYVPQSeevDWSFPVLV--EDVVMMG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 262 R------LRLPKtltrEQKKQRALDVIQELGLERCQDTMIGGafvrgVSGGERKRVSIGNEIIINPSLLLLDEPTSGLDS 335
Cdd:PRK15056 105 RyghmgwLRRAK----KRDRQIVTAALARVDMVEFRHRQIGE-----LSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
170 180
....*....|....*....|....*....
gi 79597808 336 TTALRTILMLHDIAEAGKTVITTIHQPSS 364
Cdd:PRK15056 176 KTEARIISLLRELRDEGKTMLVSTHNLGS 204
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
178-360 |
1.29e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 68.99 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 178 EILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYS----KYLKSKIGFVTQ--DDVLFPhL 251
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQR--GRVKVMGREVNaeneKWVRSKVGLVFQdpDDQVFS-S 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 252 TVKETLTYAARlrlPKTLTREQKKQRALDVIQELGLERCQDTMiggafVRGVSGGERKRVSIGNEIIINPSLLLLDEPTS 331
Cdd:PRK13647 96 TVWDDVAFGPV---NMGLDKDEVERRVEEALKAVRMWDFRDKP-----PYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMA 167
|
170 180 190
....*....|....*....|....*....|..
gi 79597808 332 GLD--STTALRTIL-MLHdiaEAGKTVITTIH 360
Cdd:PRK13647 168 YLDprGQETLMEILdRLH---NQGKTVIVATH 196
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
176-337 |
1.35e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 68.64 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYSKYLKS-------KIGFVTQDDVLF 248
Cdd:PRK11831 19 NRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDH--GEILFDGENIPAMSRSrlytvrkRMSMLFQSGALF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 249 PHLTVKETLTYAAR--LRLPKTLTREQKKQRaldvIQELGLERCQDTMIGgafvrGVSGGERKRVSIGNEIIINPSLLLL 326
Cdd:PRK11831 97 TDMNVFDNVAYPLRehTQLPAPLLHSTVMMK----LEAVGLRGAAKLMPS-----ELSGGMARRAALARAIALEPDLIMF 167
|
170
....*....|.
gi 79597808 327 DEPTSGLDSTT 337
Cdd:PRK11831 168 DEPFVGQDPIT 178
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
178-393 |
1.61e-12 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 70.92 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 178 EILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYSKY----LKSKIGFVTQDDVLFPHlTV 253
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARS--GEILLNGFSLKDIdrhtLRQFINYLPQEPYIFSG-SI 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 254 KETLTYAARlrlPKTltREQKKQRALDV------IQELGLERCQDTMIGGAfvrGVSGGERKRVSIGNEIIINPSLLLLD 327
Cdd:TIGR01193 565 LENLLLGAK---ENV--SQDEIWAACEIaeikddIENMPLGYQTELSEEGS---SISGGQKQRIALARALLTDSKVLILD 636
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79597808 328 EPTSGLDSTTALRTILMLHDIAEagKTVITTIHQPSsrLFHRFDKLILLGRGSLLYFGKSSEALDY 393
Cdd:TIGR01193 637 ESTSNLDTITEKKIVNNLLNLQD--KTIIFVAHRLS--VAKQSDKIIVLDHGKIIEQGSHDELLDR 698
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
133-356 |
1.65e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 70.44 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 133 MIPEDIEAGKKKPKFQAEPTLpifLKFRDVTYKvvikkltSSVEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAG 212
Cdd:COG3845 237 MVGREVLLRVEKAPAEPGEVV---LEVENLSVR-------DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAG 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 213 RISQSStgGSVTYNDKPYS-----KYLKSKIGFVTQD---DVLFPHLTVKE--TLTYAARLRLPK--TLTREQKKQRALD 280
Cdd:COG3845 307 LRPPAS--GSIRLDGEDITglsprERRRLGVAYIPEDrlgRGLVPDMSVAEnlILGRYRRPPFSRggFLDRKAIRAFAEE 384
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79597808 281 VIQELGLeRCQDTmigGAFVRGVSGGERKRVSIGNEIIINPSLLLLDEPTSGLD--STTALRTILMlhDIAEAGKTVI 356
Cdd:COG3845 385 LIEEFDV-RTPGP---DTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDvgAIEFIHQRLL--ELRDAGAAVL 456
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
177-360 |
1.96e-12 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 67.21 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 177 KEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGrISQSSTGgSVTYNDKPYSK-------YLKSKIGFVTQDDVLFP 249
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICG-IERPSAG-KIWFSGHDITRlknrevpFLRRQIGMIFQDHHLLM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 250 HLTVKETLTyaarlrLPKTL---TREQKKQRALDVIQELGL-ERCQDtmiggaFVRGVSGGERKRVSIGNEIIINPSLLL 325
Cdd:PRK10908 93 DRTVYDNVA------IPLIIagaSGDDIRRRVSAALDKVGLlDKAKN------FPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190
....*....|....*....|....*....|....*
gi 79597808 326 LDEPTSGLDSTTALRTILMLHDIAEAGKTVITTIH 360
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATH 195
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
157-380 |
2.36e-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: 2.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 157 LKFRDVTY-----KVVIKKLTSSVEkeiltgisgsvnPGEVLALMGPSGSGKTTLLSLLAGrISQSSTGgsvtyndkpys 231
Cdd:cd03223 1 IELENLSLatpdgRVLLKDLSFEIK------------PGDRLLITGPSGTGKSSLFRALAG-LWPWGSG----------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 232 kylksKIGFVTQDDVLF-------PHLTVKETLTYAARLRLpktltreqkkqraldviqelglercqdtmiggafvrgvS 304
Cdd:cd03223 57 -----RIGMPEGEDLLFlpqrpylPLGTLREQLIYPWDDVL--------------------------------------S 93
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79597808 305 GGERKRVSIGNEIIINPSLLLLDEPTSGLDSTTALRtilMLHDIAEAGKTVITTIHQPSSRLFHRFdKLILLGRGS 380
Cdd:cd03223 94 GGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDR---LYQLLKELGITVISVGHRPSLWKFHDR-VLDLDGEGG 165
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
160-356 |
2.66e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 69.81 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 160 RDVTYKVV--IKKLTSSVEKEIlTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGriSQSSTGGSVTYNDK---PYSKY- 233
Cdd:PRK09700 258 SNLAHETVfeVRNVTSRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFG--VDKRAGGEIRLNGKdisPRSPLd 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 234 -LKSKIGFVTQ---DDVLFPHLTVKETLTYAARLRLPK-----TLTREQKKQRALDVIQELGLERCQDTmigGAFVRGVS 304
Cdd:PRK09700 335 aVKKGMAYITEsrrDNGFFPNFSIAQNMAISRSLKDGGykgamGLFHEVDEQRTAENQRELLALKCHSV---NQNITELS 411
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 79597808 305 GGERKRVSIGNEIIINPSLLLLDEPTSGLDSTTALRTILMLHDIAEAGKTVI 356
Cdd:PRK09700 412 GGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVIL 463
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
182-334 |
5.26e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 66.55 E-value: 5.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 182 GISGSVNPGEVLALMGPSGSGKTTLLSLLAGriSQSSTGGSVTYNDKP---YSKYLKSKIGFVT--QDDVLFPHLTVKET 256
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTG--FYKPTGGTILLRGQHiegLPGHQIARMGVVRtfQHVRLFREMTVIEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 257 LTYAARLRLP--------KTLTREQKKQRALDV----IQELGLERCQDTMIGgafvrGVSGGERKRVSIGNEIIINPSLL 324
Cdd:PRK11300 101 LLVAQHQQLKtglfsgllKTPAFRRAESEALDRaatwLERVGLLEHANRQAG-----NLAYGQQRRLEIARCMVTQPEIL 175
|
170
....*....|
gi 79597808 325 LLDEPTSGLD 334
Cdd:PRK11300 176 MLDEPAAGLN 185
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
187-358 |
6.78e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 65.64 E-value: 6.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 187 VNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYSKYLKSK-IGFVTQDDVLFPHLTVKETLTYAARL-- 263
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVES--GQIQIDGKTATRGDRSRfMAYLGHLPGLKADLSTLENLHFLCGLhg 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 264 RLPKtltreQKKQRALDVIqelGLERCQDTMiggafVRGVSGGERKRVSIGnEIIINPS-LLLLDEPTSGLD--STTALR 340
Cdd:PRK13543 112 RRAK-----QMPGSALAIV---GLAGYEDTL-----VRQLSAGQKKRLALA-RLWLSPApLWLLDEPYANLDleGITLVN 177
|
170
....*....|....*...
gi 79597808 341 TILMLHdIAEAGKTVITT 358
Cdd:PRK13543 178 RMISAH-LRGGGAALVTT 194
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
178-363 |
7.66e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 66.02 E-value: 7.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 178 EILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSSTG---------GSVTYNDKPYSKYLKSKIGFVTQDDVLF 248
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEArvegevrlfGRNIYSPDVDPIEVRREVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 249 PHLTVKETLtyAARLRLPKTLtreqKKQRALDVIQELGL------ERCQDTMigGAFVRGVSGGERKRVSIGNEIIINPS 322
Cdd:PRK14267 98 PHLTIYDNV--AIGVKLNGLV----KSKKELDERVEWALkkaalwDEVKDRL--NDYPSNLSGGQRQRLVIARALAMKPK 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 79597808 323 LLLLDEPTSGLDSTTALRTILMLHDIAEAGKTVITTiHQPS 363
Cdd:PRK14267 170 ILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVT-HSPA 209
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
158-335 |
9.60e-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: 68.27 E-value: 9.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 158 KFRDVTYKVVIKKLTSSVEKEILTGIS---------------GSVNPGEVLALMGPSGSGKTTLLSLLAGRIsqSSTGGS 222
Cdd:COG1245 319 RIRDEPIEFEVHAPRREKEEETLVEYPdltksyggfslevegGEIREGEVLGIVGPNGIGKTTFAKILAGVL--KPDEGE 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 223 VTYND----KPysKYLKSKIgfvtqddvlfpHLTVKETLTYAARLRLPKTLTREQkkqraldVIQELGLERCQDTMigga 298
Cdd:COG1245 397 VDEDLkisyKP--QYISPDY-----------DGTVEEFLRSANTDDFGSSYYKTE-------IIKPLGLEKLLDKN---- 452
|
170 180 190
....*....|....*....|....*....|....*..
gi 79597808 299 fVRGVSGGERKRVSIGNEIIINPSLLLLDEPTSGLDS 335
Cdd:COG1245 453 -VKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 488
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
186-359 |
1.24e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 66.67 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 186 SVNPGEVLALMGPSGSGKT----TLLSLLA--GRIsqsstGGSVTYN--------DKPYSKYLKSKIGFVTQDDV--LFP 249
Cdd:PRK09473 38 SLRAGETLGIVGESGSGKSqtafALMGLLAanGRI-----GGSATFNgreilnlpEKELNKLRAEQISMIFQDPMtsLNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 250 HLTVKETLTYAarLRLPKTLTREQ---KKQRALDVIQeLGLERCQDTMIGGAFvrgvSGGERKRVSIGNEIIINPSLLLL 326
Cdd:PRK09473 113 YMRVGEQLMEV--LMLHKGMSKAEafeESVRMLDAVK-MPEARKRMKMYPHEF----SGGMRQRVMIAMALLCRPKLLIA 185
|
170 180 190
....*....|....*....|....*....|...
gi 79597808 327 DEPTSGLDSTTALRTILMLHDIAEAGKTVITTI 359
Cdd:PRK09473 186 DEPTTALDVTVQAQIMTLLNELKREFNTAIIMI 218
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
180-411 |
1.34e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 65.78 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 180 LTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSSTGGSVTYNDK-PYSKY--LKSKIGFVTQD-DVLFPHLTVKE 255
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgDFSKLqgIRKLVGIVFQNpETQFVGRTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 256 TLTYAAR-LRLPKTLTReQKKQRALdviQELGLERCQDTMiggafVRGVSGGERKRVSIGNEIIINPSLLLLDEPTSGLD 334
Cdd:PRK13644 98 DLAFGPEnLCLPPIEIR-KRVDRAL---AEIGLEKYRHRS-----PKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 335 ---STTALRTILMLHdiaEAGKTVITTIHQPSSrlFHRFDKLILLGRGSLLYFGKSSEALDYFS--SIGCSPLIAMNPAE 409
Cdd:PRK13644 169 pdsGIAVLERIKKLH---EKGKTIVYITHNLEE--LHDADRIIVMDRGKIVLEGEPENVLSDVSlqTLGLTPPSLIELAE 243
|
..
gi 79597808 410 FL 411
Cdd:PRK13644 244 NL 245
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
176-423 |
1.51e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 66.41 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRIsQSSTG----GSVTYNDKPYS---------------KYLKS 236
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLI-KSKYGtiqvGDIYIGDKKNNhelitnpyskkiknfKELRR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 237 KIGFVTQddvlFPHL-----TVKETLTYA-ARLRLPKtltrEQKKQRALDVIQELGLErcQDTMIGGAFvrGVSGGERKR 310
Cdd:PRK13631 117 RVSMVFQ----FPEYqlfkdTIEKDIMFGpVALGVKK----SEAKKLAKFYLNKMGLD--DSYLERSPF--GLSGGQKRR 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 311 VSIGNEIIINPSLLLLDEPTSGLDSTTALRTILMLHDIAEAGKTVITTIHQPSSRLfHRFDKLILLGRGSLLYFGKSSE- 389
Cdd:PRK13631 185 VAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVL-EVADEVIVMDKGKILKTGTPYEi 263
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 79597808 390 ----ALDYFSSIGCSP-------LIAMNPA-EFLLDLANGNINDIS 423
Cdd:PRK13631 264 ftdqHIINSTSIQVPRviqvindLIKKDPKyKKLYQKQPRTIEQLA 309
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
551-745 |
2.18e-11 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 63.68 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 551 GLLFFIAVFWGFFpVFTAIFAFPQERAMLNKERAADMyRLSAYFLARTTSDLPLDFILPSLFLLVVYFMTGLRISPYPFF 630
Cdd:COG0842 8 GLLAMSLLFTALM-LTALSIAREREQGTLERLLVTPV-SRLEILLGKVLAYLLRGLLQALLVLLVALLFFGVPLRGLSLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 631 LSMLTVFLCIIAAQGLGLAIGAILMDLKKATTLASVTVMTFMLAGGFF--VKKVPVFISWIRYLSFNYHTYKLLLkvqyq 708
Cdd:COG0842 86 LLLLVLLLFALAFSGLGLLISTLARSQEQASAISNLVILPLTFLSGAFfpIESLPGWLQAIAYLNPLTYFVEALR----- 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 79597808 709 dfAVSINGMRIDNGLTEVAALVVMIFGYRLLAYLSLR 745
Cdd:COG0842 161 --ALFLGGAGLADVWPSLLVLLAFAVVLLALALRLFR 195
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
175-336 |
4.01e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 66.27 E-value: 4.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 175 VEKEILTGISGSVNPGEVLALMGPSGSGKT-TLLSLLagRISQSS-----------TGGSVTYNDKPYSKYLK-SKIGFV 241
Cdd:PRK15134 20 TVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSIL--RLLPSPpvvypsgdirfHGESLLHASEQTLRGVRgNKIAMI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 242 TQDDV--LFPHLTVKETLtyAARLRLPKTLTREQKKQRALDVIQELGLERCQDTMigGAFVRGVSGGERKRVSIGNEIII 319
Cdd:PRK15134 98 FQEPMvsLNPLHTLEKQL--YEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRL--TDYPHQLSGGERQRVMIAMALLT 173
|
170
....*....|....*..
gi 79597808 320 NPSLLLLDEPTSGLDST 336
Cdd:PRK15134 174 RPELLIADEPTTALDVS 190
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
179-391 |
6.12e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 63.69 E-value: 6.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 179 ILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSSTG------GSVTYNDKPYSKYLKSKIG-----FVTQDDVL 247
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPrgarvtGDVTLNGEPLAAIDAPRLArlravLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 248 FPhLTVKETLTYAarlRLPKTLTREQKKQRALDVIQElGLERCQDTMIGGAFVRGVSGGERKRVSIG---------NEII 318
Cdd:PRK13547 96 FA-FSAREIVLLG---RYPHARRAGALTHRDGEIAWQ-ALALAGATALVGRDVTTLSGGELARVQFArvlaqlwppHDAA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79597808 319 INPSLLLLDEPTSGLDSTTALRTILMLHDIA-EAGKTVITTIHQPSSRLFHRfDKLILLGRGSLLYFGKSSEAL 391
Cdd:PRK13547 171 QPPRYLLLDEPTAALDLAHQHRLLDTVRRLArDWNLGVLAIVHDPNLAARHA-DRIAMLADGAIVAHGAPADVL 243
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
166-394 |
6.95e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 63.18 E-value: 6.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 166 VVIKKLTSSVEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTyndkpyskyLKSKI------- 238
Cdd:COG1134 28 LLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS--GRVE---------VNGRVsallelg 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 239 -GFVtqddvlfPHLTVKETLTYAARLRlpkTLTREQKKQRALDVIQ--ELglercqdtmigGAF----VRGVSGGERKRV 311
Cdd:COG1134 97 aGFH-------PELTGRENIYLNGRLL---GLSRKEIDEKFDEIVEfaEL-----------GDFidqpVKTYSSGMRARL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 312 SIGNEIIINPSLLLLDEPTSGLDSTTALRTILMLHDIAEAGKTVITTIHQPSS--RLfhrFDKLILLGRGSLLYFGKSSE 389
Cdd:COG1134 156 AFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAvrRL---CDRAIWLEKGRLVMDGDPEE 232
|
....*
gi 79597808 390 ALDYF 394
Cdd:COG1134 233 VIAAY 237
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
176-431 |
2.64e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 62.12 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSSTGGS------VTYNDKPYSKyLKSKIGFVTQD-DVLF 248
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSkitvdgITLTAKTVWD-IREKVGIVFQNpDNQF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 249 PHLTVKETLTYAARLRlpkTLTREQKKQRALDVIQELGLERCQDtmiggAFVRGVSGGERKRVSIGNEIIINPSLLLLDE 328
Cdd:PRK13640 98 VGATVGDDVAFGLENR---AVPRPEMIKIVRDVLADVGMLDYID-----SEPANLSGGQKQRVAIAGILAVEPKIIILDE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 329 PTSGLDSTTALRTILMLHDIA-EAGKTVITTIHQPSSRlfHRFDKLILLGRGSLLyfgKSSEALDYFSSIGCSPLIAMNp 407
Cdd:PRK13640 170 STSMLDPAGKEQILKLIRKLKkKNNLTVISITHDIDEA--NMADQVLVLDDGKLL---AQGSPVEIFSKVEMLKEIGLD- 243
|
250 260
....*....|....*....|....*
gi 79597808 408 AEFLLDLANGNIN-DISVPSELDDR 431
Cdd:PRK13640 244 IPFVYKLKNKLKEkGISVPQEINTE 268
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
176-360 |
3.38e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 61.54 E-value: 3.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPY----SKYLKSKIGFVTQDDVLFPHL 251
Cdd:PRK10253 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAH--GHVWLDGEHIqhyaSKEVARRIGLLAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 252 TVKETLtyaARLRLPK----TLTREQKKQRALDVIQELGLercqdTMIGGAFVRGVSGGERKRVSIGNEIIINPSLLLLD 327
Cdd:PRK10253 97 TVQELV---ARGRYPHqplfTRWRKEDEEAVTKAMQATGI-----THLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
|
170 180 190
....*....|....*....|....*....|....
gi 79597808 328 EPTSGLDSTTALRTILMLHDI-AEAGKTVITTIH 360
Cdd:PRK10253 169 EPTTWLDISHQIDLLELLSELnREKGYTLAAVLH 202
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
180-333 |
3.48e-10 |
|
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: 62.92 E-value: 3.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 180 LTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSSTGGSVTYNDKPY-----SKYLKSKIGFVTQDDVLFPHLTVK 254
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYWSGSPLkasniRDTERAGIVIIHQELTLVPELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 255 ETLTYAARLRLPKTLTREQKK-QRALDVIQELGLERCQDTMIGGAFvrgvSGGERKRVSIGNEIIINPSLLLLDEPTSGL 333
Cdd:TIGR02633 97 ENIFLGNEITLPGGRMAYNAMyLRAKNLLRELQLDADNVTRPVGDY----GGGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
177-334 |
3.68e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.21 E-value: 3.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 177 KEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGrISQSSTGGSVtyndkPYSKYlksKIGFVTQDDVLFPHLTVKET 256
Cdd:PRK11819 20 KQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-VDKEFEGEAR-----PAPGI---KVGYLPQEPQLDPEKTVREN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 257 L------TYAARLRL---------P-----KTLTREQKKQralDVIQELG-------LE------RCQDtmiGGAFVRGV 303
Cdd:PRK11819 91 VeegvaeVKAALDRFneiyaayaePdadfdALAAEQGELQ---EIIDAADawdldsqLEiamdalRCPP---WDAKVTKL 164
|
170 180 190
....*....|....*....|....*....|.
gi 79597808 304 SGGERKRVSIGNEIIINPSLLLLDEPTSGLD 334
Cdd:PRK11819 165 SGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
176-360 |
4.52e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 61.29 E-value: 4.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStGGSVTYNDKPYSKY---LKSKIGFVTQD-DVLFPHL 251
Cdd:PRK13650 19 EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAES-GQIIIDGDLLTEENvwdIRHKIGMVFQNpDNQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 252 TVKETLTYAARlrlPKTLTREQKKQRALDVIQELGLERCQDTMIGGafvrgVSGGERKRVSIGNEIIINPSLLLLDEPTS 331
Cdd:PRK13650 98 TVEDDVAFGLE---NKGIPHEEMKERVNEALELVGMQDFKEREPAR-----LSGGQKQRVAIAGAVAMRPKIIILDEATS 169
|
170 180 190
....*....|....*....|....*....|
gi 79597808 332 GLDSTTALRTILMLHDIAEA-GKTVITTIH 360
Cdd:PRK13650 170 MLDPEGRLELIKTIKGIRDDyQMTVISITH 199
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
183-356 |
5.46e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 61.68 E-value: 5.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 183 ISGSVNPGEVLALMGPSGSGKTtlLSLLA--------GRISQSS---TGGSVT-YNDKPYSKYLKSKIGFVTQDDV--LF 248
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKS--VSSLAimglidypGRVMAEKlefNGQDLQrISEKERRNLVGAEVAMIFQDPMtsLN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 249 PHLTVKETLTYAarLRLPKTLTREQKKQRALDVIQELGLERCQDTMigGAFVRGVSGGERKRVSIGNEIIINPSLLLLDE 328
Cdd:PRK11022 104 PCYTVGFQIMEA--IKVHQGGNKKTRRQRAIDLLNQVGIPDPASRL--DVYPHQLSGGMSQRVMIAMAIACRPKLLIADE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 79597808 329 PTSGLDSTTALRTI---------------LMLHD---IAEAGKTVI 356
Cdd:PRK11022 180 PTTALDVTIQAQIIelllelqqkenmalvLITHDlalVAEAAHKII 225
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
173-379 |
7.87e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 62.69 E-value: 7.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 173 SSVEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSSTGGSVtyndkpyskyLKSKIGFVTQDDVLFpHLT 252
Cdd:PLN03232 626 SKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV----------IRGSVAYVPQVSWIF-NAT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 253 VKETLTYAARLrlpktltREQKKQRALDVI---QELGLERCQD-TMIGGafvRGV--SGGERKRVSIGNEIIINPSLLLL 326
Cdd:PLN03232 695 VRENILFGSDF-------ESERYWRAIDVTalqHDLDLLPGRDlTEIGE---RGVniSGGQKQRVSMARAVYSNSDIYIF 764
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 79597808 327 DEPTSGLDSTTALRTI--LMLHDIaeAGKTVITTIHQpsSRLFHRFDKLILLGRG 379
Cdd:PLN03232 765 DDPLSALDAHVAHQVFdsCMKDEL--KGKTRVLVTNQ--LHFLPLMDRIILVSEG 815
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
162-342 |
1.01e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 61.75 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 162 VTYKVVIKKLTS-SVEKEiltgiSGSVNPGEVLALMGPSGSGKTTLLSLLAGRIsqSSTGGSVT------YndKPysKYL 234
Cdd:PRK13409 341 VEYPDLTKKLGDfSLEVE-----GGEIYEGEVIGIVGPNGIGKTTFAKLLAGVL--KPDEGEVDpelkisY--KP--QYI 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 235 KSKigfvtqddvlfPHLTVKETLTyaarlRLPKTLTREQKKQralDVIQELGLERCQDTMiggafVRGVSGGERKRVSIG 314
Cdd:PRK13409 410 KPD-----------YDGTVEDLLR-----SITDDLGSSYYKS---EIIKPLQLERLLDKN-----VKDLSGGELQRVAIA 465
|
170 180 190
....*....|....*....|....*....|.
gi 79597808 315 NEIIINPSLLLLDEPTSGLDS---TTALRTI 342
Cdd:PRK13409 466 ACLSRDADLYLLDEPSAHLDVeqrLAVAKAI 496
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
166-343 |
1.09e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 61.45 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 166 VVIKKLTSSVEKEIL-TGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDkpyskylKSKIGFVTQD 244
Cdd:PRK15064 320 LEVENLTKGFDNGPLfKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDS--GTVKWSE-------NANIGYYAQD 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 245 dvlfphltvketltYAARLRLPKTLTreqkkqralDVIQELGLERCQDTMIGGAF-------------VRGVSGGERKRV 311
Cdd:PRK15064 391 --------------HAYDFENDLTLF---------DWMSQWRQEGDDEQAVRGTLgrllfsqddikksVKVLSGGEKGRM 447
|
170 180 190
....*....|....*....|....*....|....
gi 79597808 312 SIGNEIIINPSLLLLDEPTSGLD--STTALRTIL 343
Cdd:PRK15064 448 LFGKLMMQKPNVLVMDEPTNHMDmeSIESLNMAL 481
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
180-360 |
1.17e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.48 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 180 LTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSSTGGSVTYNDKPyskyLKSK---------IGFVTQDDVLFPH 250
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTYEGEIIFEGEE----LQASnirdteragIAIIHQELALVKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 251 LTVKET------LTYAARLRLPKTLTREQKkqraldVIQELGLERCQDTMiggafVRGVSGGERKRVSIGNEIIINPSLL 324
Cdd:PRK13549 97 LSVLENiflgneITPGGIMDYDAMYLRAQK------LLAQLKLDINPATP-----VGNLGLGQQQLVEIAKALNKQARLL 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 79597808 325 LLDEPTSGLdsTTALRTILM--LHDIAEAGKTVITTIH 360
Cdd:PRK13549 166 ILDEPTASL--TESETAVLLdiIRDLKAHGIACIYISH 201
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
168-360 |
1.20e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 60.11 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 168 IKKLTSSVEKEI----LTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYSKY----LKSKIG 239
Cdd:PRK13642 7 VENLVFKYEKESdvnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFE--GKVKIDGELLTAEnvwnLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 240 FVTQD-DVLFPHLTVKETLTYAARlrlPKTLTREQKKQR---ALDVIQELGLERCQDTMIggafvrgvSGGERKRVSIGN 315
Cdd:PRK13642 85 MVFQNpDNQFVGATVEDDVAFGME---NQGIPREEMIKRvdeALLAVNMLDFKTREPARL--------SGGQKQRVAVAG 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 79597808 316 EIIINPSLLLLDEPTSGLDSTTALRTILMLHDIAEAGK-TVITTIH 360
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQlTVLSITH 199
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
178-391 |
1.56e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 59.42 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 178 EILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRIsqSSTGGSVTYNDKPYS----KYLKSKIGFVTQD--DVLFPHL 251
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMI--EPTSGELLIDDHPLHfgdySYRSQRIRMIFQDpsTSLNPRQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 252 TVKETLTYAarLRLPKTLTREQKKQRALDVIQELGLERCQdtmiGGAFVRGVSGGERKRVSIGNEIIINPSLLLLDEPTS 331
Cdd:PRK15112 105 RISQILDFP--LRLNTDLEPEQREKQIIETLRQVGLLPDH----ASYYPHMLAPGQKQRLGLARALILRPKVIIADEALA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79597808 332 GLDSTTALRTI-LMLHDIAEAGKTVItTIHQPSSRLFHRFDKLILLGRGSLLYFGKSSEAL 391
Cdd:PRK15112 179 SLDMSMRSQLInLMLELQEKQGISYI-YVTQHLGMMKHISDQVLVMHQGEVVERGSTADVL 238
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
177-389 |
2.01e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 58.89 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 177 KEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLaGRISQSSTGGSVT-----YNDKPYSKY-----LKSKIGFVTQDDV 246
Cdd:PRK14258 20 QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEgrvefFNQNIYERRvnlnrLRRQVSMVHPKPN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 247 LFPhLTVKETLTYAARL--RLPKTltreqkkqrALDVIQELGL------ERCQDTMIGGAFvrGVSGGERKRVSIGNEII 318
Cdd:PRK14258 99 LFP-MSVYDNVAYGVKIvgWRPKL---------EIDDIVESALkdadlwDEIKHKIHKSAL--DLSGGQQQRLCIARALA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 319 INPSLLLLDEPTSGLDSTTALRTILMLHDI---AEAGKTVIT-TIHQPS-----SRLFHRFDKLIllgrGSLLYFGKSSE 389
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASMKVESLIQSLrlrSELTMVIVShNLHQVSrlsdfTAFFKGNENRI----GQLVEFGLTKK 242
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
121-337 |
2.08e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.20 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 121 EISDSKPfsddemIPEDIEAGKKKPKFQAeptlpifLKFRDVTYKVVIKKltssvEKEILTGISGSVNPGEVLALMGPSG 200
Cdd:PTZ00265 360 EIINRKP------LVENNDDGKKLKDIKK-------IQFKNVRFHYDTRK-----DVEIYKDLNFTLTEGKTYAFVGESG 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 201 SGKTTLLSLLAgRIsQSSTGGSVTYND----KPYS-KYLKSKIGFVTQDDVLFPHlTVKETLTYA--------------- 260
Cdd:PTZ00265 422 CGKSTILKLIE-RL-YDPTEGDIIINDshnlKDINlKWWRSKIGVVSQDPLLFSN-SIKNNIKYSlyslkdlealsnyyn 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 261 ---------------ARLR-------LPKTLTREQ-----------KKQRALDVIQEL-------GLERCQDTMIGGAFV 300
Cdd:PTZ00265 499 edgndsqenknkrnsCRAKcagdlndMSNTTDSNEliemrknyqtiKDSEVVDVSKKVlihdfvsALPDKYETLVGSNAS 578
|
250 260 270
....*....|....*....|....*....|....*..
gi 79597808 301 RgVSGGERKRVSIGNEIIINPSLLLLDEPTSGLDSTT 337
Cdd:PTZ00265 579 K-LSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
139-348 |
2.22e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 60.64 E-value: 2.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 139 EAGKKKPKFQAE---PTLPIfLKFRDVTYKVVIKK-LTSSVEKEI--LTGISGSVNPGEVLALMGPSGSGKTT----LLS 208
Cdd:PRK10261 294 HPAKQEPPIEQDtvvDGEPI-LQVRNLVTRFPLRSgLLNRVTREVhaVEKVSFDLWPGETLSLVGESGSGKSTtgraLLR 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 209 LLagrisqSSTGGSVTYNDK-----PYSKY--LKSKIGFVTQDDvlFPHLTVKETLTYAAR--LRLPKTLTREQKKQRAL 279
Cdd:PRK10261 373 LV------ESQGGEIIFNGQridtlSPGKLqaLRRDIQFIFQDP--YASLDPRQTVGDSIMepLRVHGLLPGKAAAARVA 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79597808 280 DVIQELGLERCQDTMIGGAFvrgvSGGERKRVSIGNEIIINPSLLLLDEPTSGLDSTTALRTILMLHDI 348
Cdd:PRK10261 445 WLLERVGLLPEHAWRYPHEF----SGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDL 509
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
232-376 |
2.87e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 60.81 E-value: 2.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 232 KYLKSKIGFVTQDDVLFpHLTVKETLTYAArlrlpKTLTREQKKQ----RALDVIQElGLERCQDTMIGgAFVRGVSGGE 307
Cdd:PTZ00265 1292 KDLRNLFSIVSQEPMLF-NMSIYENIKFGK-----EDATREDVKRackfAAIDEFIE-SLPNKYDTNVG-PYGKSLSGGQ 1363
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79597808 308 RKRVSIGNEIIINPSLLLLDEPTSGLDSTTAL---RTILMLHDiaEAGKTVITTIHQPSSrlFHRFDKLILL 376
Cdd:PTZ00265 1364 KQRIAIARALLREPKILLLDEATSSLDSNSEKlieKTIVDIKD--KADKTIITIAHRIAS--IKRSDKIVVF 1431
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
157-392 |
5.25e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 57.84 E-value: 5.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 157 LKFRDVTYKVvikkltSSVEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGrISQSSTGgSVTYNDKPYS----K 232
Cdd:PRK13648 8 IVFKNVSFQY------QSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIG-IEKVKSG-EIFYNNQAITddnfE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 233 YLKSKIGFVTQD-DVLFPHLTVKetltYAARLRLPKTLTREQKKQRAL-DVIQELG-LERCQDTmiggafVRGVSGGERK 309
Cdd:PRK13648 80 KLRKHIGIVFQNpDNQFVGSIVK----YDVAFGLENHAVPYDEMHRRVsEALKQVDmLERADYE------PNALSGGQKQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 310 RVSIGNEIIINPSLLLLDEPTSGLDSTTALRTILMLHDI-AEAGKTVITTIHQPSSRLfhRFDKLILLGRGSLLYFGKSS 388
Cdd:PRK13648 150 RVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVkSEHNITIISITHDLSEAM--EADHVIVMNKGTVYKEGTPT 227
|
....
gi 79597808 389 EALD 392
Cdd:PRK13648 228 EIFD 231
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
182-360 |
5.91e-09 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 58.56 E-value: 5.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 182 GISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISqsSTGGSVTY--------NDKPYsKYLKSKIGFVTQDDV--LFPHL 251
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVK--ATDGEVAWlgkdllgmKDDEW-RAVRSDIQMIFQDPLasLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 252 TVKETLTYAARLRLPKtLTREQKKQRALDVIQELGLercQDTMIGgAFVRGVSGGERKRVSIGNEIIINPSLLLLDEPTS 331
Cdd:PRK15079 116 TIGEIIAEPLRTYHPK-LSRQEVKDRVKAMMLKVGL---LPNLIN-RYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170 180 190
....*....|....*....|....*....|
gi 79597808 332 GLDSTTALRTILMLHDI-AEAGKTVITTIH 360
Cdd:PRK15079 191 ALDVSIQAQVVNLLQQLqREMGLSLIFIAH 220
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
179-389 |
7.44e-09 |
|
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: 57.56 E-value: 7.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 179 ILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNdkpyskylkSKIGFVTQDDVLFPHlTVKETLT 258
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSE--GKIKHS---------GRISFSSQFSWIMPG-TIKENII 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 259 YAarlrlpktLTREQkkQRALDVIQELGLERC------QDTMIGGAFVRGVSGGERKRVSIGNEIIINPSLLLLDEPTSG 332
Cdd:cd03291 120 FG--------VSYDE--YRYKSVVKACQLEEDitkfpeKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGY 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79597808 333 LDSTTALRTI------LMlhdiaeAGKTVITTihqpSSRLFH--RFDKLILLGRGSLLYFGKSSE 389
Cdd:cd03291 190 LDVFTEKEIFescvckLM------ANKTRILV----TSKMEHlkKADKILILHEGSSYFYGTFSE 244
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
176-342 |
7.48e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 58.96 E-value: 7.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYSKY----LKSKIGFVTQDDVLFphl 251
Cdd:PRK10790 353 DNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTE--GEIRLDGRPLSSLshsvLRQGVAMVQQDPVVL--- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 252 tvketltyAARLRLPKTLTR---EQKKQRALDVIQELGLERcqdTMIGGAFVR------GVSGGERKRVSIGNEIIINPS 322
Cdd:PRK10790 428 --------ADTFLANVTLGRdisEEQVWQALETVQLAELAR---SLPDGLYTPlgeqgnNLSVGQKQLLALARVLVQTPQ 496
|
170 180
....*....|....*....|....*.
gi 79597808 323 LLLLDEPTSGLDSTT------ALRTI 342
Cdd:PRK10790 497 ILILDEATANIDSGTeqaiqqALAAV 522
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
176-360 |
9.66e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 57.06 E-value: 9.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYS--------KYLKSKIGFVTQ--DD 245
Cdd:PRK13649 19 EGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQ--GSVRVDDTLITstsknkdiKQIRKKVGLVFQfpES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 246 VLFPHlTVKETLTYAarlrlPKT--LTREQKKQRALDVIQELGLErcQDTMIGGAFvrGVSGGERKRVSIGNEIIINPSL 323
Cdd:PRK13649 97 QLFEE-TVLKDVAFG-----PQNfgVSQEEAEALAREKLALVGIS--ESLFEKNPF--ELSGGQMRRVAIAGILAMEPKI 166
|
170 180 190
....*....|....*....|....*....|....*..
gi 79597808 324 LLLDEPTSGLDSTTALRTILMLHDIAEAGKTVITTIH 360
Cdd:PRK13649 167 LVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTH 203
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
179-389 |
1.20e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 58.77 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 179 ILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNdkpyskylkSKIGFVTQDDVLFPHlTVKETLT 258
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSE--GKIKHS---------GRISFSPQTSWIMPG-TIKDNII 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 259 YAarlrLPKTLTREQKKQRALDVIQELGLERCQDTMIGGAFVRGVSGGERKRVSIGNEIIINPSLLLLDEPTSGLDSTTA 338
Cdd:TIGR01271 509 FG----LSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTE 584
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 339 lrtilmlHDIAE-------AGKTVITTihqpSSRLFH--RFDKLILLGRGSLLYFGKSSE 389
Cdd:TIGR01271 585 -------KEIFEsclcklmSNKTRILV----TSKLEHlkKADKILLLHEGVCYFYGTFSE 633
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
182-334 |
1.40e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.09 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 182 GISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISqsSTGGSVTYNDKPYSKY-----LKSKIGFVTQD---DVLFPHLTV 253
Cdd:PRK10762 270 DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALP--RTSGYVTLDGHEVVTRspqdgLANGIVYISEDrkrDGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 254 KETLTYAARLRLPKT---LTREQKKQRALDVIQELGLER-CQDTMIGGafvrgVSGGERKRVSIGNEIIINPSLLLLDEP 329
Cdd:PRK10762 348 KENMSLTALRYFSRAggsLKHADEQQAVSDFIRLFNIKTpSMEQAIGL-----LSGGNQQKVAIARGLMTRPKVLILDEP 422
|
....*
gi 79597808 330 TSGLD 334
Cdd:PRK10762 423 TRGVD 427
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
173-335 |
1.48e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.60 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 173 SSVEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSSTGGSVtyndkpyskyLKSKIGFVTQDDVLFpHLT 252
Cdd:PLN03130 626 SKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV----------IRGTVAYVPQVSWIF-NAT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 253 VKETLTYAARLRLPKTltreqkkQRALDVIqelGLERCQDTMIGGAFV----RGV--SGGERKRVSIGNEIIINPSLLLL 326
Cdd:PLN03130 695 VRDNILFGSPFDPERY-------ERAIDVT---ALQHDLDLLPGGDLTeigeRGVniSGGQKQRVSMARAVYSNSDVYIF 764
|
....*....
gi 79597808 327 DEPTSGLDS 335
Cdd:PLN03130 765 DDPLSALDA 773
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
180-442 |
1.50e-08 |
|
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: 58.42 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 180 LTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTyndkpyskyLKSKIGFVTQDdVLFPHLTVKETLTY 259
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVE--GHVH---------MKGSVAYVPQQ-AWIQNDSLRENILF 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 260 AARLRLPktltREQKKQRALDVIQELGLERCQD-TMIGGAFVRgVSGGERKRVSIGNEIIINPSLLLLDEPTSGLDSTTA 338
Cdd:TIGR00957 722 GKALNEK----YYQQVLEACALLPDLEILPSGDrTEIGEKGVN-LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVG 796
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 339 LRtiLMLHDIAE----AGKTVITTIHQPSsrLFHRFDKLILLGRGSLLYFGKSSEALDYFSSIgcspliamnpAEFLLDL 414
Cdd:TIGR00957 797 KH--IFEHVIGPegvlKNKTRILVTHGIS--YLPQVDVIIVMSGGKISEMGSYQELLQRDGAF----------AEFLRTY 862
|
250 260
....*....|....*....|....*...
gi 79597808 415 ANgniNDISVPSELDDRVQVGNSGRETQ 442
Cdd:TIGR00957 863 AP---DEQQGHLEDSWTALVSGEGKEAK 887
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
552-742 |
1.51e-08 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.
Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 57.40 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 552 LLFFIAVFWGFFPVFTAIFAFPQERAMLNKERAADM-YRLSAYFLARTTSDLPLdFILPSLFLLVVYFmtGLRISPYPFF 630
Cdd:pfam12698 163 LVGLILMIIILIGAAIIAVSIVEEKESRIKERLLVSgVSPLQYWLGKILGDFLV-GLLQLLIILLLLF--GIGIPFGNLG 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 631 LSMLTVFLCIIAAQGLGLAIGAILmdlkKATTLASVTVMTFML------AGGFFVKKVPVFISWIRYLSFNYHTYKLLLK 704
Cdd:pfam12698 240 LLLLLFLLYGLAYIALGYLLGSLF----KNSEDAQSIIGIVILllsgffGGLFPLEDPPSFLQWIFSIIPFFSPIDGLLR 315
|
170 180 190
....*....|....*....|....*....|....*...
gi 79597808 705 VQYQDFAVSIngmridngLTEVAALVVMIFGYRLLAYL 742
Cdd:pfam12698 316 LIYGDSLWEI--------APSLIILLLFAVVLLLLALL 345
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
178-385 |
2.66e-08 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 54.73 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 178 EILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAgRISQSSTgGSVTYNDKPYSKY----LKSKIGFVTQDDVLFPHlTV 253
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALF-RFLEAEE-GKIEIDGIDISTIpledLRSSLTIIPQDPTLFSG-TI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 254 KETLTyaarlrlPKTLTREQKKQRALDViQELGLErcqdtmiggafvrgVSGGERKRVSIGNEIIINPSLLLLDEPTSGL 333
Cdd:cd03369 99 RSNLD-------PFDEYSDEEIYGALRV-SEGGLN--------------LSQGQRQLLCLARALLKRPRVLVLDEATASI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 79597808 334 DSTT-AL--RTILMLHdiaeAGKTVITTIHQPSSRLfhRFDKLILLGRGSLLYFG 385
Cdd:cd03369 157 DYATdALiqKTIREEF----TNSTILTIAHRLRTII--DYDKILVMDAGEVKEYD 205
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
180-338 |
3.48e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.55 E-value: 3.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 180 LTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGrISQSSTgGSVTYNDKPYS-KYLKSK----IGFVTQDDVLFPHLTVK 254
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTG-IYTRDA-GSILYLGKEVTfNGPKSSqeagIGIIHQELNLIPQLTIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 255 ETLtyaarlrlpkTLTREQKK-----------QRALDVIQELGLERCQDTMIGgafvrGVSGGERKRVSIGNEIIINPSL 323
Cdd:PRK10762 98 ENI----------FLGREFVNrfgridwkkmyAEADKLLARLNLRFSSDKLVG-----ELSIGEQQMVEIAKVLSFESKV 162
|
170
....*....|....*.
gi 79597808 324 LLLDEPTSGL-DSTTA 338
Cdd:PRK10762 163 IIMDEPTDALtDTETE 178
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
176-334 |
4.51e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 56.72 E-value: 4.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStggsvtyNDKPYSKYLksKIGFVTQDDVLFphLTVKE 255
Cdd:PRK10636 324 DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVS-------GEIGLAKGI--KLGYFAQHQLEF--LRADE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 256 T-LTYAARLRlPKTLtreqkKQRALDVIQELGLERCQDTMIGGAFvrgvSGGERKRVSIGNEIIINPSLLLLDEPTSGLD 334
Cdd:PRK10636 393 SpLQHLARLA-PQEL-----EQKLRDYLGGFGFQGDKVTEETRRF----SGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
179-334 |
5.13e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 56.33 E-value: 5.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 179 ILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRIsqSSTGGSVTYndkPYSKYLkskiGFVTQDDvlfPHLTV----- 253
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEI--SADGGSYTF---PGNWQL----AWVNQET---PALPQpaley 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 254 -----KETLTYAARLRlpktLTREQKKQRA-------LDVIQELGLE-RCQDTMIGGAF--------VRGVSGGERKRVS 312
Cdd:PRK10636 84 vidgdREYRQLEAQLH----DANERNDGHAiatihgkLDAIDAWTIRsRAASLLHGLGFsneqlerpVSDFSGGWRMRLN 159
|
170 180
....*....|....*....|..
gi 79597808 313 IGNEIIINPSLLLLDEPTSGLD 334
Cdd:PRK10636 160 LAQALICRSDLLLLDEPTNHLD 181
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
183-381 |
5.51e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 55.99 E-value: 5.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 183 ISGSVNPGEVLALMGPSGSGKTTLLSLLAGrISQSSTGGSVTYNDKPYS-----KYLKSKIGFVTQD---DVLFPHLTVK 254
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFG-AYPGKFEGNVFINGKPVDirnpaQAIRAGIAMVPEDrkrHGIVPILGVG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 255 ETLTYAARLRLP-KTLTREQKKQRALDV-IQELGLERCQ-DTMIGGafvrgVSGGERKRVSIGNEIIINPSLLLLDEPTS 331
Cdd:TIGR02633 358 KNITLSVLKSFCfKMRIDAAAELQIIGSaIQRLKVKTASpFLPIGR-----LSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 79597808 332 GLDSTTALRTILMLHDIAEAGKTVITTihqpSSRLFHRF---DKLILLGRGSL 381
Cdd:TIGR02633 433 GVDVGAKYEIYKLINQLAQEGVAIIVV----SSELAEVLglsDRVLVIGEGKL 481
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
176-422 |
8.21e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 54.63 E-value: 8.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISqSSTGGSVTYNDK-PYS-------KYLKSKIGFVTQddvl 247
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLII-SETGQTIVGDYAiPANlkkikevKRLRKEIGLVFQ---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 248 FPHL-----TVKETLTYAarlrlPKTLTreQKKQRALDVIQELgLERCQ---DTMIGGAFvrGVSGGERKRVSIGNEIII 319
Cdd:PRK13645 98 FPEYqlfqeTIEKDIAFG-----PVNLG--ENKQEAYKKVPEL-LKLVQlpeDYVKRSPF--ELSGGQKRRVALAGIIAM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 320 NPSLLLLDEPTSGLDSTTALRTI-LMLHDIAEAGKTVITTIHQpSSRLFHRFDKLILLGRGSLLYFGKSSEAldyFSSIG 398
Cdd:PRK13645 168 DGNTLVLDEPTGGLDPKGEEDFInLFERLNKEYKKRIIMVTHN-MDQVLRIADEVIVMHEGKVISIGSPFEI---FSNQE 243
|
250 260 270
....*....|....*....|....*....|....
gi 79597808 399 CSPLIAMNPAEFL----------LDLANGNINDI 422
Cdd:PRK13645 244 LLTKIEIDPPKLYqlmyklknkgIDLLNKNIRTI 277
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
175-389 |
9.13e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.94 E-value: 9.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 175 VEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVtyndkpyskYLKSKIGFVTQ----------D 244
Cdd:PTZ00243 671 EPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISE--GRV---------WAERSIAYVPQqawimnatvrG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 245 DVLFPHLTVKETLTYAARLrlpktltreqkKQRALDVIQ-ELGLErcqdTMIGGAFVrGVSGGERKRVSIGNEIIINPSL 323
Cdd:PTZ00243 740 NILFFDEEDAARLADAVRV-----------SQLEADLAQlGGGLE----TEIGEKGV-NLSGGQKARVSLARAVYANRDV 803
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79597808 324 LLLDEPTSGLDSTTALRTILMLHDIAEAGKTVITTIHQpsSRLFHRFDKLILLGRGSLLYFGKSSE 389
Cdd:PTZ00243 804 YLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQ--VHVVPRADYVVALGDGRVEFSGSSAD 867
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
186-360 |
1.07e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 53.91 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 186 SVNPGEVLALMGPSGSGKTTLLSLLAGRIsQSSTGgsvTYNDKPyskylkskigfvTQDDVLfPHLTVKETLTYAARLR- 264
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAGKL-KPNLG---KFDDPP------------DWDEIL-DEFRGSELQNYFTKLLe 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 265 --------------LPKT--------LTREQKKQRALDVIQELGLERCQDTMIggafvRGVSGGERKRVSIGNEIIINPS 322
Cdd:cd03236 85 gdvkvivkpqyvdlIPKAvkgkvgelLKKKDERGKLDELVDQLELRHVLDRNI-----DQLSGGELQRVAIAAALARDAD 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 79597808 323 LLLLDEPTSGLDSTTALRTILMLHDIAEAGKTVITTIH 360
Cdd:cd03236 160 FYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEH 197
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
148-334 |
1.17e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.02 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 148 QAEPTLP-----IFLKFRDVTYKvvikkltssvEKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGrisqsstggs 222
Cdd:PRK10938 249 SARHALPaneprIVLNNGVVSYN----------DRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG---------- 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 223 vtynDKP--YSKYL----------------KSKIGFVTQDdvlfPHL------TVKETL---------TYAA---RLRlp 266
Cdd:PRK10938 309 ----DHPqgYSNDLtlfgrrrgsgetiwdiKKHIGYVSSS----LHLdyrvstSVRNVIlsgffdsigIYQAvsdRQQ-- 378
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79597808 267 ktltreQKKQRALDViqeLGLercqDTMIGGAFVRGVSGGERKRVSIGNEIIINPSLLLLDEPTSGLD 334
Cdd:PRK10938 379 ------KLAQQWLDI---LGI----DKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
180-334 |
1.18e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.52 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 180 LTGISGSVNPGEVLALMGPSGSGKTTLLSLLAG-RISQSST----GGSVTynDKPYSKYLKSKIGFVTQ--DDVLFPHLT 252
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGaRKIQQGRvevlGGDMA--DARHRRAVCPRIAYMPQglGKNLYPTLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 253 VKETLTYAARLRlpkTLTREQKKQRaldvIQEL----GLERCQDTMIGgafvrGVSGGERKRVSIGNEIIINPSLLLLDE 328
Cdd:NF033858 95 VFENLDFFGRLF---GQDAAERRRR----IDELlratGLAPFADRPAG-----KLSGGMKQKLGLCCALIHDPDLLILDE 162
|
....*.
gi 79597808 329 PTSGLD 334
Cdd:NF033858 163 PTTGVD 168
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
176-337 |
1.60e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.96 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSV---TyndkpyskylKSKIGFVTQddvlfphlt 252
Cdd:PRK11147 331 GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADS--GRIhcgT----------KLEVAYFDQ--------- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 253 vketltYAARLRLPKTltreqkkqraldVIQELGlERCQDTMIGGA----------F----------VRGVSGGERKRVS 312
Cdd:PRK11147 390 ------HRAELDPEKT------------VMDNLA-EGKQEVMVNGRprhvlgylqdFlfhpkramtpVKALSGGERNRLL 450
|
170 180
....*....|....*....|....*.
gi 79597808 313 IGnEIIINPS-LLLLDEPTSGLDSTT 337
Cdd:PRK11147 451 LA-RLFLKPSnLLILDEPTNDLDVET 475
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
158-361 |
2.43e-07 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 53.27 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 158 KFRDV--TYKVVIKKLTSsvekeiLTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRisQSSTGGSVTYNDKPYSKY-- 233
Cdd:PRK11153 3 ELKNIskVFPQGGRTIHA------LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLL--ERPTSGRVLVDGQDLTALse 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 234 -----LKSKIGFVTQ-----------DDVLFPhltvketltyaarLRLPKTlTREQKKQRALDVIQELGLERCQDtmigg 297
Cdd:PRK11153 75 kelrkARRQIGMIFQhfnllssrtvfDNVALP-------------LELAGT-PKAEIKARVTELLELVGLSDKAD----- 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 79597808 298 AFVRGVSGGERKRVSIGNEIIINPSLLLLDEPTSGLD-STTalRTIL-MLHDI-AEAGKTVITTIHQ 361
Cdd:PRK11153 136 RYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDpATT--RSILeLLKDInRELGLTIVLITHE 200
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
189-379 |
2.73e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 50.45 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 189 PGEVLALMGPSGSGKTTLLSLLAGrisqsstggsvtyndkpysKYLKSKIGFVTQDDvlfphltvkETLTYAARLRLPKT 268
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALAR-------------------ELGPPGGGVIYIDG---------EDILEEVLDQLLLI 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 269 LTREQKKQRALDVIQELGLERCQDTmiggafvrgvsggerkrvsigneiiiNPSLLLLDEPTSGLDSTT------ALRTI 342
Cdd:smart00382 53 IVGGKKASGSGELRLRLALALARKL--------------------------KPDVLILDEITSLLDAEQeallllLEELR 106
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 79597808 343 LMLHDIAEAGKTVITTIHQP----SSRLFHRFDKLILLGRG 379
Cdd:smart00382 107 LLLLLKSEKNLTVILTTNDEkdlgPALLRRRFDRRIVLLLI 147
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
183-357 |
4.91e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 53.32 E-value: 4.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 183 ISGSVNPGEVLALMGPSGSGKT-TLLSLLagRISQSStGGSV------------------TYNDKPYSKYLKSKIGFVTQ 243
Cdd:PRK10261 35 LSFSLQRGETLAIVGESGSGKSvTALALM--RLLEQA-GGLVqcdkmllrrrsrqvielsEQSAAQMRHVRGADMAMIFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 244 DDV--LFPHLTVKETLtyAARLRLPKTLTREQKKQRALDVIQELGLERCQdtMIGGAFVRGVSGGERKRVSIGNEIIINP 321
Cdd:PRK10261 112 EPMtsLNPVFTVGEQI--AESIRLHQGASREEAMVEAKRMLDQVRIPEAQ--TILSRYPHQLSGGMRQRVMIAMALSCRP 187
|
170 180 190
....*....|....*....|....*....|....*....
gi 79597808 322 SLLLLDEPTSGLDSTTA---LRTILMLHDIAEAGKTVIT 357
Cdd:PRK10261 188 AVLIADEPTTALDVTIQaqiLQLIKVLQKEMSMGVIFIT 226
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
176-361 |
6.22e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 50.72 E-value: 6.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 176 EKEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYN----DKPYSKYLKsKIGFVTQDDVLFPHL 251
Cdd:PRK13540 13 DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEK--GEILFErqsiKKDLCTYQK-QLCFVGHRSGINPYL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 252 TVKETLTYaarlrlpkTLTREQKKQRALDVIQELGLERCQDTMIGgafvrGVSGGERKRVSIGNEIIINPSLLLLDEPTS 331
Cdd:PRK13540 90 TLRENCLY--------DIHFSPGAVGITELCRLFSLEHLIDYPCG-----LLSSGQKRQVALLRLWMSKAKLWLLDEPLV 156
|
170 180 190
....*....|....*....|....*....|
gi 79597808 332 GLDSTTALRTILMLHDIAEAGKTVITTIHQ 361
Cdd:PRK13540 157 ALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
269-389 |
6.24e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 52.04 E-value: 6.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 269 LTREQKKQRALDViqelgLERCQDTMIGGAFVRGVSGGERKRVSIGNEIIINPSLLLLDEPTSGLDSTTALRTILMLHDI 348
Cdd:NF000106 116 LSRKDARARADEL-----LERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSM 190
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 79597808 349 AEAGKTVITTIH--QPSSRLFHrfdKLILLGRGSLLYFGKSSE 389
Cdd:NF000106 191 VRDGATVLLTTQymEEAEQLAH---ELTVIDRGRVIADGKVDE 230
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
189-360 |
6.55e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.89 E-value: 6.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 189 PGEVLALMGPSGSGKTTLLSLLAGRIsQSSTGGsvtYNDKPyskylkskigfvTQDDVLfPHLTVKETLTYAARLR---- 264
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGEL-IPNLGD---YEEEP------------SWDEVL-KRFRGTELQNYFKKLYngei 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 265 -----------LPKT--------LTREQKKQRALDVIQELGLERCQDTMIggafvRGVSGGERKRVSIGNEIIINPSLLL 325
Cdd:PRK13409 161 kvvhkpqyvdlIPKVfkgkvrelLKKVDERGKLDEVVERLGLENILDRDI-----SELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190
....*....|....*....|....*....|....*
gi 79597808 326 LDEPTSGLDSTTALRTILMLHDIAEaGKTVITTIH 360
Cdd:PRK13409 236 FDEPTSYLDIRQRLNVARLIRELAE-GKYVLVVEH 269
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
189-360 |
7.27e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 52.48 E-value: 7.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 189 PGEVLALMGPSGSGKTTLLSLLAGRIsQSSTGGsvtYNDKPyskylkskigfvTQDDVLfPHLTVKETLTYAARLR---- 264
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGEL-KPNLGD---YDEEP------------SWDEVL-KRFRGTELQDYFKKLAngei 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 265 -----------LPKT--------LTREQKKQRALDVIQELGLERCQDTMIggafvRGVSGGERKRVSIGNEIIINPSLLL 325
Cdd:COG1245 161 kvahkpqyvdlIPKVfkgtvrelLEKVDERGKLDELAEKLGLENILDRDI-----SELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190
....*....|....*....|....*....|....*
gi 79597808 326 LDEPTSGLDSTTALRTILMLHDIAEAGKTVITTIH 360
Cdd:COG1245 236 FDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEH 270
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
190-334 |
1.02e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 52.43 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 190 GEVLALMGPSGSGKTTLLSLLAGRISQSST-----GGSVTYNDKPyskyLKSKIGFVTQDDVLFPHLTVKETLTYAARL- 263
Cdd:NF033858 292 GEIFGFLGSNGCGKSTTMKMLTGLLPASEGeawlfGQPVDAGDIA----TRRRVGYMSQAFSLYGELTVRQNLELHARLf 367
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79597808 264 RLPKtltrEQKKQRALDVIQELGLERCQDTMIGGafvrgVSGGERKRVSIGNEIIINPSLLLLDEPTSGLD 334
Cdd:NF033858 368 HLPA----AEIAARVAEMLERFDLADVADALPDS-----LPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
180-386 |
1.70e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 48.86 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 180 LTGISGSVNPGEVLALMGPSGSGKTTLlsllagrisqsstggsvtyndkpyskylkskigfvtqddvlfphltVKETLTY 259
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL----------------------------------------------VNEGLYA 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 260 AARLRLPKTLTREQKK--------QRALDV-IQELGLERCQDTMiggafvrgvSGGERKRVSIGNEIIINP--SLLLLDE 328
Cdd:cd03238 45 SGKARLISFLPKFSRNklifidqlQFLIDVgLGYLTLGQKLSTL---------SGGELQRVKLASELFSEPpgTLFILDE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 79597808 329 PTSGLDSTTALRTILMLHDIAEAGKTVITTIHQPssRLFHRFDKLILLGRGSLLYFGK 386
Cdd:cd03238 116 PSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNL--DVLSSADWIIDFGPGSGKSGGK 171
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
177-391 |
3.33e-06 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. 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: 213255 [Multi-domain] Cd Length: 257 Bit Score: 49.14 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 177 KEILTGISGSVNPGEVLALMGPSGSGKTTlLSLLAGRISQSSTgGSVTYNDKPYSKY----LKSKIGFVTQDDVLFphlt 252
Cdd:cd03288 34 KPVLKHVKAYIKPGQKVGICGRTGSGKSS-LSLAFFRMVDIFD-GKIVIDGIDISKLplhtLRSRLSIILQDPILF---- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 253 vketlTYAARLRL-PKTLTREQKKQRALDVIQelgLERCQDTMIGG--AFV----RGVSGGERKRVSIGNEIIINPSLLL 325
Cdd:cd03288 108 -----SGSIRFNLdPECKCTDDRLWEALEIAQ---LKNMVKSLPGGldAVVteggENFSVGQRQLFCLARAFVRKSSILI 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79597808 326 LDEPTSGLDSTTA--LRTILMlhdIAEAGKTVITTIHQPSSRLfhRFDKLILLGRGSLLYFGKSSEAL 391
Cdd:cd03288 180 MDEATASIDMATEniLQKVVM---TAFADRTVVTIAHRVSTIL--DADLVLVLSRGILVECDTPENLL 242
|
|
| ABC2_membrane_7 |
pfam19055 |
ABC-2 type transporter; |
360-666 |
5.25e-06 |
|
ABC-2 type transporter;
Pssm-ID: 465963 [Multi-domain] Cd Length: 409 Bit Score: 49.52 E-value: 5.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 360 HQPSSRLFHRFDKLILLGRGSL-LYFGKSSEALDYFSSIGCSPLIAMNPAEFLLDLANGNI------------------- 419
Cdd:pfam19055 1 HQPSYTLFKMFDDLILLAKGGLtVYHGPVKKVEEYFAGLGINVPERVNPPDHFIDILEGIVkpstssgvdykqlpvrwml 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 420 -NDISVPSEL------DDRVQVGNSGRETQTGKPSPAavHEYLVEAYETRVAEQEKKKlldpvplDE------EAKAKST 486
Cdd:pfam19055 81 hNGYPVPPDMlqnadgIAASSGENSSNGTNPGVGSEE--QSFAGELWQDVKSNVELKR-------DHirhnflKSKDLSN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 487 RlkRQWGTcwWEQYCILFCRGLKERRHEyfswLRVTQV-----LSTAVILGLLWWQSDirTPMGlqdQAG---------L 552
Cdd:pfam19055 152 R--RTPGV--FRQYRYFLGRVGKQRLRE----ARIQAVdylilLLAGACLGTLAKVSD--ETFG---ALGytytiiavsL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 553 LFFIAvfwgffpvftAIFAFPQERAMLNKERAADMYRLsAYFLARTTSDLPLDFILPSLFLLVVYFMTGLRISpypfFLS 632
Cdd:pfam19055 219 LCKIA----------ALRSFSLDKLQYWRESASGMSSL-AYFLAKDTIDHFNTVIKPLVYLSMFYFFNNPRSS----FAD 283
|
330 340 350
....*....|....*....|....*....|....*
gi 79597808 633 MLTVFLCII-AAQGLGLAIgAILMDLKKAtTLASV 666
Cdd:pfam19055 284 NYIVLLCLVyCVTGIAYAL-AIFFEPGPA-QLWSV 316
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
180-360 |
5.52e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 48.66 E-value: 5.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 180 LTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNdkpyskylkSKIGFVTQDDVLFPHLTVKETLTY 259
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTV--GKVDRN---------GEVSVIAISAGLSGQLTGIENIEF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 260 AArlrLPKTLTREQKKQRALDVIQ--ELGLERCQDtmiggafVRGVSGGERKRVSIGNEIIINPSLLLLDEPTSGLDSTT 337
Cdd:PRK13546 109 KM---LCMGFKRKEIKAMTPKIIEfsELGEFIYQP-------VKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTF 178
|
170 180
....*....|....*....|...
gi 79597808 338 ALRTILMLHDIAEAGKTVITTIH 360
Cdd:PRK13546 179 AQKCLDKIYEFKEQNKTIFFVSH 201
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
179-361 |
6.17e-06 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 48.70 E-value: 6.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 179 ILTGISGSVNPGEVLALMGPSGSGKTTLLSLLagrISQSSTGGS-----VTYNDKPYSKYLKSkIGFVTQDDVLFphltv 253
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAF---LRLLNTEGDiqidgVSWNSVPLQKWRKA-FGVIPQKVFIF----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 254 ketltyAARLRLPKTLTREQKKQRALDVIQELGLERCQD--------TMIGGAFVrgVSGGERKRVSIGNEIIINPSLLL 325
Cdd:cd03289 90 ------SGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEqfpgqldfVLVDGGCV--LSHGHKQLMCLARSVLSKAKILL 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 79597808 326 LDEPTSGLDSTT--ALRTILMLhdiAEAGKTVITTIHQ 361
Cdd:cd03289 162 LDEPSAHLDPITyqVIRKTLKQ---AFADCTVILSEHR 196
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
168-350 |
7.02e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 48.16 E-value: 7.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 168 IKKLTSSVEKEILTGISGSVNPGEVLALMGPSGSGKT----TLLSLLAGRISQssTGGSVTYNDKPY--SKYLKSKIGFV 241
Cdd:PRK10418 7 LRNIALQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQ--TAGRVLLDGKPVapCALRGRKIATI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 242 TQD--DVLFPHLT----VKETLtyaarlrlpKTLTREQKKQRALDVIQELGLErcQDTMIGGAFVRGVSGGERKRVSIGN 315
Cdd:PRK10418 85 MQNprSAFNPLHTmhthARETC---------LALGKPADDATLTAALEAVGLE--NAARVLKLYPFEMSGGMLQRMMIAL 153
|
170 180 190
....*....|....*....|....*....|....*
gi 79597808 316 EIIINPSLLLLDEPTSGLDSTTALRTILMLHDIAE 350
Cdd:PRK10418 154 ALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQ 188
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
180-334 |
1.19e-05 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 46.94 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 180 LTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYNDKPYSKYL--------KSKIGFVTQDDVLFpHL 251
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLE--GKVHWSNKNESEPSfeatrsrnRYSVAYAAQKPWLL-NA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 252 TVKETLTYAARLrlpktltreqKKQRALDVIQELGLERCQD-------TMIGGafvRGV--SGGERKRVSIGNEIIINPS 322
Cdd:cd03290 94 TVEENITFGSPF----------NKQRYKAVTDACSLQPDIDllpfgdqTEIGE---RGInlSGGQRQRICVARALYQNTN 160
|
170
....*....|..
gi 79597808 323 LLLLDEPTSGLD 334
Cdd:cd03290 161 IVFLDDPFSALD 172
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
183-356 |
1.56e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 48.37 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 183 ISGSVNPGEVLALMGPSGSGKTTLLSLLAGriSQSSTGGSVTYNDKPYSkyLKSKIGFVTQDDVL----------FPHLT 252
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYG--ATRRTAGQVYLDGKPID--IRSPRDAIRAGIMLcpedrkaegiIPVHS 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 253 VKETLTYAAR---LRLPKTLTREQKKQRALDVIQELGLE-RCQDTMIggafvRGVSGGERKRVSIGNEIIINPSLLLLDE 328
Cdd:PRK11288 348 VADNINISARrhhLRAGCLINNRWEAENADRFIRSLNIKtPSREQLI-----MNLSGGNQQKAILGRWLSEDMKVILLDE 422
|
170 180
....*....|....*....|....*....
gi 79597808 329 PTSGLDsTTALRTIL-MLHDIAEAGKTVI 356
Cdd:PRK11288 423 PTRGID-VGAKHEIYnVIYELAAQGVAVL 450
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
177-337 |
1.60e-05 |
|
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: 48.75 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 177 KEILTGISGSVNPGEVLALMGPSGSGKTTLLSLLagrISQSSTGGS-----VTYNDKPYSKYLKSkIGFVTQDDVLFPHL 251
Cdd:TIGR01271 1232 RAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSAL---LRLLSTEGEiqidgVSWNSVTLQTWRKA-FGVIPQKVFIFSGT 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 252 TVKETLTYAarlrlpktltrEQKKQRALDVIQELGL----ERCQD----TMIGGAFVrgVSGGERKRVSIGNEIIINPSL 323
Cdd:TIGR01271 1308 FRKNLDPYE-----------QWSDEEIWKVAEEVGLksviEQFPDkldfVLVDGGYV--LSNGHKQLMCLARSILSKAKI 1374
|
170
....*....|....
gi 79597808 324 LLLDEPTSGLDSTT 337
Cdd:TIGR01271 1375 LLLDEPSAHLDPVT 1388
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
183-334 |
3.70e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 46.85 E-value: 3.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 183 ISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSSTGgSVTYNDKPYS-----KYLKSKIGFVTQD---DVLFPHLTVK 254
Cdd:PRK13549 281 VSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWEG-EIFIDGKPVKirnpqQAIAQGIAMVPEDrkrDGIVPVMGVG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 255 ETLTYAA--RLRLPKTLTREQKKQRALDVIQELGLeRCQDTMIGgafVRGVSGGERKRVSIGNEIIINPSLLLLDEPTSG 332
Cdd:PRK13549 360 KNITLAAldRFTGGSRIDDAAELKTILESIQRLKV-KTASPELA---IARLSGGNQQKAVLAKCLLLNPKILILDEPTRG 435
|
..
gi 79597808 333 LD 334
Cdd:PRK13549 436 ID 437
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
180-356 |
6.08e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 46.20 E-value: 6.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 180 LTG-----ISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSstGGSVTYNDKPYSKY-----LKSKIGFVTQD---DV 246
Cdd:PRK15439 274 LTGegfrnISLEVRAGEILGLAGVVGAGRTELAETLYGLRPAR--GGRIMLNGKEINALstaqrLARGLVYLPEDrqsSG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 247 LF---------PHLTVKETLTYAARLRLPKTLTReqkKQRALDViqelgleRCQDtmiGGAFVRGVSGGERKRVSIGNEI 317
Cdd:PRK15439 352 LYldaplawnvCALTHNRRGFWIKPARENAVLER---YRRALNI-------KFNH---AEQAARTLSGGNQQKVLIAKCL 418
|
170 180 190
....*....|....*....|....*....|....*....
gi 79597808 318 IINPSLLLLDEPTSGLDSTTALRTILMLHDIAEAGKTVI 356
Cdd:PRK15439 419 EASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVL 457
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
269-378 |
1.09e-04 |
|
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: 43.50 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 269 LTREQKKQRALDVIQElGLERCQDTMIGGAFVRGVSGGERKRVSI----GNEIIINPSLLLLDEPTSGLDSTTALRTILM 344
Cdd:cd03227 45 LGGAQSATRRRSGVKA-GCIVAAVSAELIFTRLQLSGGEKELSALalilALASLKPRPLYILDEIDRGLDPRDGQALAEA 123
|
90 100 110
....*....|....*....|....*....|....
gi 79597808 345 LHDIAEAGKTVITTIHQPssRLFHRFDKLILLGR 378
Cdd:cd03227 124 ILEHLVKGAQVIVITHLP--ELAELADKLIHIKK 155
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
183-390 |
1.81e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 44.41 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 183 ISGSVNPGEVLALMGPSGSGKttllSLLAGRISQSS------TGGSVTYND--------KPYSKYLKSKIGFVTQD--DV 246
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGK----SLIAKAICGVTkdnwrvTADRMRFDDidllrlspRERRKLVGHNVSMIFQEpqSC 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 247 LFPHLTVKETL-------TYAARLRlpktlTR-EQKKQRALDVIQELGLERCQDTMigGAFVRGVSGGERKRVSIGNEII 318
Cdd:PRK15093 102 LDPSERVGRQLmqnipgwTYKGRWW-----QRfGWRKRRAIELLHRVGIKDHKDAM--RSFPYELTEGECQKVMIAIALA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79597808 319 INPSLLLLDEPTSGLDSTTALRTILMLHDIAEAGKTVITTIHQPSSRLFHRFDKLillgrgSLLYFGKSSEA 390
Cdd:PRK15093 175 NQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKI------NVLYCGQTVET 240
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
179-391 |
4.07e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 44.20 E-value: 4.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 179 ILTGISGSVNPGEVLALMGPSGSGKTTLLSLLAgRISQSSTgGSVTYNDKPYSKY----LKSKIGFVTQDDVLFPHlTVK 254
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALF-RIVELEK-GRIMIDDCDVAKFgltdLRRVLSIIPQSPVLFSG-TVR 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 255 ---ETLTYAARLRLPKTLTREQKKqralDVIQE--LGLErcQDTMIGGafvRGVSGGERKRVSIGNEIIINPSLLLLDEP 329
Cdd:PLN03232 1328 fniDPFSEHNDADLWEALERAHIK----DVIDRnpFGLD--AEVSEGG---ENFSVGQRQLLSLARALLRRSKILVLDEA 1398
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79597808 330 TSGLDSTTalrTILMLHDIAEAGKTVITTIhqpssrLFHRF------DKLILLGRGSLLYFGKSSEAL 391
Cdd:PLN03232 1399 TASVDVRT---DSLIQRTIREEFKSCTMLV------IAHRLntiidcDKILVLSSGQVLEYDSPQELL 1457
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
180-345 |
4.56e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 43.62 E-value: 4.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 180 LTGISGSVNPGEVLALMGPSGSGKTTLLSLLAGRISQSSTGGSVTYNDKPYS-KYLKS--KIGFVT--QDDVLFPHLTVK 254
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSYEGEILFDGEVCRfKDIRDseALGIVIihQELALIPYLSIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 255 ETLtyaarlrlpkTLTREQKK----------QRALDVIQELGLERCQDTMIGGAfvrGVsgGERKRVSIGNEIIINPSLL 324
Cdd:NF040905 97 ENI----------FLGNERAKrgvidwnetnRRARELLAKVGLDESPDTLVTDI---GV--GKQQLVEIAKALSKDVKLL 161
|
170 180
....*....|....*....|....
gi 79597808 325 LLDEPTSGL---DSTTALRTILML 345
Cdd:NF040905 162 ILDEPTAALneeDSAALLDLLLEL 185
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
190-360 |
4.98e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.70 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 190 GEVLALMGPSGSGKTTLLSLLAGR-------------ISQSSTGGSVTY------NDKPYSKYLKSKIGFVTQD-DVLFP 249
Cdd:PLN03073 203 GRHYGLVGRNGTGKTTFLRYMAMHaidgipkncqilhVEQEVVGDDTTAlqcvlnTDIERTQLLEEEAQLVAQQrELEFE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 250 HLTVKETLTYAARLRLPKTLTREQKKQRALDVIQELGLE-RCQDTMIGGAF--------VRGVSGGERKRVSIGNEIIIN 320
Cdd:PLN03073 283 TETGKGKGANKDGVDKDAVSQRLEEIYKRLELIDAYTAEaRAASILAGLSFtpemqvkaTKTFSGGWRMRIALARALFIE 362
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 79597808 321 PSLLLLDEPTSGLDsttaLRTILMLHD-IAEAGKTVITTIH 360
Cdd:PLN03073 363 PDLLLLDEPTNHLD----LHAVLWLETyLLKWPKTFIVVSH 399
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
291-356 |
1.50e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 41.64 E-value: 1.50e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79597808 291 QDTMIGGafvrgVSGGERKRVSIGNEIIINPSLLLLDEPTSGLDSTTALRTILMLHDIAEAGKTVI 356
Cdd:PRK10982 385 HRTQIGS-----LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGII 445
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
179-409 |
1.78e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 42.07 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 179 ILTGISGSVNPGEVLALMGPSGSGKTTLLsLLAGRISQsSTGGSVTYNDKPYSKY----LKSKIGFVTQDDVLF------ 248
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLL-LTFMRMVE-VCGGEIRVNGREIGAYglreLRRQFSMIPQDPVLFdgtvrq 1402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 249 ---PHLTVKETLTYAArLRLPKTLTREQKKQRALDV-IQELGLErcqdtmiggafvrgVSGGERKRVSIGNEIIINPS-L 323
Cdd:PTZ00243 1403 nvdPFLEASSAEVWAA-LELVGLRERVASESEGIDSrVLEGGSN--------------YSVGQRQLMCMARALLKKGSgF 1467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 324 LLLDEPTSGLDSttAL-RTILMLHDIAEAGKTVITTIHqpssRLfH---RFDKLILLGRGSLLYFGKSSEALDYFSSIGC 399
Cdd:PTZ00243 1468 ILMDEATANIDP--ALdRQIQATVMSAFSAYTVITIAH----RL-HtvaQYDKIIVMDHGAVAEMGSPRELVMNRQSIFH 1540
|
250
....*....|
gi 79597808 400 SPLIAMNPAE 409
Cdd:PTZ00243 1541 SMVEALGRSE 1550
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
304-361 |
1.86e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 40.68 E-value: 1.86e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79597808 304 SGGERKRVSIGNEIIiNPS----LLLLDEPTSGLDSTTALRTILMLHDIAEAGKTVITTIHQ 361
Cdd:cd03271 171 SGGEAQRIKLAKELS-KRStgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHN 231
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
185-360 |
3.15e-03 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 39.09 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 185 GSVNPGEVLALMGPSGSGKTTLLSLLAGRIsqsstggsvtyndKPyskylkskigfvTQDDVLFPHLTVKETLTYAArlr 264
Cdd:cd03222 20 GVVKEGEVIGIVGPNGTGKTTAVKILAGQL-------------IP------------NGDNDEWDGITPVYKPQYID--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 265 lpktltreqkkqraldviqelglercqdtmiggafvrgVSGGERKRVSIGNEIIINPSLLLLDEPTSGLDSTTALRTILM 344
Cdd:cd03222 72 --------------------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARA 113
|
170
....*....|....*..
gi 79597808 345 L-HDIAEAGKTVITTIH 360
Cdd:cd03222 114 IrRLSEEGKKTALVVEH 130
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
189-337 |
3.70e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 40.70 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 189 PGEVLALMGPSGSGKTTLLSLLAGRISQSStgGSVTYN----------DKP-------YSkYLKSKIGFVTQddvlfpHL 251
Cdd:PRK11147 28 DNERVCLVGRNGAGKSTLMKILNGEVLLDD--GRIIYEqdlivarlqqDPPrnvegtvYD-FVAEGIEEQAE------YL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79597808 252 TvketlTYAARLRL------PKTLTREQKKQRALD-------------VIQELGLErcQDTMIGGafvrgVSGGERKRVS 312
Cdd:PRK11147 99 K-----RYHDISHLvetdpsEKNLNELAKLQEQLDhhnlwqlenrineVLAQLGLD--PDAALSS-----LSGGWLRKAA 166
|
170 180
....*....|....*....|....*
gi 79597808 313 IGNEIIINPSLLLLDEPTSGLDSTT 337
Cdd:PRK11147 167 LGRALVSNPDVLLLDEPTNHLDIET 191
|
|
| |
