|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
64-644 |
2.88e-84 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 276.93 E-value: 2.88e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 64 LSSISGIMGPG-LNAIMGPQDGSRSLLLDVLAARRdPCGL--SGDILINGKPRPAN-FKCTSGYIPQNDVVLGTVTVRDN 139
Cdd:TIGR00955 41 LKNVSGVAKPGeLLAVMGSSGAGKTTLMNALAFRS-PKGVkgSGSVLLNGMPIDAKeMRAISAYVQQDDLFIPTLTVREH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 140 LEFSAALRLPMTVTRDEKRRRINEVLELLHLEKEQN--------VKPRSKGLRKRTSIAMELVTEHPILFLDDPTTGLDL 211
Cdd:TIGR00955 120 LMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANtrigvpgrVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDS 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 212 RTTTDVISILRRMSMKGKTIIFSINQPQYSIFRFFDSLTLVASGKLMFHGPARDALEYFTSAGYQYESHNNPADFFLDVI 291
Cdd:TIGR00955 200 FMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAVPFFSDLGHPCPENYNPADFYVQVL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 292 NGGfpdteedghEADENEEFVERQHQVTGKLANMYAQSPLHSATRARLDqllgEQKLDRSSAVETTC--VTPFWHQLGWI 369
Cdd:TIGR00955 280 AVI---------PGSENESRERIEKICDSFAVSDIGRDMLVNTNLWSGK----AGGLVKDSENMEGIgyNASWWTQFYAL 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 370 TRRSFKNFLGFPWVTTIQVIIIVILAVVVGTAFrlLQNVCTELQMRAILILLltgFQCITSVT----AGELFVIDQDR-- 443
Cdd:TIGR00955 347 LKRSWLSVLRDPLLLKVRLIQTMMTAILIGLIY--LGQGLTQKGVQNINGAL---FLFLTNMTfqnvFPVINVFTAELpv 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 444 FLHEHTSGYYRVSSYFFGKLLAELiPRRLLPSTIFTLITYFIAGLRTSVRGFFTMTFTIMMLAYSASSL-SLSLGAGENV 522
Cdd:TIGR00955 422 FLRETRSGLYRVSAYFLAKTIAEL-PLFIILPALFTSITYWMIGLRSGATHFLTFLFLVTLVANVATSFgYLISCAFSST 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 523 AAITTLLVTIYFVFMLfFSGLSLDTGFLPV-LSWIRYFSIPHYGFRALLHNEFLGQNFCPEYNTEEVSRCQNyvicTGEE 601
Cdd:TIGR00955 501 SMALTVGPPFVIPFLL-FGGFFINSDSIPVyFKWLSYLSWFRYGNEGLLINQWSDVDNIECTSANTTGPCPS----SGEV 575
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1046858258 602 FLEIQGFHLSSwgFWENHLALACTMIILLTITYVQLLLLKKRK 644
Cdd:TIGR00955 576 ILETLSFRNAD--LYLDLIGLVILIFFFRLLAYFALRIRIRRK 616
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
35-261 |
4.43e-61 |
|
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: 202.01 E-value: 4.43e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 35 AVLSFHNISYreTVQSGfPLRQQTRVmerLSSISGIMGPG-LNAIMGPQDGSRSLLLDVLAARRDPCGLSGDILINGKPR 113
Cdd:cd03213 2 VTLSFRNLTV--TVKSS-PSKSGKQL---LKNVSGKAKPGeLTAIMGPSGAGKSTLLNALAGRRTGLGVSGEVLINGRPL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 114 PA-NFKCTSGYIPQNDVVLGTVTVRDNLEFSAALrlpmtvtrdekrRRInevlellhlekeqnvkprSKGLRKRTSIAME 192
Cdd:cd03213 76 DKrSFRKIIGYVPQDDILHPTLTVRETLMFAAKL------------RGL------------------SGGERKRVSIALE 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046858258 193 LVTEHPILFLDDPTTGLDLRTTTDVISILRRMSMKGKTIIFSINQPQYSIFRFFDSLTLVASGKLMFHG 261
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
64-574 |
3.38e-51 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 187.78 E-value: 3.38e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 64 LSSISGIMGPG-LNAIMGPQDGSRSLLLDVLAARRDPCGLSGDILIN-GKPRPANFKCTsGYIPQNDVVLGTVTVRDNLE 141
Cdd:PLN03211 84 LNGVTGMASPGeILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANnRKPTKQILKRT-GFVTQDDILYPHLTVRETLV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 142 FSAALRLPMTVTRDEKRRRINEVLELLHLEKEQN-------VKPRSKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTT 214
Cdd:PLN03211 163 FCSLLRLPKSLTKQEKILVAESVISELGLTKCENtiignsfIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 215 TDVISILRRMSMKGKTIIFSINQPQYSIFRFFDSLTLVASGKLMFHGPARDALEYFTSAGYQYESHNNPADFFLDVINGg 294
Cdd:PLN03211 243 YRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESVGFSPSFPMNPADFLLDLANG- 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 295 fpDTEEDGheADENEEFVERQHQVTGK---LANMYAQSPLHSATRARLDQLLGEQKLDRSSAVETTCVTPFWHQLGWITR 371
Cdd:PLN03211 322 --VCQTDG--VSEREKPNVKQSLVASYntlLAPKVKAAIEMSHFPQANARFVGSASTKEHRSSDRISISTWFNQFSILLQ 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 372 RSFK-------NFLGfpwVTTIQVIIIVILAVVVGTAFRLLQNVCTELQMRAILILLLTGFQCItsvtagelFVIDQDR- 443
Cdd:PLN03211 398 RSLKerkhesfNTLR---VFQVIAAALLAGLMWWHSDFRDVQDRLGLLFFISIFWGVFPSFNSV--------FVFPQERa 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 444 -FLHEHTSGYYRVSSYFFGKLLAELiPRRLLPSTIFTLITYFIAGLRTSVrGFFTMTFTIMMLAYSASSLSLSLGAgenv 522
Cdd:PLN03211 467 iFVKERASGMYTLSSYFMARIVGDL-PMELILPTIFLTVTYWMAGLKPEL-GAFLLTLLVLLGYVLVSQGLGLALG---- 540
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1046858258 523 AAI--TTLLVTIYFVFMLFFsglSLDTGFL-----PVLSWIRYFSIPHYGFRALLHNEF 574
Cdd:PLN03211 541 AAImdAKKASTIVTVTMLAF---VLTGGFYvhklpSCMAWIKYISTTFYSYRLLINVQY 596
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
24-561 |
2.92e-50 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 188.78 E-value: 2.92e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 24 NTSDPETLTKEAVLSFHNISYRETVQSGfplrqqTRVMerLSSISGIMGPG-LNAIMGPQDGSRSLLLDVLAARRDpCGL 102
Cdd:TIGR00956 747 DEKDMEKESGEDIFHWRNLTYEVKIKKE------KRVI--LNNVDGWVKPGtLTALMGASGAGKTTLLNVLAERVT-TGV 817
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 103 --SGDILINGKPRPANFKCTSGYIPQNDVVLGTVTVRDNLEFSAALRLPMTVTRDEKRRRINEVLELLHLE--KEQNVKP 178
Cdd:TIGR00956 818 itGGDRLVNGRPLDSSFQRSIGYVQQQDLHLPTSTVRESLRFSAYLRQPKSVSKSEKMEYVEEVIKLLEMEsyADAVVGV 897
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 179 RSKGL----RKRTSIAMELVTEhP--ILFLDDPTTGLDLRTTTDVISILRRMSMKGKTIIFSINQPQYSIFRFFDSLTLV 252
Cdd:TIGR00956 898 PGEGLnveqRKRLTIGVELVAK-PklLLFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAILFEEFDRLLLL 976
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 253 ASG-KLMFHGP----ARDALEYFTSAG-YQYESHNNPADFFLDVINGgfpdteedGHEADENEEFVErqhqvtgklanMY 326
Cdd:TIGR00956 977 QKGgQTVYFGDlgenSHTIINYFEKHGaPKCPEDANPAEWMLEVIGA--------APGAHANQDYHE-----------VW 1037
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 327 AQSPLHSATRARLDQL---LGEQKLDRSSAVETTCVTPFWHQLGWITRRSFKNF---LGFPW----VTTIQVIIIVILAV 396
Cdd:TIGR00956 1038 RNSSEYQAVKNELDRLeaeLSKAEDDNDPDALSKYAASLWYQFKLVLWRTFQQYwrtPDYLYskffLTIFAALFIGFTFF 1117
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 397 VVGTAFRLLQNVCteLQMRAILILLLTGFQCI--TSVTAGELFvidqdrFLHEHTSGYYRVSSYFFGKLLAElIPRRLLP 474
Cdd:TIGR00956 1118 KVGTSLQGLQNQM--FAVFMATVLFNPLIQQYlpPFVAQRDLY------EVRERPSRTFSWLAFIAAQITVE-IPYNLVA 1188
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 475 STIFTLITYFIAGL--------RTSVRGFFTMTFTIMMLAYSASSLSLSLGAGEN--VAAIttlLVTIYFVFMLFFSGLS 544
Cdd:TIGR00956 1189 GTIFFFIWYYPVGFywnasktgQVHERGVLFWLLSTMFFLYFSTLGQMVISFNPNadNAAV---LASLLFTMCLSFCGVL 1265
|
570
....*....|....*..
gi 1046858258 545 LDTGFLPVLsWIRYFSI 561
Cdd:TIGR00956 1266 APPSRMPGF-WIFMYRC 1281
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
36-255 |
5.46e-47 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 163.95 E-value: 5.46e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 36 VLSFHNISYreTVqsgfPLRQQTRVMerLSSISGIMGPG-LNAIMGPQDGSRSLLLDVLAARRDPCGLSGDILINGKPRP 114
Cdd:cd03232 3 VLTWKNLNY--TV----PVKGGKRQL--LNNISGYVKPGtLTALMGESGAGKTTLLDVLAGRKTAGVITGEILINGRPLD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 115 ANFKCTSGYIPQNDVVLGTVTVRDNLEFSAALRlpmtvtrdekrrrinevlellHLEKEQnvkprskglRKRTSIAMELV 194
Cdd:cd03232 75 KNFQRSTGYVEQQDVHSPNLTVREALRFSALLR---------------------GLSVEQ---------RKRLTIGVELA 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046858258 195 TEHPILFLDDPTTGLDLRTTTDVISILRRMSMKGKTIIFSINQPQYSIFRFFDSLTLVASG 255
Cdd:cd03232 125 AKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRG 185
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
77-261 |
3.88e-41 |
|
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: 149.34 E-value: 3.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 77 AIMGPQDGSRSLLLDVLAARRDPCG-LSGDILINGKPR-PANFKCTSGYIPQNDVVLGTVTVRDNLEFSAALRLPMTvTR 154
Cdd:cd03234 37 AILGSSGSGKTTLLDAISGRVEGGGtTSGQILFNGQPRkPDQFQKCVAYVRQDDILLPGLTVRETLTYTAILRLPRK-SS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 155 DEKRRRINEVLELLHLEKEQ----NVKPRSKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMSMKGKT 230
Cdd:cd03234 116 DAIRKKRVEDVLLRDLALTRiggnLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRI 195
|
170 180 190
....*....|....*....|....*....|.
gi 1046858258 231 IIFSINQPQYSIFRFFDSLTLVASGKLMFHG 261
Cdd:cd03234 196 VILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
51-642 |
1.77e-39 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 156.04 E-value: 1.77e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 51 GFPLRQQTRVMERLSSISGIMGPG-LNAIMGPQDGSRSLLLDVLAARRD--PCGLSGDILING------KPRpanFKCTS 121
Cdd:TIGR00956 64 KLKKFRDTKTFDILKPMDGLIKPGeLTVVLGRPGSGCSTLLKTIASNTDgfHIGVEGVITYDGitpeeiKKH---YRGDV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 122 GYIPQNDVVLGTVTVRDNLEFSAALRLPMT----VTRDEKRRRINEV-LELLHLEKEQN-------VKPRSKGLRKRTSI 189
Cdd:TIGR00956 141 VYNAETDVHFPHLTVGETLDFAARCKTPQNrpdgVSREEYAKHIADVyMATYGLSHTRNtkvgndfVRGVSGGERKRVSI 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 190 AMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMSMKGKTIIF-SINQPQYSIFRFFDSLTLVASGKLMFHGPARDALE 268
Cdd:TIGR00956 221 AEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLvAIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAKQ 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 269 YFTSAGYQYESHNNPADFFLDVINggfPDTEEdgheadENEEFVERQHQVTGKLANMYAQSPLHSATRARLDQLLGE--- 345
Cdd:TIGR00956 301 YFEKMGFKCPDRQTTADFLTSLTS---PAERQ------IKPGYEKKVPRTPQEFETYWRNSPEYAQLMKEIDEYLDRcse 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 346 ----QKLDRSSAVETTCVT--------PFWHQLGWITRRSFKNFLGFPWVTTIQVIIIVILAVVVGTAF-RLLQNVCTEL 412
Cdd:TIGR00956 372 sdtkEAYRESHVAKQSKRTrpsspytvSFSMQVKYCLARNFLRMKGNPSFTLFMVFGNIIMALILSSVFyNLPKNTSDFY 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 413 QMRAILI--LLLTGFQCITsvtagELFVIDQDRFLHEHTSGY--YRVSSYFFGKLLAElIPRRLLPSTIFTLITYFIAGL 488
Cdd:TIGR00956 452 SRGGALFfaILFNAFSSLL-----EIASMYEARPIVEKHRKYalYHPSADAIASIISE-IPFKIIESVVFNIILYFMVNF 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 489 RTSVRGFFTMTFTIMMlaysasSLSLSLGAGENVAAITTLLVTIYFVFMLFFSGLSLDTGF-LPVLS------WIRYFSI 561
Cdd:TIGR00956 526 RRTAGRFFFYLLILFI------CTLAMSHLFRSIGAVTKTLSEAMTPAAILLLALSIYTGFaIPRPSmlgwskWIYYVNP 599
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 562 PHYGFRALLHNEFLGQNF-CPEY-----NTEEVSRcqNYVICT------------GEEFLEIQGFHLSSWgFWENhLALA 623
Cdd:TIGR00956 600 LAYAFESLMVNEFHGRRFeCSQYvpsggGYDNLGV--TNKVCTvvgaepgqdyvdGDDYLKLSFQYYNSH-KWRN-FGII 675
|
650
....*....|....*....
gi 1046858258 624 CTMIILLTITYVQLLLLKK 642
Cdd:TIGR00956 676 IGFTVFFFFVYILLTEFNK 694
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
37-290 |
2.00e-37 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 150.00 E-value: 2.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 37 LSFHNISY-----RETVQSGFPlrqQTRvMERLSSISGIMGPG-LNAIMGPQDGSRSLLLDVLAARRDPCGLSGDILING 110
Cdd:PLN03140 868 MSFDDVNYfvdmpAEMKEQGVT---EDR-LQLLREVTGAFRPGvLTALMGVSGAGKTTLMDVLAGRKTGGYIEGDIRISG 943
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 111 KP-RPANFKCTSGYIPQNDVVLGTVTVRDNLEFSAALRLPMTVTRDEKRRRINEVLELLHLEkeqNVKPRSKGL------ 183
Cdd:PLN03140 944 FPkKQETFARISGYCEQNDIHSPQVTVRESLIYSAFLRLPKEVSKEEKMMFVDEVMELVELD---NLKDAIVGLpgvtgl 1020
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 184 ----RKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMSMKGKTIIFSINQPQYSIFRFFDSLTLVA-SGKLM 258
Cdd:PLN03140 1021 steqRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKrGGQVI 1100
|
250 260 270
....*....|....*....|....*....|....*...
gi 1046858258 259 FHGP----ARDALEYFTS--AGYQYESHNNPADFFLDV 290
Cdd:PLN03140 1101 YSGPlgrnSHKIIEYFEAipGVPKIKEKYNPATWMLEV 1138
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
100-270 |
2.41e-30 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 119.40 E-value: 2.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 100 CGL----SGDILINGKP---RPANFKCTSGYIPQNDVVLGTVTVRDNLEFSAALRlpmTVTRDEKRRRINEVLELLHLEK 172
Cdd:COG1131 47 LGLlrptSGEVRVLGEDvarDPAEVRRRIGYVPQEPALYPDLTVRENLRFFARLY---GLPRKEARERIDELLELFGLTD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 173 EQNVKPR--SKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMSMKGKTIIFSinqpqyS-----IFRF 245
Cdd:COG1131 124 AADRKVGtlSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLS------ThyleeAERL 197
|
170 180
....*....|....*....|....*
gi 1046858258 246 FDSLTLVASGKLMFHGPARDALEYF 270
Cdd:COG1131 198 CDRVAIIDKGRIVADGTPDELKARL 222
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
51-314 |
8.00e-22 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 101.08 E-value: 8.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 51 GFPLRQQTRVMeRLSSISGIMGPG-LNAIMGPQDGSRSLLLDVLAARRDPC-GLSGDILINGK------PRPanfkcTSG 122
Cdd:PLN03140 169 GINLAKKTKLT-ILKDASGIIKPSrMTLLLGPPSSGKTTLLLALAGKLDPSlKVSGEITYNGYrlnefvPRK-----TSA 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 123 YIPQNDVVLGTVTVRDNLEFSAALR-------LPMTVTRDEKRRRI---NEV---------------------LELLHLE 171
Cdd:PLN03140 243 YISQNDVHVGVMTVKETLDFSARCQgvgtrydLLSELARREKDAGIfpeAEVdlfmkatamegvksslitdytLKILGLD 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 172 -------KEQNVKPRSKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRM-SMKGKTIIFSINQPQYSIF 243
Cdd:PLN03140 323 ickdtivGDEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIvHLTEATVLMSLLQPAPETF 402
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046858258 244 RFFDSLTLVASGKLMFHGPARDALEYFTSAGYQYESHNNPADFFLDVINggfpDTEEDGHEADENE--------EFVER 314
Cdd:PLN03140 403 DLFDDIILLSEGQIVYQGPRDHILEFFESCGFKCPERKGTADFLQEVTS----KKDQEQYWADRNKpyryisvsEFAER 477
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
34-261 |
8.28e-22 |
|
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: 93.87 E-value: 8.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 34 EAVLSFHNISYREtvqsgfplRQQTRVMERLSSISGIMGPG-LNAIMGPQDGSRSLLLDVLAARRDPCG-LSGDILING- 110
Cdd:cd03233 1 ASTLSWRNISFTT--------GKGRSKIPILKDFSGVVKPGeMVLVLGRPGSGCSTLLKALANRTEGNVsVEGDIHYNGi 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 111 --KPRPANFKCTSGYIPQNDVVLGTVTVRDNLEFSAALRlpmtvtrdekrrrinevlellhleKEQNVKPRSKGLRKRTS 188
Cdd:cd03233 73 pyKEFAEKYPGEIIYVSEEDVHFPTLTVRETLDFALRCK------------------------GNEFVRGISGGERKRVS 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046858258 189 IAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMSMK-GKTIIFSINQPQYSIFRFFDSLTLVASGKLMFHG 261
Cdd:cd03233 129 IAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVlKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
77-234 |
4.48e-21 |
|
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: 91.76 E-value: 4.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 77 AIMGPqDGS-RSLLLDVLAARRDPcgLSGDILINGKP----RPANFKCTSGYIPQN-DVVLGTVTVRDNLEFSaaLRLpM 150
Cdd:cd03225 31 LIVGP-NGSgKSTLLRLLNGLLGP--TSGEVLVDGKDltklSLKELRRKVGLVFQNpDDQFFGPTVEEEVAFG--LEN-L 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 151 TVTRDEKRRRINEVLELLHLEKEQNVKPR--SKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMSMKG 228
Cdd:cd03225 105 GLPEEEIEERVEEALELVGLEGLRDRSPFtlSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEG 184
|
....*.
gi 1046858258 229 KTIIFS 234
Cdd:cd03225 185 KTIIIV 190
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
369-572 |
1.66e-20 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 90.03 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 369 ITRRSFKNFLGFPWVTTIQVIIIVILAVVVGTAFRLLQNVCTELQMRAIL--ILLLTGFQCITSVTAgeLFVIDQDRFLH 446
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLGNQQGGLNRPGLLffSILFNAFSALSGISP--VFEKERGVLYR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 447 EHTSGYYRVSSYFFGKLLAElIPRRLLPSTIFTLITYFIAGLRTSVRGFFTMTFTIMMLAYSASSLSLSLGAGENVAAIT 526
Cdd:pfam01061 79 ELASPLYSPSAYVLAKILSE-LPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1046858258 527 TLLVTIYFVFMLFFSGLSLDTGFLPV-LSWIRYFSIPHYGFRALLHN 572
Cdd:pfam01061 158 SQLGPLVLLPLLLLSGFFIPIDSMPVwWQWIYYLNPLTYAIEALRAN 204
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
64-261 |
1.87e-20 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 89.94 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 64 LSSISGIMGPGLNAIMGPQDGSRSLLLDVLAARRDPCglSGDILINGKP---RPANFKCTSGYIPQNDVVLGTVTVRDNL 140
Cdd:cd03264 16 LDGVSLTLGPGMYGLLGPNGAGKTTLMRILATLTPPS--SGTIRIDGQDvlkQPQKLRRRIGYLPQEFGVYPNFTVREFL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 141 EFSAALRlpmTVTRDEKRRRINEVLELLHLE--KEQNVKPRSKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVI 218
Cdd:cd03264 94 DYIAWLK---GIPSKEVKARVDEVLELVNLGdrAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFR 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1046858258 219 SILRRMSmKGKTIIFSINQPQySIFRFFDSLTLVASGKLMFHG 261
Cdd:cd03264 171 NLLSELG-EDRIVILSTHIVE-DVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
77-234 |
3.99e-20 |
|
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: 89.49 E-value: 3.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 77 AIMGPQDGSRSLLLDVLAARRDPCglSGDILINGK---PRPANFKCTSGYIPQNDVVLGTVTVRDNLEFSAALRlpmTVT 153
Cdd:cd03263 32 GLLGHNGAGKTTTLKMLTGELRPT--SGTAYINGYsirTDRKAARQSLGYCPQFDALFDELTVREHLRFYARLK---GLP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 154 RDEKRRRINEVLELLHLEKEQNVKPR--SKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMSmKGKTI 231
Cdd:cd03263 107 KSEIKEEVELLLRVLGLTDKANKRARtlSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVR-KGRSI 185
|
...
gi 1046858258 232 IFS 234
Cdd:cd03263 186 ILT 188
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
77-233 |
2.51e-19 |
|
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: 87.16 E-value: 2.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 77 AIMGPQdGS-RSLLLDVLAARRDPCglSGDILINGKP-------RPANFKCTS-GYIPQNDVVLGTVTVRDNLEfsaalr 147
Cdd:cd03255 34 AIVGPS-GSgKSTLLNILGGLDRPT--SGEVRVDGTDisklsekELAAFRRRHiGFVFQSFNLLPDLTALENVE------ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 148 LPMTVT---RDEKRRRINEVLELLHLEKEQNVKPR--SKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILR 222
Cdd:cd03255 105 LPLLLAgvpKKERRERAEELLERVGLGDRLNHYPSelSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLR 184
|
170
....*....|..
gi 1046858258 223 RMS-MKGKTIIF 233
Cdd:cd03255 185 ELNkEAGTTIVV 196
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
89-238 |
1.42e-18 |
|
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: 84.45 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 89 LLDVLAARRDPcgLSGDILINGKP---RPANFKCTSGYIPQNDVVLGTVTVRDNLEFSAALRlPMTVTRDekrrRINEVL 165
Cdd:COG4133 44 LLRILAGLLPP--SAGEVLWNGEPirdAREDYRRRLAYLGHADGLKPELTVRENLRFWAALY-GLRADRE----AIDEAL 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046858258 166 ELLHLEKEQNVKPR--SKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMSMKGKTIIFSINQP 238
Cdd:COG4133 117 EAVGLAGLADLPVRqlSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQP 191
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
100-268 |
1.53e-18 |
|
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: 85.08 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 100 CGL----SGDILINGKP-RPANFKCTS---GYIPQN-DVVLGTVTVRDNLEFS-AALRLPmtvtRDEKRRRINEVLELLH 169
Cdd:COG1122 48 NGLlkptSGEVLVDGKDiTKKNLRELRrkvGLVFQNpDDQLFAPTVEEDVAFGpENLGLP----REEIRERVEEALELVG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 170 LE--KEQNVKPRSKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMSMKGKTIIFSINQPQYsIFRFFD 247
Cdd:COG1122 124 LEhlADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDL-VAELAD 202
|
170 180
....*....|....*....|.
gi 1046858258 248 SLTLVASGKLMFHGPARDALE 268
Cdd:COG1122 203 RVIVLDDGRIVADGTPREVFS 223
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
64-261 |
2.73e-18 |
|
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: 83.96 E-value: 2.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 64 LSSISGIMGPG-LNAIMGPQDGSRSLLLDVLAARRDPCglSGDILING---KPRPANFKCTSGYIPQNDVVLGTVTVRDN 139
Cdd:cd03266 21 VDGVSFTVKPGeVTGLLGPNGAGKTTTLRMLAGLLEPD--AGFATVDGfdvVKEPAEARRRLGFVSDSTGLYDRLTAREN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 140 LEFSAALRlpmTVTRDEKRRRINEVLELLHLEK--EQNVKPRSKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDV 217
Cdd:cd03266 99 LEYFAGLY---GLKGDELTARLEELADRLGMEEllDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRAL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1046858258 218 ISILRRMSMKGKTIIFSINQPQySIFRFFDSLTLVASGKLMFHG 261
Cdd:cd03266 176 REFIRQLRALGKCILFSTHIMQ-EVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
77-233 |
1.10e-17 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 82.42 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 77 AIMGPQDGSRSLLLDVLAARRDPCglSGDILING---KPRPANFKCTSGYIPQNDVVLGTVTVRDNLEFSAALrlpMTVT 153
Cdd:cd03265 30 GLLGPNGAGKTTTIKMLTTLLKPT--SGRATVAGhdvVREPREVRRRIGIVFQDLSVDDELTGWENLYIHARL---YGVP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 154 RDEKRRRINEVLELLHL--EKEQNVKPRSKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMSMKGKTI 231
Cdd:cd03265 105 GAERRERIDELLDFVGLleAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMT 184
|
..
gi 1046858258 232 IF 233
Cdd:cd03265 185 IL 186
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
100-234 |
1.14e-17 |
|
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: 80.90 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 100 CGL----SGDILINGKP---RPANFKCTSGYIPQNDVVLGTVTVRDNLEFSaalrlpmtvtrdekrrrinevlellhlek 172
Cdd:cd03230 47 LGLlkpdSGEIKVLGKDikkEPEEVKRRIGYLPEEPSLYENLTVRENLKLS----------------------------- 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046858258 173 eqnvkprsKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMSMKGKTIIFS 234
Cdd:cd03230 98 --------GGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLS 151
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
64-261 |
1.25e-17 |
|
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: 81.81 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 64 LSSISGIMGPG-LNAIMGPQDGSRSLLLDVLAarrdpcGL----SGDILINGKPrPANFKCTSGYIPQNDVVLGT--VTV 136
Cdd:cd03235 15 LEDVSFEVKPGeFLAIVGPNGAGKSTLLKAIL------GLlkptSGSIRVFGKP-LEKERKRIGYVPQRRSIDRDfpISV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 137 RDnleFSAALRLPMTV----TRDEKRRRINEVLELLHLE--KEQNVKPRSKGLRKRTSIAMELVTEHPILFLDDPTTGLD 210
Cdd:cd03235 88 RD---VVLMGLYGHKGlfrrLSKADKAKVDEALERVGLSelADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1046858258 211 LRTTTDVISILRRMSMKGKTIIFS---INQpqysIFRFFDSLTLVAsGKLMFHG 261
Cdd:cd03235 165 PKTQEDIYELLRELRREGMTILVVthdLGL----VLEYFDRVLLLN-RTVVASG 213
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
77-232 |
1.58e-16 |
|
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: 80.90 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 77 AIMGPQDGSRSLLLDVLAARRDPCglSGDILINGK---PRPANFKCTSGYIPQNDVVLGTVTVRDNLEFSAALrlpMTVT 153
Cdd:TIGR01188 23 GFLGPNGAGKTTTIRMLTTLLRPT--SGTARVAGYdvvREPRKVRRSIGIVPQYASVDEDLTGRENLEMMGRL---YGLP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 154 RDEKRRRINEVLELLHLEKEQN--VKPRSKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMSMKGKTI 231
Cdd:TIGR01188 98 KDEAEERAEELLELFELGEAADrpVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDYIRALKEEGVTI 177
|
.
gi 1046858258 232 I 232
Cdd:TIGR01188 178 L 178
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
77-233 |
3.60e-16 |
|
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: 77.90 E-value: 3.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 77 AIMGPQDGSRSLLLDVLAarrdpcGL----SGDILINGKP-RPANFKCtsGYIPQNDVVLGTVTVRDNLEFSAALRLpmt 151
Cdd:cd03293 34 ALVGPSGCGKSTLLRIIA------GLerptSGEVLVDGEPvTGPGPDR--GYVFQQDALLPWLTVLDNVALGLELQG--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 152 VTRDEKRRRINEVLELLHLEKEQNVKPR--SKGLRKRTSIAMELVTEHPILFLDDPTTGLD--LRTT--TDVISILRRMs 225
Cdd:cd03293 103 VPKAEARERAEELLELVGLSGFENAYPHqlSGGMRQRVALARALAVDPDVLLLDEPFSALDalTREQlqEELLDIWRET- 181
|
....*...
gi 1046858258 226 mkGKTIIF 233
Cdd:cd03293 182 --GKTVLL 187
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
77-265 |
3.74e-16 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 78.31 E-value: 3.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 77 AIMGPQDGSRSLLLDVLAARRDPcgLSGDILINGKPRPAN-------FKCTSGYIPQNDVVLGTVTVRDNLEFSaaLRLP 149
Cdd:cd03261 30 AIIGPSGSGKSTLLRLIVGLLRP--DSGEVLIDGEDISGLseaelyrLRRRMGMLFQSGALFDSLTVFENVAFP--LREH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 150 MTVTRDEKRRRINEVLELLHLEKEQNVKPR--SKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMS-M 226
Cdd:cd03261 106 TRLSEEEIREIVLEKLEAVGLRGAEDLYPAelSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKkE 185
|
170 180 190
....*....|....*....|....*....|....*....
gi 1046858258 227 KGKTIIFSINQPQySIFRFFDSLTLVASGKLMFHGPARD 265
Cdd:cd03261 186 LGLTSIMVTHDLD-TAFAIADRIAVLYDGKIVAEGTPEE 223
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
64-207 |
6.17e-15 |
|
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: 72.30 E-value: 6.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 64 LSSISGIMGPG-LNAIMGPqDGS-RSLLLDVLAARRDPcgLSGDILINGKPRPAN----FKCTSGYIPQNDVVLGTVTVR 137
Cdd:pfam00005 1 LKNVSLTLNPGeILALVGP-NGAgKSTLLKLIAGLLSP--TEGTILLDGQDLTDDerksLRKEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046858258 138 DNLEFSAALRLPMtvtRDEKRRRINEVLELLHLEKEQNVKPR------SKGLRKRTSIAMELVTEHPILFLDDPTT 207
Cdd:pfam00005 78 ENLRLGLLLKGLS---KREKDARAEEALEKLGLGDLADRPVGerpgtlSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
77-261 |
6.92e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 75.05 E-value: 6.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 77 AIMGPQDGSRSLLLDVLAARRDPcgLSGDILINGKP----RPANFKCTSGYIPQNDVVLGTVTVRDNLEF--SAALRLPM 150
Cdd:PRK11231 32 ALIGPNGCGKSTLLKCFARLLTP--QSGTVFLGDKPismlSSRQLARRLALLPQHHLTPEGITVRELVAYgrSPWLSLWG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 151 TVTRDEkRRRINEVLELLHLEK--EQNVKPRSKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMSMKG 228
Cdd:PRK11231 110 RLSAED-NARVNQAMEQTRINHlaDRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQG 188
|
170 180 190
....*....|....*....|....*....|....*.
gi 1046858258 229 KTII---FSINQPQysifRFFDSLTLVASGKLMFHG 261
Cdd:PRK11231 189 KTVVtvlHDLNQAS----RYCDHLVVLANGHVMAQG 220
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
77-268 |
8.89e-15 |
|
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: 77.25 E-value: 8.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 77 AIMGPqDGS--RSLLLDVLAARRDPCGLSGDILINGKP----RPANFKCTSGYIPQN-DVVLGTVTVRDNLEFsaALRLp 149
Cdd:COG1123 36 ALVGE-SGSgkSTLALALMGLLPHGGRISGEVLLDGRDllelSEALRGRRIGMVFQDpMTQLNPVTVGDQIAE--ALEN- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 150 MTVTRDEKRRRINEVLELLHLEKEQNVKPR--SKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMSMK 227
Cdd:COG1123 112 LGLSRAEARARVLELLEAVGLERRLDRYPHqlSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRE 191
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1046858258 228 -GKTIIFsINQPQYSIFRFFDSLTLVASGKLMFHGPARDALE 268
Cdd:COG1123 192 rGTTVLL-ITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
103-261 |
9.26e-15 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 73.47 E-value: 9.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 103 SGDILINGKPRPANFKCTSGYIPQNDVVLGTVTVRDNLEFSAALRlpmTVTRDEKRRRINEVLELLHLE--KEQNVKPRS 180
Cdd:cd03269 54 SGEVLFDGKPLDIAARNRIGYLPEERGLYPKMKVIDQLVYLAQLK---GLKKEEARRRIDEWLERLELSeyANKRVEELS 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 181 KGLRKRTSIAMELVTEHPILFLDDPTTGLD---LRTTTDVISILRRmsmKGKTIIFSINQPQySIFRFFDSLTLVASGKL 257
Cdd:cd03269 131 KGNQQKVQFIAAVIHDPELLILDEPFSGLDpvnVELLKDVIRELAR---AGKTVILSTHQME-LVEELCDRVLLLNKGRA 206
|
....
gi 1046858258 258 MFHG 261
Cdd:cd03269 207 VLYG 210
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
75-261 |
1.80e-13 |
|
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: 69.00 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 75 LNAIMGPqDGS-RSLLLDVLAARRDPCglSGDILINGKP----RPANFKCTSGYIPQndvvlgtvtvrdnlefsaALrlp 149
Cdd:cd03214 27 IVGILGP-NGAgKSTLLKTLAGLLKPS--SGEILLDGKDlaslSPKELARKIAYVPQ------------------AL--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 150 mtvtrdekrrrinEVLELLHLeKEQNVKPRSKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMS-MKG 228
Cdd:cd03214 83 -------------ELLGLAHL-ADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLArERG 148
|
170 180 190
....*....|....*....|....*....|....*.
gi 1046858258 229 KTIIFS---INQpqysIFRFFDSLTLVASGKLMFHG 261
Cdd:cd03214 149 KTVVMVlhdLNL----AARYADRVILLKDGRIVAQG 180
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
78-234 |
2.76e-13 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 69.36 E-value: 2.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 78 IMGPQDGSRSLLLDVLAARRDPCglSGDILINGKP-------RPANFKCTSGYIPQNDVVLGTVTVRDNLEFsaALRLpM 150
Cdd:cd03292 32 LVGPSGAGKSTLLKLIYKEELPT--SGTIRVNGQDvsdlrgrAIPYLRRKIGVVFQDFRLLPDRNVYENVAF--ALEV-T 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 151 TVTRDEKRRRINEVLELLHLEKEQNVKPR--SKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMSMKG 228
Cdd:cd03292 107 GVPPREIRKRVPAALELVGLSHKHRALPAelSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAG 186
|
....*.
gi 1046858258 229 KTIIFS 234
Cdd:cd03292 187 TTVVVA 192
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
75-256 |
4.57e-13 |
|
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: 67.27 E-value: 4.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 75 LNAIMGPqDGS-RSLLLDVLAARRDPCglSGDILINGKPrpanfkctsgyipqndvvlgtvtvrdnlefsaalrlPMTVT 153
Cdd:cd00267 27 IVALVGP-NGSgKSTLLRAIAGLLKPT--SGEILIDGKD------------------------------------IAKLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 154 RDEKRRRINEVLELlhlekeqnvkprSKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMSMKGKTIIF 233
Cdd:cd00267 68 LEELRRRIGYVPQL------------SGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVII 135
|
170 180
....*....|....*....|...
gi 1046858258 234 SINQPQYsIFRFFDSLTLVASGK 256
Cdd:cd00267 136 VTHDPEL-AELAADRVIVLKDGK 157
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
122-265 |
3.87e-12 |
|
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: 66.41 E-value: 3.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 122 GYIPQNDVVLGTVTVRDNLefSAALRLpMTVTRDEKRRRINEVLELLHLEKEQNVKPR--SKGLRKRTSIAMELVTEHPI 199
Cdd:cd03218 78 GYLPQEASIFRKLTVEENI--LAVLEI-RGLSKKEREEKLEELLEEFHITHLRKSKASslSGGERRRVEIARALATNPKF 154
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046858258 200 LFLDDPTTGLDLRTTTDVISILRRMSMKGKTI---------IFSINQPQYSIFrffdsltlvaSGKLMFHGPARD 265
Cdd:cd03218 155 LLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVlitdhnvreTLSITDRAYIIY----------EGKVLAEGTPEE 219
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
150-261 |
1.34e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 65.41 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 150 MTVTRDEKRRRINEVLELLHLE--KEQNVKPRSKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMSMK 227
Cdd:PRK13638 106 LGVPEAEITRRVDEALTLVDAQhfRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQ 185
|
90 100 110
....*....|....*....|....*....|....
gi 1046858258 228 GKTIIFSINQPQYsIFRFFDSLTLVASGKLMFHG 261
Cdd:PRK13638 186 GNHVIISSHDIDL-IYEISDAVYVLRQGQILTHG 218
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
135-268 |
1.91e-11 |
|
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: 64.62 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 135 TVRDNLEFsaALRLPMTVTRDEKRRRINEVLELLHLEKEQNVKPR--SKGLRKRTSIAMELVTEHPILFLDDPTTGLDLR 212
Cdd:COG1127 98 TVFENVAF--PLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSelSGGMRKRVALARALALDPEILLYDEPTAGLDPI 175
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 213 TTTDVISILRRM--SMKGKTIIFS--INqpqySIFRFFDSLTLVASGKLMFHGPARDALE 268
Cdd:COG1127 176 TSAVIDELIRELrdELGLTSVVVThdLD----SAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
77-261 |
2.13e-11 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 63.67 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 77 AIMGPQDGSRSLLLDVLAARRDPCglSGDILING--------KPRPANFkctsgyIPQNDVVLGTVTVRDN--LEFSAAL 146
Cdd:cd03298 28 AIVGPSGSGKSTLLNLIAGFETPQ--SGRVLINGvdvtaappADRPVSM------LFQENNLFAHLTVEQNvgLGLSPGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 147 RLpmtvtRDEKRRRINEVLELLHLEKEQNVKPR--SKGLRKRTSIAMELVTEHPILFLDDPTTGLD--LRT-TTDVISIL 221
Cdd:cd03298 100 KL-----TAEDRQAIEVALARVGLAGLEKRLPGelSGGERQRVALARVLVRDKPVLLLDEPFAALDpaLRAeMLDLVLDL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1046858258 222 RRmsMKGKTIIFSINQPQySIFRFFDSLTLVASGKLMFHG 261
Cdd:cd03298 175 HA--ETKMTVLMVTHQPE-DAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
126-265 |
3.23e-11 |
|
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: 63.61 E-value: 3.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 126 QNDVVLGTVTVRDNLEFSAALRLPMTV-------TRDEKRRRINEVLELLHLEKEQNVKPR--SKGLRKRTSIAMELVTE 196
Cdd:cd03219 82 QIPRLFPELTVLENVMVAAQARTGSGLllararrEEREARERAEELLERVGLADLADRPAGelSYGQQRRLEIARALATD 161
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046858258 197 HPILFLDDPTTGLDLRTTTDVISILRRMSMKGKTIIFsINQPQYSIFRFFDSLTLVASGKLMFHGPARD 265
Cdd:cd03219 162 PKLLLLDEPAAGLNPEETEELAELIRELRERGITVLL-VEHDMDVVMSLADRVTVLDQGRVIAEGTPDE 229
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
77-256 |
3.52e-11 |
|
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: 62.20 E-value: 3.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 77 AIMGPQDGSRSLLLDVLAarrdpcGL----SGDILINGKP------RPANFKCTSGYIPQNDVVLGTVTVRDNLEFsaal 146
Cdd:cd03229 30 ALLGPSGSGKSTLLRCIA------GLeepdSGSILIDGEDltdledELPPLRRRIGMVFQDFALFPHLTVLENIAL---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 147 rlpmtvtrdekrrrinevlellhlekeqnvkPRSKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRM-S 225
Cdd:cd03229 100 -------------------------------GLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLqA 148
|
170 180 190
....*....|....*....|....*....|.
gi 1046858258 226 MKGKTIIFSINQPQYsIFRFFDSLTLVASGK 256
Cdd:cd03229 149 QLGITVVLVTHDLDE-AARLADRVVVLRDGK 178
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
75-224 |
4.37e-11 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 63.51 E-value: 4.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 75 LNAIMGPQDGSRSLLLDVLAARRDPCglSGDILINGK------PRPANFkctsGYIPQNDVVLGTVTVRDNLEFsaALRL 148
Cdd:cd03296 30 LVALLGPSGSGKTTLLRLIAGLERPD--SGTILFGGEdatdvpVQERNV----GFVFQHYALFRHMTVFDNVAF--GLRV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 149 PMTVTR---DEKRRRINEVLELLHLEKEQNVKPR--SKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRR 223
Cdd:cd03296 102 KPRSERppeAEIRAKVHELLKLVQLDWLADRYPAqlSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRR 181
|
.
gi 1046858258 224 M 224
Cdd:cd03296 182 L 182
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
77-233 |
5.21e-11 |
|
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: 63.02 E-value: 5.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 77 AIMGPQDGSRSLLLDVLAARRDPCglSGDILINGKP---RPANfKCTSGYIPQNDVVLGTVTVRDNLEFsaALRLpMTVT 153
Cdd:cd03300 30 TLLGPSGCGKTTLLRLIAGFETPT--SGEILLDGKDitnLPPH-KRPVNTVFQNYALFPHLTVFENIAF--GLRL-KKLP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 154 RDEKRRRINEVLELLHLEKEQNVKPR--SKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMSMK-GKT 230
Cdd:cd03300 104 KAEIKERVAEALDLVQLEGYANRKPSqlSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKElGIT 183
|
...
gi 1046858258 231 IIF 233
Cdd:cd03300 184 FVF 186
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
77-265 |
6.97e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 63.56 E-value: 6.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 77 AIMGPQDGSRSLLLDVLAARRDPCglSGDILINGKPRP------ANFKCTSGYIPQN-DVVLGTVTVRDNLEFSAalrLP 149
Cdd:PRK13639 32 ALLGPNGAGKSTLFLHFNGILKPT--SGEVLIKGEPIKydkkslLEVRKTVGIVFQNpDDQLFAPTVEEDVAFGP---LN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 150 MTVTRDEKRRRINEVLELLHLEKEQNVKPR--SKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMSMK 227
Cdd:PRK13639 107 LGLSKEEVEKRVKEALKAVGMEGFENKPPHhlSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE 186
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1046858258 228 GKTIIFSINQ----PQYSifrffDSLTLVASGKLMFHGPARD 265
Cdd:PRK13639 187 GITIIISTHDvdlvPVYA-----DKVYVMSDGKIIKEGTPKE 223
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
77-263 |
2.16e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 61.73 E-value: 2.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 77 AIMGPQDGSRSLLLDVLAARRDPCglSGDILINGKPRPA----NFKCTSGYIPQNDVVLGTVTVRdnlEFSAALRLP--- 149
Cdd:PRK10575 41 GLIGHNGSGKSTLLKMLGRHQPPS--EGEILLDAQPLESwsskAFARKVAYLPQQLPAAEGMTVR---ELVAIGRYPwhg 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 150 -MTVTRDEKRRRINEVLELLHLEKEQN--VKPRSKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMS- 225
Cdd:PRK10575 116 aLGRFGAADREKVEEAISLVGLKPLAHrlVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSq 195
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1046858258 226 MKGKTII---FSINQPQysifRFFDSLTLVASGKLMFHGPA 263
Cdd:PRK10575 196 ERGLTVIavlHDINMAA----RYCDYLVALRGGEMIAQGTP 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
100-233 |
3.42e-10 |
|
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: 63.00 E-value: 3.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 100 CGL----SGDILINGKPRPANFKCTS-------GYIPQN-DVVL-GTVTVRDNLEFsaALRLPMTVTRDEKRRRINEVLE 166
Cdd:COG1123 312 LGLlrptSGSILFDGKDLTKLSRRSLrelrrrvQMVFQDpYSSLnPRMTVGDIIAE--PLRLHGLLSRAERRERVAELLE 389
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046858258 167 LLHLEKEQ-NVKPR--SKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMS-MKGKTIIF 233
Cdd:COG1123 390 RVGLPPDLaDRYPHelSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQrELGLTYLF 460
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
46-261 |
6.50e-10 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 60.04 E-value: 6.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 46 ETVQSGFplRQQTRVMERLSSISGIMGPG-LNAIMGPQDGSRSLLLDVLAARRDPCglSGDILINGKpRPanFKCTSGYI 124
Cdd:cd03267 21 GSLKSLF--KRKYREVEALKGISFTIEKGeIVGFIGPNGAGKTTTLKILSGLLQPT--SGEVRVAGL-VP--WKRRKKFL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 125 PQNDVVLGTVT-------VRDNLEFSAAL-RLPmtvtRDEKRRRINEVLELLHLEKE--QNVKPRSKGLRKRTSIAMELV 194
Cdd:cd03267 94 RRIGVVFGQKTqlwwdlpVIDSFYLLAAIyDLP----PARFKKRLDELSELLDLEELldTPVRQLSLGQRMRAEIAAALL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046858258 195 TEHPILFLDDPTTGLDLRTTTDVISILRRMSMKGKTIIFSINQPQYSIFRFFDSLTLVASGKLMFHG 261
Cdd:cd03267 170 HEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
77-265 |
1.24e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 59.61 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 77 AIMGPQDGSRSLLLDVLAARRDPcgLSGDILINGK--PRPANFKCTS--GYIPQNDVVLGTVTVRdnlEFSAALRLP--- 149
Cdd:PRK10253 37 AIIGPNGCGKSTLLRTLSRLMTP--AHGHVWLDGEhiQHYASKEVARriGLLAQNATTPGDITVQ---ELVARGRYPhqp 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 150 -MTVTRDEKRRRINEVLE---LLHLEKeQNVKPRSKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMS 225
Cdd:PRK10253 112 lFTRWRKEDEEAVTKAMQatgITHLAD-QSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELN 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1046858258 226 M-KGKT---IIFSINQPqysiFRFFDSLTLVASGKLMFHGPARD 265
Cdd:PRK10253 191 ReKGYTlaaVLHDLNQA----CRYASHLIALREGKIVAQGAPKE 230
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
89-265 |
1.59e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 59.35 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 89 LLDVLAArrDpcglSGDILINGKPRPANFKCTSGYIP------QNdvvlgtVTVRDNLEFSAALRlpmTVTRDEKRRRIN 162
Cdd:COG4152 47 ILGILAP--D----SGEVLWDGEPLDPEDRRRIGYLPeerglyPK------MKVGEQLVYLARLK---GLSKAEAKRRAD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 163 EVLELLHLEKEQNVKPR--SKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMSMKGKTIIFSINQPQy 240
Cdd:COG4152 112 EWLERLGLGDRANKKVEelSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQME- 190
|
170 180
....*....|....*....|....*
gi 1046858258 241 SIFRFFDSLTLVASGKLMFHGPARD 265
Cdd:COG4152 191 LVEELCDRIVIINKGRKVLSGSVDE 215
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
77-265 |
1.73e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 59.09 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 77 AIMGPQDGSRSLLLDVLAARRDPCglSGDILINGKPRP------ANFKCTSGYIPQN-DVVLGTVTVRDNLEFSAA-LRL 148
Cdd:PRK13636 36 AILGGNGAGKSTLFQNLNGILKPS--SGRILFDGKPIDysrkglMKLRESVGMVFQDpDNQLFSASVYQDVSFGAVnLKL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 149 PmtvtRDEKRRRINEVLELLHLEKEQNvKPR---SKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMS 225
Cdd:PRK13636 114 P----EDEVRKRVDNALKRTGIEHLKD-KPThclSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQ 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1046858258 226 MK-GKTIIFSINQ----PQYSifrffDSLTLVASGKLMFHGPARD 265
Cdd:PRK13636 189 KElGLTIIIATHDidivPLYC-----DNVFVMKEGRVILQGNPKE 228
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
103-233 |
2.13e-09 |
|
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: 58.29 E-value: 2.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 103 SGDILINGKPRPAN-------FKCTSGYIPQN-DVVLG-TVTVRDNLEFSAALRLPMTVtRDEKRRRINEVLELLHLEKE 173
Cdd:cd03257 59 SGSIIFDGKDLLKLsrrlrkiRRKEIQMVFQDpMSSLNpRMTIGEQIAEPLRIHGKLSK-KEARKEAVLLLLVGVGLPEE 137
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046858258 174 Q-NVKPR--SKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRM-SMKGKTIIF 233
Cdd:cd03257 138 VlNRYPHelSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLqEELGLTLLF 201
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
78-234 |
2.23e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 59.46 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 78 IMGPQDGSRSLLLDVLAARRDPCglSGDILINGKPRPANFKCTS---GYIPQNDVVLGTVTVRDNL-EFSAALRLpmtvt 153
Cdd:PRK13536 72 LLGPNGAGKSTIARMILGMTSPD--AGKITVLGVPVPARARLARariGVVPQFDNLDLEFTVRENLlVFGRYFGM----- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 154 rdeKRRRINEV----LELLHLEKEQN--VKPRSKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMSMK 227
Cdd:PRK13536 145 ---STREIEAVipslLEFARLESKADarVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLAR 221
|
....*..
gi 1046858258 228 GKTIIFS 234
Cdd:PRK13536 222 GKTILLT 228
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
75-261 |
2.41e-09 |
|
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: 60.80 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 75 LNAIMGPQDGSRSLLLDVLAARRDPCglSGDILINGKPRPANF---KCTSGYIPQNDVVLGTVTVRDNLEFSAALRlpmT 151
Cdd:TIGR01257 958 ITAFLGHNGAGKTTTLSILTGLLPPT--SGTVLVGGKDIETNLdavRQSLGMCPQHNILFHHLTVAEHILFYAQLK---G 1032
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 152 VTRDEKRRRINEVLEL--LHLEKEQNVKPRSKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMSmKGK 229
Cdd:TIGR01257 1033 RSWEEAQLEMEAMLEDtgLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYR-SGR 1111
|
170 180 190
....*....|....*....|....*....|..
gi 1046858258 230 TIIFSINQPQYSIFrFFDSLTLVASGKLMFHG 261
Cdd:TIGR01257 1112 TIIMSTHHMDEADL-LGDRIAIISQGRLYCSG 1142
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
77-237 |
2.64e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 58.66 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 77 AIMGPQDGSRSLLLDVLAARRDPCglSGDILINGKP-RPANFK---CTSGYIPQN-DVVLGTVTVRDNLEFSaalrlPMT 151
Cdd:PRK13652 34 AVIGPNGAGKSTLFRHFNGILKPT--SGSVLIRGEPiTKENIRevrKFVGLVFQNpDDQIFSPTVEQDIAFG-----PIN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 152 VTRDEK--RRRINEVLELLHLEKEQNVKPR--SKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMSMK 227
Cdd:PRK13652 107 LGLDEEtvAHRVSSALHMLGLEELRDRVPHhlSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPET 186
|
170
....*....|.
gi 1046858258 228 -GKTIIFSINQ 237
Cdd:PRK13652 187 yGMTVIFSTHQ 197
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
78-234 |
3.01e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 58.66 E-value: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 78 IMGPQDGSRSLLLDVLAARRDPcgLSGDILINGKPRPANFKCTS---GYIPQNDVVLGTVTVRDNLE-FSAALRLPMTvt 153
Cdd:PRK13537 38 LLGPNGAGKTTTLRMLLGLTHP--DAGSISLCGEPVPSRARHARqrvGVVPQFDNLDPDFTVRENLLvFGRYFGLSAA-- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 154 rdEKRRRINEVLELLHLEKEQNVKPR--SKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMSMKGKTI 231
Cdd:PRK13537 114 --AARALVPPLLEFAKLENKADAKVGelSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTI 191
|
...
gi 1046858258 232 IFS 234
Cdd:PRK13537 192 LLT 194
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
77-261 |
6.78e-09 |
|
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: 55.78 E-value: 6.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 77 AIMGPQDGSRSLLLDVLAARRDPcgLSGDILINGKPRPANFKCTSGYIpqndvvlGTVTVRDNLeFSAALRlpmtvtrde 156
Cdd:cd03247 32 ALLGRSGSGKSTLLQLLTGDLKP--QQGEITLDGVPVSDLEKALSSLI-------SVLNQRPYL-FDTTLR--------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 157 krrrinevlellhlekeQNVKPR-SKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMsMKGKTIIFsI 235
Cdd:cd03247 93 -----------------NNLGRRfSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEV-LKDKTLIW-I 153
|
170 180
....*....|....*....|....*.
gi 1046858258 236 NQPQYSIFRfFDSLTLVASGKLMFHG 261
Cdd:cd03247 154 THHLTGIEH-MDKILFLENGKIIMQG 178
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
142-267 |
7.44e-09 |
|
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: 57.02 E-value: 7.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 142 FSAALRLPMTVTrDEKRRRINEVLELLHLE--KEQNVKPRSKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVIS 219
Cdd:COG1119 105 FFDSIGLYREPT-DEQRERARELLELLGLAhlADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLA 183
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1046858258 220 ILRRMSMKG-KTIIFSINQPQYsIFRFFDSLTLVASGKLMFHGPARDAL 267
Cdd:COG1119 184 LLDKLAAEGaPTLVLVTHHVEE-IPPGITHVLLLKDGRVVAAGPKEEVL 231
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
77-232 |
1.32e-08 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 57.15 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 77 AIMGPQDGSRSLLLDVLAARRDPCglSGDILINGKP--------RPANFkctsgyIPQNDVVLGTVTVRDNLEFSAAL-R 147
Cdd:PRK11607 49 ALLGASGCGKSTLLRMLAGFEQPT--AGQIMLDGVDlshvppyqRPINM------MFQSYALFPHMTVEQNIAFGLKQdK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 148 LPmtvtRDEKRRRINEVLELLHLEKEQNVKPR--SKGLRKRTSIAMELVTEHPILFLDDPTTGLDL----RTTTDVISIL 221
Cdd:PRK11607 121 LP----KAEIASRVNEMLGLVHMQEFAKRKPHqlSGGQRQRVALARSLAKRPKLLLLDEPMGALDKklrdRMQLEVVDIL 196
|
170 180
....*....|....*....|....*.
gi 1046858258 222 RR---------------MSMKGKTII 232
Cdd:PRK11607 197 ERvgvtcvmvthdqeeaMTMAGRIAI 222
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
150-261 |
1.42e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 57.05 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 150 MTVTRDEKRRRINEVLELLHLEKE--QNVKPRSKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMSMK 227
Cdd:NF000106 114 LDLSRKDARARADELLERFSLTEAagRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD 193
|
90 100 110
....*....|....*....|....*....|....
gi 1046858258 228 GKTIIFSiNQPQYSIFRFFDSLTLVASGKLMFHG 261
Cdd:NF000106 194 GATVLLT-TQYMEEAEQLAHELTVIDRGRVIADG 226
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
122-267 |
1.72e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 55.67 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 122 GYIPQNDVVLGTVTVRDNLefSAALRLPMTVTRDEKRRRINEVLELLHLEKEQNV--KPRSKGLRKRTSIAMELVTEHPI 199
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNL--MAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSmgQSLSGGERRRVEIARALAANPKF 158
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046858258 200 LFLDDPTTGLDLRTTTDVISILRRMSMKGKTIIFSINQPQYSIfRFFDSLTLVASGKLMFHGPARDAL 267
Cdd:PRK10895 159 ILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETL-AVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
35-239 |
6.00e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 55.89 E-value: 6.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 35 AVLSFHNIsyRETVQSGfplRQQTRVmerLSSISGIMGPG-LNAIMGPQDGSRSLLLDVLA------------ARRDPCG 101
Cdd:PRK10535 3 ALLELKDI--RRSYPSG---EEQVEV---LKGISLDIYAGeMVAIVGASGSGKSTLMNILGcldkptsgtyrvAGQDVAT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 102 LSGDILinGKPRPANFkctsGYIPQNDVVLGTVTVRDNLEFSAALrlpMTVTRDEKRRRINEVLELLHLEKEQNVKPR-- 179
Cdd:PRK10535 75 LDADAL--AQLRREHF----GFIFQRYHLLSHLTAAQNVEVPAVY---AGLERKQRLLRAQELLQRLGLEDRVEYQPSql 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 180 SKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMSMKGKTIIFSINQPQ 239
Cdd:PRK10535 146 SGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQ 205
|
|
| ABC2_membrane_7 |
pfam19055 |
ABC-2 type transporter; |
237-293 |
7.48e-08 |
|
ABC-2 type transporter;
Pssm-ID: 465963 [Multi-domain] Cd Length: 409 Bit Score: 54.91 E-value: 7.48e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1046858258 237 QPQYSIFRFFDSLTLVASGKLM-FHGPARDALEYFTSAGYQYESHNNPADFFLDVING 293
Cdd:pfam19055 2 QPSYTLFKMFDDLILLAKGGLTvYHGPVKKVEEYFAGLGINVPERVNPPDHFIDILEG 59
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
67-232 |
8.30e-08 |
|
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: 53.21 E-value: 8.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 67 ISGIMGP---G----LNAIMGpqdgsrsllldvLAARRdpcglSGDILINGKP---RPANFKCTSG--YIPQNDVVLGTV 134
Cdd:cd03224 28 IVALLGRngaGkttlLKTIMG------------LLPPR-----SGSIRFDGRDitgLPPHERARAGigYVPEGRRIFPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 135 TVRDNLEFSAALRlpmtvTRDEKRRRINEVLELLhlekeqnvkPRSKGLRKR------------TSIAMELVTEHPILFL 202
Cdd:cd03224 91 TVEENLLLGAYAR-----RRAKRKARLERVYELF---------PRLKERRKQlagtlsggeqqmLAIARALMSRPKLLLL 156
|
170 180 190
....*....|....*....|....*....|
gi 1046858258 203 DDPTTGLDLRTTTDVISILRRMSMKGKTII 232
Cdd:cd03224 157 DEPSEGLAPKIVEEIFEAIRELRDEGVTIL 186
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
64-230 |
1.22e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 52.90 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 64 LSSISGIMGPG-LNAIMGPQDGSRSLLLDVLAARRDPCglSGDILINGKP--------RPANFKCTSGYIPQNDVVLGTV 134
Cdd:PRK11629 25 LHNVSFSIGEGeMMAIVGSSGSGKSTLLHLLGGLDTPT--SGDVIFNGQPmsklssaaKAELRNQKLGFIYQFHHLLPDF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 135 TVRDNLefsAALRLPMTVTRDEKRRRINEVLELLHLEKEQNVKPR--SKGLRKRTSIAMELVTEHPILFLDDPTTGLDLR 212
Cdd:PRK11629 103 TALENV---AMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSelSGGERQRVAIARALVNNPRLVLADEPTGNLDAR 179
|
170
....*....|....*...
gi 1046858258 213 TTTDVISILRRMSMKGKT 230
Cdd:PRK11629 180 NADSIFQLLGELNRLQGT 197
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
34-257 |
1.69e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.15 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 34 EAVLSFHNISyretvqSGFPlrqqtrVMERLSSISGIMGPG-LNAIMGPQDGSRSLLLDVLAARRDPCglSGDILINGKP 112
Cdd:PRK11288 2 SPYLSFDGIG------KTFP------GVKALDDISFDCRAGqVHALMGENGAGKSTLLKILSGNYQPD--AGSILIDGQE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 113 RpaNFKCTSGYIPQNDVV----LGTV---TVRDNLEFSaalRLPMT---VTRDEKRRRINEVLELL--HLEKEQNVKPRS 180
Cdd:PRK11288 68 M--RFASTTAALAAGVAIiyqeLHLVpemTVAENLYLG---QLPHKggiVNRRLLNYEAREQLEHLgvDIDPDTPLKYLS 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046858258 181 KGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMSMKGKTIIFsINQPQYSIFRFFDSLTLVASGKL 257
Cdd:PRK11288 143 IGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILY-VSHRMEEIFALCDAITVFKDGRY 218
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
135-234 |
1.83e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 52.82 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 135 TVRDNLEFSAalrLPMTVTRDEKRRRINEVLELLHLEKEQNVKPR--SKGLRKRTSIAMELVTEHPILFLDDPTTGLDLR 212
Cdd:PRK13647 96 TVWDDVAFGP---VNMGLDKDEVERRVEEALKAVRMWDFRDKPPYhlSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPR 172
|
90 100
....*....|....*....|..
gi 1046858258 213 TTTDVISILRRMSMKGKTIIFS 234
Cdd:PRK13647 173 GQETLMEILDRLHNQGKTVIVA 194
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
77-267 |
2.08e-07 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 53.69 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 77 AIMGPQDGSRSLLLDVLAARRDPCglSGDILINGKPRPANFKCTSGY----IPQNDVVLGTVTVRDNLEFSaalRLPMTv 152
Cdd:PRK09536 33 GLVGPNGAGKTTLLRAINGTLTPT--AGTVLVAGDDVEALSARAASRrvasVPQDTSLSFEFDVRQVVEMG---RTPHR- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 153 TR-----DEKRRRINEVLELLHLEK--EQNVKPRSKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMS 225
Cdd:PRK09536 107 SRfdtwtETDRAAVERAMERTGVAQfaDRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLV 186
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1046858258 226 MKGKTIIFSINQPQYSIfRFFDSLTLVASGKLMFHGPARDAL 267
Cdd:PRK09536 187 DDGKTAVAAIHDLDLAA-RYCDELVLLADGRVRAAGPPADVL 227
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
77-238 |
2.26e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 51.80 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 77 AIMGPQDGSRSLLLDVLAarrdpcGL----SGDILINGK----PRPANfKCTsgYIPQNDVVLGTVTVRDNLEFSAALRl 148
Cdd:PRK13539 32 VLTGPNGSGKTTLLRLIA------GLlppaAGTIKLDGGdiddPDVAE-ACH--YLGHRNAMKPALTVAENLEFWAAFL- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 149 pmtvtrDEKRRRINEVLELLHLEKEQNVKPR--SKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMSM 226
Cdd:PRK13539 102 ------GGEELDIAAALEAVGLAPLAHLPFGylSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAHLA 175
|
170
....*....|..
gi 1046858258 227 KGKTIIFSINQP 238
Cdd:PRK13539 176 QGGIVIAATHIP 187
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
32-261 |
3.59e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 53.29 E-value: 3.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 32 TKEAVLSFHNISYretvqsGFPLRQQTrVMERLS-SISgimgPGLN-AIMGPQDGSRSLLLDVLAARRDPcgLSGDILIN 109
Cdd:PRK11160 334 ADQVSLTLNNVSF------TYPDQPQP-VLKGLSlQIK----AGEKvALLGRTGCGKSTLLQLLTRAWDP--QQGEILLN 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 110 GKP----RPANFKCTSGYIPQNdVVLGTVTVRDNLEFSAALrlpmtvTRDEKrrrINEVLELLHLEK-EQNVK------- 177
Cdd:PRK11160 401 GQPiadySEAALRQAISVVSQR-VHLFSATLRDNLLLAAPN------ASDEA---LIEVLQQVGLEKlLEDDKglnawlg 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 178 ----PRSKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMsMKGKTIIF------SINQpqysifrfFD 247
Cdd:PRK11160 471 eggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEH-AQNKTVLMithrltGLEQ--------FD 541
|
250
....*....|....
gi 1046858258 248 SLTLVASGKLMFHG 261
Cdd:PRK11160 542 RICVMDNGQIIEQG 555
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
103-273 |
5.02e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 51.81 E-value: 5.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 103 SGDILINGKP-RPANFKCTSGYIPQND-------VVLGTVTVRDNLEFSAALRLPmtvtRDEKRRRINEVLELLHLE--K 172
Cdd:PRK15056 61 SGKISILGQPtRQALQKNLVAYVPQSEevdwsfpVLVEDVVMMGRYGHMGWLRRA----KKRDRQIVTAALARVDMVefR 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 173 EQNVKPRSKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMSMKGKTIIFSINQPQySIFRFFDsLTLV 252
Cdd:PRK15056 137 HRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLG-SVTEFCD-YTVM 214
|
170 180
....*....|....*....|.
gi 1046858258 253 ASGKLMFHGPARDAleyFTSA 273
Cdd:PRK15056 215 VKGTVLASGPTETT---FTAE 232
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
150-232 |
7.56e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 51.24 E-value: 7.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 150 MTVTRDEKRRRINEVLELLHLEkeQNVKPRSK-----GLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRM 224
Cdd:PRK13651 134 MGVSKEEAKKRAAKYIELVGLD--ESYLQRSPfelsgGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNL 211
|
....*...
gi 1046858258 225 SMKGKTII 232
Cdd:PRK13651 212 NKQGKTII 219
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
67-233 |
7.87e-07 |
|
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: 49.74 E-value: 7.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 67 ISGIMGPGlnaimgpqdgsRSLLLDVLAARRDPcgLSGDILINGKPRPAN-----FKCTSGYIP---QNDVVLGTVTVRD 138
Cdd:cd03215 31 IAGLVGNG-----------QTELAEALFGLRPP--ASGEITLDGKPVTRRsprdaIRAGIAYVPedrKREGLVLDLSVAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 139 NLEFSAALrlpmtvtrdekrrrinevlellhlekeqnvkprSKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVI 218
Cdd:cd03215 98 NIALSSLL---------------------------------SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIY 144
|
170
....*....|....*
gi 1046858258 219 SILRRMSMKGKTIIF 233
Cdd:cd03215 145 RLIRELADAGKAVLL 159
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
78-238 |
9.05e-07 |
|
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: 49.80 E-value: 9.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 78 IMGPQDGSRSLLLDVLAARRDPcgLSGDILINGkpRPANFKCTSG-----YIPQNDVVLGTVTVRDNLEFSAAlrlpmtv 152
Cdd:cd03231 31 VTGPNGSGKTTLLRILAGLSPP--LAGRVLLNG--GPLDFQRDSIargllYLGHAPGIKTTLSVLENLRFWHA------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 153 trDEKRRRINEVLELLHLEKEQN--VKPRSKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMSMKGKT 230
Cdd:cd03231 100 --DHSDEQVEEALARVGLNGFEDrpVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGM 177
|
....*...
gi 1046858258 231 IIFSINQP 238
Cdd:cd03231 178 VVLTTHQD 185
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
77-237 |
3.42e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 48.62 E-value: 3.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 77 AIMGPQDGSRSLLLDVLAARRDpcGLSGDILINGKP--------RPANFKCTSGYIPQNDVVLGTVTVRDNLEFSAALRl 148
Cdd:PRK10584 40 ALIGESGSGKSTLLAILAGLDD--GSSGEVSLVGQPlhqmdeeaRAKLRAKHVGFVFQSFMLIPTLNALENVELPALLR- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 149 pmTVTRDEKRRRINEVLELLHLEKEQNVKPR--SKGLRKRTSIAMELVTEHPILFLDDPTTGLDlRTTTDVISILrrmsm 226
Cdd:PRK10584 117 --GESSRQSRNGAKALLEQLGLGKRLDHLPAqlSGGEQQRVALARAFNGRPDVLFADEPTGNLD-RQTGDKIADL----- 188
|
170
....*....|.
gi 1046858258 227 kgktiIFSINQ 237
Cdd:PRK10584 189 -----LFSLNR 194
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
28-211 |
4.42e-06 |
|
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: 48.24 E-value: 4.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 28 PETLtkEAVLSFHNISYretvqsGFPLRQQTRVmerLSSISGIMGPG-LNAIMGPQDGSRSLLLDVLAARRDPCGlsGDI 106
Cdd:cd03248 5 PDHL--KGIVKFQNVTF------AYPTRPDTLV---LQDVSFTLHPGeVTALVGPSGSGKSTVVALLENFYQPQG--GQV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 107 LINGKPRPANFKC----TSGYIPQNDVVLGTvTVRDNLEFSAALRLPMTVTRDEKRRRINEVLELLHLEKEQNVKPR--- 179
Cdd:cd03248 72 LLDGKPISQYEHKylhsKVSLVGQEPVLFAR-SLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKgsq 150
|
170 180 190
....*....|....*....|....*....|...
gi 1046858258 180 -SKGLRKRTSIAMELVTEHPILFLDDPTTGLDL 211
Cdd:cd03248 151 lSGGQKQRVAIARALIRNPQVLILDEATSALDA 183
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
154-261 |
5.95e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 48.47 E-value: 5.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 154 RDEKRRRINEVLELLHLEKEQNVKPR---SKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMSMKGKT 230
Cdd:PRK13645 123 KQEAYKKVPELLKLVQLPEDYVKRSPfelSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKK 202
|
90 100 110
....*....|....*....|....*....|.
gi 1046858258 231 IIFSINQPQYSIFRFFDSLTLVASGKLMFHG 261
Cdd:PRK13645 203 RIIMVTHNMDQVLRIADEVIVMHEGKVISIG 233
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
77-232 |
6.41e-06 |
|
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: 48.00 E-value: 6.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 77 AIMGPQDGSRSLLLDVLAARRDPCglSGDILINGKPrPANFKCTS-----GYIPQnDVVLGTVTVRDNLEFSaalrlpmt 151
Cdd:cd03251 32 ALVGPSGSGKSTLVNLIPRFYDVD--SGRILIDGHD-VRDYTLASlrrqiGLVSQ-DVFLFNDTVAENIAYG-------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 152 vTRDEKRRRINEVLELLHLEK---------EQNVKPR----SKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVI 218
Cdd:cd03251 100 -RPGATREEVEEAARAANAHEfimelpegyDTVIGERgvklSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQ 178
|
170
....*....|....
gi 1046858258 219 SILRRMsMKGKTII 232
Cdd:cd03251 179 AALERL-MKNRTTF 191
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
135-210 |
6.58e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 49.35 E-value: 6.58e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046858258 135 TVRDNLEFSAAL-RLPmtvtRDEKRRRINEVLELLHLEKEQNVKPRS--KGLRKRTSIAMELVTEHPILFLDDPTTGLD 210
Cdd:NF033858 355 TVRQNLELHARLfHLP----AAEIAARVAEMLERFDLADVADALPDSlpLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
155-265 |
7.82e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 48.12 E-value: 7.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 155 DEKRRRINEVLELLHLEKEqNVKPRSK-----GLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMSMKGK 229
Cdd:PRK13637 117 EEIENRVKRAMNIVGLDYE-DYKDKSPfelsgGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYN 195
|
90 100 110
....*....|....*....|....*....|....*.
gi 1046858258 230 TIIFSINQPQYSIFRFFDSLTLVASGKLMFHGPARD 265
Cdd:PRK13637 196 MTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPRE 231
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
80-233 |
8.97e-06 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 48.49 E-value: 8.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 80 GPQDGSRSLLLDVLAARRDPCglSGDILINGK-----PrPAnfKCTSGYIPQNDVVLGTVTVRDNLEFsaALRLPmTVTR 154
Cdd:PRK11000 36 GPSGCGKSTLLRMIAGLEDIT--SGDLFIGEKrmndvP-PA--ERGVGMVFQSYALYPHLSVAENMSF--GLKLA-GAKK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 155 DEKRRRINEVLELLHLEKEQNVKPR--SKGLRKRTSIAMELVTEHPILFLDDPTTGLD--LRTTTDV-ISIL-RRMsmkG 228
Cdd:PRK11000 108 EEINQRVNQVAEVLQLAHLLDRKPKalSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaaLRVQMRIeISRLhKRL---G 184
|
....*
gi 1046858258 229 KTIIF 233
Cdd:PRK11000 185 RTMIY 189
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
152-268 |
2.01e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 47.04 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 152 VTRDEKRRRINEVLELLHLEKE---QNVKPRSKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMSMKG 228
Cdd:PRK13643 115 IPKEKAEKIAAEKLEMVGLADEfweKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSG 194
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1046858258 229 KTIIFsINQPQYSIFRFFDSLTLVASGKLMFHGPARDALE 268
Cdd:PRK13643 195 QTVVL-VTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
78-233 |
2.71e-05 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 46.86 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 78 IMGPQDGSRSLLLDVLAARRDPCglSGDILINGK-----P---RPAN--FkctsgyipQNDVVLGTVTVRDNLEFsaALR 147
Cdd:PRK09452 45 LLGPSGCGKTTVLRLIAGFETPD--SGRIMLDGQdithvPaenRHVNtvF--------QSYALFPHMTVFENVAF--GLR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 148 LpMTVTRDEKRRRINEVLELLHLEKEQNVKPR--SKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMS 225
Cdd:PRK09452 113 M-QKTPAAEITPRVMEALRMVQLEEFAQRKPHqlSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQ 191
|
....*....
gi 1046858258 226 MK-GKTIIF 233
Cdd:PRK09452 192 RKlGITFVF 200
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-262 |
4.17e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 45.86 E-value: 4.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 17 QGDLPETNTSDPETLTKEAVLSFHNISYRETVQSGFPLRQQTrvmerlssisgimgpglnAIMGPQDGSRSLLLDVLAAR 96
Cdd:PRK14271 9 QSGAADVDAAAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVT------------------SLMGPTGSGKTTFLRTLNRM 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 97 RDPCG---LSGDILINGKP-----RPANFKCTSGYIPQNDVVLgTVTVRDNLefSAALRLPMTVTRDEKR----RRINEV 164
Cdd:PRK14271 71 NDKVSgyrYSGDVLLGGRSifnyrDVLEFRRRVGMLFQRPNPF-PMSIMDNV--LAGVRAHKLVPRKEFRgvaqARLTEV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 165 LELLHLEKEQNVKP--RSKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMSMKGKTIIFSINQPQYSi 242
Cdd:PRK14271 148 GLWDAVKDRLSDSPfrLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAA- 226
|
250 260
....*....|....*....|
gi 1046858258 243 fRFFDSLTLVASGKLMFHGP 262
Cdd:PRK14271 227 -RISDRAALFFDGRLVEEGP 245
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
135-232 |
4.56e-05 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 45.46 E-value: 4.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 135 TVRDNLEFSaalRLPMTVTR--DEKRRRINEVLELLHLE--KEQNVKPRSKGLRKRTSIAMELVTEHPILFLDDPTTGLD 210
Cdd:COG4604 91 TVRELVAFG---RFPYSKGRltAEDREIIDEAIAYLDLEdlADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLD 167
|
90 100
....*....|....*....|...
gi 1046858258 211 LRTTTDVISILRRMS-MKGKTII 232
Cdd:COG4604 168 MKHSVQMMKLLRRLAdELGKTVV 190
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
64-213 |
4.67e-05 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 45.46 E-value: 4.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 64 LSSISGIMGPG-LNAIMGPQDGSRSLLLDVLAARRDPCglSGDILINGKP--RPAnfkCTSGYIPQNDVVLGTVTVRDNL 140
Cdd:PRK11248 17 LEDINLTLESGeLLVVLGPSGCGKTTLLNLIAGFVPYQ--HGSITLDGKPveGPG---AERGVVFQNEGLLPWRNVQDNV 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046858258 141 EFSAALRlpmTVTRDEKRRRINEVLELLHLEKEQNVKP--RSKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRT 213
Cdd:PRK11248 92 AFGLQLA---GVEKMQRLEIAHQMLKKVGLEGAEKRYIwqLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT 163
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-232 |
4.79e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 46.32 E-value: 4.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 4 SNDPIVIPMIERRQGDLPETNTSDPETLTKEAVLSFHNISYRETVQS---GFPLRQQtrvmERLSsISGIMGPG----LN 76
Cdd:PRK09700 233 SNDDIVRLMVGRELQNRFNAMKENVSNLAHETVFEVRNVTSRDRKKVrdiSFSVCRG----EILG-FAGLVGSGrtelMN 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 77 AIMGPqdgsrsllldvlaarrDPCgLSGDILINGK---PRPA--NFKCTSGYIPQN---DVVLGTVTVRDNLEFSAALRL 148
Cdd:PRK09700 308 CLFGV----------------DKR-AGGEIRLNGKdisPRSPldAVKKGMAYITESrrdNGFFPNFSIAQNMAISRSLKD 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 149 -----PMTVTRDEKRRRINEVL-ELLHLE---KEQNVKPRSKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVIS 219
Cdd:PRK09700 371 ggykgAMGLFHEVDEQRTAENQrELLALKchsVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYK 450
|
250
....*....|...
gi 1046858258 220 ILRRMSMKGKTII 232
Cdd:PRK09700 451 VMRQLADDGKVIL 463
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
103-233 |
7.41e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 45.08 E-value: 7.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 103 SGDILINGkprpanfkctsgYIPQND---------VVLGT-------VTVRDNLEFSAAL-RLPmtvtRDEKRRRINEVL 165
Cdd:COG4586 76 SGEVRVLG------------YVPFKRrkefarrigVVFGQrsqlwwdLPAIDSFRLLKAIyRIP----DAEYKKRLDELV 139
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 166 ELLHLEKEQNVKPR--SKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMSMKGKTIIF 233
Cdd:COG4586 140 ELLDLGELLDTPVRqlSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTIL 209
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
77-212 |
7.78e-05 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 44.57 E-value: 7.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 77 AIMGPQDGSRSLLLDVLAARRDPCglSGDILINGKP--------RPAN--FkctsgyipQNDVVLGTVTVRDN--LEFSA 144
Cdd:PRK10771 29 AILGPSGAGKSTLLNLIAGFLTPA--SGSLTLNGQDhtttppsrRPVSmlF--------QENNLFSHLTVAQNigLGLNP 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046858258 145 ALRLpmtvtRDEKRRRINEVLELLHLEKEQNVKPR--SKGLRKRTSIAMELVTEHPILFLDDPTTGLD--LR 212
Cdd:PRK10771 99 GLKL-----NAAQREKLHAIARQMGIEDLLARLPGqlSGGQRQRVALARCLVREQPILLLDEPFSALDpaLR 165
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
135-233 |
7.85e-05 |
|
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: 45.04 E-value: 7.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 135 TVRDNLEfsAALRLPMTVTRDEKRRRINEVLELLHLEKEQNVKPR-----SKGLRKRTSIAMELVTEHPILFLDDPTTGL 209
Cdd:COG0444 104 TVGDQIA--EPLRIHGGLSKAEARERAIELLERVGLPDPERRLDRyphelSGGMRQRVMIARALALEPKLLIADEPTTAL 181
|
90 100
....*....|....*....|....*
gi 1046858258 210 DLRTTTDVISILRRMSMK-GKTIIF 233
Cdd:COG0444 182 DVTIQAQILNLLKDLQRElGLAILF 206
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
125-235 |
9.53e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 44.79 E-value: 9.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 125 PQNDVVlgTVTVRDNLEFSAALRlpmTVTRDEKRRRINEVLELLHLEKEQNVKPR--SKGLRKRTSIAMELVTEHPILFL 202
Cdd:PRK13640 93 PDNQFV--GATVGDDVAFGLENR---AVPRPEMIKIVRDVLADVGMLDYIDSEPAnlSGGQKQRVAIAGILAVEPKIIIL 167
|
90 100 110
....*....|....*....|....*....|...
gi 1046858258 203 DDPTTGLDLRTTTDVISILRRMSMKGKTIIFSI 235
Cdd:PRK13640 168 DESTSMLDPAGKEQILKLIRKLKKKNNLTVISI 200
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
152-232 |
9.94e-05 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 44.57 E-value: 9.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 152 VTRDEKRRRINEVLELLHLEKEQNVK---PRSKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMSMKG 228
Cdd:PRK10619 123 LSKQEARERAVKYLAKVGIDERAQGKypvHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEG 202
|
....
gi 1046858258 229 KTII 232
Cdd:PRK10619 203 KTMV 206
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
160-233 |
1.12e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 45.33 E-value: 1.12e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046858258 160 RINEVLELLHLEKEQNVKPRSKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILrrMSMKGkTIIF 233
Cdd:PRK11147 138 RINEVLAQLGLDPDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL--KTFQG-SIIF 208
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
103-233 |
1.12e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 45.02 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 103 SGDILINGKPRPANfkctS---------GYIPQNDVVLGTVTVRDNL----EFSAALRLPmtvtRDEKRRRINEVLELLH 169
Cdd:COG3845 59 SGEILIDGKPVRIR----SprdaialgiGMVHQHFMLVPNLTVAENIvlglEPTKGGRLD----RKAARARIRELSERYG 130
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 170 LEkeqnVKPRSK------GLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMSMKGKTIIF 233
Cdd:COG3845 131 LD----VDPDAKvedlsvGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIF 196
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
64-265 |
1.25e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 45.16 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 64 LSSISGIMGPG-LNAIMGPQDGSRSLLLDVLAARRDPCglSGDILINGKPRPA-----NFKCTSGYIPQNDVVLGTVTVR 137
Cdd:PRK09700 21 LKSVNLTVYPGeIHALLGENGAGKSTLMKVLSGIHEPT--KGTITINNINYNKldhklAAQLGIGIIYQELSVIDELTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 138 DNLEFSaalRLPM-------TVTRDEKRRRINEVLEL--LHLEKEQNVKPRSKGLRKRTSIAMELVTEHPILFLDDPTTG 208
Cdd:PRK09700 99 ENLYIG---RHLTkkvcgvnIIDWREMRVRAAMMLLRvgLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1046858258 209 LDLRTTTDVISILRRMSMKGKTIIFsINQPQYSIFRFFDSLTLVASGKLMFHGPARD 265
Cdd:PRK09700 176 LTNKEVDYLFLIMNQLRKEGTAIVY-ISHKLAEIRRICDRYTVMKDGSSVCSGMVSD 231
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
64-223 |
1.35e-04 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 43.93 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 64 LSSISGIMGPG-LNAIMGPQDGSRSLLLDVLAARRDPCglSGDILINGKP----RPANFKCTSGYIPQNDVVLGTvTVRD 138
Cdd:PRK10247 23 LNNISFSLRAGeFKLITGPSGCGKSTLLKIVASLISPT--SGTLLFEGEDistlKPEIYRQQVSYCAQTPTLFGD-TVYD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 139 NLEFSAALRlpmTVTRDEKR-----RRINEVLELLhlekEQNVKPRSKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRT 213
Cdd:PRK10247 100 NLIFPWQIR---NQQPDPAIflddlERFALPDTIL----TKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESN 172
|
170
....*....|
gi 1046858258 214 TTDVISILRR 223
Cdd:PRK10247 173 KHNVNEIIHR 182
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
103-234 |
1.59e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 45.00 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 103 SGDILINGKPRPANFK---CTSGYIPQNDVVLGTVTVRDNLEFSAALRlpmTVTRDEKRRRINEVLELLHLE--KEQNVK 177
Cdd:TIGR01257 1993 SGDATVAGKSILTNISdvhQNMGYCPQFDAIDDLLTGREHLYLYARLR---GVPAEEIEKVANWSIQSLGLSlyADRLAG 2069
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046858258 178 PRSKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTT----TDVISILRrmsmKGKTIIFS 234
Cdd:TIGR01257 2070 TYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARrmlwNTIVSIIR----EGRAVVLT 2126
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
141-226 |
2.24e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 44.46 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 141 EFSAALRLPMTVTRDEKRRRINEVLELLHLEKEQNVKPR-----SKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTT 215
Cdd:PRK10261 126 QIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRyphqlSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQA 205
|
90
....*....|....*
gi 1046858258 216 DVISILR----RMSM 226
Cdd:PRK10261 206 QILQLIKvlqkEMSM 220
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
182-233 |
3.08e-04 |
|
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: 41.65 E-value: 3.08e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1046858258 182 GLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMSMKGKTIIF 233
Cdd:cd03216 86 GERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIF 137
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
103-233 |
3.89e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 43.47 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 103 SGDILINGKPRpaNFKCTS-------GYIPQNDVVLGTVTVRDNLEFSAALRLPMTVTRDEKRRRINEVLELLHLekeqN 175
Cdd:COG1129 58 SGEILLDGEPV--RFRSPRdaqaagiAIIHQELNLVPNLSVAENIFLGREPRRGGLIDWRAMRRRARELLARLGL----D 131
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046858258 176 VKPRSK------GLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMSMKGKTIIF 233
Cdd:COG1129 132 IDPDTPvgdlsvAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIY 195
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
152-271 |
4.40e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 42.92 E-value: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 152 VTRDEKRRRINEVLELLHLEK---EQNVKPRSKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMSMKG 228
Cdd:PRK13631 147 VKKSEAKKLAKFYLNKMGLDDsylERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANN 226
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1046858258 229 KTiIFSINQPQYSIFRFFDSLTLVASGKLMFHGparDALEYFT 271
Cdd:PRK13631 227 KT-VFVITHTMEHVLEVADEVIVMDKGKILKTG---TPYEIFT 265
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
103-232 |
6.41e-04 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 42.84 E-value: 6.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 103 SGDILINGKPrPANFKCTS-----GYIPQnDVVLGTVTVRDNLEFSAAlrlpmTVTRDEkrrrINEVLELLHLEK----- 172
Cdd:COG1132 394 SGRILIDGVD-IRDLTLESlrrqiGVVPQ-DTFLFSGTIRENIRYGRP-----DATDEE----VEEAAKAAQAHEfieal 462
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046858258 173 ----EQNVKPRSKGL----RKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMsMKGKTII 232
Cdd:COG1132 463 pdgyDTVVGERGVNLsggqRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERL-MKGRTTI 529
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
67-233 |
7.69e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 42.31 E-value: 7.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 67 ISGIMGPG----LNAIMGpqdgsrsllldvlAARRDpcglSGDILINGKPrpANFKCTS-------GYIPQN---DVVLG 132
Cdd:COG1129 283 IAGLVGAGrtelARALFG-------------ADPAD----SGEIRLDGKP--VRIRSPRdairagiAYVPEDrkgEGLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 133 TVTVRDNLEFSA--ALRLPMTVTRDEKRRRINEVLELLhlekeqNVKPRSKGLRKRT-S--------IAMELVTEHPILF 201
Cdd:COG1129 344 DLSIRENITLASldRLSRGGLLDRRRERALAEEYIKRL------RIKTPSPEQPVGNlSggnqqkvvLAKWLATDPKVLI 417
|
170 180 190
....*....|....*....|....*....|..
gi 1046858258 202 LDDPTTGLDLRTTTDVISILRRMSMKGKTIIF 233
Cdd:COG1129 418 LDEPTRGIDVGAKAEIYRLIRELAAEGKAVIV 449
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
180-265 |
1.36e-03 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 41.25 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 180 SKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMSMKGKTIIFSINQPQYSIFRFFDSLTLVASGKLMF 259
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTME 242
|
....*.
gi 1046858258 260 HGPARD 265
Cdd:PRK09473 243 YGNARD 248
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
77-224 |
1.38e-03 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 40.84 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 77 AIMGPQDGSRSL----LLDVLAA--RRdpcgLSGDILINGKP-RPANFKC-TSGYIPQN-----DVVLgtvTVRDN-LEF 142
Cdd:PRK10418 33 ALVGGSGSGKSLtcaaALGILPAgvRQ----TAGRVLLDGKPvAPCALRGrKIATIMQNprsafNPLH---TMHTHaRET 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 143 SAALRLPMTvtrdekRRRINEVLELLHLEKEQNVKPR-----SKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDV 217
Cdd:PRK10418 106 CLALGKPAD------DATLTAALEAVGLENAARVLKLypfemSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARI 179
|
....*..
gi 1046858258 218 ISILRRM 224
Cdd:PRK10418 180 LDLLESI 186
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
152-232 |
1.41e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 40.88 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 152 VTRDEKRRRINEVLELLHLEKE---QNVKPRSKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMSMKG 228
Cdd:PRK13649 116 VSQEEAEALAREKLALVGISESlfeKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSG 195
|
....
gi 1046858258 229 KTII 232
Cdd:PRK13649 196 MTIV 199
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
56-267 |
1.54e-03 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 40.69 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 56 QQTRVMERLSSISGIMGPGLNA-IMGPQDGSRSLLLDVLAarrdpcGL---SGDILINGKP----RPANFKCTSGYIPQN 127
Cdd:PRK03695 4 NDVAVSTRLGPLSAEVRAGEILhLVGPNGAGKSTLLARMA------GLlpgSGSIQFAGQPleawSAAELARHRAYLSQQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 128 DVVLGTVTVRDNLefsaALRLPMTVTRDEKRRRINEVLELLHLEK--EQNVKPRSKGLRKRTSIAMELVTEHP------- 198
Cdd:PRK03695 78 QTPPFAMPVFQYL----TLHQPDKTRTEAVASALNEVAEALGLDDklGRSVNQLSGGEWQRVRLAAVVLQVWPdinpagq 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046858258 199 ILFLDDPTTGLDLRTTTDVISILRRMSMKGKTIIFS---INQpqysIFRFFDSLTLVASGKLMFHGPARDAL 267
Cdd:PRK03695 154 LLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSshdLNH----TLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
135-267 |
1.78e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 40.74 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 135 TVRDNLEFSAA-LRLPMTvtrdEKRRRINEVLELLHLEKEQNVKPR--SKGLRKRTSIAMELVTEHPILFLDDPTTGLDL 211
Cdd:PRK13644 94 TVEEDLAFGPEnLCLPPI----EIRKRVDRALAEIGLEKYRHRSPKtlSGGQGQCVALAGILTMEPECLIFDEVTSMLDP 169
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1046858258 212 RTTTDVISILRRMSMKGKTIIFSINQPQYsiFRFFDSLTLVASGKLMFHGPARDAL 267
Cdd:PRK13644 170 DSGIAVLERIKKLHEKGKTIVYITHNLEE--LHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
152-232 |
1.85e-03 |
|
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: 40.43 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 152 VTRDEKRRRINEVLELLHLEK--EQNVKPRSKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMSMKGK 229
Cdd:cd03236 111 LKKKDERGKLDELVDQLELRHvlDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDN 190
|
...
gi 1046858258 230 TII 232
Cdd:cd03236 191 YVL 193
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
135-271 |
3.16e-03 |
|
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: 40.56 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 135 TVRDNLEFSAALRLPmtvtrDE-KRRRINEVLELLHL--EKEQNVKPR-----SKGLRKRTSIAMELVTEHPILFLDDPT 206
Cdd:TIGR03269 381 TVLDNLTEAIGLELP-----DElARMKAVITLKMVGFdeEKAEEILDKypdelSEGERHRVALAQVLIKEPRIVILDEPT 455
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046858258 207 TGLDLRTTTDVI-SILR-RMSMKGKTIIFSINQPqySIFRFFDSLTLVASGKLMFHGPARDALEYFT 271
Cdd:TIGR03269 456 GTMDPITKVDVThSILKaREEMEQTFIIVSHDMD--FVLDVCDRAALMRDGKIVKIGDPEEIVEELT 520
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
178-210 |
3.47e-03 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 39.52 E-value: 3.47e-03
10 20 30
....*....|....*....|....*....|....*
gi 1046858258 178 PR--SKGLRKRTSIAMELVTEHPILFLDDPTTGLD 210
Cdd:PRK11701 149 PTtfSGGMQQRLQIARNLVTHPRLVFMDEPTGGLD 183
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
149-265 |
3.47e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 40.00 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 149 PMT--VTRDEKRRRINEVLELLHLEKEqnVKPRSK-----GLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISIL 221
Cdd:PRK13634 111 PMNfgVSEEDAKQKAREMIELVGLPEE--LLARSPfelsgGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMF 188
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1046858258 222 RRMSM-KGKTIIFSINQPQySIFRFFDSLTLVASGKLMFHGPARD 265
Cdd:PRK13634 189 YKLHKeKGLTTVLVTHSME-DAARYADQIVVMHKGTVFLQGTPRE 232
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
180-224 |
5.01e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 40.07 E-value: 5.01e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1046858258 180 SKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRM 224
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLREL 202
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| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
173-232 |
7.97e-03 |
|
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: 37.69 E-value: 7.97e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046858258 173 EQNVKPRSKGLRKRTSIAMEL-VTEHPILF-LDDPTTGLDLRTTTDVISILRRMSMKGKTII 232
Cdd:cd03238 82 GQKLSTLSGGELQRVKLASELfSEPPGTLFiLDEPSTGLHQQDINQLLEVIKGLIDLGNTVI 143
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
180-268 |
8.58e-03 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 38.73 E-value: 8.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046858258 180 SKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMSMKGKTIIFSINQPQYSIFRFFDSLTLVASGKLMF 259
Cdd:COG4170 160 TEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVE 239
|
....*....
gi 1046858258 260 HGPARDALE 268
Cdd:COG4170 240 SGPTEQILK 248
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
180-234 |
9.02e-03 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 38.93 E-value: 9.02e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1046858258 180 SKGLRKRTSIAMELVTEHPILFLDDPTTGLDLRTTTDVISILRRMSmKGKTIIFS 234
Cdd:PRK10789 453 SGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWG-EGRTVIIS 506
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|
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