|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1-564 |
1.86e-100 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 316.99 E-value: 1.86e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 1 MCILGSSGSGKTTLLDAMSGRLGRAGTFLGEVYVNGRALRREQFQDCFSYVLQSDTLLSSLTVRETLHYTALLAIRRGNP 80
Cdd:TIGR00955 54 LAVMGSSGAGKTTLMNALAFRSPKGVKGSGSVLLNGMPIDAKEMRAISAYVQQDDLFIPTLTVREHLMFQAHLRMPRRVT 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 81 GSfQKK--VEAVMAELSLSHVADRLIGNYS-LGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVEL 157
Cdd:TIGR00955 134 KK-EKRerVDEVLQALGLRKCANTRIGVPGrVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 158 ARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGTPAEMLDFFNDCGYPCPEHSNPFDFYMDLTSVDtqsKEREIET 237
Cdd:TIGR00955 213 AQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAVPFFSDLGHPCPENYNPADFYVQVLAVI---PGSENES 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 238 SKRVQMIESAYKKSAICHKTLKNIeRMKHLKTLPMV-----PFKTKDSPGVFSKLGVLLRRVTRNLVRNKLAVITRLLQN 312
Cdd:TIGR00955 290 RERIEKICDSFAVSDIGRDMLVNT-NLWSGKAGGLVkdsenMEGIGYNASWWTQFYALLKRSWLSVLRDPLLLKVRLIQT 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 313 LIMGLF--LLFFVLRVRSnvlKGaIQDRVGLLYQFVGATPYTGMLNAVNLFPVLRAVSDQESQDGLYQKWQMMLAYALHV 390
Cdd:TIGR00955 369 MMTAILigLIYLGQGLTQ---KG-VQNINGALFLFLTNMTFQNVFPVINVFTAELPVFLRETRSGLYRVSAYFLAKTIAE 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 391 LPFSVVATMIFSSVCYWTLGLHPEVARFGYFSAALLAPHLIGEFLTLVLLGIVQNPNIVNSVVALLSIAgVLVGSGFLRN 470
Cdd:TIGR00955 445 LPLFIILPALFTSITYWMIGLRSGATHFLTFLFLVTLVANVATSFGYLISCAFSSTSMALTVGPPFVIP-FLLFGGFFIN 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 471 IQEMPIPFKIISYFTFQKYCSEILVVNEFYGL-NFTCGSSNvsvTTNPMCAFTQGIQfieKTCPGATSRFTMNFLILYSF 549
Cdd:TIGR00955 524 SDSIPVYFKWLSYLSWFRYGNEGLLINQWSDVdNIECTSAN---TTGPCPSSGEVIL---ETLSFRNADLYLDLIGLVIL 597
|
570
....*....|....*
gi 767915018 550 IPALVILGIVVFKIR 564
Cdd:TIGR00955 598 IFFFRLLAYFALRIR 612
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1-194 |
8.72e-97 |
|
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: 294.18 E-value: 8.72e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 1 MCILGSSGSGKTTLLDAMSGRLGRAGTFLGEVYVNGRALRREQFQDCFSYVLQSDTLLSSLTVRETLHYTALLAIRRGNP 80
Cdd:cd03234 36 MAILGSSGSGKTTLLDAISGRVEGGGTTSGQILFNGQPRKPDQFQKCVAYVRQDDILLPGLTVRETLTYTAILRLPRKSS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 81 GSFQKKVEAVMaelSLSHVADRLIGNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARR 160
Cdd:cd03234 116 DAIRKKRVEDV---LLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARR 192
|
170 180 190
....*....|....*....|....*....|....
gi 767915018 161 NRIVVLTIHQPRSELFQLFDKIAILSFGELIFCG 194
Cdd:cd03234 193 NRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1-523 |
4.40e-61 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 213.59 E-value: 4.40e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 1 MCILGSSGSGKTTLLDAMSGRLgRAGTFLGEVYVNGRALRREQFQDCfSYVLQSDTLLSSLTVRETLHYTALLAIrrgnP 80
Cdd:PLN03211 97 LAVLGPSGSGKSTLLNALAGRI-QGNNFTGTILANNRKPTKQILKRT-GFVTQDDILYPHLTVRETLVFCSLLRL----P 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 81 GSFQKKV-----EAVMAELSLSHVADRLIGNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLV 155
Cdd:PLN03211 171 KSLTKQEkilvaESVISELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLG 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 156 ELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGTPAEMLDFFNDCGYPCPEHSNPFDFYMDLTSVDTQS---KE 232
Cdd:PLN03211 251 SLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESVGFSPSFPMNPADFLLDLANGVCQTdgvSE 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 233 REIETSKrvQMIESAYkkSAICHKTLKNIERMKHLKTLP---MVPFKTKDSPGV--------FSKLGVLLRRV---TRNL 298
Cdd:PLN03211 331 REKPNVK--QSLVASY--NTLLAPKVKAAIEMSHFPQANarfVGSASTKEHRSSdrisistwFNQFSILLQRSlkeRKHE 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 299 VRNKLAVITRLLQNLIMGLFLLFFVLRvrsnvlkgAIQDRVGLLY---QFVGATPYTgmlNAVNLFPVLRAVSDQESQDG 375
Cdd:PLN03211 407 SFNTLRVFQVIAAALLAGLMWWHSDFR--------DVQDRLGLLFfisIFWGVFPSF---NSVFVFPQERAIFVKERASG 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 376 LYQKWQMMLAYALHVLPFSVVATMIFSSVCYWTLGLHPEVARFGYFSAALLAPHLIGEFLTLVLLGIVQNPNIVNSVVAL 455
Cdd:PLN03211 476 MYTLSSYFMARIVGDLPMELILPTIFLTVTYWMAGLKPELGAFLLTLLVLLGYVLVSQGLGLALGAAIMDAKKASTIVTV 555
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767915018 456 LSIAGVLVGsGFLrnIQEMPIPFKIISYFTFQKYCSEILvVNEFYG----LNFTCGSSNVSVTTNPMCAFTQ 523
Cdd:PLN03211 556 TMLAFVLTG-GFY--VHKLPSCMAWIKYISTTFYSYRLL-INVQYGegkrISSLLGCSLPHGSDRASCKFVE 623
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
3-194 |
2.48e-56 |
|
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: 187.76 E-value: 2.48e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLGRAGTfLGEVYVNGRALRREQFQDCFSYVLQSDTLLSSLTVRETLHYTALLAirrgnpgs 82
Cdd:cd03213 40 IMGPSGAGKSTLLNALAGRRTGLGV-SGEVLINGRPLDKRSFRKIIGYVPQDDILHPTLTVRETLMFAAKLR-------- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 83 fqkkveavmaelslshvadrlignyslgGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNR 162
Cdd:cd03213 111 ----------------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGR 162
|
170 180 190
....*....|....*....|....*....|..
gi 767915018 163 IVVLTIHQPRSELFQLFDKIAILSFGELIFCG 194
Cdd:cd03213 163 TIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
3-559 |
9.19e-51 |
|
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: 9.19e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRL-GRAGTFLGEVYVNGRALR--REQFQDCFSYVLQSDTLLSSLTVRETLHYTALLAIRRGN 79
Cdd:TIGR00956 92 VLGRPGSGCSTLLKTIASNTdGFHIGVEGVITYDGITPEeiKKHYRGDVVYNAETDVHFPHLTVGETLDFAARCKTPQNR 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 80 PGSFQKKVEA------VMAELSLSHVADRLIGNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVL 153
Cdd:TIGR00956 172 PDGVSREEYAkhiadvYMATYGLSHTRNTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRA 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 154 LVELAR-RNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGTPAEMLDFFNDCGYPCPEHSNPFDFymdLTSVdTQSKE 232
Cdd:TIGR00956 252 LKTSANiLDTTPLVAIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAKQYFEKMGFKCPDRQTTADF---LTSL-TSPAE 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 233 REI--ETSKRV----QMIESAYKKS-------AICHKTLKNIERMKHLKTLPMVPFKTKD------SPGVFSKLGVLLRR 293
Cdd:TIGR00956 328 RQIkpGYEKKVprtpQEFETYWRNSpeyaqlmKEIDEYLDRCSESDTKEAYRESHVAKQSkrtrpsSPYTVSFSMQVKYC 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 294 VTRNLVR---NKLAVITRLLQNLIMGLFLLFFVLRVRSNVLKGAIqdRVGLLYQFVGATPYTGMLNAVNLFPVlRAVSDQ 370
Cdd:TIGR00956 408 LARNFLRmkgNPSFTLFMVFGNIIMALILSSVFYNLPKNTSDFYS--RGGALFFAILFNAFSSLLEIASMYEA-RPIVEK 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 371 ESQDGLYQKWQMMLAYALHVLPFSVVATMIFSSVCYWTLGLHPEVARFGY-----FSAALLAPHL---IGEFLTLVLLGi 442
Cdd:TIGR00956 485 HRKYALYHPSADAIASIISEIPFKIIESVVFNIILYFMVNFRRTAGRFFFyllilFICTLAMSHLfrsIGAVTKTLSEA- 563
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 443 vqnpnivNSVVALLSIAGVLVgSGFLRNIQEMPIPFKIISYFTFQKYCSEILVVNEFYGLNFTC--------GSSNVSVt 514
Cdd:TIGR00956 564 -------MTPAAILLLALSIY-TGFAIPRPSMLGWSKWIYYVNPLAYAFESLMVNEFHGRRFECsqyvpsggGYDNLGV- 634
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 767915018 515 TNPMCA---------FTQGIQFIEKTCPGATSRFTMNFLILYSFIPALVILGIV 559
Cdd:TIGR00956 635 TNKVCTvvgaepgqdYVDGDDYLKLSFQYYNSHKWRNFGIIIGFTVFFFFVYIL 688
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-201 |
3.38e-43 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 154.07 E-value: 3.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 2 CILGSSGSGKTTLLDAMSGRLgRAGTflGEVYVNGRALRRE--QFQDCFSYVLQSDTLLSSLTVRETLHYTALLairRGN 79
Cdd:COG1131 30 GLLGPNGAGKTTTIRMLLGLL-RPTS--GEVRVLGEDVARDpaEVRRRIGYVPQEPALYPDLTVRENLRFFARL---YGL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 80 PGS-FQKKVEAVMAELSLSHVADRLIGNYSLGgistgERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELA 158
Cdd:COG1131 104 PRKeARERIDELLELFGLTDAADRKVGTLSGG-----MKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 767915018 159 RRNRIVVLTIHQPrSELFQLFDKIAILSFGELIFCGTPAEMLD 201
Cdd:COG1131 179 AEGKTVLLSTHYL-EEAERLCDRVAIIDKGRIVADGTPDELKA 220
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
2-201 |
5.76e-39 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 143.07 E-value: 5.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 2 CILGSSGSGKTTLLDAMSGRLgRAGTflGEVYVNGRALRRE--QFQDCFSYVLQSDTLLSSLTVRETLHYTALLairRGN 79
Cdd:COG4555 31 GLLGPNGAGKTTLLRMLAGLL-KPDS--GSILIDGEDVRKEprEARRQIGVLPDERGLYDRLTVRENIRYFAEL---YGL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 80 PGS-FQKKVEAVMAELSLSHVADRLIGNYSlggisTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELA 158
Cdd:COG4555 105 FDEeLKKRIEELIELLGLEEFLDRRVGELS-----TGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 767915018 159 RRNRIVVLTIHQPrSELFQLFDKIAILSFGELIFCGTPAEMLD 201
Cdd:COG4555 180 KEGKTVLFSSHIM-QEVEALCDRVVILHKGKVVAQGSLDELRE 221
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
3-518 |
6.74e-39 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 152.96 E-value: 6.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLGRAGTFLGEVYVNGRAlRREQFQDCFSYVLQSDTLLSSLTVRETLHYTALLaiRRGNPGS 82
Cdd:TIGR00956 794 LMGASGAGKTTLLNVLAERVTTGVITGGDRLVNGRP-LDSSFQRSIGYVQQQDLHLPTSTVRESLRFSAYL--RQPKSVS 870
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 83 FQKK---VEAVMAELSLSHVADRLIGnYSLGGISTGERRRVSIAAQLLQDPKVMLF-DEPTTGLDCMTANQIVVLLVELA 158
Cdd:TIGR00956 871 KSEKmeyVEEVIKLLEMESYADAVVG-VPGEGLNVEQRKRLTIGVELVAKPKLLLFlDEPTSGLDSQTAWSICKLMRKLA 949
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 159 RRNRIVVLTIHQPRSELFQLFDKIAILSFG-ELIFCGTPAE----MLDFFNDCGYP-CPEHSNPFDFYMDLTSVDTqske 232
Cdd:TIGR00956 950 DHGQAILCTIHQPSAILFEEFDRLLLLQKGgQTVYFGDLGEnshtIINYFEKHGAPkCPEDANPAEWMLEVIGAAP---- 1025
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 233 reieTSKRVQMIESAYKKSAICHKTLKNIERM-KHLKTLPMVPFKTKDSPGVFSKLGVLLRRVTRNLV---RNKLAVITR 308
Cdd:TIGR00956 1026 ----GAHANQDYHEVWRNSSEYQAVKNELDRLeAELSKAEDDNDPDALSKYAASLWYQFKLVLWRTFQqywRTPDYLYSK 1101
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 309 LLQNLIMGLFLLFFVLRVRSNvLKGaIQDRVGLLYQFVgaTPYTGMLNA-VNLFPVLRAVSD-QESQDGLYQKWQMMLAY 386
Cdd:TIGR00956 1102 FFLTIFAALFIGFTFFKVGTS-LQG-LQNQMFAVFMAT--VLFNPLIQQyLPPFVAQRDLYEvRERPSRTFSWLAFIAAQ 1177
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 387 ALHVLPFSVVATMIFSSVCYWTLGLHPEVA-------RFGYFSAALLAPHLIgeFLTLVLLGIVQNPNIVN-SVVALLSI 458
Cdd:TIGR00956 1178 ITVEIPYNLVAGTIFFFIWYYPVGFYWNASktgqvheRGVLFWLLSTMFFLY--FSTLGQMVISFNPNADNaAVLASLLF 1255
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767915018 459 AGVLVGSGFLRNIQEMPiPFKIISY----FTfqkYCSEILVVNEFYGLNFTCGSSNVSVTTNPM 518
Cdd:TIGR00956 1256 TMCLSFCGVLAPPSRMP-GFWIFMYrcspFT---YLVQALLSTGLADVPVTCKVKELLTFNPPS 1315
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
3-500 |
1.04e-36 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 146.53 E-value: 1.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLGRAGTFLGEVYVNGRALRREQFQDCFSYVLQSDTLLSSLTVRETLHYTAL---------- 72
Cdd:PLN03140 196 LLGPPSSGKTTLLLALAGKLDPSLKVSGEITYNGYRLNEFVPRKTSAYISQNDVHVGVMTVKETLDFSARcqgvgtrydl 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 73 ---LAIRRGNPGSF-QKKVEAVMAELSLSHVADRLIGNYSLG------------------GISTGERRRVSIAAQLLQDP 130
Cdd:PLN03140 276 lseLARREKDAGIFpEAEVDLFMKATAMEGVKSSLITDYTLKilgldickdtivgdemirGISGGQKKRVTTGEMIVGPT 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 131 KVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVL-TIHQPRSELFQLFDKIAILSFGELIFCGTPAEMLDFFNDCGYP 209
Cdd:PLN03140 356 KTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLmSLLQPAPETFDLFDDIILLSEGQIVYQGPRDHILEFFESCGFK 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 210 CPEHSNPFDFYMDLTS--------VDTQSKEREIETSKRVQMIESAYKKSaichktlknieRMKHLKTLPMVPFKTKDSP 281
Cdd:PLN03140 436 CPERKGTADFLQEVTSkkdqeqywADRNKPYRYISVSEFAERFKSFHVGM-----------QLENELSVPFDKSQSHKAA 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 282 GVFSKLGVLLRRVTRN--------LVRNKLAVITRLLQNLIMGLFLLFFVLRVR---SNVLKGAIqdrvgllyqFVGATP 350
Cdd:PLN03140 505 LVFSKYSVPKMELLKAcwdkewllMKRNAFVYVFKTVQIIIVAAIASTVFLRTEmhtRNEEDGAL---------YIGALL 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 351 YTGMLNAVNLFPVLRAVSDQ-----ESQDGLYQ-KWQMMLAYALHVLPFSVVATMIFSSVCYWTLGLHPEVARFgyFSAA 424
Cdd:PLN03140 576 FSMIINMFNGFAELALMIQRlpvfyKQRDLLFHpPWTFTLPTFLLGIPISIIESVVWVVITYYSIGFAPEASRF--FKQL 653
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767915018 425 LLApHLIGEF---LTLVLLGIVQNPNIVNSVVALLSIAGVLVGsGFLRNIQEMPIPFKIISYFTFQKYCSEILVVNEFY 500
Cdd:PLN03140 654 LLV-FLIQQMaagIFRLIASVCRTMIIANTGGALVLLLVFLLG-GFILPKGEIPNWWEWAYWVSPLSYGFNALAVNEMF 730
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1-198 |
3.10e-35 |
|
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: 131.86 E-value: 3.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 1 MCILGSSGSGKTTLLDAMSGRLgRAGTflGEVYVNGRALR--REQFQDCFSYVLQSDTLLSSLTVRETLHYTALLairRG 78
Cdd:cd03263 31 FGLLGHNGAGKTTTLKMLTGEL-RPTS--GTAYINGYSIRtdRKAARQSLGYCPQFDALFDELTVREHLRFYARL---KG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 79 NPGSFQKK-VEAVMAELSLSHVADRLIGNYSlggisTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVEL 157
Cdd:cd03263 105 LPKSEIKEeVELLLRVLGLTDKANKRARTLS-----GGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEV 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 767915018 158 aRRNRIVVLTIHQPRsELFQLFDKIAILSFGELIFCGTPAE 198
Cdd:cd03263 180 -RKGRSIILTTHSMD-EAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
3-194 |
4.47e-35 |
|
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: 130.44 E-value: 4.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRlGRAGTFLGEVYVNGRALRrEQFQDCFSYVLQSDTLLSSLTVRETLHYTALLAirrgnpgs 82
Cdd:cd03232 38 LMGESGAGKTTLLDVLAGR-KTAGVITGEILINGRPLD-KNFQRSTGYVEQQDVHSPNLTVREALRFSALLR-------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 83 fqkkveavmaelslshvadrlignyslgGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNR 162
Cdd:cd03232 108 ----------------------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQ 159
|
170 180 190
....*....|....*....|....*....|...
gi 767915018 163 IVVLTIHQPRSELFQLFDKIAIL-SFGELIFCG 194
Cdd:cd03232 160 AILCTIHQPSASIFEKFDRLLLLkRGGKTVYFG 192
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
2-201 |
2.09e-34 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 130.55 E-value: 2.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 2 CILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRAL----RREQFQdCFSYVLQSDTLLSSLTVRETLhytaLLAiRR 77
Cdd:COG1120 31 ALLGPNGSGKSTLLRALAGLLKPSS---GEVLLDGRDLaslsRRELAR-RIAYVPQEPPAPFGLTVRELV----ALG-RY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 78 GNPGSFQK-------KVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDcmTANQI 150
Cdd:COG1120 102 PHLGLFGRpsaedreAVEEALERTGLEHLADRPVDE-----LSGGERQRVLIARALAQEPPLLLLDEPTSHLD--LAHQL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767915018 151 VVL--LVELAR-RNRIVVLTIHQPrsEL-FQLFDKIAILSFGELIFCGTPAEMLD 201
Cdd:COG1120 175 EVLelLRRLAReRGRTVVMVLHDL--NLaARYADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-201 |
1.17e-30 |
|
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: 119.70 E-value: 1.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 1 MCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNG-----------RALRREqfqdcFSYVLQSDTLLSSLTVRETLHY 69
Cdd:COG1127 34 LAIIGGSGSGKSVLLKLIIGLLRPDS---GEILVDGqditglsekelYELRRR-----IGMLFQGGALFDSLTVFENVAF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 70 tALLAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQ 149
Cdd:COG1127 106 -PLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSE-----LSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAV 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767915018 150 IVVLLVELARRNRIVVLTI-HQpRSELFQLFDKIAILSFGELIFCGTPAEMLD 201
Cdd:COG1127 180 IDELIRELRDELGLTSVVVtHD-LDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
3-421 |
3.81e-30 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 126.50 E-value: 3.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRlgRAGTFL-GEVYVNGRALRREQFQDCFSYVLQSDTLLSSLTVRETLHYTALLaiRRGNPG 81
Cdd:PLN03140 911 LMGVSGAGKTTLMDVLAGR--KTGGYIeGDIRISGFPKKQETFARISGYCEQNDIHSPQVTVRESLIYSAFL--RLPKEV 986
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 82 SFQKK---VEAVMAELSLSHVADRLIGNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTAnQIVVLLVela 158
Cdd:PLN03140 987 SKEEKmmfVDEVMELVELDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAA-AIVMRTV--- 1062
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 159 rRN-----RIVVLTIHQPRSELFQLFDKIAILSF-GELIFCGT----PAEMLDFFNDC-GYP-CPEHSNPFDFYMDLTSV 226
Cdd:PLN03140 1063 -RNtvdtgRTVVCTIHQPSIDIFEAFDELLLMKRgGQVIYSGPlgrnSHKIIEYFEAIpGVPkIKEKYNPATWMLEVSSL 1141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 227 DTQSKeREIETSKRvqmiesaYKKSAICHktlKNIERMKHLKTLPM----VPFKTKDSPGVFSKLGVLL--------RRV 294
Cdd:PLN03140 1142 AAEVK-LGIDFAEH-------YKSSSLYQ---RNKALVKELSTPPPgasdLYFATQYSQSTWGQFKSCLwkqwwtywRSP 1210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 295 TRNLVRNKLAVITRLlqnLIMGLFLLFFVLRVRSNVLKGAIqdrvGLLYqfvGATPYTGMLNAVNLFPVL---RAVSDQE 371
Cdd:PLN03140 1211 DYNLVRFFFTLAAAL---MVGTIFWKVGTKRSNANDLTMVI----GAMY---AAVLFVGINNCSTVQPMVaveRTVFYRE 1280
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 767915018 372 SQDGLYQKWQMMLAYALHVLPFSVVATMIFSSVCYWTLGLHPEVARFGYF 421
Cdd:PLN03140 1281 RAAGMYSALPYAIAQVVCEIPYVLIQTTYYTLIVYAMVAFEWTAAKFFWF 1330
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-171 |
5.94e-30 |
|
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: 116.81 E-value: 5.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 1 MCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALR--REQFQDCFSYVLQSDTLLSSLTVRETLHYTALLAIRRG 78
Cdd:COG4133 31 LALTGPNGSGKTTLLRILAGLLPPSA---GEVLWNGEPIRdaREDYRRRLAYLGHADGLKPELTVRENLRFWAALYGLRA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 79 NPGSfqkkVEAVMAELSLSHVADRLIGNYSlggisTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELA 158
Cdd:COG4133 108 DREA----IDEALEAVGLAGLADLPVRQLS-----AGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHL 178
|
170
....*....|...
gi 767915018 159 RRNRIVVLTIHQP 171
Cdd:COG4133 179 ARGGAVLLTTHQP 191
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1-201 |
1.78e-29 |
|
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: 116.45 E-value: 1.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 1 MCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGR---ALRREQFQDC---FSYVLQSDTLLSSLTVRETLHYtALLA 74
Cdd:cd03261 29 LAIIGPSGSGKSTLLRLIVGLLRPDS---GEVLIDGEdisGLSEAELYRLrrrMGMLFQSGALFDSLTVFENVAF-PLRE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 75 IRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLL 154
Cdd:cd03261 105 HTRLSEEEIREIVLEKLEAVGLRGAEDLYPAE-----LSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLI 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 767915018 155 VELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGTPAEMLD 201
Cdd:cd03261 180 RSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
2-189 |
3.41e-29 |
|
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: 114.87 E-value: 3.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 2 CILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRREQFQDCF---SYVLQ-SDTLLSSLTVRETLhytALLAIRR 77
Cdd:cd03225 31 LIVGPNGSGKSTLLRLLNGLLGPTS---GEVLVDGKDLTKLSLKELRrkvGLVFQnPDDQFFGPTVEEEV---AFGLENL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 78 GNPGS-FQKKVEAVMAELSLSHVADRLIgnYSLGGistGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVE 156
Cdd:cd03225 105 GLPEEeIEERVEEALELVGLEGLRDRSP--FTLSG---GQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKK 179
|
170 180 190
....*....|....*....|....*....|...
gi 767915018 157 LARRNRIVVLTIHQPrSELFQLFDKIAILSFGE 189
Cdd:cd03225 180 LKAEGKTIIIVTHDL-DLLLELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-200 |
4.46e-29 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 115.12 E-value: 4.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 2 CILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRALRREQFQDCFS---YVLQ-SDTLLSSLTVRETLHYtALLaiRR 77
Cdd:COG1122 31 AIIGPNGSGKSTLLRLLNG-LLKPTS--GEVLVDGKDITKKNLRELRRkvgLVFQnPDDQLFAPTVEEDVAF-GPE--NL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 78 GNPGSF-QKKVEAVMAELSLSHVADRLIgnYSLggiSTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVE 156
Cdd:COG1122 105 GLPREEiRERVEEALELVGLEHLADRPP--HEL---SGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKR 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 767915018 157 LARRNRIVVLTIHQPRsELFQLFDKIAILSFGELIFCGTPAEML 200
Cdd:COG1122 180 LNKEGKTVIIVTHDLD-LVAELADRVIVLDDGRIVADGTPREVF 222
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-201 |
5.24e-28 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 112.49 E-value: 5.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 1 MCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRREQFQdcFSYVLQSDTLLSS--LTVRETL---HYTALLAI 75
Cdd:COG1121 35 VAIVGPNGAGKSTLLKAILGLLPPTS---GTVRLFGKPPRRARRR--IGYVPQRAEVDWDfpITVRDVVlmgRYGRRGLF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 76 RRGNPGSFQkKVEAVMAELSLSHVADRLIGnySLGGistGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLV 155
Cdd:COG1121 110 RRPSRADRE-AVDEALERVGLEDLADRPIG--ELSG---GQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLR 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767915018 156 ELARRNRIVVLTIHQPrSELFQLFDKIAILSfGELIFCGTPAEMLD 201
Cdd:COG1121 184 ELRREGKTILVVTHDL-GAVREYFDRVLLLN-RGLVAHGPPEEVLT 227
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3-194 |
6.53e-27 |
|
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: 108.43 E-value: 6.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRL-GRAGTflgeVYVNGRALR--REQFQDCFSYVLQSDTLLSSLTVRETLHYTALLaiRRGN 79
Cdd:cd03264 30 LLGPNGAGKTTLMRILATLTpPSSGT----IRIDGQDVLkqPQKLRRRIGYLPQEFGVYPNFTVREFLDYIAWL--KGIP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 80 PGSFQKKVEAVMAELSLSHVADRLIGNYSlGGIstgeRRRVSIAAQLLQDPKVMLFDEPTTGLDcmTANQIVV--LLVEL 157
Cdd:cd03264 104 SKEVKARVDEVLELVNLGDRAKKKIGSLS-GGM----RRRVGIAQALVGDPSILIVDEPTAGLD--PEERIRFrnLLSEL 176
|
170 180 190
....*....|....*....|....*....|....*..
gi 767915018 158 ArRNRIVVLTIHQpRSELFQLFDKIAILSFGELIFCG 194
Cdd:cd03264 177 G-EDRIVILSTHI-VEDVESLCNQVAVLNKGKLVFEG 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-201 |
1.16e-26 |
|
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: 113.84 E-value: 1.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 1 MCILGSSGSGKTTLLDAMSGRLGRAGTFLGEVYVNGRALRREQFQDC---FSYVLQS-DTLLSSLTVRETLHYTalLAIR 76
Cdd:COG1123 35 VALVGESGSGKSTLALALMGLLPHGGRISGEVLLDGRDLLELSEALRgrrIGMVFQDpMTQLNPVTVGDQIAEA--LENL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 77 RGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVE 156
Cdd:COG1123 113 GLSRAEARARVLELLEAVGLERRLDRYPHQ-----LSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRE 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 767915018 157 LARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGTPAEMLD 201
Cdd:COG1123 188 LQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-194 |
1.19e-26 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 107.61 E-value: 1.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 2 CILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRAL------RREqfqdcFSYVLQSDTLLSSLTVRETLHYTalLAI 75
Cdd:cd03259 30 ALLGPSGCGKTTLLRLIAG-LERPDS--GEILIDGRDVtgvppeRRN-----IGMVFQDYALFPHLTVAENIAFG--LKL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 76 RRGNPGSFQKKVEAVMAELSLSHVADRLIgnyslGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLV 155
Cdd:cd03259 100 RGVPKAEIRARVRELLELVGLEGLLNRYP-----HELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELK 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 767915018 156 ELARRNRI-VVLTIHQPrSELFQLFDKIAILSFGELIFCG 194
Cdd:cd03259 175 ELQRELGItTIYVTHDQ-EEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
3-140 |
1.49e-26 |
|
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: 105.42 E-value: 1.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALR---REQFQDCFSYVLQSDTLLSSLTVRETLHYTALLAIRRGN 79
Cdd:pfam00005 16 LVGPNGAGKSTLLKLIAGLLSPTE---GTILLDGQDLTddeRKSLRKEIGYVFQDPQLFPRLTVRENLRLGLLLKGLSKR 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767915018 80 PgsFQKKVEAVMAELSLSHVADRLIGNYSlGGISTGERRRVSIAAQLLQDPKVMLFDEPTT 140
Cdd:pfam00005 93 E--KDARAEEALEKLGLGDLADRPVGERP-GTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
2-194 |
4.06e-26 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 105.21 E-value: 4.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 2 CILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALR---REQFQDCFSYVLQsdtllssltvretlhytallairrg 78
Cdd:cd03214 29 GILGPNGAGKSTLLKTLAGLLKPSS---GEILLDGKDLAslsPKELARKIAYVPQ------------------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 79 npgsfqkkveaVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDcmTANQIVVL--LVE 156
Cdd:cd03214 81 -----------ALELLGLAHLADRPFNE-----LSGGERQRVLLARALAQEPPILLLDEPTSHLD--IAHQIELLelLRR 142
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 767915018 157 LAR-RNRIVVLTIHQPrsEL-FQLFDKIAILSFGELIFCG 194
Cdd:cd03214 143 LAReRGKTVVMVLHDL--NLaARYADRVILLKDGRIVAQG 180
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
3-194 |
9.96e-26 |
|
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: 104.65 E-value: 9.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLGRAGTFLGEVYVNGRALR--REQFQDCFSYVLQSDTLLSSLTVRETLHYTAllairrgnp 80
Cdd:cd03233 38 VLGRPGSGCSTLLKALANRTEGNVSVEGDIHYNGIPYKefAEKYPGEIIYVSEEDVHFPTLTVRETLDFAL--------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 81 gsfqkkveavmaelslshvadRLIGNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARR 160
Cdd:cd03233 109 ---------------------RCKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADV 167
|
170 180 190
....*....|....*....|....*....|....*
gi 767915018 161 NRIVVL-TIHQPRSELFQLFDKIAILSFGELIFCG 194
Cdd:cd03233 168 LKTTTFvSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1-190 |
1.46e-25 |
|
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: 103.25 E-value: 1.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 1 MCILGSSGSGKTTLLDAMSGRLgRAGTflGEVYVNGRALRRE--QFQDCFSYVLQSDTLLSSLTVRETLHYtallairrg 78
Cdd:cd03230 29 YGLLGPNGAGKTTLIKIILGLL-KPDS--GEIKVLGKDIKKEpeEVKRRIGYLPEEPSLYENLTVRENLKL--------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 79 npgsfqkkveavmaelslshvadrlignyslggiSTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELA 158
Cdd:cd03230 97 ----------------------------------SGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELK 142
|
170 180 190
....*....|....*....|....*....|..
gi 767915018 159 RRNRIVVLTIHQPrSELFQLFDKIAILSFGEL 190
Cdd:cd03230 143 KEGKTILLSSHIL-EEAERLCDRVAILNNGRI 173
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
2-194 |
1.79e-25 |
|
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: 104.15 E-value: 1.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 2 CILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRREQFQdcFSYVLQSDTLLSS--LTVRETLhytaLLAiRRGN 79
Cdd:cd03235 29 AIVGPNGAGKSTLLKAILGLLKPTS---GSIRVFGKPLEKERKR--IGYVPQRRSIDRDfpISVRDVV----LMG-LYGH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 80 PGSFQ-------KKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVV 152
Cdd:cd03235 99 KGLFRrlskadkAKVDEALERVGLSELADRQIGE-----LSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767915018 153 LLVELARRNRIVVLTIHQPrSELFQLFDKIAILSfGELIFCG 194
Cdd:cd03235 174 LLRELRREGMTILVVTHDL-GLVLEYFDRVLLLN-RTVVASG 213
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1-199 |
2.00e-25 |
|
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: 104.37 E-value: 2.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 1 MCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRRE--QFQDCFSYVLQSDTLLSSLTVRETLHYTALLAirrG 78
Cdd:cd03265 29 FGLLGPNGAGKTTTIKMLTTLLKPTS---GRATVAGHDVVREprEVRRRIGIVFQDLSVDDELTGWENLYIHARLY---G 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 79 NPGS-FQKKVEAVMAELSLSHVADRLIGNYSlggisTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVEL 157
Cdd:cd03265 103 VPGAeRRERIDELLDFVGLLEAADRLVKTYS-----GGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767915018 158 ARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGTPAEM 199
Cdd:cd03265 178 KEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1-190 |
2.92e-25 |
|
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: 103.72 E-value: 2.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 1 MCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGR-----------ALRREQFqdcfSYVLQSDTLLSSLTVRETLhy 69
Cdd:cd03255 33 VAIVGPSGSGKSTLLNILGG-LDRPTS--GEVRVDGTdisklsekelaAFRRRHI----GFVFQSFNLLPDLTALENV-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 70 tALLAIRRGNPGSFQK-KVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTAN 148
Cdd:cd03255 104 -ELPLLLAGVPKKERReRAEELLERVGLGDRLNHYPSE-----LSGGQQQRVAIARALANDPKIILADEPTGNLDSETGK 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 767915018 149 QIVVLLVELAR-RNRIVVLTIHQPrsELFQLFDKIAILSFGEL 190
Cdd:cd03255 178 EVMELLRELNKeAGTTIVVVTHDP--ELAEYADRIIELRDGKI 218
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-198 |
5.66e-25 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 103.67 E-value: 5.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 2 CILGSSGSGKTTLLDAMSGRLgRAGTflGEVYVNGRALRREQ------------FQdcfsyVLQsdtLLSSLTVRETL-- 67
Cdd:cd03219 30 GLIGPNGAGKTTLFNLISGFL-RPTS--GSVLFDGEDITGLPpheiarlgigrtFQ-----IPR---LFPELTVLENVmv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 68 ------HYTALLAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTG 141
Cdd:cd03219 99 aaqartGSGLLLARARREEREARERAEELLERVGLADLADRPAGE-----LSYGQQRRLEIARALATDPKLLLLDEPAAG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767915018 142 LDCMTANQIVVLLVELARRNRIVVLTIHQPRSeLFQLFDKIAILSFGELIFCGTPAE 198
Cdd:cd03219 174 LNPEETEELAELIRELRERGITVLLVEHDMDV-VMSLADRVTVLDQGRVIAEGTPDE 229
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
3-194 |
7.62e-25 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 102.76 E-value: 7.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRREQFQDCFS-------YVLQSDTLLSSLTVRETLHYtallAI 75
Cdd:cd03297 28 IFGASGAGKSTLLRCIAGLEKPDG---GTIVLNGTVLFDSRKKINLPpqqrkigLVFQQYALFPHLNVRENLAF----GL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 76 RRGNPGSFQKKVEAVMAELSLSHVADRlignySLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLV 155
Cdd:cd03297 101 KRKRNREDRISVDELLDLLGLDHLLNR-----YPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELK 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 767915018 156 ELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCG 194
Cdd:cd03297 176 QIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-191 |
8.83e-25 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 102.81 E-value: 8.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 2 CILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGR-----------ALRREQfqdcFSYVLQSDTLLSSLTVRETLhyt 70
Cdd:COG1136 38 AIVGPSGSGKSTLLNILGG-LDRPTS--GEVLIDGQdisslserelaRLRRRH----IGFVFQFFNLLPELTALENV--- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 71 AL-LAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQ 149
Cdd:COG1136 108 ALpLLLAGVSRKERRERARELLERVGLGDRLDHRPSQ-----LSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEE 182
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 767915018 150 IVVLLVELARR-NRIVVLTIHQPRseLFQLFDKIAILSFGELI 191
Cdd:COG1136 183 VLELLRELNRElGTTIVMVTHDPE--LAARADRVIRLRDGRIV 223
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-186 |
1.43e-24 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 101.78 E-value: 1.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 2 CILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRALRREQFQdcFSYVLQSDTLLSSLTVRETlhyTAL-LAIRRGNP 80
Cdd:cd03293 34 ALVGPSGCGKSTLLRIIAG-LERPTS--GEVLVDGEPVTGPGPD--RGYVFQQDALLPWLTVLDN---VALgLELQGVPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 81 GSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARR 160
Cdd:cd03293 106 AEARERAEELLELVGLSGFENAYPHQ-----LSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRE 180
|
170 180
....*....|....*....|....*.
gi 767915018 161 NRIVVLTIHQPRSELFQLFDKIAILS 186
Cdd:cd03293 181 TGKTVLLVTHDIDEAVFLADRVVVLS 206
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-200 |
3.61e-24 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 106.39 E-value: 3.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGrlgragtFL----GEVYVNG---RALRREQFQDCFSYVLQSDTLLSSlTVRETLhytaLLAi 75
Cdd:COG4987 366 IVGPSGSGKSTLLALLLR-------FLdpqsGSITLGGvdlRDLDEDDLRRRIAVVPQRPHLFDT-TLRENL----RLA- 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 76 rrgNPGSFQKKVEAVMAELSLSHVADRLIG--NYSLG----GISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQ 149
Cdd:COG4987 433 ---RPDATDEELWAALERVGLGDWLAALPDglDTWLGeggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQA 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 767915018 150 IVVLLVELArRNRIVVLTIHQPRseLFQLFDKIAILSFGELIFCGTPAEML 200
Cdd:COG4987 510 LLADLLEAL-AGRTVLLITHRLA--GLERMDRILVLEDGRIVEQGTHEELL 557
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
2-189 |
5.18e-24 |
|
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: 98.47 E-value: 5.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 2 CILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRR---EQFQDCFSYVLQsdtllssltvretlhytallairrg 78
Cdd:cd00267 29 ALVGPNGSGKSTLLRAIAGLLKPTS---GEILIDGKDIAKlplEELRRRIGYVPQ------------------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 79 npgsfqkkveavmaelslshvadrlignyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELA 158
Cdd:cd00267 81 ---------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELA 127
|
170 180 190
....*....|....*....|....*....|.
gi 767915018 159 RRNRIVVLTIHQPrSELFQLFDKIAILSFGE 189
Cdd:cd00267 128 EEGRTVIIVTHDP-ELAELAADRVIVLKDGK 157
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-200 |
7.94e-24 |
|
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: 100.31 E-value: 7.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 4 LGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRALRR----EQFQDCFSYVLQSDTLLSSLTVRETLhyTALLAIRRGN 79
Cdd:cd03218 32 LGPNGAGKTTTFYMIVG-LVKPDS--GKILLDGQDITKlpmhKRARLGIGYLPQEASIFRKLTVEENI--LAVLEIRGLS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 80 PGSFQKKVEAVMAELSLSHVADRLigNYSLGGistGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELAR 159
Cdd:cd03218 107 KKEREEKLEELLEEFHITHLRKSK--ASSLSG---GERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKD 181
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 767915018 160 RNRIVVLTIHQPRsELFQLFDKIAILSFGELIFCGTPAEML 200
Cdd:cd03218 182 RGIGVLITDHNVR-ETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
3-199 |
4.95e-23 |
|
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: 99.77 E-value: 4.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRL----GRAGTFLGEVYVNGRALRREqfqdcFSYVLQSDTLLSSLTVRETLHYTALLairRG 78
Cdd:TIGR01188 24 FLGPNGAGKTTTIRMLTTLLrptsGTARVAGYDVVREPRKVRRS-----IGIVPQYASVDEDLTGRENLEMMGRL---YG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 79 NPGSF-QKKVEAVMAELSLSHVADRLIGNYSlGGIstgeRRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVEL 157
Cdd:TIGR01188 96 LPKDEaEERAEELLELFELGEAADRPVGTYS-GGM----RRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDYIRAL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767915018 158 ARRNRIVVLTIHQpRSELFQLFDKIAILSFGELIFCGTPAEM 199
Cdd:TIGR01188 171 KEEGVTILLTTHY-MEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
3-200 |
1.02e-22 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 99.79 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRAL---RREQF----QDCFSYVLQSDTLLSSLTVRETLHYtallAI 75
Cdd:COG4148 30 LFGPSGSGKTTLLRAIAG-LERPDS--GRIRLGGEVLqdsARGIFlpphRRRIGYVFQEARLFPHLSVRGNLLY----GR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 76 RRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLV 155
Cdd:COG4148 103 KRAPRAERRISFDEVVELLGIGHLLDRRPAT-----LSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767915018 156 ELARRNRIVVLTI-HQPRsELFQLFDKIAILSFGELIFCGTPAEML 200
Cdd:COG4148 178 RLRDELDIPILYVsHSLD-EVARLADHVVLLEQGRVVASGPLAEVL 222
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-201 |
1.17e-22 |
|
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: 101.52 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNG-----------RALRRE-Q--FQDCFSyvlqsdTLLSSLTVRETLH 68
Cdd:COG1123 296 LVGESGSGKSTLARLLLGLLRPTS---GSILFDGkdltklsrrslRELRRRvQmvFQDPYS------SLNPRMTVGDIIA 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 69 YtALLAIRRGNPGSFQKKVEAVMAELSLS-HVADRLIgnYSLGGistGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTA 147
Cdd:COG1123 367 E-PLRLHGLLSRAERRERVAELLERVGLPpDLADRYP--HELSG---GQRQRVAIARALALEPKLLILDEPTSALDVSVQ 440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767915018 148 NQIVVLLVELARRNRivvLTIhqprseLF---------QLFDKIAILSFGELIFCGTPAEMLD 201
Cdd:COG1123 441 AQILNLLRDLQRELG---LTY------LFishdlavvrYIADRVAVMYDGRIVEDGPTEEVFA 494
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
3-200 |
3.70e-22 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 95.48 E-value: 3.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRAL------RREqfqdcFSYVLQSDTLLSSLTVRETLHYTalLAIR 76
Cdd:cd03299 30 ILGPTGSGKSVLLETIAGFIKPDS---GKILLNGKDItnlppeKRD-----ISYVPQNYALFPHMTVYKNIAYG--LKKR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 77 RGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVE 156
Cdd:cd03299 100 KVDKKEIERKVLEIAEMLGIDHLLNRKPET-----LSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKK 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 767915018 157 LARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGTPAEML 200
Cdd:cd03299 175 IRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-192 |
3.80e-22 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 94.59 E-value: 3.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 2 CILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGralrrEQFQDCFSYVLQSDTLLSS------LTVRETLHYTALLAI 75
Cdd:cd03268 30 GFLGPNGAGKTTTMKIILG-LIKPDS--GEITFDG-----KSYQKNIEALRRIGALIEApgfypnLTARENLRLLARLLG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 76 RRgnpgsfQKKVEAVMAELSLSHVADRLIGNYSLGgistgERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLV 155
Cdd:cd03268 102 IR------KKRIDEVLDVVGLKDSAKKKVKGFSLG-----MKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELIL 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 767915018 156 ELARRNRIVVLTIHQpRSELFQLFDKIAILSFGELIF 192
Cdd:cd03268 171 SLRDQGITVLISSHL-LSEIQKVADRIGIINKGKLIE 206
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-190 |
9.51e-22 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 93.34 E-value: 9.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 2 CILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGR--------ALRREqfqdcFSYVLQSDTLLSSlTVRETLHYTALL 73
Cdd:COG4619 30 AITGPSGSGKSTLLRALADLDPPTS---GEIYLDGKplsampppEWRRQ-----VAYVPQEPALWGG-TVRDNLPFPFQL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 74 AIRRGNPgsfqKKVEAVMAELSLSH-VADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVV 152
Cdd:COG4619 101 RERKFDR----ERALELLERLGLPPdILDKPVER-----LSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEE 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 767915018 153 LLVEL-ARRNRIVVLTIHQPRsELFQLFDKIAILSFGEL 190
Cdd:COG4619 172 LLREYlAEEGRAVLWVSHDPE-QIERVADRVLTLEAGRL 209
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
2-186 |
2.13e-21 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 94.00 E-value: 2.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 2 CILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRALRREQfQDCfSYVLQSDTLLSSLTVRE--TLHytalLAIRRGN 79
Cdd:COG1116 41 ALVGPSGCGKSTLLRLIAG-LEKPTS--GEVLVDGKPVTGPG-PDR-GVVFQEPALLPWLTVLDnvALG----LELRGVP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 80 PGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELAR 159
Cdd:COG1116 112 KAERRERARELLELVGLAGFEDAYPHQ-----LSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQ 186
|
170 180
....*....|....*....|....*...
gi 767915018 160 RNRIVVLTI-HQPRsELFQLFDKIAILS 186
Cdd:COG1116 187 ETGKTVLFVtHDVD-EAVFLADRVVVLS 213
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-194 |
4.46e-21 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 92.05 E-value: 4.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLgRAGTflGEVYVNGRALRREQFQDC--FSYVLQSDTLLSSLTVRETLHYTALLairRG-N 79
Cdd:cd03266 36 LLGPNGAGKTTTLRMLAGLL-EPDA--GFATVDGFDVVKEPAEARrrLGFVSDSTGLYDRLTARENLEYFAGL---YGlK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 80 PGSFQKKVEAVMAELSLSHVADRlignySLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELAR 159
Cdd:cd03266 110 GDELTARLEELADRLGMEELLDR-----RVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRA 184
|
170 180 190
....*....|....*....|....*....|....*
gi 767915018 160 RNRIVVLTIHQpRSELFQLFDKIAILSFGELIFCG 194
Cdd:cd03266 185 LGKCILFSTHI-MQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-200 |
5.46e-21 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 91.87 E-value: 5.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAM-------SGRLGRAGTFLGEVyvNGRALRreQFQDCFSYVLQSDTLLSSLTVRETLHYTALLAi 75
Cdd:cd03258 36 IIGRSGAGKSTLIRCInglerptSGSVLVDGTDLTLL--SGKELR--KARRRIGMIFQHFNLLSSRTVFENVALPLEIA- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 76 rrGNPGSFQ-KKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLL 154
Cdd:cd03258 111 --GVPKAEIeERVLELLELVGLEDKADAYPAQ-----LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 767915018 155 VELARRNRIVVLTI-HQpRSELFQLFDKIAILSFGELIFCGTPAEML 200
Cdd:cd03258 184 RDINRELGLTIVLItHE-MEVVKRICDRVAVMEKGEVVEEGTVEEVF 229
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
4-194 |
9.05e-21 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 91.63 E-value: 9.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 4 LGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRA--LRREQFQDCFSYVL-QSDTLLSSLTVRETlhYTALLAIRRGNP 80
Cdd:cd03267 53 IGPNGAGKTTTLKILSGLLQPTS---GEVRVAGLVpwKRRKKFLRRIGVVFgQKTQLWWDLPVIDS--FYLLAAIYDLPP 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 81 GSFQKKVEAVMAELSLSHVADRLIGNYSLGgistgERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELAR- 159
Cdd:cd03267 128 ARFKKRLDELSELLDLEELLDTPVRQLSLG-----QRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRe 202
|
170 180 190
....*....|....*....|....*....|....*
gi 767915018 160 RNRIVVLTIHQPRsELFQLFDKIAILSFGELIFCG 194
Cdd:cd03267 203 RGTTVLLTSHYMK-DIEALARRVLVIDKGRLLYDG 236
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-169 |
9.40e-21 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 90.39 E-value: 9.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRREQFQDCFSYVLQ-SDTLLSSLTVRETLHYTAllairrGNPG 81
Cdd:cd03226 31 LTGKNGAGKTTLAKILAGLIKESS---GSILLNGKPIKAKERRKSIGYVMQdVDYQLFTDSVREELLLGL------KELD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 82 SFQKKVEAVMAELSLSHVADRLigNYSLGGistGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRN 161
Cdd:cd03226 102 AGNEQAETVLKDLDLYALKERH--PLSLSG---GQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQG 176
|
....*...
gi 767915018 162 RIVVLTIH 169
Cdd:cd03226 177 KAVIVITH 184
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
3-200 |
1.11e-20 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 91.18 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRALRR----EQFQDCFSYVLQSDTLLSSLTVRETLhyTALLAIR-R 77
Cdd:TIGR04406 32 LLGPNGAGKTTSFYMIVG-LVRPDA--GKILIDGQDITHlpmhERARLGIGYLPQEASIFRKLTVEENI--MAVLEIRkD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 78 GNPGSFQKKVEAVMAELSLSHVADRLigNYSLGGistGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVEL 157
Cdd:TIGR04406 107 LDRAEREERLEALLEEFQISHLRDNK--AMSLSG---GERRRVEIARALATNPKFILLDEPFAGVDPIAVGDIKKIIKHL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 767915018 158 ARRNRIVVLTIHQPRsELFQLFDKIAILSFGELIFCGTPAEML 200
Cdd:TIGR04406 182 KERGIGVLITDHNVR-ETLDICDRAYIISDGKVLAEGTPAEIV 223
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
3-198 |
1.52e-20 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 91.09 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNG-----------RALRREqfqdcFSYVLQSDTLLSSLTVRET----- 66
Cdd:cd03256 32 LIGPSGAGKSTLLRCLNGLVEPTS---GSVLIDGtdinklkgkalRQLRRQ-----IGMIFQQFNLIERLSVLENvlsgr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 67 LHYTALL-AIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCM 145
Cdd:cd03256 104 LGRRSTWrSLFGLFPKEEKQRALAALERVGLLDKAYQRADQ-----LSGGQQQRVAIARALMQQPKLILADEPVASLDPA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767915018 146 TANQIVVLLVELAR-RNRIVVLTIHQPrsELF-QLFDKIAILSFGELIFCGTPAE 198
Cdd:cd03256 179 SSRQVMDLLKRINReEGITVIVSLHQV--DLArEYADRIVGLKDGRIVFDGPPAE 231
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
3-200 |
3.02e-20 |
|
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of this protein family are the ATP-binding subunit of an ABC transporter system that is associated with PQQ biosynthesis and PQQ-dependent alcohol dehydrogenases. While this family shows homology to several efflux ABC transporter subunits, the presence of a periplasmic substrate-binding protein and association with systems for catabolism of alcohols suggests a role in import rather than detoxification. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 274822 [Multi-domain] Cd Length: 236 Bit Score: 90.04 E-value: 3.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLdAMSGRLGRAGTflGEVYVNGRALRREQFQDCFSY--VLQSDTLLSSLTVRETLHYTALL-AIRRGN 79
Cdd:TIGR03864 32 LLGPNGAGKSTLF-SLLTRLYVAQS--GQISVAGHDLRRAPRAALARLgvVFQQPTLDLDLSVRQNLRYHAALhGLSRAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 80 PgsfQKKVEAVMAELSLSHVADRLIGnySLGGistGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELAR 159
Cdd:TIGR03864 109 A---RARIAELLARLGLAERADDKVR--ELNG---GHRRRVEIARALLHRPALLLLDEPTVGLDPASRAAITAHVRALAR 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 767915018 160 RNRIVVL-TIHqprselfqLFDKIA------ILSFGELIFCGTPAEML 200
Cdd:TIGR03864 181 DQGLSVLwATH--------LVDEIEasdrlvVLHRGRVLADGAAAELR 220
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
4-201 |
3.91e-20 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 89.70 E-value: 3.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 4 LGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRAL------RREQFQdcFSYVLQSDTLLSSLTVRETLhyTALLAIRR 77
Cdd:COG1137 35 LGPNGAGKTTTFYMIVGLVKPDS---GRIFLDGEDIthlpmhKRARLG--IGYLPQEASIFRKLTVEDNI--LAVLELRK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 78 GNPGSFQKKVEAVMAELSLSHVADRLigNYSLGGistGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVEL 157
Cdd:COG1137 108 LSKKEREERLEELLEEFGITHLRKSK--AYSLSG---GERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 767915018 158 ARRNRIVVLTIHQPRsELFQLFDKIAILSFGELIFCGTPAEMLD 201
Cdd:COG1137 183 KERGIGVLITDHNVR-ETLGICDRAYIISEGKVLAEGTPEEILN 225
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-200 |
4.17e-20 |
|
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: 89.76 E-value: 4.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLgrAGTFLGEVYVNGRALRREQFQD------CFSYVLQsDTLLSSLTVRETL--------- 67
Cdd:COG1119 34 ILGPNGAGKSTLLSLITGDL--PPTYGNDVRLFGERRGGEDVWElrkrigLVSPALQ-LRFPRDETVLDVVlsgffdsig 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 68 ---HYTALLairrgnpgsfQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDC 144
Cdd:COG1119 111 lyrEPTDEQ----------RERARELLELLGLAHLADRPFGT-----LSQGEQRRVLIARALVKDPELLILDEPTAGLDL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767915018 145 MTANQIVVLLVELARRNRIVVLTI-HQPrSELFQLFDKIAILSFGELIFCGTPAEML 200
Cdd:COG1119 176 GARELLLALLDKLAAEGAPTLVLVtHHV-EEIPPGITHVLLLKDGRVVAAGPKEEVL 231
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-172 |
4.43e-20 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 89.42 E-value: 4.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 2 CILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGR-----------ALRREQfqdcFSYVLQSDTLLSSLTVREtlhYT 70
Cdd:COG4181 42 AIVGASGSGKSTLLGLLAG-LDRPTS--GTVRLAGQdlfaldedaraRLRARH----VGFVFQSFQLLPTLTALE---NV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 71 ALLAIRRGNPGSFQkKVEAVMAELSLSHvadRLiGNYSlGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQI 150
Cdd:COG4181 112 MLPLELAGRRDARA-RARALLERVGLGH---RL-DHYP-AQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQI 185
|
170 180
....*....|....*....|...
gi 767915018 151 VVLLVELARRNRI-VVLTIHQPR 172
Cdd:COG4181 186 IDLLFELNRERGTtLVLVTHDPA 208
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-200 |
1.17e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 88.68 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLgRAGTflGEVYVNGRAL----------RREqfqdcfsyVL-QSDTLLSSLTVRETLhytA 71
Cdd:PRK13548 33 ILGPNGAGKSTLLRALSGEL-SPDS--GEVRLNGRPLadwspaelarRRA--------VLpQHSSLSFPFTVEEVV---A 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 72 L-LAIRRGNPGSFQKKVEAVMAELSLSHVADRLignY-SLGGistGERRRVSIA---AQLLQD---PKVMLFDEPTTGLD 143
Cdd:PRK13548 99 MgRAPHGLSRAEDDALVAAALAQVDLAHLAGRD---YpQLSG---GEQQRVQLArvlAQLWEPdgpPRWLLLDEPTSALD 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767915018 144 cmTANQIVVL--LVELARRNR---IVVLtiHqprsELFQ--LF-DKIAILSFGELIFCGTPAEML 200
Cdd:PRK13548 173 --LAHQHHVLrlARQLAHERGlavIVVL--H----DLNLaaRYaDRIVLLHQGRLVADGTPAEVL 229
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
290-497 |
2.07e-19 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 86.56 E-value: 2.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 290 LLRRVTRNLVRNKLAVITRLLQNLIMGLFL--LFFVLRvrsnvLKGAIQDRVGLLYQFVGATPYTGMLNAVNLFPVLRAV 367
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFgtLFGNLG-----NQQGGLNRPGLLFFSILFNAFSALSGISPVFEKERGV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 368 SDQESQDGLYQKWQMMLAYALHVLPFSVVATMIFSSVCYWTLGLHPEVARFGYFSAALLAPHLIGEFLTLVLLGIVQNPN 447
Cdd:pfam01061 76 LYRELASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFE 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767915018 448 IVNSVVALLSIAGVLVgSGFLRNIQEMPIPFKIISYFTFQKYCSEILVVN 497
Cdd:pfam01061 156 DASQLGPLVLLPLLLL-SGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-168 |
2.72e-19 |
|
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: 86.79 E-value: 2.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 1 MCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGR---ALRREQFQDC---FSYVLQsDTLLS---SLTVRETLhyTA 71
Cdd:cd03257 34 LGLVGESGSGKSTLARAILG-LLKPTS--GSIIFDGKdllKLSRRLRKIRrkeIQMVFQ-DPMSSlnpRMTIGEQI--AE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 72 LLAIRRGNPGSFQKKvEAVMAELSLSHVADRLIGNY--SLGGistGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQ 149
Cdd:cd03257 108 PLRIHGKLSKKEARK-EAVLLLLVGVGLPEEVLNRYphELSG---GQRQRVAIARALALNPKLLIADEPTSALDVSVQAQ 183
|
170
....*....|....*....
gi 767915018 150 IVVLLVELARRNRIVVLTI 168
Cdd:cd03257 184 ILDLLKKLQEELGLTLLFI 202
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-201 |
2.86e-19 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 86.72 E-value: 2.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 2 CILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRR----EQFQDCFSYVLQSDTLLSSLTVRETLhytaLLAIRR 77
Cdd:cd03224 30 ALLGRNGAGKTTLLKTIMGLLPPRS---GSIRFDGRDITGlpphERARAGIGYVPEGRRIFPELTVEENL----LLGAYA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 78 GNPGSFQKKVEAVMAELS-LSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVE 156
Cdd:cd03224 103 RRRAKRKARLERVYELFPrLKERRKQLAGT-----LSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 767915018 157 LARRnRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGTPAEMLD 201
Cdd:cd03224 178 LRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-200 |
3.33e-19 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 86.97 E-value: 3.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 2 CILGSSGSGKTTLLdAMSGRLGRAGTflGEVYVNGR--------ALRREqfqdcFSYVLQSDTLLSSLTVRETLhyTALL 73
Cdd:cd03295 31 VLIGPSGSGKTTTM-KMINRLIEPTS--GEIFIDGEdireqdpvELRRK-----IGYVIQQIGLFPHMTVEENI--ALVP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 74 AIRRGNPGSFQKKVEAVMAELSL--SHVADRlignYSlGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIV 151
Cdd:cd03295 101 KLLKWPKEKIRERADELLALVGLdpAEFADR----YP-HELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQ 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767915018 152 VLLVELARR-NRIVVLTIHQpRSELFQLFDKIAILSFGELIFCGTPAEML 200
Cdd:cd03295 176 EEFKRLQQElGKTIVFVTHD-IDEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
2-206 |
1.37e-18 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 85.77 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 2 CILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNG-----------RALRREQFqdcfSYVLQSDTLLSSLTVRETLHYT 70
Cdd:cd03294 54 VIMGLSGSGKSTLLRCINRLIEPTS---GKVLIDGqdiaamsrkelRELRRKKI----SMVFQSFALLPHRTVLENVAFG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 71 alLAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQI 150
Cdd:cd03294 127 --LEVQGVPRAEREERAAEALELVGLEGWEHKYPDE-----LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREM 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767915018 151 VVLLVEL-ARRNRIVVLTIHQPrSELFQLFDKIAILSFGELIFCGTPAEML---------DFFNDC 206
Cdd:cd03294 200 QDELLRLqAELQKTIVFITHDL-DEALRLGDRIAIMKDGRLVQVGTPEEILtnpandyvrEFFRGV 264
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1-189 |
1.70e-18 |
|
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: 83.39 E-value: 1.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 1 MCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRAL-----RREQFQDCFSYVLQSDTLLSSLTVRETLHYtallai 75
Cdd:cd03229 29 VALLGPSGSGKSTLLRCIAGLEEPDS---GSILIDGEDLtdledELPPLRRRIGMVFQDFALFPHLTVLENIAL------ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 76 rrgnpgsfqkkveavmaelslshvadrlignyslgGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLV 155
Cdd:cd03229 100 -----------------------------------GLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLK 144
|
170 180 190
....*....|....*....|....*....|....*
gi 767915018 156 ELARRNRI-VVLTIHQPRsELFQLFDKIAILSFGE 189
Cdd:cd03229 145 SLQAQLGItVVLVTHDLD-EAARLADRVVVLRDGK 178
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-200 |
1.76e-18 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 89.12 E-value: 1.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 2 CILGSSGSGKTTLLDAMSGrlgragtFL----GEVYVNGRALR---REQFQDCFSYVLQSDTLLSSlTVRETlhytalla 74
Cdd:COG2274 505 AIVGRSGSGKSTLLKLLLG-------LYeptsGRILIDGIDLRqidPASLRRQIGVVLQDVFLFSG-TIREN-------- 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 75 IRRGNPGSFQKKVEAVMAELSLSHVADRLIGNYSL------GGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTAN 148
Cdd:COG2274 569 ITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTvvgeggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEA 648
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767915018 149 QIVVLLVELArRNRIVVLTIHqpRSELFQLFDKIAILSFGELIFCGTPAEML 200
Cdd:COG2274 649 IILENLRRLL-KGRTVIIIAH--RLSTIRLADRIIVLDKGRIVEDGTHEELL 697
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
1-172 |
2.31e-18 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 83.94 E-value: 2.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 1 MCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGR-----------ALRREQFqdcfSYVLQSDTLLSSLTVRETLHY 69
Cdd:TIGR02211 34 VAIVGSSGSGKSTLLHLLGG-LDNPTS--GEVLFNGQslsklssneraKLRNKKL----GFIYQFHHLLPDFTALENVAM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 70 TALlaIRRGNPGSFQKKVEAVMAELSLSHvadRLigNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQ 149
Cdd:TIGR02211 107 PLL--IGKKSVKEAKERAYEMLEKVGLEH---RI--NHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNNAKI 179
|
170 180
....*....|....*....|....
gi 767915018 150 IVVLLVELARRNRI-VVLTIHQPR 172
Cdd:TIGR02211 180 IFDLMLELNRELNTsFLVVTHDLE 203
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
3-172 |
2.45e-18 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 83.56 E-value: 2.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRAL--RREQFQDCFSYVLQSDTLLSSLTVRETLHYTALLAirrgnp 80
Cdd:TIGR01189 31 VTGPNGIGKTTLLRILAGLLRPDS---GEVRWNGTPLaeQRDEPHENILYLGHLPGLKPELSALENLHFWAAIH------ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 81 GSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARR 160
Cdd:TIGR01189 102 GGAQRTIEDALAAVGLTGFEDLPAAQ-----LSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHLAR 176
|
170
....*....|..
gi 767915018 161 NRIVVLTIHQPR 172
Cdd:TIGR01189 177 GGIVLLTTHQDL 188
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
2-198 |
4.70e-18 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 85.92 E-value: 4.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 2 CILGSSGSGKTTLLDAMSGrlgragtFL----GEVYVNGRAL------RREqfqdcFSYVLQSDTLLSSLTVRETLHYTa 71
Cdd:COG3842 35 ALLGPSGCGKTTLLRMIAG-------FEtpdsGRILLDGRDVtglppeKRN-----VGMVFQDYALFPHLTVAENVAFG- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 72 lLAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIV 151
Cdd:COG3842 102 -LRMRGVPKAEIRARVAELLELVGLEGLADRYPHQ-----LSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMR 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 767915018 152 VLLVELARRNRIVVLTI-HQpRSELFQLFDKIAILSFGELIFCGTPAE 198
Cdd:COG3842 176 EELRRLQRELGITFIYVtHD-QEEALALADRIAVMNDGRIEQVGTPEE 222
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
3-188 |
6.47e-18 |
|
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: 82.16 E-value: 6.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRAL--RREQFQDCFSYVLQSDTLLSSLTVRETLHYTALLAIRRGnp 80
Cdd:cd03231 31 VTGPNGSGKTTLLRILAGLSPPLA---GRVLLNGGPLdfQRDSIARGLLYLGHAPGIKTTLSVLENLRFWHADHSDEQ-- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 81 gsfqkkVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARR 160
Cdd:cd03231 106 ------VEEALARVGLNGFEDRPVAQ-----LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCAR 174
|
170 180
....*....|....*....|....*...
gi 767915018 161 NRIVVLTIHQPrseLFQLFDKIAILSFG 188
Cdd:cd03231 175 GGMVVLTTHQD---LGLSEAGARELDLG 199
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-201 |
9.71e-18 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 84.74 E-value: 9.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 1 MCILGSSGSGKTTLLDAMSGrlgragtfL-----GEVYVNGR------ALRREqfqdcFSYVLQSDTLLSSLTVRETLhy 69
Cdd:COG3839 32 LVLLGPSGCGKSTLLRMIAG--------LedptsGEILIGGRdvtdlpPKDRN-----IAMVFQSYALYPHMTVYENI-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 70 tAL-LAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNysLGGistGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTAN 148
Cdd:COG3839 97 -AFpLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQ--LSG---GQRQRVALGRALVREPKVFLLDEPLSNLDAKLRV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767915018 149 QIVVLLVELARRNRIVVL--TiHQPrSELFQLFDKIAILSFGELIFCGTPAEMLD 201
Cdd:COG3839 171 EMRAEIKRLHRRLGTTTIyvT-HDQ-VEAMTLADRIAVMNDGRIQQVGTPEELYD 223
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-169 |
1.03e-17 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 82.41 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSG--RLGRagtflGEVYVNGR---ALRREQ-----------FQDCfsyvlqsdTLLSSLTVRET 66
Cdd:COG2884 33 LTGPSGAGKSTLLKLLYGeeRPTS-----GQVLVNGQdlsRLKRREipylrrrigvvFQDF--------RLLPDRTVYEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 67 LHYtALLAIRRgNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMT 146
Cdd:COG2884 100 VAL-PLRVTGK-SRKEIRRRVREVLDLVGLSDKAKALPHE-----LSGGEQQRVAIARALVNRPELLLADEPTGNLDPET 172
|
170 180
....*....|....*....|...
gi 767915018 147 ANQIVVLLVELARRNRIVVLTIH 169
Cdd:COG2884 173 SWEIMELLEEINRRGTTVLIATH 195
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
3-189 |
1.47e-17 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 80.50 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGrlgragtFL----GEVYVNGRALR---REQFQDCFSYVLQsDTLLSSLTVRETLhytallai 75
Cdd:cd03228 33 IVGPSGSGKSTLLKLLLR-------LYdptsGEILIDGVDLRdldLESLRKNIAYVPQ-DPFLFSGTIRENI-------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 76 rrgnpgsfqkkveavmaelslshvadrlignyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLV 155
Cdd:cd03228 97 ------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALR 140
|
170 180 190
....*....|....*....|....*....|....
gi 767915018 156 ELaRRNRIVVLTIHqpRSELFQLFDKIAILSFGE 189
Cdd:cd03228 141 AL-AKGKTVIVIAH--RLSTIRDADRIIVLDDGR 171
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
3-201 |
7.46e-17 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 79.80 E-value: 7.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGrlgragtFL----GEVYVNGRAL-RREQFQDCFSYVLQSDTLLSSLTVRETLhytaLLAIR- 76
Cdd:COG3840 30 ILGPSGAGKSTLLNLIAG-------FLppdsGRILWNGQDLtALPPAERPVSMLFQENNLFPHLTVAQNI----GLGLRp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 77 RGNPGSFQK-KVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLV 155
Cdd:COG3840 99 GLKLTAEQRaQVEQALERVGLAGLLDRLPGQ-----LSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVD 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 767915018 156 ELARRNRIVVLTI-HQPRsELFQLFDKIAILSFGELIFCGTPAEMLD 201
Cdd:COG3840 174 ELCRERGLTVLMVtHDPE-DAARIADRVLLVADGRIAADGPTAALLD 219
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
3-169 |
9.03e-17 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 79.37 E-value: 9.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMsgrLGRAGTFLGEVYVNGRA---LRREQ---FQDCFSYVLQSDTLLSSLTVRETLHYTalLAIR 76
Cdd:cd03292 32 LVGPSGAGKSTLLKLI---YKEELPTSGTIRVNGQDvsdLRGRAipyLRRKIGVVFQDFRLLPDRNVYENVAFA--LEVT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 77 RGNPGSFQKKVEAVMAELSLSHVADRLIGnyslgGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVE 156
Cdd:cd03292 107 GVPPREIRKRVPAALELVGLSHKHRALPA-----ELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKK 181
|
170
....*....|...
gi 767915018 157 LARRNRIVVLTIH 169
Cdd:cd03292 182 INKAGTTVVVATH 194
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
3-201 |
9.56e-17 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 79.58 E-value: 9.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNG---RALRREQFQDCFSYVLQsDTLLSSLTVRETlhytallaIRRGN 79
Cdd:cd03254 34 IVGPTGAGKTTLINLLMRFYDPQK---GQILIDGidiRDISRKSLRSMIGVVLQ-DTFLFSGTIMEN--------IRLGR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 80 PGSFQKKVEAVMAELSLSHVADRLIGNY------SLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVL 153
Cdd:cd03254 102 PNATDEEVIEAAKEAGAHDFIMKLPNGYdtvlgeNGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 767915018 154 LVELaRRNRIVVLTIHQPRSELFQlfDKIAILSFGELIFCGTPAEMLD 201
Cdd:cd03254 182 LEKL-MKGRTSIIIAHRLSTIKNA--DKILVLDDGKIIEEGTHDELLA 226
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-185 |
1.19e-16 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 83.10 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRALR---REQFQDCFSYVLQSDTLLSSlTVRETLhytaLLAIRRGN 79
Cdd:TIGR02857 353 LVGPSGAGKSTLLNLLLG-FVDPTE--GSIAVNGVPLAdadADSWRDQIAWVPQHPFLFAG-TIAENI----RLARPDAS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 80 PGSFQKKVEAV-----MAELSLSHvaDRLIGNYSlGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLL 154
Cdd:TIGR02857 425 DAEIREALERAgldefVAALPQGL--DTPIGEGG-AGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEAL 501
|
170 180 190
....*....|....*....|....*....|.
gi 767915018 155 VELArRNRIVVLTIHQPrsELFQLFDKIAIL 185
Cdd:TIGR02857 502 RALA-QGRTVLLVTHRL--ALAALADRIVVL 529
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
3-171 |
1.79e-16 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 82.41 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNG---RALRREQFQDCFSYVLQSDTLLSSlTVRETLhytallaiRRGN 79
Cdd:TIGR02868 366 ILGPSGSGKSTLLATLAGLLDPLQ---GEVTLDGvpvSSLDQDEVRRRVSVCAQDAHLFDT-TVRENL--------RLAR 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 80 PGSFQKKVEAVMAELSLSHVADRLIGNYS--LGG----ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVL 153
Cdd:TIGR02868 434 PDATDEELWAALERVGLADWLRALPDGLDtvLGEggarLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLED 513
|
170
....*....|....*...
gi 767915018 154 LVElARRNRIVVLTIHQP 171
Cdd:TIGR02868 514 LLA-ALSGRTVVLITHHL 530
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-171 |
1.93e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 77.99 E-value: 1.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 1 MCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRREQFQDCFSYVLQSDTLLSSLTVRETLHYTAllAIRRGNP 80
Cdd:PRK13539 31 LVLTGPNGSGKTTLLRLIAGLLPPAA---GTIKLDGGDIDDPDVAEACHYLGHRNAMKPALTVAENLEFWA--AFLGGEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 81 GSfqkkVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDcmTANQIVVLLVELARR 160
Cdd:PRK13539 106 LD----IAAALEAVGLAPLAHLPFGY-----LSAGQKRRVALARLLVSNRPIWILDEPTAALD--AAAVALFAELIRAHL 174
|
170
....*....|...
gi 767915018 161 NR--IVVLTIHQP 171
Cdd:PRK13539 175 AQggIVIAATHIP 187
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-198 |
2.87e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 79.77 E-value: 2.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLgRAGTflGEVYVNGRALRREQfQDCFSYVLQSDTLLSSLTVRETLHYtalLAIRRG-NPG 81
Cdd:COG4152 32 LLGPNGAGKTTTIRIILGIL-APDS--GEVLWDGEPLDPED-RRRIGYLPEERGLYPKMKVGEQLVY---LARLKGlSKA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 82 SFQKKVEAVMAELSLSHVADRLIGNYSLGgistgERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRN 161
Cdd:COG4152 105 EAKRRADEWLERLGLGDRANKKVEELSKG-----NQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKG 179
|
170 180 190
....*....|....*....|....*....|....*...
gi 767915018 162 RIVVLTIHQPRS-ElfQLFDKIAILSFGELIFCGTPAE 198
Cdd:COG4152 180 TTVIFSSHQMELvE--ELCDRIVIINKGRKVLSGSVDE 215
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
3-169 |
3.66e-16 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 77.08 E-value: 3.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRAL---------RREQFQdcfsYVLQS-DTLLSSLTVRETLHYTAL 72
Cdd:TIGR01166 23 LLGANGAGKSTLLLHLNGLLRPQS---GAVLIDGEPLdysrkglleRRQRVG----LVFQDpDDQLFAADVDQDVAFGPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 73 -LAirrGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIV 151
Cdd:TIGR01166 96 nLG---LSEAEVERRVREALTAVGASGLRERPTHC-----LSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGREQML 167
|
170
....*....|....*...
gi 767915018 152 VLLVELARRNRIVVLTIH 169
Cdd:TIGR01166 168 AILRRLRAEGMTVVISTH 185
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-200 |
3.75e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 79.12 E-value: 3.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRRE-----QFQDCFSYVLQS-DTLLSSLTVRETLHYTALlaiR 76
Cdd:PRK13636 37 ILGGNGAGKSTLFQNLNGILKPSS---GRILFDGKPIDYSrkglmKLRESVGMVFQDpDNQLFSASVYQDVSFGAV---N 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 77 RGNP-GSFQKKVEAVMAELSLSHVADRlignySLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLV 155
Cdd:PRK13636 111 LKLPeDEVRKRVDNALKRTGIEHLKDK-----PTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLV 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767915018 156 ELARRNRIVVLtIHQPRSELFQLF-DKIAILSFGELIFCGTPAEML 200
Cdd:PRK13636 186 EMQKELGLTII-IATHDIDIVPLYcDNVFVMKEGRVILQGNPKEVF 230
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
3-200 |
9.00e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 77.24 E-value: 9.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLGR-AGTFLGE------VYVNGRALRReqfqdcFSYVLQSDTLLSSLTVRETLhyTALLAI 75
Cdd:PRK10895 34 LLGPNGAGKTTTFYMVVGIVPRdAGNIIIDdedislLPLHARARRG------IGYLPQEASIFRRLSVYDNL--MAVLQI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 76 RRG-NPGSFQKKVEAVMAELSLSHVADrlignySLG-GISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVL 153
Cdd:PRK10895 106 RDDlSAEQREDRANELMEEFHIEHLRD------SMGqSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRI 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 767915018 154 LVELARRNRIVVLTIHQPRsELFQLFDKIAILSFGELIFCGTPAEML 200
Cdd:PRK10895 180 IEHLRDSGLGVLITDHNVR-ETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-200 |
1.02e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 76.98 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSgRLGRagTFLGEVYVNGRALRR---EQFQDCFSYVLQSDTLLSSLTVREtlhytaLLAIRRGN 79
Cdd:PRK11231 33 LIGPNGCGKSTLLKCFA-RLLT--PQSGTVFLGDKPISMlssRQLARRLALLPQHHLTPEGITVRE------LVAYGRSP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 80 PGSF--------QKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIV 151
Cdd:PRK11231 104 WLSLwgrlsaedNARVNQAMEQTRINHLADRRLTD-----LSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELM 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767915018 152 VLLVELARRNRIVVLTIHqprsELFQ---LFDKIAILSFGELIFCGTPAEML 200
Cdd:PRK11231 179 RLMRELNTQGKTVVTVLH----DLNQasrYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1-190 |
1.03e-15 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 76.14 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 1 MCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRREQFQD-CFSYVLQSDTLLSSLTVRETLHYTalLAIRRGN 79
Cdd:cd03301 29 VVLLGPSGCGKTTTLRMIAGLEEPTS---GRIYIGGRDVTDLPPKDrDIAMVFQNYALYPHMTVYDNIAFG--LKLRKVP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 80 PGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELAR 159
Cdd:cd03301 104 KDEIDERVREVAELLQIEHLLDRKPKQ-----LSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQ 178
|
170 180 190
....*....|....*....|....*....|.
gi 767915018 160 RNRIVVLTIHQPRSELFQLFDKIAILSFGEL 190
Cdd:cd03301 179 RLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
3-200 |
1.57e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 76.75 E-value: 1.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDaMSGRLGRAGTflGEVYVNGRAL---RREQFQDCFSYVLQSDTLLSSLTVREtlhytaLLAIRR-- 77
Cdd:PRK10575 42 LIGHNGSGKSTLLK-MLGRHQPPSE--GEILLDAQPLeswSSKAFARKVAYLPQQLPAAEGMTVRE------LVAIGRyp 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 78 --GNPGSF----QKKVEAVMAELSLSHVADRLIGnySLGGistGERRRVSIAAQLLQDPKVMLFDEPTTGLDcmTANQIV 151
Cdd:PRK10575 113 whGALGRFgaadREKVEEAISLVGLKPLAHRLVD--SLSG---GERQRAWIAMLVAQDSRCLLLDEPTSALD--IAHQVD 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 767915018 152 VL-LVE-LARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGTPAEML 200
Cdd:PRK10575 186 VLaLVHrLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELM 236
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
3-201 |
1.72e-15 |
|
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: 76.22 E-value: 1.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRALRREQFQD-CFSYVLQSDTLLSSLTVRETLHYTalLAIR----R 77
Cdd:cd03296 33 LLGPSGSGKTTLLRLIAG-LERPDS--GTILFGGEDATDVPVQErNVGFVFQHYALFRHMTVFDNVAFG--LRVKprseR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 78 GNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVEL 157
Cdd:cd03296 108 PPEAEIRAKVHELLKLVQLDWLADRYPAQ-----LSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 767915018 158 ARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGTPAEMLD 201
Cdd:cd03296 183 HDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYD 226
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-160 |
2.05e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 76.01 E-value: 2.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 1 MCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRAL-------RREQFQDCFSYVLQSDTLLSSLTVRETLHYTALl 73
Cdd:PRK11629 38 MAIVGSSGSGKSTLLHLLGG-LDTPTS--GDVIFNGQPMsklssaaKAELRNQKLGFIYQFHHLLPDFTALENVAMPLL- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 74 aIRRGNPGSFQKKVEAVMAELSLSHVAdrligNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVL 153
Cdd:PRK11629 114 -IGKKKPAEINSRALEMLAAVGLEHRA-----NHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQL 187
|
....*..
gi 767915018 154 LVELARR 160
Cdd:PRK11629 188 LGELNRL 194
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-200 |
3.34e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 78.71 E-value: 3.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLL-------DAMSGrlgragtflgEVYVNGRALRR---EQFQDCFSYVLQSDTLLSSlTVRETLhytaL 72
Cdd:PRK11160 371 LLGRTGCGKSTLLqlltrawDPQQG----------EILLNGQPIADyseAALRQAISVVSQRVHLFSA-TLRDNL----L 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 73 LAirrgNPGSFQKKVEAVMAELSLSHVADrliGNYSL------GG--ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDC 144
Cdd:PRK11160 436 LA----APNASDEALIEVLQQVGLEKLLE---DDKGLnawlgeGGrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDA 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767915018 145 MTANQIVVLLVELArRNRIVVLTIHqpRSELFQLFDKIAILSFGELIFCGTPAEML 200
Cdd:PRK11160 509 ETERQILELLAEHA-QNKTVLMITH--RLTGLEQFDRICVMDNGQIIEQGTHQELL 561
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-206 |
4.40e-15 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 78.90 E-value: 4.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 4 LGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRR--EQFQDCFSYVLQSDTLLSSLTVRETLHYTALLAIRRGNPG 81
Cdd:TIGR01257 962 LGHNGAGKTTTLSILTGLLPPTS---GTVLVGGKDIETnlDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEA 1038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 82 sfQKKVEAVMAELSLSHVAdrligNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRN 161
Cdd:TIGR01257 1039 --QLEMEAMLEDTGLHHKR-----NEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGR 1111
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 767915018 162 RIVVLTIHQPRSELfqLFDKIAILSFGELIFCGTPAemldFFNDC 206
Cdd:TIGR01257 1112 TIIMSTHHMDEADL--LGDRIAIISQGRLYCSGTPL----FLKNC 1150
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-208 |
4.40e-15 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 78.90 E-value: 4.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRR--EQFQDCFSYVLQSDTLLSSLTVRETLHYTALLairRGNP 80
Cdd:TIGR01257 1970 LLGVNGAGKTTTFKMLTGDTTVTS---GDATVAGKSILTniSDVHQNMGYCPQFDAIDDLLTGREHLYLYARL---RGVP 2043
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 81 GsfqKKVEAV----MAELSLSHVADRLIGNYSlggisTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVE 156
Cdd:TIGR01257 2044 A---EEIEKVanwsIQSLGLSLYADRLAGTYS-----GGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVS 2115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767915018 157 LARRNRIVVLTIHQpRSELFQLFDKIAILSFGELIFCGTPAEMLDFFNDcGY 208
Cdd:TIGR01257 2116 IIREGRAVVLTSHS-MEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGD-GY 2165
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
3-201 |
5.74e-15 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 74.44 E-value: 5.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLD-------AMSGRLGRAGTFLGevYVNGRALRREqfqdcFSYVLQSDTLLSSlTVRETlhytallaI 75
Cdd:cd03252 33 IVGRSGSGKSTLTKliqrfyvPENGRVLVDGHDLA--LADPAWLRRQ-----VGVVLQENVLFNR-SIRDN--------I 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 76 RRGNPGSFQKKVEAVmAELSLSHV--------ADRLIGNYSLGgISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTA 147
Cdd:cd03252 97 ALADPGMSMERVIEA-AKLAGAHDfiselpegYDTIVGEQGAG-LSGGQRQRIAIARALIHNPRILIFDEATSALDYESE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767915018 148 NQIVVLLVELArRNRIVVLTIHqpRSELFQLFDKIAILSFGELIFCGTPAEMLD 201
Cdd:cd03252 175 HAIMRNMHDIC-AGRTVIIIAH--RLSTVKNADRIIVMEKGRIVEQGSHDELLA 225
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3-199 |
6.20e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 75.11 E-value: 6.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRRE-----QFQDCFSYVLQ-SDTLLSSLTVRETLHYTALlair 76
Cdd:PRK13639 33 LLGPNGAGKSTLFLHFNGILKPTS---GEVLIKGEPIKYDkksllEVRKTVGIVFQnPDDQLFAPTVEEDVAFGPL---- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 77 rgNPG----SFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVV 152
Cdd:PRK13639 106 --NLGlskeEVEKRVKEALKAVGMEGFENKPPHH-----LSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMK 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 767915018 153 LLVELARRNRIVVLTIHQprSELFQLF-DKIAILSFGELIFCGTPAEM 199
Cdd:PRK13639 179 LLYDLNKEGITIIISTHD--VDLVPVYaDKVYVMSDGKIIKEGTPKEV 224
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
3-171 |
6.26e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 73.68 E-value: 6.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRALR--REQFQDCFSYVLQSDTLLSSLTVRETLHYTALLAirrGNP 80
Cdd:PRK13538 32 IEGPNGAGKTSLLRILAG-LARPDA--GEVLWQGEPIRrqRDEYHQDLLYLGHQPGIKTELTALENLRFYQRLH---GPG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 81 GSFQkkVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARR 160
Cdd:PRK13538 106 DDEA--LWEALAQVGLAGFEDVPVRQ-----LSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQ 178
|
170
....*....|.
gi 767915018 161 NRIVVLTIHQP 171
Cdd:PRK13538 179 GGMVILTTHQD 189
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
3-200 |
7.22e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 74.58 E-value: 7.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLgragTFLGEVYVNGRAL----------RReqfqdcfSYVLQSDTLLSSLTVretLHYTAL 72
Cdd:PRK03695 27 LVGPNGAGKSTLLARMAGLL----PGSGSIQFAGQPLeawsaaelarHR-------AYLSQQQTPPFAMPV---FQYLTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 73 LAIRRGNPGSFQKKVEAVMAELSLshvADRLigNYSLGGISTGERRRVSIAAQLLQ-------DPKVMLFDEPTTGLDCM 145
Cdd:PRK03695 93 HQPDKTRTEAVASALNEVAEALGL---DDKL--GRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDVA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767915018 146 TANQIVVLLVELARRNRIVVLTIHQPRSELFQLfDKIAILSFGELIFCGTPAEML 200
Cdd:PRK03695 168 QQAALDRLLSELCQQGIAVVMSSHDLNHTLRHA-DRVWLLKQGKLLASGRRDEVL 221
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
3-194 |
1.35e-14 |
|
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: 72.91 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRREQFQD-CFSYVLQSDTLLSSLTVRETLHytalLAIrrgNPG 81
Cdd:cd03298 29 IVGPSGSGKSTLLNLIAGFETPQS---GRVLINGVDVTAAPPADrPVSMLFQENNLFAHLTVEQNVG----LGL---SPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 82 -----SFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVE 156
Cdd:cd03298 99 lkltaEDRQAIEVALARVGLAGLEKRLPGE-----LSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLD 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 767915018 157 LARRNRIVVLTI-HQPrSELFQLFDKIAILSFGELIFCG 194
Cdd:cd03298 174 LHAETKMTVLMVtHQP-EDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
3-201 |
1.67e-14 |
|
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: 73.04 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRAL------RREqfqdcFSYVLQSDTLLSSLTVRETLHYTalLAIR 76
Cdd:cd03300 31 LLGPSGCGKTTLLRLIAGFETPTS---GEILLDGKDItnlpphKRP-----VNTVFQNYALFPHLTVFENIAFG--LRLK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 77 RGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVE 156
Cdd:cd03300 101 KLPKAEIKERVAEALDLVQLEGYANRKPSQ-----LSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKR 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 767915018 157 LARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGTPAEMLD 201
Cdd:cd03300 176 LQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYE 220
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3-200 |
1.76e-14 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 76.36 E-value: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGrlgragtFL----GEVYVNG---RALRREQFQDCFSYVLQsDTLLSSLTVREtlhytallAI 75
Cdd:COG1132 371 LVGPSGSGKSTLVNLLLR-------FYdptsGRILIDGvdiRDLTLESLRRQIGVVPQ-DTFLFSGTIRE--------NI 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 76 RRGNPGSFQKKVEAVMAELSLSHVADRL-------IGNyslGGI--STGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMT 146
Cdd:COG1132 435 RYGRPDATDEEVEEAAKAAQAHEFIEALpdgydtvVGE---RGVnlSGGQRQRIAIARALLKDPPILILDEATSALDTET 511
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 147 ANQIVVLLVELaRRNRIVVL------TIhqprselfQLFDKIAILSFGELIFCGTPAEML 200
Cdd:COG1132 512 EALIQEALERL-MKGRTTIViahrlsTI--------RNADRILVLDDGRIVEQGTHEELL 562
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
3-201 |
1.80e-14 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 73.03 E-value: 1.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLL-------DAMSGRlgragtflgeVYVNGRALRR---EQFQDCFSYVLQsDTLLSSLTVRETlhytal 72
Cdd:cd03253 32 IVGPSGSGKSTILrllfrfyDVSSGS----------ILIDGQDIREvtlDSLRRAIGVVPQ-DTVLFNDTIGYN------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 73 laIRRGNPGSFQKKVEAVmAELSlsHVADRLIG---NYS--LG--G--ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLD 143
Cdd:cd03253 95 --IRYGRPDATDEEVIEA-AKAA--QIHDKIMRfpdGYDtiVGerGlkLSGGEKQRVAIARAILKNPPILLLDEATSALD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767915018 144 CMTANQIVVLLVELArRNRIVVLTIHQPRSELFQlfDKIAILSFGELIFCGTPAEMLD 201
Cdd:cd03253 170 THTEREIQAALRDVS-KGRTTIVIAHRLSTIVNA--DKIIVLKDGRIVERGTHEELLA 224
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
3-200 |
2.43e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 74.88 E-value: 2.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALR----REQFQDCFSyVLQSDTLLSSLTVRETL------HYTal 72
Cdd:PRK09536 34 LVGPNGAGKTTLLRAINGTLTPTA---GTVLVAGDDVEalsaRAASRRVAS-VPQDTSLSFEFDVRQVVemgrtpHRS-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 73 laiRRGNPGSFQKK-VEAVMAELSLSHVADRlignySLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIV 151
Cdd:PRK09536 108 ---RFDTWTETDRAaVERAMERTGVAQFADR-----PVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767915018 152 VLLVELARRNRIVVLTIHQprSELFQLF-DKIAILSFGELIFCGTPAEML 200
Cdd:PRK09536 180 ELVRRLVDDGKTAVAAIHD--LDLAARYcDELVLLADGRVRAAGPPADVL 227
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
3-190 |
3.12e-14 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 70.71 E-value: 3.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALR---REQFQDCFSYVLQSDTLLSsltvretlhytallairrgn 79
Cdd:cd03246 33 IIGPSGSGKSTLARLILGLLRPTS---GRVRLDGADISqwdPNELGDHVGYLPQDDELFS-------------------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 80 pGSfqkkveavmaelslshVADRLignyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELAR 159
Cdd:cd03246 90 -GS----------------IAENI--------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKA 144
|
170 180 190
....*....|....*....|....*....|.
gi 767915018 160 RNRIVVLTIHQPrsELFQLFDKIAILSFGEL 190
Cdd:cd03246 145 AGATRIVIAHRP--ETLASADRILVLEDGRV 173
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
3-201 |
3.31e-14 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 74.03 E-value: 3.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRalrreqfqDCFS----------YVLQSDTLLSSLTVRETLHYTal 72
Cdd:COG1118 33 LLGPSGSGKTTLLRIIAG-LETPDS--GRIVLNGR--------DLFTnlpprerrvgFVFQHYALFPHMTVAENIAFG-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 73 LAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVV 152
Cdd:COG1118 100 LRVRPPSKAEIRARVEELLELVQLEGLADRYPSQ-----LSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRR 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767915018 153 LLVELARRNRIVVLTI-HQpRSELFQLFDKIAILSFGELIFCGTPAEMLD 201
Cdd:COG1118 175 WLRRLHDELGGTTVFVtHD-QEEALELADRVVVMNQGRIEQVGTPDEVYD 223
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-170 |
3.40e-14 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 71.79 E-value: 3.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 2 CILGSSGSGKTTLLDAMSgRLGRAGTflGEVYVNG----------RALRREqfqdcFSYVLQSDTLLSSLTVRETLHYtA 71
Cdd:cd03262 30 VIIGPSGSGKSTLLRCIN-LLEEPDS--GTIIIDGlkltddkkniNELRQK-----VGMVFQQFNLFPHLTVLENITL-A 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 72 LLAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIV 151
Cdd:cd03262 101 PIKVKGMSKAEAEERALELLEKVGLADKADAYPAQ-----LSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVL 175
|
170
....*....|....*....
gi 767915018 152 VLLVELARRNRIVVLTIHQ 170
Cdd:cd03262 176 DVMKDLAEEGMTMVVVTHE 194
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
5-201 |
5.05e-14 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 71.88 E-value: 5.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 5 GSSGSGKTTLL-------DAMSGRLGRAGTFLGEVYVNgrALRREqfqdcFSYVLQsDTLLSSLTVRETlhytallaIRR 77
Cdd:cd03251 35 GPSGSGKSTLVnliprfyDVDSGRILIDGHDVRDYTLA--SLRRQ-----IGLVSQ-DVFLFNDTVAEN--------IAY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 78 GNPGSFQKKVEAVmAELSLSH-VADRLIGNY--SLG--GI--STGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQI 150
Cdd:cd03251 99 GRPGATREEVEEA-ARAANAHeFIMELPEGYdtVIGerGVklSGGQRQRIAIARALLKDPPILILDEATSALDTESERLV 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 767915018 151 VVLLVELArRNRIVVLTIHqpRSELFQLFDKIAILSFGELIFCGTPAEMLD 201
Cdd:cd03251 178 QAALERLM-KNRTTFVIAH--RLSTIENADRIVVLEDGKIVERGTHEELLA 225
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
2-201 |
5.39e-14 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 71.56 E-value: 5.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 2 CILGSSGSGKTTLLdamsgrlgRAGTFL-----GEVYVNG----------RALRREqfqdcFSYVLQSDTLLSSLTVRE- 65
Cdd:COG1126 31 VIIGPSGSGKSTLL--------RCINLLeepdsGTITVDGedltdskkdiNKLRRK-----VGMVFQQFNLFPHLTVLEn 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 66 -TLhytALLAIRRgnpgsfQKKVEAV---MAELS---LSHVADRlignY--SLGGistGERRRVSIAAQLLQDPKVMLFD 136
Cdd:COG1126 98 vTL---APIKVKK------MSKAEAEeraMELLErvgLADKADA----YpaQLSG---GQQQRVAIARALAMEPKVMLFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767915018 137 EPTTGLDCMTANQIVVLLVELARRNR-IVVLTiHqprsEL-F--QLFDKIAILSFGELIFCGTPAEMLD 201
Cdd:COG1126 162 EPTSALDPELVGEVLDVMRDLAKEGMtMVVVT-H----EMgFarEVADRVVFMDGGRIVEEGPPEEFFE 225
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-170 |
5.45e-14 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 71.97 E-value: 5.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 1 MCILGSSGSGKTTLLDAM-------SGRLGRAGT---FLGEVYVN-GRALRREqfqdcFSYVLQSDTLLSSLTVRETLhY 69
Cdd:PRK11124 31 LVLLGPSGAGKSSLLRVLnllemprSGTLNIAGNhfdFSKTPSDKaIRELRRN-----VGMVFQQYNLWPHLTVQQNL-I 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 70 TALLAIRRGNPGSFQKKVEAVMAELSLSHVADRlignYSLGgISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQ 149
Cdd:PRK11124 105 EAPCRVLGLSKDQALARAEKLLERLRLKPYADR----FPLH-LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQ 179
|
170 180
....*....|....*....|.
gi 767915018 150 IVVLLVELARRNRIVVLTIHQ 170
Cdd:PRK11124 180 IVSIIRELAETGITQVIVTHE 200
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
3-191 |
7.61e-14 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 71.08 E-value: 7.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNG--------RALRREqfqdcFSYVLQSDTLLSSlTVRETLHYTALLA 74
Cdd:cd03245 35 IIGRVGSGKSTLLKLLAG-LYKPTS--GSVLLDGtdirqldpADLRRN-----IGYVPQDVTLFYG-TLRDNITLGAPLA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 75 irrgnpgsfqkKVEAVMAELSLSHVADrLIGNYSLG----------GISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDC 144
Cdd:cd03245 106 -----------DDERILRAAELAGVTD-FVNKHPNGldlqigergrGLSGGQRQAVALARALLNDPPILLLDEPTSAMDM 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 767915018 145 MTANQIVVLLVELARRNRIVVLTiHqpRSELFQLFDKIAILSFGELI 191
Cdd:cd03245 174 NSEERLKERLRQLLGDKTLIIIT-H--RPSLLDLVDRIIVMDSGRIV 217
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
2-204 |
7.93e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 72.58 E-value: 7.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 2 CILGSSGSGKTTLLDAMSGRL-GRAGTF-LGEVYVNGRALRREQFQDCFSYVLQSDTLLSSLT--VRETLHY-----TAL 72
Cdd:PRK13631 56 FIIGNSGSGKSTLVTHFNGLIkSKYGTIqVGDIYIGDKKNNHELITNPYSKKIKNFKELRRRVsmVFQFPEYqlfkdTIE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 73 LAIRRGNPGSFQKKVEAvmAELSLSHVADRLIGNYSLG----GISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTAN 148
Cdd:PRK13631 136 KDIMFGPVALGVKKSEA--KKLAKFYLNKMGLDDSYLErspfGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEH 213
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767915018 149 QIVVLLVELARRNRIVVLTIHQpRSELFQLFDKIAILSFGELIFCGTPAEMldFFN 204
Cdd:PRK13631 214 EMMQLILDAKANNKTVFVITHT-MEHVLEVADEVIVMDKGKILKTGTPYEI--FTD 266
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-200 |
8.43e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 71.62 E-value: 8.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSgRL-----------GRAGTFLGEVY-VNGRALRREqfqdcFSYVLQSDTLLSSLTVRETLHYt 70
Cdd:PRK14246 41 IMGPSGSGKSTLLKVLN-RLieiydskikvdGKVLYFGKDIFqIDAIKLRKE-----VGMVFQQPNPFPHLSIYDNIAY- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 71 ALLAIRRGNPGSFQKKVEAVMAELSL-SHVADRLigNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQ 149
Cdd:PRK14246 114 PLKSHGIKEKREIKKIVEECLRKVGLwKEVYDRL--NSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQA 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 767915018 150 IVVLLVELARRNRIVVLTiHQPRsELFQLFDKIAILSFGELIFCGTPAEML 200
Cdd:PRK14246 192 IEKLITELKNEIAIVIVS-HNPQ-QVARVADYVAFLYNGELVEWGSSNEIF 240
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1-194 |
8.98e-14 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 70.39 E-value: 8.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 1 MCILGSSGSGKTTLLDAMsgrlgrAGTFL---GEVYVNGRALRREQFQDcFSYVLQSDTLLSSLTVRETLHYTALLairR 77
Cdd:cd03269 29 FGLLGPNGAGKTTTIRMI------LGIILpdsGEVLFDGKPLDIAARNR-IGYLPEERGLYPKMKVIDQLVYLAQL---K 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 78 G-NPGSFQKKVEAVMAELSLSHVADRlignySLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVE 156
Cdd:cd03269 99 GlKKEEARRRIDEWLERLELSEYANK-----RVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRE 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 767915018 157 LARRNRIVVLTIHQpRSELFQLFDKIAILSFGELIFCG 194
Cdd:cd03269 174 LARAGKTVILSTHQ-MELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
3-191 |
1.38e-13 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 70.29 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLGRAGTFL--GEVYVNGR----------ALRREqfqdcFSYVLQSDTLLSsLTVRETLHYT 70
Cdd:cd03260 31 LIGPSGCGKSTLLRLLNRLNDLIPGAPdeGEVLLDGKdiydldvdvlELRRR-----VGMVFQKPNPFP-GSIYDNVAYG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 71 alLAIRrgnpGSFQKKVEAVMAELSLS------HVADRLIGnyslGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDC 144
Cdd:cd03260 105 --LRLH----GIKLKEELDERVEEALRkaalwdEVKDRLHA----LGLSGGQQQRLCLARALANEPEVLLLDEPTSALDP 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767915018 145 MTANQIVVLLVELARRNRIVVLT--IHQPRSelfqLFDKIAILSFGELI 191
Cdd:cd03260 175 ISTAKIEELIAELKKEYTIVIVThnMQQAAR----VADRTAFLLNGRLV 219
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-158 |
1.51e-13 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 70.43 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 1 MCILGSSGSGKTTLLDAM-------SGRLGRAG-TFLGEVYVN---GRALRREqfqdcFSYVLQSDTLLSSLTVRETLhY 69
Cdd:COG4161 31 LVLLGPSGAGKSSLLRVLnlletpdSGQLNIAGhQFDFSQKPSekaIRLLRQK-----VGMVFQQYNLWPHLTVMENL-I 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 70 TALLAIRRGNPGSFQKKVEAVMAELSLSHVADRlignYSLGgISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQ 149
Cdd:COG4161 105 EAPCKVLGLSKEQAREKAMKLLARLRLTDKADR----FPLH-LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQ 179
|
....*....
gi 767915018 150 IVVLLVELA 158
Cdd:COG4161 180 VVEIIRELS 188
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-190 |
2.09e-13 |
|
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: 68.61 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRReqfqdcfsyvlqsdtllssLTVREtlhytallAIRRGN--- 79
Cdd:cd03215 31 IAGLVGNGQTELAEALFGLRPPAS---GEITLDGKPVTR-------------------RSPRD--------AIRAGIayv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 80 PGSfqKKVEAVMAELSlshVADRLIGNYSLGGistGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELAR 159
Cdd:cd03215 81 PED--RKREGLVLDLS---VAENIALSSLLSG---GNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELAD 152
|
170 180 190
....*....|....*....|....*....|..
gi 767915018 160 RNR-IVVLTIHQPrsELFQLFDKIAILSFGEL 190
Cdd:cd03215 153 AGKaVLLISSELD--ELLGLCDRILVMYEGRI 182
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-160 |
2.31e-13 |
|
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: 71.24 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 1 MCILGSSGSGKTTLLDAMSGRLGRAGTFLGEVYVNGR---ALRREQFQD----CFSYVLQSDtlLSSL----TVRETLHY 69
Cdd:COG0444 34 LGLVGESGSGKSTLARAILGLLPPPGITSGEILFDGEdllKLSEKELRKirgrEIQMIFQDP--MTSLnpvmTVGDQIAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 70 tALLAIRRGNPGSFQKKVEAVMAELSLSHVADRLiGNY--SLGGistGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTA 147
Cdd:COG0444 112 -PLRIHGGLSKAEARERAIELLERVGLPDPERRL-DRYphELSG---GMRQRVMIARALALEPKLLIADEPTTALDVTIQ 186
|
170
....*....|...
gi 767915018 148 NQIVVLLVELARR 160
Cdd:COG0444 187 AQILNLLKDLQRE 199
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
3-172 |
2.44e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 69.81 E-value: 2.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLL-------DAMSGRLGRAGTFLGEVYVNGRALRREQFqdcFSYVLQSDTLLSSLTVRETLHYTALLai 75
Cdd:PRK10584 41 LIGESGSGKSTLLailagldDGSSGEVSLVGQPLHQMDEEARAKLRAKH---VGFVFQSFMLIPTLNALENVELPALL-- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 76 RRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLV 155
Cdd:PRK10584 116 RGESSRQSRNGAKALLEQLGLGKRLDHLPAQ-----LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLF 190
|
170
....*....|....*...
gi 767915018 156 ELARR-NRIVVLTIHQPR 172
Cdd:PRK10584 191 SLNREhGTTLILVTHDLQ 208
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1-194 |
3.50e-13 |
|
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: 68.11 E-value: 3.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 1 MCILGSSGSGKTTLLDAMSGRLGRAgtfLGEVYVNGR--ALRREQFQDCFSYVLQSDTLLSSlTVRETLHytallaiRRg 78
Cdd:cd03247 31 IALLGRSGSGKSTLLQLLTGDLKPQ---QGEITLDGVpvSDLEKALSSLISVLNQRPYLFDT-TLRNNLG-------RR- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 79 npgsfqkkveavmaelslshvadrlignyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELA 158
Cdd:cd03247 99 ---------------------------------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVL 145
|
170 180 190
....*....|....*....|....*....|....*.
gi 767915018 159 rRNRIVVLTIHQPRSelFQLFDKIAILSFGELIFCG 194
Cdd:cd03247 146 -KDKTLIWITHHLTG--IEHMDKILFLENGKIIMQG 178
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-200 |
3.66e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 70.02 E-value: 3.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 2 CILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRRE---QFQDCFSYVLQS-DTLLSSLTVRETLHYTalLAIRR 77
Cdd:PRK13632 39 AILGHNGSGKSTISKILTGLLKPQS---GEIKIDGITISKEnlkEIRKKIGIIFQNpDNQFIGATVEDDIAFG--LENKK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 78 GNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVEL 157
Cdd:PRK13632 114 VPPKKMKDIIDDLAKKVGMEDYLDKEPQN-----LSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDL 188
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 767915018 158 ARRNRIVVLTIHQPRSELFqLFDKIAILSFGELIFCGTPAEML 200
Cdd:PRK13632 189 RKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEIL 230
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
3-169 |
4.20e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 69.91 E-value: 4.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSG--RLGRagtflGEVYVNGRALRREQFQDCFSYVLQSDTLLSSLTVretLHYTALLAIRRGNP 80
Cdd:PRK15056 38 LVGVNGSGKSTLFKALMGfvRLAS-----GKISILGQPTRQALQKNLVAYVPQSEEVDWSFPV---LVEDVVMMGRYGHM 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 81 GSF-------QKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVL 153
Cdd:PRK15056 110 GWLrrakkrdRQIVTAALARVDMVEFRHRQIGE-----LSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISL 184
|
170
....*....|....*.
gi 767915018 154 LVELARRNRIVVLTIH 169
Cdd:PRK15056 185 LRELRDEGKTMLVSTH 200
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-195 |
5.72e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 69.27 E-value: 5.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLGRAGTFLGEVYVNGRALRRE--------QFQDCFSYVLQSDTLLSSLTVRETLHYTAL-- 72
Cdd:PRK09984 35 LLGPSGSGKSTLLRHLSGLITGDKSAGSHIELLGRTVQREgrlardirKSRANTGYIFQQFNLVNRLSVLENVLIGALgs 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 73 -----LAIRRGNPGSFQKKVEAvMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTA 147
Cdd:PRK09984 115 tpfwrTCFSWFTREQKQRALQA-LTRVGMVHFAHQRVST-----LSGGQQQRVAIARALMQQAKVILADEPIASLDPESA 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767915018 148 NQIVVLLVELARRNRI-VVLTIHQPRSELfQLFDKIAILSFGELIFCGT 195
Cdd:PRK09984 189 RIVMDTLRDINQNDGItVVVTLHQVDYAL-RYCERIVALRQGHVFYDGS 236
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-198 |
6.50e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 71.41 E-value: 6.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGrlgragtFL---GEVYVNG---RALRREQFQDCFSYVLQSDTLLSSlTVRETLhytaLLair 76
Cdd:PRK11174 381 LVGPSGAGKTSLLNALLG-------FLpyqGSLKINGielRELDPESWRKHLSWVGQNPQLPHG-TLRDNV----LL--- 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 77 rGNPGSFQKKVEAVMAELSLSHVADRL-------IGNYSlGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQ 149
Cdd:PRK11174 446 -GNPDASDEQLQQALENAWVSEFLPLLpqgldtpIGDQA-AGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQL 523
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 767915018 150 IVVLLVELARRNRIVVLTiHQprseLFQL--FDKIAILSFGELIFCGTPAE 198
Cdd:PRK11174 524 VMQALNAASRRQTTLMVT-HQ----LEDLaqWDQIWVMQDGQIVQQGDYAE 569
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
3-200 |
1.41e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 68.31 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRL-----GRAGTFLGEVYVNGRALRREQFQD--CFSYVL-QSDTLLSSLTVRETLHYTALLA 74
Cdd:PRK13547 32 LLGRNGAGKSTLLKALAGDLtgggaPRGARVTGDVTLNGEPLAAIDAPRlaRLRAVLpQAAQPAFAFSAREIVLLGRYPH 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 75 IRRGNPGSFQKKvEAVMAELSLSHvADRLIGNySLGGISTGERRRVSIA---AQL------LQDPKVMLFDEPTTGLDCM 145
Cdd:PRK13547 112 ARRAGALTHRDG-EIAWQALALAG-ATALVGR-DVTTLSGGELARVQFArvlAQLwpphdaAQPPRYLLLDEPTAALDLA 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767915018 146 TANQIVVLLVELARRNRIVVLTI-HQPRSELfQLFDKIAILSFGELIFCGTPAEML 200
Cdd:PRK13547 189 HQHRLLDTVRRLARDWNLGVLAIvHDPNLAA-RHADRIAMLADGAIVAHGAPADVL 243
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
3-171 |
1.64e-12 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 70.14 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMsGRLGRAGTflGEVYVNGR-----------ALRREQFqdcfSYVLQSDTLLSSLTVRETLHYTA 71
Cdd:PRK10535 39 IVGASGSGKSTLMNIL-GCLDKPTS--GTYRVAGQdvatldadalaQLRREHF----GFIFQRYHLLSHLTAAQNVEVPA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 72 LLAirrGNP-GSFQKKVEAVMAELSLshvADRLigNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQI 150
Cdd:PRK10535 112 VYA---GLErKQRLLRAQELLQRLGL---EDRV--EYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEV 183
|
170 180
....*....|....*....|.
gi 767915018 151 VVLLVELARRNRIVVLTIHQP 171
Cdd:PRK10535 184 MAILHQLRDRGHTVIIVTHDP 204
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
3-170 |
2.43e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 67.30 E-value: 2.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLdamsgrlgRAGTFL-----GEVYVNGRALR-------------REQFQDC---FSYVLQSDTLLSSL 61
Cdd:PRK10619 36 IIGSSGSGKSTFL--------RCINFLekpseGSIVVNGQTINlvrdkdgqlkvadKNQLRLLrtrLTMVFQHFNLWSHM 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 62 TVRETLHYTALLAIrrgnpgSFQKKVEAVMAELSLSHVA--DRLIGNYSLGgISTGERRRVSIAAQLLQDPKVMLFDEPT 139
Cdd:PRK10619 108 TVLENVMEAPIQVL------GLSKQEARERAVKYLAKVGidERAQGKYPVH-LSGGQQQRVSIARALAMEPEVLLFDEPT 180
|
170 180 190
....*....|....*....|....*....|.
gi 767915018 140 TGLDCMTANQIVVLLVELARRNRIVVLTIHQ 170
Cdd:PRK10619 181 SALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-198 |
2.63e-12 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 67.48 E-value: 2.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 2 CILGSSGSGKTTLLDAMSGRLgRAGTflGEVYVNG-----------RALRRE-----QF---QdcfsyvlqsdtlLSSLT 62
Cdd:TIGR04521 35 AIIGHTGSGKSTLIQHLNGLL-KPTS--GTVTIDGrditakkkkklKDLRKKvglvfQFpehQ------------LFEET 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 63 VRETLHYtallairrGnPGSF-------QKKVEAVMAELSLSH-VADRlignySLGGISTGERRRVSIAAQLLQDPKVML 134
Cdd:TIGR04521 100 VYKDIAF--------G-PKNLglseeeaEERVKEALELVGLDEeYLER-----SPFELSGGQMRRVAIAGVLAMEPEVLI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767915018 135 FDEPTTGLDCMTANQIVVLLVELAR-RNRIVVLTIHQpRSELFQLFDKIAILSFGELIFCGTPAE 198
Cdd:TIGR04521 166 LDEPTAGLDPKGRKEILDLFKRLHKeKGLTVILVTHS-MEDVAEYADRVIVMHKGKIVLDGTPRE 229
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
3-191 |
2.65e-12 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 68.29 E-value: 2.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSgRLGRAGTflGEVYVNGR--------ALRREQ------FQDcFSyvlqsdtLLSSLTVRETLh 68
Cdd:PRK11153 36 VIGASGAGKSTLIRCIN-LLERPTS--GRVLVDGQdltalsekELRKARrqigmiFQH-FN-------LLSSRTVFDNV- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 69 ytAL-LAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTA 147
Cdd:PRK11153 104 --ALpLELAGTPKAEIKARVTELLELVGLSDKADRYPAQ-----LSGGQKQRVAIARALASNPKVLLCDEATSALDPATT 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 767915018 148 NQIVVLLVELARRNRIVVLTI-HQpRSELFQLFDKIAILSFGELI 191
Cdd:PRK11153 177 RSILELLKDINRELGLTIVLItHE-MDVVKRICDRVAVIDAGRLV 220
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
3-213 |
2.79e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 67.45 E-value: 2.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLG-RAGTF-LGEVYVNGRALRREqfqdcFSYVLQSDTLLSSLTVRETLHYTALLAIRRG-- 78
Cdd:PRK13643 37 LIGHTGSGKSTLLQHLNGLLQpTEGKVtVGDIVVSSTSKQKE-----IKPVRKKVGVVFQFPESQLFEETVLKDVAFGpq 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 79 NPGSFQKKVEAVMAElSLSHVA-DRLIGNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVEL 157
Cdd:PRK13643 112 NFGIPKEKAEKIAAE-KLEMVGlADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESI 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767915018 158 ARRNRIVVLTIHQpRSELFQLFDKIAILSFGELIFCGTPAEM---LDFF--NDCGYPCPEH 213
Cdd:PRK13643 191 HQSGQTVVLVTHL-MDDVADYADYVYLLEKGHIISCGTPSDVfqeVDFLkaHELGVPKATH 250
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-201 |
3.03e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 67.93 E-value: 3.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTT----LLDAMSGRLGRAgTFLGE-VYVNGRALRREqfqdcFSYVLQSDTLLSSLTVRETL----HYTALL 73
Cdd:PRK13536 72 LLGPNGAGKSTiarmILGMTSPDAGKI-TVLGVpVPARARLARAR-----IGVVPQFDNLDLEFTVRENLlvfgRYFGMS 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 74 AirrgnpgsfqKKVEAVMAEL----SLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQ 149
Cdd:PRK13536 146 T----------REIEAVIPSLlefaRLESKADARVSD-----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHL 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767915018 150 IVVLLVELARRNRIVVLTIHQpRSELFQLFDKIAILSFGELIFCGTPAEMLD 201
Cdd:PRK13536 211 IWERLRSLLARGKTILLTTHF-MEEAERLCDRLCVLEAGRKIAEGRPHALID 261
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
5-199 |
3.03e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 68.13 E-value: 3.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 5 GSSGSGKTTLL-------DAMSGRLgragtFLGEVYVN-----GRALrreqfqdcfSYVLQSDTLLSSLTVRETLHYTAL 72
Cdd:PRK11000 36 GPSGCGKSTLLrmiagleDITSGDL-----FIGEKRMNdvppaERGV---------GMVFQSYALYPHLSVAENMSFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 73 LAirRGNPGSFQKKVEAVMAELSLSHVADRlignySLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVV 152
Cdd:PRK11000 102 LA--GAKKEEINQRVNQVAEVLQLAHLLDR-----KPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRI 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 767915018 153 LLVELARR-NRIVVLTIHQpRSELFQLFDKIAILSFGELIFCGTPAEM 199
Cdd:PRK11000 175 EISRLHKRlGRTMIYVTHD-QVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-160 |
3.62e-12 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 68.94 E-value: 3.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSgRLGRAGtflGEVYVNG-----------RALRRE-Q--FQDCFSyvlqsdtllsSL----TVR 64
Cdd:COG4172 317 LVGESGSGKSTLGLALL-RLIPSE---GEIRFDGqdldglsrralRPLRRRmQvvFQDPFG----------SLsprmTVG 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 65 ET------LHYTALLAIRRgnpgsfQKKVEAVMAELSLSH-VADRLIGNYSlgGistGERRRVSIAAQLLQDPKVMLFDE 137
Cdd:COG4172 383 QIiaeglrVHGPGLSAAER------RARVAEALEEVGLDPaARHRYPHEFS--G---GQRQRIAIARALILEPKLLVLDE 451
|
170 180
....*....|....*....|...
gi 767915018 138 PTTGLDCMTANQIVVLLVELARR 160
Cdd:COG4172 452 PTSALDVSVQAQILDLLRDLQRE 474
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-200 |
3.73e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 66.47 E-value: 3.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSG--RLGRAGTFLGEVYVNGRAL---------RREQFqdcfsyVLQSDTLLSSLTVRETLHYTA 71
Cdd:PRK14247 34 LMGPSGSGKSTLLRVFNRliELYPEARVSGEVYLDGQDIfkmdvielrRRVQM------VFQIPNPIPNLSIFENVALGL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 72 LLAIRRGNPGSFQKKVEAVMAELSL-SHVADRLigNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQI 150
Cdd:PRK14247 108 KLNRLVKSKKELQERVRWALEKAQLwDEVKDRL--DAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKI 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767915018 151 VVLLVELARRNRIVVLTiHQPrSELFQLFDKIAILSFGELIFCGTPAEML 200
Cdd:PRK14247 186 ESLFLELKKDMTIVLVT-HFP-QQAARISDYVAFLYKGQIVEWGPTREVF 233
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
3-198 |
4.28e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 66.99 E-value: 4.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNG----------RALRRE-----QFQDcfsYVLQSDTLLSSLtvretl 67
Cdd:PRK13637 38 LIGHTGSGKSTLIQHLNGLLKPTS---GKIIIDGvditdkkvklSDIRKKvglvfQYPE---YQLFEETIEKDI------ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 68 hytALLAIRRG-NPGSFQKKVEAVMAELSLSH--VADRlignySLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDC 144
Cdd:PRK13637 106 ---AFGPINLGlSEEEIENRVKRAMNIVGLDYedYKDK-----SPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767915018 145 MTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGTPAE 198
Cdd:PRK13637 178 KGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPRE 231
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-213 |
4.36e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 66.40 E-value: 4.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSG--RLGRAGTFLGEVYVNGRALRRE-----QFQDCFSYVLQSDTLLSSLTVRET----LHYTA 71
Cdd:PRK14267 35 LMGPSGCGKSTLLRTFNRllELNEEARVEGEVRLFGRNIYSPdvdpiEVRREVGMVFQYPNPFPHLTIYDNvaigVKLNG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 72 LLAIRrgnpGSFQKKVEAVMAELSL-SHVADRLigNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQI 150
Cdd:PRK14267 115 LVKSK----KELDERVEWALKKAALwDEVKDRL--NDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKI 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767915018 151 VVLLVELARRNRIVVLTiHQPrSELFQLFDKIAILSFGELIFCGtPAEMLdFFNdcgypcPEH 213
Cdd:PRK14267 189 EELLFELKKEYTIVLVT-HSP-AQAARVSDYVAFLYLGKLIEVG-PTRKV-FEN------PEH 241
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-198 |
5.46e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 67.42 E-value: 5.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 1 MCILGSSGSGKTTLLDAM-------SGRLGRAGTFLGEVYVNGRALrreqfqdcfSYVLQSDTLLSSLTVRETLHY--TA 71
Cdd:PRK10851 31 VALLGPSGSGKTTLLRIIaglehqtSGHIRFHGTDVSRLHARDRKV---------GFVFQHYALFRHMTVFDNIAFglTV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 72 LLAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIV 151
Cdd:PRK10851 102 LPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQ-----LSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 767915018 152 VLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGTPAE 198
Cdd:PRK10851 177 RWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQ 223
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
3-199 |
6.26e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 66.36 E-value: 6.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRREQFQDCFSYV----LQSDTLLSSLTVRETLhytALLAIRRG 78
Cdd:PRK13652 35 VIGPNGAGKSTLFRHFNGILKPTS---GSVLIRGEPITKENIREVRKFVglvfQNPDDQIFSPTVEQDI---AFGPINLG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 79 -NPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVEL 157
Cdd:PRK13652 109 lDEETVAHRVSSALHMLGLEELRDRVPHH-----LSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 767915018 158 ARR-NRIVVLTIHQpRSELFQLFDKIAILSFGELIFCGTPAEM 199
Cdd:PRK13652 184 PETyGMTVIFSTHQ-LDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
3-191 |
9.24e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 66.82 E-value: 9.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRALRREQFQDCFS-------YVLQSDTLLSSLTVRETLHYtallAI 75
Cdd:PRK11144 29 IFGRSGAGKTSLINAISG-LTRPQK--GRIVLNGRVLFDAEKGICLPpekrrigYVFQDARLFPHYKVRGNLRY----GM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 76 RRGNPGSFQKKVEAvmaeLSLSHVADRLIGnySLGGistGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLV 155
Cdd:PRK11144 102 AKSMVAQFDKIVAL----LGIEPLLDRYPG--SLSG---GEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLE 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 767915018 156 ELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELI 191
Cdd:PRK11144 173 RLAREINIPILYVSHSLDEILRLADRVVVLEQGKVK 208
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-169 |
9.45e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 66.26 E-value: 9.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGR--ALRREQFQDCFSYVL-QSDTLLSSLTVRETLHYTAllAIRRGN 79
Cdd:COG4586 53 FIGPNGAGKSTTIKMLTGILVPTS---GEVRVLGYvpFKRRKEFARRIGVVFgQRSQLWWDLPAIDSFRLLK--AIYRIP 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 80 PGSFQKKVEAVMAELSLSHVADRLIGNYSLGgistgERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVEL-A 158
Cdd:COG4586 128 DAEYKKRLDELVELLDLGELLDTPVRQLSLG-----QRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnR 202
|
170
....*....|.
gi 767915018 159 RRNRIVVLTIH 169
Cdd:COG4586 203 ERGTTILLTSH 213
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-201 |
1.24e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 65.98 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSG-RLGRAGT--FLGEVyVNGRALRREQFqdcFSYVLQSDTLLSSLTVRETL----HYTALLAi 75
Cdd:PRK13537 38 LLGPNGAGKTTTLRMLLGlTHPDAGSisLCGEP-VPSRARHARQR---VGVVPQFDNLDPDFTVRENLlvfgRYFGLSA- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 76 rrgnpGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLV 155
Cdd:PRK13537 113 -----AAARALVPPLLEFAKLENKADAKVGE-----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLR 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767915018 156 ELARRNRIVVLTIHQpRSELFQLFDKIAILSFGELIFCGTPAEMLD 201
Cdd:PRK13537 183 SLLARGKTILLTTHF-MEEAERLCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
3-169 |
1.35e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 65.90 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLGRAGTFLGEVYVNGRA-----------LRREQ----FQDCFSyvlqsdTLLSSLTVRETL 67
Cdd:PRK09473 47 IVGESGSGKSQTAFALMGLLAANGRIGGSATFNGREilnlpekelnkLRAEQismiFQDPMT------SLNPYMRVGEQL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 68 HYTALLAIRRGNPGSFQKKV---EAV-MAElslshvADRLIGNYSlGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLD 143
Cdd:PRK09473 121 MEVLMLHKGMSKAEAFEESVrmlDAVkMPE------ARKRMKMYP-HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALD 193
|
170 180
....*....|....*....|....*..
gi 767915018 144 CMTANQIVVLLVELARR-NRIVVLTIH 169
Cdd:PRK09473 194 VTVQAQIMTLLNELKREfNTAIIMITH 220
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-203 |
1.40e-11 |
|
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: 67.13 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSG-------------------------RLGRAGT---------------FLGEVYVNGRALRRE 42
Cdd:TIGR03269 31 ILGRSGAGKSVLMHVLRGmdqyeptsgriiyhvalcekcgyveRPSKVGEpcpvcggtlepeevdFWNLSDKLRRRIRKR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 43 ---QFQDCFSYVLQSDTLLSSLTVRETLHYTALLAIRRGnpgsfQKKVEAVMAELSLSHVADRLIGnyslggistGERRR 119
Cdd:TIGR03269 111 iaiMLQRTFALYGDDTVLDNVLEALEEIGYEGKEAVGRA-----VDLIEMVQLSHRITHIARDLSG---------GEKQR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 120 VSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRI-VVLTIHQPRSeLFQLFDKIAILSFGELIFCGTPAE 198
Cdd:TIGR03269 177 VVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGIsMVLTSHWPEV-IEDLSDKAIWLENGEIKEEGTPDE 255
|
....*
gi 767915018 199 MLDFF 203
Cdd:TIGR03269 256 VVAVF 260
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-213 |
1.53e-11 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 65.87 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNG-----------RALRREqfqdcFSYVLQSDTLLSSLTVRETLhytA 71
Cdd:COG1135 36 IIGYSGAGKSTLIRCINL-LERPTS--GSVLVDGvdltalserelRAARRK-----IGMIFQHFNLLSSRTVAENV---A 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 72 L-LAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQI 150
Cdd:COG1135 105 LpLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQ-----LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSI 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767915018 151 VVLLVELARRNRI-VVLTIHQP---RselfQLFDKIAILSFGELIFCGTpaeMLDFFNDcgypcPEH 213
Cdd:COG1135 180 LDLLKDINRELGLtIVLITHEMdvvR----RICDRVAVLENGRIVEQGP---VLDVFAN-----PQS 234
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
3-201 |
1.80e-11 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 66.21 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSgRLGRAGTflGEVYVNG-----------RALRREQFqdcfSYVLQSDTLLSSLTVRETLHYTA 71
Cdd:PRK10070 59 IMGLSGSGKSTMVRLLN-RLIEPTR--GQVLIDGvdiakisdaelREVRRKKI----AMVFQSFALMPHMTVLDNTAFGM 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 72 LLAirrGNPGSFQKkveavmaELSLSHVADRLIGNYSLG---GISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTAN 148
Cdd:PRK10070 132 ELA---GINAEERR-------EKALDALRQVGLENYAHSypdELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767915018 149 QIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGTPAEMLD 201
Cdd:PRK10070 202 EMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-219 |
1.93e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 64.41 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMS--GRLGRAGTFLGEVYVNGR----------ALRREqfqdcFSYVLQSDTLLSsLTVRETLHYT 70
Cdd:PRK14239 36 LIGPSGSGKSTLLRSINrmNDLNPEVTITGSIVYNGHniysprtdtvDLRKE-----IGMVFQQPNPFP-MSIYENVVYG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 71 ALLAirrgnpGSFQKKV--EAVmaELSL------SHVADRLigNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGL 142
Cdd:PRK14239 110 LRLK------GIKDKQVldEAV--EKSLkgasiwDEVKDRL--HDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSAL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767915018 143 DCMTANQIVVLLVELarRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGTPAEMldFFNdcgypcPEHSNPFDF 219
Cdd:PRK14239 180 DPISAGKIEETLLGL--KDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQM--FMN------PKHKETEDY 246
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-198 |
2.85e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 66.30 E-value: 2.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 4 LGSSGSGKTT-------LLDAMSGR---LGRagtflgEVYVNGRALRREqfqdcFSYVLQSDTLLSSLTVRE--TLHytA 71
Cdd:NF033858 298 LGSNGCGKSTtmkmltgLLPASEGEawlFGQ------PVDAGDIATRRR-----VGYMSQAFSLYGELTVRQnlELH--A 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 72 LLairrgnpgsFQ-------KKVEAVMAELSLSHVADRLIGNYSLGgistgERRRVSIAAQLLQDPKVMLFDEPTTGLDC 144
Cdd:NF033858 365 RL---------FHlpaaeiaARVAEMLERFDLADVADALPDSLPLG-----IRQRLSLAVAVIHKPELLILDEPTSGVDP 430
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767915018 145 MTANQIVVLLVELARRNRIvvlTI----HqprselfqlF-------DKIAILSFGELIFCGTPAE 198
Cdd:NF033858 431 VARDMFWRLLIELSREDGV---TIfistH---------FmneaercDRISLMHAGRVLASDTPAA 483
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
3-168 |
4.07e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 63.06 E-value: 4.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGralrreqfQDC---------FSYVLQSDTLLSSLTVRETLHytalL 73
Cdd:PRK10771 30 ILGPSGAGKSTLLNLIAGFLTPAS---GSLTLNG--------QDHtttppsrrpVSMLFQENNLFSHLTVAQNIG----L 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 74 AIrrgNPG-----SFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTAN 148
Cdd:PRK10771 95 GL---NPGlklnaAQREKLHAIARQMGIEDLLARLPGQ-----LSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQ 166
|
170 180
....*....|....*....|
gi 767915018 149 QIVVLLVELARRNRIVVLTI 168
Cdd:PRK10771 167 EMLTLVSQVCQERQLTLLMV 186
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-168 |
4.12e-11 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 63.57 E-value: 4.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 1 MCILGSSGSGKTTLLDAMSGRLG-RAGTF-LGEVYVNGRALRReqfqdcfSYVLQSDTLLSSLTVRETLHYTALLAirrG 78
Cdd:PRK11248 30 LVVLGPSGCGKTTLLNLIAGFVPyQHGSItLDGKPVEGPGAER-------GVVFQNEGLLPWRNVQDNVAFGLQLA---G 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 79 NPGSFQKKVEAVM-AELSLSHVADRLIgnYSLGGistGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVEL 157
Cdd:PRK11248 100 VEKMQRLEIAHQMlKKVGLEGAEKRYI--WQLSG---GQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKL 174
|
170
....*....|.
gi 767915018 158 ARRNRIVVLTI 168
Cdd:PRK11248 175 WQETGKQVLLI 185
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
3-199 |
5.04e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 64.36 E-value: 5.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRALRREQFQD---CFsyVLQSDTLLSSLTVRETLHYTalLAIRRGN 79
Cdd:PRK11432 37 LLGPSGCGKTTVLRLVAG-LEKPTE--GQIFIDGEDVTHRSIQQrdiCM--VFQSYALFPHMSLGENVGYG--LKMLGVP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 80 PGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELAR 159
Cdd:PRK11432 110 KEERKQRVKEALELVDLAGFEDRYVDQ-----ISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQ 184
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 767915018 160 RNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGTPAEM 199
Cdd:PRK11432 185 QFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
2-143 |
6.01e-11 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 62.90 E-value: 6.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 2 CILGSSGSGKTTLLdamsgrlgRAGTFL-----GEVYVNGRALR-------------REQFQDC---FSYVLQSDTLLSS 60
Cdd:COG4598 38 SIIGSSGSGKSTFL--------RCINLLetpdsGEIRVGGEEIRlkpdrdgelvpadRRQLQRIrtrLGMVFQSFNLWSH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 61 LTVRET-----LHytaLLAIRRGNPgsfQKKVEAVMAELSLSHVADrlignYSLGGISTGERRRVSIAAQLLQDPKVMLF 135
Cdd:COG4598 110 MTVLENvieapVH---VLGRPKAEA---IERAEALLAKVGLADKRD-----AYPAHLSGGQQQRAAIARALAMEPEVMLF 178
|
....*...
gi 767915018 136 DEPTTGLD 143
Cdd:COG4598 179 DEPTSALD 186
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
3-170 |
7.04e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 62.85 E-value: 7.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAM-------SGRLGragtfLGEVYVNG-RALRREQ-----FQDCFSYVLQSDTLLSSLTVRETLHY 69
Cdd:PRK11264 34 IIGPSGSGKTTLLRCInlleqpeAGTIR-----VGDITIDTaRSLSQQKglirqLRQHVGFVFQNFNLFPHRTVLENIIE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 70 TALlaIRRGNP-GSFQKKVEAVMAELSLSHVAD----RLIGnyslggistGERRRVSIAAQLLQDPKVMLFDEPTTGLDC 144
Cdd:PRK11264 109 GPV--IVKGEPkEEATARARELLAKVGLAGKETsyprRLSG---------GQQQRVAIARALAMRPEVILFDEPTSALDP 177
|
170 180
....*....|....*....|....*.
gi 767915018 145 MTANQIVVLLVELARRNRIVVLTIHQ 170
Cdd:PRK11264 178 ELVGEVLNTIRQLAQEKRTMVIVTHE 203
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-185 |
8.70e-11 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 61.72 E-value: 8.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 2 CILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRalrreqfqdcFSYVLQSDTLLSSlTVRETlhytallaIRRGNPg 81
Cdd:cd03250 35 AIVGPVGSGKSSLLSALLGELEKLS---GSVSVPGS----------IAYVSQEPWIQNG-TIREN--------ILFGKP- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 82 sFQKK-----VEA--------VMAELSLSHVADRlignyslgGI--STGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMT 146
Cdd:cd03250 92 -FDEEryekvIKAcalepdleILPDGDLTEIGEK--------GInlSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 767915018 147 ANQIV--VLLVELaRRNRIVVLTIHQPrsELFQLFDKIAIL 185
Cdd:cd03250 163 GRHIFenCILGLL-LNNKTRILVTHQL--QLLPHADQIVVL 200
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-143 |
9.66e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 64.32 E-value: 9.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 2 CILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRaLRreqfqdcFSYVLQSDTLLSSLTVRETL-------------- 67
Cdd:COG0488 28 GLVGRNGAGKSTLLKILAGELEPDS---GEVSIPKG-LR-------IGYLPQEPPLDDDLTVLDTVldgdaelraleael 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 68 ---------------HYTALLA-IRRGNPGSFQKKVEAVMAELSLSHV-ADRLIGNYSlgGistGERRRVSIAAQLLQDP 130
Cdd:COG0488 97 eeleaklaepdedleRLAELQEeFEALGGWEAEARAEEILSGLGFPEEdLDRPVSELS--G---GWRRRVALARALLSEP 171
|
170
....*....|...
gi 767915018 131 KVMLFDEPTTGLD 143
Cdd:COG0488 172 DLLLLDEPTNHLD 184
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-201 |
1.89e-10 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 61.26 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAM-------SGRLGRAGTFLGEVYVNGRALRREQfqdcfSYVLQSDTLLSSLTVRETLHYTALlAI 75
Cdd:PRK09493 32 IIGPSGSGKSTLLRCInkleeitSGDLIVDGLKVNDPKVDERLIRQEA-----GMVFQQFYLFPHLTALENVMFGPL-RV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 76 RRGNPGSFQKKVEAVMAELSLSHVAdrligNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLV 155
Cdd:PRK09493 106 RGASKEEAEKQARELLAKVGLAERA-----HHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQ 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767915018 156 ELARRNRIVVLTIHQprselFQLFDKIAilsfGELIFC--------GTPAEMLD 201
Cdd:PRK09493 181 DLAEEGMTMVIVTHE-----IGFAEKVA----SRLIFIdkgriaedGDPQVLIK 225
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-191 |
2.01e-10 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 59.36 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 2 CILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALrreqfqdcfsyvlqsdtllSSLTVREtlhytallAIRRGnpg 81
Cdd:cd03216 30 ALLGENGAGKSTLMKILSGLYKPDS---GEILVDGKEV-------------------SFASPRD--------ARRAG--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 82 sfqkkVEAVmaelslshvadrlignYSLggiSTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRN 161
Cdd:cd03216 77 -----IAMV----------------YQL---SVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQG 132
|
170 180 190
....*....|....*....|....*....|
gi 767915018 162 RIVVLTIHQPRsELFQLFDKIAILSFGELI 191
Cdd:cd03216 133 VAVIFISHRLD-EVFEIADRVTVLRDGRVV 161
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
3-200 |
3.99e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 60.77 E-value: 3.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRREQFQDC---FSYVLQSDTLLSSLTVRETL------HYTALL 73
Cdd:PRK10253 38 IIGPNGCGKSTLLRTLSRLMTPAH---GHVWLDGEHIQHYASKEVarrIGLLAQNATTPGDITVQELVargrypHQPLFT 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 74 AIRRGNpgsfQKKVEAVMAELSLSHVADRlignySLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVL 153
Cdd:PRK10253 115 RWRKED----EEAVTKAMQATGITHLADQ-----SVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLEL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 767915018 154 LVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGTPAEML 200
Cdd:PRK10253 186 LSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
5-170 |
4.56e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.58 E-value: 4.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 5 GSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRREQ--FQDCFSYVLQSDTLLSSLTVRETLHYTalLAIRRGNPGs 82
Cdd:PRK13540 34 GSNGAGKTTLLKLIAGLLNPEK---GEILFERQSIKKDLctYQKQLCFVGHRSGINPYLTLRENCLYD--IHFSPGAVG- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 83 fqkkVEAVMAELSLSHVADrlignYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNR 162
Cdd:PRK13540 108 ----ITELCRLFSLEHLID-----YPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGG 178
|
....*...
gi 767915018 163 IVVLTIHQ 170
Cdd:PRK13540 179 AVLLTSHQ 186
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-143 |
5.99e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 59.94 E-value: 5.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 1 MCILGSSGSGKTTLLDAMSGRL----------GRAGTFLgEVYVNGRALRREQFQDCFSYVLQS--DTLLSSLT----VR 64
Cdd:PRK11701 35 LGIVGESGSGKTTLLNALSARLapdagevhyrMRDGQLR-DLYALSEAERRRLLRTEWGFVHQHprDGLRMQVSaggnIG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 65 ETL------HYTALlairRGNPGSFQKKVEAVMAELslshvaDRLIGNYSlGGIstgeRRRVSIAAQLLQDPKVMLFDEP 138
Cdd:PRK11701 114 ERLmavgarHYGDI----RATAGDWLERVEIDAARI------DDLPTTFS-GGM----QQRLQIARNLVTHPRLVFMDEP 178
|
....*
gi 767915018 139 TTGLD 143
Cdd:PRK11701 179 TGGLD 183
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-200 |
7.46e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 60.02 E-value: 7.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALR---------REQ----FQD----CFSYVLQSDTLLS--SLTV 63
Cdd:PRK13638 32 LVGANGCGKSTLFMNLSGLLRPQK---GAVLWQGKPLDyskrgllalRQQvatvFQDpeqqIFYTDIDSDIAFSlrNLGV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 64 RETlhytallairrgnpgSFQKKVEAVMAELSLSHVADRLIGnyslgGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLD 143
Cdd:PRK13638 109 PEA---------------EITRRVDEALTLVDAQHFRHQPIQ-----CLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767915018 144 CMTANQIVVLLVELARRNRIVVLTIHQPrSELFQLFDKIAILSFGELIFCGTPAEML 200
Cdd:PRK13638 169 PAGRTQMIAIIRRIVAQGNHVIISSHDI-DLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-199 |
1.22e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 60.23 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGrlgragtF----LGEVYVNGRALRR-EQFQDCFSYVLQSDTLLSSLTVRETLHYTalLAIRR 77
Cdd:PRK11607 50 LLGASGCGKSTLLRMLAG-------FeqptAGQIMLDGVDLSHvPPYQRPINMMFQSYALFPHMTVEQNIAFG--LKQDK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 78 GNPGSFQKKVEAVMAELSLSHVADRliGNYSLGGistGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVEL 157
Cdd:PRK11607 121 LPKAEIASRVNEMLGLVHMQEFAKR--KPHQLSG---GQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDI 195
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767915018 158 ARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGTPAEM 199
Cdd:PRK11607 196 LERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-142 |
1.65e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 60.43 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 2 CILGSSGSGKTTLLDAMSGrlgragtFL----GEVYVNGRALRREQFQDCFSY----VLQSDTLLSSLTVRETLhytaLL 73
Cdd:COG3845 35 ALLGENGAGKSTLMKILYG-------LYqpdsGEILIDGKPVRIRSPRDAIALgigmVHQHFMLVPNLTVAENI----VL 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767915018 74 AIRRGNPGSF-----QKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGL 142
Cdd:COG3845 104 GLEPTKGGRLdrkaaRARIRELSERYGLDVDPDAKVED-----LSVGEQQRVEILKALYRGARILILDEPTAVL 172
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1-200 |
2.76e-09 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 57.93 E-value: 2.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 1 MCILGSSGSGKTTLLdAMSGRLgrAGTFLGEVYVNGRALRR---EQFQDCFSYVLQSDTLLSSlTVRETlhytallaIRR 77
Cdd:cd03249 32 VALVGSSGCGKSTVV-SLLERF--YDPTSGEILLDGVDIRDlnlRWLRSQIGLVSQEPVLFDG-TIAEN--------IRY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 78 GNPGSFQKKVEAV--MAEL-----SLSHVADRLIGNY--SLGGistGERRRVSIAAQLLQDPKVMLFDEPTTGLDcmTAN 148
Cdd:cd03249 100 GKPDATDEEVEEAakKANIhdfimSLPDGYDTLVGERgsQLSG---GQKQRIAIARALLRNPKILLLDEATSALD--AES 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767915018 149 QIVVL-LVELARRNRIVVLTIHqpRSELFQLFDKIAILSFGELIFCGTPAEML 200
Cdd:cd03249 175 EKLVQeALDRAMKGRTTIVIAH--RLSTIRNADLIAVLQNGQVVEQGTHDELM 225
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-200 |
2.94e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 58.48 E-value: 2.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 2 CILGSSGSGKTTLLDAMSGRL--GRAGTFLGEVYVNG--------RALRRE-----QFQDcfsYVLQSDTLLSSLtvret 66
Cdd:PRK13645 41 CVIGTTGSGKSTMIQLTNGLIisETGQTIVGDYAIPAnlkkikevKRLRKEiglvfQFPE---YQLFQETIEKDI----- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 67 lhytALLAIRRG-NPGSFQKKVEAVMAELSLShvadRLIGNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCM 145
Cdd:PRK13645 113 ----AFGPVNLGeNKQEAYKKVPELLKLVQLP----EDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPK 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767915018 146 TANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGTPAEML 200
Cdd:PRK13645 185 GEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-200 |
3.04e-09 |
|
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: 59.43 E-value: 3.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRL----GRAGTFLGEVYVN---------GRALRR----EQFQDCFSYvlqsDTLLSSLTVRE 65
Cdd:TIGR03269 315 IVGTSGAGKTTLSKIIAGVLeptsGEVNVRVGDEWVDmtkpgpdgrGRAKRYigilHQEYDLYPH----RTVLDNLTEAI 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 66 TLHYTALLAIRRG-----NPGSFQKKVEAVmaelsLSHVADRLignyslggiSTGERRRVSIAAQLLQDPKVMLFDEPTT 140
Cdd:TIGR03269 391 GLELPDELARMKAvitlkMVGFDEEKAEEI-----LDKYPDEL---------SEGERHRVALAQVLIKEPRIVILDEPTG 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767915018 141 GLDCMTANQivvllvelarrnriVVLTIHQPRSELFQLF--------------DKIAILSFGELIFCGTPAEML 200
Cdd:TIGR03269 457 TMDPITKVD--------------VTHSILKAREEMEQTFiivshdmdfvldvcDRAALMRDGKIVKIGDPEEIV 516
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-200 |
4.09e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 57.88 E-value: 4.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 1 MCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALrreQFQDcFSYVLQSDTLL-----SSLTVRETLHYTALLAI 75
Cdd:PRK15112 42 LAIIGENGSGKSTLAKMLAGMIEPTS---GELLIDDHPL---HFGD-YSYRSQRIRMIfqdpsTSLNPRQRISQILDFPL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 76 RRGNPGSFQKKVEAVMAELslshvadRLIG------NYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQ 149
Cdd:PRK15112 115 RLNTDLEPEQREKQIIETL-------RQVGllpdhaSYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQ 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 767915018 150 IVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGTPAEML 200
Cdd:PRK15112 188 LINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVL 238
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-205 |
5.11e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 58.68 E-value: 5.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGrlGRAGTFLGEVYVNGRALRREQFQDCFSYVL-------QSDTLLSSLTVRETLHYTAL--- 72
Cdd:TIGR02633 291 VAGLVGAGRTELVQALFG--AYPGKFEGNVFINGKPVDIRNPAQAIRAGIamvpedrKRHGIVPILGVGKNITLSVLksf 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 73 LAIRRGNPGSFQKKVEAVMAELSLSHVADRLignySLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVV 152
Cdd:TIGR02633 369 CFKMRIDAAAELQIIGSAIQRLKVKTASPFL----PIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYK 444
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767915018 153 LLVELARRNrIVVLTIHQPRSELFQLFDKIAILSFGELifCGtpaemlDFFND 205
Cdd:TIGR02633 445 LINQLAQEG-VAIIVVSSELAEVLGLSDRVLVIGEGKL--KG------DFVNH 488
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-190 |
5.35e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 58.64 E-value: 5.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSG---SGKTTLLDAMSGRLGRAGtflGEVYVNGRALR----REQFQDCFSYVLQS---DTLLSSLTVRETLHYTAL 72
Cdd:PRK09700 291 ILGFAGlvgSGRTELMNCLFGVDKRAG---GEIRLNGKDISprspLDAVKKGMAYITESrrdNGFFPNFSIAQNMAISRS 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 73 LAIRR--GNPGSFQKKVEAVMAELSLSHVADRLIG-NYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQ 149
Cdd:PRK09700 368 LKDGGykGAMGLFHEVDEQRTAENQRELLALKCHSvNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAE 447
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 767915018 150 IVVLLVELARRNrIVVLTIHQPRSELFQLFDKIAILSFGEL 190
Cdd:PRK09700 448 IYKVMRQLADDG-KVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
3-169 |
6.45e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 56.99 E-value: 6.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRL-GRAGTFLGEVYVNG--RALRREQFQDCFSYVLQSDtllssLTVRETLHYTALL-AIRRG 78
Cdd:cd03236 31 LVGPNGIGKSTALKILAGKLkPNLGKFDDPPDWDEilDEFRGSELQNYFTKLLEGD-----VKVIVKPQYVDLIpKAVKG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 79 NPGSFQKKV------EAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDC---MTANQ 149
Cdd:cd03236 106 KVGELLKKKdergklDELVDQLELRHVLDRNIDQ-----LSGGELQRVAIAAALARDADFYFFDEPSSYLDIkqrLNAAR 180
|
170 180
....*....|....*....|
gi 767915018 150 IVvllVELARRNRIVVLTIH 169
Cdd:cd03236 181 LI---RELAEDDNYVLVVEH 197
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
3-143 |
6.78e-09 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 56.65 E-value: 6.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRL----GRAGTFLGEVyvngralrreqfqdcfSYVLQSDTLLSSLTVRETLHytallAIRRG 78
Cdd:cd03237 30 ILGPNGIGKTTFIKMLAGVLkpdeGDIEIELDTV----------------SYKPQYIKADYEGTVRDLLS-----SITKD 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767915018 79 NPGSFQKKVEaVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLD 143
Cdd:cd03237 89 FYTHPYFKTE-IAKPLQIEQILDREVPE-----LSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3-198 |
1.06e-08 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 57.26 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGrlgragtF----LGEVYVNGRALRR---EQFQdcFSYVLQSDTLLSSLTVRETLHYtALLAI 75
Cdd:PRK09452 45 LLGPSGCGKTTVLRLIAG-------FetpdSGRIMLDGQDITHvpaENRH--VNTVFQSYALFPHMTVFENVAF-GLRMQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 76 RRGNPgSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLV 155
Cdd:PRK09452 115 KTPAA-EITPRVMEALRMVQLEEFAQRKPHQ-----LSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELK 188
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 767915018 156 ELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGTPAE 198
Cdd:PRK09452 189 ALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPRE 231
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
3-199 |
1.13e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 56.31 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGR---ALRREQFQDC---FSYVLQSDTLLSSLTVRETLHY-----TA 71
Cdd:PRK11831 38 IMGPSGIGKTTLLRLIGGQIAPDH---GEILFDGEnipAMSRSRLYTVrkrMSMLFQSGALFTDMNVFDNVAYplrehTQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 72 LlairrgnPGSFQKKVeaVMaeLSLSHVADRLIGNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIV 151
Cdd:PRK11831 115 L-------PAPLLHST--VM--MKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLV 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 767915018 152 VLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGTPAEM 199
Cdd:PRK11831 184 KLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
3-172 |
1.50e-08 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 55.84 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLGRAGTfLGEVYVNG----------RAlRREQFqdcfsYVLQSDTLLSSLTVRETLHyTAL 72
Cdd:COG0396 31 IMGPNGSGKSTLAKVLMGHPKYEVT-SGSILLDGedilelspdeRA-RAGIF-----LAFQYPVEIPGVSVSNFLR-TAL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 73 LAIRRGNPGS--FQKKVEAVMAELSLSH-VADRlignySL-GGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDcMTAN 148
Cdd:COG0396 103 NARRGEELSAreFLKLLKEKMKELGLDEdFLDR-----YVnEGFSGGEKKRNEILQMLLLEPKLAILDETDSGLD-IDAL 176
|
170 180
....*....|....*....|....*
gi 767915018 149 QIVVLLV-ELARRNRIVVLTIHQPR 172
Cdd:COG0396 177 RIVAEGVnKLRSPDRGILIITHYQR 201
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
3-200 |
2.15e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 55.27 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRlGRAGTflGEVYVNGRALRREQ----FQDCFSYVLQSDTLLSSLTVRETLHYTALLAIRRg 78
Cdd:PRK11614 36 LIGANGAGKTTLLGTLCGD-PRATS--GRIVFDGKDITDWQtakiMREAVAIVPEGRRVFSRMTVEENLAMGGFFAERD- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 79 npgSFQKKVEAVMAelSLSHVADRLIgnYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELa 158
Cdd:PRK11614 112 ---QFQERIKWVYE--LFPRLHERRI--QRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQL- 183
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767915018 159 RRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGTPAEML 200
Cdd:PRK11614 184 REQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALL 225
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
3-208 |
2.17e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 55.56 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLgRAGTflGEVYVNG------------RALRREqfqdcFSYVLQ-SDTLLSSLTV-RETLH 68
Cdd:PRK13646 38 IVGQTGSGKSTLIQNINALL-KPTT--GTVTVDDitithktkdkyiRPVRKR-----IGMVFQfPESQLFEDTVeREIIF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 69 ytallairrgNPGSFQKKVEAVMA---ELSLSHVADRLIGNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCM 145
Cdd:PRK13646 110 ----------GPKNFKMNLDEVKNyahRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQ 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767915018 146 TANQIVVLLVEL-ARRNRIVVLTIHQpRSELFQLFDKIAILSFGELIFCGTPAEMldfFNDCGY 208
Cdd:PRK13646 180 SKRQVMRLLKSLqTDENKTIILVSHD-MNEVARYADEVIVMKEGSIVSQTSPKEL---FKDKKK 239
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-201 |
2.25e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 56.76 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 5 GSSGSGKTTLLDAMSGrLGRAGTFLGEVYVNGRALRREQFQDC----FSYVLQSDTLLSSLTVRET--LHYTALLAIRRG 78
Cdd:TIGR02633 34 GENGAGKSTLMKILSG-VYPHGTWDGEIYWSGSPLKASNIRDTeragIVIIHQELTLVPELSVAENifLGNEITLPGGRM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 79 NPGSFQKKVEAVMAELSLSHVAD-RLIGNYSLGgistgERRRVSIAAQLLQDPKVMLFDEPTTGLdcmTANQIVVLL--- 154
Cdd:TIGR02633 113 AYNAMYLRAKNLLRELQLDADNVtRPVGDYGGG-----QQQLVEIAKALNKQARLLILDEPSSSL---TEKETEILLdii 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 767915018 155 VELARRNrIVVLTIHQPRSELFQLFDKIAILSFGELIfCGTPAEMLD 201
Cdd:TIGR02633 185 RDLKAHG-VACVYISHKLNEVKAVCDTICVIRDGQHV-ATKDMSTMS 229
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
112-188 |
2.40e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 56.64 E-value: 2.40e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767915018 112 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFG 188
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNG 233
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
84-199 |
2.73e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 55.90 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 84 QKKVEAVMAELSLSHVADRLIGNYSlGGIstgeRRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRI 163
Cdd:NF000106 122 RARADELLERFSLTEAAGRAAAKYS-GGM----RRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGAT 196
|
90 100 110
....*....|....*....|....*....|....*.
gi 767915018 164 VVLTIhQPRSELFQLFDKIAILSFGELIFCGTPAEM 199
Cdd:NF000106 197 VLLTT-QYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-199 |
2.73e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 56.57 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 1 MCILGSSGSGKTTLLDAMSGRLgRAGTflGEVYVNGRALRREQFQDCF----SYVLQSDTLLSSLTVRETLhYTALLAIR 76
Cdd:COG1129 33 HALLGENGAGKSTLMKILSGVY-QPDS--GEILLDGEPVRFRSPRDAQaagiAIIHQELNLVPNLSVAENI-FLGREPRR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 77 RG--NPGSFQKKVEAVMAELSLSHVADRLIGNYSLGgistgERRRVSIAAQLLQDPKVMLFDEPTTGLdcmTANQIVVLL 154
Cdd:COG1129 109 GGliDWRAMRRRARELLARLGLDIDPDTPVGDLSVA-----QQQLVEIARALSRDARVLILDEPTASL---TEREVERLF 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767915018 155 V---ELARRNRIVVLTIHqpR-SELFQLFDKIAILSFGELIFCGTPAEM 199
Cdd:COG1129 181 RiirRLKAQGVAIIYISH--RlDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-191 |
2.89e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.55 E-value: 2.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 1 MCILGSSGSGKTTLLDAMSGRLGR-AGT--FLG-EVYVNGralRREQFQDCFSYVLQSDTLLSSLTVRETLhytaLLAIR 76
Cdd:PRK10762 33 MALVGENGAGKSTMMKVLTGIYTRdAGSilYLGkEVTFNG---PKSSQEAGIGIIHQELNLIPQLTIAENI----FLGRE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 77 RGNP-GSFQ-KKV----EAVMAELSLSHVADRLIGNYSLggistGERRRVSIAAQLLQDPKVMLFDEPTTGL-DCMTANQ 149
Cdd:PRK10762 106 FVNRfGRIDwKKMyaeaDKLLARLNLRFSSDKLVGELSI-----GEQQMVEIAKVLSFESKVIIMDEPTDALtDTETESL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767915018 150 IVVlLVELARRNRIVVLTIHQPRsELFQLFDKIAILSFGELI 191
Cdd:PRK10762 181 FRV-IRELKSQGRGIVYISHRLK-EIFEICDDVTVFRDGQFI 220
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
4-191 |
2.97e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.46 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 4 LGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRALR----REQFQDCFSYVLQSDTLLSSLTVRETLhYTALLAIRRGn 79
Cdd:PRK11288 36 MGENGAGKSTLLKILSG-NYQPDA--GSILIDGQEMRfastTAALAAGVAIIYQELHLVPEMTVAENL-YLGQLPHKGG- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 80 pgSFQKKVEAVMAELSLSHVADRLIGNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELAR 159
Cdd:PRK11288 111 --IVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRA 188
|
170 180 190
....*....|....*....|....*....|..
gi 767915018 160 RNRIVVLTIHQpRSELFQLFDKIAILSFGELI 191
Cdd:PRK11288 189 EGRVILYVSHR-MEEIFALCDAITVFKDGRYV 219
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
3-199 |
3.38e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 55.22 E-value: 3.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNG------------RALRREqfqdcFSYVLQ-SDTLLSSLTVRETLHY 69
Cdd:PRK13641 38 LVGHTGSGKSTLMQHFNALLKPSS---GTITIAGyhitpetgnknlKKLRKK-----VSLVFQfPEAQLFENTVLKDVEF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 70 TALlairrgNPG-SFQKKVEAVMAELSLSHVADRLIgNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTAN 148
Cdd:PRK13641 110 GPK------NFGfSEDEAKEKALKWLKKVGLSEDLI-SKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRK 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 767915018 149 QIVVLLVELARRNRIVVLTIHQpRSELFQLFDKIAILSFGELIFCGTPAEM 199
Cdd:PRK13641 183 EMMQLFKDYQKAGHTVILVTHN-MDDVAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
8-191 |
4.15e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 55.79 E-value: 4.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 8 GSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRREQFQDC----FSYV---LQSDTLLSSLTVRETLHYTALLAIRRG-- 78
Cdd:COG1129 288 GAGRTELARALFGADPADS---GEIRLDGKPVRIRSPRDAiragIAYVpedRKGEGLVLDLSIRENITLASLDRLSRGgl 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 79 -NPGSFQKKVEAVMAELSL-SHVADRLIGNYSlgGistGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVE 156
Cdd:COG1129 365 lDRRRERALAEEYIKRLRIkTPSPEQPVGNLS--G---GNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRE 439
|
170 180 190
....*....|....*....|....*....|....*....
gi 767915018 157 LARRNR-IVVLTihqprSEL---FQLFDKIAILSFGELI 191
Cdd:COG1129 440 LAAEGKaVIVIS-----SELpelLGLSDRILVMREGRIV 473
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
3-168 |
4.29e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 54.69 E-value: 4.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGR---ALRREQ-----------FQDCFSYVLQSDTLLSSLtvRETL- 67
Cdd:PRK10419 43 LLGRSGCGKSTLARLLVG-LESPSQ--GNVSWRGEplaKLNRAQrkafrrdiqmvFQDSISAVNPRKTVREII--REPLr 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 68 HYTALLAIRRgnpgsfQKKVEAV--MAELSLSHvADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCM 145
Cdd:PRK10419 118 HLLSLDKAER------LARASEMlrAVDLDDSV-LDKRPPQ-----LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLV 185
|
170 180
....*....|....*....|...
gi 767915018 146 TANQIVVLLVELARRNRIVVLTI 168
Cdd:PRK10419 186 LQAGVIRLLKKLQQQFGTACLFI 208
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
3-200 |
4.32e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 54.61 E-value: 4.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLG-RAGTFLGEVYVNGRALRREQFQDCFSYVLQS-DTLLSSLTVRETLHYTAL-LAIrrgN 79
Cdd:PRK13644 33 IIGKNGSGKSTLALHLNGLLRpQKGKVLVSGIDTGDFSKLQGIRKLVGIVFQNpETQFVGRTVEEDLAFGPEnLCL---P 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 80 PGSFQKKVEAVMAELSLSHVADRlignySLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELAR 159
Cdd:PRK13644 110 PIEIRKRVDRALAEIGLEKYRHR-----SPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 767915018 160 RNRIVVLTIHQprSELFQLFDKIAILSFGELIFCGTPAEML 200
Cdd:PRK13644 185 KGKTIVYITHN--LEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-168 |
4.93e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 55.87 E-value: 4.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSgRLGRAGtflGEVYVNGRAL------------RREQ--FQDCFSyvlqsdTLLSSLTVRE--- 65
Cdd:PRK15134 317 LVGESGSGKSTTGLALL-RLINSQ---GEIWFDGQPLhnlnrrqllpvrHRIQvvFQDPNS------SLNPRLNVLQiie 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 66 ---TLHYTALLAIRRgnpgsfQKKVEAVMAELSLSHVA-DRLIGNYSlggisTGERRRVSIAAQLLQDPKVMLFDEPTTG 141
Cdd:PRK15134 387 eglRVHQPTLSAAQR------EQQVIAVMEEVGLDPETrHRYPAEFS-----GGQRQRIAIARALILKPSLIILDEPTSS 455
|
170 180
....*....|....*....|....*..
gi 767915018 142 LDCMTANQIVVLLVELARRNRIVVLTI 168
Cdd:PRK15134 456 LDKTVQAQILALLKSLQQKHQLAYLFI 482
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
3-169 |
5.00e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 55.95 E-value: 5.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGR----LGR--------------AGTFLGEvY----VNG--RALRREQFQDCFSYVLqsdtll 58
Cdd:COG1245 104 ILGPNGIGKSTALKILSGElkpnLGDydeepswdevlkrfRGTELQD-YfkklANGeiKVAHKPQYVDLIPKVF------ 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 59 sSLTVRETLHYTAllaiRRGnpgsfqkKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEP 138
Cdd:COG1245 177 -KGTVRELLEKVD----ERG-------KLDELAEKLGLENILDRDISE-----LSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190
....*....|....*....|....*....|....
gi 767915018 139 TTGLDC---MTANQIVvllVELARRNRIVVLTIH 169
Cdd:COG1245 240 SSYLDIyqrLNVARLI---RELAEEGKYVLVVEH 270
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
112-199 |
5.10e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 54.64 E-value: 5.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 112 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELAR-RNRIVVLTIHQpRSELFQLFDKIAILSFGEL 190
Cdd:PRK13634 146 LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKeKGLTTVLVTHS-MEDAARYADQIVVMHKGTV 224
|
....*....
gi 767915018 191 IFCGTPAEM 199
Cdd:PRK13634 225 FLQGTPREI 233
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
3-199 |
5.31e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.14 E-value: 5.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLGRAGTflGEVYVNGRAlrreqfqdcfSYVLQSDTLLSSlTVRETLHYTAllairRGNPGS 82
Cdd:PLN03232 648 IVGGTGEGKTSLISAMLGELSHAET--SSVVIRGSV----------AYVPQVSWIFNA-TVRENILFGS-----DFESER 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 83 FQKKVEAVmaelSLSHVADRLIGN--YSLG----GISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVE 156
Cdd:PLN03232 710 YWRAIDVT----ALQHDLDLLPGRdlTEIGergvNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMK 785
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 767915018 157 LARRNRIVVLTIHQprSELFQLFDKIAILSFGELIFCGTPAEM 199
Cdd:PLN03232 786 DELKGKTRVLVTNQ--LHFLPLMDRIILVSEGMIKEEGTFAEL 826
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
3-170 |
6.15e-08 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 53.49 E-value: 6.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMsgrLGRAGTFLGEVYVNGRALRREQFQDCFS-------YVLQSDTLLSSlTVRETLHYtallai 75
Cdd:cd03290 32 IVGQVGCGKSSLLLAI---LGEMQTLEGKVHWSNKNESEPSFEATRSrnrysvaYAAQKPWLLNA-TVEENITF------ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 76 rrGNPGSFQKkVEAVMAELSLSHVADRL-------IGNYSLGgISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTAN 148
Cdd:cd03290 102 --GSPFNKQR-YKAVTDACSLQPDIDLLpfgdqteIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSD 177
|
170 180
....*....|....*....|....
gi 767915018 149 QIVV--LLVELARRNRIVVLTIHQ 170
Cdd:cd03290 178 HLMQegILKFLQDDKRTLVLVTHK 201
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-196 |
9.72e-08 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 52.88 E-value: 9.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 2 CILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGR---ALRREQFQDCFSYVLQsDTLLSSLTVRETL----HYTalla 74
Cdd:cd03244 34 GIVGRTGSGKSSLLLALFRLVELSS---GSILIDGVdisKIGLHDLRSRISIIPQ-DPVLFSGTIRSNLdpfgEYS---- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 75 irrgnpgsfQKKVEAVMAELSL-SHVADRLIGNYSL---GG--ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTAN 148
Cdd:cd03244 106 ---------DEELWQALERVGLkEFVESLPGGLDTVveeGGenLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767915018 149 QIVVLLVElARRNRIvVLTI-HqpRSELFQLFDKIAILSFGELIFCGTP 196
Cdd:cd03244 177 LIQKTIRE-AFKDCT-VLTIaH--RLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
3-198 |
1.02e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 53.46 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALR--------REQFQDCFSYV--LQSDTLLSSLTVRETLHY-TA 71
Cdd:PRK11300 36 LIGPNGAGKTTVFNCLTGFYKPTG---GTILLRGQHIEglpghqiaRMGVVRTFQHVrlFREMTVIENLLVAQHQQLkTG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 72 LLAIRRGNPGSFQKKVEAV-MAELSLSHVADRLIGNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQI 150
Cdd:PRK11300 113 LFSGLLKTPAFRRAESEALdRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKEL 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 767915018 151 VVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGTPAE 198
Cdd:PRK11300 193 DELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEE 240
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1-241 |
1.10e-07 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 53.71 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 1 MCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRAlrreQFQDCFSYVLQSdtllsslTVRETLHYTALLAIRRgnp 80
Cdd:cd03291 66 LAITGSTGSGKTSLLMLILGELEPSE---GKIKHSGRI----SFSSQFSWIMPG-------TIKENIIFGVSYDEYR--- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 81 gsFQKKVEAVMAELSLSHVADRLIGNYSLGGI--STGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLV--E 156
Cdd:cd03291 129 --YKSVVKACQLEEDITKFPEKDNTVLGEGGItlSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVckL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 157 LARRNRIVVLTihqpRSELFQLFDKIAILSFGELIFCGTPAEMLDFFndcgypcPEHSNPFdfyMDLTSVDTQSKERE-- 234
Cdd:cd03291 207 MANKTRILVTS----KMEHLKKADKILILHEGSSYFYGTFSELQSLR-------PDFSSKL---MGYDTFDQFSAERRns 272
|
....*....
gi 767915018 235 --IETSKRV 241
Cdd:cd03291 273 ilTETLRRF 281
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-143 |
1.32e-07 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 54.30 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLG-RAGTFlgevyVNGRALRreqfqdcFSYVLQS-DTLLSSLTVRETlhytallaIRRGNP 80
Cdd:COG0488 346 LIGPNGAGKSTLLKLLAGELEpDSGTV-----KLGETVK-------IGYFDQHqEELDPDKTVLDE--------LRDGAP 405
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767915018 81 GSFQKKVEAVMAELSLS-HVADRLIGnySLGGistGERRRVSIAAQLLQDPKVMLFDEPTTGLD 143
Cdd:COG0488 406 GGTEQEVRGYLGRFLFSgDDAFKPVG--VLSG---GEKARLALAKLLLSPPNVLLLDEPTNHLD 464
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
4-199 |
1.58e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 53.21 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 4 LGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRREQFQDCFSYVLQSDTLLSSLTVRETLHYTALLAIRRG--NPG 81
Cdd:PRK13649 39 IGHTGSGKSTIMQLLNGLHVPTQ---GSVRVDDTLITSTSKNKDIKQIRKKVGLVFQFPESQLFEETVLKDVAFGpqNFG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 82 SFQKKVEAVMAE-LSLSHVADRLIGN--YSLGGistGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELA 158
Cdd:PRK13649 116 VSQEEAEALAREkLALVGISESLFEKnpFELSG---GQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLH 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 767915018 159 RRNRIVVLTIHqprselfqLFDKIA-------ILSFGELIFCGTPAEM 199
Cdd:PRK13649 193 QSGMTIVLVTH--------LMDDVAnyadfvyVLEKGKLVLSGKPKDI 232
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
3-143 |
1.63e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.04 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGR----LGR--------------AGTFLG----EVYVNG-RALRREQFQDCFSYVLQSdtlls 59
Cdd:PRK13409 104 ILGPNGIGKTTAVKILSGElipnLGDyeeepswdevlkrfRGTELQnyfkKLYNGEiKVVHKPQYVDLIPKVFKG----- 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 60 slTVRETLHYTAllaiRRGnpgsfqkKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPT 139
Cdd:PRK13409 179 --KVRELLKKVD----ERG-------KLDEVVERLGLENILDRDISE-----LSGGELQRVAIAAALLRDADFYFFDEPT 240
|
....
gi 767915018 140 TGLD 143
Cdd:PRK13409 241 SYLD 244
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-143 |
1.66e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 53.85 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSG---SGKTTLLDAMSGRLGRAGtflGEVYVNGRALRREQFQDCFSYVL-------QSDTLLSSLTVRETLHYTAL 72
Cdd:PRK10762 280 ILGVSGlmgAGRTELMKVLYGALPRTS---GYVTLDGHEVVTRSPQDGLANGIvyisedrKRDGLVLGMSVKENMSLTAL 356
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767915018 73 LAIRRGNpGSFQKKVE--AVMAELSLSHV----ADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLD 143
Cdd:PRK10762 357 RYFSRAG-GSLKHADEqqAVSDFIRLFNIktpsMEQAIGL-----LSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
77-199 |
1.80e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 52.88 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 77 RGNPGS-FQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLV 155
Cdd:PRK13640 113 RAVPRPeMIKIVRDVLADVGMLDYIDSEPAN-----LSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIR 187
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 767915018 156 ELARRNRIVVLTIHQPRSELfQLFDKIAILSFGELIFCGTPAEM 199
Cdd:PRK13640 188 KLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEI 230
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
3-190 |
2.03e-07 |
|
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: 52.09 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALrrEQFQDCF-----SYVLQSDTLLSSlTVRETLHYtallairr 77
Cdd:cd03248 45 LVGPSGSGKSTVVALLENFYQPQG---GQVLLDGKPI--SQYEHKYlhskvSLVGQEPVLFAR-SLQDNIAY-------- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 78 gnpGSFQKKVEAVMAELSLSHvADRLIGNYSLG----------GISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTA 147
Cdd:cd03248 111 ---GLQSCSFECVKEAAQKAH-AHSFISELASGydtevgekgsQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESE 186
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 767915018 148 NQIVVLLVELARRNRIVVLTiHqpRSELFQLFDKIAILSFGEL 190
Cdd:cd03248 187 QQVQQALYDWPERRTVLVIA-H--RLSTVERADQILVLDGGRI 226
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
5-143 |
2.26e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 51.77 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 5 GSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRALRREQFQDCFSYVLQSDTLLSSLTVRETLHYTALLAIRRGN--PGS 82
Cdd:PRK13543 44 GDNGAGKTTLLRVLAG-LLHVES--GQIQIDGKTATRGDRSRFMAYLGHLPGLKADLSTLENLHFLCGLHGRRAKqmPGS 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767915018 83 fqkkveaVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLD 143
Cdd:PRK13543 121 -------ALAIVGLAGYEDTLVRQ-----LSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
111-169 |
2.44e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 52.78 E-value: 2.44e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 767915018 111 GISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIH 169
Cdd:PRK13651 165 ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTH 223
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-201 |
2.64e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 52.43 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLdamsgrLGRAGTFL---GEVYVNGRALRREQ-----------FQDcfsyvlqSDTLLSSLTVRETLh 68
Cdd:PRK13647 36 LLGPNGAGKSTLL------LHLNGIYLpqrGRVKVMGREVNAENekwvrskvglvFQD-------PDDQVFSSTVWDDV- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 69 ytALLAIRRG-NPGSFQKKVEAVMAELSLSHVADRliGNYSLggiSTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTA 147
Cdd:PRK13647 102 --AFGPVNMGlDKDEVERRVEEALKAVRMWDFRDK--PPYHL---SYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767915018 148 NQIVVLLVELARRNRIVVLTIHQPRSELfQLFDKIAILSFGELIFCGTPAEMLD 201
Cdd:PRK13647 175 ETLMEILDRLHNQGKTVIVATHDVDLAA-EWADQVIVLKEGRVLAEGDKSLLTD 227
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
3-199 |
2.95e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 52.01 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRREQ----FQDCFSYVLQS-DTLLSSLTVRETLHYTAL-LAIR 76
Cdd:PRK13633 41 ILGRNGSGKSTIAKHMNALLIPSE---GKVYVDGLDTSDEEnlwdIRNKAGMVFQNpDNQIVATIVEEDVAFGPEnLGIP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 77 rgnPGSFQKKVEAVMAELSLSHVADrlignYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVE 156
Cdd:PRK13633 118 ---PEEIRERVDESLKKVGMYEYRR-----HAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKE 189
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 767915018 157 LARRNRIVVLTIHQPRSELFQLfDKIAILSFGELIFCGTPAEM 199
Cdd:PRK13633 190 LNKKYGITIILITHYMEEAVEA-DRIIVMDSGKVVMEGTPKEI 231
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-233 |
3.08e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 52.02 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLGRAG--TFLGEVYVNGRALRreQFQDCFSYVLQSDTLLSSLTVRETLHYTALLAIRRGNP 80
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMNDKVSgyRYSGDVLLGGRSIF--NYRDVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAHK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 81 ----GSFQKKVEAVMAELSL-SHVADRLigNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLV 155
Cdd:PRK14271 130 lvprKEFRGVAQARLTEVGLwDAVKDRL--SDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIR 207
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767915018 156 ELArrNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGtPAEMLdffndcgYPCPEHSNPFDFYMDLTSvDTQSKER 233
Cdd:PRK14271 208 SLA--DRLTVIIVTHNLAQAARISDRAALFFDGRLVEEG-PTEQL-------FSSPKHAETARYVAGLSG-DVKDAKR 274
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
3-186 |
3.66e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 51.25 E-value: 3.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLGRAgtfLGEVYVNGR---ALRREQFQDCFSYVLQSDTLLSSlTVRETLHYTALlaIRRGN 79
Cdd:PRK10247 38 ITGPSGCGKSTLLKIVASLISPT---SGTLLFEGEdisTLKPEIYRQQVSYCAQTPTLFGD-TVYDNLIFPWQ--IRNQQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 80 PGsfQKKVEAVMAELSLshvaDRLIGNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDcmTANQIVV--LLVEL 157
Cdd:PRK10247 112 PD--PAIFLDDLERFAL----PDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALD--ESNKHNVneIIHRY 183
|
170 180
....*....|....*....|....*....
gi 767915018 158 ARRNRIVVLTIHQPRSELFQLfDKIAILS 186
Cdd:PRK10247 184 VREQNIAVLWVTHDKDEINHA-DKVITLQ 211
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
113-168 |
5.41e-07 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 52.38 E-value: 5.41e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 767915018 113 STGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTI 168
Cdd:COG4172 158 SGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLI 213
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
3-196 |
5.65e-07 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 50.49 E-value: 5.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTL-------LDAMSGRLGRAGTFLGEVYVngRALRREqfqdcFSYVLQSDTLLSSlTVRETL----HYTA 71
Cdd:cd03369 39 IVGRTGAGKSTLilalfrfLEAEEGKIEIDGIDISTIPL--EDLRSS-----LTIIPQDPTLFSG-TIRSNLdpfdEYSD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 72 llairrgnpgsfqkkvEAVMAELSLSHVADRLignyslggiSTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIV 151
Cdd:cd03369 111 ----------------EEIYGALRVSEGGLNL---------SQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQ 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767915018 152 VLLVELArrNRIVVLTI-HQPRSELfqLFDKIAILSFGELIFCGTP 196
Cdd:cd03369 166 KTIREEF--TNSTILTIaHRLRTII--DYDKILVMDAGEVKEYDHP 207
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-143 |
6.85e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 52.24 E-value: 6.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGrlgragtfLGEVYvNGRALRREQFQdcFSYVLQSDTLLSSLTVRETL--------------- 67
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAG--------VDKDF-NGEARPQPGIK--VGYLPQEPQLDPTKTVRENVeegvaeikdaldrfn 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 68 -----------HYTALLAirrgNPGSFQKKVEAVMA---ELSLSHVADRL---IGNYSLGGISTGERRRVSIAAQLLQDP 130
Cdd:TIGR03719 105 eisakyaepdaDFDKLAA----EQAELQEIIDAADAwdlDSQLEIAMDALrcpPWDADVTKLSGGERRRVALCRLLLSKP 180
|
170
....*....|...
gi 767915018 131 KVMLFDEPTTGLD 143
Cdd:TIGR03719 181 DMLLLDEPTNHLD 193
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
3-169 |
6.90e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 50.26 E-value: 6.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRALRREQFQDC------FSYVLQSDTLLSSLTVRETLHYTALLAIR 76
Cdd:PRK10908 33 LTGHSGAGKSTLLKLICG-IERPSA--GKIWFSGHDITRLKNREVpflrrqIGMIFQDHHLLMDRTVYDNVAIPLIIAGA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 77 RGNpgSFQKKVEAVMAELSLSHVADrligNYSLGgISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVE 156
Cdd:PRK10908 110 SGD--DIRRRVSAALDKVGLLDKAK----NFPIQ-LSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEE 182
|
170
....*....|...
gi 767915018 157 LARRNRIVVLTIH 169
Cdd:PRK10908 183 FNRVGVTVLMATH 195
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
3-157 |
6.92e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 51.50 E-value: 6.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLldamsgrlGRAGTFL-----GEVYVNG----------RALRREQFQdcfsYVLQSDtlLSSLTVRETL 67
Cdd:PRK11308 46 VVGESGCGKSTL--------ARLLTMIetptgGELYYQGqdllkadpeaQKLLRQKIQ----IVFQNP--YGSLNPRKKV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 68 HY---------TALLAIRRgnpgsfQKKVEAVMAELSL--SHvADRLIGNYSlggisTGERRRVSIAAQLLQDPKVMLFD 136
Cdd:PRK11308 112 GQileepllinTSLSAAER------REKALAMMAKVGLrpEH-YDRYPHMFS-----GGQRQRIAIARALMLDPDVVVAD 179
|
170 180
....*....|....*....|.
gi 767915018 137 EPTTGLDCMTANQIVVLLVEL 157
Cdd:PRK11308 180 EPVSALDVSVQAQVLNLMMDL 200
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1-199 |
8.30e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 52.22 E-value: 8.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 1 MCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRAlrreQFQDCFSYVLQS---DTLLSSLTVREtLHYTALlairr 77
Cdd:TIGR01271 455 LAVAGSTGSGKSSLLMMIMGELEPSE---GKIKHSGRI----SFSPQTSWIMPGtikDNIIFGLSYDE-YRYTSV----- 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 78 gnpgsfqkkVEAVMAELSLSHVADRLIGNYSLGGI--STGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIV--VL 153
Cdd:TIGR01271 522 ---------IKACQLEEDIALFPEKDKTVLGEGGItlSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFesCL 592
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767915018 154 LVELARRNRIVVLTihqpRSELFQLFDKIAILSFGELIFCGTPAEM 199
Cdd:TIGR01271 593 CKLMSNKTRILVTS----KLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
108-188 |
9.99e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.27 E-value: 9.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 108 SLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNR-IVVLTIHQPrsELFQLFDKIAILS 186
Cdd:PRK10982 388 QIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKgIIIISSEMP--ELLGITDRILVMS 465
|
..
gi 767915018 187 FG 188
Cdd:PRK10982 466 NG 467
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
111-208 |
1.26e-06 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 49.45 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 111 GISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGEL 190
Cdd:cd03217 104 GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIKPDRVHVLYDGRI 183
|
90
....*....|....*...
gi 767915018 191 IFCGtPAEMLDFFNDCGY 208
Cdd:cd03217 184 VKSG-DKELALEIEKKGY 200
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
3-169 |
1.30e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 50.51 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLGRAGTFLGE-VYVNGRALR------REQ---------FQDCfsyvlqsdtlLSSLTVRET 66
Cdd:PRK11022 38 IVGESGSGKSVSSLAIMGLIDYPGRVMAEkLEFNGQDLQrisekeRRNlvgaevamiFQDP----------MTSLNPCYT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 67 LHYTALLAIRRGNPGSFQKKVEAVMAELSLSHVAD---RL-IGNYSLGGistGERRRVSIAAQLLQDPKVMLFDEPTTGL 142
Cdd:PRK11022 108 VGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDpasRLdVYPHQLSG---GMSQRVMIAMAIACRPKLLIADEPTTAL 184
|
170 180
....*....|....*....|....*...
gi 767915018 143 DCMTANQIVVLLVELARR-NRIVVLTIH 169
Cdd:PRK11022 185 DVTIQAQIIELLLELQQKeNMALVLITH 212
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
5-201 |
1.39e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.08 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 5 GSSGSGKTTLLDAMSGrLGRAGTFLGEVYVNGRALR----REQFQDCFSYVLQSDTLLSSLTVRET------------LH 68
Cdd:PRK13549 38 GENGAGKSTLMKVLSG-VYPHGTYEGEIIFEGEELQasniRDTERAGIAIIHQELALVKELSVLENiflgneitpggiMD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 69 YTALLAirrgnpgsfqkKVEAVMAELSLSHVADRLIGNYSLggistGERRRVSIAAQLLQDPKVMLFDEPTTGLdcmTAN 148
Cdd:PRK13549 117 YDAMYL-----------RAQKLLAQLKLDINPATPVGNLGL-----GQQQLVEIAKALNKQARLLILDEPTASL---TES 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767915018 149 QIVVLL--VELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIfcGT-PAEMLD 201
Cdd:PRK13549 178 ETAVLLdiIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHI--GTrPAAGMT 231
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
3-165 |
1.81e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 51.28 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLgrAGTFLGEVYVNGRAlrreqfqdcfSYVLQSDTLLSSlTVRETLHYTALLairrgNPGS 82
Cdd:PLN03130 648 IVGSTGEGKTSLISAMLGEL--PPRSDASVVIRGTV----------AYVPQVSWIFNA-TVRDNILFGSPF-----DPER 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 83 FQKKVEAVmaelSLSHVADRL-------IGNYSLGgISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIV--VL 153
Cdd:PLN03130 710 YERAIDVT----ALQHDLDLLpggdlteIGERGVN-ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFdkCI 784
|
170
....*....|..
gi 767915018 154 LVELARRNRIVV 165
Cdd:PLN03130 785 KDELRGKTRVLV 796
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
112-200 |
2.51e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 49.80 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 112 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELI 191
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
....*....
gi 767915018 192 FCGTPAEML 200
Cdd:PRK15093 239 ETAPSKELV 247
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
3-162 |
2.83e-06 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 49.96 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLL-------DAMSGRLGRAGTFLGEVyvNGRALRREqfqdcFSYVLQsDTLLSSLTVRETlhytallaI 75
Cdd:PRK13657 366 IVGPTGAGKSTLInllqrvfDPQSGRILIDGTDIRTV--TRASLRRN-----IAVVFQ-DAGLFNRSIEDN--------I 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 76 RRGNPGSFQKKV-EAVMAELSLSHVADRLIGNYSLGG-----ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQ 149
Cdd:PRK13657 430 RVGRPDATDEEMrAAAERAQAHDFIERKPDGYDTVVGergrqLSGGERQRLAIARALLKDPPILILDEATSALDVETEAK 509
|
170
....*....|...
gi 767915018 150 IVVLLVELaRRNR 162
Cdd:PRK13657 510 VKAALDEL-MKGR 521
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-201 |
3.08e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 50.05 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRR---EQFQDCFSY-VLQSDTLLSSLTVRETLhytallAIRRG 78
Cdd:PRK15439 42 LLGGNGAGKSTLMKIIAGIVPPDS---GTLEIGGNPCARltpAKAHQLGIYlVPQEPLLFPNLSVKENI------LFGLP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 79 NPGSFQKKVEAVMAELSLShvadrLIGNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELA 158
Cdd:PRK15439 113 KRQASMQKMKQLLAALGCQ-----LDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELL 187
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 767915018 159 RRNRIVVLTIHQPRsELFQLFDKIAILSFGELIFCGTPAEMLD 201
Cdd:PRK15439 188 AQGVGIVFISHKLP-EIRQLADRISVMRDGTIALSGKTADLST 229
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
3-201 |
4.26e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 49.94 E-value: 4.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMsgrLGRAGTFLGEVYVNGRAlrreqfqdcfSYVLQSdTLLSSLTVRETLHYTALLairrgNPGS 82
Cdd:TIGR00957 669 VVGQVGCGKSSLLSAL---LAEMDKVEGHVHMKGSV----------AYVPQQ-AWIQNDSLRENILFGKAL-----NEKY 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 83 FQKKVEA--VMAELSLSHVADRL-IGNYSLGgISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIV--VLLVEL 157
Cdd:TIGR00957 730 YQQVLEAcaLLPDLEILPSGDRTeIGEKGVN-LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFehVIGPEG 808
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 767915018 158 ARRNRIVVLTIHQpRSELFQLfDKIAILSFGELIFCGTPAEMLD 201
Cdd:TIGR00957 809 VLKNKTRILVTHG-ISYLPQV-DVIIVMSGGKISEMGSYQELLQ 850
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-189 |
4.80e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 48.49 E-value: 4.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAmsgrLGRAGTFLGEVYVNGRA----------------LRREqfqdcFSYVLQSDTLLSsLTVRET 66
Cdd:PRK14258 38 IIGPSGCGKSTFLKC----LNRMNELESEVRVEGRVeffnqniyerrvnlnrLRRQ-----VSMVHPKPNLFP-MSVYDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 67 LHYTALLAIRRGNPgSFQKKVEAVMAELSL-SHVADRLigNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCM 145
Cdd:PRK14258 108 VAYGVKIVGWRPKL-EIDDIVESALKDADLwDEIKHKI--HKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPI 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 767915018 146 TANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGE 189
Cdd:PRK14258 185 ASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNE 228
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-215 |
4.98e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 48.55 E-value: 4.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLGRagtFLGEVYVNGRALRREQFQDC---FSYVLQS-DTLLSSLTVRETLhytALLAIRRG 78
Cdd:PRK13642 38 IIGQNGSGKSTTARLIDGLFEE---FEGKVKIDGELLTAENVWNLrrkIGMVFQNpDNQFVGATVEDDV---AFGMENQG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 79 NP-GSFQKKVEAVMAELSLSHVADRlignySLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVEL 157
Cdd:PRK13642 112 IPrEEMIKRVDEALLAVNMLDFKTR-----EPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEI 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767915018 158 ARRNRIVVLTIHQPRSELFQlFDKIAILSFGELIFCGTPAEMLDFFND---CGYPCPEHSN 215
Cdd:PRK13642 187 KEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDmveIGLDVPFSSN 246
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
110-190 |
5.05e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 49.28 E-value: 5.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 110 GGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNrIVVLTIHQPRSELFQLFDKIAILSFGE 189
Cdd:PRK15439 402 RTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQN-VAVLFISSDLEEIEQMADRVLVMHQGE 480
|
.
gi 767915018 190 L 190
Cdd:PRK15439 481 I 481
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-194 |
6.23e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.08 E-value: 6.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 1 MCILGSSGSGKTTlldamSGR--LGRAGTFLGEVYVNGR-----------ALRREQ---FQDCFSyvlqsdtllsSLTVR 64
Cdd:PRK10261 353 LSLVGESGSGKST-----TGRalLRLVESQGGEIIFNGQridtlspgklqALRRDIqfiFQDPYA----------SLDPR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 65 ETLHYTALLAIR---RGNPGSFQKKVEAVMAELSL--SHvADRLIGNYSlggisTGERRRVSIAAQLLQDPKVMLFDEPT 139
Cdd:PRK10261 418 QTVGDSIMEPLRvhgLLPGKAAAARVAWLLERVGLlpEH-AWRYPHEFS-----GGQRQRICIARALALNPKVIIADEAV 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767915018 140 TGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCG 194
Cdd:PRK10261 492 SALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-194 |
8.61e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 48.63 E-value: 8.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRR----EQFQDCFSYVLQSDTLLSSLTVRETLhYTALLAIRR- 77
Cdd:PRK09700 36 LLGENGAGKSTLMKVLSGIHEPTK---GTITINNINYNKldhkLAAQLGIGIIYQELSVIDELTVLENL-YIGRHLTKKv 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 78 -GNPGSFQKKVEAVMAELsLSHVADRLIGNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVE 156
Cdd:PRK09700 112 cGVNIIDWREMRVRAAMM-LLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQ 190
|
170 180 190
....*....|....*....|....*....|....*...
gi 767915018 157 LARRNRIVVLTIHQpRSELFQLFDKIAILSFGELIFCG 194
Cdd:PRK09700 191 LRKEGTAIVYISHK-LAEIRRICDRYTVMKDGSSVCSG 227
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
3-200 |
8.89e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 48.79 E-value: 8.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSgRLGRAGTflGEVYVNGRALRREQFQDCFS--YVLQSDTLLSSLTVRETLhytallairrgNP 80
Cdd:TIGR00957 1317 IVGRTGAGKSSLTLGLF-RINESAE--GEIIIDGLNIAKIGLHDLRFkiTIIPQDPVLFSGSLRMNL-----------DP 1382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 81 GSfQKKVEAVMAELSLSHV-------ADRLIGNYSLGG--ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANqiv 151
Cdd:TIGR00957 1383 FS-QYSDEEVWWALELAHLktfvsalPDKLDHECAEGGenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDN--- 1458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767915018 152 vlLVELARRNRI---VVLTIHQpRSELFQLFDKIAILSFGELIFCGTPAEML 200
Cdd:TIGR00957 1459 --LIQSTIRTQFedcTVLTIAH-RLNTIMDYTRVIVLDKGEVAEFGAPSNLL 1507
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-199 |
1.33e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 47.71 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRR---EQFQDC-FSYVL---QSDTLLSSLTVRE----TLHYTA 71
Cdd:COG3845 289 IAGVAGNGQSELAEALAGLRPPAS---GSIRLDGEDITGlspRERRRLgVAYIPedrLGRGLVPDMSVAEnlilGRYRRP 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 72 LLAiRRG--NPGSFQKKVEAVMAELSL-SHVADRLIGNYSLGGIstgerRRVSIAAQLLQDPKVMLFDEPTTGLDCMTAN 148
Cdd:COG3845 366 PFS-RGGflDRKAIRAFAEELIEEFDVrTPGPDTPARSLSGGNQ-----QKVILARELSRDPKLLIAAQPTRGLDVGAIE 439
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 767915018 149 QIVVLLVELARRNRIVVLtIHQPRSELFQLFDKIAILSFGELIFCGTPAEM 199
Cdd:COG3845 440 FIHQRLLELRDAGAAVLL-ISEDLDEILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
2-171 |
1.52e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 46.49 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 2 CILGSSGSGKTTLLDAMSGrlgragtflgevyvngrALRREQFQDCFsyVLQSDTLLSSLTVRETLhytallairrGNPG 81
Cdd:COG2401 60 LIVGASGSGKSTLLRLLAG-----------------ALKGTPVAGCV--DVPDNQFGREASLIDAI----------GRKG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 82 SFQKKVEaVMAELSLSHVA------DRLignyslggiSTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLV 155
Cdd:COG2401 111 DFKDAVE-LLNAVGLSDAVlwlrrfKEL---------STGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQ 180
|
170
....*....|....*..
gi 767915018 156 ELARRNRI-VVLTIHQP 171
Cdd:COG2401 181 KLARRAGItLVVATHHY 197
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
3-159 |
1.56e-05 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 47.39 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTT-------LLDAMSGR---LGRAGTFLGEVyvNGRALRRE-Q--FQDCfsyvlqsdtlLSSLTVRETLHY 69
Cdd:PRK15079 52 VVGESGCGKSTfaraiigLVKATDGEvawLGKDLLGMKDD--EWRAVRSDiQmiFQDP----------LASLNPRMTIGE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 70 TALLAIRRGNP----GSFQKKVEAVMAELSLshvADRLIGNYSlGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCM 145
Cdd:PRK15079 120 IIAEPLRTYHPklsrQEVKDRVKAMMLKVGL---LPNLINRYP-HEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 195
|
170
....*....|....
gi 767915018 146 TANQIVVLLVELAR 159
Cdd:PRK15079 196 IQAQVVNLLQQLQR 209
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
3-143 |
2.18e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 46.76 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGrlgragtfL-----GEVYVNGR-------ALRreqfqDCfSYVLQSDTLLSSLTVRETLHYT 70
Cdd:PRK11650 35 LVGPSGCGKSTLLRMVAG--------LeritsGEIWIGGRvvnelepADR-----DI-AMVFQNYALYPHMSVRENMAYG 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767915018 71 alLAIRRGNPGSFQKKVEAVMAELSLSHVADR----LignyslggiSTGERRRVSIAAQLLQDPKVMLFDEPTTGLD 143
Cdd:PRK11650 101 --LKIRGMPKAEIEERVAEAARILELEPLLDRkpreL---------SGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
3-200 |
2.49e-05 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 46.94 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTT---LL----DAMSGrlgragtflgEVYVNGRALR-------REQFqdcfSYVLQS-----DTLLSSLTV 63
Cdd:PRK11176 374 LVGRSGSGKSTianLLtrfyDIDEG----------EILLDGHDLRdytlaslRNQV----ALVSQNvhlfnDTIANNIAY 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 64 RETLHYT---ALLAIRRGNPGSFQKKVEavmaelslsHVADRLIG-NYSLggISTGERRRVSIAAQLLQDPKVMLFDEPT 139
Cdd:PRK11176 440 ARTEQYSreqIEEAARMAYAMDFINKMD---------NGLDTVIGeNGVL--LSGGQRQRIAIARALLRDSPILILDEAT 508
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767915018 140 TGLDCMTANQIVVLLVELaRRNRIVVLTIHqpRSELFQLFDKIAILSFGELIFCGTPAEML 200
Cdd:PRK11176 509 SALDTESERAIQAALDEL-QKNRTSLVIAH--RLSTIEKADEILVVEDGEIVERGTHAELL 566
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
95-186 |
2.83e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.33 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 95 SLSHVADRLIGNYSlGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQpRSE 174
Cdd:PTZ00265 1343 SLPNKYDTNVGPYG-KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIA 1420
|
90
....*....|..
gi 767915018 175 LFQLFDKIAILS 186
Cdd:PTZ00265 1421 SIKRSDKIVVFN 1432
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
3-201 |
3.25e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 45.90 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRALRREQFQDCFSY---VLQSDtllSSLTVRETLHYTALLAIRrGN 79
Cdd:PRK13648 40 IVGHNGSGKSTIAKLMIG-IEKVKS--GEIFYNNQAITDDNFEKLRKHigiVFQNP---DNQFVGSIVKYDVAFGLE-NH 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 80 PGSFQKKVEAVMAELSLSHVADRliGNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELAR 159
Cdd:PRK13648 113 AVPYDEMHRRVSEALKQVDMLER--ADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKS 190
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767915018 160 RNRIVVLTIHQPRSELFQLfDKIAILSFGELIFCGTPAEMLD 201
Cdd:PRK13648 191 EHNITIISITHDLSEAMEA-DHVIVMNKGTVYKEGTPTEIFD 231
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
3-198 |
3.73e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 46.70 E-value: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLdamsgrlgraGTFLGEVYVN-GRALRREQFqdcfSYVLQSDTLLSSlTVRETLhytalLAIRRGNPG 81
Cdd:PTZ00243 691 VLGATGSGKSTLL----------QSLLSQFEISeGRVWAERSI----AYVPQQAWIMNA-TVRGNI-----LFFDEEDAA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 82 SFQKKVEAVMAELSLSHVADRL---IGNYSLGgISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIV--VLLVE 156
Cdd:PTZ00243 751 RLADAVRVSQLEADLAQLGGGLeteIGEKGVN-LSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVeeCFLGA 829
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767915018 157 LARRNRivVLTIHQprSELFQLFDKIAILSFGELIFCGTPAE 198
Cdd:PTZ00243 830 LAGKTR--VLATHQ--VHVVPRADYVVALGDGRVEFSGSSAD 867
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-143 |
5.43e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.88 E-value: 5.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMsgrlgrAGT---FLGEVyvngralrreQFQDCFS--YVLQSDTLLSSLTVRETL-----HYTAL 72
Cdd:PRK11819 38 VLGLNGAGKSTLLRIM------AGVdkeFEGEA----------RPAPGIKvgYLPQEPQLDPEKTVRENVeegvaEVKAA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 73 LA------IRRGNPGSFQKKVEAVMAELS--------------LSHVADRL---IGNYSLGGISTGERRRVSIAAQLLQD 129
Cdd:PRK11819 102 LDrfneiyAAYAEPDADFDALAAEQGELQeiidaadawdldsqLEIAMDALrcpPWDAKVTKLSGGERRRVALCRLLLEK 181
|
170
....*....|....
gi 767915018 130 PKVMLFDEPTTGLD 143
Cdd:PRK11819 182 PDMLLLDEPTNHLD 195
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-190 |
5.63e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 45.69 E-value: 5.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSG---SGKTTLLDAMSGrlGRAGTFLGEVYVNGRALRREQFQDCFSYVL-------QSDTLLSSLTVRETLHYTAL 72
Cdd:PRK13549 290 ILGIAGlvgAGRTELVQCLFG--AYPGRWEGEIFIDGKPVKIRNPQQAIAQGIamvpedrKRDGIVPVMGVGKNITLAAL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 73 LAIRRG---NPGSFQKKVEAVMAELSLSHVADRLignySLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQ 149
Cdd:PRK13549 368 DRFTGGsriDDAAELKTILESIQRLKVKTASPEL----AIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYE 443
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 767915018 150 IVVLLVELARRNrIVVLTIHQPRSELFQLFDKIAILSFGEL 190
Cdd:PRK13549 444 IYKLINQLVQQG-VAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
3-200 |
7.31e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.39 E-value: 7.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLgragTFL-GEVYVNGRALRR---EQFQDCFSYVLQSDT--LLS------SLTVRETLhyt 70
Cdd:PRK10938 34 FVGANGSGKSALARALAGEL----PLLsGERQSQFSHITRlsfEQLQKLVSDEWQRNNtdMLSpgeddtGRTTAEII--- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 71 aLLAIRRGNpgsfqkKVEAVMAELSLSHVADRLIgNYslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQI 150
Cdd:PRK10938 107 -QDEVKDPA------RCEQLAQQFGITALLDRRF-KY----LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767915018 151 VVLLVELARRNRIVVLTIHQpRSELFQLFDKIAILSFGELIFCGTPAEML 200
Cdd:PRK10938 175 AELLASLHQSGITLVLVLNR-FDEIPDFVQFAGVLADCTLAETGEREEIL 223
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
113-169 |
1.03e-04 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 42.44 E-value: 1.03e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 767915018 113 STGERRRVSIAAQLLQDPKVMLFDEPTTGLDcMTAnqIVVLLVELARRNRIVVLTIH 169
Cdd:cd03221 72 SGGEKMRLALAKLLLENPNLLLLDEPTNHLD-LES--IEALEEALKEYPGTVILVSH 125
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-201 |
1.10e-04 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 45.10 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 2 CILGSSGSGKTTLLdAMSGRLGRAGTflGEVYVNGRALrrEQFQDCFSY----VLQSDTLLSSLTVRETLHYtallairr 77
Cdd:TIGR00958 511 ALVGPSGSGKSTVA-ALLQNLYQPTG--GQVLLDGVPL--VQYDHHYLHrqvaLVGQEPVLFSGSVRENIAY-------- 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 78 gnpGSFQKKVEAVMAELSLSHvADRLIGNYSLGG----------ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCmta 147
Cdd:TIGR00958 578 ---GLTDTPDEEIMAAAKAAN-AHDFIMEFPNGYdtevgekgsqLSGGQKQRIAIARALVRKPRVLILDEATSALDA--- 650
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767915018 148 nQIVVLLVEL-ARRNRIVVLTIHqpRSELFQLFDKIAILSFGELIFCGTPAEMLD 201
Cdd:TIGR00958 651 -ECEQLLQESrSRASRTVLLIAH--RLSTVERADQILVLKKGSVVEMGTHKQLME 702
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
3-143 |
2.35e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.03 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLG-RAGTFLGEVYVngralrreqfqdcfSYVLQSDTLLSSLTVREtlhytaLLAIRRGNPG 81
Cdd:PRK13409 370 IVGPNGIGKTTFAKLLAGVLKpDEGEVDPELKI--------------SYKPQYIKPDYDGTVED------LLRSITDDLG 429
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767915018 82 SFQKKVEaVMAELSLSHVADRlignySLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLD 143
Cdd:PRK13409 430 SSYYKSE-IIKPLQLERLLDK-----NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
2-143 |
3.74e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 43.40 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 2 CILGSSGSGKTTLLDAMSG------------------RLG----RAGTflGEVY------VNGRALRREQFQDCFSYVLQ 53
Cdd:PRK11147 33 CLVGRNGAGKSTLMKILNGevllddgriiyeqdlivaRLQqdppRNVE--GTVYdfvaegIEEQAEYLKRYHDISHLVET 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 54 --SDTLLSSL-TVRETLHYTallairrgNPGSFQKKVEAVMAELSLShvadrliGNYSLGGISTGERRRVSIAAQLLQDP 130
Cdd:PRK11147 111 dpSEKNLNELaKLQEQLDHH--------NLWQLENRINEVLAQLGLD-------PDAALSSLSGGWLRKAALGRALVSNP 175
|
170
....*....|...
gi 767915018 131 KVMLFDEPTTGLD 143
Cdd:PRK11147 176 DVLLLDEPTNHLD 188
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
3-143 |
4.73e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 42.85 E-value: 4.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSGRLG-RAGTFLGEVYVngralrreqfqdcfSY---VLQSDtllSSLTVRETLhytallaiRRG 78
Cdd:COG1245 371 IVGPNGIGKTTFAKILAGVLKpDEGEVDEDLKI--------------SYkpqYISPD---YDGTVEEFL--------RSA 425
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767915018 79 NPGSFQ-KKVEAVMAE-LSLSHVADRlignySLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLD 143
Cdd:COG1245 426 NTDDFGsSYYKTEIIKpLGLEKLLDK-----NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3-190 |
5.06e-04 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 41.97 E-value: 5.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLL-------DAMSGRLGRAGTFLGEVyvngRALRREQFQDCfsyvlqsdTLLSSLTVRETLHytalLAI 75
Cdd:PRK11247 43 VVGRSGCGKSTLLrllagleTPSAGELLAGTAPLAEA----REDTRLMFQDA--------RLLPWKKVIDNVG----LGL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 76 RrgnpGSFQKKVEAVMAELSLshvADRliGNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLV 155
Cdd:PRK11247 107 K----GQWRDAALQALAAVGL---ADR--ANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIE 177
|
170 180 190
....*....|....*....|....*....|....*
gi 767915018 156 ELARRNRIVVLTIHQPRSELFQLFDKIAILSFGEL 190
Cdd:PRK11247 178 SLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
3-170 |
5.91e-04 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 42.98 E-value: 5.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAmsgrLGRAGTFLGEVYVNG---RALRREQFQDCFSYVLQSDTLLSSlTVRETLHYTALLAirrgn 79
Cdd:TIGR01271 1250 LLGRTGSGKSTLLSA----LLRLLSTEGEIQIDGvswNSVTLQTWRKAFGVIPQKVFIFSG-TFRKNLDPYEQWS----- 1319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 80 pgsfQKKVEAVMAELSLSHVADRLIG--NYSL--GG--ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTAnQIVVL 153
Cdd:TIGR01271 1320 ----DEEIWKVAEEVGLKSVIEQFPDklDFVLvdGGyvLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTL-QIIRK 1394
|
170
....*....|....*..
gi 767915018 154 LVELARRNRIVVLTIHQ 170
Cdd:TIGR01271 1395 TLKQSFSNCTVILSEHR 1411
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
112-195 |
6.53e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 42.54 E-value: 6.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 112 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELI 191
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
....
gi 767915018 192 FCGT 195
Cdd:PRK10261 249 ETGS 252
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
106-172 |
7.32e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 40.77 E-value: 7.32e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767915018 106 NYSLGGISTGERRRVSIAAQLLQDPK--VMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPR 172
Cdd:cd03238 82 GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLD 150
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
107-187 |
7.69e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 40.42 E-value: 7.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 107 YSLGGISTGERRRVSIAAQL----LQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPrsELFQLFDKI 182
Cdd:cd03227 73 FTRLQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLP--ELAELADKL 150
|
....*
gi 767915018 183 AILSF 187
Cdd:cd03227 151 IHIKK 155
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
3-200 |
8.43e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 42.66 E-value: 8.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDAMSgRLGRAGTflGEVYVNGRALRREQFQD---CFSYVLQSDTLLSSlTVRETLhytallairrgN 79
Cdd:PLN03232 1267 VVGRTGAGKSSMLNALF-RIVELEK--GRIMIDDCDVAKFGLTDlrrVLSIIPQSPVLFSG-TVRFNI-----------D 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 80 PgsFQKKVEAVMAE-LSLSHVADrLIGNYSLG----------GISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTAN 148
Cdd:PLN03232 1332 P--FSEHNDADLWEaLERAHIKD-VIDRNPFGldaevseggeNFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDS 1408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767915018 149 QIVVLLVELARRNRIVVLTiHqpRSELFQLFDKIAILSFGELIFCGTPAEML 200
Cdd:PLN03232 1409 LIQRTIREEFKSCTMLVIA-H--RLNTIIDCDKILVLSSGQVLEYDSPQELL 1457
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
95-170 |
1.38e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.94 E-value: 1.38e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767915018 95 SLSHVADRLIGNySLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVEL-ARRNRIVVLTIHQ 170
Cdd:PTZ00265 564 ALPDKYETLVGS-NASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRITIIIAHR 639
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
3-27 |
1.69e-03 |
|
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.
Pssm-ID: 206733 [Multi-domain] Cd Length: 268 Bit Score: 40.65 E-value: 1.69e-03
10 20
....*....|....*....|....*...
gi 767915018 3 ILGSSGSGKTTLLDAM---SGRLGRAGT 27
Cdd:cd04170 4 LVGHSGSGKTTLAEALlyaTGAIDRLGR 31
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
100-166 |
1.70e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 41.05 E-value: 1.70e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767915018 100 ADRLIGNyslggISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVL 166
Cdd:PRK11288 390 REQLIMN-----LSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLF 451
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
112-165 |
2.91e-03 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 39.09 E-value: 2.91e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 767915018 112 ISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDC---MTANQIVVLLVELARRNRIVV 165
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIeqrLNAARAIRRLSEEGKKTALVV 128
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
3-19 |
8.83e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 34.88 E-value: 8.83e-03
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
3-199 |
9.87e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 38.99 E-value: 9.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 3 ILGSSGSGKTTLLDamsgrlgragTFL-------GEVYVNGR--------ALRREqfqdcFSYVLQsDTLLSSLTVRETL 67
Cdd:PTZ00243 1341 IVGRTGSGKSTLLL----------TFMrmvevcgGEIRVNGReigayglrELRRQ-----FSMIPQ-DPVLFDGTVRQNV 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915018 68 hytallairrgNPGSfQKKVEAVMAELSL----SHVADRLIG----------NYSLGgistgERRRVSIAAQLLQ-DPKV 132
Cdd:PTZ00243 1405 -----------DPFL-EASSAEVWAALELvglrERVASESEGidsrvleggsNYSVG-----QRQLMCMARALLKkGSGF 1467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767915018 133 MLFDEPTTGLDCMTANQIVVLlVELARRNRIVVLTIHqpRSELFQLFDKIAILSFGELIFCGTPAEM 199
Cdd:PTZ00243 1468 ILMDEATANIDPALDRQIQAT-VMSAFSAYTVITIAH--RLHTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
|
| |
