|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1-497 |
6.17e-77 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 253.05 E-value: 6.17e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLAdptKDLIDNSCIRINNEKGTLPK--RLVGVVWQEDLLLPNL 78
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSP---KGVKGSGSVLLNGMPIDAKEmrAISAYVQQDDLFIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 79 TVHETVRFAARLKTPKEQTDGEVEVLVEETLSQLGLTHVQHSLIGGGAGKRGISGGERKRVAVAVELVARPSVLLLDEPT 158
Cdd:TIGR00955 115 TVREHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 159 SGLDSSTAFKLMLTLKELASLGHAIAVVIHQPRTSIFNLFDNLLLLQKGNVVYEGKASevkrylEACPLCTKL----PPE 234
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPD------QAVPFFSDLghpcPEN 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 235 TGLADWLMDMI-----DEDEKRDGGGKlpaLWKNHsskqpQANDATNSADQqlqstgfNTTPRRMLDKRLSSLAELKSEP 309
Cdd:TIGR00955 269 YNPADFYVQVLavipgSENESRERIEK---ICDSF-----AVSDIGRDMLV-------NTNLWSGKAGGLVKDSENMEGI 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 310 KFQTGFVTQLRLLAKRAS----KQQRGERITRVATLLTACWIAftALAWGrIPDTSIYVFNRASLLFFMIIAQSNGVVVS 385
Cdd:TIGR00955 334 GYNASWWTQFYALLKRSWlsvlRDPLLLKVRLIQTMMTAILIG--LIYLG-QGLTQKGVQNINGALFLFLTNMTFQNVFP 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 386 SMMAFSSERRLLSRERAKKLYGVLPYFIAKTLSDMVNSVALPLLYGCVVYWLCNFRATAVAFFTFALTYYLTIAAAQSTG 465
Cdd:TIGR00955 411 VINVFTAELPVFLRETRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGATHFLTFLFLVTLVANVATSFG 490
|
490 500 510
....*....|....*....|....*....|..
gi 224007385 466 LFLSIAIPNFAVALLLAPLLTVCLMILGGFYI 497
Cdd:TIGR00955 491 YLISCAFSSTSMALTVGPPFVIPFLLFGGFFI 522
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1-497 |
7.38e-64 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 218.98 E-value: 7.38e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLladptkdlIDNSC----IRINNEKGTLPK-RLVGVVWQEDLLL 75
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGR--------IQGNNftgtILANNRKPTKQIlKRTGFVTQDDILY 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 76 PNLTVHETVRFAARLKTPKEQTDGEVEVLVEETLSQLGLTHVQHSLIGGgAGKRGISGGERKRVAVAVELVARPSVLLLD 155
Cdd:PLN03211 153 PHLTVRETLVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGN-SFIRGISGGERKRVSIAHEMLINPSLLILD 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 156 EPTSGLDSSTAFKLMLTLKELASLGHAIAVVIHQPRTSIFNLFDNLLLLQKGNVVYEGKASEVKRYLEACPLCTKLPpeT 235
Cdd:PLN03211 232 EPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESVGFSPSFP--M 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 236 GLADWLMDM------IDEDEKRDGGGKLPALWKNHSS-KQPQANDATNSADqqlqstgFNTTPRRMLDKRLSSLAELKSE 308
Cdd:PLN03211 310 NPADFLLDLangvcqTDGVSEREKPNVKQSLVASYNTlLAPKVKAAIEMSH-------FPQANARFVGSASTKEHRSSDR 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 309 PKFQTGFvTQLRLLAKRASKQQRGERIT--RVATLLTACWIAftALAWGRIPDTSIYvfNRASLLFFMIIAQsnGVVVS- 385
Cdd:PLN03211 383 ISISTWF-NQFSILLQRSLKERKHESFNtlRVFQVIAAALLA--GLMWWHSDFRDVQ--DRLGLLFFISIFW--GVFPSf 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 386 -SMMAFSSERRLLSRERAKKLYGVLPYFIAKTLSDMVNSVALPLLYGCVVYWLCNFRATAVAFFTFALTYYLTIAAAQST 464
Cdd:PLN03211 456 nSVFVFPQERAIFVKERASGMYTLSSYFMARIVGDLPMELILPTIFLTVTYWMAGLKPELGAFLLTLLVLLGYVLVSQGL 535
|
490 500 510
....*....|....*....|....*....|...
gi 224007385 465 GLFLSIAIPNFAVALLLAPLLTVCLMILGGFYI 497
Cdd:PLN03211 536 GLALGAAIMDAKKASTIVTVTMLAFVLTGGFYV 568
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1-213 |
2.45e-55 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 183.52 E-value: 2.45e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLladpTKDLIDNSCIRINNEKGTL--PKRLVGVVWQEDLLLPNL 78
Cdd:cd03213 22 KQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGR----RTGLGVSGEVLINGRPLDKrsFRKIIGYVPQDDILHPTL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 79 TVHETVRFAARLktpkeqtdgevevlveetlsqlglthvqhsligggagkRGISGGERKRVAVAVELVARPSVLLLDEPT 158
Cdd:cd03213 98 TVRETLMFAAKL--------------------------------------RGLSGGERKRVSIALELVSNPSLLFLDEPT 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 224007385 159 SGLDSSTAFKLMLTLKELASLGHAIAVVIHQPRTSIFNLFDNLLLLQKGNVVYEG 213
Cdd:cd03213 140 SGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1-213 |
3.81e-53 |
|
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: 179.00 E-value: 3.81e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLADptkDLIDNSCIRINNE---KGTLPKRlVGVVWQEDLLLPN 77
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEG---GGTTSGQILFNGQprkPDQFQKC-VAYVRQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 78 LTVHETVRFAARLKTPKEQTDGEVEVLVEET-LSQLGLTHVQHSLIgggagkRGISGGERKRVAVAVELVARPSVLLLDE 156
Cdd:cd03234 96 LTVRETLTYTAILRLPRKSSDAIRKKRVEDVlLRDLALTRIGGNLV------KGISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 224007385 157 PTSGLDSSTAFKLMLTLKELASLGHAIAVVIHQPRTSIFNLFDNLLLLQKGNVVYEG 213
Cdd:cd03234 170 PTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1-497 |
2.24e-40 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 156.04 E-value: 2.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLADPTKDliDNSCIRINN-EKGTLPKRLVG-VVW--QEDLLLP 76
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIG--VEGVITYDGiTPEEIKKHYRGdVVYnaETDVHFP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 77 NLTVHETVRFAARLKTPKEQTDG-----EVEVLVEETLSQLGLTHVQHSLIGGGAgKRGISGGERKRVAVAVELVARPSV 151
Cdd:TIGR00956 152 HLTVGETLDFAARCKTPQNRPDGvsreeYAKHIADVYMATYGLSHTRNTKVGNDF-VRGVSGGERKRVSIAEASLGGAKI 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 152 LLLDEPTSGLDSSTAFKLMLTLKELASLGHAIAVV-IHQPRTSIFNLFDNLLLLQKGNVVYEGKASEVKRYLEACPLctK 230
Cdd:TIGR00956 231 QCWDNATRGLDSATALEFIRALKTSANILDTTPLVaIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAKQYFEKMGF--K 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 231 LPPETGLADWLMDMIDEDE---KRDGGGKLP-------ALWKNHSSKQPQANDATNSADQQLQSTGFNTTPRRMLDKRls 300
Cdd:TIGR00956 309 CPDRQTTADFLTSLTSPAErqiKPGYEKKVPrtpqefeTYWRNSPEYAQLMKEIDEYLDRCSESDTKEAYRESHVAKQ-- 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 301 SLAELKSEPkFQTGFVTQLRLLAKRASKQQRGERITRVATLLTACWIAF-TALAWGRIPDTSIYVFNRASLLFFMII--A 377
Cdd:TIGR00956 387 SKRTRPSSP-YTVSFSMQVKYCLARNFLRMKGNPSFTLFMVFGNIIMALiLSSVFYNLPKNTSDFYSRGGALFFAILfnA 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 378 QSNGVVVSSMMafsSERRLLSRERAKKLYGVLPYFIAKTLSDMVNSVALPLLYGCVVYWLCNFRATAVAFFTFALtyYLT 457
Cdd:TIGR00956 466 FSSLLEIASMY---EARPIVEKHRKYALYHPSADAIASIISEIPFKIIESVVFNIILYFMVNFRRTAGRFFFYLL--ILF 540
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 224007385 458 IAAAQSTGLFLSIA--IPNFAVALLLAPLLTVCLMILGGFYI 497
Cdd:TIGR00956 541 ICTLAMSHLFRSIGavTKTLSEAMTPAAILLLALSIYTGFAI 582
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1-459 |
8.53e-40 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 154.11 E-value: 8.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLadpTKDLIDNScIRINN--EKGTLPKRLVGVVWQEDLLLPNL 78
Cdd:TIGR00956 776 RVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERV---TTGVITGG-DRLVNgrPLDSSFQRSIGYVQQQDLHLPTS 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 79 TVHETVRFAARLKTPKEQTDGEVEVLVEETLSQLGLTHVQHSLIGGgAGKrGISGGERKRVAVAVELVARPSVLL-LDEP 157
Cdd:TIGR00956 852 TVRESLRFSAYLRQPKSVSKSEKMEYVEEVIKLLEMESYADAVVGV-PGE-GLNVEQRKRLTIGVELVAKPKLLLfLDEP 929
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 158 TSGLDSSTAFKLMLTLKELASLGHAIAVVIHQPRTSIFNLFDNLLLLQKG-NVVYEGKASE----VKRYLE--ACPLCtk 230
Cdd:TIGR00956 930 TSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAILFEEFDRLLLLQKGgQTVYFGDLGEnshtIINYFEkhGAPKC-- 1007
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 231 lPPETGLADWLMDMI----------DEDEKrdgggklpalWKNHSSKQpqandATNSADQQLqstgfNTTPrrmldkrls 300
Cdd:TIGR00956 1008 -PEDANPAEWMLEVIgaapgahanqDYHEV----------WRNSSEYQ-----AVKNELDRL-----EAEL--------- 1057
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 301 SLAELKSEP----KFQTGFVTQLRLLAKRASKQ---QRGERITRVA-TLLTACWIAFTALAWGripdTSIYVFNRASLLF 372
Cdd:TIGR00956 1058 SKAEDDNDPdalsKYAASLWYQFKLVLWRTFQQywrTPDYLYSKFFlTIFAALFIGFTFFKVG----TSLQGLQNQMFAV 1133
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 373 FMIIAQSNGVVVSSMMAFSSERRLLS-RERAKKLYGVLPYFIAKTLSDMVNSVALPLLYGCVVYWLCNFRATAVAFFT-- 449
Cdd:TIGR00956 1134 FMATVLFNPLIQQYLPPFVAQRDLYEvRERPSRTFSWLAFIAAQITVEIPYNLVAGTIFFFIWYYPVGFYWNASKTGQvh 1213
|
490
....*....|..
gi 224007385 450 --FALTYYLTIA 459
Cdd:TIGR00956 1214 erGVLFWLLSTM 1225
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1-213 |
1.14e-37 |
|
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: 136.60 E-value: 1.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGllaDPTKDLIDNScIRINNEKGTLP-KRLVGVVWQEDLLLPNLT 79
Cdd:cd03232 20 RQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG---RKTAGVITGE-ILINGRPLDKNfQRSTGYVEQQDVHSPNLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 80 VHETVRFAARLktpkeqtdgevevlveetlsqlglthvqhsligggagkRGISGGERKRVAVAVELVARPSVLLLDEPTS 159
Cdd:cd03232 96 VREALRFSALL--------------------------------------RGLSVEQRKRLTIGVELAAKPSILFLDEPTS 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 224007385 160 GLDSSTAFKLMLTLKELASLGHAIAVVIHQPRTSIFNLFDNLLLLQK-GNVVYEG 213
Cdd:cd03232 138 GLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRgGKTVYFG 192
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
3-450 |
7.10e-34 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 136.51 E-value: 7.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGllaDPTKDLIDNScIRINNekgtLPK------RLVGVVWQEDLLLP 76
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG---RKTGGYIEGD-IRISG----FPKkqetfaRISGYCEQNDIHSP 966
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 77 NLTVHETVRFAARLKTPKEQTDGEVEVLVEETLSQLGLTHVQHSLIGGgAGKRGISGGERKRVAVAVELVARPSVLLLDE 156
Cdd:PLN03140 967 QVTVRESLIYSAFLRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGL-PGVTGLSTEQRKRLTIAVELVANPSIIFMDE 1045
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 157 PTSGLDSSTAFKLMLTLKELASLGHAIAVVIHQPRTSIFNLFDNLLLLQK-GNVVYEG----KASEVKRYLEACPLCTKL 231
Cdd:PLN03140 1046 PTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKRgGQVIYSGplgrNSHKIIEYFEAIPGVPKI 1125
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 232 PPETGLADWLMDMidedekrdgggklpalwknhSSKQPQANDATNSADQQLQSTGFNTTprRMLDKRLSSLAELKSEPKF 311
Cdd:PLN03140 1126 KEKYNPATWMLEV--------------------SSLAAEVKLGIDFAEHYKSSSLYQRN--KALVKELSTPPPGASDLYF 1183
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 312 QTGFVTQL-----RLLAKRASKQQRGERITRVATLLT-ACWIAFTALAW------GRIPDTSIYVFNRASLLFFMIIaqS 379
Cdd:PLN03140 1184 ATQYSQSTwgqfkSCLWKQWWTYWRSPDYNLVRFFFTlAAALMVGTIFWkvgtkrSNANDLTMVIGAMYAAVLFVGI--N 1261
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224007385 380 NGVVVSSMMAFssERRLLSRERAKKLYGVLPYFIAKTLSDMVNSVALPLLYGCVVYWLCNFRATAVAFFTF 450
Cdd:PLN03140 1262 NCSTVQPMVAV--ERTVFYRERAAGMYSALPYAIAQVVCEIPYVLIQTTYYTLIVYAMVAFEWTAAKFFWF 1330
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
3-191 |
2.54e-33 |
|
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: 125.68 E-value: 2.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLaDPTKD--LIDNSCIRINNEKGTLPKRL--VGVVWQEDLLLPNL 78
Cdd:cd03255 19 ALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLD-RPTSGevRVDGTDISKLSEKELAAFRRrhIGFVFQSFNLLPDL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 79 TVHETVRFAARLKTPKeqtDGEVEVLVEETLSQLGLTHVQHSLIGGgagkrgISGGERKRVAVAVELVARPSVLLLDEPT 158
Cdd:cd03255 98 TALENVELPLLLAGVP---KKERRERAEELLERVGLGDRLNHYPSE------LSGGQQQRVAIARALANDPKIILADEPT 168
|
170 180 190
....*....|....*....|....*....|....
gi 224007385 159 SGLDSSTAFKLMLTLKELASL-GHAIAVVIHQPR 191
Cdd:cd03255 169 GNLDSETGKEVMELLRELNKEaGTTIVVVTHDPE 202
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-223 |
2.62e-32 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 123.25 E-value: 2.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLAdPT--------KDLIDNScirinnekgTLPKRLVGVVWQEDLL 74
Cdd:COG1131 15 ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLR-PTsgevrvlgEDVARDP---------AEVRRRIGYVPQEPAL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 75 LPNLTVHETVRFAARLK-TPKEqtdgEVEVLVEETLSQLGLTHVQHSLIgggagkRGISGGERKRVAVAVELVARPSVLL 153
Cdd:COG1131 85 YPDLTVRENLRFFARLYgLPRK----EARERIDELLELFGLTDAADRKV------GTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 154 LDEPTSGLDSSTAFKLMLTLKELASLGHAI----------------AVVIHqprtsifnlfdnllllqKGNVVYEGKASE 217
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELAAEGKTVllsthyleeaerlcdrVAIID-----------------KGRIVADGTPDE 217
|
....*..
gi 224007385 218 VK-RYLE 223
Cdd:COG1131 218 LKaRLLE 224
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1-189 |
1.42e-31 |
|
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: 120.65 E-value: 1.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLAdPTKD--LIDNSCIRINNEKGTLpkRLVGVVWQ--EDLLLp 76
Cdd:cd03225 14 RPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLG-PTSGevLVDGKDLTKLSLKELR--RKVGLVFQnpDDQFF- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 77 NLTVHETVRFAAR-LKTPKEqtdgEVEVLVEETLSQLGLTHVQ----HSLigggagkrgiSGGERKRVAVAVELVARPSV 151
Cdd:cd03225 90 GPTVEEEVAFGLEnLGLPEE----EIEERVEEALELVGLEGLRdrspFTL----------SGGQKQRVAIAGVLAMDPDI 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 224007385 152 LLLDEPTSGLDSSTAFKLMLTLKELASLGHAIAVVIHQ 189
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHD 193
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
4-178 |
3.68e-31 |
|
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: 119.71 E-value: 3.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKIS---PYQLTAWMGPSGSGKTSLVSVAAGLLAdPTKDLID-------NSCIRINnekgtLP--KRLVGVVWQE 71
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEK-PDGGTIVlngtvlfDSRKKIN-----LPpqQRKIGLVFQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 72 DLLLPNLTVHETVRFAARLKTPKEQTDgevevLVEETLSQLGLTHVQhsliggGAGKRGISGGERKRVAVAVELVARPSV 151
Cdd:cd03297 84 YALFPHLNVRENLAFGLKRKRNREDRI-----SVDELLDLLGLDHLL------NRYPAQLSGGEKQRVALARALAAQPEL 152
|
170 180
....*....|....*....|....*..
gi 224007385 152 LLLDEPTSGLDSSTAFKLMLTLKELAS 178
Cdd:cd03297 153 LLLDEPFSALDRALRLQLLPELKQIKK 179
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
4-159 |
2.68e-30 |
|
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: 115.05 E-value: 2.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLaDPTKDLIDNSCIRINNEKGTLPKRLVGVVWQEDLLLPNLTVHET 83
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLL-SPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224007385 84 VRFAARLKTPKEQTDGEVevlVEETLSQLGLTHVQHSLIGGGAGkrGISGGERKRVAVAVELVARPSVLLLDEPTS 159
Cdd:pfam00005 80 LRLGLLLKGLSKREKDAR---AEEALEKLGLGDLADRPVGERPG--TLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-191 |
2.73e-30 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 117.45 E-value: 2.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLAdPT--------KDLIDNSciriNNEKGTLPKRLVGVVWQEDLL 74
Cdd:COG1136 23 ALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDR-PTsgevlidgQDISSLS----ERELARLRRRHIGFVFQFFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 75 LPNLTVHETVRFAARL-KTPKEqtdgEVEVLVEETLSQLGLTHVQHSLIGGgagkrgISGGERKRVAVAVELVARPSVLL 153
Cdd:COG1136 98 LPELTALENVALPLLLaGVSRK----ERRERARELLERVGLGDRLDHRPSQ------LSGGQQQRVAIARALVNRPKLIL 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 224007385 154 LDEPTSGLDSSTAFKLMLTLKELA-SLGHAIAVVIHQPR 191
Cdd:COG1136 168 ADEPTGNLDSKTGEEVLELLRELNrELGTTIVMVTHDPE 206
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1-189 |
1.81e-28 |
|
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: 112.98 E-value: 1.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLAdPTKD--LIDNSCIRINNEKGTLPKRL-VGVVWQEDLLLPN 77
Cdd:cd03261 13 RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLR-PDSGevLIDGEDISGLSEAELYRLRRrMGMLFQSGALFDS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 78 LTVHETVRFAARLKTpkEQTDGEVEVLVEETLSQLGLTHVQHSLIGGgagkrgISGGERKRVAVAVELVARPSVLLLDEP 157
Cdd:cd03261 92 LTVFENVAFPLREHT--RLSEEEIREIVLEKLEAVGLRGAEDLYPAE------LSGGMKKRVALARALALDPELLLYDEP 163
|
170 180 190
....*....|....*....|....*....|....*
gi 224007385 158 TSGLD--SSTAF-KLMLTLKElaSLGHAIAVVIHQ 189
Cdd:cd03261 164 TAGLDpiASGVIdDLIRSLKK--ELGLTSIMVTHD 196
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-187 |
4.75e-28 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 111.30 E-value: 4.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISP---YQLTawmGPSGSGKTSLVSVAAGLLaDPTKDLIdnsciRINNEK-GTLPK-------RLVGVVWQE 71
Cdd:COG2884 17 ALSDVSLEIEKgefVFLT---GPSGAGKSTLLKLLYGEE-RPTSGQV-----LVNGQDlSRLKRreipylrRRIGVVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 72 DLLLPNLTVHETVRFAARL--KTPKEqtdgeVEVLVEETLSQLGLTHVQHSLIgggagkRGISGGERKRVAVAVELVARP 149
Cdd:COG2884 88 FRLLPDRTVYENVALPLRVtgKSRKE-----IRRRVREVLDLVGLSDKAKALP------HELSGGEQQRVAIARALVNRP 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 224007385 150 SVLLLDEPTSGLDSSTAFKLMLTLKELASLGhaIAVVI 187
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEINRRG--TTVLI 192
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
3-176 |
1.01e-27 |
|
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: 110.25 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLaDPTKDLIdnsciRINNEKGTLPKRLVGVVWQEDLLLPNLTVHE 82
Cdd:cd03293 19 ALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLE-RPTSGEV-----LVDGEPVTGPGPDRGYVFQQDALLPWLTVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 83 TVRFAARLKtpkEQTDGEVEVLVEETLSQLGLTHVQHSLIgggagkRGISGGERKRVAVAVELVARPSVLLLDEPTSGLD 162
Cdd:cd03293 93 NVALGLELQ---GVPKAEARERAEELLELVGLSGFENAYP------HQLSGGMRQRVALARALAVDPDVLLLDEPFSALD 163
|
170
....*....|....
gi 224007385 163 SSTAFKLMLTLKEL 176
Cdd:cd03293 164 ALTREQLQEELLDI 177
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1-189 |
1.30e-27 |
|
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: 110.11 E-value: 1.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLAdPTKD--LIDNSCIRINNEKgTLPKRlVGVVWQ--EDLLLp 76
Cdd:COG1122 14 TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLK-PTSGevLVDGKDITKKNLR-ELRRK-VGLVFQnpDDQLF- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 77 NLTVHETVRFAAR-LKTPKEqtdgEVEVLVEETLSQLGLTHVQ----HSLigggagkrgiSGGERKRVAVAVELVARPSV 151
Cdd:COG1122 90 APTVEEDVAFGPEnLGLPRE----EIRERVEEALELVGLEHLAdrppHEL----------SGGQKQRVAIAGVLAMEPEV 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 224007385 152 LLLDEPTSGLDSSTAFKLMLTLKELASLGHAIAVVIHQ 189
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHD 193
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
3-170 |
2.01e-27 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 110.56 E-value: 2.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLaDPTKdlidnSCIRINNEKGTLPKRLVGVVWQEDLLLPNLTVHE 82
Cdd:COG1116 26 ALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLE-KPTS-----GEVLVDGKPVTGPGPDRGVVFQEPALLPWLTVLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 83 TVRFAARLK-TPKEqtdgEVEVLVEETLSQLGLTHVQHSLIgggagkRGISGGERKRVAVAVELVARPSVLLLDEPTSGL 161
Cdd:COG1116 100 NVALGLELRgVPKA----ERRERARELLELVGLAGFEDAYP------HQLSGGMRQRVAIARALANDPEVLLMDEPFGAL 169
|
....*....
gi 224007385 162 DSSTAFKLM 170
Cdd:COG1116 170 DALTRERLQ 178
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
322-497 |
2.31e-27 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 108.90 E-value: 2.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 322 LAKRASKQQRGERITRVATLLTAC-WIAFTALAWGRIPDTSIyVFNRASLLFFMIIAQSNGVVVSSMMAFSSERRLLSRE 400
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPIlMALIFGTLFGNLGNQQG-GLNRPGLLFFSILFNAFSALSGISPVFEKERGVLYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 401 RAKKLYGVLPYFIAKTLSDMVNSVALPLLYGCVVYWLCNFRATAVAFFTFALTYYLTIAAAQSTGLFLSIAIPNFAVALL 480
Cdd:pfam01061 80 LASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDASQ 159
|
170
....*....|....*..
gi 224007385 481 LAPLLTVCLMILGGFYI 497
Cdd:pfam01061 160 LGPLVLLPLLLLSGFFI 176
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-188 |
5.76e-27 |
|
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: 107.88 E-value: 5.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLlADPTKDLIDNSCIRINNEKGT-LPK--RLVGVVWQEDLLLPNLTV 80
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKE-ELPTSGTIRVNGQDVSDLRGRaIPYlrRKIGVVFQDFRLLPDRNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 81 HETVRFAARLKTPKEQtdgEVEVLVEETLSQLGLTHVQHSLigggagKRGISGGERKRVAVAVELVARPSVLLLDEPTSG 160
Cdd:cd03292 96 YENVAFALEVTGVPPR---EIRKRVPAALELVGLSHKHRAL------PAELSGGEQQRVAIARAIVNSPTILIADEPTGN 166
|
170 180
....*....|....*....|....*...
gi 224007385 161 LDSSTAFKLMLTLKELASLGHAIAVVIH 188
Cdd:cd03292 167 LDPDTTWEIMNLLKKINKAGTTVVVATH 194
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-188 |
1.20e-26 |
|
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: 108.21 E-value: 1.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLAdptkdlIDNSCIRINNEK-GTLPK----RLVGVVWQEDLLL 75
Cdd:COG1120 14 RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLK------PSSGEVLLDGRDlASLSRrelaRRIAYVPQEPPAP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 76 PNLTVHETV---RFAARlkTPKEQTDGEVEVLVEETLSQLGLTHVQHSLIGGgagkrgISGGERKRVAVAVELVARPSVL 152
Cdd:COG1120 88 FGLTVRELValgRYPHL--GLFGRPSAEDREAVEEALERTGLEHLADRPVDE------LSGGERQRVLIARALAQEPPLL 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 224007385 153 LLDEPTSGLDSSTAFKLMLTLKELA-SLGHAIAVVIH 188
Cdd:COG1120 160 LLDEPTSHLDLAHQLEVLELLRRLArERGRTVVMVLH 196
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
3-190 |
1.97e-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: 106.45 E-value: 1.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLADPTKDlidnscIRINNEKGT-LP--KRLVGVVWQEDLLLPNLT 79
Cdd:cd03259 15 ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGE------ILIDGRDVTgVPpeRRNIGMVFQDYALFPHLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 80 VHETVRFAARLKTPKEQtdgEVEVLVEETLSQLGLTHVQHSLIgggagkRGISGGERKRVAVAVELVARPSVLLLDEPTS 159
Cdd:cd03259 89 VAENIAFGLKLRGVPKA---EIRARVRELLELVGLEGLLNRYP------HELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190
....*....|....*....|....*....|..
gi 224007385 160 GLDSSTAFKLMLTLKEL-ASLGHAIAVVIHQP 190
Cdd:cd03259 160 ALDAKLREELREELKELqRELGITTIYVTHDQ 191
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-251 |
5.96e-26 |
|
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: 106.10 E-value: 5.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLadptkdLIDNSCIRINNE----KGTLPKRLVGVVWQEDLLLPNL 78
Cdd:COG4555 16 ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLL------KPDSGSILIDGEdvrkEPREARRQIGVLPDERGLYDRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 79 TVHETVRFAARLKtpkEQTDGEVEVLVEETLSQLGLTHVQHSLIGGgagkrgISGGERKRVAVAVELVARPSVLLLDEPT 158
Cdd:COG4555 90 TVRENIRYFAELY---GLFDEELKKRIEELIELLGLEEFLDRRVGE------LSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 159 SGLD--SSTAFKLMltLKELASLGHAIAVVIHQPRTsIFNLFDNLLLLQKGNVVYEGKASEVKRYLEacplctklppETG 236
Cdd:COG4555 161 NGLDvmARRLLREI--LRALKKEGKTVLFSSHIMQE-VEALCDRVVILHKGKVVAQGSLDELREEIG----------EEN 227
|
250
....*....|....*
gi 224007385 237 LADWLMDMIDEDEKR 251
Cdd:COG4555 228 LEDAFVALIGSEEGE 242
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1-213 |
6.19e-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: 6.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLadPTKDLIDNScIRINN----EKGTLPKRLVGVVWQEDLLLP 76
Cdd:cd03233 20 IPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRT--EGNVSVEGD-IHYNGipykEFAEKYPGEIIYVSEEDVHFP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 77 NLTVHETVRFAARLKtpkeqtdgevevlveetlsqlglthvqhsligGGAGKRGISGGERKRVAVAVELVARPSVLLLDE 156
Cdd:cd03233 97 TLTVRETLDFALRCK--------------------------------GNEFVRGISGGERKRVSIAEALVSRASVLCWDN 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 224007385 157 PTSGLDSSTAFKLMLTLKELA-SLGHAIAVVIHQPRTSIFNLFDNLLLLQKGNVVYEG 213
Cdd:cd03233 145 STRGLDSSTALEILKCIRTMAdVLKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-188 |
9.31e-26 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 105.56 E-value: 9.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLAdPTKdlidnSCIRINNEKGTLPKRLVGVVWQE---DLLLPn 77
Cdd:COG1121 19 RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLP-PTS-----GTVRLFGKPPRRARRRIGYVPQRaevDWDFP- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 78 LTVHETV---RFAAR--LKTPKeQTDGEvevLVEETLSQLGLTHVQHSLIGGgagkrgISGGERKRVAVAVELVARPSVL 152
Cdd:COG1121 92 ITVRDVVlmgRYGRRglFRRPS-RADRE---AVDEALERVGLEDLADRPIGE------LSGGQQQRVLLARALAQDPDLL 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 224007385 153 LLDEPTSGLDSSTAFKLMLTLKELASLGHAIAVVIH 188
Cdd:COG1121 162 LLDEPFAGVDAATEEALYELLRELRREGKTILVVTH 197
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-162 |
1.21e-25 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 104.10 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLADPTkdlidnSC---IRINNEK-GTLP--KRLVGVVWQEDLL 74
Cdd:COG4136 14 RPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAF------SAsgeVLLNGRRlTALPaeQRRIGILFQDDLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 75 LPNLTVHETVRFAARLKTPKEQTDgeveVLVEETLSQLGLTHVQHSLIGGgagkrgISGGERKRVAVAVELVARPSVLLL 154
Cdd:COG4136 88 FPHLSVGENLAFALPPTIGRAQRR----ARVEQALEEAGLAGFADRDPAT------LSGGQRARVALLRALLAEPRALLL 157
|
....*...
gi 224007385 155 DEPTSGLD 162
Cdd:COG4136 158 DEPFSKLD 165
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-188 |
1.83e-25 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 104.34 E-value: 1.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLAdPtkdliDNSCIRINNEKGT-LP--KRLVGVVWQEDLLLPNLTV 80
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIK-P-----DSGKILLNGKDITnLPpeKRDISYVPQNYALFPHMTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 81 HETVRFAARLKTPKEQtdgEVEVLVEETLSQLGLTHVQHSligggaGKRGISGGERKRVAVAVELVARPSVLLLDEPTSG 160
Cdd:cd03299 89 YKNIAYGLKKRKVDKK---EIERKVLEIAEMLGIDHLLNR------KPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 224007385 161 LDSSTAFKLMLTLK------------------ELASLGHAIAVVIH 188
Cdd:cd03299 160 LDVRTKEKLREELKkirkefgvtvlhvthdfeEAWALADKVAIMLN 205
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1-188 |
2.34e-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: 103.38 E-value: 2.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLaDPTKdlidnSCIRINNEKGTLPKRLVGVVWQEDLLLPN--L 78
Cdd:cd03235 12 HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLL-KPTS-----GSIRVFGKPLEKERKRIGYVPQRRSIDRDfpI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 79 TVHETV--------RFAARLKTPKEQtdgevevLVEETLSQLGLTHVQHSLIGGgagkrgISGGERKRVAVAVELVARPS 150
Cdd:cd03235 86 SVRDVVlmglyghkGLFRRLSKADKA-------KVDEALERVGLSELADRQIGE------LSGGQQQRVLLARALVQDPD 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 224007385 151 VLLLDEPTSGLDSSTAFKLMLTLKELASLGHAIAVVIH 188
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTH 190
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
3-163 |
4.26e-25 |
|
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: 102.97 E-value: 4.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLaDPTKD--LIDNSCIRINNEKgtlPKRLVGVVWQEDLLLPNLTV 80
Cdd:cd03263 17 AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGEL-RPTSGtaYINGYSIRTDRKA---ARQSLGYCPQFDALFDELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 81 HETVRFAARLKTPKEQtdgEVEVLVEETLSQLGLTHVQHSLIgggagkRGISGGERKRVAVAVELVARPSVLLLDEPTSG 160
Cdd:cd03263 93 REHLRFYARLKGLPKS---EIKEEVELLLRVLGLTDKANKRA------RTLSGGMKRKLSLAIALIGGPSVLLLDEPTSG 163
|
...
gi 224007385 161 LDS 163
Cdd:cd03263 164 LDP 166
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
3-176 |
4.54e-24 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 103.25 E-value: 4.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLaDPTK-DlidnscIRINNEKGT-LP--KRLVGVVWQEDLLLPNL 78
Cdd:COG3842 20 ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFE-TPDSgR------ILLDGRDVTgLPpeKRNVGMVFQDYALFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 79 TVHETVRFAARL-KTPKEqtdgEVEVLVEETLSQLGLTHVQHSLIgggagkRGISGGERKRVAVAVELVARPSVLLLDEP 157
Cdd:COG3842 93 TVAENVAFGLRMrGVPKA----EIRARVAELLELVGLEGLADRYP------HQLSGGQQQRVALARALAPEPRVLLLDEP 162
|
170
....*....|....*....
gi 224007385 158 TSGLDSSTAFKLMLTLKEL 176
Cdd:COG3842 163 LSALDAKLREEMREELRRL 181
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-188 |
7.13e-24 |
|
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: 100.05 E-value: 7.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLAdPTKD--LIDNSCIRINNEKGTLPKRL-VGVVWQEDLLLPN 77
Cdd:COG1127 18 RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLR-PDSGeiLVDGQDITGLSEKELYELRRrIGMLFQGGALFDS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 78 LTVHETVRFAARLKTpkEQTDGEVEVLVEETLSQLGLTHVQHSLIGGgagkrgISGGERKRVAVAVELVARPSVLLLDEP 157
Cdd:COG1127 97 LTVFENVAFPLREHT--DLSEAEIRELVLEKLELVGLPGAADKMPSE------LSGGMRKRVALARALALDPEILLYDEP 168
|
170 180 190
....*....|....*....|....*....|....
gi 224007385 158 TSGLD--SSTAF-KLMLTLKElaSLGHAIAVVIH 188
Cdd:COG1127 169 TAGLDpiTSAVIdELIRELRD--ELGLTSVVVTH 200
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1-188 |
9.44e-24 |
|
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: 99.18 E-value: 9.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGL--LADPTKD----LIDNSCIRINNEKGTLPKRLVGVVWQEDLL 74
Cdd:cd03260 13 KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndLIPGAPDegevLLDGKDIYDLDVDVLELRRRVGMVFQKPNP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 75 LPnLTVHETVRFAARLKTpkEQTDGEVEVLVEETLSQLGLthvqHSLIGGGAGKRGISGGERKRVAVAVELVARPSVLLL 154
Cdd:cd03260 93 FP-GSIYDNVAYGLRLHG--IKLKEELDERVEEALRKAAL----WDEVKDRLHALGLSGGQQQRLCLARALANEPEVLLL 165
|
170 180 190
....*....|....*....|....*....|....
gi 224007385 155 DEPTSGLDSSTAFKLMLTLKELASlGHAIAVVIH 188
Cdd:cd03260 166 DEPTSALDPISTAKIEELIAELKK-EYTIVIVTH 198
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-165 |
1.02e-23 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 100.32 E-value: 1.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLAdPTKdlidnSCIRINNEKGTLPKRLVGVVWQEDLLLPNLTVHE 82
Cdd:COG4525 22 ALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLA-PSS-----GEITLDGVPVTGPGADRGVVFQKDALLPWLNVLD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 83 TVRFAARLK-TPKEqtdgEVEVLVEETLSQLGLthvqhsligGGAGKRGI---SGGERKRVAVAVELVARPSVLLLDEPT 158
Cdd:COG4525 96 NVAFGLRLRgVPKA----ERRARAEELLALVGL---------ADFARRRIwqlSGGMRQRVGIARALAADPRFLLMDEPF 162
|
....*..
gi 224007385 159 SGLDSST 165
Cdd:COG4525 163 GALDALT 169
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-188 |
1.07e-23 |
|
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: 99.43 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLAdPTKdlidnSCIRINNEKGT-LP-----KRLVGVVWQEDLLLPN 77
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLR-PTS-----GSVLFDGEDITgLPpheiaRLGIGRTFQIPRLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 78 LTVHETVRFAARLKTPK-------EQTDGEVEVLVEETLSQLGLTHVQHSLIGGgagkrgISGGERKRVAVAVELVARPS 150
Cdd:cd03219 90 LTVLENVMVAAQARTGSglllaraRREEREARERAEELLERVGLADLADRPAGE------LSYGQQRRLEIARALATDPK 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 224007385 151 VLLLDEPTSGLDSSTAFKLMLTLKELASLGHAIAVVIH 188
Cdd:cd03219 164 LLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEH 201
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
3-188 |
1.61e-23 |
|
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: 98.85 E-value: 1.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLlADPTKDLIDNSCIRINNekgtLP--KRLVGVVWQEDLLLPNLTV 80
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGF-ETPTSGEILLDGKDITN----LPphKRPVNTVFQNYALFPHLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 81 HETVRFAARLKTPKEQtdgEVEVLVEETLSQLGLTHVQHSLIgggagkRGISGGERKRVAVAVELVARPSVLLLDEPTSG 160
Cdd:cd03300 90 FENIAFGLRLKKLPKA---EIKERVAEALDLVQLEGYANRKP------SQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180
....*....|....*....|....*....
gi 224007385 161 LDSSTAFKLMLTLKEL-ASLGHAIAVVIH 188
Cdd:cd03300 161 LDLKLRKDMQLELKRLqKELGITFVFVTH 189
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
6-220 |
1.69e-23 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 101.73 E-value: 1.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 6 DVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLADPTKDL-IDNSCIRINNEKGTLP--KRLVGVVWQEDLLLPNLTVHE 82
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIvLNGRTLFDSRKGIFLPpeKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 83 TVRFAARLKTPKEQTDGEvevlvEETLSQLGLTHvqhsLIGGGAGKrgISGGERKRVAVAVELVARPSVLLLDEPTSGLD 162
Cdd:TIGR02142 95 NLRYGMKRARPSERRISF-----ERVIELLGIGH----LLGRLPGR--LSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 224007385 163 SSTAFKLMLTLKEL-ASLGHAIAVVIHQPrTSIFNLFDNLLLLQKGNVVYEGKASEVKR 220
Cdd:TIGR02142 164 DPRKYEILPYLERLhAEFGIPILYVSHSL-QEVLRLADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
3-189 |
5.04e-23 |
|
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: 96.83 E-value: 5.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLladptkDLIDNSCIRINNEKGTLPKRL-------VGVVWQEDLLL 75
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLL------EEPDSGTIIIDGLKLTDDKKNinelrqkVGMVFQQFNLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 76 PNLTVHETVRFAAR--LKTPKEqtdgEVEVLVEETLSQLGLTHVQHSLIGGgagkrgISGGERKRVAVAVELVARPSVLL 153
Cdd:cd03262 89 PHLTVLENITLAPIkvKGMSKA----EAEERALELLEKVGLADKADAYPAQ------LSGGQQQRVAIARALAMNPKVML 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 224007385 154 LDEPTSGLDSSTAFKLMLTLKELASLGHAIAVVIHQ 189
Cdd:cd03262 159 FDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHE 194
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3-162 |
6.36e-23 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 96.49 E-value: 6.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPyQLTAWMGPSGSGKTSLVSVAAGLLAdPTKDLIdnsciRINNEKGTLPK----RLVGVVWQEDLLLPNL 78
Cdd:cd03264 15 ALDGVSLTLGP-GMYGLLGPNGAGKTTLMRILATLTP-PSSGTI-----RIDGQDVLKQPqklrRRIGYLPQEFGVYPNF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 79 TVHETVRFAARLKtpkEQTDGEVEVLVEETLSQLGLTHVQHSLIGGgagkrgISGGERKRVAVAVELVARPSVLLLDEPT 158
Cdd:cd03264 88 TVREFLDYIAWLK---GIPSKEVKARVDEVLELVNLGDRAKKKIGS------LSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
....
gi 224007385 159 SGLD 162
Cdd:cd03264 159 AGLD 162
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1-190 |
1.23e-22 |
|
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: 96.48 E-value: 1.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLaDPTKDLIDNSCIRINNEKGTL---PKRLVGVVWQEDLLLPN 77
Cdd:cd03256 14 KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLV-EPTSGSVLIDGTDINKLKGKAlrqLRRQIGMIFQQFNLIER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 78 LTV-----------HETVRFAARLKTPKEQtdgeveVLVEETLSQLGLTHVqhsligggAGKRG--ISGGERKRVAVAVE 144
Cdd:cd03256 93 LSVlenvlsgrlgrRSTWRSLFGLFPKEEK------QRALAALERVGLLDK--------AYQRAdqLSGGQQQRVAIARA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 224007385 145 LVARPSVLLLDEPTSGLDSSTAFKLMLTLKELA-SLGHAIAVVIHQP 190
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRINrEEGITVIVSLHQV 205
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
3-189 |
1.60e-22 |
|
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: 94.56 E-value: 1.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLADPTKD-LIDNSCIRINNEKGTLPKRLVGVVWQEDLLLPNLTVH 81
Cdd:cd03229 15 VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSiLIDGEDLTDLEDELPPLRRRIGMVFQDFALFPHLTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 82 ETVRFaarlktpkeqtdgevevlveetlsqlglthvqhsligggagkrGISGGERKRVAVAVELVARPSVLLLDEPTSGL 161
Cdd:cd03229 95 ENIAL-------------------------------------------GLSGGQQQRVALARALAMDPDVLLLDEPTSAL 131
|
170 180
....*....|....*....|....*....
gi 224007385 162 DSSTAFKLMLTLKEL-ASLGHAIAVVIHQ 189
Cdd:cd03229 132 DPITRREVRALLKSLqAQLGITVVLVTHD 160
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
6-162 |
1.99e-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: 98.25 E-value: 1.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 6 DVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLAdptkdlIDNSCIRINNE------KGT-LP--KRLVGVVWQEDLLLP 76
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLER------PDSGRIRLGGEvlqdsaRGIfLPphRRRIGYVFQEARLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 77 NLTVHETVRFAARlKTPKEQTDGEVEVLVEetlsQLGLTHvqhsLIgggagKRGI---SGGERKRVAVAVELVARPSVLL 153
Cdd:COG4148 91 HLSVRGNLLYGRK-RAPRAERRISFDEVVE----LLGIGH----LL-----DRRPatlSGGERQRVAIGRALLSSPRLLL 156
|
....*....
gi 224007385 154 LDEPTSGLD 162
Cdd:COG4148 157 MDEPLAALD 165
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1-192 |
2.35e-22 |
|
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: 93.46 E-value: 2.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLaDPTKDLIDNSCIRINNEKGTLPKRLVGVVWQedlllpnltv 80
Cdd:cd00267 12 RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLL-KPTSGEILIDGKDIAKLPLEELRRRIGYVPQ---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 81 hetvrfaarlktpkeqtdgevevlveetlsqlglthvqhsligggagkrgISGGERKRVAVAVELVARPSVLLLDEPTSG 160
Cdd:cd00267 81 --------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSG 110
|
170 180 190
....*....|....*....|....*....|..
gi 224007385 161 LDSSTAFKLMLTLKELASLGHAIAVVIHQPRT 192
Cdd:cd00267 111 LDPASRERLLELLRELAEEGRTVIIVTHDPEL 142
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-166 |
2.46e-22 |
|
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: 95.58 E-value: 2.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 2 SILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLladptkDLIDNSCIRIN-------NEKG--TLPKRLVGVVWQED 72
Cdd:COG4181 26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGL------DRPTSGTVRLAgqdlfalDEDAraRLRARHVGFVFQSF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 73 LLLPNLTVHETVRfaarlkTPKE-QTDGEVEVLVEETLSQLGLTH-VQHSligggagKRGISGGERKRVAVAVELVARPS 150
Cdd:COG4181 100 QLLPTLTALENVM------LPLElAGRRDARARARALLERVGLGHrLDHY-------PAQLSGGEQQRVALARAFATEPA 166
|
170
....*....|....*.
gi 224007385 151 VLLLDEPTSGLDSSTA 166
Cdd:COG4181 167 ILFADEPTGNLDAATG 182
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-163 |
2.49e-22 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 97.91 E-value: 2.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLaDPtkdliDNSCIRINNE--KGTLP--KRLVGVVWQEDLLLPNLT 79
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLE-TP-----DSGRIVLNGRdlFTNLPprERRVGFVFQHYALFPHMT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 80 VHETVRFAARLKTPKEQtdgEVEVLVEETLSQLGLTHVqhsligggaGKR---GISGGERKRVAVAVELVARPSVLLLDE 156
Cdd:COG1118 92 VAENIAFGLRVRPPSKA---EIRARVEELLELVQLEGL---------ADRypsQLSGGQRQRVALARALAVEPEVLLLDE 159
|
....*..
gi 224007385 157 PTSGLDS 163
Cdd:COG1118 160 PFGALDA 166
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
3-188 |
2.68e-22 |
|
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: 95.01 E-value: 2.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLladptkDLIDNSCIRINNEKGT-LP--KRLVGVVWQEDLLLPNLT 79
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGL------EEPTSGRIYIGGRDVTdLPpkDRDIAMVFQNYALYPHMT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 80 VHETVRFAARL-KTPKEqtdgEVEVLVEETLSQLGLTHVQHSLigggagKRGISGGERKRVAVAVELVARPSVLLLDEPT 158
Cdd:cd03301 89 VYDNIAFGLKLrKVPKD----EIDERVREVAELLQIEHLLDRK------PKQLSGGQRQRVALGRAIVREPKVFLMDEPL 158
|
170 180 190
....*....|....*....|....*....|.
gi 224007385 159 SGLDSSTAFKLMLTLKEL-ASLGHAIAVVIH 188
Cdd:cd03301 159 SNLDAKLRVQMRAELKRLqQRLGTTTIYVTH 189
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1-192 |
4.94e-22 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 99.06 E-value: 4.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLaDPTKdlidnSCIRINnekGTLPKRLVGVVWQEDL------- 73
Cdd:COG4988 350 RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFL-PPYS-----GSILIN---GVDLSDLDPASWRRQIawvpqnp 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 74 LLPNLTVHETVRFAARLKTPKEqtdgevevlVEETLSQLGLTHVQHSLIGG-----GAGKRGISGGERKRVAVAVELVAR 148
Cdd:COG4988 421 YLFAGTIRENLRLGRPDASDEE---------LEAALEAAGLDEFVAALPDGldtplGEGGRGLSGGQAQRLALARALLRD 491
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 224007385 149 PSVLLLDEPTSGLDSSTAFKLMLTLKELASlGHAIAVVIHQPRT 192
Cdd:COG4988 492 APLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLAL 534
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-188 |
9.69e-22 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 93.94 E-value: 9.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLlADPtkdliDNSCIRINNEKGT---LPKRLVGVVWQEDLLLPNLTV 80
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGL-ERP-----DSGTILFGGEDATdvpVQERNVGFVFQHYALFRHMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 81 HETVRFAARLKTPKEQTD-GEVEVLVEETLSQLGLThvqhsliggGAGKR---GISGGERKRVAVAVELVARPSVLLLDE 156
Cdd:cd03296 92 FDNVAFGLRVKPRSERPPeAEIRAKVHELLKLVQLD---------WLADRypaQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190
....*....|....*....|....*....|...
gi 224007385 157 PTSGLDSSTAFKLMLTLKELA-SLGHAIAVVIH 188
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRLHdELHVTTVFVTH 195
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-176 |
1.11e-21 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 94.10 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLADptkdliDNSCIRINNEKGTLPK-----RLVGVVWQEdlllPN 77
Cdd:COG1124 20 VLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERP------WSGEVTFDGRPVTRRRrkafrRRVQMVFQD----PY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 78 LTVH--ETVRfaARLKTP-KEQTDGEVEVLVEETLSQLGLTH-----VQHSLigggagkrgiSGGERKRVAVAVELVARP 149
Cdd:COG1124 90 ASLHprHTVD--RILAEPlRIHGLPDREERIAELLEQVGLPPsfldrYPHQL----------SGGQRQRVAIARALILEP 157
|
170 180
....*....|....*....|....*..
gi 224007385 150 SVLLLDEPTSGLDSSTAFKLMLTLKEL 176
Cdd:COG1124 158 ELLLLDEPTSALDVSVQAEILNLLKDL 184
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
3-188 |
1.51e-21 |
|
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: 92.10 E-value: 1.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLaDPTKD--LIDNSCIRINNEKGTLPKRLVGVVWQ--EDLLLPNl 78
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLL-RPQSGavLIDGEPLDYSRKGLLERRQRVGLVFQdpDDQLFAA- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 79 TVHETVRFAAR-LKTPKEqtdgEVEVLVEETLSQLGLTHVQHSLIgggagkRGISGGERKRVAVAVELVARPSVLLLDEP 157
Cdd:TIGR01166 85 DVDQDVAFGPLnLGLSEA----EVERRVREALTAVGASGLRERPT------HCLSGGEKKRVAIAGAVAMRPDVLLLDEP 154
|
170 180 190
....*....|....*....|....*....|.
gi 224007385 158 TSGLDSSTAFKLMLTLKELASLGHAIAVVIH 188
Cdd:TIGR01166 155 TAGLDPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
3-191 |
2.21e-21 |
|
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: 92.41 E-value: 2.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLlADPTKDLIDNSCIRIN----NEKGTLPKRLVGVVWQEDLLLPNL 78
Cdd:TIGR02211 20 VLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGL-DNPTSGEVLFNGQSLSklssNERAKLRNKKLGFIYQFHHLLPDF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 79 TVHETVRFAARLKtpkEQTDGEVEVLVEETLSQLGLTH-VQHsligggagKRG-ISGGERKRVAVAVELVARPSVLLLDE 156
Cdd:TIGR02211 99 TALENVAMPLLIG---KKSVKEAKERAYEMLEKVGLEHrINH--------RPSeLSGGERQRVAIARALVNQPSLVLADE 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 224007385 157 PTSGLDSSTA---FKLMLTLKELasLGHAIAVVIHQPR 191
Cdd:TIGR02211 168 PTGNLDNNNAkiiFDLMLELNRE--LNTSFLVVTHDLE 203
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3-183 |
2.32e-21 |
|
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: 90.92 E-value: 2.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLAdPTKD--LIDNSCIRINNEKgtlPKRLVGVVWQEDLLLPNLTV 80
Cdd:cd03230 15 ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLK-PDSGeiKVLGKDIKKEPEE---VKRRIGYLPEEPSLYENLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 81 HETVRFaarlktpkeqtdgevevlveetlsqlglthvqhsligggagkrgiSGGERKRVAVAVELVARPSVLLLDEPTSG 160
Cdd:cd03230 91 RENLKL---------------------------------------------SGGMKQRLALAQALLHDPELLILDEPTSG 125
|
170 180
....*....|....*....|...
gi 224007385 161 LDSSTAFKLMLTLKELASLGHAI 183
Cdd:cd03230 126 LDPESRREFWELLRELKKEGKTI 148
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-188 |
4.72e-21 |
|
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: 96.13 E-value: 4.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLaDPTKD--LIDNSCIRINNEKGTLPKR-LVGVVWQ--EDLLLPN 77
Cdd:COG1123 280 AVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLL-RPTSGsiLFDGKDLTKLSRRSLRELRrRVQMVFQdpYSSLNPR 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 78 LTVHETVRFAARLKtpKEQTDGEVEVLVEETLSQLGL--THVQ---HSLigggagkrgiSGGERKRVAVAVELVARPSVL 152
Cdd:COG1123 359 MTVGDIIAEPLRLH--GLLSRAERRERVAELLERVGLppDLADrypHEL----------SGGQRQRVAIARALALEPKLL 426
|
170 180 190
....*....|....*....|....*....|....*..
gi 224007385 153 LLDEPTSGLDSSTAFKLMLTLKEL-ASLGHAIAVVIH 188
Cdd:COG1123 427 ILDEPTSALDVSVQAQILNLLRDLqRELGLTYLFISH 463
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-165 |
9.65e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 91.68 E-value: 9.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLAdptkdlIDNSCIRINNEKGTLPKRLVGVVWQEDLLLPNLTV 80
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVP------YQHGSITLDGKPVEGPGAERGVVFQNEGLLPWRNV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 81 HETVRFAARLK-TPKEQTdgevEVLVEETLSQLGLThvqhsliggGAGKRGI---SGGERKRVAVAVELVARPSVLLLDE 156
Cdd:PRK11248 88 QDNVAFGLQLAgVEKMQR----LEIAHQMLKKVGLE---------GAEKRYIwqlSGGQRQRVGIARALAANPQLLLLDE 154
|
....*....
gi 224007385 157 PTSGLDSST 165
Cdd:PRK11248 155 PFGALDAFT 163
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1-191 |
1.43e-20 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 94.83 E-value: 1.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLaDPTKdlidnSCIRINN-EKGTLPK----RLVGVVWQEDLLL 75
Cdd:COG4987 348 RPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFL-DPQS-----GSITLGGvDLRDLDEddlrRRIAVVPQRPHLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 76 pNLTVHETVRFAArlktpKEQTDGEVEvlveETLSQLGLTHVQHSLIGG-----GAGKRGISGGERKRVAVAVELVARPS 150
Cdd:COG4987 422 -DTTLRENLRLAR-----PDATDEELW----AALERVGLGDWLAALPDGldtwlGEGGRRLSGGERRRLALARALLRDAP 491
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 224007385 151 VLLLDEPTSGLDSSTAFKLMLTLKELASlGHAIAVVIHQPR 191
Cdd:COG4987 492 ILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRLA 531
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
3-192 |
4.09e-20 |
|
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: 87.44 E-value: 4.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLaDPTKD--LIDNSCIRiNNEKGTLPKRlVGVVWQEDLLLpNLTV 80
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLY-DPTSGeiLIDGVDLR-DLDLESLRKN-IAYVPQDPFLF-SGTI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 81 HETVrfaarlktpkeqtdgevevlveetlsqlglthvqhsligggagkrgISGGERKRVAVAVELVARPSVLLLDEPTSG 160
Cdd:cd03228 93 RENI----------------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSA 126
|
170 180 190
....*....|....*....|....*....|..
gi 224007385 161 LDSSTAFKLMLTLKELASlGHAIAVVIHQPRT 192
Cdd:cd03228 127 LDPETEALILEALRALAK-GKTVIVIAHRLST 157
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-188 |
4.16e-20 |
|
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: 88.58 E-value: 4.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLL-ADPTKDLIDNscIRINNEKGTLPKRLvGVVWQEDLLLPNLTVHE 82
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLePDAGFATVDG--FDVVKEPAEARRRL-GFVSDSTGLYDRLTARE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 83 TVRFAARLKTPKEQtdgEVEVLVEETLSQLGLTHVQHSLIGGgagkrgISGGERKRVAVAVELVARPSVLLLDEPTSGLD 162
Cdd:cd03266 98 NLEYFAGLYGLKGD---ELTARLEELADRLGMEELLDRRVGG------FSTGMRQKVAIARALVHDPPVLLLDEPTTGLD 168
|
170 180
....*....|....*....|....*.
gi 224007385 163 SSTAFKLMLTLKELASLGHAIAVVIH 188
Cdd:cd03266 169 VMATRALREFIRQLRALGKCILFSTH 194
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
4-187 |
4.80e-20 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 89.06 E-value: 4.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLlADPTkdlidNSCIRINNEKGTLPKRLVGVVWQEDLLLPNLTVHET 83
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGL-AQPT-----SGGVILEGKQITEPGPDRMVVFQNYSLLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 84 VRFAARLKTPKEQTdGEVEVLVEETLSQLGLTHVQHSLIGGgagkrgISGGERKRVAVAVELVARPSVLLLDEPTSGLDS 163
Cdd:TIGR01184 75 IALAVDRVLPDLSK-SERRAIVEEHIALVGLTEAADKRPGQ------LSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
|
170 180
....*....|....*....|....
gi 224007385 164 STAFKLMLTLKELASLGHAIAVVI 187
Cdd:TIGR01184 148 LTRGNLQEELMQIWEEHRVTVLMV 171
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-192 |
7.00e-20 |
|
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: 92.97 E-value: 7.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLaDPTK--------DL--IDNSCIRinnekgtlpkRLVGVVWQED 72
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLY-EPTSgrilidgiDLrqIDPASLR----------RQIGVVLQDV 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 73 LLLP-----NLTVH------ETVRFAARLktpkeqtdgeveVLVEETLSQL--GLthvqHSLIG-GGAGkrgISGGERKR 138
Cdd:COG2274 559 FLFSgtireNITLGdpdatdEEIIEAARL------------AGLHDFIEALpmGY----DTVVGeGGSN---LSGGQRQR 619
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 224007385 139 VAVAVELVARPSVLLLDEPTSGLDSSTAFKLMLTLKELasLGHAIAVVI-HQPRT 192
Cdd:COG2274 620 LAIARALLRNPRILILDEATSALDAETEAIILENLRRL--LKGRTVIIIaHRLST 672
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
2-244 |
1.14e-19 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 92.99 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 2 SILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLaDPTKDLIDNSCIRINNEKGTLPKRLVGVVWQEDLLLPNLTVH 81
Cdd:PLN03140 179 TILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKL-DPSLKVSGEITYNGYRLNEFVPRKTSAYISQNDVHVGVMTVK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 82 ETVRFAARLK------------TPKEQTDG---EVEV----------------LVEETLSQLGLTHVQHSLIGGGAgKRG 130
Cdd:PLN03140 258 ETLDFSARCQgvgtrydllselARREKDAGifpEAEVdlfmkatamegvksslITDYTLKILGLDICKDTIVGDEM-IRG 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 131 ISGGERKRVAVAVELVARPSVLLLDEPTSGLDSSTAFKLMLTLKELASLGHA-IAVVIHQPRTSIFNLFDNLLLLQKGNV 209
Cdd:PLN03140 337 ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEAtVLMSLLQPAPETFDLFDDIILLSEGQI 416
|
250 260 270
....*....|....*....|....*....|....*
gi 224007385 210 VYEGKASEVKRYLEACPLctKLPPETGLADWLMDM 244
Cdd:PLN03140 417 VYQGPRDHILEFFESCGF--KCPERKGTADFLQEV 449
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-190 |
1.30e-19 |
|
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: 87.15 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISP---YQLTawmGPSGSGKTSLVSVAAGLLAdPTKDLIDNSCIRINNEKGTLPKRLvGVVWQEDLLLPN 77
Cdd:COG4133 15 RLLFSGLSFTLAAgeaLALT---GPNGSGKTTLLRILAGLLP-PSAGEVLWNGEPIRDAREDYRRRL-AYLGHADGLKPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 78 LTVHETVRFAARLKtpKEQTDGEvevLVEETLSQLGLTHVQHSLIgggagkRGISGGERKRVAVAVELVARPSVLLLDEP 157
Cdd:COG4133 90 LTVRENLRFWAALY--GLRADRE---AIDEALEAVGLAGLADLPV------RQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190
....*....|....*....|....*....|...
gi 224007385 158 TSGLDSSTAFKLMLTLKELASLGHAIAVVIHQP 190
Cdd:COG4133 159 FTALDAAGVALLAELIAAHLARGGAVLLTTHQP 191
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1-190 |
4.87e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 84.98 E-value: 4.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLAdPTKdlidNSCIRInnekgtlPKRLVGVVWQ---EDLLLPn 77
Cdd:NF040873 5 RPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLR-PTS----GTVRRA-------GGARVAYVPQrseVPDSLP- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 78 LTVHETV---RFAARlkTPKEQTDGEVEVLVEETLSQLGLTHVQHSLIGGgagkrgISGGERKRVAVAVELVARPSVLLL 154
Cdd:NF040873 72 LTVRDLVamgRWARR--GLWRRLTRDDRAAVDDALERVGLADLAGRQLGE------LSGGQRQRALLAQGLAQEADLLLL 143
|
170 180 190
....*....|....*....|....*....|....*.
gi 224007385 155 DEPTSGLDSSTAFKLMLTLKELASLGHAIAVVIHQP 190
Cdd:NF040873 144 DEPTTGLDAESRERIIALLAEEHARGATVVVVTHDL 179
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1-190 |
5.68e-19 |
|
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: 84.41 E-value: 5.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLAdPTKdlidnscirinnekgtlpkrlvGVVWQEDLLLPNLTV 80
Cdd:cd03214 12 RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLK-PSS----------------------GEILLDGKDLASLSP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 81 HETVRFAArlktpkeqtdgevevLVEETLSQLGLTHVQHSLIgggagkRGISGGERKRVAVAVELVARPSVLLLDEPTSG 160
Cdd:cd03214 69 KELARKIA---------------YVPQALELLGLAHLADRPF------NELSGGERQRVLLARALAQEPPILLLDEPTSH 127
|
170 180 190
....*....|....*....|....*....|.
gi 224007385 161 LDSSTAFKLMLTLKELA-SLGHAIAVVIHQP 190
Cdd:cd03214 128 LDIAHQIELLELLRRLArERGKTVVMVLHDL 158
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
21-162 |
5.80e-19 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 88.21 E-value: 5.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 21 GPSGSGKTSLVSVAAGLLaDPT--KDLIDNscIRINNekgtLP--KRLVGVVWQEDLLLPNLTVHETVRFAARL-KTPKE 95
Cdd:COG3839 36 GPSGCGKSTLLRMIAGLE-DPTsgEILIGG--RDVTD----LPpkDRNIAMVFQSYALYPHMTVYENIAFPLKLrKVPKA 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 224007385 96 qtdgEVEVLVEETLSQLGLTHVQHSLIgggagkRGISGGERKRVAVAVELVARPSVLLLDEPTSGLD 162
Cdd:COG3839 109 ----EIDRRVREAAELLGLEDLLDRKP------KQLSGGQRQRVALGRALVREPKVFLLDEPLSNLD 165
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-186 |
9.54e-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: 85.25 E-value: 9.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLAdPT--------KDLIDNScirinNEKGTLPKRLVGVVWQEDL- 73
Cdd:cd03257 20 ALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLK-PTsgsiifdgKDLLKLS-----RRLRKIRRKEIQMVFQDPMs 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 74 -LLPNLTVHETVRFAARLKTPKEQTDgEVEVLVEETLSQLGLTHVQ-----HSLigggagkrgiSGGERKRVAVAVELVA 147
Cdd:cd03257 94 sLNPRMTIGEQIAEPLRIHGKLSKKE-ARKEAVLLLLVGVGLPEEVlnrypHEL----------SGGQRQRVAIARALAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 224007385 148 RPSVLLLDEPTSGLDSSTAFKLMLTLKELAS-LG-------HAIAVV 186
Cdd:cd03257 163 NPKLLIADEPTSALDVSVQAQILDLLKKLQEeLGltllfitHDLGVV 209
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-190 |
9.85e-19 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 88.88 E-value: 9.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLlADPTKD--LIDNSCIRINNEKGTLpkRLVGVVWQEDLLLPNlTVH 81
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGF-VDPTEGsiAVNGVPLADADADSWR--DQIAWVPQHPFLFAG-TIA 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 82 ETVRFAARlktpkEQTDGEVEvlveETLSQLGLTHVQHSLIGG-----GAGKRGISGGERKRVAVAVELVARPSVLLLDE 156
Cdd:TIGR02857 414 ENIRLARP-----DASDAEIR----EALERAGLDEFVAALPQGldtpiGEGGAGLSGGQAQRLALARAFLRDAPLLLLDE 484
|
170 180 190
....*....|....*....|....*....|....
gi 224007385 157 PTSGLDSSTAFKLMLTLKELASlGHAIAVVIHQP 190
Cdd:TIGR02857 485 PTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRL 517
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-188 |
1.09e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 85.90 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLaDPTKD--LIDNSCIRINNeKGTLPKR-LVGVVWQ---EDLLLPn 77
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGIL-KPTSGevLIKGEPIKYDK-KSLLEVRkTVGIVFQnpdDQLFAP- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 78 lTVHETVRFAA-RLKTPKEqtdgEVEVLVEETLSQLGLTHVQ----HSLigggagkrgiSGGERKRVAVAVELVARPSVL 152
Cdd:PRK13639 95 -TVEEDVAFGPlNLGLSKE----EVEKRVKEALKAVGMEGFEnkppHHL----------SGGQKKRVAIAGILAMKPEII 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 224007385 153 LLDEPTSGLDSSTAFKLMLTLKELASLGHAIAVVIH 188
Cdd:PRK13639 160 VLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTH 195
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1-189 |
1.28e-18 |
|
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: 84.19 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLADPTKDLIDNSCIRINNEKgtlPKRLVGVVWQEDLLLPNLTV 80
Cdd:cd03268 13 KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIE---ALRRIGALIEAPGFYPNLTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 81 HETVRFAARLKTPKEQTdgevevlVEETLSQLGLTHVQHSLIGGgagkrgISGGERKRVAVAVELVARPSVLLLDEPTSG 160
Cdd:cd03268 90 RENLRLLARLLGIRKKR-------IDEVLDVVGLKDSAKKKVKG------FSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180
....*....|....*....|....*....
gi 224007385 161 LDSSTAFKLMLTLKELASLGHAIAVVIHQ 189
Cdd:cd03268 157 LDPDGIKELRELILSLRDQGITVLISSHL 185
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-189 |
1.31e-18 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 85.19 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSvAAGLLADPTKDLIDNSCIRIN-----NEKGTLPKRL---VGVVWQED 72
Cdd:PRK11264 16 QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLR-CINLLEQPEAGTIRVGDITIDtarslSQQKGLIRQLrqhVGFVFQNF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 73 LLLPNLTVHETVRFAARL--KTPKEqtdgEVEVLVEETLSQLGLTHVQHSLigggagKRGISGGERKRVAVAVELVARPS 150
Cdd:PRK11264 95 NLFPHRTVLENIIEGPVIvkGEPKE----EATARARELLAKVGLAGKETSY------PRRLSGGQQQRVAIARALAMRPE 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 224007385 151 VLLLDEPTSGLDSSTAFKLMLTLKELASLGHAIAVVIHQ 189
Cdd:PRK11264 165 VILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHE 203
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
4-188 |
1.49e-18 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 85.09 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLAdPT--KdlidnscIRINNEK--GTLPKRLV--GVV--WQEDLLL 75
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYR-PTsgR-------ILFDGRDitGLPPHRIArlGIArtFQNPRLF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 76 PNLTVHETVRFAARLKTPK------------EQTDGEVEVLVEETLSQLGLTHVQHSLIGGgagkrgISGGERKRVAVAV 143
Cdd:COG0411 92 PELTVLENVLVAAHARLGRgllaallrlpraRREEREARERAEELLERVGLADRADEPAGN------LSYGQQRRLEIAR 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 224007385 144 ELVARPSVLLLDEPTSGLDSSTAFKLMLTLKEL-ASLGHAIAVVIH 188
Cdd:COG0411 166 ALATEPKLLLLDEPAAGLNPEETEELAELIRRLrDERGITILLIEH 211
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-191 |
1.63e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 84.45 E-value: 1.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 2 SILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLADPTKD--LIDNSCIRINNE-KGTLPKRLVGVVWQEDLLLPNL 78
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEvsLVGQPLHQMDEEaRAKLRAKHVGFVFQSFMLIPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 79 TVHETVRFAARLKTpkeQTDGEVEVLVEETLSQLGLthvqhsligggaGKR------GISGGERKRVAVAVELVARPSVL 152
Cdd:PRK10584 104 NALENVELPALLRG---ESSRQSRNGAKALLEQLGL------------GKRldhlpaQLSGGEQQRVALARAFNGRPDVL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 224007385 153 LLDEPTSGLDSSTAFKLMLTLKEL-ASLGHAIAVVIHQPR 191
Cdd:PRK10584 169 FADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDLQ 208
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-218 |
2.65e-18 |
|
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: 87.65 E-value: 2.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLADPTKD----LIDNSCIRINNEKgtLPKRLVGVVWQE-DLLL 75
Cdd:COG1123 19 VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRIsgevLLDGRDLLELSEA--LRGRRIGMVFQDpMTQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 76 PNLTVHETVRFAARLKtpkEQTDGEVEVLVEETLSQLGLTHVQHSLIGGgagkrgISGGERKRVAVAVELVARPSVLLLD 155
Cdd:COG1123 97 NPVTVGDQIAEALENL---GLSRAEARARVLELLEAVGLERRLDRYPHQ------LSGGQRQRVAIAMALALDPDLLIAD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224007385 156 EPTSGLDSSTAFKLMLTLKEL-ASLGHAIAVVIHQPRTsIFNLFDNLLLLQKGNVVYEGKASEV 218
Cdd:COG1123 168 EPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGV-VAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3-176 |
3.13e-18 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 86.15 E-value: 3.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLladptkDLIDNSCIRINNEKGT-LP--KRLVGVVWQEDLLLPNLT 79
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGF------ETPDSGRIMLDGQDIThVPaeNRHVNTVFQSYALFPHMT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 80 VHETVRFAARL-KTPKEqtdgEVEVLVEETLSQLGLTHVqhsligggAGKR--GISGGERKRVAVAVELVARPSVLLLDE 156
Cdd:PRK09452 103 VFENVAFGLRMqKTPAA----EITPRVMEALRMVQLEEF--------AQRKphQLSGGQQQRVAIARAVVNKPKVLLLDE 170
|
170 180
....*....|....*....|....
gi 224007385 157 PTSGLDsstaFKL---M-LTLKEL 176
Cdd:PRK09452 171 SLSALD----YKLrkqMqNELKAL 190
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1-165 |
4.04e-18 |
|
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: 83.43 E-value: 4.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLaDPTKD--LIDNSCIRINNEKgTLpKRLVGVVWQEDLLLPNl 78
Cdd:cd03254 16 KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFY-DPQKGqiLIDGIDIRDISRK-SL-RSMIGVVLQDTFLFSG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 79 TVHETVRFAaRLKTPKEqtdgevevLVEETLSQLGLTHVQHSLIGG-----GAGKRGISGGERKRVAVAVELVARPSVLL 153
Cdd:cd03254 92 TIMENIRLG-RPNATDE--------EVIEAAKEAGAHDFIMKLPNGydtvlGENGGNLSQGERQLLAIARAMLRDPKILI 162
|
170
....*....|..
gi 224007385 154 LDEPTSGLDSST 165
Cdd:cd03254 163 LDEATSNIDTET 174
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
1-162 |
5.40e-18 |
|
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: 83.09 E-value: 5.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLADptkdliDNSCIRINNEKGT-LP----KRL-VGVVWQEDLL 74
Cdd:TIGR04406 14 RKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRP------DAGKILIDGQDIThLPmherARLgIGYLPQEASI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 75 LPNLTVHETVRfaARLKTPKEQTDGEVEVLVEETLSQLGLTHVQHSLIGGgagkrgISGGERKRVAVAVELVARPSVLLL 154
Cdd:TIGR04406 88 FRKLTVEENIM--AVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMS------LSGGERRRVEIARALATNPKFILL 159
|
....*...
gi 224007385 155 DEPTSGLD 162
Cdd:TIGR04406 160 DEPFAGVD 167
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
3-190 |
5.43e-18 |
|
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: 86.65 E-value: 5.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLADPTKDLIDNScIRINNEKGTLPKRLVGVVWQEdlllPNL---T 79
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDG-VPVSSLDQDEVRRRVSVCAQD----AHLfdtT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 80 VHETVRFAArlktpKEQTDGEVEvlveETLSQLGLTHVQHSLIGG-----GAGKRGISGGERKRVAVAVELVARPSVLLL 154
Cdd:TIGR02868 425 VRENLRLAR-----PDATDEELW----AALERVGLADWLRALPDGldtvlGEGGARLSGGERQRLALARALLADAPILLL 495
|
170 180 190
....*....|....*....|....*....|....*.
gi 224007385 155 DEPTSGLDSSTAFKLMLTLKElASLGHAIAVVIHQP 190
Cdd:TIGR02868 496 DEPTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-218 |
8.78e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 83.36 E-value: 8.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLADPTKDLIDNSCIRINNEKGTLPKR-LVGVVWQE-DLLLPNLTVH 81
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKLReSVGMVFQDpDNQLFSASVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 82 ETVRFAA-RLKTPKEqtdgEVEVLVEETLSQLGLTHVQHSligggaGKRGISGGERKRVAVAVELVARPSVLLLDEPTSG 160
Cdd:PRK13636 102 QDVSFGAvNLKLPED----EVRKRVDNALKRTGIEHLKDK------PTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAG 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 224007385 161 LDSSTAFKLMLTLKELAS-LGHAIAVVIHQPRTsIFNLFDNLLLLQKGNVVYEGKASEV 218
Cdd:PRK13636 172 LDPMGVSEIMKLLVEMQKeLGLTIIIATHDIDI-VPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-191 |
9.89e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 82.79 E-value: 9.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLA--DPT-----------KDLIDNSCIRINNEkgtlpkrlVGV 67
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiyDSKikvdgkvlyfgKDIFQIDAIKLRKE--------VGM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 68 VWQEDLLLPNLTVHETVRFAARLKTPKEQTdgEVEVLVEETLSQLGLTHVQHSLIGGGAGKrgISGGERKRVAVAVELVA 147
Cdd:PRK14246 95 VFQQPNPFPHLSIYDNIAYPLKSHGIKEKR--EIKKIVEECLRKVGLWKEVYDRLNSPASQ--LSGGQQQRLTIARALAL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 224007385 148 RPSVLLLDEPTSGLD---SSTAFKLMLTLKELAslghAIAVVIHQPR 191
Cdd:PRK14246 171 KPKVLLMDEPTSMIDivnSQAIEKLITELKNEI----AIVIVSHNPQ 213
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-189 |
9.92e-18 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 82.45 E-value: 9.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLADPTKDLI-DNSCIRINNEKGTLPKRLVGVVWQEDLLLPNLTVH 81
Cdd:PRK09493 16 VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIvDGLKVNDPKVDERLIRQEAGMVFQQFYLFPHLTAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 82 ETVRFAARlkTPKEQTDGEVEVLVEETLSQLGLTHVQHSLIGGgagkrgISGGERKRVAVAVELVARPSVLLLDEPTSGL 161
Cdd:PRK09493 96 ENVMFGPL--RVRGASKEEAEKQARELLAKVGLAERAHHYPSE------LSGGQQQRVAIARALAVKPKLMLFDEPTSAL 167
|
170 180
....*....|....*....|....*...
gi 224007385 162 DSSTAFKLMLTLKELASLGHAIAVVIHQ 189
Cdd:PRK09493 168 DPELRHEVLKVMQDLAEEGMTMVIVTHE 195
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
3-219 |
1.12e-17 |
|
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: 81.71 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLAdPT--------KDLIDNSCIRINnekgtlpKRLVGVVWQEDLL 74
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLP-PRsgsirfdgRDITGLPPHERA-------RAGIGYVPEGRRI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 75 LPNLTVHETVRFAARLKTPKEQTDGEVEVLV-----EETLSQLGLThvqhsligggagkrgISGGERKRVAVAVELVARP 149
Cdd:cd03224 87 FPELTVEENLLLGAYARRRAKRKARLERVYElfprlKERRKQLAGT---------------LSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 150 SVLLLDEPTSGLDSSTAFKLMLTLKELASLGHAIaVVIHQPRTSIFNLFDNLLLLQKGNVVYEGKASEVK 219
Cdd:cd03224 152 KLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTI-LLVEQNARFALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-165 |
1.14e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 81.46 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLAdPTKDLIdnsciRINNEKGTLPKRLVGVVW--QEDLLLPNL 78
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLP-PAAGTI-----KLDGGDIDDPDVAEACHYlgHRNAMKPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 79 TVHETVRFAARLKtpkeqtdGEVEVLVEETLSQLGLTHVQHslIGGGAgkrgISGGERKRVAVAVELVARPSVLLLDEPT 158
Cdd:PRK13539 89 TVAENLEFWAAFL-------GGEELDIAAALEAVGLAPLAH--LPFGY----LSAGQKRRVALARLLVSNRPIWILDEPT 155
|
....*..
gi 224007385 159 SGLDSST 165
Cdd:PRK13539 156 AALDAAA 162
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
3-188 |
1.37e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 81.79 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLADPTKDLI--DNSCIRINNE-KGTLPKRLVGVVWQEDLLLPNLT 79
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIfnGQPMSKLSSAaKAELRNQKLGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 80 VHETVRFAARL--KTPKEQTDGEVEVLveetlSQLGLTH-VQHSligggagKRGISGGERKRVAVAVELVARPSVLLLDE 156
Cdd:PRK11629 104 ALENVAMPLLIgkKKPAEINSRALEML-----AAVGLEHrANHR-------PSELSGGERQRVAIARALVNNPRLVLADE 171
|
170 180 190
....*....|....*....|....*....|...
gi 224007385 157 PTSGLDSSTAFKLMLTLKEL-ASLGHAIAVVIH 188
Cdd:PRK11629 172 PTGNLDARNADSIFQLLGELnRLQGTAFLVVTH 204
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-177 |
1.57e-17 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 85.22 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLaDPTKD--LIDNSCIRinnekgTLPK----RLVGVVWQEDLL 74
Cdd:COG1132 353 RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFY-DPTSGriLIDGVDIR------DLTLeslrRQIGVVPQDTFL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 75 LpNLTVHETVRFAArlktpKEQTDGEVE-----VLVEETLSQL--GL-THVqhsligggaGKRGI--SGGERKRVAVAVE 144
Cdd:COG1132 426 F-SGTIRENIRYGR-----PDATDEEVEeaakaAQAHEFIEALpdGYdTVV---------GERGVnlSGGQRQRIAIARA 490
|
170 180 190
....*....|....*....|....*....|...
gi 224007385 145 LVARPSVLLLDEPTSGLDSSTAFKLMLTLKELA 177
Cdd:COG1132 491 LLKDPPILILDEATSALDTETEALIQEALERLM 523
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1-217 |
1.97e-17 |
|
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: 81.51 E-value: 1.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLvsvaAGLL---ADPTKdlidnSCIRINNE---KGTLP--KRLVGVVWQeD 72
Cdd:cd03253 14 RPVLKDVSFTIPAGKKVAIVGPSGSGKSTI----LRLLfrfYDVSS-----GSILIDGQdirEVTLDslRRAIGVVPQ-D 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 73 LLLPNLTVHETVRFAaRLKTpkeqTDGEVEVLVE--------ETLSQLGLTHVqhsligggaGKRG--ISGGERKRVAVA 142
Cdd:cd03253 84 TVLFNDTIGYNIRYG-RPDA----TDEEVIEAAKaaqihdkiMRFPDGYDTIV---------GERGlkLSGGEKQRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 224007385 143 VELVARPSVLLLDEPTSGLDSSTAFKLMLTLKELASlGHAIAVVIHqpRTSIFNLFDNLLLLQKGNVVYEGKASE 217
Cdd:cd03253 150 RAILKNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAH--RLSTIVNADKIIVLKDGRIVERGTHEE 221
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1-188 |
2.33e-17 |
|
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: 80.38 E-value: 2.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLaDPTKdlidnSCIRINNEKGTLPKRL--VGVVWQE-DLLLPN 77
Cdd:cd03226 13 TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLI-KESS-----GSILLNGKPIKAKERRksIGYVMQDvDYQLFT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 78 LTVHETVRFAARLkTPKEQTDGEvEVLVEETLSQLGLTHvQHSLigggagkrgiSGGERKRVAVAVELVARPSVLLLDEP 157
Cdd:cd03226 87 DSVREELLLGLKE-LDAGNEQAE-TVLKDLDLYALKERH-PLSL----------SGGQKQRLAIAAALLSGKDLLIFDEP 153
|
170 180 190
....*....|....*....|....*....|.
gi 224007385 158 TSGLDSSTAFKLMLTLKELASLGHAIAVVIH 188
Cdd:cd03226 154 TSGLDYKNMERVGELIRELAAQGKAVIVITH 184
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-189 |
2.90e-17 |
|
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: 81.09 E-value: 2.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLAdPTKD--LIDNSCI-RINNEKGTLPKRLVGVVWQEDLLLPNLTV 80
Cdd:cd03258 21 LKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLER-PTSGsvLVDGTDLtLLSGKELRKARRRIGMIFQHFNLLSSRTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 81 HETVRFAARL-KTPKEqtdgEVEVLVEETLSQLGLTHVQHSLIGGgagkrgISGGERKRVAVAVELVARPSVLLLDEPTS 159
Cdd:cd03258 100 FENVALPLEIaGVPKA----EIEERVLELLELVGLEDKADAYPAQ------LSGGQKQRVGIARALANNPKVLLCDEATS 169
|
170 180 190
....*....|....*....|....*....|.
gi 224007385 160 GLDSSTAFKLMLTLKEL-ASLGHAIAVVIHQ 189
Cdd:cd03258 170 ALDPETTQSILALLRDInRELGLTIVLITHE 200
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
15-213 |
2.95e-17 |
|
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: 80.23 E-value: 2.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 15 QLTAWMGPSGSGKTSLVSVAAGLladptkDLIDNSCIRINN-EKGTLP--KRLVGVVWQEDLLLPNLTVHETVRFA--AR 89
Cdd:cd03298 25 EITAIVGPSGSGKSTLLNLIAGF------ETPQSGRVLINGvDVTAAPpaDRPVSMLFQENNLFAHLTVEQNVGLGlsPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 90 LKTPKEQTDGevevlVEETLSQLGLthvqhsligGGAGKR---GISGGERKRVAVAVELVARPSVLLLDEPTSGLDSSTA 166
Cdd:cd03298 99 LKLTAEDRQA-----IEVALARVGL---------AGLEKRlpgELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 224007385 167 FKLM-LTLKELASLGHAIAVVIHQPRTSIFNLFDNLLLLQkGNVVYEG 213
Cdd:cd03298 165 AEMLdLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDN-GRIAAQG 211
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1-190 |
3.23e-17 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 80.25 E-value: 3.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLladptkDLIDNSCIRINNEK-GTLP----KRLVGVVWQEDLLL 75
Cdd:COG4619 13 KPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADL------DPPTSGEIYLDGKPlSAMPppewRRQVAYVPQEPALW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 76 PNlTVHETVRFAARLKTPKEQTDgevevLVEETLSQLGLTH------VQHsligggagkrgISGGERKRVAVAVELVARP 149
Cdd:COG4619 87 GG-TVRDNLPFPFQLRERKFDRE-----RALELLERLGLPPdildkpVER-----------LSGGERQRLALIRALLLQP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 224007385 150 SVLLLDEPTSGLDSSTAFKLM-LTLKELASLGHAIAVVIHQP 190
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEeLLREYLAEEGRAVLWVSHDP 191
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
8-191 |
3.96e-17 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 80.57 E-value: 3.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 8 STKISPYQLTAWMGPSGSGKTSLVSVAAGLLAdptkdlIDNSCIRINNEK--GTLP-KRLVGVVWQEDLLLPNLTVHETV 84
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLP------PDSGRILWNGQDltALPPaERPVSMLFQENNLFPHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 85 RFA--ARLK-TPKEQTDgevevlVEETLSQLGLThvqhsliggGAGKR---GISGGERKRVAVAVELV-ARPsVLLLDEP 157
Cdd:COG3840 93 GLGlrPGLKlTAEQRAQ------VEQALERVGLA---------GLLDRlpgQLSGGQRQRVALARCLVrKRP-ILLLDEP 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 224007385 158 TSGLDSstAFKL-MLTL-KELA-SLGHAIAVVIHQPR 191
Cdd:COG3840 157 FSALDP--ALRQeMLDLvDELCrERGLTVLMVTHDPE 191
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
3-163 |
4.47e-17 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 82.77 E-value: 4.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLADPTKDL-IDNscIRINNekgtLP--KRLVGVVWQEDLLLPNLT 79
Cdd:PRK11000 18 ISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLfIGE--KRMND----VPpaERGVGMVFQSYALYPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 80 VHETVRFAARL-KTPKEQTDGEVEVlVEETLsQLGlthvqHSLiggGAGKRGISGGERKRVAVAVELVARPSVLLLDEPT 158
Cdd:PRK11000 92 VAENMSFGLKLaGAKKEEINQRVNQ-VAEVL-QLA-----HLL---DRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPL 161
|
....*
gi 224007385 159 SGLDS 163
Cdd:PRK11000 162 SNLDA 166
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-218 |
4.75e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 80.71 E-value: 4.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLA-DPTKDLIDNSCIRInnekgtLP-----KRLVGVVWQEDLL 74
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPrDAGNIIIDDEDISL------LPlharaRRGIGYLPQEASI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 75 LPNLTVHETVrfAARLKTPKEQTDGEVEVLVEETLSQLGLTHVQHSLigggagKRGISGGERKRVAVAVELVARPSVLLL 154
Cdd:PRK10895 90 FRRLSVYDNL--MAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSM------GQSLSGGERRRVEIARALAANPKFILL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224007385 155 DEPTSGLDSSTAFKLMLTLKELASLGHAIAVVIHQPRTSIFNLFDNLLLLQkGNVVYEGKASEV 218
Cdd:PRK10895 162 DEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQ-GHLIAHGTPTEI 224
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-186 |
6.73e-17 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 80.13 E-value: 6.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLAdPTKDlidNSCIRINNEKGTLP----KRLVGVV--WQEDLL 74
Cdd:COG1119 16 KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLP-PTYG---NDVRLFGERRGGEDvwelRKRIGLVspALQLRF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 75 LPNLTVHETVR--FAARLKTPKEQTDGEVEvLVEETLSQLGLTHVQHSLIGGgagkrgISGGERKRVAVAVELVARPSVL 152
Cdd:COG1119 92 PRDETVLDVVLsgFFDSIGLYREPTDEQRE-RARELLELLGLAHLADRPFGT------LSQGEQRRVLIARALVKDPELL 164
|
170 180 190
....*....|....*....|....*....|....
gi 224007385 153 LLDEPTSGLDSSTAFKLMLTLKELASLGhAIAVV 186
Cdd:COG1119 165 ILDEPTAGLDLGARELLLALLDKLAAEG-APTLV 197
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1-187 |
9.62e-17 |
|
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: 79.51 E-value: 9.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLL-ADPTKDLIDNSCIRinnekgTLP----KRL-VGVVWQEDLL 74
Cdd:cd03218 13 RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVkPDSGKILLDGQDIT------KLPmhkrARLgIGYLPQEASI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 75 LPNLTVHETVRFAARL-KTPKEQTDGEVEVLVEEtlsqLGLTHVQHSLigGGAgkrgISGGERKRVAVAVELVARPSVLL 153
Cdd:cd03218 87 FRKLTVEENILAVLEIrGLSKKEREEKLEELLEE----FHITHLRKSK--ASS----LSGGERRRVEIARALATNPKFLL 156
|
170 180 190
....*....|....*....|....*....|....
gi 224007385 154 LDEPTSGLDSSTAFKLMLTLKELASLGhaIAVVI 187
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKILKDRG--IGVLI 188
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1-165 |
1.43e-16 |
|
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: 78.81 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSvaagLLA---DPTKD--LIDNSCIRinneKGTLP--KRLVGVVWQeDL 73
Cdd:cd03251 15 PPVLRDISLDIPAGETVALVGPSGSGKSTLVN----LIPrfyDVDSGriLIDGHDVR----DYTLAslRRQIGLVSQ-DV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 74 LLPNLTVHETVRFAARLKTPKEqtdgevevlVEETLSQLGLTHVQHSLIGG---GAGKRGI--SGGERKRVAVAVELVAR 148
Cdd:cd03251 86 FLFNDTVAENIAYGRPGATREE---------VEEAARAANAHEFIMELPEGydtVIGERGVklSGGQRQRIAIARALLKD 156
|
170
....*....|....*..
gi 224007385 149 PSVLLLDEPTSGLDSST 165
Cdd:cd03251 157 PPILILDEATSALDTES 173
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-218 |
2.10e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 78.80 E-value: 2.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLADPTKDLIDNSCIRINNEKGTLP----KRLVGVVWQEDLLLPNL 78
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYLDGQDIFKMDvielRRRVQMVFQIPNPIPNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 79 TVHETVRFAARLKTpKEQTDGEVEVLVEETLSQLGLTHVQHSLIGGGAGKrgISGGERKRVAVAVELVARPSVLLLDEPT 158
Cdd:PRK14247 98 SIFENVALGLKLNR-LVKSKKELQERVRWALEKAQLWDEVKDRLDAPAGK--LSGGQQQRLCIARALAFQPEVLLADEPT 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 224007385 159 SGLDSSTAFK---LMLTLKElaslGHAIAVVIHQPRTSiFNLFDNLLLLQKGNVVYEGKASEV 218
Cdd:PRK14247 175 ANLDPENTAKiesLFLELKK----DMTIVLVTHFPQQA-ARISDYVAFLYKGQIVEWGPTREV 232
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
3-189 |
2.30e-16 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 78.52 E-value: 2.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAaGLLADPtkdliDNSCIRINNEKGTLPKRL-----------VGVVWQE 71
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLRVL-NLLETP-----DSGQLNIAGHQFDFSQKPsekairllrqkVGMVFQQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 72 DLLLPNLTVHETVRFAA--RLKTPKEQTDGEVEVLveetLSQLGLTHVQHSLigggagKRGISGGERKRVAVAVELVARP 149
Cdd:COG4161 91 YNLWPHLTVMENLIEAPckVLGLSKEQAREKAMKL----LARLRLTDKADRF------PLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 224007385 150 SVLLLDEPTSGLDSSTAFKLMLTLKELASLGHAIAVVIHQ 189
Cdd:COG4161 161 QVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHE 200
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-188 |
2.46e-16 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 78.62 E-value: 2.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLAdPTKDLIdnsciRINN-EKGTLPK----RLVGVVWQEDLLL 75
Cdd:COG4559 14 RTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELT-PSSGEV-----RLNGrPLAAWSPwelaRRRAVLPQHSSLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 76 PNLTVHETVRFAArlkTPKEQTDGEVEVLVEETLSQLGLTHVQHSLIgggagkRGISGGERKRVAVAVELV-------AR 148
Cdd:COG4559 88 FPFTVEEVVALGR---APHGSSAAQDRQIVREALALVGLAHLAGRSY------QTLSGGEQQRVQLARVLAqlwepvdGG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 224007385 149 PSVLLLDEPTSGLDSSTAFKLMLTLKELASLGHAIAVVIH 188
Cdd:COG4559 159 PRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLH 198
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-188 |
3.69e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 78.27 E-value: 3.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLAdptkdlIDNSCIRINN------EKGTLPKRLvGVVWQEDLL 74
Cdd:PRK13548 15 RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELS------PDSGEVRLNGrpladwSPAELARRR-AVLPQHSSL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 75 LPNLTVHETVRFAArlkTPKEQTDGEVEVLVEETLSQLGLTHVQHSLIgggagkRGISGGERKRVAVAVELV------AR 148
Cdd:PRK13548 88 SFPFTVEEVVAMGR---APHGLSRAEDDALVAAALAQVDLAHLAGRDY------PQLSGGEQQRVQLARVLAqlwepdGP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 224007385 149 PSVLLLDEPTSGLDSSTAFKLMLTLKELA-SLGHAIAVVIH 188
Cdd:PRK13548 159 PRWLLLDEPTSALDLAHQHHVLRLARQLAhERGLAVIVVLH 199
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1-218 |
5.94e-16 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 77.14 E-value: 5.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGL-LADPTKDLIDNSCIRINNEkgTLPKRLVGVVWQEDLLLpNLT 79
Cdd:cd03252 15 PVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFyVPENGRVLVDGHDLALADP--AWLRRQVGVVLQENVLF-NRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 80 VHETVRFAaRLKTPKEQTDgEVEVLV--EETLSQLGLTHVQhslIGGGAGKrGISGGERKRVAVAVELVARPSVLLLDEP 157
Cdd:cd03252 92 IRDNIALA-DPGMSMERVI-EAAKLAgaHDFISELPEGYDT---IVGEQGA-GLSGGQRQRIAIARALIHNPRILIFDEA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224007385 158 TSGLDSSTAFKLMLTLKELASlGHAIAVVIHqpRTSIFNLFDNLLLLQKGNVVYEGKASEV 218
Cdd:cd03252 166 TSALDYESEHAIMRNMHDICA-GRTVIIIAH--RLSTVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
4-191 |
9.50e-16 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 76.09 E-value: 9.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLaDPTKD--LIDNSCIRinnekgTLP----KRLVGVVWQeDLLLPN 77
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLY-KPTSGsvLLDGTDIR------QLDpadlRRNIGYVPQ-DVTLFY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 78 LTVHETVRFAARlktpkEQTDGEVEVLVEET-LSQLGLTHvQHSL---IG-GGagkRGISGGERKRVAVAVELVARPSVL 152
Cdd:cd03245 92 GTLRDNITLGAP-----LADDERILRAAELAgVTDFVNKH-PNGLdlqIGeRG---RGLSGGQRQAVALARALLNDPPIL 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 224007385 153 LLDEPTSGLDSSTAFKLMLTLKELASlGHAIAVVIHQPR 191
Cdd:cd03245 163 LLDEPTSAMDMNSEERLKERLRQLLG-DKTLIIITHRPS 200
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-165 |
1.15e-15 |
|
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: 75.87 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 6 DVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLAdPTKDLIDNSCIRINNEKGTLpKRLVGVVWQEDLLLPNLTVHETVR 85
Cdd:cd03265 18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLK-PTSGRATVAGHDVVREPREV-RRRIGIVFQDLSVDDELTGWENLY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 86 FAARLKTPKEQtdgEVEVLVEETLSQLGLTHVQHSLIgggagkRGISGGERKRVAVAVELVARPSVLLLDEPTSGLDSST 165
Cdd:cd03265 96 IHARLYGVPGA---ERRERIDELLDFVGLLEAADRLV------KTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQT 166
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-162 |
1.36e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 79.34 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLaDPTKDLIdnscirinnekgTLPKRL-VGVVWQEDLLLPNLT 79
Cdd:COG0488 11 RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGEL-EPDSGEV------------SIPKGLrIGYLPQEPPLDDDLT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 80 VHETV------------RFA----------------ARLKTPKEQTDG-EVEVLVEETLSQLGLTHVQH-----SLiggg 125
Cdd:COG0488 78 VLDTVldgdaelraleaELEeleaklaepdedlerlAELQEEFEALGGwEAEARAEEILSGLGFPEEDLdrpvsEL---- 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 224007385 126 agkrgiSGGERKRVAVAVELVARPSVLLLDEPTSGLD 162
Cdd:COG0488 154 ------SGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-162 |
1.54e-15 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 75.84 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLAdptkdlIDNSCIRINNEKGT-LP--KRL---VGVVWQEDLL 74
Cdd:COG1137 16 RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVK------PDSGRIFLDGEDIThLPmhKRArlgIGYLPQEASI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 75 LPNLTVHETVRFAARL--KTPKEQTDgEVEVLVEEtlsqLGLTHVQHSLigGGAgkrgISGGERKRVAVAVELVARPSVL 152
Cdd:COG1137 90 FRKLTVEDNILAVLELrkLSKKEREE-RLEELLEE----FGITHLRKSK--AYS----LSGGERRRVEIARALATNPKFI 158
|
170
....*....|
gi 224007385 153 LLDEPTSGLD 162
Cdd:COG1137 159 LLDEPFAGVD 168
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-162 |
1.61e-15 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 75.80 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLladptkDLIDNSCIRINNEKGTLPK-------RLVGVVWQEDLLL 75
Cdd:COG1126 16 VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLL------EEPDSGTITVDGEDLTDSKkdinklrRKVGMVFQQFNLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 76 PNLTVHETVRFAAR--LKTPKEqtdgEVEVLVEETLSQLGLTHVQHS----LigggagkrgiSGGERKRVAVAVELVARP 149
Cdd:COG1126 90 PHLTVLENVTLAPIkvKKMSKA----EAEERAMELLERVGLADKADAypaqL----------SGGQQQRVAIARALAMEP 155
|
170
....*....|...
gi 224007385 150 SVLLLDEPTSGLD 162
Cdd:COG1126 156 KVMLFDEPTSALD 168
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
3-163 |
2.14e-15 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 75.65 E-value: 2.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSvaagLLA---DPTKD--LIDNSCIRINNEKGTlpKRLVGVVWQEDLLLPN 77
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVS----LLErfyDPTSGeiLLDGVDIRDLNLRWL--RSQIGLVSQEPVLFDG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 78 lTVHETVRFAARlktpkeqtDGEVEvLVEETLSQLGLTHVQHSLIGGG---AGKRG--ISGGERKRVAVAVELVARPSVL 152
Cdd:cd03249 92 -TIAENIRYGKP--------DATDE-EVEEAAKKANIHDFIMSLPDGYdtlVGERGsqLSGGQKQRIAIARALLRNPKIL 161
|
170
....*....|.
gi 224007385 153 LLDEPTSGLDS 163
Cdd:cd03249 162 LLDEATSALDA 172
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
3-192 |
2.34e-15 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 73.79 E-value: 2.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLAdPTKDLIDNSCIRINNEKGTLPKRLVGVVWQEDLLLPNlTVHE 82
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLR-PTSGRVRLDGADISQWDPNELGDHVGYLPQDDELFSG-SIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 83 TVrfaarlktpkeqtdgevevlveetlsqlglthvqhsligggagkrgISGGERKRVAVAVELVARPSVLLLDEPTSGLD 162
Cdd:cd03246 95 NI----------------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLD 128
|
170 180 190
....*....|....*....|....*....|
gi 224007385 163 SSTAFKLMLTLKELASLGHAIAVVIHQPRT 192
Cdd:cd03246 129 VEGERALNQAIAALKAAGATRIVIAHRPET 158
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
4-188 |
2.52e-15 |
|
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: 76.66 E-value: 2.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLAdPTKDLIDNSCIRINNEKGTLpKRLVGVVWQEDLLLPNLTVHET 83
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLR-PTSGTARVAGYDVVREPRKV-RRSIGIVPQYASVDEDLTGREN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 84 VRFAARLKTPKEQtdgEVEVLVEETLSQLGLTHVQHSLIGGgagkrgISGGERKRVAVAVELVARPSVLLLDEPTSGLDS 163
Cdd:TIGR01188 87 LEMMGRLYGLPKD---EAEERAEELLELFELGEAADRPVGT------YSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDP 157
|
170 180
....*....|....*....|....*
gi 224007385 164 STAFKLMLTLKELASLGHAIAVVIH 188
Cdd:TIGR01188 158 RTRRAIWDYIRALKEEGVTILLTTH 182
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-213 |
2.63e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 75.82 E-value: 2.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLL-ADPTK----DLIDNSCIRINNEKGTLPKRL--VGVVWQEDLLLP 76
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItGDKSAgshiELLGRTVQREGRLARDIRKSRanTGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 77 NLTVHETVRFAARLKTPKEQT-----DGEVEVLVEETLSQLGLTHVQHSLIGGgagkrgISGGERKRVAVAVELVARPSV 151
Cdd:PRK09984 100 RLSVLENVLIGALGSTPFWRTcfswfTREQKQRALQALTRVGMVHFAHQRVST------LSGGQQQRVAIARALMQQAKV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 224007385 152 LLLDEPTSGLDSSTAFKLMLTLKEL-ASLGHAIAVVIHQPRTSIFNLFDNLLLLQkGNVVYEG 213
Cdd:PRK09984 174 ILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQ-GHVFYDG 235
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
3-189 |
3.74e-15 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 74.24 E-value: 3.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLADptkdliDNSCIRINNEK-GTLPKRLVGVVWQEDLLLPNLTVH 81
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILP------DSGEVLFDGKPlDIAARNRIGYLPEERGLYPKMKVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 82 ETVRFAARLKTPKEQtdgEVEVLVEETLSQLGLTHVQHSLIgggagkRGISGGERKRVAVAVELVARPSVLLLDEPTSGL 161
Cdd:cd03269 89 DQLVYLAQLKGLKKE---EARRRIDEWLERLELSEYANKRV------EELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180
....*....|....*....|....*...
gi 224007385 162 DSSTAFKLMLTLKELASLGHAIAVVIHQ 189
Cdd:cd03269 160 DPVNVELLKDVIRELARAGKTVILSTHQ 187
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-188 |
8.73e-15 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 74.30 E-value: 8.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLadptkDLIDNsC-----IRINNE----KGTLPKRL---VGVVWQ 70
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMN-----DLIPG-ArvegeILLDGEdiydPDVDVVELrrrVGMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 71 EdlllPN---LTVHETVRFAARL--KTPKeqtdGEVEVLVEETLSQLGL-THVQHSLigggagKR---GISGGERKRV-- 139
Cdd:COG1117 100 K----PNpfpKSIYDNVAYGLRLhgIKSK----SELDEIVEESLRKAALwDEVKDRL------KKsalGLSGGQQQRLci 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 224007385 140 --AVAVElvarPSVLLLDEPTSGLDS-STAfK---LMLTLKElaslGHAIAVVIH 188
Cdd:COG1117 166 arALAVE----PEVLLMDEPTSALDPiSTA-KieeLILELKK----DYTIVIVTH 211
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-162 |
1.06e-14 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 75.64 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 6 DVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLlADPTKDLIdnscIRINNEKGTLP--KRLVGVVWQEDLLLPNLTVHET 83
Cdd:PRK11607 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGF-EQPTAGQI----MLDGVDLSHVPpyQRPINMMFQSYALFPHMTVEQN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 84 VRFAARL-KTPKeqtdGEVEVLVEEtlsQLGLTHVQHsligggAGKRG---ISGGERKRVAVAVELVARPSVLLLDEPTS 159
Cdd:PRK11607 112 IAFGLKQdKLPK----AEIASRVNE---MLGLVHMQE------FAKRKphqLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
...
gi 224007385 160 GLD 162
Cdd:PRK11607 179 ALD 181
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
3-176 |
1.38e-14 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 75.12 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLADPTKDL----IDNSCIRINNekgtlpkRLVGVVWQEDLLLPNL 78
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIrfhgTDVSRLHARD-------RKVGFVFQHYALFRHM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 79 TVHETVRFAARLKTPKEQTDG-EVEVLVEETLSQLGLTHVqhsligggAGK--RGISGGERKRVAVAVELVARPSVLLLD 155
Cdd:PRK10851 90 TVFDNIAFGLTVLPRRERPNAaAIKAKVTQLLEMVQLAHL--------ADRypAQLSGGQKQRVALARALAVEPQILLLD 161
|
170 180
....*....|....*....|.
gi 224007385 156 EPTSGLDSSTAFKLMLTLKEL 176
Cdd:PRK10851 162 EPFGALDAQVRKELRRWLRQL 182
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
6-162 |
1.79e-14 |
|
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: 73.45 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 6 DVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLaDPT--KDLIDNSCIRINNEKG--TLPKRLVGVVWQEDLLLPNLTVH 81
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLI-EPTsgKVLIDGQDIAAMSRKElrELRRKKISMVFQSFALLPHRTVL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 82 ETVRFAARLKTPKEQtdgEVEVLVEETLSQLGLTHVQHSLIGGgagkrgISGGERKRVAVAVELVARPSVLLLDEPTSGL 161
Cdd:cd03294 121 ENVAFGLEVQGVPRA---EREERAAEALELVGLEGWEHKYPDE------LSGGMQQRVGLARALAVDPDILLMDEAFSAL 191
|
.
gi 224007385 162 D 162
Cdd:cd03294 192 D 192
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
4-188 |
1.88e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 73.63 E-value: 1.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLAdPTKD--LIDNSCIR---INNEKGTLPKRlVGVVWQ--EDLLLP 76
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHV-PTQGsvRVDDTLITstsKNKDIKQIRKK-VGLVFQfpESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 77 NlTVHETVRFAAR-LKTPKEqtdgEVEVLVEETLSQLGLTHvqhSLIGGGAGKrgISGGERKRVAVAVELVARPSVLLLD 155
Cdd:PRK13649 101 E-TVLKDVAFGPQnFGVSQE----EAEALAREKLALVGISE---SLFEKNPFE--LSGGQMRRVAIAGILAMEPKILVLD 170
|
170 180 190
....*....|....*....|....*....|...
gi 224007385 156 EPTSGLDSSTAFKLMLTLKELASLGHAIAVVIH 188
Cdd:PRK13649 171 EPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTH 203
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
4-188 |
1.89e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 73.27 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSvAAGLLADPTKDLIDNSCIRINNEKGTLPK-------RLVGVVWQEdlllP 76
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLR-SINRMNDLNPEVTITGSIVYNGHNIYSPRtdtvdlrKEIGMVFQQ----P 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 77 N---LTVHETVRFAARLKTPKEQtdgevEVL---VEETLSQLGL-----THVQHSLIGggagkrgISGGERKRVAVAVEL 145
Cdd:PRK14239 96 NpfpMSIYENVVYGLRLKGIKDK-----QVLdeaVEKSLKGASIwdevkDRLHDSALG-------LSGGQQQRVCIARVL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 224007385 146 VARPSVLLLDEPTSGLDSSTAFKLMLTLKELASlGHAIAVVIH 188
Cdd:PRK14239 164 ATSPKIILLDEPTSALDPISAGKIEETLLGLKD-DYTMLLVTR 205
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1-191 |
1.97e-14 |
|
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: 72.01 E-value: 1.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLADPTKDLIDNSciRINNEKGTLPKRLVGVVWQEDLLLPNLTV 80
Cdd:TIGR01189 13 RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNG--TPLAEQRDEPHENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 81 HETVRFAARLKTPKEQTdgevevlVEETLSQLGLTHVQHSLIgggagkRGISGGERKRVAVAVELVARPSVLLLDEPTSG 160
Cdd:TIGR01189 91 LENLHFWAAIHGGAQRT-------IEDALAAVGLTGFEDLPA------AQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170 180 190
....*....|....*....|....*....|.
gi 224007385 161 LDSSTAFKLMLTLKELASLGHAIAVVIHQPR 191
Cdd:TIGR01189 158 LDKAGVALLAGLLRAHLARGGIVLLTTHQDL 188
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
18-162 |
2.25e-14 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 72.31 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 18 AWMGPSGSGKTSLVSVAAGLLADPTKDLidnsciRINNEKGTL---PKRLVGVVWQEDLLLPNLTVHETVRFAAR--LKT 92
Cdd:PRK10771 29 AILGPSGAGKSTLLNLIAGFLTPASGSL------TLNGQDHTTtppSRRPVSMLFQENNLFSHLTVAQNIGLGLNpgLKL 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 93 PKEQTDgevevLVEETLSQLGLTHVQHSLIGGgagkrgISGGERKRVAVAVELVARPSVLLLDEPTSGLD 162
Cdd:PRK10771 103 NAAQRE-----KLHAIARQMGIEDLLARLPGQ------LSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
15-162 |
3.00e-14 |
|
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: 75.82 E-value: 3.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 15 QLTAWMGPSGSGKTSLVSVAAGLLAdPTKD--LIDNSCIRINNEkgtLPKRLVGVVWQEDLLLPNLTVHETVRFAARLK- 91
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLP-PTSGtvLVGGKDIETNLD---AVRQSLGMCPQHNILFHHLTVAEHILFYAQLKg 1032
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224007385 92 TPKEQTDGEVEVLVEETlsqlGLTHVQHSligggaGKRGISGGERKRVAVAVELVARPSVLLLDEPTSGLD 162
Cdd:TIGR01257 1033 RSWEEAQLEMEAMLEDT----GLHHKRNE------EAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVD 1093
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
4-241 |
4.30e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 72.84 E-value: 4.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLaDPTKDLI---DNSCIRINNEKGTLP-KRLVGVVWQ--EDLLLPN 77
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLL-QPTEGKVtvgDIVVSSTSKQKEIKPvRKKVGVVFQfpESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 78 lTVHETVRFAAR-LKTPKEqtdgEVEVLVEETLSQLGLTHVQHSligggAGKRGISGGERKRVAVAVELVARPSVLLLDE 156
Cdd:PRK13643 101 -TVLKDVAFGPQnFGIPKE----KAEKIAAEKLEMVGLADEFWE-----KSPFELSGGQMRRVAIAGILAMEPEVLVLDE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 157 PTSGLDSSTAFKLMLTLKELASLGHAIAVVIHQpRTSIFNLFDNLLLLQKGNVVYEGKASEVKR---YLEACPLctKLPP 233
Cdd:PRK13643 171 PTAGLDPKARIEMMQLFESIHQSGQTVVLVTHL-MDDVADYADYVYLLEKGHIISCGTPSDVFQevdFLKAHEL--GVPK 247
|
....*...
gi 224007385 234 ETGLADWL 241
Cdd:PRK13643 248 ATHFADQL 255
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-188 |
5.07e-14 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 71.56 E-value: 5.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLaDPTKDLIDNSCIRINNEKGTLPKRLVGVVWQEDLLLPNLTVHET 83
Cdd:cd03295 17 VNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLI-EPTSGEIFIDGEDIREQDPVELRRKIGYVIQQIGLFPHMTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 84 VRFAARL-KTPKEQTDGEVEvlveETLSQLGLTHVQ------HSLigggagkrgiSGGERKRVAVAVELVARPSVLLLDE 156
Cdd:cd03295 96 IALVPKLlKWPKEKIRERAD----ELLALVGLDPAEfadrypHEL----------SGGQQQRVGVARALAADPPLLLMDE 161
|
170 180 190
....*....|....*....|....*....|....*
gi 224007385 157 PTSGLDSSTAFKL---MLTLKELasLGHAIAVVIH 188
Cdd:cd03295 162 PFGALDPITRDQLqeeFKRLQQE--LGKTIVFVTH 194
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
6-177 |
1.06e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 72.21 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 6 DVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLAdPtkdliDNSCIRINN------EKGT-LP--KRLVGVVWQEDLLLP 76
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTR-P-----QKGRIVLNGrvlfdaEKGIcLPpeKRRIGYVFQDARLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 77 NLTVHETVRFAARlKTPKEQTDGEVEVLVEETLsqlgLTHVQHSLigggagkrgiSGGERKRVAVAVELVARPSVLLLDE 156
Cdd:PRK11144 90 HYKVRGNLRYGMA-KSMVAQFDKIVALLGIEPL----LDRYPGSL----------SGGEKQRVAIGRALLTAPELLLMDE 154
|
170 180
....*....|....*....|.
gi 224007385 157 PTSGLDSSTAFKLMLTLKELA 177
Cdd:PRK11144 155 PLASLDLPRKRELLPYLERLA 175
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
20-163 |
1.09e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 72.44 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 20 MGPSGSGKTSLVSVAAGLlADPTkdlidNSCIRINNE---KGTLPKRLVGVVWQEDLLLPNLTVHETVRFAAR-LKTPKE 95
Cdd:PRK11432 38 LGPSGCGKTTVLRLVAGL-EKPT-----EGQIFIDGEdvtHRSIQQRDICMVFQSYALFPHMSLGENVGYGLKmLGVPKE 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224007385 96 qtdgEVEVLVEETLSQLGLthvqhsligGGAGKR---GISGGERKRVAVAVELVARPSVLLLDEPTSGLDS 163
Cdd:PRK11432 112 ----ERKQRVKEALELVDL---------AGFEDRyvdQISGGQQQRVALARALILKPKVLLFDEPLSNLDA 169
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
2-188 |
1.50e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 72.18 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 2 SILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLAdPTKDLIDNSCIRINNEKGTLPKRLVGVVWQEDLLLPNLTVH 81
Cdd:PRK09536 17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLT-PTAGTVLVAGDDVEALSARAASRRVASVPQDTSLSFEFDVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 82 ETVRFAARLKTPKEQTDGEV-EVLVEETLSQLGLTHVQHSLIgggagkRGISGGERKRVAVAVELVARPSVLLLDEPTSG 160
Cdd:PRK09536 96 QVVEMGRTPHRSRFDTWTETdRAAVERAMERTGVAQFADRPV------TSLSGGERQRVLLARALAQATPVLLLDEPTAS 169
|
170 180
....*....|....*....|....*...
gi 224007385 161 LDSSTAFKLMLTLKELASLGHAIAVVIH 188
Cdd:PRK09536 170 LDINHQVRTLELVRRLVDDGKTAVAAIH 197
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
4-188 |
1.87e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 70.63 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLAdPTKDLIDNSCIRINNEKGT-----LPKRlVGVVWQ--EDLLLP 76
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLK-PSSGTITIAGYHITPETGNknlkkLRKK-VSLVFQfpEAQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 77 NlTVHETVRFAarlktPKE--QTDGEVEVLVEETLSQLGLTH--VQHSLIGggagkrgISGGERKRVAVAVELVARPSVL 152
Cdd:PRK13641 101 N-TVLKDVEFG-----PKNfgFSEDEAKEKALKWLKKVGLSEdlISKSPFE-------LSGGQMRRVAIAGVMAYEPEIL 167
|
170 180 190
....*....|....*....|....*....|....*.
gi 224007385 153 LLDEPTSGLDSSTAFKLMLTLKELASLGHAIAVVIH 188
Cdd:PRK13641 168 CLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTH 203
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1-176 |
2.25e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 72.30 E-value: 2.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVsvaaGLLA---DPTKD--LIDNSCIRINNEKGTlpKRLVGVVWQEDLLL 75
Cdd:PRK13657 348 RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLI----NLLQrvfDPQSGriLIDGTDIRTVTRASL--RRNIAVVFQDAGLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 76 pNLTVHETVRFAarlktpKEQ-TDGEVEvLVEETLSQLGLTHVQHSLIGGGAGKRG--ISGGERKRVAVAVELVARPSVL 152
Cdd:PRK13657 422 -NRSIEDNIRVG------RPDaTDEEMR-AAAERAQAHDFIERKPDGYDTVVGERGrqLSGGERQRLAIARALLKDPPIL 493
|
170 180
....*....|....*....|....
gi 224007385 153 LLDEPTSGLDSSTAFKLMLTLKEL 176
Cdd:PRK13657 494 ILDEATSALDVETEAKVKAALDEL 517
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
7-189 |
2.83e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 72.18 E-value: 2.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 7 VSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLadPTKdlidnSCIRINN-EKGTLPK----RLVGVVWQEDLLLpnltvH 81
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL--PYQ-----GSLKINGiELRELDPeswrKHLSWVGQNPQLP-----H 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 82 ETVRFAARLKTPkEQTDGEVEVLVE-----ETLSQL--GLTHVqhslIGGGAGkrGISGGERKRVAVAVELVARPSVLLL 154
Cdd:PRK11174 437 GTLRDNVLLGNP-DASDEQLQQALEnawvsEFLPLLpqGLDTP----IGDQAA--GLSVGQAQRLALARALLQPCQLLLL 509
|
170 180 190
....*....|....*....|....*....|....*
gi 224007385 155 DEPTSGLDSSTAFKLMLTLKElASLGHAIAVVIHQ 189
Cdd:PRK11174 510 DEPTASLDAHSEQLVMQALNA-ASRRQTTLMVTHQ 543
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-165 |
4.72e-13 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 70.11 E-value: 4.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAgLLADPTKdlidnSCIRINNEK-GTLPKR-L------VGVVWQEDLLL 75
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCIN-LLERPTS-----GSVLVDGVDlTALSEReLraarrkIGMIFQHFNLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 76 PNLTVHETVRFAARL-KTPKEqtdgEVEVLVEETLSQLGLTHvqhsligggagKRG-----ISGGERKRVAVAVELVARP 149
Cdd:COG1135 95 SSRTVAENVALPLEIaGVPKA----EIRKRVAELLELVGLSD-----------KADaypsqLSGGQKQRVGIARALANNP 159
|
170
....*....|....*.
gi 224007385 150 SVLLLDEPTSGLDSST 165
Cdd:COG1135 160 KVLLCDEATSALDPET 175
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
3-190 |
7.50e-13 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 70.91 E-value: 7.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAaGLLADPTKDL--IDNSCIRI--NNEKGTLPKRLVGVVWQEDLLLPNL 78
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNIL-GCLDKPTSGTyrVAGQDVATldADALAQLRREHFGFIFQRYHLLSHL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 79 TVHETVRF-AARLKTPKEQTDGEVEVLveetLSQLGL---THVQHSligggagkrGISGGERKRVAVAVELVARPSVLLL 154
Cdd:PRK10535 102 TAAQNVEVpAVYAGLERKQRLLRAQEL----LQRLGLedrVEYQPS---------QLSGGQQQRVSIARALMNGGQVILA 168
|
170 180 190
....*....|....*....|....*....|....*.
gi 224007385 155 DEPTSGLDSSTAFKLMLTLKELASLGHAIAVVIHQP 190
Cdd:PRK10535 169 DEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDP 204
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1-190 |
1.01e-12 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 67.13 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLADPTKDlidnscIRINNEkgtlPKRLVGVVWQEDLL----LP 76
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGR------VLLNGG----PLDFQRDSIARGLLylghAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 77 N----LTVHETVRFAARLKTpkeqTDGevevlVEETLSQLGLTHVQHSLIGGgagkrgISGGERKRVAVAVELVARPSVL 152
Cdd:cd03231 83 GikttLSVLENLRFWHADHS----DEQ-----VEEALARVGLNGFEDRPVAQ------LSAGQQRRVALARLLLSGRPLW 147
|
170 180 190
....*....|....*....|....*....|....*...
gi 224007385 153 LLDEPTSGLDSSTAFKLMLTLKELASLGHAIAVVIHQP 190
Cdd:cd03231 148 ILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQD 185
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-176 |
1.09e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 68.29 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLA--DPTKDLIDNSCIRINNEKGTLPKRLVGVVWQE-DLLLPN 77
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLpdDNPNSKITVDGITLTAKTVWDIREKVGIVFQNpDNQFVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 78 LTVHETVRFAARLK-TPKEqtdgEVEVLVEETLSQLGLTHVQHSligggaGKRGISGGERKRVAVAVELVARPSVLLLDE 156
Cdd:PRK13640 100 ATVGDDVAFGLENRaVPRP----EMIKIVRDVLADVGMLDYIDS------EPANLSGGQKQRVAIAGILAVEPKIIILDE 169
|
170 180
....*....|....*....|
gi 224007385 157 PTSGLDSSTAFKLMLTLKEL 176
Cdd:PRK13640 170 STSMLDPAGKEQILKLIRKL 189
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1-162 |
1.72e-12 |
|
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: 66.73 E-value: 1.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLaDPTKD--LIDNSCIRINNEKgtLPKRLVGVVWQEDLLLPNl 78
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFY-QPQGGqvLLDGKPISQYEHK--YLHSKVSLVGQEPVLFAR- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 79 TVHETVRFAArlktpkeqTDGEVEVLVEetlsqLGLTHVQHSLIGG-------GAGKRG--ISGGERKRVAVAVELVARP 149
Cdd:cd03248 103 SLQDNIAYGL--------QSCSFECVKE-----AAQKAHAHSFISElasgydtEVGEKGsqLSGGQKQRVAIARALIRNP 169
|
170
....*....|...
gi 224007385 150 SVLLLDEPTSGLD 162
Cdd:cd03248 170 QVLILDEATSALD 182
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
3-222 |
1.87e-12 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 66.93 E-value: 1.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLAdPTKDlidnsCIRINNEK--GTLPKRLV--GVVW--QEDLLLP 76
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLP-PRSG-----SIRFDGEDitGLPPHRIArlGIGYvpEGRRIFP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 77 NLTVHETVRFAARLKTPKEQTDGEVE-------VLvEETLSQLGLThvqhsligggagkrgISGGERKRVAVAVELVARP 149
Cdd:COG0410 92 SLTVEENLLLGAYARRDRAEVRADLErvyelfpRL-KERRRQRAGT---------------LSGGEQQMLAIGRALMSRP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 150 SVLLLDEPTSGLDSSTAFKLMLTLKELASLGHAI----------------AVVIhqprtsifnlfdnllllQKGNVVYEG 213
Cdd:COG0410 156 KLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTIllveqnarfaleiadrAYVL-----------------ERGRIVLEG 218
|
250
....*....|....*.
gi 224007385 214 KASE-------VKRYL 222
Cdd:COG0410 219 TAAElladpevREAYL 234
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-188 |
1.89e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 67.35 E-value: 1.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLADPT-------KDLIDNSCIRINNEKGTLPKRLvgvvwqedl 73
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSgtvflgdKPISMLSSRQLARRLALLPQHH--------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 74 LLP-NLTVHETVRFA--------ARLKTPKEQtdgevevLVEETLSQLGLTHVqhsligggAGKR--GISGGERKRVAVA 142
Cdd:PRK11231 86 LTPeGITVRELVAYGrspwlslwGRLSAEDNA-------RVNQAMEQTRINHL--------ADRRltDLSGGQRQRAFLA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 224007385 143 VELVARPSVLLLDEPTSGLDSSTAFKLMLTLKELASLGHAIAVVIH 188
Cdd:PRK11231 151 MVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLH 196
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1-188 |
2.15e-12 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 69.46 E-value: 2.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLvsvaAGLLA---DPTKD--LIDNSCIRinnekgTLPK----RLVGVVWQe 71
Cdd:COG5265 371 RPILKGVSFEVPAGKTVAIVGPSGAGKSTL----ARLLFrfyDVTSGriLIDGQDIR------DVTQaslrAAIGIVPQ- 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 72 DLLLPNLTVHETVRFAaRLktpkEQTDGEVEVLVEetLSQLglthvqHSLIGG---GA----GKRG--ISGGERKRVAVA 142
Cdd:COG5265 440 DTVLFNDTIAYNIAYG-RP----DASEEEVEAAAR--AAQI------HDFIESlpdGYdtrvGERGlkLSGGEKQRVAIA 506
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 224007385 143 VELVARPSVLLLDEPTSGLDSSTAFKLMLTLKELASlGHAIAVVIH 188
Cdd:COG5265 507 RTLLKNPPILIFDEATSALDSRTERAIQAALREVAR-GRTTLVIAH 551
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
3-189 |
2.27e-12 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 66.96 E-value: 2.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSV-------AAGLL--ADPTKDLIDNscirINNEKGTLPKRLVGVVWQEDL 73
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVlnllempRSGTLniAGNHFDFSKT----PSDKAIRELRRNVGMVFQQYN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 74 LLPNLTVHETVRFAAR--LKTPKEQTDGEVEvlveETLSQLGLTHV-----QHsligggagkrgISGGERKRVAVAVELV 146
Cdd:PRK11124 93 LWPHLTVQQNLIEAPCrvLGLSKDQALARAE----KLLERLRLKPYadrfpLH-----------LSGGQQQRVAIARALM 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 224007385 147 ARPSVLLLDEPTSGLDSSTAFKLMLTLKELASLGHAIAVVIHQ 189
Cdd:PRK11124 158 MEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHE 200
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
4-188 |
2.38e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 67.11 E-value: 2.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSVAagllaDPTKDLIdNSCiRIN----------NEKGTLP---KRLVGVVWQ 70
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCF-----NRLNDLI-PGF-RVEgkvtfhgknlYAPDVDPvevRRRIGMVFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 71 EDLLLPNlTVHETVRFAARLKTPKeqtdGEVEVLVEETLSQLGL-THVQHSLIGGGAGkrgISGGERKRVAVAVELVARP 149
Cdd:PRK14243 99 KPNPFPK-SIYDNIAYGARINGYK----GDMDELVERSLRQAALwDEVKDKLKQSGLS---LSGGQQQRLCIARAIAVQP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 224007385 150 SVLLLDEPTSGLDSSTAFK---LMLTLKElaslGHAIAVVIH 188
Cdd:PRK14243 171 EVILMDEPCSALDPISTLRieeLMHELKE----QYTIIIVTH 208
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-188 |
2.79e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 67.52 E-value: 2.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLADptkdliDNSCIRINNEkgTLPKRL------VGVVWQEDLL 74
Cdd:PRK13537 20 KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHP------DAGSISLCGE--PVPSRArharqrVGVVPQFDNL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 75 LPNLTVHETVR-FAARLKTPKEQTDGEVEVLVE-ETLSQLGLTHVqhsligggagkRGISGGERKRVAVAVELVARPSVL 152
Cdd:PRK13537 92 DPDFTVRENLLvFGRYFGLSAAAARALVPPLLEfAKLENKADAKV-----------GELSGGMKRRLTLARALVNDPDVL 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 224007385 153 LLDEPTSGLDSSTAFKLMLTLKELASLGHAIAVVIH 188
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTH 196
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
1-163 |
3.03e-12 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 68.97 E-value: 3.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLaDPTKDLIDNSCIRINNEKGTLPKRLVGVVWQeDLLLPNLTV 80
Cdd:TIGR02203 345 RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFY-EPDSGQILLDGHDLADYTLASLRRQVALVSQ-DVVLFNDTI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 81 HETVRFAARLKTPKEQTDgevEVLVEETLSQL--GLTHVQHSLIGGGAGKrgISGGERKRVAVAVELVARPSVLLLDEPT 158
Cdd:TIGR02203 423 ANNIAYGRTEQADRAEIE---RALAAAYAQDFvdKLPLGLDTPIGENGVL--LSGGQRQRLAIARALLKDAPILILDEAT 497
|
....*
gi 224007385 159 SGLDS 163
Cdd:TIGR02203 498 SALDN 502
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-244 |
3.37e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 66.95 E-value: 3.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLADPTKDLIDNSCIRINNEKGTLPKRL-VGVVWQE-DLLLPNLTV 80
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALRQqVATVFQDpEQQIFYTDI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 81 HETVRFAAR-LKTPKEqtdgEVEVLVEETLSQLGLTHVQHSLIgggagkRGISGGERKRVAVAVELVARPSVLLLDEPTS 159
Cdd:PRK13638 96 DSDIAFSLRnLGVPEA----EITRRVDEALTLVDAQHFRHQPI------QCLSHGQKKRVAIAGALVLQARYLLLDEPTA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 160 GLDSSTAFKLMLTLKELASLGHAIAVVIHQPRTsIFNLFDNLLLLQKGNVVYEGKASEVKRyleacplCTKLPPETGLAD 239
Cdd:PRK13638 166 GLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDL-IYEISDAVYVLRQGQILTHGAPGEVFA-------CTEAMEQAGLTQ 237
|
....*.
gi 224007385 240 -WLMDM 244
Cdd:PRK13638 238 pWLVKL 243
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-188 |
3.66e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 66.29 E-value: 3.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLADPTKDLIDNSCIRInnekGTLPKRLvgvvwQEDLLLPnLTV 80
Cdd:PRK09544 17 RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRI----GYVPQKL-----YLDTTLP-LTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 81 HetvRFAaRLKTPKEQTDgevevlveeTLSQLGLTHVQHSLiggGAGKRGISGGERKRVAVAVELVARPSVLLLDEPTSG 160
Cdd:PRK09544 87 N---RFL-RLRPGTKKED---------ILPALKRVQAGHLI---DAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQG 150
|
170 180
....*....|....*....|....*....
gi 224007385 161 LDSSTAFKLMLTLKEL-ASLGHAIAVVIH 188
Cdd:PRK09544 151 VDVNGQVALYDLIDQLrRELDCAVLMVSH 179
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
3-217 |
1.17e-11 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 67.05 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSlvsVAAGL--LADPT--KDLIDNSCIRINNEKGTlpKRLVGVVWQEDLLLpNL 78
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKST---VAALLqnLYQPTggQVLLDGVPLVQYDHHYL--HRQVALVGQEPVLF-SG 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 79 TVHETVRFAARLKTPKEQTDGEVEVLVEETLSqlGLTHVQHSLIGGGAGKRgiSGGERKRVAVAVELVARPSVLLLDEPT 158
Cdd:TIGR00958 570 SVRENIAYGLTDTPDEEIMAAAKAANAHDFIM--EFPNGYDTEVGEKGSQL--SGGQKQRIAIARALVRKPRVLILDEAT 645
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 224007385 159 SGLDSSTAFklmlTLKELASLGHAIAVVIHQpRTSIFNLFDNLLLLQKGNVVYEGKASE 217
Cdd:TIGR00958 646 SALDAECEQ----LLQESRSRASRTVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQ 699
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-190 |
1.26e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 64.86 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLaDPTKDLIDNSCIRINNEKGTLPK-------RLVGVVWQEDLLL 75
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLL-ELNEEARVEGEVRLFGRNIYSPDvdpievrREVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 76 PNLTVHETVRFAARL-KTPKEQtdGEVEVLVEETLSQLGLTHVQHSLIGGGAGKrgISGGERKRVAVAVELVARPSVLLL 154
Cdd:PRK14267 98 PHLTIYDNVAIGVKLnGLVKSK--KELDERVEWALKKAALWDEVKDRLNDYPSN--LSGGQRQRLVIARALAMKPKILLM 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 224007385 155 DEPTSGLDSSTAFKLMLTLKELASlGHAIAVVIHQP 190
Cdd:PRK14267 174 DEPTANIDPVGTAKIEELLFELKK-EYTIVLVTHSP 208
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
4-162 |
2.18e-11 |
|
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: 63.89 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLAdPTKDLIDNSCIRINNEKGTLPKRLVGVVWQEDLLLPNLTVHET 83
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQ-PTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKTQLWWDLPVIDS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 84 VRFAARL-KTPKEQTDGEVEVLVEetlsQLGLTHVQHSLIgggagkRGISGGERKRVAVAVELVARPSVLLLDEPTSGLD 162
Cdd:cd03267 116 FYLLAAIyDLPPARFKKRLDELSE----LLDLEELLDTPV------RQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
4-162 |
2.35e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 64.30 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLaDPT--KDLIDNSCIRINNEKGTLPKRLVGVVWQ--EDLLLPNlT 79
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLL-KPTsgKIIIDGVDITDKKVKLSDIRKKVGLVFQypEYQLFEE-T 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 80 VHETVRFAarlktPKE--QTDGEVEVLVEETLSQLGLTHVQHsligggAGKR--GISGGERKRVAVAVELVARPSVLLLD 155
Cdd:PRK13637 101 IEKDIAFG-----PINlgLSEEEIENRVKRAMNIVGLDYEDY------KDKSpfELSGGQKRRVAIAGVVAMEPKILILD 169
|
....*..
gi 224007385 156 EPTSGLD 162
Cdd:PRK13637 170 EPTAGLD 176
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1-218 |
2.66e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 63.85 E-value: 2.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLADPTKDL-IDNSCIRINNEKGTlpKRLVGVVWQEDLLLPNLT 79
Cdd:PRK10253 20 YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwLDGEHIQHYASKEV--ARRIGLLAQNATTPGDIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 80 VHETVrfaARLKTPKE----QTDGEVEVLVEETLSQLGLTHVQHSLIGGgagkrgISGGERKRVAVAVELVARPSVLLLD 155
Cdd:PRK10253 98 VQELV---ARGRYPHQplftRWRKEDEEAVTKAMQATGITHLADQSVDT------LSGGQRQRAWIAMVLAQETAIMLLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224007385 156 EPTSGLDSSTAFKLMLTLKEL-ASLGHAIAVVIHQPRTSIfNLFDNLLLLQKGNVVYEGKASEV 218
Cdd:PRK10253 169 EPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQAC-RYASHLIALREGKIVAQGAPKEI 231
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4-188 |
2.80e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 64.34 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLADPT---------------KDLIDNSCIRINNEKGTLPK------ 62
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTgtiewifkdeknkkkTKEKEKVLEKLVIQKTRFKKikkike 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 63 --RLVGVVWQ-EDLLLPNLTVHETVRFAAR-LKTPKEqtdgEVEVLVEETLSQLGL--THVQHSLIGggagkrgISGGER 136
Cdd:PRK13651 103 irRRVGVVFQfAEYQLFEQTIEKDIIFGPVsMGVSKE----EAKKRAAKYIELVGLdeSYLQRSPFE-------LSGGQK 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 224007385 137 KRVAVAVELVARPSVLLLDEPTSGLDSSTAFKLMLTLKELASLGHAIAVVIH 188
Cdd:PRK13651 172 RRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTH 223
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
18-218 |
4.34e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 63.67 E-value: 4.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 18 AWMGPSGSGKTSLVSVAAGLLAdPT--KDLIDNSCIRINNEKGTlpKRLVGVVWQE-DLLLPNLTVHETVRFAARLKTPK 94
Cdd:PRK13652 34 AVIGPNGAGKSTLFRHFNGILK-PTsgSVLIRGEPITKENIREV--RKFVGLVFQNpDDQIFSPTVEQDIAFGPINLGLD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 95 EQTdgeVEVLVEETLSQLGLTH----VQHSLigggagkrgiSGGERKRVAVAVELVARPSVLLLDEPTSGLDSSTAFKLM 170
Cdd:PRK13652 111 EET---VAHRVSSALHMLGLEElrdrVPHHL----------SGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELI 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 224007385 171 LTLKELA-SLGHAIAVVIHQPRTsIFNLFDNLLLLQKGNVVYEGKASEV 218
Cdd:PRK13652 178 DFLNDLPeTYGMTVIFSTHQLDL-VPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-165 |
4.39e-11 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 64.05 E-value: 4.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSVAaGLLADPT--KDLIDNSCIRINNEKG-TLPKRLVGVVWQEDLLLPNLTV 80
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCI-NLLERPTsgRVLVDGQDLTALSEKElRKARRQIGMIFQHFNLLSSRTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 81 HETVRFAARL-KTPKEqtdgEVEVLVEETLSQLGLTHvqhsligggagKRG-----ISGGERKRVAVAVELVARPSVLLL 154
Cdd:PRK11153 100 FDNVALPLELaGTPKA----EIKARVTELLELVGLSD-----------KADrypaqLSGGQKQRVAIARALASNPKVLLC 164
|
170
....*....|.
gi 224007385 155 DEPTSGLDSST 165
Cdd:PRK11153 165 DEATSALDPAT 175
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
3-191 |
5.27e-11 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 62.78 E-value: 5.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGllaDPTKDLIDNScIRINNEkgtlpkrlvgvvwqeDLLlpNLTVHE 82
Cdd:COG0396 15 ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMG---HPKYEVTSGS-ILLDGE---------------DIL--ELSPDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 83 -------------------TVRF----AARLKTPKEQTDGEVEVLVEETLSQLGLTHvqhSLIgggagKR----GISGGE 135
Cdd:COG0396 74 raragiflafqypveipgvSVSNflrtALNARRGEELSAREFLKLLKEKMKELGLDE---DFL-----DRyvneGFSGGE 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 224007385 136 RKRVAVAVELVARPSVLLLDEPTSGLDSStAFKLM-LTLKELASLGHAIAVVIHQPR 191
Cdd:COG0396 146 KKRNEILQMLLLEPKLAILDETDSGLDID-ALRIVaEGVNKLRSPDRGILIITHYQR 201
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
4-176 |
6.15e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 62.85 E-value: 6.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLL-ADPTKDLIDNSCIRINNEKGTlpKRLVGVVWQEDlllPNLTVHE 82
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEkVKSGEIFYNNQAITDDNFEKL--RKHIGIVFQNP---DNQFVGS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 83 TVRF--AARLKTPKEQTDGEVEVlVEETLSQLGLT----HVQHSLigggagkrgiSGGERKRVAVAVELVARPSVLLLDE 156
Cdd:PRK13648 100 IVKYdvAFGLENHAVPYDEMHRR-VSEALKQVDMLeradYEPNAL----------SGGQKQRVAIAGVLALNPSVIILDE 168
|
170 180
....*....|....*....|
gi 224007385 157 PTSGLDSSTAFKLMLTLKEL 176
Cdd:PRK13648 169 ATSMLDPDARQNLLDLVRKV 188
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-169 |
8.91e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 62.36 E-value: 8.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLV-------SVAAGLLADPTKDLIDNSCI--RINNEKgtlPKRLVGVVWQE 71
Cdd:PRK14258 20 QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLkclnrmnELESEVRVEGRVEFFNQNIYerRVNLNR---LRRQVSMVHPK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 72 DLLLPnLTVHETVRFAARLK--TPKEQTDGevevLVEETLSQLGL-THVQHSLiggGAGKRGISGGERKRVAVAVELVAR 148
Cdd:PRK14258 97 PNLFP-MSVYDNVAYGVKIVgwRPKLEIDD----IVESALKDADLwDEIKHKI---HKSALDLSGGQQQRLCIARALAVK 168
|
170 180
....*....|....*....|.
gi 224007385 149 PSVLLLDEPTSGLDSSTAFKL 169
Cdd:PRK14258 169 PKVLLMDEPCFGLDPIASMKV 189
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1-190 |
9.84e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 61.51 E-value: 9.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLadptKDLIDNSCIRINNEKgtlpkrlvgvVWQEDLLLPNLtv 80
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL----KGTPVAGCVDVPDNQ----------FGREASLIDAI-- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 81 hetvrfaARLKTPKEqtdgevevlVEETLSQLGLTHVQHSLigggAGKRGISGGERKRVAVAVELVARPSVLLLDEPTSG 160
Cdd:COG2401 107 -------GRKGDFKD---------AVELLNAVGLSDAVLWL----RRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSH 166
|
170 180 190
....*....|....*....|....*....|.
gi 224007385 161 LDSSTAFKLMLTLKELA-SLGHAIAVVIHQP 190
Cdd:COG2401 167 LDRQTAKRVARNLQKLArRAGITLVVATHHY 197
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-162 |
1.05e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 62.34 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLAdPTKDLIDNSCIRINNEKGTLPKRLVGVVWQE-DLLLPNLTVHE 82
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLL-PEAGTITVGGMVLSEETVWDVRRQVGMVFQNpDNQFVGATVQD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 83 TVRFAarLKT---PKEQTdgeVEvLVEETLSQLG----LTHVQHSLigggagkrgiSGGERKRVAVAVELVARPSVLLLD 155
Cdd:PRK13635 102 DVAFG--LENigvPREEM---VE-RVDQALRQVGmedfLNREPHRL----------SGGQKQRVAIAGVLALQPDIIILD 165
|
....*..
gi 224007385 156 EPTSGLD 162
Cdd:PRK13635 166 EATSMLD 172
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-181 |
1.49e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 63.29 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLadptkdlidnsciriNNEKGT--LPKrlvgvvwQEDLL---- 74
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLW---------------PYGSGRiaRPA-------GARVLflpq 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 75 ---LPNLTVHETVRFAArlkTPKEQTDGEVEvlveETLSQLGLTHVQHSLIGGGAGKRGISGGERKRVAVAVELVARPSV 151
Cdd:COG4178 434 rpyLPLGTLREALLYPA---TAEAFSDAELR----EALEAVGLGHLAERLDEEADWDQVLSLGEQQRLAFARLLLHKPDW 506
|
170 180 190
....*....|....*....|....*....|....*.
gi 224007385 152 LLLDEPTSGLDSSTAFKLMLTLKE------LASLGH 181
Cdd:COG4178 507 LFLDEATSALDEENEAALYQLLREelpgttVISVGH 542
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-188 |
1.73e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 61.04 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGlLADPTKDLI---DNSCIRINNEKGTLPKRLVGVVWQEDLLLPN 77
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICG-IERPSAGKIwfsGHDITRLKNREVPFLRRQIGMIFQDHHLLMD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 78 LTVHETVRFAARLKTPKEQtdgEVEVLVEETLSQLGLTHVQHSLigggagKRGISGGERKRVAVAVELVARPSVLLLDEP 157
Cdd:PRK10908 94 RTVYDNVAIPLIIAGASGD---DIRRRVSAALDKVGLLDKAKNF------PIQLSGGEQQRVGIARAVVNKPAVLLADEP 164
|
170 180 190
....*....|....*....|....*....|.
gi 224007385 158 TSGLDSSTAFKLMLTLKELASLGHAIAVVIH 188
Cdd:PRK10908 165 TGNLDDALSEGILRLFEEFNRVGVTVLMATH 195
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
3-176 |
2.22e-10 |
|
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 upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 61.29 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLaDPTKDLIDNSCIRINNEKgTLPK--RLVGVVWQE-DLLLPNLT 79
Cdd:TIGR04520 17 ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLL-LPTSGKVTVDGLDTLDEE-NLWEirKKVGMVFQNpDNQFVGAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 80 VHETVRFAAR-LKTPKEqtdgEVEVLVEETLSQLGLTHVQ----HSLigggagkrgiSGGERKRVAVAVELVARPSVLLL 154
Cdd:TIGR04520 95 VEDDVAFGLEnLGVPRE----EMRKRVDEALKLVGMEDFRdrepHLL----------SGGQKQRVAIAGVLAMRPDIIIL 160
|
170 180
....*....|....*....|..
gi 224007385 155 DEPTSGLDSSTAFKLMLTLKEL 176
Cdd:TIGR04520 161 DEATSMLDPKGRKEVLETIRKL 182
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-220 |
2.73e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 61.28 E-value: 2.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLADptkdliDNSCIRINNEKGTL-PKRLVGVVWQEDLLLPNLTVHE 82
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAP------DSGEVLWDGEPLDPeDRRRIGYLPEERGLYPKMKVGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 83 TVRFAARLK--TPKEqtdgeVEVLVEETLSQLGLTHVQHSLIgggagkRGISGGERKRVAVAVELVARPSVLLLDEPTSG 160
Cdd:COG4152 91 QLVYLARLKglSKAE-----AKRRADEWLERLGLGDRANKKV------EELSKGNQQKVQLIAALLHDPELLILDEPFSG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224007385 161 LDSSTAFKLMLTLKELASLGHAI----------------AVVIHqprtsifnlfdnllllqKGNVVYEGKASEVKR 220
Cdd:COG4152 160 LDPVNVELLKDVIRELAAKGTTVifsshqmelveelcdrIVIIN-----------------KGRKVLSGSVDEIRR 218
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1-213 |
2.76e-10 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 62.83 E-value: 2.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLaDPTKDLIDNSCIRINN-EKGTLpKRLVGVVWQEDLLLPNlT 79
Cdd:TIGR01193 487 SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFF-QARSGEILLNGFSLKDiDRHTL-RQFINYLPQEPYIFSG-S 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 80 VHETVRFAARLKTPKEQTDGEVEVL-VEETLSQLGLTHvQHSLIGGGAGkrgISGGERKRVAVAVELVARPSVLLLDEPT 158
Cdd:TIGR01193 564 ILENLLLGAKENVSQDEIWAACEIAeIKDDIENMPLGY-QTELSEEGSS---ISGGQKQRIALARALLTDSKVLILDEST 639
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 224007385 159 SGLDSSTAFKLmltLKELASLGH-AIAVVIHqpRTSIFNLFDNLLLLQKGNVVYEG 213
Cdd:TIGR01193 640 SNLDTITEKKI---VNNLLNLQDkTIIFVAH--RLSVAKQSDKIIVLDHGKIIEQG 690
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
20-189 |
6.63e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 60.25 E-value: 6.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 20 MGPSGSGKTSLVSVAAGLL-----------------ADPTKDLIDNSCIRINNEKGTlpKRLVGVVWQ--EDLLLPNlTV 80
Cdd:PRK13631 58 IGNSGSGKSTLVTHFNGLIkskygtiqvgdiyigdkKNNHELITNPYSKKIKNFKEL--RRRVSMVFQfpEYQLFKD-TI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 81 HETVRFA-ARLKTPKEqtdgEVEVLVEETLSQLGL--THVQHSLIGggagkrgISGGERKRVAVAVELVARPSVLLLDEP 157
Cdd:PRK13631 135 EKDIMFGpVALGVKKS----EAKKLAKFYLNKMGLddSYLERSPFG-------LSGGQKRRVAIAGILAIQPEILIFDEP 203
|
170 180 190
....*....|....*....|....*....|..
gi 224007385 158 TSGLDSSTAFKLMLTLKELASLGHAIAVVIHQ 189
Cdd:PRK13631 204 TAGLDPKGEHEMMQLILDAKANNKTVFVITHT 235
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
20-188 |
7.54e-10 |
|
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: 60.97 E-value: 7.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 20 MGPSGSGKTSLVSVAAGLLaDPTKDLIdnsCIRINNE------KGTL----PKRLVGVVWQEDLLLPNLTVHETVRFAAR 89
Cdd:TIGR03269 316 VGTSGAGKTTLSKIIAGVL-EPTSGEV---NVRVGDEwvdmtkPGPDgrgrAKRYIGILHQEYDLYPHRTVLDNLTEAIG 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 90 LKTPKE----------QTDGEVEVLVEETLSQLglthvQHSLigggagkrgiSGGERKRVAVAVELVARPSVLLLDEPTS 159
Cdd:TIGR03269 392 LELPDElarmkavitlKMVGFDEEKAEEILDKY-----PDEL----------SEGERHRVALAQVLIKEPRIVILDEPTG 456
|
170 180 190
....*....|....*....|....*....|
gi 224007385 160 GLDSSTAFKLMLT-LKELASLGHAIAVVIH 188
Cdd:TIGR03269 457 TMDPITKVDVTHSiLKAREEMEQTFIIVSH 486
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1-162 |
7.60e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 60.03 E-value: 7.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLaDPTKdlidnSCIRINNE---KGTLPKRL------VGVVWQ- 70
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLL-QPTS-----GTVTIGERvitAGKKNKKLkplrkkVGIVFQf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 71 -EDLLLPNlTVHETVRFA-ARLKTPKEqtdgEVEVLVEETLSQLGLTH--VQHSLIgggagkrGISGGERKRVAVAVELV 146
Cdd:PRK13634 94 pEHQLFEE-TVEKDICFGpMNFGVSEE----DAKQKAREMIELVGLPEelLARSPF-------ELSGGQMRRVAIAGVLA 161
|
170
....*....|....*.
gi 224007385 147 ARPSVLLLDEPTSGLD 162
Cdd:PRK13634 162 MEPEVLVLDEPTAGLD 177
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1-191 |
9.61e-10 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 60.92 E-value: 9.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLAdPT--KDLIDNSCIRiNNEKGTLpKRLVGVVWQEDLLLPNl 78
Cdd:COG4618 345 RPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWP-PTagSVRLDGADLS-QWDREEL-GRHIGYLPQDVELFDG- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 79 TVHETVrfaARLKTPkeqtDGEvevLVEETLSQLGLthvqHSLIGG---------GAGKRGISGGERKRVAVAVELVARP 149
Cdd:COG4618 421 TIAENI---ARFGDA----DPE---KVVAAAKLAGV----HEMILRlpdgydtriGEGGARLSGGQRQRIGLARALYGDP 486
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 224007385 150 SVLLLDEPTSGLDSSTAFKLMLTLKELASLGHAIAVVIHQPR 191
Cdd:COG4618 487 RLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS 528
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
4-193 |
1.31e-09 |
|
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: 57.33 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSvaAGLLADPTKDLIDnscirinnekgtlpkrlvgvvwqedlLLPNLTVHET 83
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLYASGKARLIS--------------------------FLPKFSRNKL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 84 VrFAARLKTpkeqtdgevevlveetLSQLGLTHVQhslIGGGAGKrgISGGERKRVAVAVELVARP--SVLLLDEPTSGL 161
Cdd:cd03238 63 I-FIDQLQF----------------LIDVGLGYLT---LGQKLST--LSGGELQRVKLASELFSEPpgTLFILDEPSTGL 120
|
170 180 190
....*....|....*....|....*....|..
gi 224007385 162 DSSTAFKLMLTLKELASLGHAIAVVIHQPRTS 193
Cdd:cd03238 121 HQQDINQLLEVIKGLIDLGNTVILIEHNLDVL 152
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1-185 |
1.59e-09 |
|
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: 60.33 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLADptkdlidnscirINNEKGTLPKRLVGVVWQEDLLLPNLTV 80
Cdd:TIGR03719 18 KEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKD------------FNGEARPQPGIKVGYLPQEPQLDPTKTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 81 HETV------------RF---AARLKTPKEQTD------GEVEVLVE-----ETLSQLGLTHVQHSLIGGGAGKRGISGG 134
Cdd:TIGR03719 86 RENVeegvaeikdaldRFneiSAKYAEPDADFDklaaeqAELQEIIDaadawDLDSQLEIAMDALRCPPWDADVTKLSGG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 224007385 135 ERKRVAVAVELVARPSVLLLDEPTSGLDSSTAFKLMLTLKELAslGHAIAV 185
Cdd:TIGR03719 166 ERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYP--GTVVAV 214
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
4-218 |
1.69e-09 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 59.66 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLaDPTKD--LIDNSCI-RINN-EKGTLPKRLVGVVWQEDLLLPNLT 79
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLI-EPTRGqvLIDGVDIaKISDaELREVRRKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 80 VHETVRFAARLKTPKEQTDGEVEVlveETLSQLGLTHVQHSLigggagKRGISGGERKRVAVAVELVARPSVLLLDEPTS 159
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKAL---DALRQVGLENYAHSY------PDELSGGMRQRVGLARALAINPDILLMDEAFS 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 224007385 160 GLDSSTAFKLMLTLKELASLGHAIAVVIHQPRTSIFNLFDNLLLLQKGNVVYEGKASEV 218
Cdd:PRK10070 194 ALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
3-170 |
1.91e-09 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 57.48 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSvaaGLLADptkdlidnscIRINNEKGTLPKRlVGVVWQEDLLLpNLTVHE 82
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLS---ALLGE----------LEKLSGSVSVPGS-IAYVSQEPWIQ-NGTIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 83 TVRFAARLKTPKEQtdgevEVL----VEETLSQLG---LTHVqhsligggaGKRGI--SGGERKRVAVAVELVARPSVLL 153
Cdd:cd03250 85 NILFGKPFDEERYE-----KVIkacaLEPDLEILPdgdLTEI---------GEKGInlSGGQKQRISLARAVYSDADIYL 150
|
170
....*....|....*..
gi 224007385 154 LDEPTSGLDSSTAFKLM 170
Cdd:cd03250 151 LDDPLSAVDAHVGRHIF 167
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
4-234 |
2.55e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 58.48 E-value: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLADPT-KDLIDNSCIRINNEKGTLPKRL---VGVVWQ-EDLLLPNL 78
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETgQTIVGDYAIPANLKKIKEVKRLrkeIGLVFQfPEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 79 TVHETVRFA-ARLKTPKEQTDGEVEVLVEetLSQLGLTHVQHSLIGggagkrgISGGERKRVAVAVELVARPSVLLLDEP 157
Cdd:PRK13645 107 TIEKDIAFGpVNLGENKQEAYKKVPELLK--LVQLPEDYVKRSPFE-------LSGGQKRRVALAGIIAMDGNTLVLDEP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 158 TSGLDSSTAFKLM-LTLKELASLGHAIAVVIHQpRTSIFNLFDNLLLLQKGNVVYEGKASEVKRYLEacpLCTKL---PP 233
Cdd:PRK13645 178 TGGLDPKGEEDFInLFERLNKEYKKRIIMVTHN-MDQVLRIADEVIVMHEGKVISIGSPFEIFSNQE---LLTKIeidPP 253
|
.
gi 224007385 234 E 234
Cdd:PRK13645 254 K 254
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1-191 |
3.34e-09 |
|
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: 56.77 E-value: 3.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGllaDPTKDLIDNScIRINNEKGT-LP-----KRLVGVVWQEDLL 74
Cdd:cd03217 13 KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG---HPKYEVTEGE-ILFKGEDITdLPpeeraRLGIFLAFQYPPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 75 LPNLTVHETVRFaarlktpkeqtdgevevlVEEtlsqlglthvqhsligggagkrGISGGERKRVAVAVELVARPSVLLL 154
Cdd:cd03217 89 IPGVKNADFLRY------------------VNE----------------------GFSGGEKKRNEILQLLLLEPDLAIL 128
|
170 180 190
....*....|....*....|....*....|....*...
gi 224007385 155 DEPTSGLDsSTAFKLML-TLKELASLGHAIAVVIHQPR 191
Cdd:cd03217 129 DEPDSGLD-IDALRLVAeVINKLREEGKSVLIITHYQR 165
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-189 |
3.46e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.91 E-value: 3.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLADptkdliDNSCIRINnekGTLPKRL-------VGV--VWQEDL 73
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPP------DSGTLEIG---GNPCARLtpakahqLGIylVPQEPL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 74 LLPNLTVHETVRFaaRLktPKEQTDGE-VEVLVEETLSQLGLtHVQhsligggAGKRGISggERKRVAVAVELVARPSVL 152
Cdd:PRK15439 97 LFPNLSVKENILF--GL--PKRQASMQkMKQLLAALGCQLDL-DSS-------AGSLEVA--DRQIVEILRGLMRDSRIL 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 224007385 153 LLDEPTSGLDSSTAFKLMLTLKELASLGHAIAVVIHQ 189
Cdd:PRK15439 163 ILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHK 199
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-188 |
3.61e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 57.82 E-value: 3.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLAdPTKDLIDNSCIRINNEKGTLPKRLVGVVWQE-DLLLPNLTVHE 82
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYL-PQRGRVKVMGREVNAENEKWVRSKVGLVFQDpDDQVFSSTVWD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 83 TVRFAARlktPKEQTDGEVEVLVEETLSQLGLTHVQHSligggaGKRGISGGERKRVAVAVELVARPSVLLLDEPTSGLD 162
Cdd:PRK13647 100 DVAFGPV---NMGLDKDEVERRVEEALKAVRMWDFRDK------PPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLD 170
|
170 180
....*....|....*....|....*.
gi 224007385 163 SSTAFKLMLTLKELASLGHAIAVVIH 188
Cdd:PRK13647 171 PRGQETLMEILDRLHNQGKTVIVATH 196
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
3-189 |
4.89e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 57.29 E-value: 4.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSvAAGLLADPTKDLI--DNSCIRINNEKG------------TLPKRLVgVV 68
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLR-CINFLEKPSEGSIvvNGQTINLVRDKDgqlkvadknqlrLLRTRLT-MV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 69 WQEDLLLPNLTVHETVrfaarLKTPKE---QTDGEVEVLVEETLSQLGLTHVQHsliggGAGKRGISGGERKRVAVAVEL 145
Cdd:PRK10619 98 FQHFNLWSHMTVLENV-----MEAPIQvlgLSKQEARERAVKYLAKVGIDERAQ-----GKYPVHLSGGQQQRVSIARAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 224007385 146 VARPSVLLLDEPTSGLDSSTAFKLMLTLKELASLGHAIAVVIHQ 189
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-176 |
4.96e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 58.56 E-value: 4.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 2 SILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLADPTKDLIDNSCIRINNEKGTLP-KRLVGVVWQE--DLLLPNL 78
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGEIWFDGQPLHNLNRRQLLPvRHRIQVVFQDpnSSLNPRL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 79 TVHETVRFAARLKTPkEQTDGEVEVLVEETLSQLGL-THVQHSLIGGgagkrgISGGERKRVAVAVELVARPSVLLLDEP 157
Cdd:PRK15134 380 NVLQIIEEGLRVHQP-TLSAAQREQQVIAVMEEVGLdPETRHRYPAE------FSGGQRQRIAIARALILKPSLIILDEP 452
|
170
....*....|....*....
gi 224007385 158 TSGLDSSTAFKLMLTLKEL 176
Cdd:PRK15134 453 TSSLDKTVQAQILALLKSL 471
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
3-177 |
6.17e-09 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 55.40 E-value: 6.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLaDPTKDLIDNSCIRINNEKGTLPKrLVGVVWQEDLLlpnltvhe 82
Cdd:cd03247 17 VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDL-KPQQGEITLDGVPVSDLEKALSS-LISVLNQRPYL-------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 83 tvrFAARLktpkeqtdgevevlveetLSQLGlthvqhsligggagkRGISGGERKRVAVAVELVARPSVLLLDEPTSGLD 162
Cdd:cd03247 87 ---FDTTL------------------RNNLG---------------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLD 130
|
170
....*....|....*
gi 224007385 163 SSTAFKLMLTLKELA 177
Cdd:cd03247 131 PITERQLLSLIFEVL 145
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-226 |
6.49e-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: 58.28 E-value: 6.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLA-DPTKDLID------NSCIRIN--NEKGTLPKRLVGVVWQEDL 73
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyEPTSGRIIyhvalcEKCGYVErpSKVGEPCPVCGGTLEPEEV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 74 LLPNLTVHETVRFAARLKTPKEQT-----DGEVEVLVEETLSQLG---------------LTHVQHSLIGGGagkRGISG 133
Cdd:TIGR03269 95 DFWNLSDKLRRRIRKRIAIMLQRTfalygDDTVLDNVLEALEEIGyegkeavgravdlieMVQLSHRITHIA---RDLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 134 GERKRVAVAVELVARPSVLLLDEPTSGLDSSTAFKLMLTLKELASlGHAIAVVI--HQPRTsIFNLFDNLLLLQKGNVVY 211
Cdd:TIGR03269 172 GEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVK-ASGISMVLtsHWPEV-IEDLSDKAIWLENGEIKE 249
|
250
....*....|....*.
gi 224007385 212 EGKASEV-KRYLEACP 226
Cdd:TIGR03269 250 EGTPDEVvAVFMEGVS 265
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-189 |
6.95e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.87 E-value: 6.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLlADPTKDLIDNSCIRINNEKGTLPKRL-VGVVWQEDLLLPNLTVHE 82
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGI-HEPTKGTITINNINYNKLDHKLAAQLgIGIIYQELSVIDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 83 TVrFAARLKTPK----EQTD-GEVEVLVEETLSQLGLTHVQHSLIGGgagkrgISGGERKRVAVAVELVARPSVLLLDEP 157
Cdd:PRK09700 100 NL-YIGRHLTKKvcgvNIIDwREMRVRAAMMLLRVGLKVDLDEKVAN------LSISHKQMLEIAKTLMLDAKVIIMDEP 172
|
170 180 190
....*....|....*....|....*....|..
gi 224007385 158 TSGLDSSTAFKLMLTLKELASLGHAIAVVIHQ 189
Cdd:PRK09700 173 TSSLTNKEVDYLFLIMNQLRKEGTAIVYISHK 204
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
21-186 |
8.35e-09 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 56.99 E-value: 8.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 21 GPSGSGKTSLVSVAAGLLADPT----------KDLIDNScirinnekgtlPKRL-------VGVVWQEDL--LLPNLTVH 81
Cdd:COG0444 38 GESGSGKSTLARAILGLLPPPGitsgeilfdgEDLLKLS-----------EKELrkirgreIQMIFQDPMtsLNPVMTVG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 82 ETVRFAARLKTPKeqTDGEVEVLVEETLSQLGLTHVQ-------HSLigggagkrgiSGGERKRVAVAVELVARPSVLLL 154
Cdd:COG0444 107 DQIAEPLRIHGGL--SKAEARERAIELLERVGLPDPErrldrypHEL----------SGGMRQRVMIARALALEPKLLIA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 224007385 155 DEPTSGLDSSTAFKLMLTLKEL-ASLG-------HAIAVV 186
Cdd:COG0444 175 DEPTTALDVTIQAQILNLLKDLqRELGlailfitHDLGVV 214
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-188 |
1.01e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 56.31 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLA-DPTKDLIDNSCI-RINNEKGTLPKRLVGVVWQEDLLLPNL 78
Cdd:PRK11831 20 RCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIApDHGEILFDGENIpAMSRSRLYTVRKRMSMLFQSGALFTDM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 79 TVHETVRFAARlktpkEQTDGEVEVL---VEETLSQLGLThvqhsliggGAGK---RGISGGERKRVAVAVELVARPSVL 152
Cdd:PRK11831 100 NVFDNVAYPLR-----EHTQLPAPLLhstVMMKLEAVGLR---------GAAKlmpSELSGGMARRAALARAIALEPDLI 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 224007385 153 LLDEPTSGLDSSTAFKLMLTLKEL-ASLGHAIAVVIH 188
Cdd:PRK11831 166 MFDEPFVGQDPITMGVLVKLISELnSALGVTCVVVSH 202
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
4-213 |
1.17e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 56.33 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLaDPTKDLIDNSCIRINN---EKGTLPKR-LVGVVWQ--EDLLLPN 77
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALL-KPTTGTVTVDDITITHktkDKYIRPVRkRIGMVFQfpESQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 78 lTVHETVRFAAR-LKTPKEqtdgEVEVLVEETLSQLGLTHVQHSLigggaGKRGISGGERKRVAVAVELVARPSVLLLDE 156
Cdd:PRK13646 102 -TVEREIIFGPKnFKMNLD----EVKNYAHRLLMDLGFSRDVMSQ-----SPFQMSGGQMRKIAIVSILAMNPDIIVLDE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 224007385 157 PTSGLDSSTAFKLMLTLKELA-SLGHAIAVVIHQpRTSIFNLFDNLLLLQKGNVVYEG 213
Cdd:PRK13646 172 PTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHD-MNEVARYADEVIVMKEGSIVSQT 228
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
4-176 |
1.72e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 55.86 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLAdPTKDLIDNSCIRINNEKGTLPKR-LVGVVWQE-DLLLPNLTVH 81
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLI-PSEGKVYVDGLDTSDEENLWDIRnKAGMVFQNpDNQIVATIVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 82 ETVRFAAR-LKTPKEqtdgEVEVLVEETLSQLGLT----HVQHSLigggagkrgiSGGERKRVAVAVELVARPSVLLLDE 156
Cdd:PRK13633 105 EDVAFGPEnLGIPPE----EIRERVDESLKKVGMYeyrrHAPHLL----------SGGQKQRVAIAGILAMRPECIIFDE 170
|
170 180
....*....|....*....|
gi 224007385 157 PTSGLDSSTAFKLMLTLKEL 176
Cdd:PRK13633 171 PTAMLDPSGRREVVNTIKEL 190
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-164 |
2.18e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 54.72 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLaDPTKDLIdnscIRINNEKGTLP----KRLVGVVWQEDLLLP 76
Cdd:PRK10247 20 AKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLI-SPTSGTL----LFEGEDISTLKpeiyRQQVSYCAQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 77 NlTVHETVRFA--ARLKTPKEQTdgevevlVEETLSQLGLThvQHSLigggagKRGI---SGGERKRVAVAVELVARPSV 151
Cdd:PRK10247 95 D-TVYDNLIFPwqIRNQQPDPAI-------FLDDLERFALP--DTIL------TKNIaelSGGEKQRISLIRNLQFMPKV 158
|
170
....*....|...
gi 224007385 152 LLLDEPTSGLDSS 164
Cdd:PRK10247 159 LLLDEITSALDES 171
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-188 |
2.40e-08 |
|
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: 53.20 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLAdPTKdlidnSCIRINNEKgtlpkrlvgvvwqedlllpnltvhet 83
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYK-PDS-----GEILVDGKE-------------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 84 VRFAarlkTPKEqtdgevevlveetlsqlglthvqhsligggAGKRGI------SGGERKRVAVAVELVARPSVLLLDEP 157
Cdd:cd03216 64 VSFA----SPRD------------------------------ARRAGIamvyqlSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190
....*....|....*....|....*....|.
gi 224007385 158 TSGLDSSTAFKLMLTLKELASLGHAIAVVIH 188
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQGVAVIFISH 140
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
3-175 |
2.55e-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: 54.42 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVaagL--LADPTKdlidnSCIRINNEK-GTLP----KRLVGVVWQEDLLL 75
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLA---LfrLVELSS-----GSILIDGVDiSKIGlhdlRSRISIIPQDPVLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 76 PNltvheTVRFaaRLKTPKEQTDGEVEvlveETLSQLGLTHVQHSLIGGG-----AGKRGISGGERKRVAVAVELVARPS 150
Cdd:cd03244 91 SG-----TIRS--NLDPFGEYSDEELW----QALERVGLKEFVESLPGGLdtvveEGGENLSVGQRQLLCLARALLRKSK 159
|
170 180
....*....|....*....|....*
gi 224007385 151 VLLLDEPTSGLDSSTAFKLMLTLKE 175
Cdd:cd03244 160 ILVLDEATASVDPETDALIQKTIRE 184
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-162 |
2.93e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 54.04 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGlLADPtkdliDNSCIRINNEkgtlPKRLVGVVWQEDLLL----- 75
Cdd:PRK13538 14 RILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAG-LARP-----DAGEVLWQGE----PIRRQRDEYHQDLLYlghqp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 76 ---PNLTVHETVRFAARLKTPkeqTDGEVevlVEETLSQLGLTHVQHSLIgggagkRGISGGERKRVAVAVELVARPSVL 152
Cdd:PRK13538 84 gikTELTALENLRFYQRLHGP---GDDEA---LWEALAQVGLAGFEDVPV------RQLSAGQQRRVALARLWLTRAPLW 151
|
170
....*....|
gi 224007385 153 LLDEPTSGLD 162
Cdd:PRK13538 152 ILDEPFTAID 161
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-273 |
2.95e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 54.99 E-value: 2.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLADPTKDLIDNSCIRINNEKGTLPKRLVGVVWQE-DLLLPNLTVHE 82
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGIVFQNpETQFVGRTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 83 TVRFAAR-LKTPKEqtdgEVEVLVEETLSQLGLTHVQHSligggaGKRGISGGERKRVAVAVELVARPSVLLLDEPTSGL 161
Cdd:PRK13644 98 DLAFGPEnLCLPPI----EIRKRVDRALAEIGLEKYRHR------SPKTLSGGQGQCVALAGILTMEPECLIFDEVTSML 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 162 DSSTAFKLMLTLKELASLGHAIAVVIHQPRTsiFNLFDNLLLLQKGNVVYEGKASEVKRYLEACPLCTKLPPETGLADWL 241
Cdd:PRK13644 168 DPDSGIAVLERIKKLHEKGKTIVYITHNLEE--LHDADRIIVMDRGKIVLEGEPENVLSDVSLQTLGLTPPSLIELAENL 245
|
250 260 270
....*....|....*....|....*....|..
gi 224007385 242 mdmidedekRDGGGKLPalWKNHSSKQPQAND 273
Cdd:PRK13644 246 ---------KMHGVVIP--WENTSSPSSFAEE 266
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
4-188 |
3.07e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 54.89 E-value: 3.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLADPTKDLidnSCIRINNEKGtLPKRLVGVVWQE---DLLLPNLTv 80
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKI---SILGQPTRQA-LQKNLVAYVPQSeevDWSFPVLV- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 81 hETVRFAAR------LKTPKEQtDGEVevlVEETLSQLGLTHVQHSLIGGgagkrgISGGERKRVAVAVELVARPSVLLL 154
Cdd:PRK15056 98 -EDVVMMGRyghmgwLRRAKKR-DRQI---VTAALARVDMVEFRHRQIGE------LSGGQKKRVFLARAIAQQGQVILL 166
|
170 180 190
....*....|....*....|....*....|....
gi 224007385 155 DEPTSGLDSSTAFKLMLTLKELASLGHAIAVVIH 188
Cdd:PRK15056 167 DEPFTGVDVKTEARIISLLRELRDEGKTMLVSTH 200
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-177 |
3.40e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 54.72 E-value: 3.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLADPTKDLIDNSCI----RINNEKGTLP-KRLVGVVWQEDLLL 75
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLlggrSIFNYRDVLEfRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 76 PnLTVHETVRFAARLK--TPKEQTDGevevLVEETLSQLGLTHVQHSLIGGGAGKrgISGGERKRVAVAVELVARPSVLL 153
Cdd:PRK14271 114 P-MSIMDNVLAGVRAHklVPRKEFRG----VAQARLTEVGLWDAVKDRLSDSPFR--LSGGQQQLLCLARTLAVNPEVLL 186
|
170 180
....*....|....*....|....
gi 224007385 154 LDEPTSGLDSSTAFKLMLTLKELA 177
Cdd:PRK14271 187 LDEPTSALDPTTTEKIEEFIRSLA 210
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-183 |
3.51e-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: 3.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLadpTKD----LIDNSCIRINN-----EKGtlpkrlVGVVWQEDLL 74
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVY---QPDsgeiLLDGEPVRFRSprdaqAAG------IAIIHQELNL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 75 LPNLTVHETVrFAARLKTPKEQTD-GEVEVLVEETLSQLGL-----THVqhsligggagkRGISGGERKRVAVAVELVAR 148
Cdd:COG1129 91 VPNLSVAENI-FLGREPRRGGLIDwRAMRRRARELLARLGLdidpdTPV-----------GDLSVAQQQLVEIARALSRD 158
|
170 180 190
....*....|....*....|....*....|....*
gi 224007385 149 PSVLLLDEPTSGLDSSTAFKLMLTLKELASLGHAI 183
Cdd:COG1129 159 ARVLILDEPTASLTEREVERLFRIIRRLKAQGVAI 193
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
4-192 |
3.68e-08 |
|
ATP-binding cassette domain I 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: 213237 [Multi-domain] Cd Length: 226 Bit Score: 54.19 E-value: 3.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSL----------------VSVAA----GLLADPTKDLIDNSCIRINNEKGTL--- 60
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryvesLSAYArqflGQMDKPDVDSIEGLSPAIAIDQKTTsrn 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 61 PKRLVGvvwqedlllpnlTVHETVRFAaRLKTPKEQTDGEVEVLVEETLSQLGLTHVQHSLigggagkrgiSGGERKRVA 140
Cdd:cd03270 91 PRSTVG------------TVTEIYDYL-RLLFARVGIRERLGFLVDVGLGYLTLSRSAPTL----------SGGEAQRIR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 224007385 141 VAVELVARPSVLL--LDEPTSGLDSSTAFKLMLTLKELASLGHAIAVVIHQPRT 192
Cdd:cd03270 148 LATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDT 201
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-188 |
4.12e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 54.84 E-value: 4.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLADptkdliDNSCIRINNE----KGTLPKRLVGVVWQEDLLLP 76
Cdd:PRK13536 54 KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSP------DAGKITVLGVpvpaRARLARARIGVVPQFDNLDL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 77 NLTVHETVRFAARLKTPKEQTdgevevlVEETLSQLglthVQHSLIGGGAGKR--GISGGERKRVAVAVELVARPSVLLL 154
Cdd:PRK13536 128 EFTVRENLLVFGRYFGMSTRE-------IEAVIPSL----LEFARLESKADARvsDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190
....*....|....*....|....*....|....
gi 224007385 155 DEPTSGLDSSTAFKLMLTLKELASLGHAIAVVIH 188
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERLRSLLARGKTILLTTH 230
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
3-176 |
4.36e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 54.35 E-value: 4.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLL-ADPTKDLIDNSCIRINN--EKgtlpKRLVGVVWQE-DLLLPNL 78
Cdd:PRK13650 22 TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLeAESGQIIIDGDLLTEENvwDI----RHKIGMVFQNpDNQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 79 TVHETVRFAARLKTPKEQtdgEVEVLVEETLSQLGLTHVQhsligggagKRG---ISGGERKRVAVAVELVARPSVLLLD 155
Cdd:PRK13650 98 TVEDDVAFGLENKGIPHE---EMKERVNEALELVGMQDFK---------EREparLSGGQKQRVAIAGAVAMRPKIIILD 165
|
170 180
....*....|....*....|.
gi 224007385 156 EPTSGLDSSTAFKLMLTLKEL 176
Cdd:PRK13650 166 EATSMLDPEGRLELIKTIKGI 186
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-177 |
5.00e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 55.60 E-value: 5.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 2 SILSDVSTKISPYQLTAWMGPSGSGKTSLVSvaagLLA---DPTKD--LIDNSCIRINNEKgTLpKRLVGVVWQEDLLLp 76
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQ----LLTrawDPQQGeiLLNGQPIADYSEA-AL-RQAISVVSQRVHLF- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 77 NLTVHETVRFAArlktpKEQTDgevEVLVEeTLSQLGLthvqHSLIGG--------GAGKRGISGGERKRVAVAVELVAR 148
Cdd:PRK11160 427 SATLRDNLLLAA-----PNASD---EALIE-VLQQVGL----EKLLEDdkglnawlGEGGRQLSGGEQRRLGIARALLHD 493
|
170 180
....*....|....*....|....*....
gi 224007385 149 PSVLLLDEPTSGLDSSTAFKLMLTLKELA 177
Cdd:PRK11160 494 APLLLLDEPTEGLDAETERQILELLAEHA 522
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1-166 |
6.31e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 55.51 E-value: 6.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLAdPTKDliDNSCIRinnekGTlpkrlVGVVWQEDLLLpNLTV 80
Cdd:PLN03130 630 RPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELP-PRSD--ASVVIR-----GT-----VAYVPQVSWIF-NATV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 81 HETVRFAARLKTPKeqtdgevevlVEETLSQLGLTHVQHSLIGGG---AGKRG--ISGGERKRVAVAVELVARPSVLLLD 155
Cdd:PLN03130 696 RDNILFGSPFDPER----------YERAIDVTALQHDLDLLPGGDlteIGERGvnISGGQKQRVSMARAVYSNSDVYIFD 765
|
170
....*....|.
gi 224007385 156 EPTSGLDSSTA 166
Cdd:PLN03130 766 DPLSALDAHVG 776
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-162 |
6.47e-08 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 55.07 E-value: 6.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLAdPTKdlidnscirinnekGTLpKRLVGVVW----QE-DLLL 75
Cdd:COG0488 328 KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELE-PDS--------------GTV-KLGETVKIgyfdQHqEELD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 76 PNLTVHETVRFAArlktpkeqtDGEVEVLVEETLSQLGLT-HVQHSLIGGgagkrgISGGERKRVAVAVELVARPSVLLL 154
Cdd:COG0488 392 PDKTVLDELRDGA---------PGGTEQEVRGYLGRFLFSgDDAFKPVGV------LSGGEKARLALAKLLLSPPNVLLL 456
|
....*...
gi 224007385 155 DEPTSGLD 162
Cdd:COG0488 457 DEPTNHLD 464
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-189 |
8.39e-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: 54.45 E-value: 8.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLADPTKD---LIDNSCIRINNEKGTLPKRLVgVVWQEDLLLPNLTV 80
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDgeiYWSGSPLKASNIRDTERAGIV-IIHQELTLVPELSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 81 HETVRFAARLKTPKEQTDGEVEVL-VEETLSQLGLTHVQHSLIGGGAGkrgisGGERKRVAVAVELVARPSVLLLDEPTS 159
Cdd:TIGR02633 96 AENIFLGNEITLPGGRMAYNAMYLrAKNLLRELQLDADNVTRPVGDYG-----GGQQQLVEIAKALNKQARLLILDEPSS 170
|
170 180 190
....*....|....*....|....*....|
gi 224007385 160 GLDSSTAFKLMLTLKELASLGHAIAVVIHQ 189
Cdd:TIGR02633 171 SLTEKETEILLDIIRDLKAHGVACVYISHK 200
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
4-166 |
9.48e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.98 E-value: 9.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLADptkdlIDNSCIRINNEKGTLPKrlvgVVWqedllLPNLTVHET 83
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSH-----AETSSVVIRGSVAYVPQ----VSW-----IFNATVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 84 VRFAARLKTpkeqtdgevevlvEETLSQLGLTHVQHSL--IGG----GAGKRG--ISGGERKRVAVAVELVARPSVLLLD 155
Cdd:PLN03232 699 ILFGSDFES-------------ERYWRAIDVTALQHDLdlLPGrdltEIGERGvnISGGQKQRVSMARAVYSNSDIYIFD 765
|
170
....*....|.
gi 224007385 156 EPTSGLDSSTA 166
Cdd:PLN03232 766 DPLSALDAHVA 776
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
21-162 |
1.06e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 53.69 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 21 GPSGSGKTSLVSVAAGLLADPTKDL-IDNSciRINNEKgtlPK-RLVGVVWQEDLLLPNLTVHETVRFAARL-KTPKEqt 97
Cdd:PRK11650 37 GPSGCGKSTLLRMVAGLERITSGEIwIGGR--VVNELE---PAdRDIAMVFQNYALYPHMSVRENMAYGLKIrGMPKA-- 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224007385 98 dgEVEVLVEETLSQLGLthvqhsligggaGK------RGISGGERKRVAVAVELVARPSVLLLDEPTSGLD 162
Cdd:PRK11650 110 --EIEERVAEAARILEL------------EPlldrkpRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
1-224 |
1.12e-07 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 52.65 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGllaDPtKDLIDNSCIRINNE------------KGtlpkrlVGVV 68
Cdd:TIGR01978 13 KEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAG---HP-SYEVTSGTILFKGQdllelepderarAG------LFLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 69 WQEDLLLPNLTVHETVRFA--ARLKTPKEQT--DGEVEVLVEETLSQLGLT--HVQHSLigggagKRGISGGERKRVAVA 142
Cdd:TIGR01978 83 FQYPEEIPGVSNLEFLRSAlnARRSARGEEPldLLDFEKLLKEKLALLDMDeeFLNRSV------NEGFSGGEKKRNEIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 143 VELVARPSVLLLDEPTSGLDSStAFKLML-TLKELASLGHAIAVVIHQPRTSIFNLFDNLLLLQKGNVVYEGKASEVKRy 221
Cdd:TIGR01978 157 QMALLEPKLAILDEIDSGLDID-ALKIVAeGINRLREPDRSFLIITHYQRLLNYIKPDYVHVLLDGRIVKSGDVELAKE- 234
|
...
gi 224007385 222 LEA 224
Cdd:TIGR01978 235 LEA 237
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
21-176 |
1.14e-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: 54.31 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 21 GPSGSGKTSLvsvAAGLLAdptkdLIDNS-CIRIN-------NEKGTLPKRL-VGVVWQEDL--LLPNLTVHETVRFAAR 89
Cdd:COG4172 319 GESGSGKSTL---GLALLR-----LIPSEgEIRFDgqdldglSRRALRPLRRrMQVVFQDPFgsLSPRMTVGQIIAEGLR 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 90 LKTPkEQTDGEVEVLVEETLSQLGLThvqhsligGGAGKRGI---SGGERKRVAVAVELVARPSVLLLDEPTSGLDSSTA 166
Cdd:COG4172 391 VHGP-GLSAAERRARVAEALEEVGLD--------PAARHRYPhefSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQ 461
|
170
....*....|
gi 224007385 167 FKLMLTLKEL 176
Cdd:COG4172 462 AQILDLLRDL 471
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-188 |
1.28e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 53.85 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLAdptkdlIDNSCIRINNEKGTL--PKRL----VGVVWQEDLLLPN 77
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYT------RDAGSILYLGKEVTFngPKSSqeagIGIIHQELNLIPQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 78 LTVHETVrFAARLKTPK------EQTDGEVEVLveetLSQLGLTHVQHSLIGGgagkrgISGGERKRVAVAVELVARPSV 151
Cdd:PRK10762 94 LTIAENI-FLGREFVNRfgridwKKMYAEADKL----LARLNLRFSSDKLVGE------LSIGEQQMVEIAKVLSFESKV 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 224007385 152 LLLDEPTSGL-DSSTAfKLMLTLKELASLGHAIAVVIH 188
Cdd:PRK10762 163 IIMDEPTDALtDTETE-SLFRVIRELKSQGRGIVYISH 199
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-223 |
1.57e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 52.69 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLaDPTKDLIDNSCIRINNEKGTLPKRLVGVVWQE-DLLLPNLTVH 81
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLL-KPQSGEIKIDGITISKENLKEIRKKIGIIFQNpDNQFIGATVE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 82 ETVRFAA--RLKTPKEQTDgevevLVEETLSQLG----LTHVQHSLigggagkrgiSGGERKRVAVAVELVARPSVLLLD 155
Cdd:PRK13632 103 DDIAFGLenKKVPPKKMKD-----IIDDLAKKVGmedyLDKEPQNL----------SGGQKQRVAIASVLALNPEIIIFD 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 224007385 156 EPTSGLD---SSTAFKLMLTL-----KELASLGHAIAVVIHQPRTSIFNlfdnllllqKGNVVYEGKASEV---KRYLE 223
Cdd:PRK13632 168 ESTSMLDpkgKREIKKIMVDLrktrkKTLISITHDMDEAILADKVIVFS---------EGKLIAQGKPKEIlnnKEILE 237
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
21-162 |
1.80e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.58 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 21 GPSGSGKTSLVSVAAGLlaDptKDlidnscirINNEKGTLPKRLVGVVWQEDLLLPNLTVHETV------------RF-- 86
Cdd:PRK11819 40 GLNGAGKSTLLRIMAGV--D--KE--------FEGEARPAPGIKVGYLPQEPQLDPEKTVRENVeegvaevkaaldRFne 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 87 -AARLKTPKEQTD------GEVEVLVE-----ETLSQL-----------GLTHVQHsligggagkrgISGGERKRVAVAV 143
Cdd:PRK11819 108 iYAAYAEPDADFDalaaeqGELQEIIDaadawDLDSQLeiamdalrcppWDAKVTK-----------LSGGERRRVALCR 176
|
170
....*....|....*....
gi 224007385 144 ELVARPSVLLLDEPTSGLD 162
Cdd:PRK11819 177 LLLEKPDMLLLDEPTNHLD 195
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1-165 |
2.25e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 51.99 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLADPTKDLIDNSCIRINNEKGTlpkRLVgvvWQEDLLLPNLTV 80
Cdd:PRK11247 25 RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDT---RLM---FQDARLLPWKKV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 81 HETVRFAARlktpkeqtdGEVEVLVEETLSQLGLTHvqhsliGGGAGKRGISGGERKRVAVAVELVARPSVLLLDEPTSG 160
Cdd:PRK11247 99 IDNVGLGLK---------GQWRDAALQALAAVGLAD------RANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
....*
gi 224007385 161 LDSST 165
Cdd:PRK11247 164 LDALT 168
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
4-187 |
2.63e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 52.02 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLADptkdliDNSCIRINNEKGTLP-----KRLVGVVWQE-DLLLPN 77
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEE------FEGKVKIDGELLTAEnvwnlRRKIGMVFQNpDNQFVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 78 LTVHETVRFAARLK-TPKEqtdgEVEVLVEETLSQLGLTHVQHSligggaGKRGISGGERKRVAVAVELVARPSVLLLDE 156
Cdd:PRK13642 97 ATVEDDVAFGMENQgIPRE----EMIKRVDEALLAVNMLDFKTR------EPARLSGGQKQRVAVAGIIALRPEIIILDE 166
|
170 180 190
....*....|....*....|....*....|.
gi 224007385 157 PTSGLDSSTAFKLMLTLKELASLGHAIAVVI 187
Cdd:PRK13642 167 STSMLDPTGRQEIMRVIHEIKEKYQLTVLSI 197
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-194 |
2.83e-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: 51.26 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 2 SILSDVSTKISPYQLTAWMGPSGSGKTSLVSvAAGLLADPtkdliDNSCIRINNEK-GTLP----KRLVGVVWQEDLLLP 76
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLIL-ALFRFLEA-----EEGKIEIDGIDiSTIPledlRSSLTIIPQDPTLFS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 77 NltvheTVRfaARLKTPKEQTDGEV-EVLveetlsqlglthvqhSLIGGGAGkrgISGGERKRVAVAVELVARPSVLLLD 155
Cdd:cd03369 96 G-----TIR--SNLDPFDEYSDEEIyGAL---------------RVSEGGLN---LSQGQRQLLCLARALLKRPRVLVLD 150
|
170 180 190
....*....|....*....|....*....|....*....
gi 224007385 156 EPTSGLDSSTAFKLMLTLKELASlGHAIAVVIHQPRTSI 194
Cdd:cd03369 151 EATASIDYATDALIQKTIREEFT-NSTILTIAHRLRTII 188
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
106-219 |
3.04e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 52.43 E-value: 3.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 106 EETLSQLGLTHvqhsliGGGAGKRGISGGERKRVAVAVELVARPSVLLLDEPTSGLDSSTAFKLMLTLKELASLGhAIAV 185
Cdd:NF000106 126 DELLERFSLTE------AAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDG-ATVL 198
|
90 100 110
....*....|....*....|....*....|....
gi 224007385 186 VIHQPRTSIFNLFDNLLLLQKGNVVYEGKASEVK 219
Cdd:NF000106 199 LTTQYMEEAEQLAHELTVIDRGRVIADGKVDELK 232
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
11-188 |
3.05e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 53.48 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 11 ISPYQLTAWMGPSGSGKTSLVSVAAGLLADPTKDL------IDNSCIRINNEKGTLPkrlvgvvwQEDLLLPNLTVHETV 84
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDAtvagksILTNISDVHQNMGYCP--------QFDAIDDLLTGREHL 2033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 85 RFAARLK-TPKEqtdgEVEVLVEETLSQLGLTHVQHSLIGGgagkrgISGGERKRVAVAVELVARPSVLLLDEPTSGLDS 163
Cdd:TIGR01257 2034 YLYARLRgVPAE----EIEKVANWSIQSLGLSLYADRLAGT------YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDP 2103
|
170 180
....*....|....*....|....*
gi 224007385 164 STAFKLMLTLKELASLGHAIAVVIH 188
Cdd:TIGR01257 2104 QARRMLWNTIVSIIREGRAVVLTSH 2128
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
131-176 |
3.44e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.79 E-value: 3.44e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 224007385 131 ISGGERKRVAVAVELVARPSVLLLDEPTSGLDSSTAFKLMLTLKEL 176
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLREL 202
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
62-186 |
4.03e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.11 E-value: 4.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 62 KRLVGVVWQEDLLLpNLTVHETVRFAARLKTPKEQTDGEVEVLVEETLSQLGlthVQHSLIGGGAGKrGISGGERKRVAV 141
Cdd:PTZ00265 1295 RNLFSIVSQEPMLF-NMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLP---NKYDTNVGPYGK-SLSGGQKQRIAI 1369
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 224007385 142 AVELVARPSVLLLDEPTSGLDSSTAF---KLMLTLKELA-----SLGHAIAVV 186
Cdd:PTZ00265 1370 ARALLREPKILLLDEATSSLDSNSEKlieKTIVDIKDKAdktiiTIAHRIASI 1422
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
132-181 |
4.82e-07 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 49.46 E-value: 4.82e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 224007385 132 SGGERKRVAVAVELVARPSVLLLDEPTSGLDSSTAFKLMLTLKE----LASLGH 181
Cdd:cd03223 93 SGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKElgitVISVGH 146
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
21-187 |
6.92e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 50.32 E-value: 6.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 21 GPSGSGKTSLVSVAAGLLADPTKDLIDNSCIRinnekgTLP----KRLVGVVWQEDLLLPNLTVHETVRfaarLKTPKEQ 96
Cdd:PRK03695 29 GPNGAGKSTLLARMAGLLPGSGSIQFAGQPLE------AWSaaelARHRAYLSQQQTPPFAMPVFQYLT----LHQPDKT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 97 TDGEVEVLVEETLSQLGLTHVQHSLIGGgagkrgISGGERKRVAVA-VELVARPSV------LLLDEPTSGLDSSTAFKL 169
Cdd:PRK03695 99 RTEAVASALNEVAEALGLDDKLGRSVNQ------LSGGEWQRVRLAaVVLQVWPDInpagqlLLLDEPMNSLDVAQQAAL 172
|
170
....*....|....*...
gi 224007385 170 MLTLKELASLGhaIAVVI 187
Cdd:PRK03695 173 DRLLSELCQQG--IAVVM 188
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
132-188 |
7.13e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 51.26 E-value: 7.13e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 224007385 132 SGGERKRVAVAVELVARPSVLLLDEPTSGLDSSTAFKLMLTLKELAS-LGHAIAVVIH 188
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKReFNTAIIMITH 220
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1-162 |
8.12e-07 |
|
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: 48.60 E-value: 8.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGlladptkdlidnsciRINNEKGTLpkrlvgvvwqedlllpnlTV 80
Cdd:cd03221 13 KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAG---------------ELEPDEGIV------------------TW 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 81 HETVRFAarlktpkeqtdgevevlveeTLSQLglthvqhsligggagkrgiSGGERKRVAVAVELVARPSVLLLDEPTSG 160
Cdd:cd03221 60 GSTVKIG--------------------YFEQL-------------------SGGEKMRLALAKLLLENPNLLLLDEPTNH 100
|
..
gi 224007385 161 LD 162
Cdd:cd03221 101 LD 102
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
129-188 |
9.57e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 50.31 E-value: 9.57e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224007385 129 RGISGGERKRVAVAVELVARPSVLLLDEPTSGLDSSTAFKLMLTLKEL-ASLGHAIAVVIH 188
Cdd:PRK11701 150 TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTH 210
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
132-165 |
1.06e-06 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 49.74 E-value: 1.06e-06
10 20 30
....*....|....*....|....*....|....
gi 224007385 132 SGGERKRVAVAVELVARPSVLLLDEPTSGLDSST 165
Cdd:COG4778 154 SGGEQQRVNIARGFIADPPLLLLDEPTASLDAAN 187
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
3-194 |
1.08e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.57 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLaDPTK-DLIDNSCIRINNEKGTLPKRLVGVVWQEDLLLPNlTVH 81
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLY-DPTEgDIIINDSHNLKDINLKWWRSKIGVVSQDPLLFSN-SIK 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 82 ETVRFAA-------------------------RLKTPKEQTDGEVEVLVEETLSQlGLTHVQ------------------ 118
Cdd:PTZ00265 478 NNIKYSLyslkdlealsnyynedgndsqenknKRNSCRAKCAGDLNDMSNTTDSN-ELIEMRknyqtikdsevvdvskkv 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 119 -------------HSLIGGGAGKrgISGGERKRVAVAVELVARPSVLLLDEPTSGLDSSTAFKLMLTLKELASLGHAIAV 185
Cdd:PTZ00265 557 lihdfvsalpdkyETLVGSNASK--LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITI 634
|
....*....
gi 224007385 186 VIHQPRTSI 194
Cdd:PTZ00265 635 IIAHRLSTI 643
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
15-188 |
1.21e-06 |
|
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: 49.67 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 15 QLTAWMGPSGSGKTSLVSVAAGlladptkDLIDNSCIRINN-EKGTLPKRLVGVVWQ---EDLLLPNLTVHETVRFAARL 90
Cdd:cd03236 27 QVLGLVGPNGIGKSTALKILAG-------KLKPNLGKFDDPpDWDEILDEFRGSELQnyfTKLLEGDVKVIVKPQYVDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 91 ktPKeQTDGEVEVLVEET---------LSQLGLTHVQHSLIgggagkRGISGGERKRVAVAVELVARPSVLLLDEPTSGL 161
Cdd:cd03236 100 --PK-AVKGKVGELLKKKdergkldelVDQLELRHVLDRNI------DQLSGGELQRVAIAAALARDADFYFFDEPSSYL 170
|
170 180
....*....|....*....|....*..
gi 224007385 162 DSSTAFKLMLTLKELASLGHAIAVVIH 188
Cdd:cd03236 171 DIKQRLNAARLIRELAEDDNYVLVVEH 197
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
2-189 |
1.21e-06 |
|
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: 49.25 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 2 SILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLADPTKDLIDNSCIRINNEKGTLPKR---LVGVVWQEDLLLpNL 78
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrySVAYAAQKPWLL-NA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 79 TVHETVRFAARLKtpKEQTDGEVEVLVEETLSQLgLTHVQHSLIgggaGKRGI--SGGERKRVAVAVELVARPSVLLLDE 156
Cdd:cd03290 94 TVEENITFGSPFN--KQRYKAVTDACSLQPDIDL-LPFGDQTEI----GERGInlSGGQRQRICVARALYQNTNIVFLDD 166
|
170 180 190
....*....|....*....|....*....|....*
gi 224007385 157 PTSGLDSSTAFKLMLT--LKELASLGHAIAVVIHQ 189
Cdd:cd03290 167 PFSALDIHLSDHLMQEgiLKFLQDDKRTLVLVTHK 201
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
132-186 |
1.44e-06 |
|
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: 48.58 E-value: 1.44e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 224007385 132 SGGERKRVAVAVELVARPSVLLLDEPTSGLDSSTAFKLMLTLKELASLGHAIAVV 186
Cdd:cd03215 106 SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLI 160
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
132-188 |
2.04e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 49.58 E-value: 2.04e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 224007385 132 SGGERKRVAVAVELVARPSVLLLDEPTSGLDSST---AFKLMLTLKE---LASL--GHAIAVVIH 188
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVqaqVLNLMMDLQQelgLSYVfiSHDLSVVEH 220
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
107-188 |
2.04e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 50.40 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 107 ETLSQLGLTHVQhslIGGGAGKrgISGGERKRVAVAVELVAR---PSVLLLDEPTSGLDSSTAFKLMLTLKELASLGHAI 183
Cdd:TIGR00630 811 QTLCDVGLGYIR---LGQPATT--LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTV 885
|
....*
gi 224007385 184 AVVIH 188
Cdd:TIGR00630 886 VVIEH 890
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
4-188 |
2.23e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.91 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGL-LADPTKDLIDNSCIRINNEKGTLPKRlVGVVWQEDLLLPNLTVHE 82
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNyQPDAGSILIDGQEMRFASTTAALAAG-VAIIYQELHLVPEMTVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 83 TV---RFAARLKTPKEQTdgevevLVEETLSQL---GLThvqhslIGGGAGKRGISGGERKRVAVAVELVARPSVLLLDE 156
Cdd:PRK11288 99 NLylgQLPHKGGIVNRRL------LNYEAREQLehlGVD------IDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDE 166
|
170 180 190
....*....|....*....|....*....|..
gi 224007385 157 PTSGLDSSTAFKLMLTLKELASLGHAIAVVIH 188
Cdd:PRK11288 167 PTSSLSAREIEQLFRVIRELRAEGRVILYVSH 198
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
78-162 |
3.21e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 49.74 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 78 LTVHETVRFAARL-KTPKEQTDGEVEVLVEetlsQLGLTHVQHSLIGGgagkrgISGGERKRVAVAVELVARPSVLLLDE 156
Cdd:NF033858 354 LTVRQNLELHARLfHLPAAEIAARVAEMLE----RFDLADVADALPDS------LPLGIRQRLSLAVAVIHKPELLILDE 423
|
....*.
gi 224007385 157 PTSGLD 162
Cdd:NF033858 424 PTSGVD 429
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-183 |
3.99e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 49.25 E-value: 3.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLAdPtkdliDNSCIRINNEKGTL--PK---RL-VGVVWQEDLLLPN 77
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQ-P-----DSGEILIDGKPVRIrsPRdaiALgIGMVHQHFMLVPN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 78 LTVHE--------TVRFAARLKTPKEQtdgevevlVEETLSQLGLtHVQ-HSLIGGgagkrgISGGERKRVavavE---- 144
Cdd:COG3845 95 LTVAEnivlglepTKGGRLDRKAARAR--------IRELSERYGL-DVDpDAKVED------LSVGEQQRV----Eilka 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 224007385 145 LVARPSVLLLDEPTSGLDSSTAFKLMLTLKELASLGHAI 183
Cdd:COG3845 156 LYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSI 194
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
21-164 |
5.28e-06 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 48.19 E-value: 5.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 21 GPSGSGKTSLVSVAAGLLaDPT--KDLIDNSCIRINNEKGTLPKRL-VGVVWQEDL--LLPNLTVHETVRFAarLKTPKE 95
Cdd:COG4608 51 GESGCGKSTLGRLLLRLE-EPTsgEILFDGQDITGLSGRELRPLRRrMQMVFQDPYasLNPRMTVGDIIAEP--LRIHGL 127
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224007385 96 QTDGEVEVLVEETLSQLGL--THVQ---HSLigggagkrgiSGGERKRVAVAVELVARPSVLLLDEPTSGLDSS 164
Cdd:COG4608 128 ASKAERRERVAELLELVGLrpEHADrypHEF----------SGGQRQRIGIARALALNPKLIVCDEPVSALDVS 191
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1-162 |
5.93e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 47.86 E-value: 5.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAaGLLADPTKD--LIDNSCIRINNEKGTlpKRLVGVVWQEdllLP-- 76
Cdd:PRK10575 24 RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-GRHQPPSEGeiLLDAQPLESWSSKAF--ARKVAYLPQQ---LPaa 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 77 -NLTVHETV------------RFAArlkTPKEQtdgevevlVEETLSQLGLTHVQHSLIGGgagkrgISGGERKRVAVAV 143
Cdd:PRK10575 98 eGMTVRELVaigrypwhgalgRFGA---ADREK--------VEEAISLVGLKPLAHRLVDS------LSGGERQRAWIAM 160
|
170 180
....*....|....*....|
gi 224007385 144 eLVARPS-VLLLDEPTSGLD 162
Cdd:PRK10575 161 -LVAQDSrCLLLDEPTSALD 179
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
107-188 |
6.09e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.06 E-value: 6.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 107 ETLSQLGLTHVQHsliggGAGKRGISGGERKRVAVAVELVA---RPSVLLLDEPTSGLDSSTAFKLMLTLKELASLGHAI 183
Cdd:PRK00635 791 HALCSLGLDYLPL-----GRPLSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTV 865
|
....*
gi 224007385 184 AVVIH 188
Cdd:PRK00635 866 VIIEH 870
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-191 |
6.31e-06 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 47.76 E-value: 6.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLlADPTKDLI---DNSCIRINNEKGTLPKRLVGVVWQEDL--LL 75
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGL-ESPSQGNVswrGEPLAKLNRAQRKAFRRDIQMVFQDSIsaVN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 76 PNLTVHETVRFAARLKTPKEQTDGEVEVLveETLSQLGLThvqhsliGGGAGKR--GISGGERKRVAVAVELVARPSVLL 153
Cdd:PRK10419 104 PRKTVREIIREPLRHLLSLDKAERLARAS--EMLRAVDLD-------DSVLDKRppQLSGGQLQRVCLARALAVEPKLLI 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 224007385 154 LDEPTSGLDSSTAFKLMLTLKEL-ASLGHAIAVVIHQPR 191
Cdd:PRK10419 175 LDEAVSNLDLVLQAGVIRLLKKLqQQFGTACLFITHDLR 213
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1-175 |
7.46e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 48.75 E-value: 7.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLADPTKDLIDNscirINNEKGTLPK--RLVGVVWQEDLLLpnl 78
Cdd:TIGR01271 1232 RAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQIDG----VSWNSVTLQTwrKAFGVIPQKVFIF--- 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 79 tvheTVRFAARLKTPKEQTDGEVEVLVEEtlsqLGLTHV--------QHSLIGGGAgkrGISGGERKRVAVAVELVARPS 150
Cdd:TIGR01271 1305 ----SGTFRKNLDPYEQWSDEEIWKVAEE----VGLKSVieqfpdklDFVLVDGGY---VLSNGHKQLMCLARSILSKAK 1373
|
170 180
....*....|....*....|....*
gi 224007385 151 VLLLDEPTSGLDSSTAFKLMLTLKE 175
Cdd:TIGR01271 1374 ILLLDEPSAHLDPVTLQIIRKTLKQ 1398
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
21-162 |
7.63e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 46.77 E-value: 7.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 21 GPSGSGKTSLVSVAAGLLAdptkdlIDNSCIRINNEKGTLPKRLVGVVWQEDL--LLPNLTVHETVRFAARLKTPK-EQT 97
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLH------VESGQIQIDGKTATRGDRSRFMAYLGHLpgLKADLSTLENLHFLCGLHGRRaKQM 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 224007385 98 DGEVEVLVeetlsqlGLTHVQHSLIgggagkRGISGGERKRVAVAVELVARPSVLLLDEPTSGLD 162
Cdd:PRK13543 118 PGSALAIV-------GLAGYEDTLV------RQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
107-189 |
7.94e-06 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 47.22 E-value: 7.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 107 ETLSQLGLTHVQhslIGGGAGKrgISGGERKRVAVAVELVAR---PSVLLLDEPTSGLDSSTAFKLMLTLKELASLGHAI 183
Cdd:cd03271 151 QTLCDVGLGYIK---LGQPATT--LSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTV 225
|
....*.
gi 224007385 184 AVVIHQ 189
Cdd:cd03271 226 VVIEHN 231
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
21-188 |
7.98e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 48.24 E-value: 7.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 21 GPSGSGKTSLVSVAAGLL--------ADPTKDLIdnscirINNEKGT-------------------------LPKRLVGV 67
Cdd:COG1245 106 GPNGIGKSTALKILSGELkpnlgdydEEPSWDEV------LKRFRGTelqdyfkklangeikvahkpqyvdlIPKVFKGT 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 68 VWqeDLLlpnltvhetvrfaarlktpkEQTD--GEVEVLVEEtlsqLGLTHVQHSLIgggagkRGISGGERKRVAVAVEL 145
Cdd:COG1245 180 VR--ELL--------------------EKVDerGKLDELAEK----LGLENILDRDI------SELSGGELQRVAIAAAL 227
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 224007385 146 VARPSVLLLDEPTSGLDSSTAFKLMLTLKELASLGHAIAVVIH 188
Cdd:COG1245 228 LRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEH 270
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
20-163 |
8.75e-06 |
|
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: 47.02 E-value: 8.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 20 MGPSGSGKTSLVSVAAGlladptkdlidnsciRINNEKGTLPKRLVGVVWQEDLLLPNLTVheTVRFAARLKTPKEQTDG 99
Cdd:cd03237 31 LGPNGIGKTTFIKMLAG---------------VLKPDEGDIEIELDTVSYKPQYIKADYEG--TVRDLLSSITKDFYTHP 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224007385 100 EVEVlveETLSQLGLTHVQHSLIgggagkRGISGGERKRVAVAVELVARPSVLLLDEPTSGLDS 163
Cdd:cd03237 94 YFKT---EIAKPLQIEQILDREV------PELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
4-187 |
9.31e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.09 E-value: 9.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVST------KISPYQLTAWMGPSGSGKTSLVSVAAGLLADPTKDLID--NSCIRINNEKgtLPKrLVGVVWQE---D 72
Cdd:PRK10938 13 LSDTKTlqlpslTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSqfSHITRLSFEQ--LQK-LVSDEWQRnntD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 73 LLLPNltVHETVRFAARLKtpkeQTDGEVEVLVEETLSQLGLTHVqhsligggAGKRGI--SGGERKRVAVAVELVARPS 150
Cdd:PRK10938 90 MLSPG--EDDTGRTTAEII----QDEVKDPARCEQLAQQFGITAL--------LDRRFKylSTGETRKTLLCQALMSEPD 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 224007385 151 VLLLDEPTSGLDSSTAFKLMLTLKELASLGHAIAVVI 187
Cdd:PRK10938 156 LLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVL 192
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
3-189 |
1.06e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 46.48 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLaDPTKDLIDNSCIRINNEKGTLPKRLVgVVWQEDLLLPNLTVHE 82
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLL-NPEKGEILFERQSIKKDLCTYQKQLC-FVGHRSGINPYLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 83 TVRFAARLKTpkeqTDGEVEVLVeeTLSQLGlthvqhSLIGGGAGKrgISGGERKRVAVAVELVARPSVLLLDEPTSGLD 162
Cdd:PRK13540 94 NCLYDIHFSP----GAVGITELC--RLFSLE------HLIDYPCGL--LSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
170 180
....*....|....*....|....*..
gi 224007385 163 SSTAFKLMLTLKELASLGHAIAVVIHQ 189
Cdd:PRK13540 160 ELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
131-162 |
1.52e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 47.31 E-value: 1.52e-05
10 20 30
....*....|....*....|....*....|..
gi 224007385 131 ISGGERKRVAVAVELVARPSVLLLDEPTSGLD 162
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-176 |
1.66e-05 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 47.32 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKtslvSVAAGLL-----ADPTKDLIDNSCIRinneKGTLP--KRLVGVVWQeDLLLP 76
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGK----STIANLLtrfydIDEGEILLDGHDLR----DYTLAslRNQVALVSQ-NVHLF 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 77 NLTVHETVRFAARLKTPKEQTDGEVEVL-VEETLSQL--GLthvqHSLIG-GGAGkrgISGGERKRVAVAVELVARPSVL 152
Cdd:PRK11176 430 NDTIANNIAYARTEQYSREQIEEAARMAyAMDFINKMdnGL----DTVIGeNGVL---LSGGQRQRIAIARALLRDSPIL 502
|
170 180
....*....|....*....|....
gi 224007385 153 LLDEPTSGLDSSTAFKLMLTLKEL 176
Cdd:PRK11176 503 ILDEATSALDTESERAIQAALDEL 526
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1-213 |
2.16e-05 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 47.01 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVS-------VAAGLLADPTKDLIDnscIRINNEKGTLpkrlvGVVWQEDL 73
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSliqrhfdVSEGDIRFHDIPLTK---LQLDSWRSRL-----AVVSQTPF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 74 LL------------PNLTvHETVRFAARLKTPKEqtdgevEVLveeTLSQLGLTHVqhsligggaGKRGI--SGGERKRV 139
Cdd:PRK10789 400 LFsdtvannialgrPDAT-QQEIEHVARLASVHD------DIL---RLPQGYDTEV---------GERGVmlSGGQKQRI 460
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224007385 140 AVAVELVARPSVLLLDEPTSGLDSSTAFKLmltLKELASLGHAIAVVIHQPRTSIFNLFDNLLLLQKGNVVYEG 213
Cdd:PRK10789 461 SIARALLLNAEILILDDALSAVDGRTEHQI---LHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRG 531
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-162 |
2.22e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 46.23 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLA-----------DPTKDLIDNscirinnekgtlpKRLVGVVW-QE 71
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVptsgevrvlgyVPFKRRKEF-------------ARRIGVVFgQR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 72 DLLLPNLTVHETVRFAARL-KTPKEQTDGEVEVLVEetlsQLGLTHV------QHSLigggagkrgisgGERKRVAVAVE 144
Cdd:COG4586 105 SQLWWDLPAIDSFRLLKAIyRIPDAEYKKRLDELVE----LLDLGELldtpvrQLSL------------GQRMRCELAAA 168
|
170
....*....|....*...
gi 224007385 145 LVARPSVLLLDEPTSGLD 162
Cdd:COG4586 169 LLHRPKILFLDEPTIGLD 186
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-190 |
3.63e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 45.59 E-value: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLADP--TKDLIDNSCIRINNE-----KGTLPKRLVGVVWQEDL 73
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaPRGARVTGDVTLNGEplaaiDAPRLARLRAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 74 LLPNLTVHETV---RFA-ARLKTPKEQTDGEVevlVEETLSQLGLThvqhSLIGGGAGKrgISGGERKRVAVAVEL---- 145
Cdd:PRK13547 94 PAFAFSAREIVllgRYPhARRAGALTHRDGEI---AWQALALAGAT----ALVGRDVTT--LSGGELARVQFARVLaqlw 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 224007385 146 -----VARPSVLLLDEPTSGLDSSTAFKLMLTLKELASLGH-AIAVVIHQP 190
Cdd:PRK13547 165 pphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNlGVLAIVHDP 215
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
3-191 |
3.98e-05 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 45.18 E-value: 3.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLlADPTKDLID---NSCIRINNEKGTLPKRLVGVVWQEDL--LLPN 77
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGL-EKPAQGTVSfrgQDLYQLDRKQRRAFRRDVQLVFQDSPsaVNPR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 78 LTVHETVRFAARLKTPKEQTDGEVEVLveETLSQLGL--THVQHSligggagKRGISGGERKRVAVAVELVARPSVLLLD 155
Cdd:TIGR02769 105 MTVRQIIGEPLRHLTSLDESEQKARIA--ELLDMVGLrsEDADKL-------PRQLSGGQLQRINIARALAVKPKLIVLD 175
|
170 180 190
....*....|....*....|....*....|....*..
gi 224007385 156 EPTSGLDSSTAFKLMLTLKEL-ASLGHAIAVVIHQPR 191
Cdd:TIGR02769 176 EAVSNLDMVLQAVILELLRKLqQAFGTAYLFITHDLR 212
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
4-186 |
5.24e-05 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 44.87 E-value: 5.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSV-------AAGLLADPTKDLIDNSCIRINNEKgtlpkrlVGVVWQEDLLLP 76
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTlcgdpraTSGRIVFDGKDITDWQTAKIMREA-------VAIVPEGRRVFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 77 NLTVHETVR----FAARlktpkEQTDGEVEvLVEETLSQLGLTHVQHsligggAGKrgISGGERKRVAVAVELVARPSVL 152
Cdd:PRK11614 94 RMTVEENLAmggfFAER-----DQFQERIK-WVYELFPRLHERRIQR------AGT--MSGGEQQMLAIGRALMSQPRLL 159
|
170 180 190
....*....|....*....|....*....|....
gi 224007385 153 LLDEPTSGLDSSTAFKLMLTLKELASLGHAIAVV 186
Cdd:PRK11614 160 LLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLV 193
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
131-192 |
5.66e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.77 E-value: 5.66e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224007385 131 ISGGERKRVAVAVELVARPS-VL-LLDEPTSGLDSSTAFKLMLTLKELASLGHAIAVVIHQPRT 192
Cdd:TIGR00630 489 LSGGEAQRIRLATQIGSGLTgVLyVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDT 552
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
3-191 |
5.97e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 44.63 E-value: 5.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGllaDPTKDLIDNSC----IRINNEKGTLPKRL-VGVVWQEDLLLPN 77
Cdd:CHL00131 22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG---HPAYKILEGDIlfkgESILDLEPEERAHLgIFLAFQYPIEIPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 78 LTVHETVRFAARLKTpKEQTDGEVEVL--VEETLSQLGLTHVQHSLIGGGAGKrGISGGERKRVAVAVELVARPSVLLLD 155
Cdd:CHL00131 99 VSNADFLRLAYNSKR-KFQGLPELDPLefLEIINEKLKLVGMDPSFLSRNVNE-GFSGGEKKRNEILQMALLDSELAILD 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 224007385 156 EPTSGLDSSTAFKLMLTLKELASLGHAIAVVIHQPR 191
Cdd:CHL00131 177 ETDSGLDIDALKIIAEGINKLMTSENSIILITHYQR 212
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-186 |
7.10e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 45.20 E-value: 7.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 6 DVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLL--ADPTKDLIDNSCIRINNEKGTLPKRLVGVvwQEDL----LLPNLT 79
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYpgKFEGNVFINGKPVDIRNPAQAIRAGIAMV--PEDRkrhgIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 80 VHETVRFAARLK-TPKEQTDGEVEV-LVEETLSQLGLTHVQHSL-IGGgagkrgISGGERKRVAVAVELVARPSVLLLDE 156
Cdd:TIGR02633 356 VGKNITLSVLKSfCFKMRIDAAAELqIIGSAIQRLKVKTASPFLpIGR------LSGGNQQKAVLAKMLLTNPRVLILDE 429
|
170 180 190
....*....|....*....|....*....|
gi 224007385 157 PTSGLDSSTAFKLMLTLKELASLGHAIAVV 186
Cdd:TIGR02633 430 PTRGVDVGAKYEIYKLINQLAQEGVAIIVV 459
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4-186 |
9.55e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 44.92 E-value: 9.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLADPTKD---LIDNSCIRINNEKGTLPKRLVgVVWQEDLLLPNLTV 80
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTYEgeiIFEGEELQASNIRDTERAGIA-IIHQELALVKELSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 81 HETVrFAARLKTPKEQTD-GEVEVLVEETLSQLGL-----THVQHsligggagkrgISGGERKRVAVAVELVARPSVLLL 154
Cdd:PRK13549 100 LENI-FLGNEITPGGIMDyDAMYLRAQKLLAQLKLdinpaTPVGN-----------LGLGQQQLVEIAKALNKQARLLIL 167
|
170 180 190
....*....|....*....|....*....|..
gi 224007385 155 DEPTSGLDSSTAFKLMLTLKELASlgHAIAVV 186
Cdd:PRK13549 168 DEPTASLTESETAVLLDIIRDLKA--HGIACI 197
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
131-186 |
1.02e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 44.85 E-value: 1.02e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224007385 131 ISGGERKRVAVAVELVARPSVLLLDEPTSGLD---SSTAFKLMLTLKELASLG-----HAIAVV 186
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDvtiQAQILQLIKVLQKEMSMGvifitHDMGVV 232
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1-191 |
1.08e-04 |
|
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: 44.93 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGlladptKDLIDNSCIRInnekGTLPKrlVGVVWQE-DLLLPNLT 79
Cdd:TIGR03719 335 KLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITG------QEQPDSGTIEI----GETVK--LAYVDQSrDALDPNKT 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 80 VHETVrfaarlktpKEQTD----GEVEVLVEETLSQLGLThvqhsliGGGAGKR--GISGGERKRVAVAVELVARPSVLL 153
Cdd:TIGR03719 403 VWEEI---------SGGLDiiklGKREIPSRAYVGRFNFK-------GSDQQKKvgQLSGGERNRVHLAKTLKSGGNVLL 466
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 224007385 154 LDEPTSGLDSSTafklmltlkeLASLGHAI------AVVIHQPR 191
Cdd:TIGR03719 467 LDEPTNDLDVET----------LRALEEALlnfagcAVVISHDR 500
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
131-165 |
1.12e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.94 E-value: 1.12e-04
10 20 30
....*....|....*....|....*....|....*
gi 224007385 131 ISGGERKRVAVAVELVARPSVLLLDEPTSGLDSST 165
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET 191
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
132-187 |
1.82e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 43.95 E-value: 1.82e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 224007385 132 SGGERKRVAVAVELVARPSVLLLDEPTSGLDSSTafklmltlkeLASLGHAI------AVVI 187
Cdd:PRK11819 447 SGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVET----------LRALEEALlefpgcAVVI 498
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
21-188 |
1.88e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.03 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 21 GPSGSGKTSLVSVAAGLL--------ADPTKDLIdnscirINNEKGT-------------------------LPKRLVGV 67
Cdd:PRK13409 106 GPNGIGKTTAVKILSGELipnlgdyeEEPSWDEV------LKRFRGTelqnyfkklyngeikvvhkpqyvdlIPKVFKGK 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 68 VWqeDLLlpnltvhetvrfaarlktpkEQTDgEVEVLvEETLSQLGLTHVQHSLIgggagkRGISGGERKRVAVAVELVA 147
Cdd:PRK13409 180 VR--ELL--------------------KKVD-ERGKL-DEVVERLGLENILDRDI------SELSGGELQRVAIAAALLR 229
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 224007385 148 RPSVLLLDEPTSGLDSSTAFKLMLTLKELASlGHAIAVVIH 188
Cdd:PRK13409 230 DADFYFFDEPTSYLDIRQRLNVARLIRELAE-GKYVLVVEH 269
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
4-166 |
2.43e-04 |
|
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: 43.78 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 4 LSDVSTKISPYQLTAWMGPSGSGKTSLVSvaaGLLADPTKdlidnscirinNEKGTLPKRLVGVVWQEdLLLPNLTVHET 83
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLS---ALLAEMDK-----------VEGHVHMKGSVAYVPQQ-AWIQNDSLREN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 84 VRFAARLKTPKEQTDGEVEVLVE--ETLSQLGLTHVqhsligggaGKRGI--SGGERKRVAVAVELVARPSVLLLDEPTS 159
Cdd:TIGR00957 719 ILFGKALNEKYYQQVLEACALLPdlEILPSGDRTEI---------GEKGVnlSGGQKQRVSLARAVYSNADIYLFDDPLS 789
|
....*..
gi 224007385 160 GLDSSTA 166
Cdd:TIGR00957 790 AVDAHVG 796
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
21-188 |
2.50e-04 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 43.16 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 21 GPSGSGKTS-------LVSVAAGLLADPTKDLIDNScirinnEKGTLPKRL-VGVVWQEDL--LLPNLTVHETVrfAARL 90
Cdd:PRK15079 54 GESGCGKSTfaraiigLVKATDGEVAWLGKDLLGMK------DDEWRAVRSdIQMIFQDPLasLNPRMTIGEII--AEPL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 91 KT--PKeQTDGEVEVLVEETLSQLGL-----THVQHSLigggagkrgiSGGERKRVAVAVELVARPSVLLLDEPTSGLDS 163
Cdd:PRK15079 126 RTyhPK-LSRQEVKDRVKAMMLKVGLlpnliNRYPHEF----------SGGQCQRIGIARALILEPKLIICDEPVSALDV 194
|
170 180 190
....*....|....*....|....*....|...
gi 224007385 164 STAFKLMLTLKELA-----SL---GHAIAVVIH 188
Cdd:PRK15079 195 SIQAQVVNLLQQLQremglSLifiAHDLAVVKH 227
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
129-183 |
2.77e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 43.50 E-value: 2.77e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 224007385 129 RGISGGERKRVAVAVELVARPSVLLLDEPTSGLDSSTAFKLMLTLKELASLGHAI 183
Cdd:PRK15439 402 RTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAV 456
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-183 |
2.98e-04 |
|
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: 43.13 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKtslvSVAA----GLLADPT-----------KDLIDNSCIRINNEKGtlpkRLVGV 67
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGK----SVTAlsilRLLPDPAahpsgsilfdgQDLLGLSERELRRIRG----NRIAM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 68 VWQEDL--LLPNLTVHETVRFAARLKTPKEQTDGEVEVLveETLSQLGLTHVQ-------HSLigggagkrgiSGGERKR 138
Cdd:COG4172 97 IFQEPMtsLNPLHTIGKQIAEVLRLHRGLSGAAARARAL--ELLERVGIPDPErrldaypHQL----------SGGQRQR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 224007385 139 VAVAVELVARPSVLLLDEPTSGLDSSTAFKLMLTLKEL-ASLGHAI 183
Cdd:COG4172 165 VMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMAL 210
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
131-186 |
3.28e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 42.99 E-value: 3.28e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 224007385 131 ISGGERKRVAVAVELVARPSVLLLDEPTSGLDSSTAFKLMLTLKELASLGHAIAVV 186
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVI 461
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
131-220 |
3.43e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 42.81 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 131 ISGGERKRVAVAVELVARPSVLLLDEPTSGLD---SSTAFKLMLTLKE-----LASLGHAIAVVIHQPRTSIFNLFdnll 202
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDvtiQAQIIELLLELQQkenmaLVLITHDLALVAEAAHKIIVMYA---- 229
|
90
....*....|....*...
gi 224007385 203 llqkGNVVYEGKASEVKR 220
Cdd:PRK11022 230 ----GQVVETGKAHDIFR 243
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-162 |
3.48e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.23 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAG-LLADPTKDLIDN--SCIRINNEKGTLPKRLVGVVWQEDlllpn 77
Cdd:PRK10636 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNeISADGGSYTFPGnwQLAWVNQETPALPQPALEYVIDGD----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 78 ltvHETVRFAARLKTPKEQTDGEVEVLVEETLSQLGLTHVQH---SLIGG-GAGK-------RGISGGERKRVAVAVELV 146
Cdd:PRK10636 89 ---REYRQLEAQLHDANERNDGHAIATIHGKLDAIDAWTIRSraaSLLHGlGFSNeqlerpvSDFSGGWRMRLNLAQALI 165
|
170
....*....|....*.
gi 224007385 147 ARPSVLLLDEPTSGLD 162
Cdd:PRK10636 166 CRSDLLLLDEPTNHLD 181
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
115-186 |
3.50e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.18 E-value: 3.50e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 224007385 115 THVQHSLIGGgagkrgISGGERKRVAVAVELVARPSVLLLDEPTSGLDSSTAFKLMLTLKELASLGHAIAVV 186
Cdd:PRK10982 382 TPGHRTQIGS------LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIII 447
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
131-186 |
4.41e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 42.85 E-value: 4.41e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 224007385 131 ISGGERKRVAVAVELVARPSVLLLDEPTSGLDSSTAFKLMLTLKELASLGHAIAVV 186
Cdd:PRK09700 410 LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMV 465
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
7-162 |
4.98e-04 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 41.90 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 7 VSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLaDPTkdlidNSCIRINNEK-GTLPKRLV---GVV--WQEDLLLPNLTV 80
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFY-KPT-----GGTILLRGQHiEGLPGHQIarmGVVrtFQHVRLFREMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 81 --------HETVR---FAARLKTPK-EQTDGEVEVLVEETLSQLGLThvqhSLIGGGAGKrgISGGERKRVAVAVELVAR 148
Cdd:PRK11300 98 ienllvaqHQQLKtglFSGLLKTPAfRRAESEALDRAATWLERVGLL----EHANRQAGN--LAYGQQRRLEIARCMVTQ 171
|
170
....*....|....
gi 224007385 149 PSVLLLDEPTSGLD 162
Cdd:PRK11300 172 PEILMLDEPAAGLN 185
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
132-187 |
5.13e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 42.71 E-value: 5.13e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 224007385 132 SGGERKRVAVAVELVAR---PSVLLLDEPTSGL---DSStafKLMLTLKELASLGHAIaVVI 187
Cdd:COG0178 828 SGGEAQRVKLASELSKRstgKTLYILDEPTTGLhfhDIR---KLLEVLHRLVDKGNTV-VVI 885
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
131-191 |
6.59e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 6.59e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 224007385 131 ISGGERKRVAVAVELVARPS--VLLLDEPTSGLDSSTAFKLMLTLKELASLGHAIAVVIHQPR 191
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQ 539
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
130-190 |
7.96e-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: 40.04 E-value: 7.96e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 224007385 130 GISGGERKRVAVAVEL----VARPSVLLLDEPTSGLDSSTAFKLMLTLKELASLGHAIAVVIHQP 190
Cdd:cd03227 77 QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLP 141
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
129-162 |
1.42e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.38 E-value: 1.42e-03
10 20 30
....*....|....*....|....*....|....
gi 224007385 129 RGISGGERKRVAVAVELVARPSVLLLDEPTSGLD 162
Cdd:PLN03073 343 KTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1-165 |
2.04e-03 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 40.86 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLVSVAAGLLAdptkdlIDNSCIRINNEK-GTLPKRL----VGVVWQE---- 71
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYP------LTEGEIRLDGRPlSSLSHSVlrqgVAMVQQDpvvl 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 72 -DLLLPNLTVHETVRfaarlktpkeqtdgevEVLVEETLSQLGLTHVQHSLIGG---GAGKRG--ISGGERKRVAVAVEL 145
Cdd:PRK10790 428 aDTFLANVTLGRDIS----------------EEQVWQALETVQLAELARSLPDGlytPLGEQGnnLSVGQKQLLALARVL 491
|
170 180
....*....|....*....|
gi 224007385 146 VARPSVLLLDEPTSGLDSST 165
Cdd:PRK10790 492 VQTPQILILDEATANIDSGT 511
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
131-187 |
2.49e-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: 2.49e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 224007385 131 ISGGERKRVAVAVELVARPSVLLLDEPTSGLDSSTAFKLMLTLKELASLGHAIAVVI 187
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVV 128
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
124-162 |
2.55e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.54 E-value: 2.55e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 224007385 124 GGAGKRG---------ISGGERKRVAVAVELVARPSVLLLDEPTSGLD 162
Cdd:PRK10636 415 GGFGFQGdkvteetrrFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
132-163 |
2.63e-03 |
|
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: 40.15 E-value: 2.63e-03
10 20 30
....*....|....*....|....*....|...
gi 224007385 132 SGGERKRVAVAVELvARPS-VLLLDEPTSGLDS 163
Cdd:COG1245 457 SGGELQRVAIAACL-SRDAdLYLLDEPSAHLDV 488
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1-165 |
2.76e-03 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 39.51 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 1 RSILSDVSTKISPYQLTAWMGPSGSGKTSLvSVAAGLLADPTK-----DLIDNSCIRINnekgTLPKRLvGVVWQEDLLL 75
Cdd:cd03288 34 KPVLKHVKAYIKPGQKVGICGRTGSGKSSL-SLAFFRMVDIFDgkiviDGIDISKLPLH----TLRSRL-SIILQDPILF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 76 PNltvheTVRFaaRLKTPKEQTDGEVEvlveETLSQLGLTHVQHSLIGG-----GAGKRGISGGERKRVAVAVELVARPS 150
Cdd:cd03288 108 SG-----SIRF--NLDPECKCTDDRLW----EALEIAQLKNMVKSLPGGldavvTEGGENFSVGQRQLFCLARAFVRKSS 176
|
170
....*....|....*
gi 224007385 151 VLLLDEPTSGLDSST 165
Cdd:cd03288 177 ILIMDEATASIDMAT 191
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
132-187 |
3.45e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.77 E-value: 3.45e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 224007385 132 SGGERKRVAVAVELVARPSVLLLDEPTSGLDSSTAFKLMLTLKELASLGHAIaVVI 187
Cdd:NF040905 406 SGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGV-IVI 460
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
3-163 |
3.79e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 40.15 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 3 ILSDVSTKISPYQLTAWMGPSGSGKTSLVsvaaglladptKDLIDNSCIrinNEKGTLPKRLVGVVWQEDLLLpNLTVHE 82
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLL-----------QSLLSQFEI---SEGRVWAERSIAYVPQQAWIM-NATVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 83 TVRF-----AARLKTPkeqtdgeVEVL-VEETLSQLGlthvqhsligGG----AGKRGI--SGGERKRVAVAVELVARPS 150
Cdd:PTZ00243 740 NILFfdeedAARLADA-------VRVSqLEADLAQLG----------GGleteIGEKGVnlSGGQKARVSLARAVYANRD 802
|
170
....*....|...
gi 224007385 151 VLLLDEPTSGLDS 163
Cdd:PTZ00243 803 VYLLDDPLSALDA 815
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
132-187 |
4.26e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 39.67 E-value: 4.26e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 224007385 132 SGGERKRVAVAVELVARP---SVLLLDEPTSGLDSSTAFKLMLTLKELASLGHAIaVVI 187
Cdd:PRK00349 832 SGGEAQRVKLAKELSKRStgkTLYILDEPTTGLHFEDIRKLLEVLHRLVDKGNTV-VVI 889
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
129-165 |
4.30e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 39.55 E-value: 4.30e-03
10 20 30
....*....|....*....|....*....|....*...
gi 224007385 129 RGISGGERKRVAVAvELVARPSVLL-LDEPTSGLDSST 165
Cdd:PRK11147 439 KALSGGERNRLLLA-RLFLKPSNLLiLDEPTNDLDVET 475
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
132-162 |
4.49e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 39.41 E-value: 4.49e-03
10 20 30
....*....|....*....|....*....|.
gi 224007385 132 SGGERKRVAVAVELVARPSVLLLDEPTSGLD 162
Cdd:PRK13409 455 SGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
20-194 |
7.54e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 36.97 E-value: 7.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 20 MGPSGSGKTSLVSVAAGLLADPTKDLIDNSCIRINNEkgtlpkrlvgvvwqedlllpnltvhetvrfaarlktpkeqtdg 99
Cdd:smart00382 8 VGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEE------------------------------------------- 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224007385 100 evevlveetlsqlglTHVQHSLIGGGAGKRGISGGERKRVAVAVELVARPSVLLLDEPTSGLDSSTAFKLML-----TLK 174
Cdd:smart00382 45 ---------------VLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrLLL 109
|
170 180
....*....|....*....|
gi 224007385 175 ELASLGHAIAVVIHQPRTSI 194
Cdd:smart00382 110 LLKSEKNLTVILTTNDEKDL 129
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
132-187 |
7.61e-03 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 38.85 E-value: 7.61e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 224007385 132 SGGERKRVAVAVELVARPSVLLLDEPTSGLDSSTAFKLMLTLKELASLGHAIaVVI 187
Cdd:COG1129 396 SGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAV-IVI 450
|
|
| |
