|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
62-678 |
5.80e-157 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 468.20 E-value: 5.80e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 62 PIFLKFEDVEYKVR--NSHASSANLVKTMVSKVVTHTNPDPDGYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGG 139
Cdd:PLN03211 37 PITLKFMDVCYRVKfeNMKNKGSNIKRILGHKPKISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 140 RL-TDNVKGKLTYNDIPYSPSVKRRIGFVTQDDVLLPQLTVEETLAFAAFLRLPSSMSKEQKYAKIEMIIKELGLERCRR 218
Cdd:PLN03211 117 RIqGNNFTGTILANNRKPTKQILKRTGFVTQDDILYPHLTVRETLVFCSLLRLPKSLTKQEKILVAESVISELGLTKCEN 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 219 TRVGGGFVKGISGGERKRASIAYEILVDPSLLLLDEPTSGLDSTSATKLLHILQGVAKAGRTVITTIHQPSSRMFHMFDK 298
Cdd:PLN03211 197 TIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDS 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 299 LLLISEGHPAFYGKARESMEYFSSLRILPEIAMNPAEFLLDLATG--QVSDISLPDELLAAKTAQPDSEEVLLKYLKQRY 376
Cdd:PLN03211 277 VLVLSEGRCLFFGKGSDAMAYFESVGFSPSFPMNPADFLLDLANGvcQTDGVSEREKPNVKQSLVASYNTLLAPKVKAAI 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 377 KTDLEPKEKEENHRNRKAPEH---LQIAIQvkkdwtlSWWDQFLILSRRTFRERRRDYFDKLRLVQSLGVAVVLGLLWWK 453
Cdd:PLN03211 357 EMSHFPQANARFVGSASTKEHrssDRISIS-------TWFNQFSILLQRSLKERKHESFNTLRVFQVIAAALLAGLMWWH 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 454 SKTdteAHLRDQVGLMFYICIFWTSSSLFGAVYVFPFEKIYLVKERKAEMYRLSVYYVCSTLCDMVAHVLYPTFFMIIVY 533
Cdd:PLN03211 430 SDF---RDVQDRLGLLFFISIFWGVFPSFNSVFVFPQERAIFVKERASGMYTLSSYFMARIVGDLPMELILPTIFLTVTY 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 534 FMAEFNRNIPCFLFTVLTILLIAITSQGAGEFLGASVLSIKRAGMIASLVLMLFLLTGGYYVQHIPKFMQWLKYLSFMHY 613
Cdd:PLN03211 507 WMAGLKPELGAFLLTLLVLLGYVLVSQGLGLALGAAIMDAKKASTIVTVTMLAFVLTGGFYVHKLPSCMAWIKYISTTFY 586
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22331045 614 GFRLLLKVQYSADQ----LFECGSKGG-----CRTLQSsssfDTINLNGGLQELWVLLAMAFGYRLCAYFCLRK 678
Cdd:PLN03211 587 SYRLLINVQYGEGKrissLLGCSLPHGsdrasCKFVEE----DVAGQISPATSVSVLIFMFVGYRLLAYLALRR 656
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
102-680 |
1.53e-125 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 385.94 E-value: 1.53e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 102 GYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDNVK--GKLTYNDIPY-SPSVKRRIGFVTQDDVLLPQLT 178
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKgsGSVLLNGMPIdAKEMRAISAYVQQDDLFIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 179 VEETLAFAAFLRLPSSMSKEQKYAKIEMIIKELGLERCRRTRVG-GGFVKGISGGERKRASIAYEILVDPSLLLLDEPTS 257
Cdd:TIGR00955 116 VREHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGvPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 258 GLDSTSATKLLHILQGVAKAGRTVITTIHQPSSRMFHMFDKLLLISEGHPAFYGKARESMEYFSSLRI-LPEiAMNPAEF 336
Cdd:TIGR00955 196 GLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAVPFFSDLGHpCPE-NYNPADF 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 337 LLD-LATGQVSDISlpdellaaktaqpdSEEVLLKYLKQRYKTDLEPK-EKEENHRNRKAPEHLQIAIQVKK-DWTLSWW 413
Cdd:TIGR00955 275 YVQvLAVIPGSENE--------------SRERIEKICDSFAVSDIGRDmLVNTNLWSGKAGGLVKDSENMEGiGYNASWW 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 414 DQFLILSRRTFRERRRD-YFDKLRLVQSLGVAVVLGLLWWKSKTdTEAHLRDQVGLMFYICIFWTSSSLFGAVYVFPFEK 492
Cdd:TIGR00955 341 TQFYALLKRSWLSVLRDpLLLKVRLIQTMMTAILIGLIYLGQGL-TQKGVQNINGALFLFLTNMTFQNVFPVINVFTAEL 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 493 IYLVKERKAEMYRLSVYYVCSTLCDMVAHVLYPTFFMIIVYFMAEFNRNIPCFLFTVLTILLIAITSQGAGEFLGASVLS 572
Cdd:TIGR00955 420 PVFLRETRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGATHFLTFLFLVTLVANVATSFGYLISCAFSS 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 573 IKRAGMIASLVLMLFLLTGGYYVQ--HIPKFMQWLKYLSFMHYGFRLLLKVQYSADQ---LFECGSKGGC----RTLQSS 643
Cdd:TIGR00955 500 TSMALTVGPPFVIPFLLFGGFFINsdSIPVYFKWLSYLSWFRYGNEGLLINQWSDVDnieCTSANTTGPCpssgEVILET 579
|
570 580 590
....*....|....*....|....*....|....*..
gi 22331045 644 SSFDTINLnggLQELWVLLAMAFGYRLCAYFCLRKKI 680
Cdd:TIGR00955 580 LSFRNADL---YLDLIGLVILIFFFRLLAYFALRIRI 613
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
93-311 |
1.32e-73 |
|
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: 235.91 E-value: 1.32e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 93 VTHTNPDPDGYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTD-NVKGKLTYNDIPYSP-SVKRRIGFVTQD 170
Cdd:cd03213 11 VTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlGVSGEVLINGRPLDKrSFRKIIGYVPQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 171 DVLLPQLTVEETLAFAAFLRlpssmskeqkyakiemiikelglercrrtrvgggfvkGISGGERKRASIAYEILVDPSLL 250
Cdd:cd03213 91 DILHPTLTVRETLMFAAKLR-------------------------------------GLSGGERKRVSIALELVSNPSLL 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22331045 251 LLDEPTSGLDSTSATKLLHILQGVAKAGRTVITTIHQPSSRMFHMFDKLLLISEGHPAFYG 311
Cdd:cd03213 134 FLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
98-311 |
7.57e-72 |
|
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: 232.16 E-value: 7.57e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 98 PDPDGYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRL--TDNVKGKLTYNDIPYSPS-VKRRIGFVTQDDVLL 174
Cdd:cd03234 14 KNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVegGGTTSGQILFNGQPRKPDqFQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 175 PQLTVEETLAFAAFLRLPSSMSKEQKyakiEMIIKELGLERCRRTRVGGGFVKGISGGERKRASIAYEILVDPSLLLLDE 254
Cdd:cd03234 94 PGLTVRETLTYTAILRLPRKSSDAIR----KKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 22331045 255 PTSGLDSTSATKLLHILQGVAKAGRTVITTIHQPSSRMFHMFDKLLLISEGHPAFYG 311
Cdd:cd03234 170 PTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
41-634 |
4.87e-62 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 224.99 E-value: 4.87e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 41 SSEIDIDeefvstyPLEDAP-LPIFLKFEDVEYKVrNSHASSANLVKTMvsKVVTHTNPDPDGYKHILKGITGSTGPGEI 119
Cdd:TIGR00956 722 SNKNDIE-------AGEVLGsTDLTDESDDVNDEK-DMEKESGEDIFHW--RNLTYEVKIKKEKRVILNNVDGWVKPGTL 791
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 120 LALMGPSGSGKTTLLKIMGGRLTDNV--KGKLTYNDIPYSPSVKRRIGFVTQDDVLLPQLTVEETLAFAAFLRLPSSMSK 197
Cdd:TIGR00956 792 TALMGASGAGKTTLLNVLAERVTTGVitGGDRLVNGRPLDSSFQRSIGYVQQQDLHLPTSTVRESLRFSAYLRQPKSVSK 871
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 198 EQKYAKIEMIIKELGLERCRRTRVG--GgfvKGISGGERKRASIAYEILVDPSLLL-LDEPTSGLDSTSATKLLHILQGV 274
Cdd:TIGR00956 872 SEKMEYVEEVIKLLEMESYADAVVGvpG---EGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL 948
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 275 AKAGRTVITTIHQPSSRMFHMFDKLLLISEGHPAFY----GKARESM-EYFSS--LRILPEIAmNPAEFLLDL---ATGQ 344
Cdd:TIGR00956 949 ADHGQAILCTIHQPSAILFEEFDRLLLLQKGGQTVYfgdlGENSHTIiNYFEKhgAPKCPEDA-NPAEWMLEVigaAPGA 1027
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 345 VSDISLPDELLAAKTAQPDSEEVllkylkQRYKTDLEPKEKEenhrnrKAPEHLqiaiqvkKDWTLSWWDQFLILSRRTF 424
Cdd:TIGR00956 1028 HANQDYHEVWRNSSEYQAVKNEL------DRLEAELSKAEDD------NDPDAL-------SKYAASLWYQFKLVLWRTF 1088
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 425 RER--RRDY-FDKLRLVqsLGVAVVLGLLWWKSKTDTEAhLRDQVGLMFYICIFWTSsslFGAVYVFPF---EKIYLVKE 498
Cdd:TIGR00956 1089 QQYwrTPDYlYSKFFLT--IFAALFIGFTFFKVGTSLQG-LQNQMFAVFMATVLFNP---LIQQYLPPFvaqRDLYEVRE 1162
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 499 RKAEMYRLSVYYVCSTLCDMVAHVLYPTFFMIIVYFMAEFNRNI-------PCFLFTVLTILLIAITSQGAGEFLGASVL 571
Cdd:TIGR00956 1163 RPSRTFSWLAFIAAQITVEIPYNLVAGTIFFFIWYYPVGFYWNAsktgqvhERGVLFWLLSTMFFLYFSTLGQMVISFNP 1242
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22331045 572 SIKRAGMIASLVLMLFLLTGGYYV--QHIPKFMQWLKYLSFMHYGFRLLLKVQYsADQLFECGSK 634
Cdd:TIGR00956 1243 NADNAAVLASLLFTMCLSFCGVLAppSRMPGFWIFMYRCSPFTYLVQALLSTGL-ADVPVTCKVK 1306
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
29-632 |
1.75e-60 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 220.37 E-value: 1.75e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 29 EFMPQAYLRNqYSSEIDIDEEFVSTYPLEDAplpiflkFEDVeyKVRNSHASSA------NLVKTMVSKVVTHTNPDPDG 102
Cdd:TIGR00956 2 EFNAKAWVKN-FRKLIDSDPIYYKPYKLGVA-------YKNL--SAYGVAADSDyqptfpNALLKILTRGFRKLKKFRDT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 103 YK-HILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTD---NVKGKLTYNDIPYSPSVKRRIGFV---TQDDVLLP 175
Cdd:TIGR00956 72 KTfDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGfhiGVEGVITYDGITPEEIKKHYRGDVvynAETDVHFP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 176 QLTVEETLAFAAFLRLPSSMSK---EQKYAK--IEMIIKELGLERCRRTRVGGGFVKGISGGERKRASIAYEILVDPSLL 250
Cdd:TIGR00956 152 HLTVGETLDFAARCKTPQNRPDgvsREEYAKhiADVYMATYGLSHTRNTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 251 LLDEPTSGLDSTSATKLLHILQGVAK-AGRTVITTIHQPSSRMFHMFDKLLLISEGHPAFYGKARESMEYFSSLRILPEI 329
Cdd:TIGR00956 232 CWDNATRGLDSATALEFIRALKTSANiLDTTPLVAIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAKQYFEKMGFKCPD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 330 AMNPAEFLLDLaTGQVSDISLPD-ELLAAKTAQP------DSEEV--LLKYLKQRYKTDLEPKEKE---ENHRNRKAPeh 397
Cdd:TIGR00956 312 RQTTADFLTSL-TSPAERQIKPGyEKKVPRTPQEfetywrNSPEYaqLMKEIDEYLDRCSESDTKEayrESHVAKQSK-- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 398 lqiAIQVKKDWTLSWWDQF-LILSRRTFRERRRDYFDKLRLVQSLGVAVVLGLLWWKSKTDT-EAHLRdqVGLMFYICIF 475
Cdd:TIGR00956 389 ---RTRPSSPYTVSFSMQVkYCLARNFLRMKGNPSFTLFMVFGNIIMALILSSVFYNLPKNTsDFYSR--GGALFFAILF 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 476 WTSSSLFGAVYVFPFEKIyLVKERKAEMYRLSVYYVCSTLCDMVAHVLYPTFFMIIVYFMAEFNRNIPCFLFTVLTILLI 555
Cdd:TIGR00956 464 NAFSSLLEIASMYEARPI-VEKHRKYALYHPSADAIASIISEIPFKIIESVVFNIILYFMVNFRRTAGRFFFYLLILFIC 542
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22331045 556 AITSQGAGEFLGASVLSIKRAGMIASLVLMLFLLTGGYYVQ--HIPKFMQWLKYLSFMHYGFRLLLKVQYSADQlFECG 632
Cdd:TIGR00956 543 TLAMSHLFRSIGAVTKTLSEAMTPAAILLLALSIYTGFAIPrpSMLGWSKWIYYVNPLAYAFESLMVNEFHGRR-FECS 620
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
93-305 |
3.84e-54 |
|
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: 183.98 E-value: 3.84e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 93 VTHTNPDPDGYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDN-VKGKLTYNDIPYSPSVKRRIGFVTQDD 171
Cdd:cd03232 9 LNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGvITGEILINGRPLDKNFQRSTGYVEQQD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 172 VLLPQLTVEETLAFAAFLRlpssmskeqkyakiemiikelglercrrtrvgggfvkGISGGERKRASIAYEILVDPSLLL 251
Cdd:cd03232 89 VHSPNLTVREALRFSALLR-------------------------------------GLSVEQRKRLTIGVELAAKPSILF 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 22331045 252 LDEPTSGLDSTSATKLLHILQGVAKAGRTVITTIHQPSSRMFHMFDKLLLISEG 305
Cdd:cd03232 132 LDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRG 185
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
62-604 |
6.58e-53 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 197.76 E-value: 6.58e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 62 PIFLKFEDVEYKVrnshassaNLVKTMVSKVVthtnpdPDGYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRL 141
Cdd:PLN03140 865 PLAMSFDDVNYFV--------DMPAEMKEQGV------TEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRK 930
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 142 TDN-VKGKLTYNDIPYSPSVKRRI-GFVTQDDVLLPQLTVEETLAFAAFLRLPSSMSKEQKYAKIEMIIKELGLERCRRT 219
Cdd:PLN03140 931 TGGyIEGDIRISGFPKKQETFARIsGYCEQNDIHSPQVTVRESLIYSAFLRLPKEVSKEEKMMFVDEVMELVELDNLKDA 1010
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 220 RVGGGFVKGISGGERKRASIAYEILVDPSLLLLDEPTSGLDSTSATKLLHILQGVAKAGRTVITTIHQPSSRMFHMFDKL 299
Cdd:PLN03140 1011 IVGLPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDEL 1090
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 300 LLISEGHPAFYGK--ARES---MEYFSSLRILPEIA--MNPAEFLLDLATgqvsdislpdelLAAktaqpdseEVLLKY- 371
Cdd:PLN03140 1091 LLMKRGGQVIYSGplGRNShkiIEYFEAIPGVPKIKekYNPATWMLEVSS------------LAA--------EVKLGId 1150
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 372 LKQRYKTdlepkeKEENHRNRKAPEHLQIAIQVKKD------WTLSWWDQF--LILSRRTFRERRRDYfDKLRLVQSLGV 443
Cdd:PLN03140 1151 FAEHYKS------SSLYQRNKALVKELSTPPPGASDlyfatqYSQSTWGQFksCLWKQWWTYWRSPDY-NLVRFFFTLAA 1223
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 444 AVVLGLLWWK--SKTDTEAHLRDQVGLMFYICIFWTSSSLFGAVYVFPFEKIYLVKERKAEMYRLSVYYVCSTLCDMVAH 521
Cdd:PLN03140 1224 ALMVGTIFWKvgTKRSNANDLTMVIGAMYAAVLFVGINNCSTVQPMVAVERTVFYRERAAGMYSALPYAIAQVVCEIPYV 1303
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 522 VLYPTFFMIIVYFMAEFNRNIPCFL------------FTVLTILLIAITSqgageflgasvlSIKRAGMIASLVLMLFLL 589
Cdd:PLN03140 1304 LIQTTYYTLIVYAMVAFEWTAAKFFwfyfisffsflyFTYYGMMTVSLTP------------NQQVAAIFAAAFYGLFNL 1371
|
570
....*....|....*..
gi 22331045 590 TGGYYVQH--IPKFMQW 604
Cdd:PLN03140 1372 FSGFFIPRpkIPKWWVW 1388
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
87-311 |
5.38e-47 |
|
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: 164.74 E-value: 5.38e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 87 TMVSKVVTHTNPDPDGYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDNVK--GKLTYNDIPYSP---SVK 161
Cdd:cd03233 3 TLSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSveGDIHYNGIPYKEfaeKYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 162 RRIGFVTQDDVLLPQLTVEETLAFAAflrlpssmskeqkyakiemiikelgleRCRrtrvGGGFVKGISGGERKRASIAY 241
Cdd:cd03233 83 GEIIYVSEEDVHFPTLTVRETLDFAL---------------------------RCK----GNEFVRGISGGERKRVSIAE 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22331045 242 EILVDPSLLLLDEPTSGLDSTSATKLLHILQGVAKA-GRTVITTIHQPSSRMFHMFDKLLLISEGHPAFYG 311
Cdd:cd03233 132 ALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVlKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
102-315 |
4.09e-44 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 158.30 E-value: 4.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 102 GYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYNDIPY---SPSVKRRIGFVTQDDVLLPQLT 178
Cdd:COG1131 11 GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLG-LLRPTSGEVRVLGEDVardPAEVRRRIGYVPQEPALYPDLT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 179 VEETLAFAAFLRlpsSMSKEQKYAKIEMIIKELGLERCRRTRVGGgfvkgISGGERKRASIAYEILVDPSLLLLDEPTSG 258
Cdd:COG1131 90 VRENLRFFARLY---GLPRKEARERIDELLELFGLTDAADRKVGT-----LSGGMKQRLGLALALLHDPELLILDEPTSG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 22331045 259 LDSTSATKLLHILQGVAKAGRTVITTIHQPsSRMFHMFDKLLLISEGHPAFYGKARE 315
Cdd:COG1131 162 LDPEARRELWELLRELAAEGKTVLLSTHYL-EEAERLCDRVAIIDKGRIVADGTPDE 217
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
104-344 |
4.94e-43 |
|
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: 155.40 E-value: 4.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 104 KHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDNvKGKLTYNDIP---YSPSVKRRIGFVTQDDVLLPQLTVE 180
Cdd:COG4555 14 VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPD-SGSILIDGEDvrkEPREARRQIGVLPDERGLYDRLTVR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 181 ETLAFAAFLRlpsSMSKEQKYAKIEMIIKELGLERCRRTRVGGgfvkgISGGERKRASIAYEILVDPSLLLLDEPTSGLD 260
Cdd:COG4555 93 ENIRYFAELY---GLFDEELKKRIEELIELLGLEEFLDRRVGE-----LSTGMKKKVALARALVHDPKVLLLDEPTNGLD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 261 STSATKLLHILQGVAKAGRTVITTIHQPSSrMFHMFDKLLLISEGHPAFYGkareSMEYFSSLRILPEIamnPAEFLLDL 340
Cdd:COG4555 165 VMARRLLREILRALKKEGKTVLFSSHIMQE-VEALCDRVVILHKGKVVAQG----SLDELREEIGEENL---EDAFVALI 236
|
....
gi 22331045 341 ATGQ 344
Cdd:COG4555 237 GSEE 240
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
93-306 |
2.36e-41 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 149.95 E-value: 2.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 93 VTHTNPDPDGYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDnVKGKLTYNDIP-YSPSVKRR-------I 164
Cdd:cd03255 6 LSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRP-TSGEVRVDGTDiSKLSEKELaafrrrhI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 165 GFVTQDDVLLPQLTVEETLAFAAFLrlpSSMSKEQKYAKIEMIIKELGLERcRRTRvgggFVKGISGGERKRASIAYEIL 244
Cdd:cd03255 85 GFVFQSFNLLPDLTALENVELPLLL---AGVPKKERRERAEELLERVGLGD-RLNH----YPSELSGGQQQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22331045 245 VDPSLLLLDEPTSGLDSTSATKLLHILQGVAK-AGRTVITTIHQPssRMFHMFDKLLLISEGH 306
Cdd:cd03255 157 NDPKIILADEPTGNLDSETGKEVMELLRELNKeAGTTIVVVTHDP--ELAEYADRIIELRDGK 217
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
100-306 |
9.71e-38 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 139.52 E-value: 9.71e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 100 PDGYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDnVKGKLTYNDIPYSPS----VKRRIGFVTQD-DVLL 174
Cdd:cd03225 10 PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGP-TSGEVLVDGKDLTKLslkeLRRKVGLVFQNpDDQF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 175 PQLTVEETLAFAAFLRlpsSMSKEQKYAKIEMIIKELGLErCRRTRVgggfVKGISGGERKRASIAyEILV-DPSLLLLD 253
Cdd:cd03225 89 FGPTVEEEVAFGLENL---GLPEEEIEERVEEALELVGLE-GLRDRS----PFTLSGGQKQRVAIA-GVLAmDPDILLLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 22331045 254 EPTSGLDSTSATKLLHILQGVAKAGRTVITTIHQPsSRMFHMFDKLLLISEGH 306
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDL-DLLLELADRVIVLEDGK 211
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
93-306 |
9.94e-38 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 140.18 E-value: 9.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 93 VTHTNPDPDGYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDNvKGKLTYNDIP---YSPSV-----KRRI 164
Cdd:COG1136 10 LTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPT-SGEVLIDGQDissLSERElarlrRRHI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 165 GFVTQDDVLLPQLTVEETLAFAAFLRlpsSMSKEQKYAKIEMIIKELGLERCRRTRVGggfvkGISGGERKRASIAYEIL 244
Cdd:COG1136 89 GFVFQFFNLLPELTALENVALPLLLA---GVSRKERRERARELLERVGLGDRLDHRPS-----QLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22331045 245 VDPSLLLLDEPTSGLDSTSATKLLHILQGVAKA-GRTVITTIHQPssRMFHMFDKLLLISEGH 306
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDP--ELAARADRVIRLRDGR 221
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
107-257 |
3.53e-37 |
|
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: 135.85 E-value: 3.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 107 LKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYNDIPYS----PSVKRRIGFVTQDDVLLPQLTVEET 182
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAG-LLSPTEGTILLDGQDLTdderKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22331045 183 LAFAAFLRLPSSMSKEqkyAKIEMIIKELGLERCRRTRVgGGFVKGISGGERKRASIAYEILVDPSLLLLDEPTS 257
Cdd:pfam00005 80 LRLGLLLKGLSKREKD---ARAEEALEKLGLGDLADRPV-GERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
100-286 |
5.09e-37 |
|
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: 138.02 E-value: 5.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 100 PDGYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDNvKGKLTYN--DIPYSP-SVKRRIGFVTQDDVLLPQ 176
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPT-SGTAYINgySIRTDRkAARQSLGYCPQFDALFDE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 177 LTVEETLAFAAFLRlpsSMSKEQKYAKIEMIIKELGLERCRRTRvgggfVKGISGGERKRASIAYEILVDPSLLLLDEPT 256
Cdd:cd03263 90 LTVREHLRFYARLK---GLPKSEIKEEVELLLRVLGLTDKANKR-----ARTLSGGMKRKLSLAIALIGGPSVLLLDEPT 161
|
170 180 190
....*....|....*....|....*....|
gi 22331045 257 SGLDSTSATKLLHILQGVaKAGRTVITTIH 286
Cdd:cd03263 162 SGLDPASRRAIWDLILEV-RKGRSIILTTH 190
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
102-306 |
6.53e-37 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 137.27 E-value: 6.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 102 GYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYN--DIPYSPSVKRRIGFVTQDDVLLPQLTV 179
Cdd:cd03259 11 GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAG-LERPDSGEILIDgrDVTGVPPERRNIGMVFQDYALFPHLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 180 EETLAFAafLRLpSSMSKEQKYAKIEMIIKELGLERCRRTRVGggfvkGISGGERKRASIAYEILVDPSLLLLDEPTSGL 259
Cdd:cd03259 90 AENIAFG--LKL-RGVPKAEIRARVRELLELVGLEGLLNRYPH-----ELSGGQQQRVALARALAREPSLLLLDEPLSAL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 22331045 260 DSTSATKLLHILQGV-AKAGRTVITTIHQPSSRMFhMFDKLLLISEGH 306
Cdd:cd03259 162 DAKLREELREELKELqRELGITTIYVTHDQEEALA-LADRIAVMNEGR 208
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
435-621 |
1.06e-36 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 136.63 E-value: 1.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 435 LRLVQSLGVAVVLGLLWWKskTDTEAHLRDQVGLMFYICIFWTSSSLFGAVYVFPFEKIYLVKERKAEMYRLSVYYVCST 514
Cdd:pfam01061 18 WRLIQPILMALIFGTLFGN--LGNQQGGLNRPGLLFFSILFNAFSALSGISPVFEKERGVLYRELASPLYSPSAYVLAKI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 515 LCDMVAHVLYPTFFMIIVYFMAEFNRNIPCFLFTVLTILLIAITSQGAGEFLGASVLSIKRAGMIASLVLMLFLLTGGYY 594
Cdd:pfam01061 96 LSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDASQLGPLVLLPLLLLSGFF 175
|
170 180
....*....|....*....|....*....
gi 22331045 595 V--QHIPKFMQWLKYLSFMHYGFRLLLKV 621
Cdd:pfam01061 176 IpiDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
93-315 |
2.66e-36 |
|
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: 136.31 E-value: 2.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 93 VTHTNPDPdgyKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYNDIPYSPS----VKRRIGFVT 168
Cdd:COG1122 6 LSFSYPGG---TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNG-LLKPTSGEVLVDGKDITKKnlreLRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 169 QDdvllP--QL---TVEETLAFAafLRlPSSMSKEQKYAKIEMIIKELGLERCRRTRVgggfvKGISGGERKRASIAyEI 243
Cdd:COG1122 82 QN----PddQLfapTVEEDVAFG--PE-NLGLPREEIRERVEEALELVGLEHLADRPP-----HELSGGQKQRVAIA-GV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22331045 244 LV-DPSLLLLDEPTSGLDSTSATKLLHILQGVAKAGRTVITTIHQPSSrMFHMFDKLLLISEGHPAFYGKARE 315
Cdd:COG1122 149 LAmEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDL-VAELADRVIVLDDGRIVADGTPRE 220
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
93-282 |
5.30e-35 |
|
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: 132.21 E-value: 5.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 93 VTHTNPDPDGYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYNDIPySPSVKRRIGFVTQDDV 172
Cdd:cd03293 6 VSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAG-LERPTSGEVLVDGEP-VTGPGPDRGYVFQQDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 173 LLPQLTVEETLAFAAFLRlpsSMSKEQKYAKIEMIIKELGLErcrrtrvggGFVKG----ISGGERKRASIAYEILVDPS 248
Cdd:cd03293 84 LLPWLTVLDNVALGLELQ---GVPKAEARERAEELLELVGLS---------GFENAyphqLSGGMRQRVALARALAVDPD 151
|
170 180 190
....*....|....*....|....*....|....*
gi 22331045 249 LLLLDEPTSGLDSTSATKL-LHILQGVAKAGRTVI 282
Cdd:cd03293 152 VLLLDEPFSALDALTREQLqEELLDIWRETGKTVL 186
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
102-315 |
7.57e-35 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 132.52 E-value: 7.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 102 GYKHILKGITGSTGPGEILALMGPSGSGKTTLLK-IMGgrLTDNVKGKLTYNDIPYSpSVKRRIGFVTQD---DVLLPqL 177
Cdd:COG1121 17 GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKaILG--LLPPTSGTVRLFGKPPR-RARRRIGYVPQRaevDWDFP-I 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 178 TVEETLAFAAF--LRLPSSMSKEQKyAKIEMIIKELGLERCRRTRVGGgfvkgISGGERKRASIAYEILVDPSLLLLDEP 255
Cdd:COG1121 93 TVRDVVLMGRYgrRGLFRRPSRADR-EAVDEALERVGLEDLADRPIGE-----LSGGQQQRVLLARALAQDPDLLLLDEP 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 256 TSGLDSTSATKLLHILQGVAKAGRTVITTIHQPSSrMFHMFDKLLLISEGHpAFYGKARE 315
Cdd:COG1121 167 FAGVDAATEEALYELLRELRREGKTILVVTHDLGA-VREYFDRVLLLNRGL-VAHGPPEE 224
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
104-315 |
1.03e-34 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 132.47 E-value: 1.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 104 KHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDNvKGKLTYNDIP---YSPS-VKRRIGFVTQDDVLLPQLTV 179
Cdd:COG1120 14 RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPS-SGEVLLDGRDlasLSRReLARRIAYVPQEPPAPFGLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 180 EETLAF--AAFLRLPSSMSKEQkYAKIEMIIKELGLERCRRTRVGggfvkGISGGERKRASIAYEILVDPSLLLLDEPTS 257
Cdd:COG1120 93 RELVALgrYPHLGLFGRPSAED-REAVEEALERTGLEHLADRPVD-----ELSGGERQRVLIARALAQEPPLLLLDEPTS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 258 GLDSTSATKLLHILQGVAK-AGRTVITTIHQPSsrMFHMF-DKLLLISEGHPAFYGKARE 315
Cdd:COG1120 167 HLDLAHQLEVLELLRRLAReRGRTVVMVLHDLN--LAARYaDRLVLLKDGRIVAQGPPEE 224
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
102-288 |
5.37e-34 |
|
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: 128.75 E-value: 5.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 102 GYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDnVKGKLTYNDIPYS---PSVKRRIGFVTQDDVLLPQLT 178
Cdd:COG4133 13 GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPP-SAGEVLWNGEPIRdarEDYRRRLAYLGHADGLKPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 179 VEETLAF-AAFLRLPSSMskeqkyAKIEMIIKELGLERCRRTRVGGgfvkgISGGERKRASIAYEILVDPSLLLLDEPTS 257
Cdd:COG4133 92 VRENLRFwAALYGLRADR------EAIDEALEAVGLAGLADLPVRQ-----LSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190
....*....|....*....|....*....|.
gi 22331045 258 GLDSTSATKLLHILQGVAKAGRTVITTIHQP 288
Cdd:COG4133 161 ALDAAGVALLAELIAAHLARGGAVLLTTHQP 191
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
104-286 |
7.69e-34 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 129.02 E-value: 7.69e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 104 KHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGG--RLTD--------NVkGKLTYNDIPYspsVKRRIGFVTQDDVL 173
Cdd:COG2884 15 REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGeeRPTSgqvlvngqDL-SRLKRREIPY---LRRRIGVVFQDFRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 174 LPQLTVEETLAFAafLRLpSSMSKEQKYAKIEMIIKELGLERcRRTRvgggFVKGISGGERKRASIAYEILVDPSLLLLD 253
Cdd:COG2884 91 LPDRTVYENVALP--LRV-TGKSRKEIRRRVREVLDLVGLSD-KAKA----LPHELSGGEQQRVAIARALVNRPELLLAD 162
|
170 180 190
....*....|....*....|....*....|...
gi 22331045 254 EPTSGLDSTSATKLLHILQGVAKAGRTVITTIH 286
Cdd:COG2884 163 EPTGNLDPETSWEIMELLEEINRRGTTVLIATH 195
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
102-315 |
1.74e-33 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 128.39 E-value: 1.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 102 GYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDNvKGKLTYNDIPYSP-------SVKRRIGFVTQDDVLL 174
Cdd:cd03261 11 GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPD-SGEVLIDGEDISGlseaelyRLRRRMGMLFQSGALF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 175 PQLTVEETLAFaaFLRLPSSMSKEQKYAKIEMIIKELGLERCRRTRVGggfvkGISGGERKRASIAYEILVDPSLLLLDE 254
Cdd:cd03261 90 DSLTVFENVAF--PLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPA-----ELSGGMKKRVALARALALDPELLLYDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22331045 255 PTSGLDSTSATKLLHILQGVAKA-GRTVITTIHQPSSrMFHMFDKLLLISEGHPAFYGKARE 315
Cdd:cd03261 163 PTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDT-AFAIADRIAVLYDGKIVAEGTPEE 223
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
104-311 |
1.93e-33 |
|
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: 127.31 E-value: 1.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 104 KHILKGITGSTGPGeILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYNDIP---YSPSVKRRIGFVTQDDVLLPQLTVE 180
Cdd:cd03264 13 KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILAT-LTPPSSGTIRIDGQDvlkQPQKLRRRIGYLPQEFGVYPNFTVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 181 ETLAFAAFL-RLPSSMSKEQkyakIEMIIKELGLERCRRTRVGGgfvkgISGGERKRASIAYEILVDPSLLLLDEPTSGL 259
Cdd:cd03264 91 EFLDYIAWLkGIPSKEVKAR----VDEVLELVNLGDRAKKKIGS-----LSGGMRRRVGIAQALVGDPSILIVDEPTAGL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 22331045 260 DSTSATKLLHILQGVAkAGRTVITTIHQPSSRMFhMFDKLLLISEGHPAFYG 311
Cdd:cd03264 162 DPEERIRFRNLLSELG-EDRIVILSTHIVEDVES-LCNQVAVLNKGKLVFEG 211
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
104-311 |
2.17e-33 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 127.26 E-value: 2.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 104 KHILKGITGSTGPGEILALMGPSGSGKTTLLK-IMGgrLTDNVKGKLTYNDIPYSPSVKRrIGFVTQD---DVLLPqLTV 179
Cdd:cd03235 12 HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKaILG--LLKPTSGSIRVFGKPLEKERKR-IGYVPQRrsiDRDFP-ISV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 180 EET--LAFAAFLRLPSSMSKEQKyAKIEMIIKELGLERCRRTRVGGgfvkgISGGERKRASIAYEILVDPSLLLLDEPTS 257
Cdd:cd03235 88 RDVvlMGLYGHKGLFRRLSKADK-AKVDEALERVGLSELADRQIGE-----LSGGQQQRVLLARALVQDPDLLLLDEPFA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 22331045 258 GLDSTSATKLLHILQGVAKAGRTVITTIHQPSSRMFHmFDKLLLIsEGHPAFYG 311
Cdd:cd03235 162 GVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEY-FDRVLLL-NRTVVASG 213
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
106-615 |
3.37e-33 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 137.28 E-value: 3.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 106 ILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDN--VKGKLTYNDIPYSPSVKRRI-GFVTQDDVLLPQLTVEET 182
Cdd:PLN03140 180 ILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkVSGEITYNGYRLNEFVPRKTsAYISQNDVHVGVMTVKET 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 183 LAFAAFLR-------LPSSMSKEQKYAKI------------------------EMIIKELGLERCRRTRVGGGFVKGISG 231
Cdd:PLN03140 260 LDFSARCQgvgtrydLLSELARREKDAGIfpeaevdlfmkatamegvksslitDYTLKILGLDICKDTIVGDEMIRGISG 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 232 GERKRASIAyEILVDPS-LLLLDEPTSGLDSTSATKLLHILQGVAKAGR-TVITTIHQPSSRMFHMFDKLLLISEGHPAF 309
Cdd:PLN03140 340 GQKKRVTTG-EMIVGPTkTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEaTVLMSLLQPAPETFDLFDDIILLSEGQIVY 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 310 YGKARESMEYFSSLRI-LPEiAMNPAEFLLDLatgqvsdislpdellaakTAQPDSEE-----------VLLKYLKQRYK 377
Cdd:PLN03140 419 QGPRDHILEFFESCGFkCPE-RKGTADFLQEV------------------TSKKDQEQywadrnkpyryISVSEFAERFK 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 378 T-----DLE-----PKEKEENHRNRKAPEHLQIAiqvKKDWTLSWWDQFLILsrrtfrERRRDYFDKLRLVQSLGVAVVL 447
Cdd:PLN03140 480 SfhvgmQLEnelsvPFDKSQSHKAALVFSKYSVP---KMELLKACWDKEWLL------MKRNAFVYVFKTVQIIIVAAIA 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 448 GLLWWKsktdTEAHLRDQVGLMFYIcifwtSSSLFGAVY-VFP-FEKIYLV--------KERKAEMYRLSVYYVCSTLCD 517
Cdd:PLN03140 551 STVFLR----TEMHTRNEEDGALYI-----GALLFSMIInMFNgFAELALMiqrlpvfyKQRDLLFHPPWTFTLPTFLLG 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 518 MVAHVLYPTFFMIIVYFMAEFNRNIPCFLFTVLTILLIAITSQGAGEFLGASVLSIKRAGMIASLVLMLFLLTGGYYV-- 595
Cdd:PLN03140 622 IPISIIESVVWVVITYYSIGFAPEASRFFKQLLLVFLIQQMAAGIFRLIASVCRTMIIANTGGALVLLLVFLLGGFILpk 701
|
570 580
....*....|....*....|
gi 22331045 596 QHIPKFMQWLKYLSFMHYGF 615
Cdd:PLN03140 702 GEIPNWWEWAYWVSPLSYGF 721
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
93-282 |
4.29e-33 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 127.90 E-value: 4.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 93 VTHTNPDPDGYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYNDIPYSPsVKRRIGFVTQDDV 172
Cdd:COG1116 13 VSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAG-LEKPTSGEVLVDGKPVTG-PGPDRGVVFQEPA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 173 LLPQLTVEETLAFAafLRLpSSMSKEQKYAKIEMIIKELGLERCRRTrvgggFVKGISGGERKRASIAYEILVDPSLLLL 252
Cdd:COG1116 91 LLPWLTVLDNVALG--LEL-RGVPKAERRERARELLELVGLAGFEDA-----YPHQLSGGMRQRVAIARALANDPEVLLM 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 22331045 253 DEPTSGLDstSATK------LLHILQgvaKAGRTVI 282
Cdd:COG1116 163 DEPFGALD--ALTRerlqdeLLRLWQ---ETGKTVL 193
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
100-315 |
1.84e-32 |
|
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: 125.76 E-value: 1.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 100 PDGyKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYNDIPYS-------PSVKRRIGFVTQDDV 172
Cdd:cd03256 11 PNG-KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNG-LVEPTSGSVLIDGTDINklkgkalRQLRRQIGMIFQQFN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 173 LLPQLTVEET-----LAFAAFLR-LPSSMSKEQKYAKIEmIIKELGLERCRRTRVGggfvkGISGGERKRASIAYEILVD 246
Cdd:cd03256 89 LIERLSVLENvlsgrLGRRSTWRsLFGLFPKEEKQRALA-ALERVGLLDKAYQRAD-----QLSGGQQQRVAIARALMQQ 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 247 PSLLLLDEPTSGLDSTSATKLLHILQGVAKA-GRTVITTIHQPSSRMFHmFDKLLLISEGHPAFYGKARE 315
Cdd:cd03256 163 PKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREY-ADRIVGLKDGRIVFDGPPAE 231
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
104-306 |
2.85e-32 |
|
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: 122.89 E-value: 2.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 104 KHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYNDIPY---SPSVKRRIGFVTQDDVLLPQLTVE 180
Cdd:cd03230 13 KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILG-LLKPDSGEIKVLGKDIkkePEEVKRRIGYLPEEPSLYENLTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 181 ETLAFaaflrlpssmskeqkyakiemiikelglercrrtrvgggfvkgiSGGERKRASIAYEILVDPSLLLLDEPTSGLD 260
Cdd:cd03230 92 ENLKL--------------------------------------------SGGMKQRLALAQALLHDPELLILDEPTSGLD 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 22331045 261 STSATKLLHILQGVAKAGRTVITTIHQPSSrMFHMFDKLLLISEGH 306
Cdd:cd03230 128 PESRREFWELLRELKKEGKTILLSSHILEE-AERLCDRVAILNNGR 172
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
116-311 |
3.00e-32 |
|
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: 124.33 E-value: 3.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 116 PGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYNDIPYS--------PSVKRRIGFVTQDDVLLPQLTVEETLAFAa 187
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAG-LEKPDGGTIVLNGTVLFdsrkkinlPPQQRKIGLVFQQYALFPHLNVRENLAFG- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 188 fLRLPSSMSKEQKYAKIemiIKELGLERCRRTRVGGgfvkgISGGERKRASIAYEILVDPSLLLLDEPTSGLDSTSATKL 267
Cdd:cd03297 100 -LKRKRNREDRISVDEL---LDLLGLDHLLNRYPAQ-----LSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 22331045 268 LHILQGVAKA-GRTVITTIHQPsSRMFHMFDKLLLISEGHPAFYG 311
Cdd:cd03297 171 LPELKQIKKNlNIPVIFVTHDL-SEAEYLADRIVVMEDGRLQYIG 214
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
102-306 |
5.20e-32 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 123.39 E-value: 5.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 102 GYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYNDIPYS----PSVKRRIGFVTQDDVLLPQl 177
Cdd:COG4619 11 GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALAD-LDPPTSGEIYLDGKPLSamppPEWRRQVAYVPQEPALWGG- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 178 TVEETLAFAAFLRlpssmSKEQKYAKIEMIIKELGL-ERCRRTRVgggfvKGISGGERKRASIAYEILVDPSLLLLDEPT 256
Cdd:COG4619 89 TVRDNLPFPFQLR-----ERKFDRERALELLERLGLpPDILDKPV-----ERLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 22331045 257 SGLDSTSATKLLHILQG-VAKAGRTVITTIHQPSSRMfHMFDKLLLISEGH 306
Cdd:COG4619 159 SALDPENTRRVEELLREyLAEEGRAVLWVSHDPEQIE-RVADRVLTLEAGR 208
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
116-260 |
6.79e-32 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 122.98 E-value: 6.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 116 PGEILALMGPSGSGKTTLLKIMGGRLTD--NVKGKLTYNDIPYS--PSVKRRIGFVTQDDVLLPQLTVEETLAFAaflrL 191
Cdd:COG4136 26 PGEILTLMGPSGSGKSTLLAAIAGTLSPafSASGEVLLNGRRLTalPAEQRRIGILFQDDLLFPHLSVGENLAFA----L 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22331045 192 PSSMSKEQKYAKIEMIIKELGLercrrtrvgGGF----VKGISGGERKRASIAYEILVDPSLLLLDEPTSGLD 260
Cdd:COG4136 102 PPTIGRAQRRARVEQALEEAGL---------AGFadrdPATLSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
104-315 |
8.53e-32 |
|
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: 123.55 E-value: 8.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 104 KHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLT-DnvKGKLTYNDIPYSP-------SVKRRIGFVTQDDVLLP 175
Cdd:COG1127 18 RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRpD--SGEILVDGQDITGlsekelyELRRRIGMLFQGGALFD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 176 QLTVEETLAFaaFLRLPSSMSKEQKYAKIEMIIKELGLErcrrtRVGGGFVKGISGGERKRASIAYEILVDPSLLLLDEP 255
Cdd:COG1127 96 SLTVFENVAF--PLREHTDLSEAEIRELVLEKLELVGLP-----GAADKMPSELSGGMRKRVALARALALDPEILLYDEP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22331045 256 TSGLDSTSATKLLH-ILQGVAKAGRTVITTIHQPSSrMFHMFDKLLLISEGHPAFYGKARE 315
Cdd:COG1127 169 TAGLDPITSAVIDElIRELRDELGLTSVVVTHDLDS-AFAIADRVAVLADGKIIAEGTPEE 228
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
100-286 |
2.52e-30 |
|
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: 118.66 E-value: 2.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 100 PDGYKhILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDNvKGKLTYNDIPYS-------PSVKRRIGFVTQDDV 172
Cdd:cd03292 11 PNGTA-ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPT-SGTIRVNGQDVSdlrgraiPYLRRKIGVVFQDFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 173 LLPQLTVEETLAFAafLRLPSSMSKE-QKyaKIEMIIKELGLERCRRTrvgggFVKGISGGERKRASIAYEILVDPSLLL 251
Cdd:cd03292 89 LLPDRNVYENVAFA--LEVTGVPPREiRK--RVPAALELVGLSHKHRA-----LPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190
....*....|....*....|....*....|....*
gi 22331045 252 LDEPTSGLDSTSATKLLHILQGVAKAGRTVITTIH 286
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATH 194
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
93-282 |
3.34e-30 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 118.76 E-value: 3.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 93 VTHTNPDPDGYKHILKGITGSTGPGEILALMGPSGSGKTTLLK-IMGgrLTDNVKGKLTYNDIPYSPSVK-------RRI 164
Cdd:cd03257 7 LSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARaILG--LLKPTSGSIIFDGKDLLKLSRrlrkirrKEI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 165 GFVTQD--DVLLPQLTVEETLAFAAFLRLPSSmSKEQKYAKIEMIIKELGLERCRRTRvgggFVKGISGGERKRASIAYE 242
Cdd:cd03257 85 QMVFQDpmSSLNPRMTIGEQIAEPLRIHGKLS-KKEARKEAVLLLLVGVGLPEEVLNR----YPHELSGGQRQRVAIARA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 22331045 243 ILVDPSLLLLDEPTSGLDSTSATKLLHILQGVAKA-GRTVI 282
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLL 200
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
99-286 |
1.78e-29 |
|
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: 116.31 E-value: 1.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 99 DPDGYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDNvKGKLTYN--DIPYSP-SVKRRIGFVTQDDVLLP 175
Cdd:cd03266 13 DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPD-AGFATVDgfDVVKEPaEARRRLGFVSDSTGLYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 176 QLTVEETLAFaaFLRLpSSMSKEQKYAKIEMIIKELGLERCRRTRVGGgfvkgISGGERKRASIAYEILVDPSLLLLDEP 255
Cdd:cd03266 92 RLTARENLEY--FAGL-YGLKGDELTARLEELADRLGMEELLDRRVGG-----FSTGMRQKVAIARALVHDPPVLLLDEP 163
|
170 180 190
....*....|....*....|....*....|.
gi 22331045 256 TSGLDSTSATKLLHILQGVAKAGRTVITTIH 286
Cdd:cd03266 164 TTGLDVMATRALREFIRQLRALGKCILFSTH 194
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
104-306 |
4.04e-29 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 113.49 E-value: 4.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 104 KHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYNDIPYS----PSVKRRIGFVtqddvllPQLtv 179
Cdd:cd00267 12 RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAG-LLKPTSGEILIDGKDIAklplEELRRRIGYV-------PQL-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 180 eetlafaaflrlpssmskeqkyakiemiikelglercrrtrvgggfvkgiSGGERKRASIAYEILVDPSLLLLDEPTSGL 259
Cdd:cd00267 82 --------------------------------------------------SGGQRQRVALARALLLNPDLLLLDEPTSGL 111
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 22331045 260 DSTSATKLLHILQGVAKAGRTVITTIHQPSSrMFHMFDKLLLISEGH 306
Cdd:cd00267 112 DPASRERLLELLRELAEEGRTVIIVTHDPEL-AELAADRVIVLKDGK 157
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
102-315 |
1.15e-28 |
|
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: 114.07 E-value: 1.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 102 GYK--HILKGITGSTGPGEILALMGPSGSGKTTLLK-IMGgrLTDNVKGKLTYN--DIPYSPS---VKRRIGFVTQDDVL 173
Cdd:cd03224 9 GYGksQILFGVSLTVPEGEIVALLGRNGAGKTTLLKtIMG--LLPPRSGSIRFDgrDITGLPPherARAGIGYVPEGRRI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 174 LPQLTVEETLAFAAFLRlpssmSKEQKYAKIEMI------IKElglercRRTRVGGGFvkgiSGGERKRASIAYEILVDP 247
Cdd:cd03224 87 FPELTVEENLLLGAYAR-----RRAKRKARLERVyelfprLKE------RRKQLAGTL----SGGEQQMLAIARALMSRP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22331045 248 SLLLLDEPTSGLDSTSATKLLHILQGVAKAGRTVItTIHQPSSRMFHMFDKLLLISEGHPAFYGKARE 315
Cdd:cd03224 152 KLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTIL-LVEQNARFALEIADRAYVLERGRVVLEGTAAE 218
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
100-318 |
1.19e-28 |
|
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: 121.02 E-value: 1.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 100 PDGyKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLtDNVKGKLTYNDIPYS----PSVKRRIGFVTQDDVLLP 175
Cdd:COG4988 347 PGG-RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFL-PPYSGSILINGVDLSdldpASWRRQIAWVPQNPYLFA 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 176 QlTVEETLAFAAflrlpSSMSKEQ-----KYAKIEMIIKEL--GLErcrrTRVG-GGFvkGISGGERKRASIAYEILVDP 247
Cdd:COG4988 425 G-TIRENLRLGR-----PDASDEEleaalEAAGLDEFVAALpdGLD----TPLGeGGR--GLSGGQAQRLALARALLRDA 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22331045 248 SLLLLDEPTSGLDSTSATKLLHILQGVAKaGRTVITTIHQPSSRMFhmFDKLLLISEGHPAFYGKARESME 318
Cdd:COG4988 493 PLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLALLAQ--ADRILVLDDGRIVEQGTHEELLA 560
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
100-345 |
1.43e-28 |
|
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: 120.39 E-value: 1.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 100 PDGYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDN--VKGKLTYNDIP---YSPSVK-RRIGFVTQD-DV 172
Cdd:COG1123 15 PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgrISGEVLLDGRDlleLSEALRgRRIGMVFQDpMT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 173 LLPQLTVEETLAFAAFLRlpsSMSKEQKYAKIEMIIKELGLERCRRTRVGGgfvkgISGGERKRASIAYEILVDPSLLLL 252
Cdd:COG1123 95 QLNPVTVGDQIAEALENL---GLSRAEARARVLELLEAVGLERRLDRYPHQ-----LSGGQRQRVAIAMALALDPDLLIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 253 DEPTSGLDSTSATKLLHILQGVAKA-GRTVITTIHQPsSRMFHMFDKLLLISEGHPAFYGKARESMEYFSSLRILPEIAM 331
Cdd:COG1123 167 DEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDL-GVVAEIADRVVVMDDGRIVEDGPPEEILAAPQALAAVPRLGA 245
|
250
....*....|....
gi 22331045 332 NPAEFLLDLATGQV 345
Cdd:COG1123 246 ARGRAAPAAAAAEP 259
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
107-286 |
2.36e-28 |
|
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: 113.58 E-value: 2.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 107 LKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDNvKGKLTYN--DIPYSPSVKRRIGFVTQDDVLLPQLTVEETLA 184
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPD-SGKILLNgkDITNLPPEKRDISYVPQNYALFPHMTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 185 FAAFLRLpssMSKEQKYAKIEMIIKELG----LERCRRTrvgggfvkgISGGERKRASIAYEILVDPSLLLLDEPTSGLD 260
Cdd:cd03299 94 YGLKKRK---VDKKEIERKVLEIAEMLGidhlLNRKPET---------LSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
170 180
....*....|....*....|....*..
gi 22331045 261 STSATKLLHILQGVAKA-GRTVITTIH 286
Cdd:cd03299 162 VRTKEKLREELKKIRKEfGVTVLHVTH 188
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
102-306 |
3.13e-28 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 111.51 E-value: 3.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 102 GYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYNDIP------YSPSVKRRIGFVTQDDVLLP 175
Cdd:cd03229 11 GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAG-LEEPDSGSILIDGEDltdledELPPLRRRIGMVFQDFALFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 176 QLTVEETLAFaaflrlpssmskeqkyakiemiikelglercrrtrvgggfvkGISGGERKRASIAYEILVDPSLLLLDEP 255
Cdd:cd03229 90 HLTVLENIAL------------------------------------------GLSGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 22331045 256 TSGLDSTSATKLLHILQGV-AKAGRTVITTIHQPSSrMFHMFDKLLLISEGH 306
Cdd:cd03229 128 TSALDPITRREVRALLKSLqAQLGITVVLVTHDLDE-AARLADRVVVLRDGK 178
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
101-318 |
4.20e-28 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 113.09 E-value: 4.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 101 DGYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGgRLTDNVKGKLTYNDIPYS----PSVKRRIGFVTQDDVLLPQ 176
Cdd:cd03253 11 DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLF-RFYDVSSGSILIDGQDIRevtlDSLRRAIGVVPQDTVLFND 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 177 lTVEETLAFAaflRLpsSMSKEQ-----KYAKIEMIIkeLGLERCRRTRVGGGFVKgISGGERKRASIAYEILVDPSLLL 251
Cdd:cd03253 90 -TIGYNIRYG---RP--DATDEEvieaaKAAQIHDKI--MRFPDGYDTIVGERGLK-LSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22331045 252 LDEPTSGLDSTSATKLLHILQGVAKaGRTVITTIHQPSSRMfhMFDKLLLISEGHPAFYGKARESME 318
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLSTIV--NADKIIVLKDGRIVERGTHEELLA 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
89-282 |
6.09e-28 |
|
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: 118.47 E-value: 6.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 89 VSKVVTHTNPDPDGYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYNDIPYSPSVK------- 161
Cdd:COG1123 263 VRNLSKRYPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLG-LLRPTSGSILFDGKDLTKLSRrslrelr 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 162 RRIGFVTQD--DVLLPQLTVEETLAFAafLRLPSSMSKEQKYAKIEMIIKELGLERCRRTRVGGGFvkgiSGGERKRASI 239
Cdd:COG1123 342 RRVQMVFQDpySSLNPRMTVGDIIAEP--LRLHGLLSRAERRERVAELLERVGLPPDLADRYPHEL----SGGQRQRVAI 415
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 22331045 240 AYEILVDPSLLLLDEPTSGLDSTSATKLLHILQGVAKA-GRTVI 282
Cdd:COG1123 416 ARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYL 459
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
100-306 |
7.11e-28 |
|
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: 110.17 E-value: 7.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 100 PDGYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMgGRLTDNVKGKLTYNDIP---YSPSVKRR-IGFVTQDDVLLP 175
Cdd:cd03228 11 PGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLL-LRLYDPTSGEILIDGVDlrdLDLESLRKnIAYVPQDPFLFS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 176 QlTVEETLafaaflrlpssmskeqkyakiemiikelglercrrtrvgggfvkgISGGERKRASIAYEILVDPSLLLLDEP 255
Cdd:cd03228 90 G-TIRENI---------------------------------------------LSGGQRQRIAIARALLRDPPILILDEA 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 22331045 256 TSGLDSTSATKLLHILQGVAKaGRTVITTIHQPSSrmFHMFDKLLLISEGH 306
Cdd:cd03228 124 TSALDPETEALILEALRALAK-GKTVIVIAHRLST--IRDADRIIVLDDGR 171
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
100-318 |
1.43e-27 |
|
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: 117.94 E-value: 1.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 100 PDGYKHILKGITGSTGPGEILALMGPSGSGKTTLLK-IMggRLTDNVKGKLTYNDIPYS----PSVKRRIGFVTQDDVLL 174
Cdd:COG4987 344 PGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLAlLL--RFLDPQSGSITLGGVDLRdldeDDLRRRIAVVPQRPHLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 175 PQlTVEETLAFAAflrlPSSmSKEQ-----KYAKIEMIIKEL--GLErcrrTRVG-GGfvKGISGGERKRASIAYEILVD 246
Cdd:COG4987 422 DT-TLRENLRLAR----PDA-TDEElwaalERVGLGDWLAALpdGLD----TWLGeGG--RRLSGGERRRLALARALLRD 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22331045 247 PSLLLLDEPTSGLDSTSATKLLHILQGVAKaGRTVITTIHQPSsrMFHMFDKLLLISEGHPAFYGKARESME 318
Cdd:COG4987 490 APILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRLA--GLERMDRILVLEDGRIVEQGTHEELLA 558
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
93-306 |
2.67e-27 |
|
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: 111.05 E-value: 2.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 93 VTHTNPDPDGYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYNDIPYSPSVK----RRIGFVT 168
Cdd:COG1124 7 LSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAG-LERPWSGEVTFDGRPVTRRRRkafrRRVQMVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 169 QD--DVLLPQLTVEETLAFAafLRLpssMSKEQKYAKIEMIIKELGLERCRRTRvgggFVKGISGGERKRASIAYEILVD 246
Cdd:COG1124 86 QDpyASLHPRHTVDRILAEP--LRI---HGLPDREERIAELLEQVGLPPSFLDR----YPHQLSGGQRQRVAIARALILE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22331045 247 PSLLLLDEPTSGLDSTSATKLLHILQGV-AKAGRTVITTIHQPsSRMFHMFDKLLLISEGH 306
Cdd:COG1124 157 PELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDL-AVVAHLCDRVAVMQNGR 216
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
102-311 |
8.94e-27 |
|
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: 108.52 E-value: 8.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 102 GYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYNDIPYSPSVKRRIGFVTQDDVLLPQLTVEE 181
Cdd:cd03269 11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILG-IILPDSGEVLFDGKPLDIAARNRIGYLPEERGLYPKMKVID 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 182 TLAFAAFLRlpsSMSKEQKYAKIEMIIKELGLERCRRTRVgggfvKGISGGERKRASIAYEILVDPSLLLLDEPTSGLDS 261
Cdd:cd03269 90 QLVYLAQLK---GLKKEEARRRIDEWLERLELSEYANKRV-----EELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 22331045 262 TSATKLLHILQGVAKAGRTVITTIHQpssrMFH---MFDKLLLISEGHPAFYG 311
Cdd:cd03269 162 VNVELLKDVIRELARAGKTVILSTHQ----MELveeLCDRVLLLNKGRAVLYG 210
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
100-289 |
1.53e-26 |
|
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: 115.32 E-value: 1.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 100 PDGYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYNDIP---YSP-SVKRRIGFVTQDDVLLP 175
Cdd:COG2274 484 PGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLG-LYEPTSGRILIDGIDlrqIDPaSLRRQIGVVLQDVFLFS 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 176 QlTVEETLAFAAflrlpSSMSKEQ-----KYAKIEMIIKEL--GLErcrrTRVG-GGfvKGISGGERKRASIAYEILVDP 247
Cdd:COG2274 563 G-TIRENITLGD-----PDATDEEiieaaRLAGLHDFIEALpmGYD----TVVGeGG--SNLSGGQRQRLAIARALLRNP 630
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 22331045 248 SLLLLDEPTSGLDSTSATKLLHILQGvAKAGRTVITTIHQPS 289
Cdd:COG2274 631 RILILDEATSALDAETEAIILENLRR-LLKGRTVIIIAHRLS 671
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
102-315 |
9.03e-26 |
|
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: 106.71 E-value: 9.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 102 GYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGG----------RLTDNVKGKLTYNDIpyspsvKRRIGFVTQD- 170
Cdd:COG1119 14 GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdlpptygndvRLFGERRGGEDVWEL------RKRIGLVSPAl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 171 -DVLLPQLTVEETLAFAAF--LRLPSSMSKEQKyAKIEMIIKELGLERCRRTRVGggfvkGISGGERKRASIAYEILVDP 247
Cdd:COG1119 88 qLRFPRDETVLDVVLSGFFdsIGLYREPTDEQR-ERARELLELLGLAHLADRPFG-----TLSQGEQRRVLIARALVKDP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22331045 248 SLLLLDEPTSGLDSTSATKLLHILQGVAKAGRTVITTI-HQ----PSSrmfhmFDKLLLISEGHPAFYGKARE 315
Cdd:COG1119 162 ELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVtHHveeiPPG-----ITHVLLLKDGRVVAAGPKEE 229
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
102-284 |
9.08e-26 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 106.11 E-value: 9.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 102 GYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMgGRLTDNVK-----------GKLTYNDIPYSPSVKRRIGFVTQD 170
Cdd:cd03260 11 GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLL-NRLNDLIPgapdegevlldGKDIYDLDVDVLELRRRVGMVFQK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 171 DVLLPqLTVEETLAFAafLRLPSSMSKEQKYAKIEMIIKELGL--ERCRRTRVGggfvkGISGGERKRASIAYEILVDPS 248
Cdd:cd03260 90 PNPFP-GSIYDNVAYG--LRLHGIKLKEELDERVEEALRKAALwdEVKDRLHAL-----GLSGGQQQRLCLARALANEPE 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 22331045 249 LLLLDEPTSGLDSTSATKLLHILQGVAKAGRTVITT 284
Cdd:cd03260 162 VLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVT 197
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
104-311 |
9.22e-26 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 104.44 E-value: 9.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 104 KHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDNvKGKLTYNDIP---YSPSVK-RRIGFVTQddvllpqltv 179
Cdd:cd03214 12 RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPS-SGEILLDGKDlasLSPKELaRKIAYVPQ---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 180 eetlafaaflrlpssmskeqkyakiemIIKELGL----ERcrrtrvgggFVKGISGGERKRASIAYEILVDPSLLLLDEP 255
Cdd:cd03214 81 ---------------------------ALELLGLahlaDR---------PFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 22331045 256 TSGLDSTSATKLLHILQGVAKA-GRTVITTIHQPsSRMFHMFDKLLLISEGHPAFYG 311
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLARErGKTVVMVLHDL-NLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
105-282 |
9.48e-26 |
|
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: 106.37 E-value: 9.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 105 HILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDNvKGKLTYN--DIPYSPSVKR-RIGFV-T-QDDVLLPQLTV 179
Cdd:cd03219 14 VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPT-SGSVLFDgeDITGLPPHEIaRLGIGrTfQIPRLFPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 180 EETLAFAAFLRLPSSM-------SKEQKYAKIEMIIKELGLERCRRTRVGGgfvkgISGGERKRASIAYEILVDPSLLLL 252
Cdd:cd03219 93 LENVMVAAQARTGSGLllararrEEREARERAEELLERVGLADLADRPAGE-----LSYGQQRRLEIARALATDPKLLLL 167
|
170 180 190
....*....|....*....|....*....|
gi 22331045 253 DEPTSGLDSTSATKLLHILQGVAKAGRTVI 282
Cdd:cd03219 168 DEPAAGLNPEETEELAELIRELRERGITVL 197
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
102-297 |
1.75e-25 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 104.65 E-value: 1.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 102 GYKH---ILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYNDIPYSPSVKRR-IGFVTQD-DVLLPQ 176
Cdd:cd03226 8 SYKKgteILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAG-LIKESSGSILLNGKPIKAKERRKsIGYVMQDvDYQLFT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 177 LTVEETLafaaflrLPSSMSKEQKYAKIEMIIKELGL----ERCRRTrvgggfvkgISGGERKRASIAYEILVDPSLLLL 252
Cdd:cd03226 87 DSVREEL-------LLGLKELDAGNEQAETVLKDLDLyalkERHPLS---------LSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 22331045 253 DEPTSGLDSTSATKLLHILQGVAKAGRTVITTIHQP------SSRMFHMFD 297
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYeflakvCDRVLLLAN 201
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
100-305 |
2.15e-25 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 104.59 E-value: 2.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 100 PDGYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYNDIPYS---PSVKRR-IGFVTQDDVLLP 175
Cdd:cd03245 13 PNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAG-LYKPTSGSVLLDGTDIRqldPADLRRnIGYVPQDVTLFY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 176 QlTVEETLAFAAflrlpssmskeqKYAKIEMIIKEL--------------GLERcrrtRVG-GGFvkGISGGERKRASIA 240
Cdd:cd03245 92 G-TLRDNITLGA------------PLADDERILRAAelagvtdfvnkhpnGLDL----QIGeRGR--GLSGGQRQAVALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22331045 241 YEILVDPSLLLLDEPTSGLDSTSATKLLHILQGVAkAGRTVITTIHQPSsrMFHMFDKLLLISEG 305
Cdd:cd03245 153 RALLNDPPILLLDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPS--LLDLVDRIIVMDSG 214
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
105-260 |
2.36e-25 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 107.88 E-value: 2.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 105 HILKGITGSTGPGEILALMGPSGSGKTTLLKIMGG--RLTDnvkGKLTYN--DIPYSPSVKRRIGFVTQDDVLLPQLTVE 180
Cdd:COG3842 19 TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGfeTPDS---GRILLDgrDVTGLPPEKRNVGMVFQDYALFPHLTVA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 181 ETLAFAafLRLpSSMSKEQKYAKIEMIIKELGLErcrrtRVGGGFVKGISGGERKRASIAYEILVDPSLLLLDEPTSGLD 260
Cdd:COG3842 96 ENVAFG--LRM-RGVPKAEIRARVAELLELVGLE-----GLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALD 167
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
102-287 |
2.57e-25 |
|
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: 104.15 E-value: 2.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 102 GYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGgRLTDNVKGKLTYNDIPYSPS------VKRRIGFVTQDDVLLP 175
Cdd:cd03262 11 GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCIN-LLEEPDSGTIIIDGLKLTDDkknineLRQKVGMVFQQFNLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 176 QLTVEETLAFAafLRLPSSMSKEQKYAKIEMIIKELGLERcrrtrVGGGFVKGISGGERKRASIAYEILVDPSLLLLDEP 255
Cdd:cd03262 90 HLTVLENITLA--PIKVKGMSKAEAEERALELLEKVGLAD-----KADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEP 162
|
170 180 190
....*....|....*....|....*....|..
gi 22331045 256 TSGLDSTSATKLLHILQGVAKAGRTVITTIHQ 287
Cdd:cd03262 163 TSALDPELVGEVLDVMKDLAEEGMTMVVVTHE 194
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
106-300 |
5.25e-25 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 103.59 E-value: 5.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 106 ILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYNDIPYSPSVKRRI--------GFVTQDDVLLPQL 177
Cdd:TIGR02211 20 VLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGG-LDNPTSGEVLFNGQSLSKLSSNERaklrnkklGFIYQFHHLLPDF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 178 TVEETLAFAAflrLPSSMSKEQKYAKIEMIIKELGLERCRRTRVGGgfvkgISGGERKRASIAYEILVDPSLLLLDEPTS 257
Cdd:TIGR02211 99 TALENVAMPL---LIGKKSVKEAKERAYEMLEKVGLEHRINHRPSE-----LSGGERQRVAIARALVNQPSLVLADEPTG 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 22331045 258 GLDSTSATKLLHILQGVAKAGRT--VITTiHQPS-----SRMFHMFDKLL 300
Cdd:TIGR02211 171 NLDNNNAKIIFDLMLELNRELNTsfLVVT-HDLElakklDRVLEMKDGQL 219
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
104-375 |
6.11e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 105.58 E-value: 6.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 104 KHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDNvKGKLTYNDIPYSPSVKRRIGFVTQDDVLLPQLTVEETL 183
Cdd:COG4152 14 KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPD-SGEVLWDGEPLDPEDRRRIGYLPEERGLYPKMKVGEQL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 184 AFAAFLRlpsSMSKEQKYAKIEMIIKELGLERCRRTRVgggfvKGISGGERKRASIAYEILVDPSLLLLDEPTSGLDSTS 263
Cdd:COG4152 93 VYLARLK---GLSKAEAKRRADEWLERLGLGDRANKKV-----EELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 264 ATKLLHILQGVAKAGRTVITTIHQpssrMFH---MFDKLLLISEGHPAFYGKARESMEYFSSLRILPEIAmNPAEFLLDL 340
Cdd:COG4152 165 VELLKDVIRELAAKGTTVIFSSHQ----MELveeLCDRIVIINKGRKVLSGSVDEIRRQFGRNTLRLEAD-GDAGWLRAL 239
|
250 260 270
....*....|....*....|....*....|....*
gi 22331045 341 AtgQVSDISLPDELLAAKTAQPDSEEVLLKYLKQR 375
Cdd:COG4152 240 P--GVTVVEEDGDGAELKLEDGADAQELLRALLAR 272
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
107-372 |
6.16e-25 |
|
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: 105.55 E-value: 6.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 107 LKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLT-DNVKGKLTYNDIPYSPS-VKRRIGFVTQDDVLLPQLTVEETLA 184
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRpTSGTARVAGYDVVREPRkVRRSIGIVPQYASVDEDLTGRENLE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 185 -FAAFLRLPSSMSKEqkyaKIEMIIKELGLERCRRTRVGGgfvkgISGGERKRASIAYEILVDPSLLLLDEPTSGLDSTS 263
Cdd:TIGR01188 89 mMGRLYGLPKDEAEE----RAEELLELFELGEAADRPVGT-----YSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 264 ATKLLHILQGVAKAGRTVITTIH------QPSSRMFHMfDKLLLISEGHP----AFYGKARESMEYFSSLRILPEIAMNP 333
Cdd:TIGR01188 160 RRAIWDYIRALKEEGVTILLTTHymeeadKLCDRIAII-DHGRIIAEGTPeelkRRLGKDTLESRPRDIQSLKVEVSMLI 238
|
250 260 270
....*....|....*....|....*....|....*....
gi 22331045 334 AEFLLDLAtgQVSDISLPDELLAAKTaqPDSEEVLLKYL 372
Cdd:TIGR01188 239 AELGETGL--GLLAVTVDSDRIKILV--PDGDETVPEIV 273
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
104-306 |
1.01e-24 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 109.10 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 104 KHILKGITGSTGPGEILALMGPSGSGKTTLLK-IMggRLTDNVKGKLTYNDIP---YSP-SVKRRIGFVTQDDVLLpQLT 178
Cdd:COG1132 353 RPVLKDISLTIPPGETVALVGPSGSGKSTLVNlLL--RFYDPTSGRILIDGVDirdLTLeSLRRQIGVVPQDTFLF-SGT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 179 VEETLAFAAflrlpSSMSKEQ-----KYAKIEMIIKEL--GLErcrrTRVGGGFVKgISGGERKRASIAYEILVDPSLLL 251
Cdd:COG1132 430 IRENIRYGR-----PDATDEEveeaaKAAQAHEFIEALpdGYD----TVVGERGVN-LSGGQRQRIAIARALLKDPPILI 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 22331045 252 LDEPTSGLDSTSATKLLHILQGVAKaGRTVITTIHQPSSRMfhMFDKLLLISEGH 306
Cdd:COG1132 500 LDEATSALDTETEALIQEALERLMK-GRTTIVIAHRLSTIR--NADRILVLDDGR 551
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
98-261 |
1.30e-24 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 103.79 E-value: 1.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 98 PDPDGYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDNvKGKLTYNDIPYS-PSVKRriGFVTQDDVLLPQ 176
Cdd:COG4525 14 PGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPS-SGEITLDGVPVTgPGADR--GVVFQKDALLPW 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 177 LTVEETLAFAafLRLpSSMSKEQKYAKIEMIIKELGLERcrrtrVGGGFVKGISGGERKRASIAYEILVDPSLLLLDEPT 256
Cdd:COG4525 91 LNVLDNVAFG--LRL-RGVPKAERRARAEELLALVGLAD-----FARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPF 162
|
....*
gi 22331045 257 SGLDS 261
Cdd:COG4525 163 GALDA 167
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
117-311 |
2.10e-24 |
|
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: 101.80 E-value: 2.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 117 GEILALMGPSGSGKTTLLKIMGGRLTDNvKGKLTYN--DIPYSPSVKRRIGFVTQDDVLLPQLTVEETLAFAaflRLPSS 194
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIAGFETPQ-SGRVLINgvDVTAAPPADRPVSMLFQENNLFAHLTVEQNVGLG---LSPGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 195 MSKEQKYAKIEMIIKELGLERCRRTRVGGgfvkgISGGERKRASIAYEILVDPSLLLLDEPTSGLDSTSATKLLHILQGV 274
Cdd:cd03298 100 KLTAEDRQAIEVALARVGLAGLEKRLPGE-----LSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDL 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 22331045 275 -AKAGRTVITTIHQPSSRMfHMFDKLLLISEGHPAFYG 311
Cdd:cd03298 175 hAETKMTVLMVTHQPEDAK-RLAQRVVFLDNGRIAAQG 211
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
93-305 |
2.27e-24 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 102.86 E-value: 2.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 93 VTHTNPDPDGyKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDNvKGKLTYNDIPYS-PSVKRriGFVTQDD 171
Cdd:PRK11248 4 ISHLYADYGG-KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQ-HGSITLDGKPVEgPGAER--GVVFQNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 172 VLLPQLTVEETLAFAafLRLpSSMSKEQKYAKIEMIIKELGLErcrrtRVGGGFVKGISGGERKRASIAYEILVDPSLLL 251
Cdd:PRK11248 80 GLLPWRNVQDNVAFG--LQL-AGVEKMQRLEIAHQMLKKVGLE-----GAEKRYIWQLSGGQRQRVGIARALAANPQLLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 22331045 252 LDEPTSGLDSTSATKLLHILQGV-AKAGRTVITTIHQPSSRMFhMFDKLLLISEG 305
Cdd:PRK11248 152 LDEPFGALDAFTREQMQTLLLKLwQETGKQVLLITHDIEEAVF-MATELVLLSPG 205
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
107-301 |
3.21e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 100.39 E-value: 3.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 107 LKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTdnvkgkltyndiPYSPSVKR----RIGFVTQ---DDVLLPqLTV 179
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLR------------PTSGTVRRaggaRVAYVPQrseVPDSLP-LTV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 180 EETLAFAAFLRL-PSSMSKEQKYAKIEMIIKELGLERCRRTRVGGgfvkgISGGERKRASIAYEILVDPSLLLLDEPTSG 258
Cdd:NF040873 75 RDLVAMGRWARRgLWRRLTRDDRAAVDDALERVGLADLAGRQLGE-----LSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 22331045 259 LDSTSATKLLHILQGVAKAGRTVITTIHQPSSRMFHmFDKLLL 301
Cdd:NF040873 150 LDAESRERIIALLAEEHARGATVVVVTHDLELVRRA-DPCVLL 191
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
114-340 |
4.01e-24 |
|
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: 104.42 E-value: 4.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 114 TGPG-EILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYNDIPYS--------PSVKRRIGFVTQDDVLLPQLTVEETLA 184
Cdd:TIGR02142 19 TLPGqGVTAIFGRSGSGKTTLIRLIAG-LTRPDEGEIVLNGRTLFdsrkgiflPPEKRRIGYVFQEARLFPHLSVRGNLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 185 FAaflrlpssMSK---EQKYAKIEMIIKELGLERCRRTRVGGgfvkgISGGERKRASIAYEILVDPSLLLLDEPTSGLDS 261
Cdd:TIGR02142 98 YG--------MKRarpSERRISFERVIELLGIGHLLGRLPGR-----LSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22331045 262 TSATKLLHILQGVAKAGRTVITTIHQPSSRMFHMFDKLLLISEGHPAFYGKARESMeyfsSLRILPEIAMNPAEFLLDL 340
Cdd:TIGR02142 165 PRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVW----ASPDLPWLAREDQGSLIEG 239
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
105-260 |
4.06e-24 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 104.38 E-value: 4.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 105 HILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTY-----NDIPysPSvKRRIGFVTQDDVLLPQLTV 179
Cdd:COG3839 17 EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAG-LEDPTSGEILIggrdvTDLP--PK-DRNIAMVFQSYALYPHMTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 180 EETLAFAafLRLpSSMSKEQKYAKIEMIIKELGLERC--RRtrvgggfVKGISGGERKRASIAYEILVDPSLLLLDEPTS 257
Cdd:COG3839 93 YENIAFP--LKL-RKVPKAEIDRRVREAAELLGLEDLldRK-------PKQLSGGQRQRVALGRALVREPKVFLLDEPLS 162
|
...
gi 22331045 258 GLD 260
Cdd:COG3839 163 NLD 165
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
102-260 |
4.13e-24 |
|
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: 101.54 E-value: 4.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 102 GYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDNvKGKLTYNDIPYS--PSVKRRIGFVTQDDVLLPQLTV 179
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPT-SGEILLDGKDITnlPPHKRPVNTVFQNYALFPHLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 180 EETLAFAafLRLPSSMSKEQKyAKIEMIIKELGLERCRRTRvgggfVKGISGGERKRASIAYEILVDPSLLLLDEPTSGL 259
Cdd:cd03300 90 FENIAFG--LRLKKLPKAEIK-ERVAEALDLVQLEGYANRK-----PSQLSGGQQQRVAIARALVNEPKVLLLDEPLGAL 161
|
.
gi 22331045 260 D 260
Cdd:cd03300 162 D 162
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
105-282 |
4.80e-24 |
|
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: 101.21 E-value: 4.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 105 HILKGITGSTGPGEILALMGPSGSGKTTLLK-IMGgrLTDNVKGKLTYN--DIPYSPS---VKRRIGFVTQDDVLLPQLT 178
Cdd:COG0410 17 HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKaISG--LLPPRSGSIRFDgeDITGLPPhriARLGIGYVPEGRRIFPSLT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 179 VEETLAFAAFLRlpssMSKEQKYAKIEMI------IKElglercRRTRVGGGfvkgISGGERKRASIAYEILVDPSLLLL 252
Cdd:COG0410 95 VEENLLLGAYAR----RDRAEVRADLERVyelfprLKE------RRRQRAGT----LSGGEQQMLAIGRALMSRPKLLLL 160
|
170 180 190
....*....|....*....|....*....|....
gi 22331045 253 DEPTSGLdstsA----TKLLHILQGVAKAGRTVI 282
Cdd:COG0410 161 DEPSLGL----AplivEEIFEIIRRLNREGVTIL 190
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
102-315 |
9.58e-24 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 100.31 E-value: 9.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 102 GYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYN--DIPYSPSVKRR---IGFVTQDDVLLPQ 176
Cdd:cd03218 11 GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVG-LVKPDSGKILLDgqDITKLPMHKRArlgIGYLPQEASIFRK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 177 LTVEETL-AFAAFLRLPssmsKEQKYAKIEMIIKELGLERCRRTRVGGgfvkgISGGERKRASIAYEILVDPSLLLLDEP 255
Cdd:cd03218 90 LTVEENIlAVLEIRGLS----KKEREEKLEELLEEFHITHLRKSKASS-----LSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 256 TSGLDSTSATKLLHILQGVAKAGRTVITTIHQpSSRMFHMFDKLLLISEGHPAFYGKARE 315
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKILKDRGIGVLITDHN-VRETLSITDRAYIIYEGKVLAEGTPEE 219
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
100-286 |
1.11e-23 |
|
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: 99.03 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 100 PDGYKhILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDNvKGKLTYNDIP--YSPS----VKRRIGFVTQD-DV 172
Cdd:TIGR01166 2 PGGPE-VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQ-SGAVLIDGEPldYSRKglleRRQRVGLVFQDpDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 173 LLPQLTVEETLAFAAflrLPSSMSKEQKYAKIEMIIKELGLE--RCRRTRVgggfvkgISGGERKRASIAYEILVDPSLL 250
Cdd:TIGR01166 80 QLFAADVDQDVAFGP---LNLGLSEAEVERRVREALTAVGASglRERPTHC-------LSGGEKKRVAIAGAVAMRPDVL 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 22331045 251 LLDEPTSGLDSTSATKLLHILQGVAKAGRTVITTIH 286
Cdd:TIGR01166 150 LLDEPTAGLDPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
102-305 |
1.53e-23 |
|
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: 99.21 E-value: 1.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 102 GYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYNDIPYS--PSVKRRIGFVTQDDVLLPQLTV 179
Cdd:cd03268 11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILG-LIKPDSGEITFDGKSYQknIEALRRIGALIEAPGFYPNLTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 180 EETL-AFAAFLRLPssmskeqkYAKIEMIIKELGLERCRRTRVgggfvKGISGGERKRASIAYEILVDPSLLLLDEPTSG 258
Cdd:cd03268 90 RENLrLLARLLGIR--------KKRIDEVLDVVGLKDSAKKKV-----KGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 22331045 259 LDSTSATKLLHILQGVAKAGRTVITTIHQpSSRMFHMFDKLLLISEG 305
Cdd:cd03268 157 LDPDGIKELRELILSLRDQGITVLISSHL-LSEIQKVADRIGIINKG 202
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
107-286 |
1.66e-23 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 99.37 E-value: 1.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 107 LKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYN--DIPYSP-SVKRRIGFVTQDDVLLPQLTVEETL 183
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTT-LLKPTSGRATVAghDVVREPrEVRRRIGIVFQDLSVDDELTGWENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 184 A-FAAFLRLPSSMSKEqkyaKIEMIIKELGLERCRRTRVgggfvKGISGGERKRASIAYEILVDPSLLLLDEPTSGLDST 262
Cdd:cd03265 95 YiHARLYGVPGAERRE----RIDELLDFVGLLEAADRLV-----KTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQ 165
|
170 180
....*....|....*....|....*
gi 22331045 263 SATKLL-HILQGVAKAGRTVITTIH 286
Cdd:cd03265 166 TRAHVWeYIEKLKEEFGMTILLTTH 190
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
100-318 |
2.12e-23 |
|
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: 104.83 E-value: 2.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 100 PDGYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGG---------RLtDNVkgkltynDI-PYSPSV-KRRIGFVT 168
Cdd:COG4618 341 PGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGvwpptagsvRL-DGA-------DLsQWDREElGRHIGYLP 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 169 QDDVLLPQlTVEETLAfaaflRLPS-SMSKEQKYAKI----EMIikeLGLERCRRTRVG-GGFvkGISGGERKRASIAYE 242
Cdd:COG4618 413 QDVELFDG-TIAENIA-----RFGDaDPEKVVAAAKLagvhEMI---LRLPDGYDTRIGeGGA--RLSGGQRQRIGLARA 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22331045 243 ILVDPSLLLLDEPTSGLDSTSATKLLHILQGVAKAGRTVITTIHQPS--SRMfhmfDKLLLISEGHPAFYGKARESME 318
Cdd:COG4618 482 LYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSllAAV----DKLLVLRDGRVQAFGPRDEVLA 555
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
116-276 |
4.20e-23 |
|
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: 101.33 E-value: 4.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 116 PGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYNDIPYS--------PSVKRRIGFVTQDDVLLPQLTVEETLAFAA 187
Cdd:COG4148 24 GRGVTALFGPSGSGKTTLLRAIAG-LERPDSGRIRLGGEVLQdsargiflPPHRRRIGYVFQEARLFPHLSVRGNLLYGR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 188 FlRLPssmsKEQKYAKIEMIIKELGLER--CRRTRvgggfvkGISGGERKRASIAYEILVDPSLLLLDEPTSGLDSTSAT 265
Cdd:COG4148 103 K-RAP----RAERRISFDEVVELLGIGHllDRRPA-------TLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKA 170
|
170
....*....|.
gi 22331045 266 KLLHILQGVAK 276
Cdd:COG4148 171 EILPYLERLRD 181
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
101-288 |
4.59e-23 |
|
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: 103.59 E-value: 4.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 101 DGYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLtDNVKGKLTYNDIPYSP----SVKRRIGFVTQDdvllPQ 176
Cdd:TIGR02868 345 PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLL-DPLQGEVTLDGVPVSSldqdEVRRRVSVCAQD----AH 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 177 L---TVEETLAFAAFLRLPSSMSKEQKYAKIEMIIKEL--GLErcrrTRVGGGfVKGISGGERKRASIAYEILVDPSLLL 251
Cdd:TIGR02868 420 LfdtTVRENLRLARPDATDEELWAALERVGLADWLRALpdGLD----TVLGEG-GARLSGGERQRLALARALLADAPILL 494
|
170 180 190
....*....|....*....|....*....|....*..
gi 22331045 252 LDEPTSGLDSTSATKLLHILQGvAKAGRTVITTIHQP 288
Cdd:TIGR02868 495 LDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
102-308 |
1.41e-22 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 97.09 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 102 GYKHILKGITGSTGPGEILALMGPSGSGKTTLLK-------IMGGRLTdnVKGkLTYNDipysPSVKRRI-----GFVTQ 169
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRcinkleeITSGDLI--VDG-LKVND----PKVDERLirqeaGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 170 DDVLLPQLTVEETLAFAAflRLPSSMSKEQKYAKIEMIIKELGL-ERcrrtrvGGGFVKGISGGERKRASIAYEILVDPS 248
Cdd:PRK09493 85 QFYLFPHLTALENVMFGP--LRVRGASKEEAEKQARELLAKVGLaER------AHHYPSELSGGQQQRVAIARALAVKPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22331045 249 LLLLDEPTSGLDSTSATKLLHILQGVAKAGRTVITTIH------QPSSRMFHMfDKLLLISEGHPA 308
Cdd:PRK09493 157 LMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHeigfaeKVASRLIFI-DKGRIAEDGDPQ 221
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
101-289 |
1.64e-22 |
|
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: 96.53 E-value: 1.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 101 DGYKHILKGITGSTGPGEILALMGPSGSGKTTLLK-IMggRLTDNVKGKLTYNDIPYSP----SVKRRIGFVTQDDVLLP 175
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINlLM--RFYDPQKGQILIDGIDIRDisrkSLRSMIGVVLQDTFLFS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 176 QlTVEETLAFAaflRLPSSMSKEQKYAK---IEMIIKEL--GLErcrrTRVG-GGfvKGISGGERKRASIAYEILVDPSL 249
Cdd:cd03254 91 G-TIMENIRLG---RPNATDEEVIEAAKeagAHDFIMKLpnGYD----TVLGeNG--GNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 22331045 250 LLLDEPTSGLDSTSATKLLHILQGVAKaGRTVITTIHQPS 289
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMK-GRTSIIIAHRLS 199
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
100-305 |
2.68e-22 |
|
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: 94.21 E-value: 2.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 100 PDGYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDnVKGKLTYNDIP---YSPSVKRR-IGFVTQDDVLLP 175
Cdd:cd03246 11 PGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRP-TSGRVRLDGADisqWDPNELGDhVGYLPQDDELFS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 176 QltveeTLAfaaflrlpssmskeqkyakiEMIikelglercrrtrvgggfvkgISGGERKRASIAYEILVDPSLLLLDEP 255
Cdd:cd03246 90 G-----SIA--------------------ENI---------------------LSGGQRQRLGLARALYGNPRILVLDEP 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 22331045 256 TSGLDSTSATKLLHILQGVAKAGRTVITTIHQPSsrMFHMFDKLLLISEG 305
Cdd:cd03246 124 NSHLDVEGERALNQAIAALKAAGATRIVIAHRPE--TLASADRILVLEDG 171
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
116-315 |
2.69e-22 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 95.98 E-value: 2.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 116 PGEILALMGPSGSGKTTLLKIMGGRLTDnVKGKLTYN--DIPYSPSVKRRIGFVTQDDVLLPQLTVEETLAFA--AFLRL 191
Cdd:COG3840 24 AGERVAILGPSGAGKSTLLNLIAGFLPP-DSGRILWNgqDLTALPPAERPVSMLFQENNLFPHLTVAQNIGLGlrPGLKL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 192 pssmSKEQKyAKIEMIIKELGLERC--RRTRVgggfvkgISGGERKRASIAYEILVDPSLLLLDEPTSGLDSTSATKLLH 269
Cdd:COG3840 103 ----TAEQR-AQVEQALERVGLAGLldRLPGQ-------LSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 22331045 270 ILQGVAKA-GRTVITTIHQPSSrMFHMFDKLLLISEGHPAFYGKARE 315
Cdd:COG3840 171 LVDELCRErGLTVLMVTHDPED-AARIADRVLLVADGRIAADGPTAA 216
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
107-306 |
3.13e-22 |
|
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: 96.25 E-value: 3.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 107 LKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDNvKGKLTYND-IPYspsvKRRIGFVTQDDVLLPQ-------LT 178
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPT-SGEVRVAGlVPW----KRRKKFLRRIGVVFGQktqlwwdLP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 179 VEETLAF-AAFLRLPSSMSKEqkyaKIEMIIKELGLERCRRTRVgggfvKGISGGERKRASIAYEILVDPSLLLLDEPTS 257
Cdd:cd03267 112 VIDSFYLlAAIYDLPPARFKK----RLDELSELLDLEELLDTPV-----RQLSLGQRMRAEIAAALLHEPEILFLDEPTI 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 22331045 258 GLDSTSATKLLHILQG-VAKAGRTVITTIHqpssrmfHMFD------KLLLISEGH 306
Cdd:cd03267 183 GLDVVAQENIRNFLKEyNRERGTTVLLTSH-------YMKDiealarRVLVIDKGR 231
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
107-261 |
3.44e-22 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 98.68 E-value: 3.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 107 LKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLT-DnvKGKLTYNDIPYS---PSVKRRIGFVTQDDVLLPQLTVEET 182
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETpD--SGRIVLNGRDLFtnlPPRERRVGFVFQHYALFPHMTVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 183 LAFAAFLRLPssmSKEQKYAKIEMIIKELGLE----RcrrtrvgggFVKGISGGERKRASIAYEILVDPSLLLLDEPTSG 258
Cdd:COG1118 96 IAFGLRVRPP---SKAEIRARVEELLELVQLEgladR---------YPSQLSGGQRQRVALARALAVEPEVLLLDEPFGA 163
|
...
gi 22331045 259 LDS 261
Cdd:COG1118 164 LDA 166
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
102-318 |
8.49e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 96.41 E-value: 8.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 102 GYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYNDIP---YSPSVKRRIGFVTQDDVLLPQLT 178
Cdd:PRK13537 18 GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLG-LTHPDAGSISLCGEPvpsRARHARQRVGVVPQFDNLDPDFT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 179 VEETL-AFAAFLrlpsSMSKEQKYAKIEMIIKELGLERCRRTRVGGgfvkgISGGERKRASIAYEILVDPSLLLLDEPTS 257
Cdd:PRK13537 97 VRENLlVFGRYF----GLSAAAARALVPPLLEFAKLENKADAKVGE-----LSGGMKRRLTLARALVNDPDVLVLDEPTT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22331045 258 GLDSTSATKLLHILQGVAKAGRTVITTIH--QPSSRMFHmfdKLLLISEGHPAFYGKARESME 318
Cdd:PRK13537 168 GLDPQARHLMWERLRSLLARGKTILLTTHfmEEAERLCD---RLCVIEEGRKIAEGAPHALIE 227
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
102-273 |
1.54e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 98.62 E-value: 1.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 102 GYKHILKGITGSTGPGEILALMGPSGSGKTT----LLKIMGGRltdnvkGKLTYNDIP---YSPS----VKRRIGFVTQD 170
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQ------GEIWFDGQPlhnLNRRqllpVRHRIQVVFQD 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 171 --DVLLPQLTVEETLAFAAFLRLPSsMSKEQKYAKIEMIIKELGLERCRRTRVGGGFvkgiSGGERKRASIAYEILVDPS 248
Cdd:PRK15134 371 pnSSLNPRLNVLQIIEEGLRVHQPT-LSAAQREQQVIAVMEEVGLDPETRHRYPAEF----SGGQRQRIAIARALILKPS 445
|
170 180
....*....|....*....|....*
gi 22331045 249 LLLLDEPTSGLDSTSATKLLHILQG 273
Cdd:PRK15134 446 LIILDEPTSSLDKTVQAQILALLKS 470
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
102-370 |
2.25e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 96.05 E-value: 2.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 102 GYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYNDIPY---SPSVKRRIGFVTQDDVLLPQLT 178
Cdd:PRK13536 52 GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILG-MTSPDAGKITVLGVPVparARLARARIGVVPQFDNLDLEFT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 179 VEETL-AFAAFLRLpssmskeqKYAKIEMIIKELgLERCRRTRVGGGFVKGISGGERKRASIAYEILVDPSLLLLDEPTS 257
Cdd:PRK13536 131 VRENLlVFGRYFGM--------STREIEAVIPSL-LEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTT 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 258 GLDSTSATKLLHILQGVAKAGRTVITTIH--QPSSRmfhMFDKLLLISEGHPAFYGKARESMEYFSSLRILPEIAMNPAE 335
Cdd:PRK13536 202 GLDPHARHLIWERLRSLLARGKTILLTTHfmEEAER---LCDRLCVLEAGRKIAEGRPHALIDEHIGCQVIEIYGGDPHE 278
|
250 260 270
....*....|....*....|....*....|....*
gi 22331045 336 fLLDLATGQVSDISLPDELLAAKTAQPDSEEVLLK 370
Cdd:PRK13536 279 -LSSLVKPYARRIEVSGETLFCYAPDPEQVRVQLR 312
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
116-282 |
3.42e-21 |
|
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: 93.56 E-value: 3.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 116 PGEILALMGPSGSGKTTLLKIMGGRLTDNvKGKLTYN--DIPYSPSVKR-RIG----F-VTQddvLLPQLTVEETLA--- 184
Cdd:COG0411 29 RGEIVGLIGPNGAGKTTLFNLITGFYRPT-SGRILFDgrDITGLPPHRIaRLGiartFqNPR---LFPELTVLENVLvaa 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 185 --------FAAFLRLPSSMSKEQK-YAKIEMIIKELGLERCRRTRVGggfvkGISGGERKRASIAYEILVDPSLLLLDEP 255
Cdd:COG0411 105 harlgrglLAALLRLPRARREEREaRERAEELLERVGLADRADEPAG-----NLSYGQQRRLEIARALATEPKLLLLDEP 179
|
170 180
....*....|....*....|....*...
gi 22331045 256 TSGLDSTSATKLLHILQGVAKA-GRTVI 282
Cdd:COG0411 180 AAGLNPEETEELAELIRRLRDErGITIL 207
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
100-307 |
3.90e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 93.99 E-value: 3.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 100 PDGYKhILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLT-DNVKGKLTYNDIPYSPS----VKRRIGFVTQ--DDV 172
Cdd:PRK13639 12 PDGTE-ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKpTSGEVLIKGEPIKYDKKslleVRKTVGIVFQnpDDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 173 LLPQlTVEETLAFAAflrLPSSMSKEQKYAKIEMIIKELGLErcrrtrvggGFVKG----ISGGERKRASIAYEILVDPS 248
Cdd:PRK13639 91 LFAP-TVEEDVAFGP---LNLGLSKEEVEKRVKEALKAVGME---------GFENKpphhLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22331045 249 LLLLDEPTSGLDSTSATKLLHILQGVAKAGRTVITTIHQ----P--SSRMFHMFDKlLLISEGHP 307
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDvdlvPvyADKVYVMSDG-KIIKEGTP 221
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
93-291 |
4.50e-21 |
|
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: 97.36 E-value: 4.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 93 VTHTNPDPDgykHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYNDIPYSP----SVKRRIGFVT 168
Cdd:TIGR02857 327 VSVAYPGRR---PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLG-FVDPTEGSIAVNGVPLADadadSWRDQIAWVP 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 169 QDDVLLPQlTVEETLAFAaflrlpssmskeQKYAKIEMIIKEL----------GLERCRRTRVG-GGfvKGISGGERKRA 237
Cdd:TIGR02857 403 QHPFLFAG-TIAENIRLA------------RPDASDAEIREALeragldefvaALPQGLDTPIGeGG--AGLSGGQAQRL 467
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 22331045 238 SIAYEILVDPSLLLLDEPTSGLDSTSATKLLHILQGVAKaGRTVITTIHQPSSR 291
Cdd:TIGR02857 468 ALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALA 520
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
104-260 |
5.00e-21 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 92.78 E-value: 5.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 104 KHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDNvKGKLTYN--DIPYSPSVKR-R--IGFvtqddvlLPQ-- 176
Cdd:COG1137 16 RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPD-SGRIFLDgeDITHLPMHKRaRlgIGY-------LPQea 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 177 -----LTVEETLAfaAFLRLpSSMSKEQKYAKIEMIIKELGLERCRRTrvgggfvKGI--SGGERKRASIAYEILVDPSL 249
Cdd:COG1137 88 sifrkLTVEDNIL--AVLEL-RKLSKKEREERLEELLEEFGITHLRKS-------KAYslSGGERRRVEIARALATNPKF 157
|
170
....*....|.
gi 22331045 250 LLLDEPTSGLD 260
Cdd:COG1137 158 ILLDEPFAGVD 168
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
116-261 |
6.03e-21 |
|
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: 92.40 E-value: 6.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 116 PGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYN--DIPYSPSVKRRIGFVTQDDVLLPQLTVEETLAFAafLRLPS 193
Cdd:cd03296 27 SGELVALLGPSGSGKTTLLRLIAG-LERPDSGTILFGgeDATDVPVQERNVGFVFQHYALFRHMTVFDNVAFG--LRVKP 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22331045 194 SMSKEQKyAKIEMIIKELgLERCRRTRVGGGFVKGISGGERKRASIAYEILVDPSLLLLDEPTSGLDS 261
Cdd:cd03296 104 RSERPPE-AEIRAKVHEL-LKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDA 169
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
102-286 |
7.85e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 92.38 E-value: 7.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 102 GYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGgRLTDNVKGKLTYNDIPYSPSVKRRIGfvtQDDVLLPQ----- 176
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFA-RLLTPQSGTVFLGDKPISMLSSRQLA---RRLALLPQhhltp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 177 --LTVEETLAF--AAFLRLPSSMSKEQKyAKIEMIIKELGLERCRRTRVgggfvKGISGGERKRASIAYEILVDPSLLLL 252
Cdd:PRK11231 89 egITVRELVAYgrSPWLSLWGRLSAEDN-ARVNQAMEQTRINHLADRRL-----TDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190
....*....|....*....|....*....|....
gi 22331045 253 DEPTSGLDSTSATKLLHILQGVAKAGRTVITTIH 286
Cdd:PRK11231 163 DEPTTYLDINHQVELMRLMRELNTQGKTVVTVLH 196
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
93-289 |
8.00e-21 |
|
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: 91.73 E-value: 8.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 93 VTHTNPDPDGYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLtdnvkgkltynDIPYSPSVK----------- 161
Cdd:COG4181 14 LTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAG-L-----------DRPTSGTVRlagqdlfalde 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 162 --------RRIGFVTQDDVLLPQLTVEETLAFAAFLRlpsSMSKEQKYAKiemiiKELGlercrrtRVGGG-----FVKG 228
Cdd:COG4181 82 dararlraRHVGFVFQSFQLLPTLTALENVMLPLELA---GRRDARARAR-----ALLE-------RVGLGhrldhYPAQ 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22331045 229 ISGGERKRASIAYEILVDPSLLLLDEPTSGLDSTSATK---LLHILQgvAKAGRTVITTIHQPS 289
Cdd:COG4181 147 LSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQiidLLFELN--RERGTTLVLVTHDPA 208
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
102-260 |
8.95e-21 |
|
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: 91.16 E-value: 8.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 102 GYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYN--DIPYSPSVKRRIGFVTQDDVLLPQLTV 179
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAG-LEEPTSGRIYIGgrDVTDLPPKDRDIAMVFQNYALYPHMTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 180 EETLAFAAFLRlpsSMSKEQKYAKIEMIIKELGLERC--RRtrvgggfVKGISGGERKRASIAYEILVDPSLLLLDEPTS 257
Cdd:cd03301 90 YDNIAFGLKLR---KVPKDEIDERVREVAELLQIEHLldRK-------PKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
...
gi 22331045 258 GLD 260
Cdd:cd03301 160 NLD 162
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
106-289 |
1.72e-20 |
|
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: 90.75 E-value: 1.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 106 ILKGITGSTGPGEILALMGPSGSGKTTLLKIMGgRLTDNVKGKLTYNDIPYS----PSVKRRIGFVTQDdVLLPQLTVEE 181
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIP-RFYDVDSGRILIDGHDVRdytlASLRRQIGLVSQD-VFLFNDTVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 182 TLAFAaflRLPSSMSKEQKYAKI----EMIIK-ELGLErcrrTRVGGGFVKgISGGERKRASIAYEILVDPSLLLLDEPT 256
Cdd:cd03251 95 NIAYG---RPGATREEVEEAARAanahEFIMElPEGYD----TVIGERGVK-LSGGQRQRIAIARALLKDPPILILDEAT 166
|
170 180 190
....*....|....*....|....*....|...
gi 22331045 257 SGLDSTSATKLLHILQGVAKaGRTVITTIHQPS 289
Cdd:cd03251 167 SALDTESERLVQAALERLMK-NRTTFVIAHRLS 198
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
104-266 |
3.40e-20 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 90.48 E-value: 3.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 104 KHILKGITGSTGPGEILALMGPSGSGKTTLLKIMgGRLTD-----NVKGKLTYN--DIpYSPSV-----KRRIGFVTQDD 171
Cdd:COG1117 24 KQALKDINLDIPENKVTALIGPSGCGKSTLLRCL-NRMNDlipgaRVEGEILLDgeDI-YDPDVdvvelRRRVGMVFQKP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 172 VLLPqLTVEETLAFAafLRLPSSMSKEQKYAKIEMIIKELGL--ErcrrtrvgggfVK--------GISGGERKRASIAY 241
Cdd:COG1117 102 NPFP-KSIYDNVAYG--LRLHGIKSKSELDEIVEESLRKAALwdE-----------VKdrlkksalGLSGGQQQRLCIAR 167
|
170 180
....*....|....*....|....*
gi 22331045 242 EILVDPSLLLLDEPTSGLDSTSATK 266
Cdd:COG1117 168 ALAVEPEVLLMDEPTSALDPISTAK 192
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
102-282 |
4.61e-20 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 89.67 E-value: 4.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 102 GYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMgGRLTDNVKGKLTYNDIPYSPS------VKRRIGFVTQDDVLLP 175
Cdd:COG1126 12 GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCI-NLLEEPDSGTITVDGEDLTDSkkdinkLRRKVGMVFQQFNLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 176 QLTVEE--TLAfaafLRLPSSMSKEQkyakIEMIIKELgLErcrrtRVG-----GGFVKGISGGERKRASIAYEILVDPS 248
Cdd:COG1126 91 HLTVLEnvTLA----PIKVKKMSKAE----AEERAMEL-LE-----RVGladkaDAYPAQLSGGQQQRVAIARALAMEPK 156
|
170 180 190
....*....|....*....|....*....|....
gi 22331045 249 LLLLDEPTSGLDSTSATKLLHILQGVAKAGRTVI 282
Cdd:COG1126 157 VMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMV 190
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
117-286 |
4.68e-20 |
|
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: 90.05 E-value: 4.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 117 GEILALMGPSGSGKTTLLKiMGGRLTDNVKGKLTYNDIP---YSPS-VKRRIGFVTQDDVLLPQLTVEETLAFaaflrLP 192
Cdd:cd03295 27 GEFLVLIGPSGSGKTTTMK-MINRLIEPTSGEIFIDGEDireQDPVeLRRKIGYVIQQIGLFPHMTVEENIAL-----VP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 193 S--SMSKEQKYAKIEMIIKELGLErcrRTRVGGGFVKGISGGERKRASIAYEILVDPSLLLLDEPTSGLDSTSATKL--- 267
Cdd:cd03295 101 KllKWPKEKIRERADELLALVGLD---PAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLqee 177
|
170 180
....*....|....*....|
gi 22331045 268 -LHILQgvaKAGRTVITTIH 286
Cdd:cd03295 178 fKRLQQ---ELGKTIVFVTH 194
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
102-260 |
6.31e-20 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 89.26 E-value: 6.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 102 GYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYNDIPYS--PSVKRR---IGFVTQDDVLLPQ 176
Cdd:TIGR04406 12 KKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVG-LVRPDAGKILIDGQDIThlPMHERArlgIGYLPQEASIFRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 177 LTVEETLAfaAFLRLPSSMSKEQKYAKIEMIIKELGLERCRRTRVGGgfvkgISGGERKRASIAYEILVDPSLLLLDEPT 256
Cdd:TIGR04406 91 LTVEENIM--AVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMS-----LSGGERRRVEIARALATNPKFILLDEPF 163
|
....
gi 22331045 257 SGLD 260
Cdd:TIGR04406 164 AGVD 167
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
102-261 |
7.28e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 91.68 E-value: 7.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 102 GYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYN--DIPYSPSVKRRIGFVTQDDVLLPQLTV 179
Cdd:PRK10851 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAG-LEHQTSGHIRFHgtDVSRLHARDRKVGFVFQHYALFRHMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 180 EETLAFAafLRL------PSSMSKEQKYAKIemiikelgLERCRRTRVGGGFVKGISGGERKRASIAYEILVDPSLLLLD 253
Cdd:PRK10851 92 FDNIAFG--LTVlprrerPNAAAIKAKVTQL--------LEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLD 161
|
....*...
gi 22331045 254 EPTSGLDS 261
Cdd:PRK10851 162 EPFGALDA 169
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
102-260 |
8.63e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.21 E-value: 8.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 102 GYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTdnvkgkltyndiPYSPSVKR----RIGFVTQDDVLLPQL 177
Cdd:COG0488 9 GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELE------------PDSGEVSIpkglRIGYLPQEPPLDDDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 178 TVEETL------------AFAAFLRLPSSMSKEQ-KYAKIEMIIKELG---LE-RCRRTRVGGGF--------VKGISGG 232
Cdd:COG0488 77 TVLDTVldgdaelraleaELEELEAKLAEPDEDLeRLAELQEEFEALGgweAEaRAEEILSGLGFpeedldrpVSELSGG 156
|
170 180
....*....|....*....|....*...
gi 22331045 233 ERKRASIAYEILVDPSLLLLDEPTSGLD 260
Cdd:COG0488 157 WRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
106-275 |
1.10e-19 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 88.72 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 106 ILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYNDIPY---SPSVK-----RRIGFVTQDDVLLPQL 177
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGG-LDTPTSGDVIFNGQPMsklSSAAKaelrnQKLGFIYQFHHLLPDF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 178 TVEETLAFAafLRLPSSMSKEQKYAKIEMIiKELGLERCRRTRVGGgfvkgISGGERKRASIAYEILVDPSLLLLDEPTS 257
Cdd:PRK11629 103 TALENVAMP--LLIGKKKPAEINSRALEML-AAVGLEHRANHRPSE-----LSGGERQRVAIARALVNNPRLVLADEPTG 174
|
170 180
....*....|....*....|....
gi 22331045 258 GLDSTSATKLLHIL------QGVA 275
Cdd:PRK11629 175 NLDARNADSIFQLLgelnrlQGTA 198
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
104-260 |
1.32e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 88.59 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 104 KHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDNV-KGKLTYN--DI-PYSPS--VKRRIGFVTQDDVLLPQL 177
Cdd:COG0396 13 KEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKYEVtSGSILLDgeDIlELSPDerARAGIFLAFQYPVEIPGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 178 TVEETLAFAAFLRLPSSMSKEQKYAKIEMIIKELGLERCRRTR-VGGGFvkgiSGGERKRASIAYEILVDPSLLLLDEPT 256
Cdd:COG0396 93 SVSNFLRTALNARRGEELSAREFLKLLKEKMKELGLDEDFLDRyVNEGF----SGGEKKRNEILQMLLLEPKLAILDETD 168
|
....
gi 22331045 257 SGLD 260
Cdd:COG0396 169 SGLD 172
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
106-290 |
1.33e-19 |
|
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: 88.37 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 106 ILKGITGSTGPGEILALMGPSGSGKTTLLKIMGgRLTDNVKGKLTYNDIPYS----PSVKRRIGFVTQDDVLLPQlTVEE 181
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLE-RFYDPTSGEILLDGVDIRdlnlRWLRSQIGLVSQEPVLFDG-TIAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 182 TLAFAAFLRLPSSMSKEQKYAKIEMIIKEL--GLErcrrTRVGGGFVKgISGGERKRASIAYEILVDPSLLLLDEPTSGL 259
Cdd:cd03249 96 NIRYGKPDATDEEVEEAAKKANIHDFIMSLpdGYD----TLVGERGSQ-LSGGQKQRIAIARALLRNPKILLLDEATSAL 170
|
170 180 190
....*....|....*....|....*....|.
gi 22331045 260 DSTSATKLLHILQGVAKaGRTVITTIHQPSS 290
Cdd:cd03249 171 DAESEKLVQEALDRAMK-GRTTIVIAHRLST 200
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
104-317 |
1.41e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 88.41 E-value: 1.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 104 KHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDNVkGKLTYND-----IPYSPSVKRRIGFVTQDDVLLPQLT 178
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDA-GNIIIDDedislLPLHARARRGIGYLPQEASIFRRLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 179 VEETLAfaAFLRLPSSMSKEQKYAKIEMIIKELGLERCRRTrvgggFVKGISGGERKRASIAYEILVDPSLLLLDEPTSG 258
Cdd:PRK10895 95 VYDNLM--AVLQIRDDLSAEQREDRANELMEEFHIEHLRDS-----MGQSLSGGERRRVEIARALAANPKFILLDEPFAG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 22331045 259 LDSTSATKLLHILQGVAKAGRTVITTIHQPSSRMfHMFDKLLLISEGHPAFYGKARESM 317
Cdd:PRK10895 168 VDPISVIDIKRIIEHLRDSGLGVLITDHNVRETL-AVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
106-288 |
1.41e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 87.62 E-value: 1.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 106 ILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYNDIPY-SPSVKRRIGFVTQDDVLLPQLTVEETLA 184
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAG-LLPPAAGTIKLDGGDIdDPDVAEACHYLGHRNAMKPALTVAENLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 185 F-AAFLRLPSSMskeqkyakIEMIIKELGLERCRRTRVGggfvkGISGGERKRASIAYEILVDPSLLLLDEPTSGLDSTS 263
Cdd:PRK13539 96 FwAAFLGGEELD--------IAAALEAVGLAPLAHLPFG-----YLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAA 162
|
170 180
....*....|....*....|....*
gi 22331045 264 ATKLLHILQGVAKAGRTVITTIHQP 288
Cdd:PRK13539 163 VALFAELIRAHLAQGGIVIAATHIP 187
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
93-287 |
1.69e-19 |
|
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: 88.02 E-value: 1.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 93 VTHTNPDPDGYKHILKGITGSTGPGEILALMGPSGSGKTTLLK--------------IMGGRLTDNVKGKLtyndipysP 158
Cdd:cd03258 7 VSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRcinglerptsgsvlVDGTDLTLLSGKEL--------R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 159 SVKRRIGFVTQDDVLLPQLTVEETLAFAafLRLpSSMSKEQKYAKIEMIIKELGLERCRRTrvgggFVKGISGGERKRAS 238
Cdd:cd03258 79 KARRRIGMIFQHFNLLSSRTVFENVALP--LEI-AGVPKAEIEERVLELLELVGLEDKADA-----YPAQLSGGQKQRVG 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 22331045 239 IAYEILVDPSLLLLDEPTSGLDSTSATKLLHILQGV-AKAGRTVITTIHQ 287
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSILALLRDInRELGLTIVLITHE 200
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
100-305 |
2.29e-19 |
|
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: 86.21 E-value: 2.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 100 PDGYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDNvKGKLTYNDIP---YSPSVKRRIGFVTQDdvllPQ 176
Cdd:cd03247 11 PEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQ-QGEITLDGVPvsdLEKALSSLISVLNQR----PY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 177 LtveetlaFAAFLRlpssmskeqkyakiemiiKELGlercRRtrvgggfvkgISGGERKRASIAYEILVDPSLLLLDEPT 256
Cdd:cd03247 86 L-------FDTTLR------------------NNLG----RR----------FSGGERQRLALARILLQDAPIVLLDEPT 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 22331045 257 SGLDSTSATKLLHILQGVAKaGRTVITTIHQPSSrmFHMFDKLLLISEG 305
Cdd:cd03247 127 VGLDPITERQLLSLIFEVLK-DKTLIWITHHLTG--IEHMDKILFLENG 172
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
107-282 |
2.76e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 91.62 E-value: 2.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 107 LKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDNvKGKLTYNDIPYSP-----SVKRRIGFVTQDDVLLPQLTVEE 181
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPD-SGEILLDGEPVRFrsprdAQAAGIAIIHQELNLVPNLSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 182 TLAFAAFLRLPSSMSKEQKYAKIEMIIKELGLERCRRTRVGggfvkGISGGERKRASIAYEILVDPSLLLLDEPTSGLDS 261
Cdd:COG1129 99 NIFLGREPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVG-----DLSVAQQQLVEIARALSRDARVLILDEPTASLTE 173
|
170 180
....*....|....*....|.
gi 22331045 262 TSATKLLHILQGVAKAGRTVI 282
Cdd:COG1129 174 REVERLFRIIRRLKAQGVAII 194
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
102-321 |
3.23e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 87.52 E-value: 3.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 102 GYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGgRLTD-----NVKGKLTYN--DIpYSPSV-----KRRIGFVTQ 169
Cdd:PRK14239 16 NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSIN-RMNDlnpevTITGSIVYNghNI-YSPRTdtvdlRKEIGMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 170 DDVLLPqLTVEETLAFAafLRLPSSMSKEQKYAKIEMIIKELGLERCRRTRVGGGFVkGISGGERKRASIAYEILVDPSL 249
Cdd:PRK14239 94 QPNPFP-MSIYENVVYG--LRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRLHDSAL-GLSGGQQQRVCIARVLATSPKI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 250 LLLDEPTSGLDSTSATKLLHILQGVaKAGRTVITTIH--QPSSRM-----FHMFDKLLLISEGHPAFYGKAR-ESMEYFS 321
Cdd:PRK14239 170 ILLDEPTSALDPISAGKIEETLLGL-KDDYTMLLVTRsmQQASRIsdrtgFFLDGDLIEYNDTKQMFMNPKHkETEDYIS 248
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
102-284 |
4.82e-19 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 86.99 E-value: 4.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 102 GYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGgRLTDNVKGKLT----YNDIPYSPSVK------RRIGFVTQDD 171
Cdd:COG4161 13 GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLN-LLETPDSGQLNiaghQFDFSQKPSEKairllrQKVGMVFQQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 172 VLLPQLTVEETLaFAAFLRLpSSMSKEQKYAKIEMIIKELGLercrrTRVGGGFVKGISGGERKRASIAYEILVDPSLLL 251
Cdd:COG4161 92 NLWPHLTVMENL-IEAPCKV-LGLSKEQAREKAMKLLARLRL-----TDKADRFPLHLSGGQQQRVAIARALMMEPQVLL 164
|
170 180 190
....*....|....*....|....*....|....
gi 22331045 252 LDEPTSGLDSTSATKLLHILQGVAKAGRT-VITT 284
Cdd:COG4161 165 FDEPTAALDPEITAQVVEIIRELSQTGITqVIVT 198
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
100-315 |
6.82e-19 |
|
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: 86.39 E-value: 6.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 100 PDGyKHILKGITGSTGPGEILALMGPSGSGKTTLLK-IMGGRLTDNVKGKLTYNDIPY--SPSVKRRIGFVTQDDVLLPQ 176
Cdd:cd03252 12 PDG-PVILDNISLRIKPGEVVGIVGRSGSGKSTLTKlIQRFYVPENGRVLVDGHDLALadPAWLRRQVGVVLQENVLFNR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 177 lTVEETLAFAAflrlpSSMSKEQ-----KYAKIEMIIKEL--GLErcrrTRVGGGFVkGISGGERKRASIAYEILVDPSL 249
Cdd:cd03252 91 -SIRDNIALAD-----PGMSMERvieaaKLAGAHDFISELpeGYD----TIVGEQGA-GLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22331045 250 LLLDEPTSGLDSTSATKLLHILQGVAkAGRTVITTIHQPSSRMfhMFDKLLLISEGHPAFYGKARE 315
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTVK--NADRIIVMEKGRIVEQGSHDE 222
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
102-317 |
8.05e-19 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 86.71 E-value: 8.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 102 GYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDNvKGKLTYNDIP---YSPSV--KRRigfvtqddVLLPQ 176
Cdd:COG4559 12 GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPS-SGEVRLNGRPlaaWSPWElaRRR--------AVLPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 177 LTveeTLAFA-------AFLRLPSSMSKEQKYAKIEMIIKELGL----ERCRRTrvgggfvkgISGGERKR-------AS 238
Cdd:COG4559 83 HS---SLAFPftveevvALGRAPHGSSAAQDRQIVREALALVGLahlaGRSYQT---------LSGGEQQRvqlarvlAQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 239 IAYEILVDPSLLLLDEPTSGLDstsatkLLH------ILQGVAKAGRTVITTIHQPS-SRMFHmfDKLLLISEGHPAFYG 311
Cdd:COG4559 151 LWEPVDGGPRWLFLDEPTSALD------LAHqhavlrLARQLARRGGGVVAVLHDLNlAAQYA--DRILLLHQGRLVAQG 222
|
....*.
gi 22331045 312 KARESM 317
Cdd:COG4559 223 TPEEVL 228
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
103-260 |
1.12e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 85.79 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 103 YKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDNvKGKLTYNDIPY--SPSVKRRIGFVTQDDVLLPQLTVE 180
Cdd:PRK10771 11 YHHLPMRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPA-SGSLTLNGQDHttTPPSRRPVSMLFQENNLFSHLTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 181 ET--LAFAAFLRLpssmSKEQKyAKIEMIIKELGLERCrRTRVGGgfvkGISGGERKRASIAYEILVDPSLLLLDEPTSG 258
Cdd:PRK10771 90 QNigLGLNPGLKL----NAAQR-EKLHAIARQMGIEDL-LARLPG----QLSGGQRQRVALARCLVREQPILLLDEPFSA 159
|
..
gi 22331045 259 LD 260
Cdd:PRK10771 160 LD 161
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
105-319 |
1.66e-18 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 87.78 E-value: 1.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 105 HILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKL-----TYNDIPysPSvKRRIGFVTQDDVLLPQLTV 179
Cdd:PRK11000 17 VISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAG-LEDITSGDLfigekRMNDVP--PA-ERGVGMVFQSYALYPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 180 EETLAFAafLRLpSSMSKEQKYAKIEMI--IKELG--LERCRrtrvgggfvKGISGGERKRASIAYEILVDPSLLLLDEP 255
Cdd:PRK11000 93 AENMSFG--LKL-AGAKKEEINQRVNQVaeVLQLAhlLDRKP---------KALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 256 TSGLDSTSATKL------LHilqgvAKAGRTVITTIHQPSSRMfHMFDKLLLISEGHPAFYGKARESMEY 319
Cdd:PRK11000 161 LSNLDAALRVQMrieisrLH-----KRLGRTMIYVTHDQVEAM-TLADKIVVLDAGRVAQVGKPLELYHY 224
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
106-289 |
2.05e-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: 2.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 106 ILKGITGSTGPGEILALMGPSGSGKTTLLKIM-------GGRLTdnvKGKLTYN-DIPYSP------SVKRRIGFVTQDD 171
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeAGTIR---VGDITIDtARSLSQqkglirQLRQHVGFVFQNF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 172 VLLPQLTVEETLafaafLRLPSSMSKEQKYAKIEmiikelgLERCRRTRVG-----GGFVKGISGGERKRASIAYEILVD 246
Cdd:PRK11264 95 NLFPHRTVLENI-----IEGPVIVKGEPKEEATA-------RARELLAKVGlagkeTSYPRRLSGGQQQRVAIARALAMR 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 22331045 247 PSLLLLDEPTSGLDSTSATKLLHILQGVAKAGRTVITTIHQPS 289
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMS 205
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
106-286 |
3.39e-18 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 88.72 E-value: 3.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 106 ILKGITGSTGPGEILALMGPSGSGKTTLLKIM-------GGRLT-DNVkgkltynDIP-YSP-SVKRRIGFVTQDDVLL- 174
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLfrfydvtSGRILiDGQ-------DIRdVTQaSLRAAIGIVPQDTVLFn 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 175 -----------PQLTVEETLAfAAflrlpssmskeqKYAKIEMIIKEL--GLErcrrTRVGGGFVKgISGGERKRASIAY 241
Cdd:COG5265 446 dtiayniaygrPDASEEEVEA-AA------------RAAQIHDFIESLpdGYD----TRVGERGLK-LSGGEKQRVAIAR 507
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 22331045 242 EILVDPSLLLLDEPTSGLDSTSATKLLHILQGVAKaGRTVITTIH 286
Cdd:COG5265 508 TLLKNPPILIFDEATSALDSRTERAIQAALREVAR-GRTTLVIAH 551
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
100-315 |
3.93e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 85.28 E-value: 3.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 100 PDGyKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDnVKGKLTYNDIPYSPSVK------RRIGFVTQD-DV 172
Cdd:PRK13636 16 SDG-THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKP-SSGRILFDGKPIDYSRKglmklrESVGMVFQDpDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 173 LLPQLTVEETLAFAAF-LRLPssmsKEQKYAKIEMIIKELGLERCRRTRVgggfvKGISGGERKRASIAYEILVDPSLLL 251
Cdd:PRK13636 94 QLFSASVYQDVSFGAVnLKLP----EDEVRKRVDNALKRTGIEHLKDKPT-----HCLSFGQKKRVAIAGVLVMEPKVLV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22331045 252 LDEPTSGLDSTSATKLLHILQGVAKA-GRTVITTIHQPSSRMFHMfDKLLLISEGHPAFYGKARE 315
Cdd:PRK13636 165 LDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYC-DNVFVMKEGRVILQGNPKE 228
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
107-315 |
4.46e-18 |
|
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: 83.67 E-value: 4.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 107 LKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYNDIPYS-PSVKRRIGFvtQDDVLLPQLTVEETLAF 185
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISG-LAQPTSGGVILEGKQITePGPDRMVVF--QNYSLLPWLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 186 AAFLRLPSsMSKEQKYAKIEMIIKELGLERCRRTRVGGgfvkgISGGERKRASIAYEILVDPSLLLLDEPTSGLDSTSAT 265
Cdd:TIGR01184 78 AVDRVLPD-LSKSERRAIVEEHIALVGLTEAADKRPGQ-----LSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 22331045 266 KLL-HILQGVAKAGRTVITTIHQPSSRMFhMFDKLLLISEGHPAFYGKARE 315
Cdd:TIGR01184 152 NLQeELMQIWEEHRVTVLMVTHDVDEALL-LSDRVVMLTNGPAANIGQILE 201
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
106-288 |
5.12e-18 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 82.79 E-value: 5.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 106 ILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYNDIPYS---PSVKRRIGFVTQDDVLLPQLTVEET 182
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAG-LLRPDSGEVRWNGTPLAeqrDEPHENILYLGHLPGLKPELSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 183 LAF-AAFLRLPSSMskeqkyakIEMIIKELGLErcrrtrvggGF----VKGISGGERKRASIAYEILVDPSLLLLDEPTS 257
Cdd:TIGR01189 94 LHFwAAIHGGAQRT--------IEDALAAVGLT---------GFedlpAAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180 190
....*....|....*....|....*....|.
gi 22331045 258 GLDSTSATKLLHILQGVAKAGRTVITTIHQP 288
Cdd:TIGR01189 157 ALDKAGVALLAGLLRAHLARGGIVLLTTHQD 187
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
102-287 |
7.95e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 83.87 E-value: 7.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 102 GYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGG----------------RLTDNVKGKLTYNDIPYSPSVKRRIG 165
Cdd:PRK10619 16 GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFlekpsegsivvngqtiNLVRDKDGQLKVADKNQLRLLRTRLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 166 FVTQDDVLLPQLTVEETLAFAAFLRLpsSMSKEQKYAKIEMIIKELGLERcrrtRVGGGFVKGISGGERKRASIAYEILV 245
Cdd:PRK10619 96 MVFQHFNLWSHMTVLENVMEAPIQVL--GLSKQEARERAVKYLAKVGIDE----RAQGKYPVHLSGGQQQRVSIARALAM 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 22331045 246 DPSLLLLDEPTSGLDSTSATKLLHILQGVAKAGRTVITTIHQ 287
Cdd:PRK10619 170 EPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
83-286 |
1.15e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 84.37 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 83 NLVKTMVSKVVTHTNpdpdgykhILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRL--------------------- 141
Cdd:PRK13651 7 NIVKIFNKKLPTELK--------ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLlpdtgtiewifkdeknkkktk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 142 ------TDNVKGKLTYNDIPYSPSVKRRIGFVTQ-DDVLLPQLTVEETLAFAaflrlPSSM--SKEQKYAKIEMIIKELG 212
Cdd:PRK13651 79 ekekvlEKLVIQKTRFKKIKKIKEIRRRVGVVFQfAEYQLFEQTIEKDIIFG-----PVSMgvSKEEAKKRAAKYIELVG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22331045 213 LERcrrtrvggGFVK----GISGGERKRASIAYEILVDPSLLLLDEPTSGLDSTSATKLLHILQGVAKAGRTVITTIH 286
Cdd:PRK13651 154 LDE--------SYLQrspfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTH 223
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
106-286 |
1.91e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 84.89 E-value: 1.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 106 ILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDNVkGKLTYNDIPY----SPSVKRRIGFVTQDDVLLPQLTVEE 181
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTA-GTVLVAGDDVealsARAASRRVASVPQDTSLSFEFDVRQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 182 TLAFAaflRLPSsMSKEQKYAKIEMIIKELGLERCRRTRVGGGFVKGISGGERKRASIAYEILVDPSLLLLDEPTSGLDS 261
Cdd:PRK09536 97 VVEMG---RTPH-RSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDI 172
|
170 180
....*....|....*....|....*
gi 22331045 262 TSATKLLHILQGVAKAGRTVITTIH 286
Cdd:PRK09536 173 NHQVRTLELVRRLVDDGKTAVAAIH 197
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
93-290 |
2.25e-17 |
|
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: 85.92 E-value: 2.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 93 VTHTNPDPDgyKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGgRLTDNVKGKLTYNDIP---YS-PSVKRRIGFVT 168
Cdd:TIGR02203 336 VTFRYPGRD--RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIP-RFYEPDSGQILLDGHDladYTlASLRRQVALVS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 169 QDdVLLPQLTVEETLAFAAFLRLPSSMSKE---QKYAKiEMIIK-ELGLErcrrTRVGGGFVKgISGGERKRASIAYEIL 244
Cdd:TIGR02203 413 QD-VVLFNDTIANNIAYGRTEQADRAEIERalaAAYAQ-DFVDKlPLGLD----TPIGENGVL-LSGGQRQRLAIARALL 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 22331045 245 VDPSLLLLDEPTSGLDSTSATKLLHILQGVAKaGRTVITTIHQPSS 290
Cdd:TIGR02203 486 KDAPILILDEATSALDNESERLVQAALERLMQ-GRTTLVIAHRLST 530
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
104-260 |
2.27e-17 |
|
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: 81.03 E-value: 2.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 104 KHILKGITGSTGPGEILALMGPSGSGKTTLLK-IMGGRLTDNVKGKLTYndipyspsvkrrigfvtqDDVLLPQLTVEE- 181
Cdd:cd03217 13 KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKtIMGHPKYEVTEGEILF------------------KGEDITDLPPEEr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 182 -----TLAFAAFLRLPSsmskeqkyAKIEMIIKELGlercrrtrvgggfvKGISGGERKRASIAYEILVDPSLLLLDEPT 256
Cdd:cd03217 75 arlgiFLAFQYPPEIPG--------VKNADFLRYVN--------------EGFSGGEKKRNEILQLLLLEPDLAILDEPD 132
|
....
gi 22331045 257 SGLD 260
Cdd:cd03217 133 SGLD 136
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
102-305 |
2.75e-17 |
|
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: 82.16 E-value: 2.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 102 GYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYNDIPYSP-------SVKRRIGFVTQD--DV 172
Cdd:TIGR02769 22 QRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLG-LEKPAQGTVSFRGQDLYQldrkqrrAFRRDVQLVFQDspSA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 173 LLPQLTVEETLAFAafLRLPSSMSKEQKYAKIEMIIKELGLercrRTRVGGGFVKGISGGERKRASIAYEILVDPSLLLL 252
Cdd:TIGR02769 101 VNPRMTVRQIIGEP--LRHLTSLDESEQKARIAELLDMVGL----RSEDADKLPRQLSGGQLQRINIARALAVKPKLIVL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 22331045 253 DEPTSGLDSTSATKLLHILQGVAKAGRTVITTIHQPSSRMFHMFDKLLLISEG 305
Cdd:TIGR02769 175 DEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKG 227
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
102-288 |
3.10e-17 |
|
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: 80.61 E-value: 3.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 102 GYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYNDIP---YSPSVKRRIGFVTQDDVLLPQLT 178
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAG-LSPPLAGRVLLNGGPldfQRDSIARGLLYLGHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 179 VEETLAFAAFLRlpssmSKEQkyakIEMIIKELGLercrrtrvgGGF----VKGISGGERKRASIAYEILVDPSLLLLDE 254
Cdd:cd03231 90 VLENLRFWHADH-----SDEQ----VEEALARVGL---------NGFedrpVAQLSAGQQRRVALARLLLSGRPLWILDE 151
|
170 180 190
....*....|....*....|....*....|....
gi 22331045 255 PTSGLDSTSATKLLHILQGVAKAGRTVITTIHQP 288
Cdd:cd03231 152 PTTALDKAGVARFAEAMAGHCARGGMVVLTTHQD 185
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
93-288 |
4.05e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 85.55 E-value: 4.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 93 VTHTNPDPDGYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMG-------GrlTDNVKGK--LTYNDIPYSPSVKRR 163
Cdd:PRK10535 10 IRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGcldkptsG--TYRVAGQdvATLDADALAQLRREH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 164 IGFVTQDDVLLPQLTVEETLAFAAFLrlpSSMSKEQKYAKIEMIIKELGLERCRRTRVGGgfvkgISGGERKRASIAYEI 243
Cdd:PRK10535 88 FGFIFQRYHLLSHLTAAQNVEVPAVY---AGLERKQRLLRAQELLQRLGLEDRVEYQPSQ-----LSGGQQQRVSIARAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 22331045 244 LVDPSLLLLDEPTSGLDSTSATKLLHILQGVAKAGRTVITTIHQP 288
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDP 204
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
116-286 |
4.44e-17 |
|
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: 81.92 E-value: 4.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 116 PGEILALMGPSGSGKTTLLKIMGgRLTDNVKGKLTYNDIPYSPSV--------KRRIGFVTQDDVLLPQLTVEETLAFAA 187
Cdd:cd03294 49 EGEIFVIMGLSGSGKSTLLRCIN-RLIEPTSGKVLIDGQDIAAMSrkelrelrRKKISMVFQSFALLPHRTVLENVAFGL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 188 FLRlpsSMSKEQKYAKIEMIIKELGLErcrrtrvggGF----VKGISGGERKRASIAYEILVDPSLLLLDEPTSGLDSTS 263
Cdd:cd03294 128 EVQ---GVPRAEREERAAEALELVGLE---------GWehkyPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLI 195
|
170 180
....*....|....*....|....
gi 22331045 264 ATKLL-HILQGVAKAGRTVITTIH 286
Cdd:cd03294 196 RREMQdELLRLQAELQKTIVFITH 219
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
107-287 |
4.82e-17 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 84.75 E-value: 4.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 107 LKGITGSTGPGEILALMGPSGSGKTTLLKIMgGRLTDNVKGKLTYNDIP---YSPSVKR-RIGFVTQDDVLLPQlTVEET 182
Cdd:TIGR02204 356 LDGLNLTVRPGETVALVGPSGAGKSTLFQLL-LRFYDPQSGRILLDGVDlrqLDPAELRaRMALVPQDPVLFAA-SVMEN 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 183 LAFAAflrlPSSMSKEQKYAKIEMIIKE--LGLERCRRTRVGGGFVkGISGGERKRASIAYEILVDPSLLLLDEPTSGLD 260
Cdd:TIGR02204 434 IRYGR----PDATDEEVEAAARAAHAHEfiSALPEGYDTYLGERGV-TLSGGQRQRIAIARAILKDAPILLLDEATSALD 508
|
170 180
....*....|....*....|....*..
gi 22331045 261 STSATKLLHILQGVAKaGRTVITTIHQ 287
Cdd:TIGR02204 509 AESEQLVQQALETLMK-GRTTLIIAHR 534
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
110-317 |
6.64e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 80.75 E-value: 6.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 110 ITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDnvKGKLTYNDIPYS----PSVKRRIGFVTQDDVLLPQLTVEETLAf 185
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG--SGSIQFAGQPLEawsaAELARHRAYLSQQQTPPFAMPVFQYLT- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 186 aafLRLPSSMSKEQKYAKIEMIIKELG----LERCrrtrvgggfVKGISGGERKRASIAYEIL-VDPS------LLLLDE 254
Cdd:PRK03695 92 ---LHQPDKTRTEAVASALNEVAEALGlddkLGRS---------VNQLSGGEWQRVRLAAVVLqVWPDinpagqLLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22331045 255 PTSGLDSTSATKLLHILQGVAKAGRTVITTIHQpSSRMFHMFDKLLLISEGHPAFYGKARESM 317
Cdd:PRK03695 160 PMNSLDVAQQAALDRLLSELCQQGIAVVMSSHD-LNHTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
102-284 |
9.73e-17 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 80.06 E-value: 9.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 102 GYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGgRLTDNVKGKLT----YNDIPYSPSVK------RRIGFVTQDD 171
Cdd:PRK11124 13 GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLN-LLEMPRSGTLNiagnHFDFSKTPSDKairelrRNVGMVFQQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 172 VLLPQLTVEETLAFAAFLRLpsSMSKEQKYAKIEMIikelgLERCRRTRVGGGFVKGISGGERKRASIAYEILVDPSLLL 251
Cdd:PRK11124 92 NLWPHLTVQQNLIEAPCRVL--GLSKDQALARAEKL-----LERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLL 164
|
170 180 190
....*....|....*....|....*....|....
gi 22331045 252 LDEPTSGLDSTSATKLLHILQGVAKAGRT-VITT 284
Cdd:PRK11124 165 FDEPTAALDPEITAQIVSIIRELAETGITqVIVT 198
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
71-286 |
9.97e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 81.67 E-value: 9.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 71 EYKVRNSHASSANLVKTMVSKvvTHTnpdpdgYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDNvKGKLT 150
Cdd:COG4586 10 TYRVYEKEPGLKGALKGLFRR--EYR------EVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPT-SGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 151 YND-IPY--SPSVKRRIGFV----TQddvLLPQLTVEETLA-FAAFLRLPssmskEQKYAK-IEMIIKELGLERCRRTRv 221
Cdd:COG4586 81 VLGyVPFkrRKEFARRIGVVfgqrSQ---LWWDLPAIDSFRlLKAIYRIP-----DAEYKKrLDELVELLDLGELLDTP- 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22331045 222 gggfVKGISGGERKRASIAYEILVDPSLLLLDEPTSGLDSTSATKLLH-ILQGVAKAGRTVITTIH 286
Cdd:COG4586 152 ----VRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREfLKEYNRERGTTILLTSH 213
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
98-262 |
1.49e-16 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 81.25 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 98 PDPDGYKHILKGITGSTGPGEILALMGPSGSGKTTLLK-IMGgrLTDN---VKGKLTYN--DI-PYSPSVKR-----RIG 165
Cdd:COG0444 12 PTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARaILG--LLPPpgiTSGEILFDgeDLlKLSEKELRkirgrEIQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 166 FVTQD--DVLLPQLTVEETLAFAafLRLPSSMSKEQKYAKIEMIIKELGL----ERCRRtrvgggFVKGISGGERKRASI 239
Cdd:COG0444 90 MIFQDpmTSLNPVMTVGDQIAEP--LRIHGGLSKAEARERAIELLERVGLpdpeRRLDR------YPHELSGGMRQRVMI 161
|
170 180
....*....|....*....|...
gi 22331045 240 AYEILVDPSLLLLDEPTSGLDST 262
Cdd:COG0444 162 ARALALEPKLLIADEPTTALDVT 184
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
106-260 |
1.55e-16 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 79.69 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 106 ILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDNV-KGKLTYNDIP---YSPSVKRRIG-FVT-QDDVLLPQLTV 179
Cdd:CHL00131 22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKIlEGDILFKGESildLEPEERAHLGiFLAfQYPIEIPGVSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 180 EEtlafaaFLRLpSSMSKEQKYAKIEM-------IIKE----LGLERCRRTR-VGGGFvkgiSGGERKRASIAYEILVDP 247
Cdd:CHL00131 102 AD------FLRL-AYNSKRKFQGLPELdplefleIINEklklVGMDPSFLSRnVNEGF----SGGEKKRNEILQMALLDS 170
|
170
....*....|...
gi 22331045 248 SLLLLDEPTSGLD 260
Cdd:CHL00131 171 ELAILDETDSGLD 183
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
82-286 |
1.83e-16 |
|
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: 83.06 E-value: 1.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 82 ANLVKTM--VSKVVthtNPDpdgyKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDnvkgkltYN-DIPYSP 158
Cdd:TIGR03719 1 AQYIYTMnrVSKVV---PPK----KEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKD-------FNgEARPQP 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 159 SVKrrIGFVTQDDVLLPQLTV----EETLA------------FAAFLRLPSSMSK---EQkyAKIEMIIKELG------- 212
Cdd:TIGR03719 67 GIK--VGYLPQEPQLDPTKTVrenvEEGVAeikdaldrfneiSAKYAEPDADFDKlaaEQ--AELQEIIDAADawdldsq 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22331045 213 LERCR---RTRVGGGFVKGISGGERKRASIAYEILVDPSLLLLDEPTSGLDSTSATKLLHILQGVAKagrTVITTIH 286
Cdd:TIGR03719 143 LEIAMdalRCPPWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG---TVVAVTH 216
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
102-262 |
2.31e-16 |
|
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: 82.42 E-value: 2.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 102 GYKHILKGITGSTGPGEILALMGPSGSGKTTL-LKIMggRLTDNvKGKLTYNDIPYSP-------SVKRRIGFVTQDDV- 172
Cdd:COG4172 297 GHVKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALL--RLIPS-EGEIRFDGQDLDGlsrralrPLRRRMQVVFQDPFg 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 173 -LLPQLTVEETLAFAafLRL-PSSMSKEQKYAKIEMIIKELGLERCRRTRVGGGFvkgiSGGERKRASIAYEILVDPSLL 250
Cdd:COG4172 374 sLSPRMTVGQIIAEG--LRVhGPGLSAAERRARVAEALEEVGLDPAARHRYPHEF----SGGQRQRIAIARALILEPKLL 447
|
170
....*....|..
gi 22331045 251 LLDEPTSGLDST 262
Cdd:COG4172 448 VLDEPTSALDVS 459
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
102-306 |
2.51e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 78.38 E-value: 2.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 102 GYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTY--NDIPY-----SPSVKRRIGFVTQDDVLL 174
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICG-IERPSAGKIWFsgHDITRlknreVPFLRRQIGMIFQDHHLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 175 PQLTVEETLAFAAFLrlpSSMSKEQKYAKIEMIIKELGLERCRRTrvgggFVKGISGGERKRASIAYEILVDPSLLLLDE 254
Cdd:PRK10908 92 MDRTVYDNVAIPLII---AGASGDDIRRRVSAALDKVGLLDKAKN-----FPIQLSGGEQQRVGIARAVVNKPAVLLADE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 22331045 255 PTSGLDSTSATKLLHILQGVAKAGRTVITTIHQP---SSRMFhmfdKLLLISEGH 306
Cdd:PRK10908 164 PTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIgliSRRSY----RMLTLSDGH 214
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
107-291 |
2.51e-16 |
|
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: 78.63 E-value: 2.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 107 LKGITGSTGPGEILALMGPSGSGKTTLLK-IMGGRLTDnvKGKLTYN------DIPYSPSV------KRRIGFVTQDDVL 173
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKcIYGNYLPD--SGSILVRhdggwvDLAQASPReilalrRRTIGYVSQFLRV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 174 LPQLTVEETLAFAAFLRlpsSMSKEQKYAKIEMIIKELGL-ERCRR----TrvgggFvkgiSGGERKRASIAYEILVDPS 248
Cdd:COG4778 105 IPRVSALDVVAEPLLER---GVDREEARARARELLARLNLpERLWDlppaT-----F----SGGEQQRVNIARGFIADPP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 22331045 249 LLLLDEPTSGLDSTSATKLLHILQGVAKAGRTVITTIHQPSSR 291
Cdd:COG4778 173 LLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVR 215
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
102-317 |
2.52e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 79.43 E-value: 2.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 102 GYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDNvKGKLTYNDIP---YSPS--VKRRigfvtqddVLLPQ 176
Cdd:PRK13548 13 GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPD-SGEVRLNGRPladWSPAelARRR--------AVLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 177 -------LTVEETLAFAaflRLPSSMSKEQKYAKIEMIIKELGLercrrTRVGGGFVKGISGGERKRASIAyEILV---- 245
Cdd:PRK13548 84 hsslsfpFTVEEVVAMG---RAPHGLSRAEDDALVAAALAQVDL-----AHLAGRDYPQLSGGEQQRVQLA-RVLAqlwe 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 246 ---DPSLLLLDEPTSGLDSTSATKLLHILQGVA-KAGRTVITTIH---QPSsrmfhMF-DKLLLISEGHPAFYGKARESM 317
Cdd:PRK13548 155 pdgPPRWLLLDEPTSALDLAHQHHVLRLARQLAhERGLAVIVVLHdlnLAA-----RYaDRIVLLHQGRLVADGTPAEVL 229
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
102-287 |
3.56e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 79.46 E-value: 3.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 102 GYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDNvKGKLTYNDIPYSPS----VKRRIGFVTQ---DDVLL 174
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPT-SGSVLIRGEPITKEnireVRKFVGLVFQnpdDQIFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 175 PqlTVEETLAFAaflrlPSSMSKEQKYAK--IEMIIKELGLERCRrTRVGggfvKGISGGERKRASIAYEILVDPSLLLL 252
Cdd:PRK13652 94 P--TVEQDIAFG-----PINLGLDEETVAhrVSSALHMLGLEELR-DRVP----HHLSGGEKKRVAIAGVIAMEPQVLVL 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 22331045 253 DEPTSGLDSTSATKLLHILQGVAKA-GRTVITTIHQ 287
Cdd:PRK13652 162 DEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQ 197
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
104-260 |
4.47e-16 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 80.38 E-value: 4.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 104 KHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYN--DIPYSPSVKRRIGFVTQDDVLLPQLTVEE 181
Cdd:PRK09452 27 KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAG-FETPDSGRIMLDgqDITHVPAENRHVNTVFQSYALFPHMTVFE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 182 TLAFAafLRLpssmskeQKYAKIEmiIKELGLERCRRTRV---GGGFVKGISGGERKRASIAYEILVDPSLLLLDEPTSG 258
Cdd:PRK09452 106 NVAFG--LRM-------QKTPAAE--ITPRVMEALRMVQLeefAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174
|
..
gi 22331045 259 LD 260
Cdd:PRK09452 175 LD 176
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
104-260 |
4.87e-16 |
|
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: 78.07 E-value: 4.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 104 KHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDNV-KGKLTYNDI---PYSPSVKRRIG-FVT-QDDVLLPQL 177
Cdd:TIGR01978 13 KEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSYEVtSGTILFKGQdllELEPDERARAGlFLAfQYPEEIPGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 178 TVEETLAFAAFLRLPSSMSKEQKYAKIEMIIKE----LGLERCRRTR-VGGGFvkgiSGGERKRASIAYEILVDPSLLLL 252
Cdd:TIGR01978 93 SNLEFLRSALNARRSARGEEPLDLLDFEKLLKEklalLDMDEEFLNRsVNEGF----SGGEKKRNEILQMALLEPKLAIL 168
|
....*...
gi 22331045 253 DEPTSGLD 260
Cdd:TIGR01978 169 DEIDSGLD 176
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
104-288 |
7.40e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 78.17 E-value: 7.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 104 KHILKGITGSTGPGEILALMGPSGSGKTTLLKIMgGRLTD------NVKGKLTY--NDIPYSPSVKRR--IGFVTQDDVL 173
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVL-NRLIEiydskiKVDGKVLYfgKDIFQIDAIKLRkeVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 174 LPQLTVEETLAFAaflrLPSSMSKEQKYAK--IEMIIKELGLERCRRTRVGGGfVKGISGGERKRASIAYEILVDPSLLL 251
Cdd:PRK14246 102 FPHLSIYDNIAYP----LKSHGIKEKREIKkiVEECLRKVGLWKEVYDRLNSP-ASQLSGGQQQRLTIARALALKPKVLL 176
|
170 180 190
....*....|....*....|....*....|....*..
gi 22331045 252 LDEPTSGLDSTSATKLLHILQGVAKAGRTVITTiHQP 288
Cdd:PRK14246 177 MDEPTSMIDIVNSQAIEKLITELKNEIAIVIVS-HNP 212
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
102-288 |
9.49e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 77.65 E-value: 9.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 102 GYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMgGRLTD-----NVKGK--LTYNDIPYSPSV--KRRIGFVTQDDV 172
Cdd:PRK14247 14 GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVF-NRLIElypeaRVSGEvyLDGQDIFKMDVIelRRRVQMVFQIPN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 173 LLPQLTVEETLAFAAFL-RLPSsmSKEQKYAKIEMIIKELGLERCRRTRVGGGFVKgISGGERKRASIAYEILVDPSLLL 251
Cdd:PRK14247 93 PIPNLSIFENVALGLKLnRLVK--SKKELQERVRWALEKAQLWDEVKDRLDAPAGK-LSGGQQQRLCIARALAFQPEVLL 169
|
170 180 190
....*....|....*....|....*....|....*..
gi 22331045 252 LDEPTSGLDSTSATKLLHILQGVAKAgRTVITTIHQP 288
Cdd:PRK14247 170 ADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFP 205
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
117-292 |
9.58e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 79.49 E-value: 9.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 117 GEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYN--DIPYSPSVKRRIGFVTQDDVLLPQLTVEETLAFAAflrlpss 194
Cdd:PRK11607 45 GEIFALLGASGCGKSTLLRMLAG-FEQPTAGQIMLDgvDLSHVPPYQRPINMMFQSYALFPHMTVEQNIAFGL------- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 195 msKEQKYAKIEM---IIKELGLERCRRtrvgggFVK----GISGGERKRASIAYEILVDPSLLLLDEPTSGLDSTSATKL 267
Cdd:PRK11607 117 --KQDKLPKAEIasrVNEMLGLVHMQE------FAKrkphQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRM 188
|
170 180
....*....|....*....|....*.
gi 22331045 268 -LHILQGVAKAGRTVITTIHQPSSRM 292
Cdd:PRK11607 189 qLEVVDILERVGVTCVMVTHDQEEAM 214
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
106-288 |
9.59e-16 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 77.13 E-value: 9.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 106 ILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKL--------TYNDIPYSPSVKRRIGFVTQDDVLLPQL 177
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAG-LDDGSSGEVslvgqplhQMDEEARAKLRAKHVGFVFQSFMLIPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 178 TVEETLAFAAFLRLPSS-MSKEQKYAkiemIIKELGL-ERCRRtrvgggFVKGISGGERKRASIAYEILVDPSLLLLDEP 255
Cdd:PRK10584 104 NALENVELPALLRGESSrQSRNGAKA----LLEQLGLgKRLDH------LPAQLSGGEQQRVALARAFNGRPDVLFADEP 173
|
170 180 190
....*....|....*....|....*....|....
gi 22331045 256 TSGLDSTSATKLLHILQGVAKA-GRTVITTIHQP 288
Cdd:PRK10584 174 TGNLDRQTGDKIADLLFSLNREhGTTLILVTHDL 207
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
117-315 |
1.38e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 77.36 E-value: 1.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 117 GEILALMGPSGSGKTTLLKIMGGRLT-DNVKG---KLTYNDIPYSPSVKRRI-------GFVTQDDVLLPQLTVEETLAF 185
Cdd:PRK09984 30 GEMVALLGPSGSGKSTLLRHLSGLITgDKSAGshiELLGRTVQREGRLARDIrksrantGYIFQQFNLVNRLSVLENVLI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 186 AAFLRLP------SSMSKEQKYAKIEMIIKeLGLERCRRTRvgggfVKGISGGERKRASIAYEILVDPSLLLLDEPTSGL 259
Cdd:PRK09984 110 GALGSTPfwrtcfSWFTREQKQRALQALTR-VGMVHFAHQR-----VSTLSGGQQQRVAIARALMQQAKVILADEPIASL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 22331045 260 DSTSATKLLHILQGVAKA-GRTVITTIHQPSSRMFHMfDKLLLISEGHPAFYGKARE 315
Cdd:PRK09984 184 DPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYC-ERIVALRQGHVFYDGSSQQ 239
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
102-289 |
1.39e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 77.19 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 102 GYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDN----VKG--KLTYNDIpYSPS-----VKRRIGFVTQD 170
Cdd:PRK14267 15 GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearVEGevRLFGRNI-YSPDvdpieVRREVGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 171 DVLLPQLTVEETLAFAafLRLPSSM-SKEQKYAKIEMIIKELGLERCRRTRVGGgFVKGISGGERKRASIAYEILVDPSL 249
Cdd:PRK14267 94 PNPFPHLTIYDNVAIG--VKLNGLVkSKKELDERVEWALKKAALWDEVKDRLND-YPSNLSGGQRQRLVIARALAMKPKI 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 22331045 250 LLLDEPTSGLDSTSATKLLHILQGVaKAGRTVITTIHQPS 289
Cdd:PRK14267 171 LLMDEPTANIDPVGTAKIEELLFEL-KKEYTIVLVTHSPA 209
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
118-305 |
1.48e-15 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 81.21 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 118 EILALMGPSGSGKTTLLKIMGGRL-----TDNVKGKltynDIPYS-PSVKRRIGFVTQDDVLLPQLTVEETLAFAAFLRl 191
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLpptsgTVLVGGK----DIETNlDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLK- 1031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 192 psSMSKEQKYAKIEMIIKELGLERCRRTRVgggfvKGISGGERKRASIAYEILVDPSLLLLDEPTSGLDSTSATKLLHIL 271
Cdd:TIGR01257 1032 --GRSWEEAQLEMEAMLEDTGLHHKRNEEA-----QDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL 1104
|
170 180 190
....*....|....*....|....*....|....
gi 22331045 272 QGVaKAGRTVITTIHQPSSRMFhMFDKLLLISEG 305
Cdd:TIGR01257 1105 LKY-RSGRTIIMSTHHMDEADL-LGDRIAIISQG 1136
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
117-340 |
1.79e-15 |
|
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: 79.83 E-value: 1.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 117 GEILALMGPSGSGKTTLLKIMGGRLTDNvKGKLTYN-DIPYSPSvkrrigFVTQDDvllpQLTVEETLAFAAFLRLPSSM 195
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILAGVLKPD-EGEVDEDlKISYKPQ------YISPDY----DGTVEEFLRSANTDDFGSSY 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 196 SKEQkyakiemIIKELGLERCRRTRVgggfvKGISGGERKRASIAYEILVDPSLLLLDEPTSGLDS---TSATKllhILQ 272
Cdd:COG1245 435 YKTE-------IIKPLGLEKLLDKNV-----KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrLAVAK---AIR 499
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22331045 273 GVAKA-GRTVITTIHQpssrmFHMFDKL---LLISEGHPAFYGKARESMeyfsSLRilpeIAMNpaEFLLDL 340
Cdd:COG1245 500 RFAENrGKTAMVVDHD-----IYLIDYIsdrLMVFEGEPGVHGHASGPM----DMR----EGMN--RFLKEL 556
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
100-306 |
2.83e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 79.10 E-value: 2.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 100 PDGYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGgRLTDNVKGKLTYNDIP---YSPSVKRR-IGFVTQDdVLLP 175
Cdd:PRK11160 349 PDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLT-RAWDPQQGEILLNGQPiadYSEAALRQaISVVSQR-VHLF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 176 QLTVEETLAFAAflrlPSSmSKEQkyakIEMIIKELGLERCRRTRVG-------GGfvKGISGGERKRASIAYEILVDPS 248
Cdd:PRK11160 427 SATLRDNLLLAA----PNA-SDEA----LIEVLQQVGLEKLLEDDKGlnawlgeGG--RQLSGGEQRRLGIARALLHDAP 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 249 LLLLDEPTSGLDSTSATKLLHILQGVAKaGRTVITTIHqpssRMFHM--FDKLLLISEGH 306
Cdd:PRK11160 496 LLLLDEPTEGLDAETERQILELLAEHAQ-NKTVLMITH----RLTGLeqFDRICVMDNGQ 550
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
116-286 |
4.31e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 75.98 E-value: 4.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 116 PGEILALMGPSGSGKTTLLKIMGgRLTDNVKGKLTYNDIPY----SPSVKRRIGFVTQDdvlLPQ---LTVEETLAFAaf 188
Cdd:PRK10575 36 AGKVTGLIGHNGSGKSTLLKMLG-RHQPPSEGEILLDAQPLeswsSKAFARKVAYLPQQ---LPAaegMTVRELVAIG-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 189 lRLP-----SSMSKEQKyAKIEMIIKELGLercrrTRVGGGFVKGISGGERKRASIAYEILVDPSLLLLDEPTSGLDSTS 263
Cdd:PRK10575 110 -RYPwhgalGRFGAADR-EKVEEAISLVGL-----KPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAH 182
|
170 180
....*....|....*....|....
gi 22331045 264 ATKLLHILQGVAKA-GRTVITTIH 286
Cdd:PRK10575 183 QVDVLALVHRLSQErGLTVIAVLH 206
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
50-286 |
4.88e-15 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 79.67 E-value: 4.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 50 FVSTYPLEDAPLPIFLKFEDVEYKvRNSHASSANlvKTMVSKVVTHTNPDPDGYKHILKGITGSTGPGEILALMGPSGSG 129
Cdd:TIGR01257 1901 FLSRWIAEPAKEPIFDEDDDVAEE-RQRIISGGN--KTDILRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAG 1977
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 130 KTTLLKIMGGRLT-----DNVKGKLTYNDIPyspSVKRRIGFVTQDDVLLPQLTVEETLAFAAFLR-LPSSmskeqkyaK 203
Cdd:TIGR01257 1978 KTTTFKMLTGDTTvtsgdATVAGKSILTNIS---DVHQNMGYCPQFDAIDDLLTGREHLYLYARLRgVPAE--------E 2046
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 204 IEMI----IKELGLErCRRTRVGGGFvkgiSGGERKRASIAYEILVDPSLLLLDEPTSGLDSTSATKLLHILQGVAKAGR 279
Cdd:TIGR01257 2047 IEKVanwsIQSLGLS-LYADRLAGTY----SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGR 2121
|
....*..
gi 22331045 280 TVITTIH 286
Cdd:TIGR01257 2122 AVVLTSH 2128
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
104-260 |
5.15e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.18 E-value: 5.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 104 KHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTdnvkgkltyndiPYSPSVKR----RIGFVTQD-DVLLPQLT 178
Cdd:COG0488 328 KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELE------------PDSGTVKLgetvKIGYFDQHqEELDPDKT 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 179 VEETLAFAAflrlpssmskeqkyakiemiikELGLERCRRTRVGG-GF--------VKGISGGERKRASIAYEILVDPSL 249
Cdd:COG0488 396 VLDELRDGA----------------------PGGTEQEVRGYLGRfLFsgddafkpVGVLSGGEKARLALAKLLLSPPNV 453
|
170
....*....|.
gi 22331045 250 LLLDEPTSGLD 260
Cdd:COG0488 454 LLLDEPTNHLD 464
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
105-282 |
5.45e-15 |
|
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: 72.85 E-value: 5.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 105 HILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDNvKGKLTYNDIPYSP-----SVKRRIGFVTQddvllpqltv 179
Cdd:cd03216 14 KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPD-SGEILVDGKEVSFasprdARRAGIAMVYQ---------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 180 eetlafaaflrlpssmskeqkyakiemiikelglercrrtrvgggfvkgISGGERKRASIAYEILVDPSLLLLDEPTSGL 259
Cdd:cd03216 83 -------------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAAL 113
|
170 180
....*....|....*....|...
gi 22331045 260 DSTSATKLLHILQGVAKAGRTVI 282
Cdd:cd03216 114 TPAEVERLFKVIRRLRAQGVAVI 136
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
100-286 |
6.46e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 75.54 E-value: 6.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 100 PDGyKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDNvKGKLTYNDIPYSPS----VKRRIGFVTQD-DVLL 174
Cdd:PRK13647 15 KDG-TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQ-RGRVKVMGREVNAEnekwVRSKVGLVFQDpDDQV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 175 PQLTVEETLAFAaflrlPSSM--SKEQKYAKIEMIIKELGLERCRRtrvgggfvKG---ISGGERKRASIAYEILVDPSL 249
Cdd:PRK13647 93 FSSTVWDDVAFG-----PVNMglDKDEVERRVEEALKAVRMWDFRD--------KPpyhLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 22331045 250 LLLDEPTSGLDSTSATKLLHILQGVAKAGRTVITTIH 286
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATH 196
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
100-373 |
1.02e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 75.02 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 100 PDGYKhILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDNvKGKLTYN-----DIPYSPSVKRRIGFVTQD-DVL 173
Cdd:PRK13644 12 PDGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQ-KGKVLVSgidtgDFSKLQGIRKLVGIVFQNpETQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 174 LPQLTVEETLAFAA-FLRLPSSMSKEqkyaKIEMIIKELGLERCRRTRVgggfvKGISGGERKRASIAYEILVDPSLLLL 252
Cdd:PRK13644 90 FVGRTVEEDLAFGPeNLCLPPIEIRK----RVDRALAEIGLEKYRHRSP-----KTLSGGQGQCVALAGILTMEPECLIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 253 DEPTSGLDSTSATKLLHILQGVAKAGRTVITTIHQPSSrmFHMFDKLLLISEGHPAFYGKArESMEYFSSLRILpeiAMN 332
Cdd:PRK13644 161 DEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEE--LHDADRIIVMDRGKIVLEGEP-ENVLSDVSLQTL---GLT 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 22331045 333 PAEfLLDLATG-QVSDISLPDEllaaKTAQPDS--EEVLLKYLK 373
Cdd:PRK13644 235 PPS-LIELAENlKMHGVVIPWE----NTSSPSSfaEEICRLFLK 273
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
119-312 |
1.08e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 76.07 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 119 ILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYND---------IpYSPSVKRRIGFVTQDDVLLPQLTVEETLAFAafl 189
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISG-LTRPQKGRIVLNGrvlfdaekgI-CLPPEKRRIGYVFQDARLFPHYKVRGNLRYG--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 190 rlpssMSKEQKyAKIEMIIKELGLE----RCRRTrvgggfvkgISGGERKRASIAYEILVDPSLLLLDEPTSGLDSTSAT 265
Cdd:PRK11144 101 -----MAKSMV-AQFDKIVALLGIEplldRYPGS---------LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKR 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 22331045 266 KLLHILQGVAKAGRTVITTIHQPSSRMFHMFDKLLLISEGHPAFYGK 312
Cdd:PRK11144 166 ELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGP 212
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
102-286 |
1.30e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 74.64 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 102 GYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGgRLTDNVKGK--LTYNDIPY--SPSVKRRIGFVTQDDVLLPQL 177
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLS-RLMTPAHGHvwLDGEHIQHyaSKEVARRIGLLAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 178 TVEETLAFAAFLRLP--SSMSKEQKYAkIEMIIKELGLercrrTRVGGGFVKGISGGERKRASIAYEILVDPSLLLLDEP 255
Cdd:PRK10253 97 TVQELVARGRYPHQPlfTRWRKEDEEA-VTKAMQATGI-----THLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190
....*....|....*....|....*....|..
gi 22331045 256 TSGLDSTSATKLLHILQGVAKA-GRTVITTIH 286
Cdd:PRK10253 171 TTWLDISHQIDLLELLSELNREkGYTLAAVLH 202
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
93-260 |
1.32e-14 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 75.50 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 93 VTHTNPDPDGYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGG--RLTdnvKGKLTYNDIP---YSPS----VKRR 163
Cdd:COG1135 7 LSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLleRPT---SGSVLVDGVDltaLSERelraARRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 164 IGFVTQDDVLLPQLTVEETLAFAafLRLpSSMSKEQKYAKIEMIIKELGLERcrrtrvgggfvKG------ISGGERKRA 237
Cdd:COG1135 84 IGMIFQHFNLLSSRTVAENVALP--LEI-AGVPKAEIRKRVAELLELVGLSD-----------KAdaypsqLSGGQKQRV 149
|
170 180
....*....|....*....|...
gi 22331045 238 SIAYEILVDPSLLLLDEPTSGLD 260
Cdd:COG1135 150 GIARALANNPKVLLCDEATSALD 172
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
112-320 |
1.35e-14 |
|
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: 73.98 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 112 GSTGPGEILALMGPSGSGKTTLLKIMGGRLT-DNVKGKLTYNDIPYSPSvkrrigFVTQDDvllpQLTVEetlafaAFLR 190
Cdd:cd03237 20 GSISESEVIGILGPNGIGKTTFIKMLAGVLKpDEGDIEIELDTVSYKPQ------YIKADY----EGTVR------DLLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 191 LPSSMSKEQKYAKIEmIIKELGLERCRRTRVgggfvKGISGGERKRASIAYEILVDPSLLLLDEPTSGLDSTS---ATKL 267
Cdd:cd03237 84 SITKDFYTHPYFKTE-IAKPLQIEQILDREV-----PELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQrlmASKV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22331045 268 lhILQGVAKAGRTVITTIHQpssrmFHMFDKL---LLISEGHPAFYGKA------RESMEYF 320
Cdd:cd03237 158 --IRRFAENNEKTAFVVEHD-----IIMIDYLadrLIVFEGEPSVNGVAnppqslRSGMNRF 212
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
100-374 |
1.81e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 74.45 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 100 PDGYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLT--DNVKGKLTYNDIPYSP----SVKRRIGFVTQD-DV 172
Cdd:PRK13640 16 PDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLpdDNPNSKITVDGITLTAktvwDIREKVGIVFQNpDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 173 LLPQLTVEETLAFAAFLRlpsSMSKEQKYAKIEMIIKELGLERcrrtrvgggFVKG----ISGGERKRASIAYEILVDPS 248
Cdd:PRK13640 96 QFVGATVGDDVAFGLENR---AVPRPEMIKIVRDVLADVGMLD---------YIDSepanLSGGQKQRVAIAGILAVEPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 249 LLLLDEPTSGLDSTSATKLLHILQGVAKA-GRTVITTIHQPSSRmfHMFDKLLLISEGHPAFYGKAResmEYFSSLRILP 327
Cdd:PRK13640 164 IIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEA--NMADQVLVLDDGKLLAQGSPV---EIFSKVEMLK 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 22331045 328 EIAMN-PAEFLLDLATGQvSDISLPDELlaaktaqpDSEEVLLKYLKQ 374
Cdd:PRK13640 239 EIGLDiPFVYKLKNKLKE-KGISVPQEI--------NTEEKLVQYLCQ 277
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
107-306 |
2.29e-14 |
|
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: 71.69 E-value: 2.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 107 LKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYNDIPYSPS-----VKRRIGFVTQD---DVLLPQLT 178
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFG-LRPPASGEITLDGKPVTRRsprdaIRAGIAYVPEDrkrEGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 179 VEETLAFAAFLrlpssmskeqkyakiemiikelglercrrtrvgggfvkgiSGGERKRASIAYEILVDPSLLLLDEPTSG 258
Cdd:cd03215 95 VAENIALSSLL----------------------------------------SGGNQQKVVLARWLARDPRVLILDEPTRG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 22331045 259 LDsTSATKLLH-ILQGVAKAGRTVITTihqpSSRM---FHMFDKLLLISEGH 306
Cdd:cd03215 135 VD-VGAKAEIYrLIRELADAGKAVLLI----SSELdelLGLCDRILVMYEGR 181
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
105-287 |
2.60e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.98 E-value: 2.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 105 HILKGITGSTGPGEILALMGPSGSGKTTLLKIMGG-----RLTDNVKGKlTYNDIPYSPSVKRRIGFVTQDDVLLPQLTV 179
Cdd:PRK09700 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGiheptKGTITINNI-NYNKLDHKLAAQLGIGIIYQELSVIDELTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 180 EETLAFAaflRLPS---------SMSKEQKYAkiEMIIKELGLERCRRTRVGggfvkGISGGERKRASIAYEILVDPSLL 250
Cdd:PRK09700 98 LENLYIG---RHLTkkvcgvniiDWREMRVRA--AMMLLRVGLKVDLDEKVA-----NLSISHKQMLEIAKTLMLDAKVI 167
|
170 180 190
....*....|....*....|....*....|....*..
gi 22331045 251 LLDEPTSGLDSTSATKLLHILQGVAKAGRTVITTIHQ 287
Cdd:PRK09700 168 IMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHK 204
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
106-362 |
3.52e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.47 E-value: 3.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 106 ILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDNvKGKLTYNDIPY---SPSVKRRIG--FVTQDDVLLPQLTVE 180
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPD-SGTLEIGGNPCarlTPAKAHQLGiyLVPQEPLLFPNLSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 181 ETLAFaaflRLPSSMSKEQkyaKIEMIIKELGLERCRRTRVGGGFVkgisgGERKRASIAYEILVDPSLLLLDEPTSGLD 260
Cdd:PRK15439 105 ENILF----GLPKRQASMQ---KMKQLLAALGCQLDLDSSAGSLEV-----ADRQIVEILRGLMRDSRILILDEPTASLT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 261 STSATKLLHILQGVAKAGRTVITTIH------QPSSRMFHMFDkllliseGHPAFYGKAREsmeyFSSLRILPeiAMNPA 334
Cdd:PRK15439 173 PAETERLFSRIRELLAQGVGIVFISHklpeirQLADRISVMRD-------GTIALSGKTAD----LSTDDIIQ--AITPA 239
|
250 260
....*....|....*....|....*...
gi 22331045 335 EFLLDLATGQVSDISLPDELLAAKTAQP 362
Cdd:PRK15439 240 AREKSLSASQKLWLELPGNRRQQAAGAP 267
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
118-333 |
5.13e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 73.12 E-value: 5.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 118 EILALMGPSGSGKTTLLKIMGGRLTDNVkGKLTYND--IPYS-------PSVKRRIGFVTQ-DDVLLPQLTVEETLAFAa 187
Cdd:PRK13645 38 KVTCVIGTTGSGKSTMIQLTNGLIISET-GQTIVGDyaIPANlkkikevKRLRKEIGLVFQfPEYQLFQETIEKDIAFG- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 188 flrlPSSM--SKEQKYAKIEMIIKELGLER--CRRTRVGggfvkgISGGERKRASIAYEILVDPSLLLLDEPTSGLDSTS 263
Cdd:PRK13645 116 ----PVNLgeNKQEAYKKVPELLKLVQLPEdyVKRSPFE------LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKG 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 264 ATKLLHILQGVAKAGRTVITTIHQPSSRMFHMFDKLLLISEGHPAFYGkarESMEYFSSLRILPEIAMNP 333
Cdd:PRK13645 186 EEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIG---SPFEIFSNQELLTKIEIDP 252
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
116-288 |
5.27e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 71.37 E-value: 5.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 116 PGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYNDIPyspsVKRrigfvtQDDVLL-------------PQLTVEET 182
Cdd:PRK13538 26 AGELVQIEGPNGAGKTSLLRILAG-LARPDAGEVLWQGEP----IRR------QRDEYHqdllylghqpgikTELTALEN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 183 LAFAAflrlpsSMSKEQKYAKIEMIIKELGLercrrtrvgGGF----VKGISGGERKRASIAYEILVDPSLLLLDEPTSG 258
Cdd:PRK13538 95 LRFYQ------RLHGPGDDEALWEALAQVGL---------AGFedvpVRQLSAGQQRRVALARLWLTRAPLWILDEPFTA 159
|
170 180 190
....*....|....*....|....*....|
gi 22331045 259 LDSTSATKLLHILQGVAKAGRTVITTIHQP 288
Cdd:PRK13538 160 IDKQGVARLEALLAQHAEQGGMVILTTHQD 189
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
102-286 |
5.28e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 72.88 E-value: 5.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 102 GYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDNvKGKLTYN--DIP-YSPS----VKRRIGFVTQDDVLL 174
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPD-HGEILFDgeNIPaMSRSrlytVRKRMSMLFQSGALF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 175 PQLTVEETLAFAafLRLPSSMSKEQKYAKIEMIIKELGLErcrrtrvGGGFVK--GISGGERKRASIAYEILVDPSLLLL 252
Cdd:PRK11831 97 TDMNVFDNVAYP--LREHTQLPAPLLHSTVMMKLEAVGLR-------GAAKLMpsELSGGMARRAALARAIALEPDLIMF 167
|
170 180 190
....*....|....*....|....*....|....*
gi 22331045 253 DEPTSGLDSTSATKLLHILQGVAKA-GRTVITTIH 286
Cdd:PRK11831 168 DEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSH 202
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
117-306 |
5.83e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 71.83 E-value: 5.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 117 GEILALMGPSGSGKTTLLKIMGG--RLTDnvkGKLTY--NDI---PYSPSVKRRIGFVTQDDVLLPQLTVEETLAFAAFL 189
Cdd:PRK11614 31 GEIVTLIGANGAGKTTLLGTLCGdpRATS---GRIVFdgKDItdwQTAKIMREAVAIVPEGRRVFSRMTVEENLAMGGFF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 190 rlpssMSKEQKYAKIEMIIKELGLERCRRTRVGGGfvkgISGGERKRASIAYEILVDPSLLLLDEPTSGLDSTSATKLLH 269
Cdd:PRK11614 108 -----AERDQFQERIKWVYELFPRLHERRIQRAGT----MSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFD 178
|
170 180 190
....*....|....*....|....*....|....*..
gi 22331045 270 ILQGVAKAGRTvITTIHQPSSRMFHMFDKLLLISEGH 306
Cdd:PRK11614 179 TIEQLREQGMT-IFLVEQNANQALKLADRGYVLENGH 214
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
117-315 |
6.20e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 74.30 E-value: 6.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 117 GEILALMGPSGSGKTTLLKIMGgRLTDNVKGKLTYN--------DIPYSPSVKRRIGFVTQDDVLLPQLTVEETLAFAAF 188
Cdd:PRK10070 54 GEIFVIMGLSGSGKSTMVRLLN-RLIEPTRGQVLIDgvdiakisDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGME 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 189 LrlpSSMSKEQKYAKIEMIIKELGLERcrrtrVGGGFVKGISGGERKRASIAYEILVDPSLLLLDEPTSGLDSTSATKLL 268
Cdd:PRK10070 133 L---AGINAEERREKALDALRQVGLEN-----YAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQ 204
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 22331045 269 -HILQGVAKAGRTVITTIHQPSSRMfHMFDKLLLISEGHPAFYGKARE 315
Cdd:PRK10070 205 dELVKLQAKHQRTIVFISHDLDEAM-RIGDRIAIMQNGEVVQVGTPDE 251
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
116-282 |
7.06e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 74.68 E-value: 7.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 116 PGEILALMGPSGSGKTTLLKIMGGRLT-DnvKGKLTYNDIPY---SPSVKRR--IGFVTQDDVLLPQLTVEETLAFAAFL 189
Cdd:COG3845 30 PGEIHALLGENGAGKSTLMKILYGLYQpD--SGEILIDGKPVrirSPRDAIAlgIGMVHQHFMLVPNLTVAENIVLGLEP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 190 RLPSSMSKEQKYAKIEMIIKELGLE-----RcrrtrvgggfVKGISGGERKRASIAYEILVDPSLLLLDEPTSGLDSTSA 264
Cdd:COG3845 108 TKGGRLDRKAARARIRELSERYGLDvdpdaK----------VEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEA 177
|
170
....*....|....*...
gi 22331045 265 TKLLHILQGVAKAGRTVI 282
Cdd:COG3845 178 DELFEILRRLAAEGKSII 195
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
102-272 |
7.90e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 72.03 E-value: 7.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 102 GYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYNDIPYSP-------SVKRRIGFVTQDDV-- 172
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVG-LESPSQGNVSWRGEPLAKlnraqrkAFRRDIQMVFQDSIsa 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 173 LLPQLTVEETLAFAafLRLPSSMSKEQKYAKIEMIIKELGLERCRRTRVGGgfvkGISGGERKRASIAYEILVDPSLLLL 252
Cdd:PRK10419 102 VNPRKTVREIIREP--LRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPP----QLSGGQLQRVCLARALAVEPKLLIL 175
|
170 180
....*....|....*....|...
gi 22331045 253 DEPTSGLD---STSATKLLHILQ 272
Cdd:PRK10419 176 DEAVSNLDlvlQAGVIRLLKKLQ 198
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
65-323 |
8.25e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 71.65 E-value: 8.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 65 LKFEDV--EYKVRNSHASSanlvktmVSKVVTHTNPDPDGYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLT 142
Cdd:COG1134 5 IEVENVskSYRLYHEPSRS-------LKELLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 143 dnvkgkltyndiPYSPSVKR--RIGFvtqddvLL-------PQLTVEETLAF-AAFLrlpsSMSKEQKYAKIEMIIK--E 210
Cdd:COG1134 78 ------------PTSGRVEVngRVSA------LLelgagfhPELTGRENIYLnGRLL----GLSRKEIDEKFDEIVEfaE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 211 LglercrrtrvgGGF----VKGISGGERKR-A-SIAyeILVDPSLLLLDEPTSGLDSTSATKLLHILQGVAKAGRTVITT 284
Cdd:COG1134 136 L-----------GDFidqpVKTYSSGMRARlAfAVA--TAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFV 202
|
250 260 270
....*....|....*....|....*....|....*....
gi 22331045 285 IHQPSSrMFHMFDKLLLISEGHPAFYGKARESMEYFSSL 323
Cdd:COG1134 203 SHSMGA-VRRLCDRAIWLEKGRLVMDGDPEEVIAAYEAL 240
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
100-287 |
1.00e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 74.50 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 100 PDGyKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLtdNVKGKLTYNDIPYS----PSVKRRIGFVTQDDvLLP 175
Cdd:PRK11174 360 PDG-KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL--PYQGSLKINGIELReldpESWRKHLSWVGQNP-QLP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 176 QLTVEETLAFAAflrlpSSMSKEQ-----KYAKIEMIIKEL--GLErcrrTRVGGGfVKGISGGERKRASIAYEILVDPS 248
Cdd:PRK11174 436 HGTLRDNVLLGN-----PDASDEQlqqalENAWVSEFLPLLpqGLD----TPIGDQ-AAGLSVGQAQRLALARALLQPCQ 505
|
170 180 190
....*....|....*....|....*....|....*....
gi 22331045 249 LLLLDEPTSGLDSTSATKLLHILQgVAKAGRTVITTIHQ 287
Cdd:PRK11174 506 LLLLDEPTASLDAHSEQLVMQALN-AASRRQTTLMVTHQ 543
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
50-289 |
1.08e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 74.23 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 50 FVSTYPLEDAPLPIFLKFEDVEYKVRNS-HASSANLVKTMVSkvVTHTNPDPDGYKHILKGITGSTGPGEILALMGPSGS 128
Cdd:PRK13657 295 FINQVFMAAPKLEEFFEVEDAVPDVRDPpGAIDLGRVKGAVE--FDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGA 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 129 GKTTLLKIMGgRLTDNVKGKLTYNDIPYS----PSVKRRIGFVTQDDVLLPQlTVEETL------AFAAFLRLPSSMSKE 198
Cdd:PRK13657 373 GKSTLINLLQ-RVFDPQSGRILIDGTDIRtvtrASLRRNIAVVFQDAGLFNR-SIEDNIrvgrpdATDEEMRAAAERAQA 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 199 QKYakIEMiiKELGLErcrrTRVGGgfvKG--ISGGERKRASIAYEILVDPSLLLLDEPTSGLDSTSATKLLHILQGVAK 276
Cdd:PRK13657 451 HDF--IER--KPDGYD----TVVGE---RGrqLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMK 519
|
250
....*....|...
gi 22331045 277 aGRTVITTIHQPS 289
Cdd:PRK13657 520 -GRTTFIIAHRLS 531
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
115-303 |
1.11e-13 |
|
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: 69.49 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 115 GPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLtynDIPyspsVKRRIGFVTQDDvLLPQLTVEETLAFaaflrlPSS 194
Cdd:cd03223 25 KPGDRLLITGPSGTGKSSLFRALAG-LWPWGSGRI---GMP----EGEDLLFLPQRP-YLPLGTLREQLIY------PWD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 195 mskeqkyakiemiiKELglercrrtrvgggfvkgiSGGERKRASIAYEILVDPSLLLLDEPTSGLDSTSATKLLHILQgv 274
Cdd:cd03223 90 --------------DVL------------------SGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLK-- 135
|
170 180
....*....|....*....|....*....
gi 22331045 275 aKAGRTVITTIHQPSSRMFHmfDKLLLIS 303
Cdd:cd03223 136 -ELGITVISVGHRPSLWKFH--DRVLDLD 161
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
81-272 |
1.59e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 73.61 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 81 SANLVKTM--VSKVVthtnpDPDgyKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDnvkgkltYN-DIPYS 157
Cdd:PRK11819 2 MAQYIYTMnrVSKVV-----PPK--KQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKE-------FEgEARPA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 158 PSVKrrIGFVTQDDVLLPQLTV----EETLA--FAAFLRL----------PSSMSK---EQkyAKIEMIIKELG------ 212
Cdd:PRK11819 68 PGIK--VGYLPQEPQLDPEKTVrenvEEGVAevKAALDRFneiyaayaepDADFDAlaaEQ--GELQEIIDAADawdlds 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22331045 213 -LERCR---RTRVGGGFVKGISGGERKRASIAYEILVDPSLLLLDEPTSGLDSTSATKLLHILQ 272
Cdd:PRK11819 144 qLEIAMdalRCPPWDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLH 207
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
118-305 |
2.74e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 71.42 E-value: 2.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 118 EILALMGPSGSGKTTLLKIMGGRLTDNvKGKLTYNDI--------------PYSPSVK------RRIGFVTQ-DDVLLPQ 176
Cdd:PRK13631 53 KIYFIIGNSGSGKSTLVTHFNGLIKSK-YGTIQVGDIyigdkknnhelitnPYSKKIKnfkelrRRVSMVFQfPEYQLFK 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 177 LTVEETLAFAAF-LRLPSSMSKEQ-KYAKIEMIIKELGLERcrrtrvgGGFvkGISGGERKRASIAYEILVDPSLLLLDE 254
Cdd:PRK13631 132 DTIEKDIMFGPVaLGVKKSEAKKLaKFYLNKMGLDDSYLER-------SPF--GLSGGQKRRVAIAGILAIQPEILIFDE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 22331045 255 PTSGLDSTSATKLLHILQGVAKAGRTVITTIHQpSSRMFHMFDKLLLISEG 305
Cdd:PRK13631 203 PTAGLDPKGEHEMMQLILDAKANNKTVFVITHT-MEHVLEVADEVIVMDKG 252
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
117-308 |
2.90e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 70.92 E-value: 2.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 117 GEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYNDIPYSPS--------VKRRIGFVTQddvlLP--QLTVEETLAFA 186
Cdd:PRK13643 32 GSYTALIGHTGSGKSTLLQHLNG-LLQPTEGKVTVGDIVVSSTskqkeikpVRKKVGVVFQ----FPesQLFEETVLKDV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 187 AFLRLPSSMSKEQ--KYA--KIEMIikELGLERCRRTRVGggfvkgISGGERKRASIAYEILVDPSLLLLDEPTSGLDST 262
Cdd:PRK13643 107 AFGPQNFGIPKEKaeKIAaeKLEMV--GLADEFWEKSPFE------LSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 22331045 263 SATKLLHILQGVAKAGRTVITTIH-----QPSSRMFHMFDKLLLISEGHPA 308
Cdd:PRK13643 179 ARIEMMQLFESIHQSGQTVVLVTHlmddvADYADYVYLLEKGHIISCGTPS 229
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
116-286 |
3.81e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 69.95 E-value: 3.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 116 PGEILALMGPSGSGKTTLLKIMGGRLTDNvKGKLTYN-------DIPYSPSVKRRI------GFVTQD--DVLLPQLT-- 178
Cdd:PRK11701 31 PGEVLGIVGESGSGKTTLLNALSARLAPD-AGEVHYRmrdgqlrDLYALSEAERRRllrtewGFVHQHprDGLRMQVSag 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 179 --VEETLafaaflrlpssMS-KEQKYAKiemiIKELGLERCRRTRVGGGFV----KGISGGERKRASIAYEILVDPSLLL 251
Cdd:PRK11701 110 gnIGERL-----------MAvGARHYGD----IRATAGDWLERVEIDAARIddlpTTFSGGMQQRLQIARNLVTHPRLVF 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 22331045 252 LDEPTSGLDSTSATKLLHILQG-VAKAGRTVITTIH 286
Cdd:PRK11701 175 MDEPTGGLDVSVQARLLDLLRGlVRELGLAVVIVTH 210
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
93-290 |
5.54e-13 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 68.65 E-value: 5.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 93 VTHTNPD-PDgyKHILKGITGSTGPGEILALMGPSGSGKTTLLKIM-------GGRLTdnVKGK-LTYNDIPYspsVKRR 163
Cdd:cd03248 17 VTFAYPTrPD--TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLenfyqpqGGQVL--LDGKpISQYEHKY---LHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 164 IGFVTQDDVLLPQlTVEETLAF----AAFLRLPSSMSKEQKYAKIEmiikelGLERCRRTRVGGgfvKG--ISGGERKRA 237
Cdd:cd03248 90 VSLVGQEPVLFAR-SLQDNIAYglqsCSFECVKEAAQKAHAHSFIS------ELASGYDTEVGE---KGsqLSGGQKQRV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 22331045 238 SIAYEILVDPSLLLLDEPTSGLDSTSATKLLHILQGvAKAGRTVITTIHQPSS 290
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYD-WPERRTVLVIAHRLST 211
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
100-311 |
5.60e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 72.05 E-value: 5.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 100 PDGYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMgGRLTDNVKGKLTYNDIPYSP----SVKRRIGFVTQDDVLLP 175
Cdd:PRK10789 324 PQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLI-QRHFDVSEGDIRFHDIPLTKlqldSWRSRLAVVSQTPFLFS 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 176 QlTVEETLAfaafLRLPSSMSKEQKYAKIEMIIKE--LGLERCRRTRVGGGFVKgISGGERKRASIAYEILVDPSLLLLD 253
Cdd:PRK10789 403 D-TVANNIA----LGRPDATQQEIEHVARLASVHDdiLRLPQGYDTEVGERGVM-LSGGQKQRISIARALLLNAEILILD 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 22331045 254 EPTSGLDSTSATKLLHILQGVAKaGRTVITTIHQPSSrmFHMFDKLLLISEGHPAFYG 311
Cdd:PRK10789 477 DALSAVDGRTEHQILHNLRQWGE-GRTVIISAHRLSA--LTEASEILVMQHGHIAQRG 531
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
65-311 |
5.87e-13 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 68.71 E-value: 5.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 65 LKFEDVEYKVRNSHASSANLVKTMVskvvtHTNPDPDGYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDN 144
Cdd:cd03220 1 IELENVSKSYPTYKGGSSSLKKLGI-----LGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 145 vKGKLTyndipyspsVKRRI--------GFvtqddvlLPQLTVEETLAFAAFLrlpSSMSKEQKYAKIEMIIKELGLERC 216
Cdd:cd03220 76 -SGTVT---------VRGRVssllglggGF-------NPELTGRENIYLNGRL---LGLSRKEIDEKIDEIIEFSELGDF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 217 RRTRvgggfVKGISGGERKRASIAYEILVDPSLLLLDEPTSGLDSTSATKLLHILQGVAKAGRTVITTIHQPSSrMFHMF 296
Cdd:cd03220 136 IDLP-----VKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSS-IKRLC 209
|
250
....*....|....*
gi 22331045 297 DKLLLISEGHPAFYG 311
Cdd:cd03220 210 DRALVLEKGKIRFDG 224
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
106-317 |
6.56e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 69.47 E-value: 6.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 106 ILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDN-------VKGKLTYNDIPYSPSVKRRIGFVTqddVLLPQlT 178
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarVTGDVTLNGEPLAAIDAPRLARLR---AVLPQ-A 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 179 VEETLAFAA-----FLRLPSSMSKEQKYAKIEMIIKElGLERCRRTRVGGGFVKGISGGERKRASIA---------YEIL 244
Cdd:PRK13547 92 AQPAFAFSAreivlLGRYPHARRAGALTHRDGEIAWQ-ALALAGATALVGRDVTTLSGGELARVQFArvlaqlwppHDAA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22331045 245 VDPSLLLLDEPTSGLDSTSATKLLHILQGVAKAGRT-VITTIHQPSSRMFHMfDKLLLISEGHPAFYGKARESM 317
Cdd:PRK13547 171 QPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHDPNLAARHA-DRIAMLADGAIVAHGAPADVL 243
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
102-260 |
1.24e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.22 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 102 GYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTdnvkgkltyndiPYSPSVKR----RIGFVTQD---DVLL 174
Cdd:PRK09544 15 GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVA------------PDEGVIKRngklRIGYVPQKlylDTTL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 175 PqLTVEEtlafaaFLRLPSSMSKEQkyakiemIIKelGLERCRRTRVGGGFVKGISGGERKRASIAYEILVDPSLLLLDE 254
Cdd:PRK09544 83 P-LTVNR------FLRLRPGTKKED-------ILP--ALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDE 146
|
....*.
gi 22331045 255 PTSGLD 260
Cdd:PRK09544 147 PTQGVD 152
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
102-267 |
1.37e-12 |
|
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: 65.55 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 102 GYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTdnvkgkltyndiPYSPSVKR----RIGFvtqddvlLPQL 177
Cdd:cd03221 11 GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELE------------PDEGIVTWgstvKIGY-------FEQL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 178 tveetlafaaflrlpssmskeqkyakiemiikelglercrrtrvgggfvkgiSGGERKRASIAYEILVDPSLLLLDEPTS 257
Cdd:cd03221 72 ----------------------------------------------------SGGEKMRLALAKLLLENPNLLLLDEPTN 99
|
170
....*....|
gi 22331045 258 GLDSTSATKL 267
Cdd:cd03221 100 HLDLESIEAL 109
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
119-284 |
1.57e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 68.58 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 119 ILALMGPSGSGKTTLLKIMGgRLTDNVKGK-------------LTYNDIPyspSVKRRIGFVTQDDVLLPQLTVEETLAF 185
Cdd:PRK14271 49 VTSLMGPTGSGKTTFLRTLN-RMNDKVSGYrysgdvllggrsiFNYRDVL---EFRRRVGMLFQRPNPFPMSIMDNVLAG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 186 aafLRLPSSMSKEQKYAKIEMIIKELGLERCRRTRVGGGFVKgISGGERKRASIAYEILVDPSLLLLDEPTSGLDSTSAT 265
Cdd:PRK14271 125 ---VRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFR-LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTE 200
|
170
....*....|....*....
gi 22331045 266 KLLHILQGVAKAGRTVITT 284
Cdd:PRK14271 201 KIEEFIRSLADRLTVIIVT 219
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
97-305 |
1.99e-12 |
|
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: 66.72 E-value: 1.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 97 NPDPDGYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTdNVKGKLTYNdipyspsvkRRIGFVTQDDVLLPq 176
Cdd:cd03250 11 DSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELE-KLSGSVSVP---------GSIAYVSQEPWIQN- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 177 LTVEETLAFAAFLRlpssmskEQKYAKIemiikelgLERCR------------RTRVGggfVKGI--SGGERKRASIAYE 242
Cdd:cd03250 80 GTIRENILFGKPFD-------EERYEKV--------IKACAlepdleilpdgdLTEIG---EKGInlSGGQKQRISLARA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22331045 243 ILVDPSLLLLDEPTSGLDSTSATKLL-HILQGVAKAGRTVITTIHQPSsrMFHMFDKLLLISEG 305
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHVGRHIFeNCILGLLLNNKTRILVTHQLQ--LLPHADQIVVLDNG 203
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
117-286 |
2.04e-12 |
|
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: 70.22 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 117 GEILALMGPSGSGKTTLLKIMGGrLTDNVKGKL-----------TYNDIPYSPSVKRRIGFVTQDDVLLPQLTVEETLAF 185
Cdd:TIGR03269 310 GEIFGIVGTSGAGKTTLSKIIAG-VLEPTSGEVnvrvgdewvdmTKPGPDGRGRAKRYIGILHQEYDLYPHRTVLDNLTE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 186 AAFLRLPSSMSKEqkyaKIEMIIKELGLERCRRTRVGGGFVKGISGGERKRASIAYEILVDPSLLLLDEPTSGLDSTSAT 265
Cdd:TIGR03269 389 AIGLELPDELARM----KAVITLKMVGFDEEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKV 464
|
170 180
....*....|....*....|..
gi 22331045 266 KLLH-ILQGVAKAGRTVITTIH 286
Cdd:TIGR03269 465 DVTHsILKAREEMEQTFIIVSH 486
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
100-286 |
2.06e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 68.12 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 100 PDGYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYNDIPYSPS----VKRRIGFVTQD-DVLL 174
Cdd:PRK13635 16 PDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNG-LLLPEAGTITVGGMVLSEEtvwdVRRQVGMVFQNpDNQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 175 PQLTVEETLAFAaflrLPSS-MSKEQKYAKIEMIIKELGLERcrrtrvgggFVK----GISGGERKRASIAYEILVDPSL 249
Cdd:PRK13635 95 VGATVQDDVAFG----LENIgVPREEMVERVDQALRQVGMED---------FLNrephRLSGGQKQRVAIAGVLALQPDI 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 22331045 250 LLLDEPTSGLDSTSATKLLHILQGVAKAGR-TVITTIH 286
Cdd:PRK13635 162 IILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITH 199
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
116-260 |
2.06e-12 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 68.60 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 116 PGEILALMGPSGSGKTTLLK-IMggRLTDNVKGKLTYN--DI-PYSPS----VKRRIGFVTQD--DVLLPQLTVEETLAF 185
Cdd:COG4608 43 RGETLGLVGESGCGKSTLGRlLL--RLEEPTSGEILFDgqDItGLSGRelrpLRRRMQMVFQDpyASLNPRMTVGDIIAE 120
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22331045 186 AafLRLPSSMSKEQKYAKIEMIIKELGLERCRRTRVGGGFvkgiSGGERKRASIAYEILVDPSLLLLDEPTSGLD 260
Cdd:COG4608 121 P--LRIHGLASKAERRERVAELLELVGLRPEHADRYPHEF----SGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
107-295 |
2.41e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 67.50 E-value: 2.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 107 LKGITGSTGPGEILALMGPSGSGKTTLLKIMgGRLTD-----NVKGKLTYNDIP-YSP-----SVKRRIGFVTQDDVLLP 175
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCF-NRLNDlipgfRVEGKVTFHGKNlYAPdvdpvEVRRRIGMVFQKPNPFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 176 QlTVEETLAFAAflrlpssmsKEQKYaKIEMiiKELgLERCRRTRVGGGFVK--------GISGGERKRASIAYEILVDP 247
Cdd:PRK14243 105 K-SIYDNIAYGA---------RINGY-KGDM--DEL-VERSLRQAALWDEVKdklkqsglSLSGGQQQRLCIARAIAVQP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 22331045 248 SLLLLDEPTSGLDSTSATK---LLHILqgvaKAGRTVITTIH--QPSSRMFHM 295
Cdd:PRK14243 171 EVILMDEPCSALDPISTLRieeLMHEL----KEQYTIIIVTHnmQQAARVSDM 219
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
107-290 |
2.92e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.60 E-value: 2.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 107 LKGITGSTGPGEILALMGPSGSGKTTLLKIMGG--RLTdnvKGKLTYNDIPYSPSVKRR-IGFVTQDD-------VLLPQ 176
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGfvRLA---SGKISILGQPTRQALQKNlVAYVPQSEevdwsfpVLVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 177 LTVEETLAFAAFLRLPssmsKEQKYAKIEMIIKELGLERCRRTRVGGgfvkgISGGERKRASIAYEILVDPSLLLLDEPT 256
Cdd:PRK15056 100 VVMMGRYGHMGWLRRA----KKRDRQIVTAALARVDMVEFRHRQIGE-----LSGGQKKRVFLARAIAQQGQVILLDEPF 170
|
170 180 190
....*....|....*....|....*....|....
gi 22331045 257 SGLDSTSATKLLHILQGVAKAGRTVITTIHQPSS 290
Cdd:PRK15056 171 TGVDVKTEARIISLLRELRDEGKTMLVSTHNLGS 204
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
107-375 |
3.32e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 67.77 E-value: 3.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 107 LKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDNvKGKLTYNDIPYS------PSVKRRIGFVTQddvlLP--QL- 177
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPT-SGKIIIDGVDITdkkvklSDIRKKVGLVFQ----YPeyQLf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 178 --TVEETLAFAaflrlPSSM--SKEQKYAKIEMIIKELGLERcRRTRVGGGFvkGISGGERKRASIAYEILVDPSLLLLD 253
Cdd:PRK13637 98 eeTIEKDIAFG-----PINLglSEEEIENRVKRAMNIVGLDY-EDYKDKSPF--ELSGGQKRRVAIAGVVAMEPKILILD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 254 EPTSGLDSTSATKLLHILQGVAKAGRTVITTIHQPSSRMFHMFDKLLLISEGHPAFYGKAResmEYFSSLRILPEIAmnp 333
Cdd:PRK13637 170 EPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPR---EVFKEVETLESIG--- 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 22331045 334 aeflldLATGQVS---------DISLPDELLAAKTAQpdseEVLLKYLKQR 375
Cdd:PRK13637 244 ------LAVPQVTylvrklrkkGFNIPDDIFTIEEAK----EEILKYLRGE 284
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
99-262 |
3.69e-12 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 69.33 E-value: 3.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 99 DPDGYKHILKGITGSTGPGEILALMGPSGSGKT-TLLKIMGgRLTDN---VKGKLTYND---IPYSPSVKR-----RIGF 166
Cdd:COG4172 18 QGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILR-LLPDPaahPSGSILFDGqdlLGLSERELRrirgnRIAM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 167 VTQDDV--LLPQLTVEETLAFAafLRLPSSMSKEQkyAKIEMIikELgLERCR----RTRVGGgFVKGISGGERKRASIA 240
Cdd:COG4172 97 IFQEPMtsLNPLHTIGKQIAEV--LRLHRGLSGAA--ARARAL--EL-LERVGipdpERRLDA-YPHQLSGGQRQRVMIA 168
|
170 180
....*....|....*....|..
gi 22331045 241 YEILVDPSLLLLDEPTSGLDST 262
Cdd:COG4172 169 MALANEPDLLIADEPTTALDVT 190
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
117-325 |
4.24e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 69.07 E-value: 4.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 117 GEILALMGPSGSGKTTLLKIMGGRLTDNvKGKLTYN-DIPYSPSvkrrigFVTQDdvllPQLTVEETLAFAAfLRLPSSM 195
Cdd:PRK13409 365 GEVIGIVGPNGIGKTTFAKLLAGVLKPD-EGEVDPElKISYKPQ------YIKPD----YDGTVEDLLRSIT-DDLGSSY 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 196 SKEQkyakiemIIKELGLERCRRTRVgggfvKGISGGERKRASIAYEILVDPSLLLLDEPTSGLDS---TSATKLlhILQ 272
Cdd:PRK13409 433 YKSE-------IIKPLQLERLLDKNV-----KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrLAVAKA--IRR 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22331045 273 GVAKAGRTVITTIHQpssrmFHMFDKL---LLISEGHPAFYGKA------RESM-EYFSSLRI 325
Cdd:PRK13409 499 IAEEREATALVVDHD-----IYMIDYIsdrLMVFEGEPGKHGHAsgpmdmREGMnRFLKELGI 556
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
100-308 |
4.49e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 69.07 E-value: 4.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 100 PDGyKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYNDipyspsvKRRIGFVTQDdVLLPQLTV 179
Cdd:COG4178 373 PDG-RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-LWPYGSGRIARPA-------GARVLFLPQR-PYLPLGTL 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 180 EETLAFAAflrLPSSMSKEQkyakIEMIIKELGLER-CRRTRVGGGFVKGISGGERKRASIAYEILVDPSLLLLDEPTSG 258
Cdd:COG4178 443 REALLYPA---TAEAFSDAE----LREALEAVGLGHlAERLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSA 515
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 22331045 259 LDSTSATKLLHILQGvAKAGRTVITTIHQPSSRMFHmfDKLLLISEGHPA 308
Cdd:COG4178 516 LDEENEAALYQLLRE-ELPGTTVISVGHRSTLAAFH--DRVLELTGDGSW 562
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
106-318 |
6.50e-12 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 68.98 E-value: 6.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 106 ILKGITGSTGPGEILALMGPSGSGKTTLLKIMgGRLTDNVKGKLTYNDIPYSP----SVKRRIGFVTQDDVLLPQlTVEE 181
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALL-QNLYQPTGGQVLLDGVPLVQydhhYLHRQVALVGQEPVLFSG-SVRE 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 182 TLAFAAFLRLPSSMSKEQKYAKIEMIIKElgLERCRRTRVG--GGFvkgISGGERKRASIAYEILVDPSLLLLDEPTSGL 259
Cdd:TIGR00958 574 NIAYGLTDTPDEEIMAAAKAANAHDFIME--FPNGYDTEVGekGSQ---LSGGQKQRIAIARALVRKPRVLILDEATSAL 648
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 22331045 260 DSTSATKLlhiLQGVAKAGRTVITTIHQPSSrmFHMFDKLLLISEGHPAFYGKARESME 318
Cdd:TIGR00958 649 DAECEQLL---QESRSRASRTVLLIAHRLST--VERADQILVLKKGSVVEMGTHKQLME 702
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
106-315 |
9.10e-12 |
|
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: 68.78 E-value: 9.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 106 ILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDNvKGKLTYNDipyspsvkrRIGFVTQDDVLLPQlTVEETLAF 185
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPS-EGKIKHSG---------RISFSPQTSWIMPG-TIKDNIIF 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 186 AAflrlpssMSKEQKYAKiemIIKELGLER-------CRRTRVGGGFVKgISGGERKRASIAYEILVDPSLLLLDEPTSG 258
Cdd:TIGR01271 510 GL-------SYDEYRYTS---VIKACQLEEdialfpeKDKTVLGEGGIT-LSGGQRARISLARAVYKDADLYLLDSPFTH 578
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22331045 259 LDSTSATKLLH--ILQGVAKAGRTVITtihqpsSRMFHM--FDKLLLISEGHPAFYGKARE 315
Cdd:TIGR01271 579 LDVVTEKEIFEscLCKLMSNKTRILVT------SKLEHLkkADKILLLHEGVCYFYGTFSE 633
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
101-260 |
9.65e-12 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 67.18 E-value: 9.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 101 DGYKHILKGITGSTGPGEILALMGPSGSGKTTLLKI-------------MGGRLTDNVKGKltyndipyspsvKRRIGFV 167
Cdd:PRK11650 14 DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMvagleritsgeiwIGGRVVNELEPA------------DRDIAMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 168 TQDDVLLPQLTVEETLAFAAFLRlpsSMSKEQKYAKIEMIIKELGLERC--RRTRvgggfvkGISGGERKRASIAYEILV 245
Cdd:PRK11650 82 FQNYALYPHMSVRENMAYGLKIR---GMPKAEIEERVAEAARILELEPLldRKPR-------ELSGGQRQRVAMGRAIVR 151
|
170
....*....|....*
gi 22331045 246 DPSLLLLDEPTSGLD 260
Cdd:PRK11650 152 EPAVFLFDEPLSNLD 166
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
106-305 |
1.10e-11 |
|
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: 64.82 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 106 ILKGITGSTGPGEILALMGPSGSGKTTL-LKIMggRLTDNVKGKLTYNDIPYSP----SVKRRIGFVTQDDVLlpqltve 180
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLlLALF--RLVELSSGSILIDGVDISKiglhDLRSRISIIPQDPVL------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 181 etlaFAAFLRlpSSMSKEQKY--AKIEMIIKELGL-ERCRRTRVGGGFV-----KGISGGERKRASIAYEILVDPSLLLL 252
Cdd:cd03244 90 ----FSGTIR--SNLDPFGEYsdEELWQALERVGLkEFVESLPGGLDTVveeggENLSVGQRQLLCLARALLRKSKILVL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 22331045 253 DEPTSGLDSTSATKLLHILQGvAKAGRTVITTIHqpssRMFHM--FDKLLLISEG 305
Cdd:cd03244 164 DEATASVDPETDALIQKTIRE-AFKDCTVLTIAH----RLDTIidSDRILVLDKG 213
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
106-315 |
1.58e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 65.41 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 106 ILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDNvKGKLTYNDIP--YSP----SVKRRIGFVTQD-DVLLPQLT 178
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQ-KGAVLWQGKPldYSKrgllALRQQVATVFQDpEQQIFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 179 VEETLAFAafLRlPSSMSKEQKYAKIEMIIKELGLERCRRTRVgggfvKGISGGERKRASIAYEILVDPSLLLLDEPTSG 258
Cdd:PRK13638 95 IDSDIAFS--LR-NLGVPEAEITRRVDEALTLVDAQHFRHQPI-----QCLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 22331045 259 LDSTSATKLLHILQGVAKAGRTVITTIHQpSSRMFHMFDKLLLISEGHPAFYGKARE 315
Cdd:PRK13638 167 LDPAGRTQMIAIIRRIVAQGNHVIISSHD-IDLIYEISDAVYVLRQGQILTHGAPGE 222
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
100-315 |
2.03e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 65.90 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 100 PDGYKHILKGITGSTGPGEILALMGPSGSGKT-TLLKIMGgRLTDN--VKGKLTYN-----DIPYSPSVKRR---IGFVT 168
Cdd:PRK09473 25 PDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMG-LLAANgrIGGSATFNgreilNLPEKELNKLRaeqISMIF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 169 QDDV--LLPQLTVEETLAfaAFLRLPSSMSKEQKYAK-IEMIIKELGLERCRRTRVgggFVKGISGGERKRASIAYEILV 245
Cdd:PRK09473 104 QDPMtsLNPYMRVGEQLM--EVLMLHKGMSKAEAFEEsVRMLDAVKMPEARKRMKM---YPHEFSGGMRQRVMIAMALLC 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 246 DPSLLLLDEPTSGLDSTSATKLLHILQGVAKAGRTVITTIHQPSSRMFHMFDKLLLISEGHPAFYGKARE 315
Cdd:PRK09473 179 RPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARD 248
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
104-286 |
2.25e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 64.67 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 104 KHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGgRLTD-----NVKGKLTY-NDIPYSPSV-----KRRIGFVTQDDV 172
Cdd:PRK14258 20 QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLN-RMNElesevRVEGRVEFfNQNIYERRVnlnrlRRQVSMVHPKPN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 173 LLPqLTVEETLAFAafLRLPSSMSKEQKYAKIEMIIKELGLERCRRTRVGGGFVKgISGGERKRASIAYEILVDPSLLLL 252
Cdd:PRK14258 99 LFP-MSVYDNVAYG--VKIVGWRPKLEIDDIVESALKDADLWDEIKHKIHKSALD-LSGGQQQRLCIARALAVKPKVLLM 174
|
170 180 190
....*....|....*....|....*....|....*
gi 22331045 253 DEPTSGLDSTSATKLLHILQGVA-KAGRTVITTIH 286
Cdd:PRK14258 175 DEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSH 209
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
116-282 |
2.79e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 66.20 E-value: 2.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 116 PGEILALMGPSGSGKTTLLK-IMGgrLTDNVKGKLTYNDIPYSPS-----VKRRIGFVTQD---DVLLPQLTVEETLAFA 186
Cdd:COG1129 277 AGEILGIAGLVGAGRTELARaLFG--ADPADSGEIRLDGKPVRIRsprdaIRAGIAYVPEDrkgEGLVLDLSIRENITLA 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 187 AFLRLPS----SMSKEQKYAkiEMIIKELGLeRCRRTRVGggfVKGISGGERKRASIAYEILVDPSLLLLDEPTSGLDST 262
Cdd:COG1129 355 SLDRLSRggllDRRRERALA--EEYIKRLRI-KTPSPEQP---VGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVG 428
|
170 180
....*....|....*....|
gi 22331045 263 SATKLLHILQGVAKAGRTVI 282
Cdd:COG1129 429 AKAEIYRLIRELAAEGKAVI 448
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
117-286 |
3.71e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 64.47 E-value: 3.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 117 GEILALMGPSGSGKTTLLKIMGGRLTDNvKGKLTYNDIPYSPS--------VKRRIGFVTQ-DDVLLPQLTVEETLAFAa 187
Cdd:PRK13641 33 GSFVALVGHTGSGKSTLMQHFNALLKPS-SGTITIAGYHITPEtgnknlkkLRKKVSLVFQfPEAQLFENTVLKDVEFG- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 188 flrlPSSMSKEQKYAKIEMI--IKELGLErcrrTRVGGGFVKGISGGERKRASIAYEILVDPSLLLLDEPTSGLDSTSAT 265
Cdd:PRK13641 111 ----PKNFGFSEDEAKEKALkwLKKVGLS----EDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRK 182
|
170 180
....*....|....*....|.
gi 22331045 266 KLLHILQGVAKAGRTVITTIH 286
Cdd:PRK13641 183 EMMQLFKDYQKAGHTVILVTH 203
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
106-311 |
3.92e-11 |
|
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: 62.81 E-value: 3.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 106 ILKGITGSTGPGEILALMGPSGSGKTTLLKIMGgRLTDNVKGKLTYNDIPYSP----SVKRRIGFVTQDDVLlpqltvee 181
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALF-RFLEAEEGKIEIDGIDISTipleDLRSSLTIIPQDPTL-------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 182 tlaFAAFLRlpSSMSKEQKYAKIEMI----IKELGLErcrrtrvgggfvkgISGGERKRASIAYEILVDPSLLLLDEPTS 257
Cdd:cd03369 94 ---FSGTIR--SNLDPFDEYSDEEIYgalrVSEGGLN--------------LSQGQRQLLCLARALLKRPRVLVLDEATA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 22331045 258 GLDSTSAtkllHILQGVAK---AGRTVITTIHQPSSRMfhMFDKLLLISEGHPAFYG 311
Cdd:cd03369 155 SIDYATD----ALIQKTIReefTNSTILTIAHRLRTII--DYDKILVMDAGEVKEYD 205
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
107-296 |
4.09e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 65.70 E-value: 4.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 107 LKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDNVkGKLTYNDIPYS-PSVKRR----IGFVTQDDVLLPQLTVEE 181
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDA-GSILIDGQEMRfASTTAAlaagVAIIYQELHLVPEMTVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 182 TLafaaFL-RLPSSM---SKEQKYAKIEMIIKELGLERCRRTRvgggfVKGISGGERKRASIAYEILVDPSLLLLDEPTS 257
Cdd:PRK11288 99 NL----YLgQLPHKGgivNRRLLNYEAREQLEHLGVDIDPDTP-----LKYLSIGQRQMVEIAKALARNARVIAFDEPTS 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 22331045 258 GLDSTSATKLLHILQGVAKAGRTVITTIHqpssRMFHMF 296
Cdd:PRK11288 170 SLSAREIEQLFRVIRELRAEGRVILYVSH----RMEEIF 204
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
104-320 |
5.25e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 65.59 E-value: 5.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 104 KHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGG-RLTDNVKGKLTYN------------------------------ 152
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmDQYEPTSGRIIYHvalcekcgyverpskvgepcpvcggtlepe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 153 -------DIPYSPSVKRRIGFVTQ--------DDVLLPQLTVEETLAFAAflrlpssmsKEQKYAKIEMIiKELGLERcR 217
Cdd:TIGR03269 93 evdfwnlSDKLRRRIRKRIAIMLQrtfalygdDTVLDNVLEALEEIGYEG---------KEAVGRAVDLI-EMVQLSH-R 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 218 RTRVGggfvKGISGGERKRASIAYEILVDPSLLLLDEPTSGLDSTSAtKLLH--ILQGVAKAGRTVITTIHQPSSrMFHM 295
Cdd:TIGR03269 162 ITHIA----RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTA-KLVHnaLEEAVKASGISMVLTSHWPEV-IEDL 235
|
250 260
....*....|....*....|....*
gi 22331045 296 FDKLLLISEGHPAFYGKARESMEYF 320
Cdd:TIGR03269 236 SDKAIWLENGEIKEEGTPDEVVAVF 260
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
104-288 |
5.40e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.05 E-value: 5.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 104 KHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDN-VKGKltyndipyspsvkrrigFVTQDDVLLPQLTVEET 182
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTpVAGC-----------------VDVPDNQFGREASLIDA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 183 LAfaaflrlpssmSKEQKYAKIEMiikelgLERC--------RRTrvgggfVKGISGGERKRASIAYEILVDPSLLLLDE 254
Cdd:COG2401 106 IG-----------RKGDFKDAVEL------LNAVglsdavlwLRR------FKELSTGQKFRFRLALLLAERPKLLVIDE 162
|
170 180 190
....*....|....*....|....*....|....*
gi 22331045 255 PTSGLDSTSATKLLHILQGVA-KAGRTVITTIHQP 288
Cdd:COG2401 163 FCSHLDRQTAKRVARNLQKLArRAGITLVVATHHY 197
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
107-260 |
5.81e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 63.89 E-value: 5.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 107 LKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYNDIPYSPSVK--------RRIGFVTQddvlLP--Q 176
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNG-LLQPTSGTVTIGERVITAGKKnkklkplrKKVGIVFQ----FPehQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 177 L---TVEETLAFAaflrlPSS--MSKEQKYAKIEMIIKELGLERCRRTRvgGGFvkGISGGERKRASIAYEILVDPSLLL 251
Cdd:PRK13634 98 LfeeTVEKDICFG-----PMNfgVSEEDAKQKAREMIELVGLPEELLAR--SPF--ELSGGQMRRVAIAGVLAMEPEVLV 168
|
....*....
gi 22331045 252 LDEPTSGLD 260
Cdd:PRK13634 169 LDEPTAGLD 177
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
106-261 |
7.36e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 64.36 E-value: 7.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 106 ILKGITGSTGP-------------GEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYN--DIPYSPSVKRRIGFVTQD 170
Cdd:PRK11432 8 VLKNITKRFGSntvidnlnltikqGTMVTLLGPSGCGKTTVLRLVAG-LEKPTEGQIFIDgeDVTHRSIQQRDICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 171 DVLLPQLTVEETLAFA-AFLRLPSSMSKEQKYAKIEMIIKELGLERcrrtrvgggFVKGISGGERKRASIAYEILVDPSL 249
Cdd:PRK11432 87 YALFPHMSLGENVGYGlKMLGVPKEERKQRVKEALELVDLAGFEDR---------YVDQISGGQQQRVALARALILKPKV 157
|
170
....*....|..
gi 22331045 250 LLLDEPTSGLDS 261
Cdd:PRK11432 158 LLFDEPLSNLDA 169
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
106-305 |
3.11e-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: 63.22 E-value: 3.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 106 ILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYNDIPYSP----SVKRRIGFVTQDDVLLPQlTVEE 181
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVG-FFQARSGEILLNGFSLKDidrhTLRQFINYLPQEPYIFSG-SILE 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 182 TLAFAAFLRLPSSMSKEQ-KYAKIEMIIKELGLERCRRTRVGGGfvkGISGGERKRASIAYEILVDPSLLLLDEPTSGLD 260
Cdd:TIGR01193 567 NLLLGAKENVSQDEIWAAcEIAEIKDDIENMPLGYQTELSEEGS---SISGGQKQRIALARALLTDSKVLILDESTSNLD 643
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 22331045 261 STSATKLLHILQGVAKagRTVITTIHQPSsrMFHMFDKLLLISEG 305
Cdd:TIGR01193 644 TITEKKIVNNLLNLQD--KTIIFVAHRLS--VAKQSDKIIVLDHG 684
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
117-286 |
3.90e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 61.30 E-value: 3.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 117 GEILALMGPSGSGKTTLLKIMGGRLTDNvKGKLTYNDIPYSP--------SVKRRIGFVTQddvlLP--QLTVEETLAFA 186
Cdd:PRK13649 33 GSYTAFIGHTGSGKSTIMQLLNGLHVPT-QGSVRVDDTLITStsknkdikQIRKKVGLVFQ----FPesQLFEETVLKDV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 187 AFLRLPSSMSKEQKYAKIEMIIKELGLERCRRTRvgGGFvkGISGGERKRASIAYEILVDPSLLLLDEPTSGLDSTSATK 266
Cdd:PRK13649 108 AFGPQNFGVSQEEAEALAREKLALVGISESLFEK--NPF--ELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKE 183
|
170 180
....*....|....*....|
gi 22331045 267 LLHILQGVAKAGRTVITTIH 286
Cdd:PRK13649 184 LMTLFKKLHQSGMTIVLVTH 203
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
71-315 |
5.03e-10 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 61.03 E-value: 5.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 71 EYKVRNSHASSANLvktMVSKVVTHTNPdpdgykhILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDNvKGKLT 150
Cdd:cd03291 27 ENNDRKHSSDDNNL---FFSNLCLVGAP-------VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPS-EGKIK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 151 YNDipyspsvkrRIGFVTQDDVLLPQlTVEETLAFAAflrlpssMSKEQKYAKiemIIKELGLER-------CRRTRVGG 223
Cdd:cd03291 96 HSG---------RISFSSQFSWIMPG-TIKENIIFGV-------SYDEYRYKS---VVKACQLEEditkfpeKDNTVLGE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 224 GFVKgISGGERKRASIAYEILVDPSLLLLDEPTSGLDSTSATKLLH--ILQGVAKAGRTVITtihqpsSRMFHM--FDKL 299
Cdd:cd03291 156 GGIT-LSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFEscVCKLMANKTRILVT------SKMEHLkkADKI 228
|
250
....*....|....*.
gi 22331045 300 LLISEGHPAFYGKARE 315
Cdd:cd03291 229 LILHEGSSYFYGTFSE 244
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
102-276 |
5.50e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 60.11 E-value: 5.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 102 GYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYNDIP---YSPSVKRR-IGFVTQDDVLLPQl 177
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVAS-LISPTSGTLLFEGEDistLKPEIYRQqVSYCAQTPTLFGD- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 178 TVEETLAFAAFLRlpSSMSKEQKYAKiEMIIKELGLERCRRTrvgggfVKGISGGERKRASIAYEILVDPSLLLLDEPTS 257
Cdd:PRK10247 96 TVYDNLIFPWQIR--NQQPDPAIFLD-DLERFALPDTILTKN------IAELSGGEKQRISLIRNLQFMPKVLLLDEITS 166
|
170
....*....|....*....
gi 22331045 258 GLDSTSATKLLHILQGVAK 276
Cdd:PRK10247 167 ALDESNKHNVNEIIHRYVR 185
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
100-342 |
5.70e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 60.77 E-value: 5.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 100 PDGYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDNvKGKLTYNDIPYS----PSVKRRIGFVTQD-DVLL 174
Cdd:PRK13632 18 PNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQ-SGEIKIDGITISkenlKEIRKKIGIIFQNpDNQF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 175 PQLTVEETLAFaaflrlpSSMSKEQKYAKIEMIIKELGlercrrTRVG-GGFVK----GISGGERKRASIAYEILVDPSL 249
Cdd:PRK13632 97 IGATVEDDIAF-------GLENKKVPPKKMKDIIDDLA------KKVGmEDYLDkepqNLSGGQKQRVAIASVLALNPEI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 250 LLLDEPTSGLDSTSATKLLHILQGVAKAG-RTVITTIHQpssrMFHMF--DKLLLISEGHPAFYGKAResmEYFSSLRIL 326
Cdd:PRK13632 164 IIFDESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHD----MDEAIlaDKVIVFSEGKLIAQGKPK---EILNNKEIL 236
|
250
....*....|....*.
gi 22331045 327 pEIAMNPAEFLLDLAT 342
Cdd:PRK13632 237 -EKAKIDSPFIYKLSK 251
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
116-286 |
6.31e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 59.48 E-value: 6.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 116 PGEILALMGPSGSGKTTLLKIMGGRLTDNvKGKLTYNDIPYSPSVKRR-IGFVTQDDVLLPQLTVEETLAFAAFL----- 189
Cdd:PRK13543 36 AGEALLVQGDNGAGKTTLLRVLAGLLHVE-SGQIQIDGKTATRGDRSRfMAYLGHLPGLKADLSTLENLHFLCGLhgrra 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 190 -RLPSSMskeqkyakiemiIKELGLERCRRTrvgggFVKGISGGERKRASIAYEILVDPSLLLLDEPTSGLDSTSATKLL 268
Cdd:PRK13543 115 kQMPGSA------------LAIVGLAGYEDT-----LVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVN 177
|
170
....*....|....*...
gi 22331045 269 HILQGVAKAGRTVITTIH 286
Cdd:PRK13543 178 RMISAHLRGGGAALVTTH 195
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
107-306 |
6.47e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 62.34 E-value: 6.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 107 LKGITGSTGPGEILALMGPSGSGKTTLLKIMGgRLTDNVKGKLTYN--DI-PYS-PSVKRRIGFVTQDdVLLPQLTVEET 182
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLT-RFYDIDEGEILLDghDLrDYTlASLRNQVALVSQN-VHLFNDTIANN 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 183 LAFAAflrlPSSMSKEQ--KYAK----IEMIIK-ELGLErcrrTRVGGGFVKgISGGERKRASIAYEILVDPSLLLLDEP 255
Cdd:PRK11176 437 IAYAR----TEQYSREQieEAARmayaMDFINKmDNGLD----TVIGENGVL-LSGGQRQRIAIARALLRDSPILILDEA 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 22331045 256 TSGLDSTSATKLLHILQGVAKaGRTVITTIHQPSSrmFHMFDKLLLISEGH 306
Cdd:PRK11176 508 TSALDTESERAIQAALDELQK-NRTSLVIAHRLST--IEKADEILVVEDGE 555
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
108-282 |
6.77e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 62.11 E-value: 6.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 108 KGITGSTGPGEILALMGPSGSGKTTLLKIMGGrlTDNVK-GKLTYNDI---PYSP--SVKRRIGFVTQ---DDVLLPQLT 178
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFG--VDKRAgGEIRLNGKdisPRSPldAVKKGMAYITEsrrDNGFFPNFS 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 179 VEETLAFAAFLRLPS--------SMSKEQKYAKIEmiiKELGLERCRRTRVGggfVKGISGGERKRASIAYEILVDPSLL 250
Cdd:PRK09700 358 IAQNMAISRSLKDGGykgamglfHEVDEQRTAENQ---RELLALKCHSVNQN---ITELSGGNQQKVLISKWLCCCPEVI 431
|
170 180 190
....*....|....*....|....*....|..
gi 22331045 251 LLDEPTSGLDSTSATKLLHILQGVAKAGRTVI 282
Cdd:PRK09700 432 IFDEPTRGIDVGAKAEIYKVMRQLADDGKVIL 463
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
107-286 |
6.91e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.87 E-value: 6.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 107 LKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrltdnV------KGKLTYNDIPYSPSVKRR-----IGFVTQDDVLLP 175
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-----VyphgtyEGEIIFEGEELQASNIRDteragIAIIHQELALVK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 176 QLTVEETLAFAAFLRLPSSMSKEQKYAKIEMIIKELGLERCRRTRVGGgfvkgISGGERKRASIAYEILVDPSLLLLDEP 255
Cdd:PRK13549 96 ELSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGN-----LGLGQQQLVEIAKALNKQARLLILDEP 170
|
170 180 190
....*....|....*....|....*....|.
gi 22331045 256 TSGLDSTSATKLLHILQGVAKAGRTVITTIH 286
Cdd:PRK13549 171 TASLTESETAVLLDIIRDLKAHGIACIYISH 201
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
107-356 |
8.22e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 60.49 E-value: 8.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 107 LKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKG-------KLTYNDIPyspSVKRRIGFVTQD-DVLLPQLT 178
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDG-LFEEFEGkvkidgeLLTAENVW---NLRRKIGMVFQNpDNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 179 VEETLAFAAflrLPSSMSKEQKYAKIE---MIIKELGLERCRRTRvgggfvkgISGGERKRASIAYEILVDPSLLLLDEP 255
Cdd:PRK13642 99 VEDDVAFGM---ENQGIPREEMIKRVDealLAVNMLDFKTREPAR--------LSGGQKQRVAVAGIIALRPEIIILDES 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 256 TSGLDSTSATKLLHILQGVA-KAGRTVITTIHQPSSRMFHmfDKLLLISEGHPAfygKARESMEYFSSLRILPEIAMN-- 332
Cdd:PRK13642 168 TSMLDPTGRQEIMRVIHEIKeKYQLTVLSITHDLDEAASS--DRILVMKAGEII---KEAAPSELFATSEDMVEIGLDvp 242
|
250 260
....*....|....*....|....*
gi 22331045 333 -PAEFLLDLATgqvSDISLPDELLA 356
Cdd:PRK13642 243 fSSNLMKDLRK---NGFDLPEKYLS 264
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
107-287 |
9.23e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 61.38 E-value: 9.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 107 LKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLT-DNVKGKLTYNDIPYSPSVKRR-----IGFVTQDDVLLPQLTVE 180
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhGTWDGEIYWSGSPLKASNIRDteragIVIIHQELTLVPELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 181 ETLAFAAFLRLPSS-MSKEQKYAKIEMIIKELGLERCRRTRVgggfVKGISGGERKRASIAYEILVDPSLLLLDEPTSGL 259
Cdd:TIGR02633 97 ENIFLGNEITLPGGrMAYNAMYLRAKNLLRELQLDADNVTRP----VGDYGGGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
170 180
....*....|....*....|....*...
gi 22331045 260 DSTSATKLLHILQGVAKAGRTVITTIHQ 287
Cdd:TIGR02633 173 TEKETEILLDIIRDLKAHGVACVYISHK 200
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
100-260 |
1.21e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 60.36 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 100 PDGYKHILKGITGSTGPGEILALMGPSGSGKTTLlkimgGRLTDNVK----GKLTYNDIP---YSPSV----KRRIGFVT 168
Cdd:PRK11308 24 PERLVKALDGVSFTLERGKTLAVVGESGCGKSTL-----ARLLTMIEtptgGELYYQGQDllkADPEAqkllRQKIQIVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 169 QDDV--LLPQLTVEETLAfaAFLRLPSSMSKEQKYAKIEMIIKELGLercrRTRVGGGFVKGISGGERKRASIAYEILVD 246
Cdd:PRK11308 99 QNPYgsLNPRKKVGQILE--EPLLINTSLSAAERREKALAMMAKVGL----RPEHYDRYPHMFSGGQRQRIAIARALMLD 172
|
170
....*....|....
gi 22331045 247 PSLLLLDEPTSGLD 260
Cdd:PRK11308 173 PDVVVADEPVSALD 186
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
107-297 |
2.14e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.40 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 107 LKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDNVkGKLTYNDIP---YSP--SVKRRIGFVTQDDVLLPQLTVEE 181
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDA-GSILYLGKEvtfNGPksSQEAGIGIIHQELNLIPQLTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 182 TLafaaFL-RLPSS----MSKEQKYAKIEMIIKELGLERCRRTRVGggfvkGISGGERKRASIAYEILVDPSLLLLDEPT 256
Cdd:PRK10762 99 NI----FLgREFVNrfgrIDWKKMYAEADKLLARLNLRFSSDKLVG-----ELSIGEQQMVEIAKVLSFESKVIIMDEPT 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 22331045 257 SGLDSTSATKLLHILQGVAKAGRTVITTIHqpssRMFHMFD 297
Cdd:PRK10762 170 DALTDTETESLFRVIRELKSQGRGIVYISH----RLKEIFE 206
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
106-271 |
2.17e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 60.49 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 106 ILKGITGSTGPGEILALMGPSGSGKT-TLLKIMggRLTDNVKGKLTYNDIPYS---------PSVKR----RIGFVTQDD 171
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvTALSIL--RLLPSPPVVYPSGDIRFHgesllhaseQTLRGvrgnKIAMIFQEP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 172 V--LLPQLTVEETLAfaAFLRLPSSMSKEQkyAKIEMIikelgleRCRRtRVG--------GGFVKGISGGERKRASIAY 241
Cdd:PRK15134 102 MvsLNPLHTLEKQLY--EVLSLHRGMRREA--ARGEIL-------NCLD-RVGirqaakrlTDYPHQLSGGERQRVMIAM 169
|
170 180 190
....*....|....*....|....*....|
gi 22331045 242 EILVDPSLLLLDEPTSGLDSTSATKLLHIL 271
Cdd:PRK15134 170 ALLTRPELLIADEPTTALDVSVQAQILQLL 199
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
104-260 |
2.52e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 58.26 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 104 KHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDNVKGKltyndipyspsvkrRIGFVTQDdvlLPQLTVEET- 182
Cdd:PRK09580 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGG--------------TVEFKGKD---LLELSPEDRa 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 183 -----LAFAAFLRLP---------SSMSKEQKYAK------------IEMIIKELGLERCRRTR-VGGGFvkgiSGGERK 235
Cdd:PRK09580 77 gegifMAFQYPVEIPgvsnqfflqTALNAVRSYRGqepldrfdfqdlMEEKIALLKMPEDLLTRsVNVGF----SGGEKK 152
|
170 180
....*....|....*....|....*
gi 22331045 236 RASIAYEILVDPSLLLLDEPTSGLD 260
Cdd:PRK09580 153 RNDILQMAVLEPELCILDESDSGLD 177
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
167-290 |
3.73e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 60.43 E-value: 3.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 167 VTQDDVLLpQLTVEETLAFAAFLRLPSSMSKEQKYAKIEMIIKELGLERcrRTRVGGgFVKGISGGERKRASIAYEILVD 246
Cdd:PTZ00265 1301 VSQEPMLF-NMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKY--DTNVGP-YGKSLSGGQKQRIAIARALLRE 1376
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 22331045 247 PSLLLLDEPTSGLDSTSaTKLLH--ILQGVAKAGRTVITTIHQPSS 290
Cdd:PTZ00265 1377 PKILLLDEATSSLDSNS-EKLIEktIVDIKDKADKTIITIAHRIAS 1421
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
117-305 |
5.63e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 59.07 E-value: 5.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 117 GEILALMGPSGSGKTTLLKIMGGRLTDNVKGKLTYNDIPYS-----PSVKRRIGFVTQD---DVLLPQLTVEETLAFAAF 188
Cdd:TIGR02633 286 GEILGVAGLVGAGRTELVQALFGAYPGKFEGNVFINGKPVDirnpaQAIRAGIAMVPEDrkrHGIVPILGVGKNITLSVL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 189 lrlpssmskeQKYAKIEMI--IKELG--LERCRRTRVGGGF----VKGISGGERKRASIAYEILVDPSLLLLDEPTSGLD 260
Cdd:TIGR02633 366 ----------KSFCFKMRIdaAAELQiiGSAIQRLKVKTASpflpIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 22331045 261 STSATKLLHILQGVAKAGRTVItTIHQPSSRMFHMFDKLLLISEG 305
Cdd:TIGR02633 436 VGAKYEIYKLINQLAQEGVAII-VVSSELAEVLGLSDRVLVIGEG 479
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
61-410 |
6.52e-09 |
|
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: 59.57 E-value: 6.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 61 LPIFLKFEDVEYKV--RNSHASSANLVKTMVSKVVTHTNPDPDgykhILKGITGSTGPGEILALMGPSGSGKTTLLKIMG 138
Cdd:TIGR00957 610 LRIFLSHEELEPDSieRRTIKPGEGNSITVHNATFTWARDLPP----TLNGITFSIPEGALVAVVGQVGCGKSSLLSALL 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 139 GRLtDNVKGKLTyndipyspsVKRRIGFVTQDdVLLPQLTVEETLAFAAFLRLP---SSMSKEQKYAKIEMiikelgLER 215
Cdd:TIGR00957 686 AEM-DKVEGHVH---------MKGSVAYVPQQ-AWIQNDSLRENILFGKALNEKyyqQVLEACALLPDLEI------LPS 748
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 216 CRRTRVGGgfvKGI--SGGERKRASIAYEILVDPSLLLLDEPTSGLDSTSATkllHILQGVAK-----AGRTVITTIHQP 288
Cdd:TIGR00957 749 GDRTEIGE---KGVnlSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGK---HIFEHVIGpegvlKNKTRILVTHGI 822
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 289 SsrMFHMFDKLLLISEGHPAFYGKARESMEYFSSLrilpeiamnpAEFLLDLATGQvSDISLPDELLAA-----KTAQPD 363
Cdd:TIGR00957 823 S--YLPQVDVIIVMSGGKISEMGSYQELLQRDGAF----------AEFLRTYAPDE-QQGHLEDSWTALvsgegKEAKLI 889
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 22331045 364 SEEVLLKYLKQRY---KTDLEPKEKEENHRNRKAPEHLQIAIQVKKDWTL 410
Cdd:TIGR00957 890 ENGMLVTDVVGKQlqrQLSASSSDSGDQSRHHGSSAELQKAEAKEETWKL 939
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
105-271 |
9.03e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 58.71 E-value: 9.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 105 HILKGITGSTGPGEILALMGPSGSGKTTLLKIMGgRLTDNVKGKLTYN-----DIPYSP--SVKRRIGFVTQDDV--LLP 175
Cdd:PRK10261 338 HAVEKVSFDLWPGETLSLVGESGSGKSTTGRALL-RLVESQGGEIIFNgqridTLSPGKlqALRRDIQFIFQDPYasLDP 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 176 QLTVEETLAFAafLRLPSSMSKEQKYAKIEMIIKELGLERCRRTRVGGGFvkgiSGGERKRASIAYEILVDPSLLLLDEP 255
Cdd:PRK10261 417 RQTVGDSIMEP--LRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEF----SGGQRQRICIARALALNPKVIIADEA 490
|
170
....*....|....*.
gi 22331045 256 TSGLDSTSATKLLHIL 271
Cdd:PRK10261 491 VSALDVSIRGQIINLL 506
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
93-260 |
1.39e-08 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 57.12 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 93 VTHTNPDPDGYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIM-------GGRLTdnVKGK-LTYNDIPYSPSVKRRI 164
Cdd:PRK11153 7 ISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCInllerptSGRVL--VDGQdLTALSEKELRKARRQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 165 GFVTQDDVLLPQLTVEETLAFAafLRLpSSMSKEQKYAKIEMIIKELGLERCRRTrvgggFVKGISGGERKRASIAYEIL 244
Cdd:PRK11153 85 GMIFQHFNLLSSRTVFDNVALP--LEL-AGTPKAEIKARVTELLELVGLSDKADR-----YPAQLSGGQKQRVAIARALA 156
|
170
....*....|....*.
gi 22331045 245 VDPSLLLLDEPTSGLD 260
Cdd:PRK11153 157 SNPKVLLCDEATSALD 172
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
116-260 |
1.50e-08 |
|
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: 57.64 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 116 PGEILALMGPSGSGKTTLLKIMGGRLTDNvKGKLTYNDipyspSVKrrIGFVTQD-DVLLPQLTVEETLafaaflrlpSS 194
Cdd:TIGR03719 347 PGGIVGVIGPNGAGKSTLFRMITGQEQPD-SGTIEIGE-----TVK--LAYVDQSrDALDPNKTVWEEI---------SG 409
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 195 MSKEQKYAKIEMIIKELglerCRRTRVGGG----FVKGISGGERKRASIAYEILVDPSLLLLDEPTSGLD 260
Cdd:TIGR03719 410 GLDIIKLGKREIPSRAY----VGRFNFKGSdqqkKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
102-300 |
1.60e-08 |
|
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: 54.29 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 102 GYKHILKGITGSTGPGEILALMGPSGSGKTTLLkimggrltdnvkgkltyndipyspsvkRRIGFVTqddvllpqltvee 181
Cdd:cd03227 6 RFPSYFVPNDVTFGEGSLTIITGPNGSGKSTIL---------------------------DAIGLAL------------- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 182 TLAFAAFLRLPSSMSKEQK-YAKIEMIIkelglercrrtrvgggFVKGISGGERKRASIAYEI---LVDP-SLLLLDEPT 256
Cdd:cd03227 46 GGAQSATRRRSGVKAGCIVaAVSAELIF----------------TRLQLSGGEKELSALALILalaSLKPrPLYILDEID 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 22331045 257 SGLDSTSATKLLHILQGVAKAGRTVITTIHQPssRMFHMFDKLL 300
Cdd:cd03227 110 RGLDPRDGQALAEAILEHLVKGAQVIVITHLP--ELAELADKLI 151
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
116-311 |
1.64e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 56.22 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 116 PGEILALMGPSGSGKTTLLKIMGGRLTDNVkGKLTYND-----IPYSPSVKRRIGF--VTQDDV----------LLPQL- 177
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNL-GKFDDPPdwdeiLDEFRGSELQNYFtkLLEGDVkvivkpqyvdLIPKAv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 178 --TVEETLafaaflrlpssmSKEQKYAKIEMIIKELGLERCRRTRVgggfvKGISGGERKRASIAYEILVDPSLLLLDEP 255
Cdd:cd03236 104 kgKVGELL------------KKKDERGKLDELVDQLELRHVLDRNI-----DQLSGGELQRVAIAAALARDADFYFFDEP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 22331045 256 TSGLDSTSATKLLHILQGVAKAGRTVITTIHQPSsrMFHMFDKLLLISEGHPAFYG 311
Cdd:cd03236 167 SSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLA--VLDYLSDYIHCLYGEPGAYG 220
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
102-306 |
1.77e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 55.84 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 102 GYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYNDIPYSpSVKRRIGFVTQDDVLLPQLTVEE 181
Cdd:PRK11247 23 GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAG-LETPSAGELLAGTAPLA-EAREDTRLMFQDARLLPWKKVID 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 182 TLAfaafLRLPSSMSKEQKYAkiemiIKELGL-ERcrrtrvGGGFVKGISGGERKRASIAYEILVDPSLLLLDEPTSGLD 260
Cdd:PRK11247 101 NVG----LGLKGQWRDAALQA-----LAAVGLaDR------ANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 22331045 261 STSATKLLHILQGV-AKAGRTVITTIHQPSSRMfHMFDKLLLISEGH 306
Cdd:PRK11247 166 ALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAV-AMADRVLLIEEGK 211
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
117-286 |
1.89e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 56.33 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 117 GEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYNDI--------PYSPSVKRRIGFVTQ-DDVLLPQLTVEETLAFAa 187
Cdd:PRK13646 33 GKYYAIVGQTGSGKSTLIQNINA-LLKPTTGTVTVDDItithktkdKYIRPVRKRIGMVFQfPESQLFEDTVEREIIFG- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 188 flrlPSS--MSKEQKYAKIEMIIKELGLERcrrtRVGGGFVKGISGGERKRASIAYEILVDPSLLLLDEPTSGLDSTSAT 265
Cdd:PRK13646 111 ----PKNfkMNLDEVKNYAHRLLMDLGFSR----DVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKR 182
|
170 180
....*....|....*....|..
gi 22331045 266 KLLHILQGVA-KAGRTVITTIH 286
Cdd:PRK13646 183 QVMRLLKSLQtDENKTIILVSH 204
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
171-286 |
2.35e-08 |
|
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: 57.33 E-value: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 171 DVLlpQLTVEETLAFaaFLRLPSSMSKEQkyakiemIIKELGLERCRRtrvgGGFVKGISGGERKRASIAYEIL---VDP 247
Cdd:TIGR00630 787 DVL--DMTVEEAYEF--FEAVPSISRKLQ-------TLCDVGLGYIRL----GQPATTLSGGEAQRIKLAKELSkrsTGR 851
|
90 100 110
....*....|....*....|....*....|....*....
gi 22331045 248 SLLLLDEPTSGLDSTSATKLLHILQGVAKAGRTVITTIH 286
Cdd:TIGR00630 852 TLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEH 890
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
99-286 |
3.01e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 55.51 E-value: 3.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 99 DPDGYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDN-----VKG-KLTYNDIPyspSVKRRIGFVTQD-D 171
Cdd:PRK13650 15 KEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAEsgqiiIDGdLLTEENVW---DIRHKIGMVFQNpD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 172 VLLPQLTVEETLAFAaflrLPSS-MSKEQKYAKIEMIIKELGL------ERCRrtrvgggfvkgISGGERKRASIAYEIL 244
Cdd:PRK13650 92 NQFVGATVEDDVAFG----LENKgIPHEEMKERVNEALELVGMqdfkerEPAR-----------LSGGQKQRVAIAGAVA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 22331045 245 VDPSLLLLDEPTSGLDSTSATKLLHILQGVAKA-GRTVITTIH 286
Cdd:PRK13650 157 MRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITH 199
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
104-260 |
3.76e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.50 E-value: 3.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 104 KHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTdnvkgkltyndiPYSPSV----KRRIGFVTQDDVLL-PQLT 178
Cdd:PRK11147 332 KQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQ------------ADSGRIhcgtKLEVAYFDQHRAELdPEKT 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 179 VEETLAfaaflrlpssmskeqkYAKIEMIIKelGLER------------CRRTRVGggfVKGISGGERKRASIAyEILVD 246
Cdd:PRK11147 400 VMDNLA----------------EGKQEVMVN--GRPRhvlgylqdflfhPKRAMTP---VKALSGGERNRLLLA-RLFLK 457
|
170
....*....|....*
gi 22331045 247 PS-LLLLDEPTSGLD 260
Cdd:PRK11147 458 PSnLLILDEPTNDLD 472
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
104-332 |
1.08e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 53.94 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 104 KHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDNvKGKLTYNDIPYSP-----SVKRRIGFVTQD-DVLLPQL 177
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPS-EGKVYVDGLDTSDeenlwDIRNKAGMVFQNpDNQIVAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 178 TVEETLAFAaflrlPSSMSKEQK--YAKIEMIIKELGLERCRRTRVgggfvKGISGGERKRASIAYEILVDPSLLLLDEP 255
Cdd:PRK13633 102 IVEEDVAFG-----PENLGIPPEeiRERVDESLKKVGMYEYRRHAP-----HLLSGGQKQRVAIAGILAMRPECIIFDEP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 256 TSGLDSTSATKLLHILQGVAK-AGRTVITTIH-----QPSSRMFHMfDKLLLISEGHPAfygkaresmEYFSSLRILPEI 329
Cdd:PRK13633 172 TAMLDPSGRREVVNTIKELNKkYGITIILITHymeeaVEADRIIVM-DSGKVVMEGTPK---------EIFKEVEMMKKI 241
|
...
gi 22331045 330 AMN 332
Cdd:PRK13633 242 GLD 244
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
98-260 |
1.14e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 55.03 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 98 PDPDGyKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYNDIPYS-PSVKRR----IGFVTQD-- 170
Cdd:COG3845 266 RDDRG-VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAG-LRPPASGSIRLDGEDITgLSPRERrrlgVAYIPEDrl 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 171 -DVLLPQLTVEETLAFAAFLRLPSS------MSKEQKYAkiEMIIKELGLercrRTRVGGGFVKGISGGERKRASIAYEI 243
Cdd:COG3845 344 gRGLVPDMSVAENLILGRYRRPPFSrggfldRKAIRAFA--EELIEEFDV----RTPGPDTPARSLSGGNQQKVILAREL 417
|
170
....*....|....*..
gi 22331045 244 LVDPSLLLLDEPTSGLD 260
Cdd:COG3845 418 SRDPKLLIAAQPTRGLD 434
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
107-305 |
1.23e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 53.64 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 107 LKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKG-------KLTYNDIPYSpsvKRRIGFVTQD--DVLLPQL 177
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAG-MIEPTSGelliddhPLHFGDYSYR---SQRIRMIFQDpsTSLNPRQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 178 TVEETLAFAafLRLPSSMSKEQKYAKIEMIIKELGLercrRTRVGGGFVKGISGGERKRASIAYEILVDPSLLLLDEPTS 257
Cdd:PRK15112 105 RISQILDFP--LRLNTDLEPEQREKQIIETLRQVGL----LPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 22331045 258 GLDSTSATKLLHI-LQGVAKAGRTVItTIHQPSSRMFHMFDKLLLISEG 305
Cdd:PRK15112 179 SLDMSMRSQLINLmLELQEKQGISYI-YVTQHLGMMKHISDQVLVMHQG 226
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
117-260 |
2.11e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 54.36 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 117 GEILALMGPSGSGKTTLLKIMGGrLTDNVKGK-------LTYNDIpyspSVKRRIGFVTQDDVLLPQLTVEETLAFAAFL 189
Cdd:NF033858 292 GEIFGFLGSNGCGKSTTMKMLTG-LLPASEGEawlfgqpVDAGDI----ATRRRVGYMSQAFSLYGELTVRQNLELHARL 366
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22331045 190 -RLPssmsKEQKYAKIEMIIKELGLERCRRTRVGGgfvkgISGGERKRASIAYEILVDPSLLLLDEPTSGLD 260
Cdd:NF033858 367 fHLP----AAEIAARVAEMLERFDLADVADALPDS-----LPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
100-282 |
2.98e-07 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 52.99 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 100 PDGYKHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDNVK---GKLTYNDI---PYSPSVKRR-----IGFVT 168
Cdd:COG4170 16 PQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHvtaDRFRWNGIdllKLSPRERRKiigreIAMIF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 169 QDDV--LLPQLTVEETLAFAaflrLPSSMSK----EQKYAKIEMIIKELglercrrTRVGggfVKG-----------ISG 231
Cdd:COG4170 96 QEPSscLDPSAKIGDQLIEA----IPSWTFKgkwwQRFKWRKKRAIELL-------HRVG---IKDhkdimnsypheLTE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 22331045 232 GERKRASIAYEILVDPSLLLLDEPTSGLDSTSATKLLHILQGVAKAGRTVI 282
Cdd:COG4170 162 GECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSI 212
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
117-305 |
4.27e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.01 E-value: 4.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 117 GEILALMGPSGSGKTTLLK-IMG---GRLTDNV--KGK-LTYNdipySP--SVKRRIGFVTQD---DVLLPQLTVEE--T 182
Cdd:PRK13549 288 GEILGIAGLVGAGRTELVQcLFGaypGRWEGEIfiDGKpVKIR----NPqqAIAQGIAMVPEDrkrDGIVPVMGVGKniT 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 183 LA----FAAFLRLPSSmsKEQKYakIEMIIKELGLercrRTRVGGGFVKGISGGERKRASIAYEILVDPSLLLLDEPTSG 258
Cdd:PRK13549 364 LAaldrFTGGSRIDDA--AELKT--ILESIQRLKV----KTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRG 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 22331045 259 LDSTSATKLLHILQGVAKAGRTVITTihqpSSRM---FHMFDKLLLISEG 305
Cdd:PRK13549 436 IDVGAKYEIYKLINQLVQQGVAIIVI----SSELpevLGLSDRVLVMHEG 481
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
170-287 |
4.30e-07 |
|
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: 51.85 E-value: 4.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 170 DDVLlpQLTVEETLAFaaFLRLPSSMSKEQkyakiemIIKELGLercrrtrvggGFVK------GISGGERKRASIAYEI 243
Cdd:cd03271 126 ADVL--DMTVEEALEF--FENIPKIARKLQ-------TLCDVGL----------GYIKlgqpatTLSGGEAQRIKLAKEL 184
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 22331045 244 L---VDPSLLLLDEPTSGLDSTSATKLLHILQGVAKAGRTVITTIHQ 287
Cdd:cd03271 185 SkrsTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHN 231
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
117-292 |
4.58e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 51.68 E-value: 4.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 117 GEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYNDIPYSPS----VKRRIGFVTQDdvllPQLT-VEETLAF-AAFLR 190
Cdd:PRK13648 35 GQWTSIVGHNGSGKSTIAKLMIG-IEKVKSGEIFYNNQAITDDnfekLRKHIGIVFQN----PDNQfVGSIVKYdVAFGL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 191 LPSSMSKEQKYAKIEMIIKELGLERCRRTRVgggfvKGISGGERKRASIAYEILVDPSLLLLDEPTSGLDSTSATKLLHI 270
Cdd:PRK13648 110 ENHAVPYDEMHRRVSEALKQVDMLERADYEP-----NALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDL 184
|
170 180
....*....|....*....|...
gi 22331045 271 LQGV-AKAGRTVITTIHQPSSRM 292
Cdd:PRK13648 185 VRKVkSEHNITIISITHDLSEAM 207
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
229-286 |
6.02e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 53.29 E-value: 6.02e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22331045 229 ISGGERKRASIAYEILV---DPSLLLLDEPTSGLDSTSATKLLHILQGVAKAGRTVITTIH 286
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEH 870
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
117-315 |
9.17e-07 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 51.25 E-value: 9.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 117 GEILALMGPSGSGKTT-------LLKIMGGRLTDNVKGKLTYNDIPYSpSVKRRIGFVTQDDV--LLPQLTVEETLAFAA 187
Cdd:PRK15079 47 GETLGVVGESGCGKSTfaraiigLVKATDGEVAWLGKDLLGMKDDEWR-AVRSDIQMIFQDPLasLNPRMTIGEIIAEPL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 188 FLRLPSsMSKEQKYAKIEMIIKELGLERCRRTRVGGGFvkgiSGGERKRASIAYEILVDPSLLLLDEPTSGLDSTSATKL 267
Cdd:PRK15079 126 RTYHPK-LSRQEVKDRVKAMMLKVGLLPNLINRYPHEF----SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQV 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 22331045 268 LHILQGVAKA-GRTVITTIHQPSSrMFHMFDKLLLISEGHPAFYGKARE 315
Cdd:PRK15079 201 VNLLQQLQREmGLSLIFIAHDLAV-VKHISDRVLVMYLGHAVELGTYDE 248
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
117-306 |
1.18e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.54 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 117 GEILALMGPSGSGKTTLLKIMGGRLTDNvKGKLTYND---IPYSPS--VKRRIGFVTQD---DVLLPQLTVEETLAFAAF 188
Cdd:PRK10762 278 GEILGVSGLMGAGRTELMKVLYGALPRT-SGYVTLDGhevVTRSPQdgLANGIVYISEDrkrDGLVLGMSVKENMSLTAL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 189 LRLPSSMSKEQKYAKIEMI--------IKELGLERCrrtrvgggfVKGISGGERKRASIAYEILVDPSLLLLDEPTSGLD 260
Cdd:PRK10762 357 RYFSRAGGSLKHADEQQAVsdfirlfnIKTPSMEQA---------IGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 22331045 261 sTSATKLLHILQGVAKA-GRTVITTihqpSSRM---FHMFDKLLLISEGH 306
Cdd:PRK10762 428 -VGAKKEIYQLINQFKAeGLSIILV----SSEMpevLGMSDRILVMHEGR 472
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
117-276 |
1.23e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 50.47 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 117 GEILALMGPSGSGKT----TLLKIM--GGRLTdnvKGKLTYNDIPYSPSVKR--RIGFVTQD--DVLLPQLT----VEET 182
Cdd:PRK10418 29 GRVLALVGGSGSGKSltcaAALGILpaGVRQT---AGRVLLDGKPVAPCALRgrKIATIMQNprSAFNPLHTmhthARET 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 183 LAfaaflrlpsSMSKEQKYAKIEMIIKELGLERcrRTRVGGGFVKGISGGERKRASIAYEILVDPSLLLLDEPTSGLDST 262
Cdd:PRK10418 106 CL---------ALGKPADDATLTAALEAVGLEN--AARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVV 174
|
170
....*....|....
gi 22331045 263 SATKLLHILQGVAK 276
Cdd:PRK10418 175 AQARILDLLESIVQ 188
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
116-286 |
1.35e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 51.71 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 116 PGEILALMGPSGSGKTTLLKIMGGRLTDN---VKGKLTYNDIpyspsVKRRIGFVTQD-----------DVLLPQL---- 177
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNlgdYDEEPSWDEV-----LKRFRGTELQDyfkklangeikVAHKPQYvdli 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 178 ------TVEETLafaaflrlpssmSKEQKYAKIEMIIKELGLERC--RRtrvgggfVKGISGGERKRASIAYEILVDPSL 249
Cdd:COG1245 173 pkvfkgTVRELL------------EKVDERGKLDELAEKLGLENIldRD-------ISELSGGELQRVAIAAALLRDADF 233
|
170 180 190
....*....|....*....|....*....|....*..
gi 22331045 250 LLLDEPTSGLDSTSATKLLHILQGVAKAGRTVITTIH 286
Cdd:COG1245 234 YFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEH 270
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
106-290 |
1.36e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.95 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 106 ILKGITGSTGPGEILALMGPSGSGKTTLLKIMGgRLTDNVKGKLTYNDIPYSPSV-----KRRIGFVTQDDVLLPQlTVE 180
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIE-RLYDPTEGDIIINDSHNLKDInlkwwRSKIGVVSQDPLLFSN-SIK 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 181 ETLAFAAF----LRLPSSMSKEQKYAKIE-----------------MIIKEL---GLERCRR------------------ 218
Cdd:PTZ00265 478 NNIKYSLYslkdLEALSNYYNEDGNDSQEnknkrnscrakcagdlnDMSNTTdsnELIEMRKnyqtikdsevvdvskkvl 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 219 -------------TRVGGGFVKgISGGERKRASIAYEILVDPSLLLLDEPTSGLDSTS---ATKLLHILQGvaKAGRTVI 282
Cdd:PTZ00265 558 ihdfvsalpdkyeTLVGSNASK-LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSeylVQKTINNLKG--NENRITI 634
|
....*...
gi 22331045 283 TTIHQPSS 290
Cdd:PTZ00265 635 IIAHRLST 642
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
107-287 |
1.48e-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: 49.64 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 107 LKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLtDNVKGKLTY-NDIPYSPSVKRR-------IGFVTQDDVLLpQLT 178
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEM-QTLEGKVHWsNKNESEPSFEATrsrnrysVAYAAQKPWLL-NAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 179 VEETLAFAaflrlpsSMSKEQKYakiEMIIKELGLE-------RCRRTRVGGgfvKGI--SGGERKRASIAYEILVDPSL 249
Cdd:cd03290 95 VEENITFG-------SPFNKQRY---KAVTDACSLQpdidllpFGDQTEIGE---RGInlSGGQRQRICVARALYQNTNI 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 22331045 250 LLLDEPTSGLDSTSATKLLH--ILQGVAKAGRTVITTIHQ 287
Cdd:cd03290 162 VFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHK 201
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
104-305 |
1.66e-06 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 49.91 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 104 KHILKGITGSTGPGEILALMGPSGSGKTTlLKIMGGRLTDNVKGKLTYN--DIPYSP--SVKRRIGFVTQDDVLlpqltv 179
Cdd:cd03288 34 KPVLKHVKAYIKPGQKVGICGRTGSGKSS-LSLAFFRMVDIFDGKIVIDgiDISKLPlhTLRSRLSIILQDPIL------ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 180 eetlaFAAFLRL---------PSSMSKEQKYAKIEMIIKEL--GLERCrRTRVGGGFvkgiSGGERKRASIAYEILVDPS 248
Cdd:cd03288 107 -----FSGSIRFnldpeckctDDRLWEALEIAQLKNMVKSLpgGLDAV-VTEGGENF----SVGQRQLFCLARAFVRKSS 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 249 LLLLDEPTSGLDstSATKllHILQGV---AKAGRTVITTIHQPSSRMfhMFDKLLLISEG 305
Cdd:cd03288 177 ILIMDEATASID--MATE--NILQKVvmtAFADRTVVTIAHRVSTIL--DADLVLVLSRG 230
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
103-288 |
3.29e-06 |
|
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: 48.79 E-value: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 103 YKHILKGITGSTGPGEILALMGPSGSGKTTLlkimgGRLTDNVKGKLTYNDiPYSPSVKRRIGFVTQDDV-----LLPQL 177
Cdd:cd03270 7 REHNLKNVDVDIPRNKLVVITGVSGSGKSSL-----AFDTIYAEGQRRYVE-SLSAYARQFLGQMDKPDVdsiegLSPAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 178 TVEETLA-------------FAAFLRLpssmskeqKYAKIEMI-----IKELGLERCRRTRVGGGfvkgISGGERKRASI 239
Cdd:cd03270 81 AIDQKTTsrnprstvgtvteIYDYLRL--------LFARVGIRerlgfLVDVGLGYLTLSRSAPT----LSGGEAQRIRL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 22331045 240 AYEI---LVDpSLLLLDEPTSGLDSTSATKLLHILQGVAKAGRTVITTIHQP 288
Cdd:cd03270 149 ATQIgsgLTG-VLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDE 199
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
117-272 |
3.97e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 50.24 E-value: 3.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 117 GEILALMGPSGSGKT-TLLKIMggRLTDNVKGKLTYNDIPYSPSVKRRIGFVTQDDV--------------------LLP 175
Cdd:PRK10261 42 GETLAIVGESGSGKSvTALALM--RLLEQAGGLVQCDKMLLRRRSRQVIELSEQSAAqmrhvrgadmamifqepmtsLNP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 176 QLTVEETLAFAafLRLPSSMSKEQKYAKIEMIIKELGLERCRRtrVGGGFVKGISGGERKRASIAYEILVDPSLLLLDEP 255
Cdd:PRK10261 120 VFTVGEQIAES--IRLHQGASREEAMVEAKRMLDQVRIPEAQT--ILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEP 195
|
170
....*....|....*..
gi 22331045 256 TSGLDSTSATKLLHILQ 272
Cdd:PRK10261 196 TTALDVTIQAQILQLIK 212
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
213-315 |
4.58e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 49.35 E-value: 4.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 213 LERCRRTRVGGGFVKGISGGERKRASIAYEILVDPSLLLLDEPTSGLDSTSATKLLHILQGVAKAGRTVITTIH--QPSS 290
Cdd:NF000106 129 LERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQymEEAE 208
|
90 100
....*....|....*....|....*
gi 22331045 291 RMFHmfdKLLLISEGHPAFYGKARE 315
Cdd:NF000106 209 QLAH---ELTVIDRGRVIADGKVDE 230
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
117-320 |
5.09e-06 |
|
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: 47.57 E-value: 5.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 117 GEILALMGPSGSGKTTLLKIMGGRLtdnvkgkltyndIPyspsvkrrigfvTQDDVLLPQLTVeetlafaaflrlpssMS 196
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQL------------IP------------NGDNDEWDGITP---------------VY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 197 KEQKYAkiemiikelglercrrtrvgggfvkgISGGERKRASIAYEILVDPSLLLLDEPTSGLDST---SATKLLHILqg 273
Cdd:cd03222 66 KPQYID--------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlNAARAIRRL-- 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 22331045 274 VAKAGRTVITTIHQpssrmFHMFDKL---LLISEGHPAFYGKA------RESMEYF 320
Cdd:cd03222 118 SEEGKKTALVVEHD-----LAVLDYLsdrIHVFEGEPGVYGIAsqpkgtREGINRF 168
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
100-289 |
5.68e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 47.32 E-value: 5.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 100 PDGYKHILKGITGSTGPGEILALMGPSGSGKTTLLkimggrltdnvkgkltyNDIPYSPSVKRRIGFVTQDDvllPQLTV 179
Cdd:cd03238 4 SGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLV-----------------NEGLYASGKARLISFLPKFS---RNKLI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 180 eetlafaaFLRLPSSMskeqkyakIEMIIKELGLERCRRTrvgggfvkgISGGERKRASIAYEILVDP--SLLLLDEPTS 257
Cdd:cd03238 64 --------FIDQLQFL--------IDVGLGYLTLGQKLST---------LSGGELQRVKLASELFSEPpgTLFILDEPST 118
|
170 180 190
....*....|....*....|....*....|..
gi 22331045 258 GLDSTSATKLLHILQGVAKAGRTVITTIHQPS 289
Cdd:cd03238 119 GLHQQDINQLLEVIKGLIDLGNTVILIEHNLD 150
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
106-287 |
6.26e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 47.64 E-value: 6.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 106 ILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYndipYSPSVKR-------RIGFVTQDDVLLPQLT 178
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAG-LLNPEKGEILF----ERQSIKKdlctyqkQLCFVGHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 179 VEETLAFaaflrlpssmskEQKYAKIEMIIKELglerCRRTRVGG--GFVKGI-SGGERKRASIAYEILVDPSLLLLDEP 255
Cdd:PRK13540 91 LRENCLY------------DIHFSPGAVGITEL----CRLFSLEHliDYPCGLlSSGQKRQVALLRLWMSKAKLWLLDEP 154
|
170 180 190
....*....|....*....|....*....|..
gi 22331045 256 TSGLDSTSATKLLHILQGVAKAGRTVITTIHQ 287
Cdd:PRK13540 155 LVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
101-306 |
6.79e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 49.28 E-value: 6.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 101 DGYKHIlkgiTGSTGPGEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYNDIPYSP-SVKRRIgfvTQDDVLLPqltv 179
Cdd:PRK15439 277 EGFRNI----SLEVRAGEILGLAGVVGAGRTELAETLYG-LRPARGGRIMLNGKEINAlSTAQRL---ARGLVYLP---- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 180 EETLAFAAFLRLPSSMS-------------KEQKYAKIemiikelgLERCRRTrVGGGF------VKGISGGERKRASIA 240
Cdd:PRK15439 345 EDRQSSGLYLDAPLAWNvcalthnrrgfwiKPARENAV--------LERYRRA-LNIKFnhaeqaARTLSGGNQQKVLIA 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22331045 241 YEILVDPSLLLLDEPTSGLDSTSATKLLHILQGVAKAGRTVItTIHQPSSRMFHMFDKLLLISEGH 306
Cdd:PRK15439 416 KCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVL-FISSDLEEIEQMADRVLVMHQGE 480
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
117-271 |
1.83e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 47.43 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 117 GEILALMGPSGSGKT-TLLKIMG-----GRLTDNvkgKLTYN--DIPYSPSVKRR------IGFVTQDDV--LLPQLTVE 180
Cdd:PRK11022 33 GEVVGIVGESGSGKSvSSLAIMGlidypGRVMAE---KLEFNgqDLQRISEKERRnlvgaeVAMIFQDPMtsLNPCYTVG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 181 ETLAFAafLRLPSSMSKEQKYAKIEMIIKELGL-ERCRRTRVgggFVKGISGGERKRASIAYEILVDPSLLLLDEPTSGL 259
Cdd:PRK11022 110 FQIMEA--IKVHQGGNKKTRRQRAIDLLNQVGIpDPASRLDV---YPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTAL 184
|
170
....*....|..
gi 22331045 260 DSTSATKLLHIL 271
Cdd:PRK11022 185 DVTIQAQIIELL 196
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
116-302 |
1.86e-05 |
|
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: 45.06 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 116 PGEILALMGPSGSGKTTLLKIMGGRLTDNVKGkltyndipyspsvkrrigfvtqddvllpqltveetlafaaFLRLPSSM 195
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGG----------------------------------------VIYIDGED 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 196 SKEQKYAKIEMIIkelglercrrtrvGGGFVKGISGGERKRASIAYEILVDPSLLLLDEPTSGLDSTSATKLLHILQGVA 275
Cdd:smart00382 41 ILEEVLDQLLLII-------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRL 107
|
170 180 190
....*....|....*....|....*....|....*..
gi 22331045 276 ------KAGRTVITTIHQP----SSRMFHMFDKLLLI 302
Cdd:smart00382 108 llllksEKNLTVILTTNDEkdlgPALLRRRFDRRIVL 144
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
117-305 |
2.31e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.05 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 117 GEILALMGPSGSGKTTLLKIMGGRLTDNVKGKLTYN-DIPYSPSVKrrigfvtqddvLLPQLTVEETLAFAaflrlpSSM 195
Cdd:PLN03232 643 GSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRgSVAYVPQVS-----------WIFNATVRENILFG------SDF 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 196 SKEQKYAKIEM--IIKELGLERCR-RTRVGGGFVKgISGGERKRASIAYEILVDPSLLLLDEPTSGLDSTSATKLLHILQ 272
Cdd:PLN03232 706 ESERYWRAIDVtaLQHDLDLLPGRdLTEIGERGVN-ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCM 784
|
170 180 190
....*....|....*....|....*....|...
gi 22331045 273 GVAKAGRTVITTIHQpsSRMFHMFDKLLLISEG 305
Cdd:PLN03232 785 KDELKGKTRVLVTNQ--LHFLPLMDRIILVSEG 815
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
107-286 |
5.33e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.58 E-value: 5.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 107 LKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTdnvkgkltyndiPYSPSVKR--RIGFVTQDDVLLPQLTVEETLA 184
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLS------------PTVGKVDRngEVSVIAISAGLSGQLTGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 185 FAAFLrlpssMSKEQKYakiemiIKELGLERCRRTRVGGGF---VKGISGGERKRASIAYEILVDPSLLLLDEPTSGLDS 261
Cdd:PRK13546 108 FKMLC-----MGFKRKE------IKAMTPKIIEFSELGEFIyqpVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQ 176
|
170 180
....*....|....*....|....*
gi 22331045 262 TSATKLLHILQGVAKAGRTVITTIH 286
Cdd:PRK13546 177 TFAQKCLDKIYEFKEQNKTIFFVSH 201
|
|
| ABC2_membrane_7 |
pfam19055 |
ABC-2 type transporter; |
286-345 |
6.74e-05 |
|
ABC-2 type transporter;
Pssm-ID: 465963 [Multi-domain] Cd Length: 409 Bit Score: 45.67 E-value: 6.74e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22331045 286 HQPSSRMFHMFDKLLLISEGH-PAFYGKARESMEYFSSLRI-LPEiAMNPAEFLLDLATGQV 345
Cdd:pfam19055 1 HQPSYTLFKMFDDLILLAKGGlTVYHGPVKKVEEYFAGLGInVPE-RVNPPDHFIDILEGIV 61
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
122-260 |
7.01e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.01 E-value: 7.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 122 LMGPSGSGKTTLLKIMGGRLTD---------NVKGKLTYNDIP-----YSPSVKRRIGFVTQDDVLLPQLTVEETLAFA- 186
Cdd:PLN03073 208 LVGRNGTGKTTFLRYMAMHAIDgipkncqilHVEQEVVGDDTTalqcvLNTDIERTQLLEEEAQLVAQQRELEFETETGk 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 187 -------AFLRLPSSMSKEQKYAKIEMIIKELGLERCRRTRVGGGF--------VKGISGGERKRASIAYEILVDPSLLL 251
Cdd:PLN03073 288 gkgankdGVDKDAVSQRLEEIYKRLELIDAYTAEARAASILAGLSFtpemqvkaTKTFSGGWRMRIALARALFIEPDLLL 367
|
....*....
gi 22331045 252 LDEPTSGLD 260
Cdd:PLN03073 368 LDEPTNHLD 376
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
117-282 |
1.06e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 45.29 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 117 GEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYNDIPYSP-----SVKRRIGFVTQD---DVLLPQLTVEETLAFAA- 187
Cdd:PRK11288 279 GEIVGLFGLVGAGRSELMKLLYG-ATRRTAGQVYLDGKPIDIrsprdAIRAGIMLCPEDrkaEGIIPVHSVADNINISAr 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 188 --FLRLPSSMSKEQKYAKIEMIIKELGLercrRTRVGGGFVKGISGGERKRASIAYEILVDPSLLLLDEPTSGLDSTSAT 265
Cdd:PRK11288 358 rhHLRAGCLINNRWEAENADRFIRSLNI----KTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKH 433
|
170
....*....|....*..
gi 22331045 266 KLLHILQGVAKAGRTVI 282
Cdd:PRK11288 434 EIYNVIYELAAQGVAVL 450
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
104-290 |
1.52e-04 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 45.09 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 104 KHILKGITGSTGPGEILALMGPSGSGKTTLLKIMGGRLTDNvKGKLTYNDIP---YSPSVKRR-IGFVTQDDVLLPQltv 179
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLT-EGEIRLDGRPlssLSHSVLRQgVAMVQQDPVVLAD--- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 180 eetlAFAAFLRLPSSMSKEQKYAKIEMI-IKEL--GLERCRRTRVGGgfvKG--ISGGERKRASIAYEILVDPSLLLLDE 254
Cdd:PRK10790 430 ----TFLANVTLGRDISEEQVWQALETVqLAELarSLPDGLYTPLGE---QGnnLSVGQKQLLALARVLVQTPQILILDE 502
|
170 180 190
....*....|....*....|....*....|....*.
gi 22331045 255 PTSGLDSTSATKLLHILQGVAKAgRTVITTIHQPSS 290
Cdd:PRK10790 503 ATANIDSGTEQAIQQALAAVREH-TTLVVIAHRLST 537
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
170-282 |
2.14e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 44.63 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 170 DDVLlpQLTVEETLAFaaFLRLPSSMSKEQkyakiemIIKELGLercrrtrvggGFVK-G-----ISGGERKRASIAYEi 243
Cdd:COG0178 783 ADVL--DMTVEEALEF--FENIPKIARKLQ-------TLQDVGL----------GYIKlGqpattLSGGEAQRVKLASE- 840
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 22331045 244 LVDPS----LLLLDEPTSGLDSTSATKLLHILQGVAKAGRTVI 282
Cdd:COG0178 841 LSKRStgktLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVV 883
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
116-290 |
3.53e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 42.17 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 116 PGEILALMGPSGSGKTTLLKIMGGRLTDNvKGKLTYNDIPYSPSVKRRIGFVTQDDVLLPQLTVEETLAFAAFLrlpsSM 195
Cdd:PRK13541 25 PSAITYIKGANGCGKSSLLRMIAGIMQPS-SGNIYYKNCNINNIAKPYCTYIGHNLGLKLEMTVFENLKFWSEI----YN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 196 SKEQKYAKIEMI-IKELGLERCRRtrvgggfvkgISGGERKRASIAYEILVDPSLLLLDEPTSGLDSTSATKLLHILQGV 274
Cdd:PRK13541 100 SAETLYAAIHYFkLHDLLDEKCYS----------LSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMK 169
|
170
....*....|....*.
gi 22331045 275 AKAGRTVITTIHQPSS 290
Cdd:PRK13541 170 ANSGGIVLLSSHLESS 185
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
176-286 |
4.14e-04 |
|
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: 43.85 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 176 QLTVEETLAFAAFLRLPssmskEQKYAKIEMIIKE---------------LGLERCRRTrvgggfvkgISGGERKRASIA 240
Cdd:TIGR00630 435 ELSIREAHEFFNQLTLT-----PEEKKIAEEVLKEirerlgflidvgldyLSLSRAAGT---------LSGGEAQRIRLA 500
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 22331045 241 YEI---LVDpSLLLLDEPTSGLDSTSATKLLHILQGVAKAGRTVITTIH 286
Cdd:TIGR00630 501 TQIgsgLTG-VLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEH 548
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
116-305 |
5.52e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.18 E-value: 5.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 116 PGEILALMGPSGSGKTTLLKIMGGRLTDNvKGKLTY--NDIPYSPS---VKRRIGFVTQDDVLLPQLTVEETLAFAAFLR 190
Cdd:PRK10982 23 PHSIHALMGENGAGKSTLLKCLFGIYQKD-SGSILFqgKEIDFKSSkeaLENGISMVHQELNLVLQRSVMDNMWLGRYPT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 191 LPSSMSKEQKYAKIEMIIKELGLERCRRTRVGggfvkGISGGERKRASIAYEILVDPSLLLLDEPTSGLDSTSATKLLHI 270
Cdd:PRK10982 102 KGMFVDQDKMYRDTKAIFDELDIDIDPRAKVA-----TLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTI 176
|
170 180 190
....*....|....*....|....*....|....*
gi 22331045 271 LQGVAKAGRTVITTIHQpSSRMFHMFDKLLLISEG 305
Cdd:PRK10982 177 IRKLKERGCGIVYISHK-MEEIFQLCDEITILRDG 210
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
466-614 |
7.15e-04 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.
Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 42.38 E-value: 7.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 466 VGLMFYICIFWTSSSLFGAVYvfpFEKIYLVKERKAEM-YRLSVYYVCSTLCDMVAHVLyptFFMIIVYFMAEFNRNIPC 544
Cdd:pfam12698 164 VGLILMIIILIGAAIIAVSIV---EEKESRIKERLLVSgVSPLQYWLGKILGDFLVGLL---QLLIILLLLFGIGIPFGN 237
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22331045 545 FLFTVLTILLIAITSQGAGEFLGASVLSIKRAGMIASLVLMLF--LLTGGYYVQHIPKFMQW-LKYLSFMHYG 614
Cdd:pfam12698 238 LGLLLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLsgFFGGLFPLEDPPSFLQWiFSIIPFFSPI 310
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
227-282 |
9.92e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.31 E-value: 9.92e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 22331045 227 KGISGGERKRASIAYEILVDPSLLLLDEPTSGLDSTSATKLLHILQGVAKAGRTVI 282
Cdd:PRK10938 134 KYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLV 189
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
518-681 |
1.57e-03 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 40.18 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 518 MVAHVLYPTFFMIIVYFMAEFNRNIP----CFLFTVLTILLIAITSQGAGEFLGASVLSIKRAGMIASLVLM-LFLLTGG 592
Cdd:COG0842 53 VLAYLLRGLLQALLVLLVALLFFGVPlrglSLLLLLLVLLLFALAFSGLGLLISTLARSQEQASAISNLVILpLTFLSGA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 593 YY-VQHIPKFMQWLKYLSFMHYGFRLLLKVqysadqlfecgskggcrtlqsssSFDTINLNGGLQELWVLLAMAFGYRLC 671
Cdd:COG0842 133 FFpIESLPGWLQAIAYLNPLTYFVEALRAL-----------------------FLGGAGLADVWPSLLVLLAFAVVLLAL 189
|
170
....*....|
gi 22331045 672 AYFCLRKKIS 681
Cdd:COG0842 190 ALRLFRRRLR 199
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
223-272 |
1.70e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.81 E-value: 1.70e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 22331045 223 GGFVKGI---SGGERK------RASIAYEILVDPSLLLLDEPTSGLDSTSATKLLHILQ 272
Cdd:PRK01156 793 GGMVEGIdslSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIE 851
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
171-282 |
1.92e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.60 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 171 DVLlpQLTVEETLAFaaflrlpssmskeqkYAKIEMIIKELglercrRT--RVGGGFVK-G-----ISGGERKRASIAYE 242
Cdd:PRK00349 788 DVL--DMTVEEALEF---------------FEAIPKIARKL------QTlvDVGLGYIKlGqpattLSGGEAQRVKLAKE 844
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 22331045 243 ILVDP---SLLLLDEPTSGLDSTSATKLLHILQGVAKAGRTVI 282
Cdd:PRK00349 845 LSKRStgkTLYILDEPTTGLHFEDIRKLLEVLHRLVDKGNTVV 887
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
117-305 |
3.09e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 40.73 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 117 GEILALMGPSGSGKTTLLKIMGGrLTDNVKGKLTYNDIPYSPS----VKRRIGFVTQDdvllpqltveetlaFAAFLRLP 192
Cdd:PRK10522 349 GELLFLIGGNGSGKSTLAMLLTG-LYQPQSGEILLDGKPVTAEqpedYRKLFSAVFTD--------------FHLFDQLL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 193 SSMSKEQKYAKIEMIIKELGLErcRRTRVGGGFVKGI--SGGERKRASIAYEILVDPSLLLLDEPTSGLDSTSA----TK 266
Cdd:PRK10522 414 GPEGKPANPALVEKWLERLKMA--HKLELEDGRISNLklSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRrefyQV 491
|
170 180 190
....*....|....*....|....*....|....*....
gi 22331045 267 LLHILQgvaKAGRTVITTIHQPSsrMFHMFDKLLLISEG 305
Cdd:PRK10522 492 LLPLLQ---EMGKTIFAISHDDH--YFIHADRLLEMRNG 525
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
229-308 |
3.12e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.48 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 229 ISGGERKRASIAYEILVDPSLLLLDEPTSGLDSTSATKLLHILQGVAKAGRTVITTihqpSSRMFHMF---DKLLLISEG 305
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIII----SSEMPELLgitDRILVMSNG 467
|
...
gi 22331045 306 HPA 308
Cdd:PRK10982 468 LVA 470
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
118-288 |
3.30e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 39.56 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 118 EILALMGPSGSGKTTLLKIMGGRLTDNVKGkltyndipYSPSVKRRIGFVTQDDvllpqlTVEETLAFAAflrlpssmsK 197
Cdd:cd03279 29 GLFLICGPTGAGKSTILDAITYALYGKTPR--------YGRQENLRSVFAPGED------TAEVSFTFQL---------G 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 198 EQKYakieMIIKELGLERCRRTRV----GGGF-------VKGISGGERKRASIAYEI----LVDPS------LLLLDEPT 256
Cdd:cd03279 86 GKKY----RVERSRGLDYDQFTRIvllpQGEFdrflarpVSTLSGGETFLASLSLALalseVLQNRggarleALFIDEGF 161
|
170 180 190
....*....|....*....|....*....|..
gi 22331045 257 SGLDSTSATKLLHILQGVAKAGRTVITTIHQP 288
Cdd:cd03279 162 GTLDPEALEAVATALELIRTENRMVGVISHVE 193
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
229-337 |
7.50e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.81 E-value: 7.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331045 229 ISGGERKRASIAYEILVDPS--LLLLDEPTSGLDSTSATKLLHILQGVAKAGRTVITTIHQpsSRMFHMFDKLLLISEGH 306
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD--EQMISLADRIIDIGPGA 554
|
90 100 110
....*....|....*....|....*....|...
gi 22331045 307 PAFYGkaresmeyfsslrilpEIAMN--PAEFL 337
Cdd:PRK00635 555 GIFGG----------------EVLFNgsPREFL 571
|
|
| |
