|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1245-1466 |
7.31e-85 |
|
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: 276.69 E-value: 7.31e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1245 LRKEYagkrkgcfsKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDALEF 1320
Cdd:cd03263 6 LTKTY---------KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirTDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1321 LGYCPQENALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVL 1400
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6005701 1401 LDEPSTGMDPEGQQQMWQAIRATFRNteRGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLK 1466
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVRKG--RSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1258-1469 |
2.37e-73 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 244.59 E-value: 2.37e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1258 SKR-KNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDALEFLGYCPQENALWP 1332
Cdd:COG1131 7 TKRyGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGedvaRDPAEVRRRIGYVPQEPALYP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1333 NLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEG 1412
Cdd:COG1131 87 DLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 6005701 1413 QQQMWQAIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKF 1469
Cdd:COG1131 167 RRELWELLRE-LAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
235-750 |
2.07e-64 |
|
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: 243.00 E-value: 2.07e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 235 SFIYYASVNVT----RERKRMKALMTMMGLRDSAFWLSWgLLYAGFIFIMALFL-ALVIRSTQFIILSGFMVVFSLFLLY 309
Cdd:TIGR01257 662 AWIYSVSMTVKsivlEKELRLKETLKNQGVSNAVIWCTW-FLDSFSIMSMSIFLlTIFIMHGRILHYSDPFILFLFLLAF 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 310 GLSLVALAFLMSILVKKSFL----TGLVVFLLTV-FWGCLGFTSlyrHLPASLEWILSLLSPFAFMLGMAQLLHLDYD-- 382
Cdd:TIGR01257 741 STATIMQCFLLSTFFSKASLaaacSGVIYFTLYLpHILCFAWQD---RMTADLKTAVSLLSPVAFGFGTEYLVRFEEQgl 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 383 ----LNSNAFPHPSDGSNLIVATNFMLaFDTCLYLALAIYFEKILPNEYGHRRPPLFFLKSSFW-----------SQTQK 447
Cdd:TIGR01257 818 glqwSNIGNSPLEGDEFSFLLSMKMML-LDAALYGLLAWYLDQVFPGDYGTPLPWYFLLQESYWlggegcstreeRALEK 896
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 448 TDHVALEDEMDADPS-FHDSF-EQAPPEFQgkEAIRIRNVTK--EYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKS 523
Cdd:TIGR01257 897 TEPLTEEMEDPEHPEgINDSFfERELPGLV--PGVCVKNLVKifEPSGRP----AVDRLNITFYENQITAFLGHNGAGKT 970
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 524 TLLNILSGLSVPTKGSVTIYNNKLSemADLENLSKLTGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEV---------- 593
Cdd:TIGR01257 971 TTLSILTGLLPPTSGTVLVGGKDIE--TNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAqlemeamled 1048
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 594 ------------------------------DKEIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEADILAD 643
Cdd:TIGR01257 1049 tglhhkrneeaqdlsggmqrklsvaiafvgDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGD 1128
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 644 RKVFLSQGKLKCAGSSLFLKKKWGIGYHLSL--QLNEI------------------------CVEE------------NI 685
Cdd:TIGR01257 1129 RIAIISQGRLYCSGTPLFLKNCFGTGFYLTLvrKMKNIqsqrggcegtcsctskgfstrcpaRVDEitpeqvldgdvnEL 1208
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6005701 686 TSLVKQHIPDAKLSAKSEGKLIYTLPLE--RTNKFPELYKDL-DSYPDLGIENYGVSMTTLNEVFLKL 750
Cdd:TIGR01257 1209 MDLVYHHVPEAKLVECIGQELIFLLPNKnfKQRAYASLFRELeETLADLGLSSFGISDTPLEEIFLKV 1276
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
480-663 |
7.46e-63 |
|
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: 213.52 E-value: 7.46e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGKPDKieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIynNKLSEMADLENLSKL 559
Cdd:cd03263 1 LQIRNLTKTYKKGTKP--AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYI--NGYSIRTDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 560 TGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKE----------------------------------------IFL 599
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEvelllrvlgltdkankrartlsggmkrklslaialiggpsVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6005701 600 LDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGSSLFLK 663
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
993-1558 |
3.17e-60 |
|
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: 229.51 E-value: 3.17e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 993 SSCPPYIAMSSIDDYKNRARSQLRISGLSPSAYWFGQALVDVSLY-----FLVFVFIYLMSYISNFEDMLLTIIHIIQIp 1067
Cdd:TIGR01257 1691 SFVPASFVLYLIQERVNKAKHLQFISGVSPTTYWLTNFLWDIMNYavsagLVVGIFIGFQKKAYTSPENLPALVALLML- 1769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1068 cavgYSFSLIFMTYVISFIFRKGRKNSGIWSFCFYVVTVFSVA-GFAFSIFESD------------IPFIFTFLIPPATM 1134
Cdd:TIGR01257 1770 ----YGWAVIPMMYPASFLFDVPSTAYVALSCANLFIGINSSAiTFVLELFENNrtllrfnamlrkLLIVFPHFCLGRGL 1845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1135 IGCLFLSSHLLFSSLFSEERmDVQPFL-------VFLIPFLHFIIFLFTLRCLEWKFGKKSMRKDPFFRISPRSSDVCQn 1207
Cdd:TIGR01257 1846 IDLALSQAVTDVYAQFGEEH-SANPFQwdligknLVAMAVEGVVYFLLTLLIQHHFFLSRWIAEPAKEPIFDEDDDVAE- 1923
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1208 peepegededvqmERVRTANALNSTNfdekpVIIASCLRKEYAGKrkgcfskrkNKIATRNVSFCVRKGEVLGLLGHNGA 1287
Cdd:TIGR01257 1924 -------------ERQRIISGGNKTD-----ILRLNELTKVYSGT---------SSPAVDRLCVGVRPGECFGLLGVNGA 1976
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1288 GKSTSIKVITGDTKPTAGQVLLKG----SGGGDALEFLGYCPQENALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVD 1363
Cdd:TIGR01257 1977 GKTTTFKMLTGDTTVTSGDATVAGksilTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQ 2056
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1364 ALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNtERGALLTTHYMAEAEA 1443
Cdd:TIGR01257 2057 SLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEA 2135
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1444 VCDRVAIMVSGRLRCIGSIQHLKSKFGKDYLLEMKVKN-----LAQVEPLHAEILRLFPQAARQERYSSLMVYKLPVEDv 1518
Cdd:TIGR01257 2136 LCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMKIKSpkddlLPDLNPVEQFFQGNFPGSVQRERHYNMLQFQVSSSS- 2214
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 6005701 1519 qpLAQAFFKLEKVKQSFDLEEYSLSQSTLEQVFLELSKEQ 1558
Cdd:TIGR01257 2215 --LARIFQLLISHKDSLLIEEYSVTQTTLDQVFVNFAKQQ 2252
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1261-1489 |
3.36e-56 |
|
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: 195.46 E-value: 3.36e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1261 KNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGD----ALEFLGYCPQENALWPNLTV 1336
Cdd:COG4555 12 GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKepreARRQIGVLPDERGLYDRLTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1337 RQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQM 1416
Cdd:COG4555 92 RENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6005701 1417 WQAIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFGKDYLLEMKVKNLAQVEPLH 1489
Cdd:COG4555 172 REILRA-LKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEENLEDAFVALIGSEEGEA 243
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1258-1456 |
1.45e-55 |
|
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: 190.69 E-value: 1.45e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1258 SKR-KNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDALEFLGYCPQENALWP 1332
Cdd:cd03230 7 SKRyGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGkdikKEPEEVKRRIGYLPEEPSLYE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1333 NLTVRQHLEvyaavkglrkgdaevaitrlvdalklqdqlkspvktLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEG 1412
Cdd:cd03230 87 NLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPES 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 6005701 1413 QQQMWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1456
Cdd:cd03230 131 RREFWELLR-ELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1258-1559 |
5.67e-55 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 194.17 E-value: 5.67e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1258 SKR-KNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSG-GGDALEFLGYCPQENALWPNLT 1335
Cdd:COG4152 8 TKRfGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPlDPEDRRRIGYLPEERGLYPKMK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1336 VRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQ 1415
Cdd:COG4152 88 VGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVEL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1416 MWQAIRAtFRntERGA--LLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFGkdyllemkvKNLAQVEPLH-AEI 1492
Cdd:COG4152 168 LKDVIRE-LA--AKGTtvIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFG---------RNTLRLEADGdAGW 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6005701 1493 LRLFPQAARQERYSSLMVYKLP-VEDVQPLaqaffkLEKVKQSFDLEEYSLSQSTLEQVFLELSKEQE 1559
Cdd:COG4152 236 LRALPGVTVVEEDGDGAELKLEdGADAQEL------LRALLARGPVREFEEVRPSLNEIFIEVVGEKA 297
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
1259-1554 |
6.59e-54 |
|
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: 191.06 E-value: 6.59e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1259 KRKNKI-ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDALEFLGYCPQENALWPN 1333
Cdd:TIGR01188 1 KVYGDFkAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGydvvREPRKVRRSIGIVPQYASVDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1334 LTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQ 1413
Cdd:TIGR01188 81 LTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1414 QQMWQAIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFGKDYlLEMKVKNLAQVEPLHAEIL 1493
Cdd:TIGR01188 161 RAIWDYIRA-LKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGKDT-LESRPRDIQSLKVEVSMLI 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6005701 1494 RLFP--QAARQERYSSLMVYKLPVEDVQPLAQAFFKlEKVKQSFDLEEYSLSQSTLEQVFLEL 1554
Cdd:TIGR01188 239 AELGetGLGLLAVTVDSDRIKILVPDGDETVPEIVE-AAIRNGIRIRSISTERPSLDDVFLKL 300
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1240-1466 |
1.28e-50 |
|
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: 178.72 E-value: 1.28e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1240 IIASCLRKEYAGKRkgcfskrknkiATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGG 1315
Cdd:cd03265 1 IEVENLVKKYGDFE-----------AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvREPR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1316 DALEFLGYCPQENALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGN 1395
Cdd:cd03265 70 EVRRRIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6005701 1396 PSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLK 1466
Cdd:cd03265 150 PEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
480-658 |
2.65e-50 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 178.33 E-value: 2.65e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEmaDLENLSKL 559
Cdd:COG1131 1 IEVRGLTKRYGDKT----ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR--DPAEVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 560 TGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDK----------------------------------------EIFL 599
Cdd:COG1131 75 IGYVPQEPALYPDLTVRENLRFFARLYGLPRKEAREridellelfgltdaadrkvgtlsggmkqrlglalallhdpELLI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 600 LDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS 658
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRElAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGT 214
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
480-653 |
2.03e-47 |
|
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: 167.57 E-value: 2.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEmaDLENLSKL 559
Cdd:cd03230 1 IEVRNLSKRYGKKT----ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK--EPEEVKRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 560 TGVCPQSNVQFDFLTVRENLRL-------FAKIKGILpqeVDKEIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFS 631
Cdd:cd03230 75 IGYLPEEPSLYENLTVRENLKLsggmkqrLALAQALL---HDPELLILDEPTSGLDPESRREFWELLRElKKEGKTILLS 151
|
170 180
....*....|....*....|..
gi 6005701 632 TQFMDEADILADRKVFLSQGKL 653
Cdd:cd03230 152 SHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1257-1460 |
3.65e-47 |
|
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: 168.23 E-value: 3.65e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1257 FSKR-KNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDAL-EFLGYCPQENALWPNL 1334
Cdd:cd03269 6 VTKRfGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAArNRIGYLPEERGLYPKM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1335 TVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQ 1414
Cdd:cd03269 86 KVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6005701 1415 QMWQAIRATFRNtERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1460
Cdd:cd03269 166 LLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1258-1457 |
1.63e-45 |
|
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: 163.52 E-value: 1.63e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1258 SKR-KNKIATRNVSFCVRKGeVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG---SGGGDAL-EFLGYCPQENALWP 1332
Cdd:cd03264 7 TKRyGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqdvLKQPQKLrRRIGYLPQEFGVYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1333 NLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEg 1412
Cdd:cd03264 86 NFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPE- 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6005701 1413 qqqmwQAIRatFRN------TERGALLTTHYMAEAEAVCDRVAIMVSGRLR 1457
Cdd:cd03264 165 -----ERIR--FRNllselgEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1239-1518 |
2.84e-45 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 166.80 E-value: 2.84e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1239 VIIASCLRKEY---------AGKRKGCFSKRKNKI-ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVl 1308
Cdd:COG4586 1 IIEVENLSKTYrvyekepglKGALKGLFRREYREVeAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1309 lkgsgggdalEFLGYCP----------------QENALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLK 1372
Cdd:COG4586 80 ----------RVLGYVPfkrrkefarrigvvfgQRSQLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1373 SPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRAtfRNTERGA--LLTTHYMAEAEAVCDRVAI 1450
Cdd:COG4586 150 TPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKE--YNRERGTtiLLTSHDMDDIEALCDRVIV 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6005701 1451 MVSGRLRCIGSIQHLKSKFGKDYLLEMKVKNLAQVEPL--HAEILRLFPQAAR-----QERYSSLMVY---KLPVEDV 1518
Cdd:COG4586 228 IDHGRIIYDGSLEELKERFGPYKTIVLELAEPVPPLELprGGEVIEREGNRVRlevdpRESLAEVLARllaRYPVRDL 305
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1256-1457 |
4.07e-45 |
|
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: 162.39 E-value: 4.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1256 CFSKR-KNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGD---ALEFLGYCPQENALW 1331
Cdd:cd03268 5 DLTKTyGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKnieALRRIGALIEAPGFY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1332 PNLTVRQHLEVYAAVKGLRKGDAEvaitRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1411
Cdd:cd03268 85 PNLTARENLRLLARLLGIRKKRID----EVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6005701 1412 GQQQMWQAIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLR 1457
Cdd:cd03268 161 GIKELRELILS-LRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
480-658 |
4.54e-41 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 151.93 E-value: 4.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIyNNKLSEMADLENLSKL 559
Cdd:COG4555 2 IEVENLSKKYGKVP----ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILI-DGEDVRKEPREARRQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 560 tGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDK----------------------------------------EIFL 599
Cdd:COG4555 77 -GVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKrieeliellgleefldrrvgelstgmkkkvalaralvhdpKVLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 600 LDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS 658
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRAlKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGS 215
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1263-1555 |
1.35e-40 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 152.65 E-value: 1.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1263 KIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDALEFLGYCPQENALWPNLTVRQ 1338
Cdd:PRK13537 20 KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGepvpSRARHARQRVGVVPQFDNLDPDFTVRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1339 HLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQ 1418
Cdd:PRK13537 100 NLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1419 AIRATFrntERGA--LLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL-KSKFGKDyLLEMKVKNLAQVEPLhaeilrL 1495
Cdd:PRK13537 180 RLRSLL---ARGKtiLLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALiESEIGCD-VIEIYGPDPVALRDE------L 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6005701 1496 FPQAARQE-RYSSLMVYklpVEDVQPLAQAffklekVKQSFDLeEYSLSQSTLEQVFLELS 1555
Cdd:PRK13537 250 APLAERTEiSGETLFCY---VRDPEPLHAR------LKGRAGL-RYLHRPANLEDVFLRLT 300
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1259-1460 |
1.32e-39 |
|
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: 146.74 E-value: 1.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1259 KRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDALEFLGYCPQENALWPNL 1334
Cdd:cd03266 14 VKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvKEPAEARRRLGFVSDSTGLYDRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1335 TVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQ 1414
Cdd:cd03266 94 TARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATR 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6005701 1415 QMWQAIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1460
Cdd:cd03266 174 ALREFIRQ-LRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1267-1436 |
2.83e-39 |
|
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: 145.31 E-value: 2.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1267 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDALEF----LGYCPQENALWPNLTVRQHLEV 1342
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDyrrrLAYLGHADGLKPELTVRENLRF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1343 YAAVKGLRKGDAevAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRA 1422
Cdd:COG4133 99 WAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAA 176
|
170
....*....|....
gi 6005701 1423 tFRNTERGALLTTH 1436
Cdd:COG4133 177 -HLARGGAVLLTTH 189
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1268-1561 |
1.19e-38 |
|
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: 159.02 E-value: 1.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1268 NVSFcvRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDALEF----LGYCPQENALWPNLTVRQHLEVY 1343
Cdd:TIGR01257 950 NITF--YENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAvrqsLGMCPQHNILFHHLTVAEHILFY 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1344 AAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIrAT 1423
Cdd:TIGR01257 1028 AQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL-LK 1106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1424 FRnTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFGKDYLLEM--KVKNL------------------- 1482
Cdd:TIGR01257 1107 YR-SGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLvrKMKNIqsqrggcegtcsctskgfs 1185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1483 ----AQVEPLHAE-------------ILRLFPQAARQERYSSLMVYKLPVEDVQPLAQA--FFKLEKVKQSFDLEEYSLS 1543
Cdd:TIGR01257 1186 trcpARVDEITPEqvldgdvnelmdlVYHHVPEAKLVECIGQELIFLLPNKNFKQRAYAslFRELEETLADLGLSSFGIS 1265
|
330
....*....|....*...
gi 6005701 1544 QSTLEQVFLELSKEQELG 1561
Cdd:TIGR01257 1266 DTPLEEIFLKVTEDADSG 1283
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1262-1455 |
1.06e-36 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 142.66 E-value: 1.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1262 NKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDALEFLGYCPQENALWPNLTVR 1337
Cdd:PRK13536 53 DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGvpvpARARLARARIGVVPQFDNLDLEFTVR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1338 QHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMW 1417
Cdd:PRK13536 133 ENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIW 212
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 6005701 1418 QAIRATFrntERGA--LLTTHYMAEAEAVCDRVAIMVSGR 1455
Cdd:PRK13536 213 ERLRSLL---ARGKtiLLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1240-1456 |
1.62e-36 |
|
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: 138.62 E-value: 1.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1240 IIASCLRKEYAGKRKGCF----------SKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVll 1309
Cdd:cd03267 1 IEVSNLSKSYRVYSKEPGligslkslfkRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1310 kgsgggdalEFLGYCP----------------QENALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKS 1373
Cdd:cd03267 79 ---------RVAGLVPwkrrkkflrrigvvfgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1374 PVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVS 1453
Cdd:cd03267 150 PVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDK 229
|
...
gi 6005701 1454 GRL 1456
Cdd:cd03267 230 GRL 232
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
480-653 |
5.31e-36 |
|
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: 136.47 E-value: 5.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLEnLSKL 559
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKE-LAAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 560 ----TGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEV----------------------------------------DK 595
Cdd:cd03255 80 rrrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERreraeellervglgdrlnhypselsggqqqrvaiaralanDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 596 EIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADiLADRKVFLSQGKL 653
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1267-1406 |
1.46e-34 |
|
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: 129.69 E-value: 1.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1267 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-SGGGDALEFL----GYCPQENALWPNLTVRQHLE 1341
Cdd:pfam00005 2 KNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGqDLTDDERKSLrkeiGYVFQDPQLFPRLTVRENLR 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6005701 1342 VYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPV----KTLSEGIKRKLCFVLSILGNPSVVLLDEPST 1406
Cdd:pfam00005 82 LGLLLKGLSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1265-1455 |
3.85e-34 |
|
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: 131.40 E-value: 3.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1265 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-------------SGggdalefLGYCPQENALW 1331
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGrditglppherarAG-------IGYVPEGRRIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1332 PNLTVRQHLEVYAAVKGLRKGDAEVAitRLVDAL-KLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDP 1410
Cdd:cd03224 88 PELTVEENLLLGAYARRRAKRKARLE--RVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 6005701 1411 EGQQQMWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1455
Cdd:cd03224 166 KIVEEIFEAIR-ELRDEGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
480-652 |
1.29e-33 |
|
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: 127.88 E-value: 1.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGKPDKIeaLKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMaDLENLSKL 559
Cdd:cd03228 1 IEFKNVSFSYPGRPKPV--LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDL-DLESLRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 560 TGVCPQSNVQFDFlTVRENL------------RLFAKikgilpqevDKEIFLLDEPTAGLDPFSRHQVWNLLKERKTDRV 627
Cdd:cd03228 78 IAYVPQDPFLFSG-TIRENIlsggqrqriaiaRALLR---------DPPILILDEATSALDPETEALILEALRALAKGKT 147
|
170 180
....*....|....*....|....*
gi 6005701 628 ILFSTQFMDEADiLADRKVFLSQGK 652
Cdd:cd03228 148 VIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1265-1456 |
2.77e-33 |
|
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: 129.09 E-value: 2.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1265 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-----------SGGGDALEFlgycpQENALWPN 1333
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGeditglppheiARLGIGRTF-----QIPRLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1334 LTVRQHLEV--------YAAVKGLRKGDAEV--AITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDE 1403
Cdd:cd03219 90 LTVLENVMVaaqartgsGLLLARARREEREAreRAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6005701 1404 PSTGMDPEGQQQMWQAIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1456
Cdd:cd03219 170 PAAGLNPEETEELAELIRE-LRERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
480-658 |
6.05e-33 |
|
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: 128.22 E-value: 6.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYkgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEmADLENLSKL 559
Cdd:COG1122 1 IELENLSFSY---PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITK-KNLRELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 560 TGVCPQ-SNVQFDFLTVRENLrLFA-KIKGILPQEVDK----------------------------------------EI 597
Cdd:COG1122 77 VGLVFQnPDDQLFAPTVEEDV-AFGpENLGLPREEIRErveealelvglehladrpphelsggqkqrvaiagvlamepEV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6005701 598 FLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS 658
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGT 217
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
481-652 |
7.34e-33 |
|
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: 125.05 E-value: 7.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 481 RIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMaDLENLSKLT 560
Cdd:cd00267 1 EIENLSFRYGGRT----ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKL-PLEELRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 561 GVCPQsnvqfdfLTVRENLRL-FAKIKGILPqevdkEIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEA 638
Cdd:cd00267 76 GYVPQ-------LSGGQRQRVaLARALLLNP-----DLLLLDEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELA 143
|
170
....*....|....
gi 6005701 639 DILADRKVFLSQGK 652
Cdd:cd00267 144 ELAADRVIVLKDGK 157
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1259-1455 |
1.47e-32 |
|
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: 126.43 E-value: 1.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1259 KRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-----SGGGDALEFLGYCPQEnalwP- 1332
Cdd:cd03225 10 PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGkdltkLSLKELRRKVGLVFQN----Pd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1333 ----NLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCfVLSIL-GNPSVVLLDEPSTG 1407
Cdd:cd03225 86 dqffGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVA-IAGVLaMDPDILLLDEPTAG 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 6005701 1408 MDPEGQQQMWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1455
Cdd:cd03225 165 LDPAGRRELLELLK-KLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
480-649 |
5.77e-32 |
|
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: 124.89 E-value: 5.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEmadlenLSKL 559
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG------PGPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 560 TGVCPQSNVQFDFLTVRENLRLFAKIKGILPQE----------------------------------------VDKEIFL 599
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALGLELQGVPKAEareraeellelvglsgfenayphqlsggmrqrvalaralaVDPDVLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6005701 600 LDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLS 649
Cdd:cd03293 155 LDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDEAVFLADRVVVLS 206
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1257-1460 |
6.89e-32 |
|
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: 124.55 E-value: 6.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1257 FSKR-KNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG---SGGGDALEFLGYCPQENALWP 1332
Cdd:cd03259 6 LSKTyGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGrdvTGVPPERRNIGMVFQDYALFP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1333 NLTVRQHLeVYA-AVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1411
Cdd:cd03259 86 HLTVAENI-AFGlKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6005701 1412 GQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1460
Cdd:cd03259 165 LREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
479-651 |
1.06e-31 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 125.59 E-value: 1.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 479 AIRIRNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEmadlenLSK 558
Cdd:COG1116 7 ALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG------PGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 559 LTGVCPQSNVQFDFLTVRENLRLFAKIKGILPQE----------------------------------------VDKEIF 598
Cdd:COG1116 81 DRGVVFQEPALLPWLTVLDNVALGLELRGVPKAErrerarellelvglagfedayphqlsggmrqrvaiaralaNDPEVL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6005701 599 LLDEPTAGLDPFSRHQVWNLL-----KERKTdrvILFSTQFMDEADILADRKVFLSQG 651
Cdd:COG1116 161 LMDEPFGALDALTRERLQDELlrlwqETGKT---VLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1267-1476 |
2.06e-31 |
|
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: 123.60 E-value: 2.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1267 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-----SGGGDALEFLGYCPQ--ENALWpNLTVRQh 1339
Cdd:COG1122 18 DDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGkditkKNLRELRRKVGLVFQnpDDQLF-APTVEE- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1340 lEV-YAAV-KGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCF--VLSIlgNPSVVLLDEPSTGMDPEGQQQ 1415
Cdd:COG1122 96 -DVaFGPEnLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIagVLAM--EPEVLVLDEPTAGLDPRGRRE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6005701 1416 MWQAIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLkskFGKDYLLE 1476
Cdd:COG1122 173 LLELLKR-LNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV---FSDYELLE 229
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
494-752 |
2.09e-31 |
|
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: 125.97 E-value: 2.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 494 DKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLenLSKLTGVCPQSNVQFDFL 573
Cdd:TIGR01188 4 GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRK--VRRSIGIVPQYASVDEDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 574 TVRENLRLFAKIKGILPQEVDK----------------------------------------EIFLLDEPTAGLDPFSRH 613
Cdd:TIGR01188 82 TGRENLEMMGRLYGLPKDEAEEraeellelfelgeaadrpvgtysggmrrrldiaaslihqpDVLFLDEPTTGLDPRTRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 614 QVWNLLKERKTDRV-ILFSTQFMDEADILADRKVFLSQGKLKCAGSSLFLKKKWGiGYHLSLQLNEICVEENITSLVKQH 692
Cdd:TIGR01188 162 AIWDYIRALKEEGVtILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLG-KDTLESRPRDIQSLKVEVSMLIAE 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6005701 693 IPDAKLSAK-----SEGKLIYTLPLERTnkFPELYKDLDSYpdlGIENYGVSMT--TLNEVFLKLEG 752
Cdd:TIGR01188 241 LGETGLGLLavtvdSDRIKILVPDGDET--VPEIVEAAIRN---GIRIRSISTErpSLDDVFLKLTG 302
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1265-1456 |
2.40e-31 |
|
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: 124.38 E-value: 2.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1265 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-----------SGGGDALEFlgycpQENALWPN 1333
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGrditglpphriARLGIARTF-----QNPRLFPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1334 LTVRQHLEV----------YAAVKGLRKGDAEVAITR-----LVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSV 1398
Cdd:COG0411 94 LTVLENVLVaaharlgrglLAALLRLPRARREEREAReraeeLLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1399 VLLDEPSTGMDPEGQQQMWQAIRATfrNTERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1456
Cdd:COG0411 174 LLLDEPAAGLNPEETEELAELIRRL--RDERGItiLLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1258-1461 |
1.47e-30 |
|
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: 121.11 E-value: 1.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1258 SKR-KNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsGGGD---------ALEFLGYCPQE 1327
Cdd:cd03218 7 SKRyGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILL---DGQDitklpmhkrARLGIGYLPQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1328 NALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTG 1407
Cdd:cd03218 84 ASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAG 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 6005701 1408 MDPEGQQQMwQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1461
Cdd:cd03218 164 VDPIAVQDI-QKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGT 216
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1262-1464 |
1.47e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 121.73 E-value: 1.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1262 NKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDALEFLGYCPQENAL-W--PnLTVRq 1338
Cdd:COG1121 18 GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIGYVPQRAEVdWdfP-ITVR- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1339 hlEV-----YAAV---KGLRKGDAEvAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDP 1410
Cdd:COG1121 96 --DVvlmgrYGRRglfRRPSRADRE-AVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 6005701 1411 EGQQQMWQAIRAtFRNTERGALLTTHYMAEAEAVCDRVaIMVSGRLRCIGSIQH 1464
Cdd:COG1121 173 ATEEALYELLRE-LRREGKTILVVTHDLGAVREYFDRV-LLLNRGLVAHGPPEE 224
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
480-653 |
2.26e-30 |
|
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: 120.01 E-value: 2.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIynnKLSEMADLENLSKL 559
Cdd:cd03268 1 LKTNDLTKTYGKKR----VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITF---DGKSYQKNIEALRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 560 TGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDK------------------------------------EIFLLDEP 603
Cdd:cd03268 74 IGALIEAPGFYPNLTARENLRLLARLLGIRKKRIDEvldvvglkdsakkkvkgfslgmkqrlgialallgnpDLLILDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6005701 604 TAGLDPFSRHQVWNLL-KERKTDRVILFSTQFMDEADILADRKVFLSQGKL 653
Cdd:cd03268 154 TNGLDPDGIKELRELIlSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1259-1455 |
2.44e-30 |
|
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: 118.12 E-value: 2.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1259 KRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGD-----ALEFLGYCPQenalwpn 1333
Cdd:cd00267 8 RYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKlpleeLRRRIGYVPQ------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1334 ltvrqhlevyaavkglrkgdaevaitrlvdalklqdqlkspvktLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQ 1413
Cdd:cd00267 81 --------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASR 116
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 6005701 1414 QQMWQAIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1455
Cdd:cd00267 117 ERLLELLRE-LAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
480-652 |
2.74e-30 |
|
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: 118.44 E-value: 2.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMAD-LENLSK 558
Cdd:cd03229 1 LELKNVSKRYGQKT----VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDeLPPLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 559 LTGVCPQSNVQFDFLTVRENLRLfaKIKGILPQEV--------DKEIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVI 628
Cdd:cd03229 77 RIGMVFQDFALFPHLTVLENIAL--GLSGGQQQRValaralamDPDVLLLDEPTSALDPITRREVRALLKSlqAQLGITV 154
|
170 180
....*....|....*....|....
gi 6005701 629 LFSTQFMDEADILADRKVFLSQGK 652
Cdd:cd03229 155 VLVTHDLDEAARLADRVVVLRDGK 178
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
477-653 |
3.45e-30 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 120.15 E-value: 3.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 477 KEAIRIRNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADlENL 556
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSE-REL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 557 SKL----TGVCPQS-NVqFDFLTVRENLRLFAKIKGILPQEVDK------------------------------------ 595
Cdd:COG1136 81 ARLrrrhIGFVFQFfNL-LPELTALENVALPLLLAGVSRKERRErarellervglgdrldhrpsqlsggqqqrvaiaral 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6005701 596 ----EIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADIlADRKVFLSQGKL 653
Cdd:COG1136 160 vnrpKLILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTHDPELAAR-ADRVIRLRDGRI 222
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
480-654 |
4.04e-30 |
|
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: 119.22 E-value: 4.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGKpdkiEALKDLVFDIYEGqITAILGHSGAGKSTLLNILSGLSVPTKGSVTIynNKLSEMADLENLSKL 559
Cdd:cd03264 1 LQLENLTKRYGKK----RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRI--DGQDVLKQPQKLRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 560 TGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKE----------------------------------------IFL 599
Cdd:cd03264 74 IGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARvdevlelvnlgdrakkkigslsggmrrrvgiaqalvgdpsILI 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6005701 600 LDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEADILADRKVFLSQGKLK 654
Cdd:cd03264 154 VDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
480-653 |
5.91e-30 |
|
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: 119.53 E-value: 5.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEM--ADLENLS 557
Cdd:cd03261 1 IELRGLTKSFGGRT----VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLseAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 558 KLTGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEV-----------------------------------------DKE 596
Cdd:cd03261 77 RRMGMLFQSGALFDSLTVFENVAFPLREHTRLSEEEireivlekleavglrgaedlypaelsggmkkrvalaralalDPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 597 IFLLDEPTAGLDPFSRHQVWNL---LKERKTDRVILFSTQfMDEADILADRKVFLSQGKL 653
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLirsLKKELGLTSIMVTHD-LDTAFAIADRIAVLYDGKI 215
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
480-663 |
9.31e-30 |
|
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: 118.63 E-value: 9.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYkgkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIynNKLSEMADLENLSKL 559
Cdd:cd03265 1 IEVENLVKKY----GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATV--AGHDVVREPREVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 560 TGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDK----------------------------------------EIFL 599
Cdd:cd03265 75 IGIVFQDLSVDDELTGWENLYIHARLYGVPGAERREridelldfvglleaadrlvktysggmrrrleiarslvhrpEVLF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6005701 600 LDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGSSLFLK 663
Cdd:cd03265 155 LDEPTIGLDPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1259-1460 |
1.33e-29 |
|
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: 118.40 E-value: 1.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1259 KRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVllKGSGGGDALEFLGYcpqenALWPNLTVRQ 1338
Cdd:cd03220 31 EVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV--TVRGRVSSLLGLGG-----GFNPELTGRE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1339 HLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEP-STGmDPEGQQQMW 1417
Cdd:cd03220 104 NIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVlAVG-DAAFQEKCQ 182
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 6005701 1418 QAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1460
Cdd:cd03220 183 RRLR-ELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1266-1460 |
2.16e-29 |
|
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: 117.40 E-value: 2.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1266 TRNVSFCVrKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDALEFL---------GYCPQENALWPNLTV 1336
Cdd:cd03297 14 TLKIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKInlppqqrkiGLVFQQYALFPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1337 RQHLEVyaAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQM 1416
Cdd:cd03297 93 RENLAF--GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 6005701 1417 WQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1460
Cdd:cd03297 171 LPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1267-1455 |
3.11e-29 |
|
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: 117.39 E-value: 3.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1267 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-------------SGggdalefLGYCPQENALWPN 1333
Cdd:COG0410 20 HGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGeditglpphriarLG-------IGYVPEGRRIFPS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1334 LTVRQHLEVYAAVKGLRKGDAEvaitRL--VDAL--KLQDQLKSPVKTLSEG------IKRKLcfvlsiLGNPSVVLLDE 1403
Cdd:COG0410 93 LTVEENLLLGAYARRDRAEVRA----DLerVYELfpRLKERRRQRAGTLSGGeqqmlaIGRAL------MSRPKLLLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6005701 1404 PSTGMDPEGQQQMWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1455
Cdd:COG0410 163 PSLGLAPLIVEEIFEIIR-RLNREGVTILLVEQNARFALEIADRAYVLERGR 213
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1262-1460 |
4.31e-29 |
|
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: 116.48 E-value: 4.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1262 NKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDALEFLGYCPQ-ENALW--PnLTVRQ 1338
Cdd:cd03235 11 GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGYVPQrRSIDRdfP-ISVRD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1339 --------HLEVYAAVKGLRKGDAEVAITRlVDALKLQDQlksPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDP 1410
Cdd:cd03235 90 vvlmglygHKGLFRRLSKADKAKVDEALER-VGLSELADR---QIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6005701 1411 EGQQQMWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVaIMVSGRLRCIG 1460
Cdd:cd03235 166 KTQEDIYELLR-ELRREGMTILVVTHDLGLVLEYFDRV-LLLNRTVVASG 213
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
483-653 |
4.45e-29 |
|
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: 115.73 E-value: 4.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 483 RNVTKEYKGKPDKIEA--LKDLVFDIYEGQITAILGHSGAGKSTLLNILSGL--SVPTKGSVTIyNNKlseMADLENLSK 558
Cdd:cd03213 7 RNLTVTVKSSPSKSGKqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLI-NGR---PLDKRSFRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 559 LTGVCPQSNVQFDFLTVRENLRLFAKIKGI---------LPQEVDKE--IFLLDEPTAGLDPFSRHQVWNLLKE-RKTDR 626
Cdd:cd03213 83 IIGYVPQDDILHPTLTVRETLMFAAKLRGLsggerkrvsIALELVSNpsLLFLDEPTSGLDSSSALQVMSLLRRlADTGR 162
|
170 180
....*....|....*....|....*...
gi 6005701 627 VILFST-QFMDEADILADRKVFLSQGKL 653
Cdd:cd03213 163 TIICSIhQPSSEIFELFDKLLLLSQGRV 190
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1247-1462 |
4.47e-29 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 117.49 E-value: 4.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1247 KEYAGKRKGcfSKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGS-------GGGdale 1319
Cdd:COG1134 25 KELLLRRRR--TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRvsallelGAG---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1320 FLgycpqenalwPNLTVRQHLEVYAAVKGLRKGDaevaITRLVDALK----LQDQLKSPVKTLSEGIKRKLCFVLSILGN 1395
Cdd:COG1134 99 FH----------PELTGRENIYLNGRLLGLSRKE----IDEKFDEIVefaeLGDFIDQPVKTYSSGMRARLAFAVATAVD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6005701 1396 PSVVLLDEP-STGmDPEGQQQMWQAIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSI 1462
Cdd:COG1134 165 PDILLVDEVlAVG-DAAFQKKCLARIRE-LRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDP 230
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1267-1461 |
1.50e-28 |
|
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: 116.30 E-value: 1.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1267 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsgGGDALE---------FLGYCPQENALWPNLTVR 1337
Cdd:COG1120 18 DDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLL----DGRDLAslsrrelarRIAYVPQEPPAPFGLTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1338 Q--------HLevyAAVKGLRKGDAEVAIT--RLVDALKLQDQlksPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTG 1407
Cdd:COG1120 94 ElvalgrypHL---GLFGRPSAEDREAVEEalERTGLEHLADR---PVDELSGGERQRVLIARALAQEPPLLLLDEPTSH 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 6005701 1408 MDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1461
Cdd:COG1120 168 LDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
481-652 |
2.35e-28 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 114.10 E-value: 2.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 481 RIRNVTKEYKGKpdKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMaDLENLSKLT 560
Cdd:cd03225 1 ELKNLSFSYPDG--ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKL-SLKELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 561 GVCPQ-SNVQFDFLTVRENLrLFA-KIKGILPQEVDK----------------------------------------EIF 598
Cdd:cd03225 78 GLVFQnPDDQFFGPTVEEEV-AFGlENLGLPEEEIEErveealelvgleglrdrspftlsggqkqrvaiagvlamdpDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6005701 599 LLDEPTAGLDPFSRHQVWNLLKERKTDRV-ILFSTQFMDEADILADRKVFLSQGK 652
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAEGKtIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1238-1461 |
1.44e-27 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 112.82 E-value: 1.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1238 PVIIASCLRKEYaGKRKgcfskrknkiATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSgggD- 1316
Cdd:COG1137 2 MTLEAENLVKSY-GKRT----------VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGE---Di 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1317 --------ALEFLGYCPQENALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCF 1388
Cdd:COG1137 68 thlpmhkrARLGIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6005701 1389 VLSILGNPSVVLLDEPSTGMDP---EGQQQMwqaIRatfRNTERGA--LLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1461
Cdd:COG1137 148 ARALATNPKFILLDEPFAGVDPiavADIQKI---IR---HLKERGIgvLITDHNVRETLGICDRAYIISEGKVLAEGT 219
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
453-672 |
2.41e-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: 119.10 E-value: 2.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 453 LEDEMDADPSfhDSFEQAPPEFQGKEAIRIRNVTKEYKGKPDkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGL 532
Cdd:COG4987 309 LNELLDAPPA--VTEPAEPAPAPGGPSLELEDVSFRYPGAGR--PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRF 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 533 SVPTKGSVTIYNNKLSEMaDLENLSKLTGVCPQSNVQFDfLTVRENLRLfAK--------------------IKGiLPQE 592
Cdd:COG4987 385 LDPQSGSITLGGVDLRDL-DEDDLRRRIAVVPQRPHLFD-TTLRENLRL-ARpdatdeelwaalervglgdwLAA-LPDG 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 593 VD---------------------------KEIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEADiLADRK 645
Cdd:COG4987 461 LDtwlgeggrrlsggerrrlalarallrdAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLE-RMDRI 539
|
250 260
....*....|....*....|....*..
gi 6005701 646 VFLSQGKLKCAGSSLFLKKKWGIGYHL 672
Cdd:COG4987 540 LVLEDGRIVEQGTHEELLAQNGRYRQL 566
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1257-1455 |
2.93e-27 |
|
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: 109.97 E-value: 2.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1257 FSKR-KNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDALEF---LGYCPQEN 1328
Cdd:cd03229 6 VSKRyGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedltDLEDELPPLrrrIGMVFQDF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1329 ALWPNLTVRQHLeVYAavkglrkgdaevaitrlvdalklqdqlkspvktLSEGIKRKLCFVLSILGNPSVVLLDEPSTGM 1408
Cdd:cd03229 86 ALFPHLTVLENI-ALG---------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSAL 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 6005701 1409 DPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1455
Cdd:cd03229 132 DPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
480-657 |
3.23e-27 |
|
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: 111.31 E-value: 3.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEmADLENLSKL 559
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 560 tGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEV----------------------------------------DKEIFL 599
Cdd:cd03266 81 -GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELtarleeladrlgmeelldrrvggfstgmrqkvaiaralvhDPPVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6005701 600 LDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAG 657
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRQlRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
479-658 |
5.11e-27 |
|
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: 111.22 E-value: 5.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 479 AIRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEM--ADLENL 556
Cdd:COG1127 5 MIEVRNLTKSFGDRV----VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLseKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 557 SKLTGVCPQSNVQFDFLTVREN----LRLF-----AKIKGI---------LPQEVDK----------------------- 595
Cdd:COG1127 81 RRRIGMLFQGGALFDSLTVFENvafpLREHtdlseAEIRELvleklelvgLPGAADKmpselsggmrkrvalaralaldp 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6005701 596 EIFLLDEPTAGLDPFSRHQVWNLLKERKTDR---VILFSTQfMDEADILADRKVFLSQGKLKCAGS 658
Cdd:COG1127 161 EILLYDEPTAGLDPITSAVIDELIRELRDELgltSVVVTHD-LDSAFAIADRVAVLADGKIIAEGT 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1265-1465 |
6.18e-27 |
|
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: 117.31 E-value: 6.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1265 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTA---GQVLLKGSGGGDALEFL-----GYCPQE--NALWPnL 1334
Cdd:COG1123 21 AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALrgrriGMVFQDpmTQLNP-V 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1335 TVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQ 1414
Cdd:COG1123 100 TVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6005701 1415 QMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL 1465
Cdd:COG1123 180 EILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1240-1455 |
9.99e-27 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 109.87 E-value: 9.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1240 IIASCLRKEYAGKRKGcfskrknKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG---SGGGD 1316
Cdd:cd03293 1 LEVRNVSKTYGGGGGA-------VTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGepvTGPGP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1317 AlefLGYCPQENALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNP 1396
Cdd:cd03293 74 D---RGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDP 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6005701 1397 SVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMvSGR 1455
Cdd:cd03293 151 DVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL-SAR 208
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
480-653 |
1.57e-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: 109.58 E-value: 1.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYkgkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGL-----SVPTKGSVTIYN-NKLSEMADL 553
Cdd:cd03260 1 IELRDLNVYY----GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGkDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 554 ENLSKLTGVCPQSNVQFDfLTVRENLRLFAKIKGI------------------LPQEVDK-------------------- 595
Cdd:cd03260 77 LELRRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIklkeelderveealrkaaLWDEVKDrlhalglsggqqqrlclara 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6005701 596 -----EIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEADILADRKVFLSQGKL 653
Cdd:cd03260 156 lanepEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
481-657 |
5.17e-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: 106.37 E-value: 5.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 481 RIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLEnLSKLT 560
Cdd:cd03214 1 EVENLSVGYGGRT----VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKE-LARKI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 561 GVCPQSNVQFDFLTVREnlRLFAKIKG----------ILPQEVDkeIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVI 628
Cdd:cd03214 76 AYVPQALELLGLAHLAD--RPFNELSGgerqrvllarALAQEPP--ILLLDEPTSHLDIAHQIELLELLRRlaRERGKTV 151
|
170 180
....*....|....*....|....*....
gi 6005701 629 LFSTQFMDEADILADRKVFLSQGKLKCAG 657
Cdd:cd03214 152 VMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1258-1461 |
6.61e-26 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 110.96 E-value: 6.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1258 SKR-KNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsgGGDALEFL-------GYCPQENA 1329
Cdd:COG3842 12 SKRyGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILL----DGRDVTGLppekrnvGMVFQDYA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1330 LWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEG------IKRKLCFvlsilgNPSVVLLDE 1403
Cdd:COG3842 88 LFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGqqqrvaLARALAP------EPRVLLLDE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6005701 1404 PSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1461
Cdd:COG3842 162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGT 219
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
479-658 |
7.52e-26 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 108.21 E-value: 7.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 479 AIRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLEnLSK 558
Cdd:COG1120 1 MLEAENLSVGYGGRP----VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRE-LAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 559 LTGVCPQSNVQFDFLTVRE--------NLRLFAKikgilPQEVDKE---------------------------------- 596
Cdd:COG1120 76 RIAYVPQEPPAPFGLTVRElvalgrypHLGLFGR-----PSAEDREaveealertglehladrpvdelsggerqrvliar 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6005701 597 -------IFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS 658
Cdd:COG1120 151 alaqeppLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1257-1456 |
1.18e-25 |
|
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: 106.82 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1257 FSKRKNKI-ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG---SGGGDALEFL-----GYCPQE 1327
Cdd:cd03257 11 FPTGGGSVkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdlLKLSRRLRKIrrkeiQMVFQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1328 --NALWPNLTVRQHLEvyAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKT-----LSEGIKRKLCFVLSILGNPSVVL 1400
Cdd:cd03257 91 pmSSLNPRMTIGEQIA--EPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNrypheLSGGQRQRVAIARALALNPKLLI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1401 LDEPSTGMDPEGQQQmwqaIRATFRN--TERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1456
Cdd:cd03257 169 ADEPTSALDVSVQAQ----ILDLLKKlqEELGLtlLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
469-658 |
1.40e-25 |
|
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: 113.70 E-value: 1.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 469 QAPPEFQGKEAIRIRNVTKEYkgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLS 548
Cdd:COG4988 326 TAPLPAAGPPSIELEDVSFSY---PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLS 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 549 EMaDLENLSKLTGVCPQSNVQFDfLTVRENLRLF------------AKIKGI------LPQ----EV------------- 593
Cdd:COG4988 403 DL-DPASWRRQIAWVPQNPYLFA-GTIRENLRLGrpdasdeeleaaLEAAGLdefvaaLPDgldtPLgeggrglsggqaq 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6005701 594 ----------DKEIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQfmDEADI-LADRKVFLSQGKLKCAGS 658
Cdd:COG4988 481 rlalarallrDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITH--RLALLaQADRILVLDDGRIVEQGT 554
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
480-653 |
1.53e-25 |
|
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: 106.90 E-value: 1.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEM--ADLENLS 557
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLsgKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 558 KLTGVCPQsnvQFDFL---TVRENLRLFAKIKGILPQEVDK--------------------------------------- 595
Cdd:cd03258 82 RRIGMIFQ---HFNLLssrTVFENVALPLEIAGVPKAEIEErvlellelvgledkadaypaqlsggqkqrvgiaralann 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6005701 596 -EIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKL 653
Cdd:cd03258 159 pKVLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1245-1456 |
1.87e-25 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 106.03 E-value: 1.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1245 LRKEYAGKRKgcfskrkNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG---SGGGDA---- 1317
Cdd:cd03255 6 LSKTYGGGGE-------KVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGtdiSKLSEKelaa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1318 --LEFLGYCPQENALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEG------IKRklcfv 1389
Cdd:cd03255 79 frRRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGqqqrvaIAR----- 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6005701 1390 lSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAvCDRVAIMVSGRL 1456
Cdd:cd03255 154 -ALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1235-1465 |
4.79e-25 |
|
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: 111.15 E-value: 4.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1235 DEKPVIIASCLRKEYAGKRKGCFskrknkIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG--- 1311
Cdd:COG1123 256 AAEPLLEVRNLSKRYPVRGKGGV------RAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGkdl 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1312 --SGGGDALEF---LGYCPQ--ENALWPNLTVRQHL-EVYAAVKGLRKGDAEVAITRLVDALKLQDQL--KSPvKTLSEG 1381
Cdd:COG1123 330 tkLSRRSLRELrrrVQMVFQdpYSSLNPRMTVGDIIaEPLRLHGLLSRAERRERVAELLERVGLPPDLadRYP-HELSGG 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1382 IKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1461
Cdd:COG1123 409 QRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGP 488
|
....
gi 6005701 1462 IQHL 1465
Cdd:COG1123 489 TEEV 492
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1235-1474 |
6.21e-25 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 112.91 E-value: 6.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1235 DEKPVIIASCLRKeyagkRKGCFskrknkIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG--- 1311
Cdd:NF033858 262 DDEPAIEARGLTM-----RFGDF------TAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGqpv 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1312 -SGGGDALEFLGYCPQENALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVL 1390
Cdd:NF033858 331 dAGDIATRRRVGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAV 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1391 SILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAvCDRVAIMVSGRLRCIGSIQHLKSKFG 1470
Cdd:NF033858 411 AVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAER-CDRISLMHAGRVLASDTPAALVAARG 489
|
....
gi 6005701 1471 KDYL 1474
Cdd:NF033858 490 AATL 493
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
449-672 |
8.38e-25 |
|
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: 112.23 E-value: 8.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 449 DHVALEDEMDADPSFhdsfeQAPPEFQGkeAIRIRNVTKEYKgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNI 528
Cdd:COG2274 450 DILDLPPEREEGRSK-----LSLPRLKG--DIELENVSFRYP--GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKL 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 529 LSGLSVPTKGSVTIYNNKLSEMaDLENLSKLTGVCPQSNVQFdFLTVRENLRLF------------AKIKGI------LP 590
Cdd:COG2274 521 LLGLYEPTSGRILIDGIDLRQI-DPASLRRQIGVVLQDVFLF-SGTIRENITLGdpdatdeeiieaARLAGLhdfieaLP 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 591 Q----EV-----------------------DKEIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQfmDEADI-LA 642
Cdd:COG2274 599 MgydtVVgeggsnlsggqrqrlaiarallrNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAH--RLSTIrLA 676
|
250 260 270
....*....|....*....|....*....|
gi 6005701 643 DRKVFLSQGKLKCAGSSLFLKKKWGIGYHL 672
Cdd:COG2274 677 DRIIVLDKGRIVEDGTHEELLARKGLYAEL 706
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
229-755 |
1.23e-24 |
|
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: 112.80 E-value: 1.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 229 CII---SF--SSFIYYasvnVTRER-KRMKALMTMMGLRDSAFWLS---WGLLyaGFIFIMALFLALVI--RSTQFIILS 297
Cdd:TIGR01257 1685 CVIfamSFvpASFVLY----LIQERvNKAKHLQFISGVSPTTYWLTnflWDIM--NYAVSAGLVVGIFIgfQKKAYTSPE 1758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 298 GFMVVFSLFLLYGLSLVALAFLMSILVK-----------KSFLTGL----VVFLLTVFWG---CLGFTSLYRHLpaslew 359
Cdd:TIGR01257 1759 NLPALVALLMLYGWAVIPMMYPASFLFDvpstayvalscANLFIGInssaITFVLELFENnrtLLRFNAMLRKL------ 1832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 360 iLSLLSPFAFMLGMAQLL----------HLDYDLNSNAFPHPSDGSNLivatnFMLAFDTCLYLALAIYFEKilpneygh 429
Cdd:TIGR01257 1833 -LIVFPHFCLGRGLIDLAlsqavtdvyaQFGEEHSANPFQWDLIGKNL-----VAMAVEGVVYFLLTLLIQH-------- 1898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 430 rrppLFFLkssfwsqTQKTDHVALEDEMDADPSFHDSFEQAPPEFQGKEAIRIRNVTKEYKGKPDKieALKDLVFDIYEG 509
Cdd:TIGR01257 1899 ----HFFL-------SRWIAEPAKEPIFDEDDDVAEERQRIISGGNKTDILRLNELTKVYSGTSSP--AVDRLCVGVRPG 1965
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 510 QITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLseMADLENLSKLTGVCPQSNVQFDFLTVRENLRLFAKIKGIL 589
Cdd:TIGR01257 1966 ECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI--LTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVP 2043
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 590 PQEVDK----------------------------------------EIFLLDEPTAGLDPFSRHQVWN-LLKERKTDRVI 628
Cdd:TIGR01257 2044 AEEIEKvanwsiqslglslyadrlagtysggnkrklstaialigcpPLVLLDEPTTGMDPQARRMLWNtIVSIIREGRAV 2123
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 629 LFSTQFMDEADILADRKVFLSQGKLKCAGSSLFLKKKWGIGYHLSLQL----NEICVEEN-ITSLVKQHIPDAKLSAKSE 703
Cdd:TIGR01257 2124 VLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMKIkspkDDLLPDLNpVEQFFQGNFPGSVQRERHY 2203
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 6005701 704 GKLIYTLPlerTNKFPELYKDLDSYPD-LGIENYGVSMTTLNEVFLKLEGKST 755
Cdd:TIGR01257 2204 NMLQFQVS---SSSLARIFQLLISHKDsLLIEEYSVTQTTLDQVFVNFAKQQT 2253
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1265-1456 |
1.55e-24 |
|
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: 101.74 E-value: 1.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1265 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSgggdaleflgycpqenalwpnltvrqhlevya 1344
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK-------------------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1345 avkglrkgdaEVAITRLVDALKL------QdqlkspvktLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQ 1418
Cdd:cd03216 63 ----------EVSFASPRDARRAgiamvyQ---------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFK 123
|
170 180 190
....*....|....*....|....*....|....*...
gi 6005701 1419 AIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1456
Cdd:cd03216 124 VIRR-LRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
480-674 |
1.57e-24 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 105.23 E-value: 1.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEY-KGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTI--YNNKLSEMADLENL 556
Cdd:TIGR04521 1 IKLKNVSYIYqPGTPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIdgRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 557 SKLTGVcpqsnVqFDF-------LTVRE-------NL---------RLFAKIKGI-LPQEV------------------- 593
Cdd:TIGR04521 81 RKKVGL-----V-FQFpehqlfeETVYKdiafgpkNLglseeeaeeRVKEALELVgLDEEYlerspfelsggqmrrvaia 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 594 -----DKEIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGSS--LFLKK 664
Cdd:TIGR04521 155 gvlamEPEVLILDEPTAGLDPKGRKEILDLFKRlhKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPreVFSDV 234
|
250
....*....|
gi 6005701 665 KWGIGYHLSL 674
Cdd:TIGR04521 235 DELEKIGLDV 244
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
480-652 |
1.82e-24 |
|
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: 102.94 E-value: 1.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTiYNNKLSEMADLENLSKL 559
Cdd:COG4133 3 LEAENLSCRRGERL----LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVL-WNGEPIRDAREDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 560 TGVCPQSNVqFDFLTVRENLRLFAKIKGILPQEVDKE--------------------------------------IFLLD 601
Cdd:COG4133 78 AYLGHADGL-KPELTVRENLRFWAALYGLRADREAIDealeavglagladlpvrqlsagqkrrvalarlllspapLWLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6005701 602 EPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQfmDEADILADRKVFLSQGK 652
Cdd:COG4133 157 EPFTALDAAGVALLAELIAAhLARGGAVLLTTH--QPLELAAARVLDLGDFK 206
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1260-1436 |
2.15e-24 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 102.64 E-value: 2.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1260 RKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGD-----ALEFLGYcpqENALWPNL 1334
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDpdvaeACHYLGH---RNAMKPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1335 TVRQHLEVYAAVKGLRKGDAEVAItrlvDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQ 1414
Cdd:PRK13539 89 TVAENLEFWAAFLGGEELDIAAAL----EAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVA 164
|
170 180
....*....|....*....|....
gi 6005701 1415 QMWQAIRAtfrNTERG--ALLTTH 1436
Cdd:PRK13539 165 LFAELIRA---HLAQGgiVIAATH 185
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1267-1456 |
3.21e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 108.57 E-value: 3.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1267 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-----SGGGDALEfLG----YcpQENALWPNLTVR 1337
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepvrfRSPRDAQA-AGiaiiH--QELNLVPNLSVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1338 Q--HLEVYAAVKGLRKGDAEVAITR-LVDALKLQDQLKSPVKTLSEGiKRKLcfVL---SILGNPSVVLLDEPSTGMDPE 1411
Cdd:COG1129 98 EniFLGREPRRGGLIDWRAMRRRAReLLARLGLDIDPDTPVGDLSVA-QQQL--VEiarALSRDARVLILDEPTASLTER 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 6005701 1412 GQQQMWQAIRaTFRntERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1456
Cdd:COG1129 175 EVERLFRIIR-RLK--AQGVaiIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
499-597 |
3.70e-24 |
|
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: 100.03 E-value: 3.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 499 LKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIyNNKLSEMADLENLSKLTGVCPQSNVQFDFLTVREN 578
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILL-DGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90
....*....|....*....
gi 6005701 579 LRLFAKIKGILPQEVDKEI 597
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARA 98
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
480-657 |
5.08e-24 |
|
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: 100.47 E-value: 5.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGKPDKIeaLKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADleNLSKL 559
Cdd:cd03247 1 LSINNVSFSYPEQEQQV--LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK--ALSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 560 TGVCPQSNVQFDfLTVRENL----------RL-FAKikgILPQEVDkeIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVI 628
Cdd:cd03247 77 ISVLNQRPYLFD-TTLRNNLgrrfsggerqRLaLAR---ILLQDAP--IVLLDEPTVGLDPITERQLLSLIFEVLKDKTL 150
|
170 180
....*....|....*....|....*....
gi 6005701 629 LFSTQFMDEADiLADRKVFLSQGKLKCAG 657
Cdd:cd03247 151 IWITHHLTGIE-HMDKILFLENGKIIMQG 178
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
479-691 |
1.34e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 102.38 E-value: 1.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 479 AIRIRNVTKEYKgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEmADLENLSK 558
Cdd:PRK13632 7 MIKVENVSFSYP--NSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISK-ENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 559 LTGVCPQS-NVQFDFLTVR-------ENLRL-FAKIKGIL----------------PQE----------------VDKEI 597
Cdd:PRK13632 84 KIGIIFQNpDNQFIGATVEddiafglENKKVpPKKMKDIIddlakkvgmedyldkePQNlsggqkqrvaiasvlaLNPEI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 598 FLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEAdILADRKVFLSQGKLKCAGS-SLFLKKKWGIG----- 669
Cdd:PRK13632 164 IIFDESTSMLDPKGKREIKKIMVDlrKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKpKEILNNKEILEkakid 242
|
250 260
....*....|....*....|....*.
gi 6005701 670 ----YHLSLQLNEICVEENITSLVKQ 691
Cdd:PRK13632 243 spfiYKLSKKLKGIDPTYNEEELIEQ 268
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1258-1460 |
3.17e-23 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 99.64 E-value: 3.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1258 SKR-KNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGD--------ALEFLGYcpqen 1328
Cdd:cd03301 7 TKRfGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDlppkdrdiAMVFQNY----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1329 ALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGM 1408
Cdd:cd03301 82 ALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6005701 1409 DPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1460
Cdd:cd03301 162 DAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
479-652 |
3.48e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 102.99 E-value: 3.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 479 AIRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENlsK 558
Cdd:PRK13536 41 AIDLAGVSKSYGDKA----VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLAR--A 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 559 LTGVCPQ-SNVQFDFlTVRENLRLFAKIKGILPQEV----------------------------------------DKEI 597
Cdd:PRK13536 115 RIGVVPQfDNLDLEF-TVRENLLVFGRYFGMSTREIeavipsllefarleskadarvsdlsggmkrrltlaralinDPQL 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6005701 598 FLLDEPTAGLDPFSRHQVW----NLLKERKTdrvILFSTQFMDEADILADRKVFLSQGK 652
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIWerlrSLLARGKT---ILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
480-653 |
5.98e-23 |
|
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: 97.11 E-value: 5.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGkpdkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIyNNKlsemadlenlskl 559
Cdd:cd03216 1 LELRGITKRFGG----VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILV-DGK------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 560 tgvcpqsnvQFDFLTVRENLRLfakikGI-----LP----QEV--------DKEIFLLDEPTAGLDPFSRHQVWNLLKER 622
Cdd:cd03216 63 ---------EVSFASPRDARRA-----GIamvyqLSvgerQMVeiaralarNARLLILDEPTAALTPAEVERLFKVIRRL 128
|
170 180 190
....*....|....*....|....*....|..
gi 6005701 623 KTDRV-ILFSTQFMDEADILADRKVFLSQGKL 653
Cdd:cd03216 129 RAQGVaVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1267-1474 |
8.41e-23 |
|
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: 98.95 E-value: 8.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1267 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSgggDALEF------LGYCPQENALWPNLTVRQHL 1340
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGK---DITNLppekrdISYVPQNYALFPHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1341 EVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAI 1420
Cdd:cd03299 93 AYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREEL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6005701 1421 RATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQ----HLKSKFGKDYL 1474
Cdd:cd03299 173 KKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEevfkKPKNEFVAEFL 230
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
455-659 |
9.44e-23 |
|
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: 104.21 E-value: 9.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 455 DEMDADPSFHDSFEQAPPEFQGKE-AIRIRNVTKEYKGK-PDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGL 532
Cdd:COG1123 235 QALAAVPRLGAARGRAAPAAAAAEpLLEVRNLSKRYPVRgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 533 SVPTKGSVTIYNNKLSEM--ADLENLSKLTGVCPQS-NVQFD-FLTVRENLRLFAKIKGILPQE---------------- 592
Cdd:COG1123 315 LRPTSGSILFDGKDLTKLsrRSLRELRRRVQMVFQDpYSSLNpRMTVGDIIAEPLRLHGLLSRAerrervaellervglp 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 593 --------------------------VDKEIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADR 644
Cdd:COG1123 395 pdladryphelsggqrqrvaiaralaLEPKLLILDEPTSALDVSVQAQILNLLRDlqRELGLTYLFISHDLAVVRYIADR 474
|
250
....*....|....*
gi 6005701 645 KVFLSQGKLKCAGSS 659
Cdd:COG1123 475 VAVMYDGRIVEDGPT 489
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1245-1465 |
1.15e-22 |
|
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: 98.42 E-value: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1245 LRKEYAGKRKgcfskrkNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDAL-E 1319
Cdd:cd03258 7 VSKVFGDTGG-------KVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGtdltLLSGKELrK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1320 F---LGYCPQENALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNP 1396
Cdd:cd03258 80 ArrrIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6005701 1397 SVVLLDEPSTGMDPEGQQQMWQAIRATfrNTERG--ALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL 1465
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDI--NRELGltIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
479-653 |
1.28e-22 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 98.98 E-value: 1.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 479 AIRIRNVTKEYkgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEM--ADLENL 556
Cdd:COG3638 2 MLELRNLSKRY---PGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALrgRALRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 557 SKLTGVCPQsnvQFDF---LTVREN---------------LRLFAK--------------IKGILPQEVDK--------- 595
Cdd:COG3638 79 RRRIGMIFQ---QFNLvprLSVLTNvlagrlgrtstwrslLGLFPPedreralealervgLADKAYQRADQlsggqqqrv 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 596 ----------EIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKL 653
Cdd:COG3638 156 aiaralvqepKLILADEPVASLDPKTARQVMDLLRRiaREDGITVVVNLHQVDLARRYADRIIGLRDGRV 225
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
479-690 |
1.56e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 100.55 E-value: 1.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 479 AIRIRNVTKEYK------G---------KPDK--IEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVT 541
Cdd:COG4586 1 IIEVENLSKTYRvyekepGlkgalkglfRREYreVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 542 I-----YNNKlsemadLENLSKLTGVCPQ-SNVQFDfLTVRENLRLFAKIKGILPQEVDK-------------------- 595
Cdd:COG4586 81 VlgyvpFKRR------KEFARRIGVVFGQrSQLWWD-LPAIDSFRLLKAIYRIPDAEYKKrldelvelldlgelldtpvr 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 596 --------------------EIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDeaDI--LADRKVFLSQG 651
Cdd:COG4586 154 qlslgqrmrcelaaallhrpKILFLDEPTIGLDVVSKEAIREFLKEynRERGTTILLTSHDMD--DIeaLCDRVIVIDHG 231
|
250 260 270
....*....|....*....|....*....|....*....
gi 6005701 652 KLKCAGSSLFLKKKWGIGYHLSLQLNEICVEENITSLVK 690
Cdd:COG4586 232 RIIYDGSLEELKERFGPYKTIVLELAEPVPPLELPRGGE 270
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1257-1460 |
1.61e-22 |
|
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: 96.35 E-value: 1.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1257 FSKRKNKIAtRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGsgggdaleflgycpQENALWPNLTV 1336
Cdd:cd03214 7 VGYGGRTVL-DDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDG--------------KDLASLSPKEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1337 RQHLEVyaavkglrkgdaevaITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQM 1416
Cdd:cd03214 72 ARKIAY---------------VPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIEL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 6005701 1417 WQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1460
Cdd:cd03214 137 LELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
480-653 |
2.28e-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: 97.79 E-value: 2.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEY-----------------KGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTI 542
Cdd:cd03267 1 IEVSNLSKSYrvyskepgligslkslfKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 543 YNNKLSEMADlENLSKLTGVCPQSN-VQFDfLTVRENLRLFAKIKGILPQE----VDK---------------------- 595
Cdd:cd03267 81 AGLVPWKRRK-KFLRRIGVVFGQKTqLWWD-LPVIDSFYLLAAIYDLPPARfkkrLDElselldleelldtpvrqlslgq 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6005701 596 --------------EIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKL 653
Cdd:cd03267 159 rmraeiaaallhepEILFLDEPTIGLDVVAQENIRNFLKEynRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1267-1455 |
3.82e-22 |
|
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: 97.46 E-value: 3.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1267 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVL-LKGS--GGGDALE---FLGYCPQENALW--PNLTVRq 1338
Cdd:COG1119 20 DDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrLFGErrGGEDVWElrkRIGLVSPALQLRfpRDETVL- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1339 hlEV-----YAAVkGLRK--GDAEVAITR-LVDALKLQDQLKSPVKTLSEGIKRKlcfVL---SILGNPSVVLLDEPSTG 1407
Cdd:COG1119 99 --DVvlsgfFDSI-GLYRepTDEQRERAReLLELLGLAHLADRPFGTLSQGEQRR---VLiarALVKDPELLILDEPTAG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 6005701 1408 MDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1455
Cdd:COG1119 173 LDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGR 220
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1256-1454 |
4.19e-22 |
|
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: 96.17 E-value: 4.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1256 CFSKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGS--GGGDALEFLGYCPQEnalwpn 1333
Cdd:cd03226 6 SFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKpiKAKERRKSIGYVMQD------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1334 ltVRQHL-------EVYAAVKGLRKGDAEVA-ITRLVDALKLQDQLksPvKTLSEGIKRKLCFVLSILGNPSVVLLDEPS 1405
Cdd:cd03226 80 --VDYQLftdsvreELLLGLKELDAGNEQAEtVLKDLDLYALKERH--P-LSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6005701 1406 TGMDPEGQQQMWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSG 1454
Cdd:cd03226 155 SGLDYKNMERVGELIR-ELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1264-1456 |
7.40e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 101.26 E-value: 7.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1264 IATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-----SGGGDALEF-LGYCPQENALWPNLTVR 1337
Cdd:COG3845 19 VANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpvriRSPRDAIALgIGMVHQHFMLVPNLTVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1338 QHLeVYAAVKG----LRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQ 1413
Cdd:COG3845 99 ENI-VLGLEPTkggrLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 6005701 1414 QQMWQAIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1456
Cdd:COG3845 178 DELFEILRR-LAAEGKSIIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1267-1456 |
8.99e-22 |
|
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: 94.54 E-value: 8.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1267 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTA--GQVLLKGSGGgDALEF---LGYCPQENALWPNLTVRQHLE 1341
Cdd:cd03213 26 KNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPL-DKRSFrkiIGYVPQDDILHPTLTVRETLM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1342 VYAAVKGLrkgdaevaitrlvdalklqdqlkspvktlSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIR 1421
Cdd:cd03213 105 FAAKLRGL-----------------------------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLR 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 6005701 1422 AtFRNTERGALLTTHY-MAEAEAVCDRVAIMVSGRL 1456
Cdd:cd03213 156 R-LADTGRTIICSIHQpSSEIFELFDKLLLLSQGRV 190
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1267-1466 |
9.95e-22 |
|
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: 95.65 E-value: 9.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1267 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDALEFL----GYCPQENALWPNLTVRQ 1338
Cdd:cd03261 17 KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGedisGLSEAELYRLrrrmGMLFQSGALFDSLTVFE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1339 HLEVYaavkgLR---KGDAEVaITRLVdALKLQ------DQLKSPVKtLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMD 1409
Cdd:cd03261 97 NVAFP-----LRehtRLSEEE-IREIV-LEKLEavglrgAEDLYPAE-LSGGMKKRVALARALALDPELLLYDEPTAGLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 6005701 1410 PEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLK 1466
Cdd:cd03261 169 PIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELR 225
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1262-1461 |
1.11e-21 |
|
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: 95.77 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1262 NKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsGGGDALEFLGYCPQEN------ALWPNLT 1335
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILL---DGKDITNLPPHKRPVNtvfqnyALFPHLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1336 VRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQ 1415
Cdd:cd03300 89 VFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6005701 1416 MWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1461
Cdd:cd03300 169 MQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
480-653 |
1.27e-21 |
|
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: 94.89 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIynnklsemaDLENLSKL 559
Cdd:cd03259 1 LELKGLSKTYGSVR----ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILI---------DGRDVTGV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 560 ------TGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDK-------------------------------------- 595
Cdd:cd03259 68 pperrnIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRArvrellelvglegllnryphelsggqqqrvalaralar 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6005701 596 --EIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKL 653
Cdd:cd03259 148 epSLLLLDEPLSALDAKLREELREELKElqRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
480-652 |
1.72e-21 |
|
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: 94.81 E-value: 1.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYkgkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLSKL 559
Cdd:cd03224 1 LEVENLNAGY----GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 560 TGVCPQSNVQFDFLTVRENLRL--FAKIKGILPQEVDK--EIF-----------------------------------LL 600
Cdd:cd03224 77 IGYVPEGRRIFPELTVEENLLLgaYARRRAKRKARLERvyELFprlkerrkqlagtlsggeqqmlaiaralmsrpkllLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6005701 601 DEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGK 652
Cdd:cd03224 157 DEPSEGLAPKIVEEIFEAIRElRDEGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
480-653 |
2.28e-21 |
|
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: 94.49 E-value: 2.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMadLENLSKL 559
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKL--SRRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 560 TGvcpqSNVQFDF----------LTVRE------------------NLRLFAKIKGI---------LPQE---------- 592
Cdd:cd03257 80 RR----KEIQMVFqdpmsslnprMTIGEqiaeplrihgklskkearKEAVLLLLVGVglpeevlnrYPHElsggqrqrva 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6005701 593 ------VDKEIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKL 653
Cdd:cd03257 156 iaralaLNPKLLIADEPTSALDVSVQAQILDLLKKlqEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
480-653 |
2.59e-21 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 93.73 E-value: 2.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGKPDkieaLKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMaDLENLSKL 559
Cdd:COG4619 1 LELEGLSFRVGGKPI----LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAM-PPPEWRRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 560 TGVCPQSNVQFDfLTVRENL-----------------RLFAKI---KGILPQEVDK-------------------EIFLL 600
Cdd:COG4619 76 VAYVPQEPALWG-GTVRDNLpfpfqlrerkfdreralELLERLglpPDILDKPVERlsggerqrlaliralllqpDVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6005701 601 DEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKL 653
Cdd:COG4619 155 DEPTSALDPENTRRVEELLREylAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
479-653 |
3.17e-21 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 97.09 E-value: 3.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 479 AIRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIynnklsemaDLENLSK 558
Cdd:COG3842 5 ALELENVSKRYGDVT----ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILL---------DGRDVTG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 559 L------TGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDK------------------------------------- 595
Cdd:COG3842 72 LppekrnVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRArvaellelvglegladryphqlsggqqqrvalarala 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6005701 596 ---EIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFST--QfmDEADILADRKVFLSQGKL 653
Cdd:COG3842 152 pepRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVThdQ--EEALALADRIAVMNDGRI 214
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1267-1462 |
3.40e-21 |
|
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: 94.07 E-value: 3.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1267 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDALEFLgycpQENALWPNLTVRQH--L 1340
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGkqitEPGPDRMVVF----QNYSLLPWLTVRENiaL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1341 EVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDP-------EGQ 1413
Cdd:TIGR01184 78 AVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAltrgnlqEEL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6005701 1414 QQMWQAIRATfrntergALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSI 1462
Cdd:TIGR01184 158 MQIWEEHRVT-------VLMVTHDVDEALLLSDRVVMLTNGPAANIGQI 199
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
480-653 |
3.72e-21 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 96.69 E-value: 3.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYN---NKLSEmADLENL 556
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGvdlTALSE-RELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 557 SKLTGVCPQsnvQFDFL---TVRENLRLFAKIKGILPQEVDK-------------------------------------- 595
Cdd:COG1135 81 RRKIGMIFQ---HFNLLssrTVAENVALPLEIAGVPKAEIRKrvaellelvglsdkadaypsqlsggqkqrvgiaralan 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6005701 596 --EIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKL 653
Cdd:COG1135 158 npKVLLCDEATSALDPETTRSILDLLKDinRELGLTIVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
479-652 |
5.53e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 95.64 E-value: 5.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 479 AIRIRNVTKEYKgkpDKIeALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLSk 558
Cdd:PRK13537 7 PIDFRNVEKRYG---DKL-VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 559 lTGVCPQ-SNVQFDFlTVRENLRLFAKIKGILPQEV----------------------------------------DKEI 597
Cdd:PRK13537 82 -VGVVPQfDNLDPDF-TVRENLLVFGRYFGLSAAAAralvppllefaklenkadakvgelsggmkrrltlaralvnDPDV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6005701 598 FLLDEPTAGLDPFSRHQVW----NLLKERKTdrvILFSTQFMDEADILADRKVFLSQGK 652
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWerlrSLLARGKT---ILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
479-658 |
6.21e-21 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 93.62 E-value: 6.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 479 AIRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNnklsemADLENLSK 558
Cdd:COG1121 6 AIELENLTVSYGGRP----VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG------KPPRRARR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 559 LTGVCPQ-SNVQFDF-LTVRE--------NLRLFAKIKGILPQEVDK--------------------------------- 595
Cdd:COG1121 76 RIGYVPQrAEVDWDFpITVRDvvlmgrygRRGLFRRPSRADREAVDEalervgledladrpigelsggqqqrvllarala 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6005701 596 ---EIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKLkCAGS 658
Cdd:COG1121 156 qdpDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREYFDRVLLLNRGLV-AHGP 221
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1263-1478 |
7.36e-21 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 94.03 E-value: 7.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1263 KIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSgggDALEflgycpqENALWpnlTVRQHLE- 1341
Cdd:TIGR04520 15 KPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGL---DTLD-------EENLW---EIRKKVGm 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1342 ---------VYAAVK-----GL--RKGDAEVAITRLVDALK---LQDQLKSPVKTLSEGIKRKLCfVLSILG-NPSVVLL 1401
Cdd:TIGR04520 82 vfqnpdnqfVGATVEddvafGLenLGVPREEMRKRVDEALKlvgMEDFRDREPHLLSGGQKQRVA-IAGVLAmRPDIIIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1402 DEPsTGM-DPEGQQQMWQAIRATfrNTERGA--LLTTHYMAEAeAVCDRVAIMVSGRLRCIGSIQHLKSKfgKDYLLEMK 1478
Cdd:TIGR04520 161 DEA-TSMlDPKGRKEVLETIRKL--NKEEGItvISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIFSQ--VELLKEIG 234
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
480-657 |
9.19e-21 |
|
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: 92.34 E-value: 9.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGKpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMAdlenlSKL 559
Cdd:cd03269 1 LEVENVTKRFGRV----TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA-----RNR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 560 TGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEV----------------------------------------DKEIFL 599
Cdd:cd03269 72 IGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEArrridewlerlelseyankrveelskgnqqkvqfiaavihDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6005701 600 LDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAG 657
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRElARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
509-657 |
1.15e-20 |
|
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: 92.17 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 509 GQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNnklSEMADLENLSKLTGVCPQSNVQFDFLTVREN--------LR 580
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING---VDVTAAPPADRPVSMLFQENNLFAHLTVEQNvglglspgLK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 581 LFA----KIKGI------------LPQEV----------------DKEIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDR 626
Cdd:cd03298 101 LTAedrqAIEVAlarvglaglekrLPGELsggerqrvalarvlvrDKPVLLLDEPFAALDPALRAEMLDLVLDlhAETKM 180
|
170 180 190
....*....|....*....|....*....|.
gi 6005701 627 VILFSTQFMDEADILADRKVFLSQGKLKCAG 657
Cdd:cd03298 181 TVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1267-1475 |
1.46e-20 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 98.37 E-value: 1.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1267 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsGGGDALEF--------LGYCPQENALWP-----N 1333
Cdd:COG2274 492 DNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILI---DGIDLRQIdpaslrrqIGVVLQDVFLFSgtireN 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1334 LTVrqhlevyaavkglrkGDAEVAITRLVDALK----------LQDQLKSPV----KTLSEGIKRKLCFVLSILGNPSVV 1399
Cdd:COG2274 569 ITL---------------GDPDATDEEIIEAARlaglhdfieaLPMGYDTVVgeggSNLSGGQRQRLAIARALLRNPRIL 633
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6005701 1400 LLDEPSTGMDPEGQQQMWQAIRATFRNteRGALLTTHYMAEAEAvCDRVAIMVSGRLRCIGSIQHLKSKFGKDYLL 1475
Cdd:COG2274 634 ILDEATSALDAETEAIILENLRRLLKG--RTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEELLARKGLYAEL 706
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
480-653 |
1.57e-20 |
|
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: 91.83 E-value: 1.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEY------------------KGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVT 541
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 542 IyNNKLSEMADLEnlsklTGVCPQsnvqfdfLTVRENLRLFAKIKGILPQEVDK-------------------------- 595
Cdd:cd03220 81 V-RGRVSSLLGLG-----GGFNPE-------LTGRENIYLNGRLLGLSRKEIDEkideiiefselgdfidlpvktyssgm 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6005701 596 --------------EIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKL 653
Cdd:cd03220 148 karlafaiatalepDILLIDEVLAVGDAAFQEKCQRRLRElLKQGKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
478-658 |
2.21e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 92.07 E-value: 2.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 478 EAIRIRNVTKEY------------------KGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGS 539
Cdd:COG1134 3 SMIEVENVSKSYrlyhepsrslkelllrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 540 VTIyNNKLSEMADLEnlsklTGVCPQsnvqfdfLTVRENLRLFAKIKGILPQEVDK------------------------ 595
Cdd:COG1134 83 VEV-NGRVSALLELG-----AGFHPE-------LTGRENIYLNGRLLGLSRKEIDEkfdeivefaelgdfidqpvktyss 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 596 ----------------EIFLLDEPTAGLDPFSRHQVWNLLKERKTD-RVILFSTQFMDEADILADRKVFLSQGKLKCAGS 658
Cdd:COG1134 150 gmrarlafavatavdpDILLVDEVLAVGDAAFQKKCLARIRELRESgRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGD 229
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
479-653 |
2.80e-20 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 94.37 E-value: 2.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 479 AIRIRNVTKEYkgkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIyNNKLseMADLEnlsk 558
Cdd:COG3839 3 SLELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILI-GGRD--VTDLP---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 559 ltgvcP---------QSNVQFDFLTVRENLrLFA-KIKGILPQEVDK--------------------------------- 595
Cdd:COG3839 72 -----PkdrniamvfQSYALYPHMTVYENI-AFPlKLRKVPKAEIDRrvreaaellgledlldrkpkqlsggqrqrvalg 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6005701 596 -------EIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKL 653
Cdd:COG3839 146 ralvrepKVFLLDEPLSNLDAKLRVEMRAEIKRlhRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRI 212
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1239-1461 |
2.82e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 91.88 E-value: 2.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1239 VIIASCLRKEYAGKRkgcfskrknkiATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSG----- 1313
Cdd:PRK10895 3 TLTAKNLAKAYKGRR-----------VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDisllp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1314 -GGDALEFLGYCPQENALWPNLTVRQHL-EVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLS 1391
Cdd:PRK10895 72 lHARARRGIGYLPQEASIFRRLSVYDNLmAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1392 ILGNPSVVLLDEPSTGMDPEGQQQMWQAIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1461
Cdd:PRK10895 152 LAANPKFILLDEPFAGVDPISVIDIKRIIEH-LRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
480-653 |
2.82e-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: 91.98 E-value: 2.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGKPdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMaDLENLSKL 559
Cdd:cd03295 1 IEFENVTKRYGGGK---KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQ-DPVELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 560 TGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEV------------------------------------------DKEI 597
Cdd:cd03295 77 IGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIreradellalvgldpaefadryphelsggqqqrvgvaralaaDPPL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6005701 598 FLLDEPTAGLDPFSRHQVWNLLK--ERKTDRVILFSTQFMDEADILADRKVFLSQGKL 653
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKrlQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEI 214
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1265-1468 |
2.90e-20 |
|
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: 96.75 E-value: 2.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1265 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsGGGDALEF--------LGYCPQeNALWPNLTV 1336
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILI---NGVDLSDLdpaswrrqIAWVPQ-NPYLFAGTI 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1337 RQHL----------EVYAAVKglrkgdaEVAITRLVDAlkLQDQLKSPV----KTLSEGIKRKLCFVLSILGNPSVVLLD 1402
Cdd:COG4988 428 RENLrlgrpdasdeELEAALE-------AAGLDEFVAA--LPDGLDTPLgeggRGLSGGQAQRLALARALLRDAPLLLLD 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6005701 1403 EPSTGMDPEGQQQMWQAIRATFRNteRGALLTTHYMAEAEAvCDRVAIMVSGRLRCIGSIQHLKSK 1468
Cdd:COG4988 499 EPTAHLDAETEAEILQALRRLAKG--RTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELLAK 561
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1236-1460 |
3.16e-20 |
|
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: 96.41 E-value: 3.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1236 EKPVIIASCLRKEYAGKRKGCFSkrknkiATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLK----- 1310
Cdd:TIGR03269 276 GEPIIKVRNVSKRYISVDRGVVK------AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgdew 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1311 -------GSGGGDALEFLGYCPQENALWPNLTVrqhLEVYAAVKGLRKGDaEVAITRLVDALKL----QDQLKSPVK--- 1376
Cdd:TIGR03269 350 vdmtkpgPDGRGRAKRYIGILHQEYDLYPHRTV---LDNLTEAIGLELPD-ELARMKAVITLKMvgfdEEKAEEILDkyp 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1377 -TLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1455
Cdd:TIGR03269 426 dELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGK 505
|
....*
gi 6005701 1456 LRCIG 1460
Cdd:TIGR03269 506 IVKIG 510
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1251-1456 |
4.12e-20 |
|
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: 90.79 E-value: 4.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1251 GKRKGCF-SKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITG---DTKPTAGQVLLKGSgGGDALEFL---GY 1323
Cdd:cd03234 7 WDVGLKAkNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQ-PRKPDQFQkcvAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1324 CPQENALWPNLTVRQHLeVYAAVKGLRKGDAEVAITRLVDALKLQD----QLKSP-VKTLSEGIKRKLCFVLSILGNPSV 1398
Cdd:cd03234 86 VRQDDILLPGLTVRETL-TYTAILRLPRKSSDAIRKKRVEDVLLRDlaltRIGGNlVKGISGGERRRVSIAVQLLWDPKV 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6005701 1399 VLLDEPSTGMDPEGQQQMWQAIRATFRnTERGALLTTHY-MAEAEAVCDRVAIMVSGRL 1456
Cdd:cd03234 165 LILDEPTSGLDSFTALNLVSTLSQLAR-RNRIVILTIHQpRSDLFRLFDRILLLSSGEI 222
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1265-1456 |
4.38e-20 |
|
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: 90.73 E-value: 4.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1265 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsGGGDALEF--------LGYCPQENALWpNLTV 1336
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLL---DGTDIRQLdpadlrrnIGYVPQDVTLF-YGTL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1337 RQHLEVyaavkglrkGDAEVAITRLVDALKLQ--DQL--KSPV----------KTLSEGIKRKLCFVLSILGNPSVVLLD 1402
Cdd:cd03245 95 RDNITL---------GAPLADDERILRAAELAgvTDFvnKHPNgldlqigergRGLSGGQRQAVALARALLNDPPILLLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 6005701 1403 EPSTGMDPEGQQQMWQAIRATFRntERGALLTTHYMAeAEAVCDRVAIMVSGRL 1456
Cdd:cd03245 166 EPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPS-LLDLVDRIIVMDSGRI 216
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
479-658 |
4.70e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 92.48 E-value: 4.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 479 AIRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIyNNKLSEMADLENLSK 558
Cdd:COG4152 1 MLELKGLTKRFGDKT----AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLW-DGEPLDPEDRRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 559 L---TGVCPQsnvqfdfLTVRENLRLFAKIKGILPQEVDKEI-------------------------------------- 597
Cdd:COG4152 76 LpeeRGLYPK-------MKVGEQLVYLARLKGLSKAEAKRRAdewlerlglgdrankkveelskgnqqkvqliaallhdp 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6005701 598 -FL-LDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS 658
Cdd:COG4152 149 eLLiLDEPFSGLDPVNVELLKDVIRElAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGS 212
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
480-621 |
6.17e-20 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 90.11 E-value: 6.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYkgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEM--ADLENLS 557
Cdd:COG2884 2 IRFENVSKRY---PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrREIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 558 KLTGVCPQsnvqfDF-----LTVRENLRLFAKIKGILPQEVDK------------------------------------- 595
Cdd:COG2884 79 RRIGVVFQ-----DFrllpdRTVYENVALPLRVTGKSRKEIRRrvrevldlvglsdkakalphelsggeqqrvaiaralv 153
|
170 180
....*....|....*....|....*....
gi 6005701 596 ---EIFLLDEPTAGLDPFSRHQVWNLLKE 621
Cdd:COG2884 154 nrpELLLADEPTGNLDPETSWEIMELLEE 182
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
478-658 |
6.31e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 91.37 E-value: 6.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 478 EAIRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLEnLS 557
Cdd:PRK13548 1 AMLEARNLSVRLGGRT----LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAE-LA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 558 KLTGVCPQ-SNVQFDFlTVRENLRLFAKIKGILPQEVD------------------------------------------ 594
Cdd:PRK13548 76 RRRAVLPQhSSLSFPF-TVEEVVAMGRAPHGLSRAEDDalvaaalaqvdlahlagrdypqlsggeqqrvqlarvlaqlwe 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6005701 595 ----KEIFLLDEPTAGLDPFSRHQVWNLLKERKTDR-----VIL----FSTQFmdeadilADRKVFLSQGKLKCAGS 658
Cdd:PRK13548 155 pdgpPRWLLLDEPTSALDLAHQHHVLRLARQLAHERglaviVVLhdlnLAARY-------ADRIVLLHQGRLVADGT 224
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
480-652 |
8.05e-20 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 90.32 E-value: 8.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYkgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEM--ADLENLS 557
Cdd:cd03256 1 IEVENLSKTY---PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLkgKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 558 KLTGVCPQS-----------NVQFDFL----TVRENLRLFAKIK-----------GILP---QEVDK------------- 595
Cdd:cd03256 78 RQIGMIFQQfnlierlsvleNVLSGRLgrrsTWRSLFGLFPKEEkqralaalervGLLDkayQRADQlsggqqqrvaiar 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6005701 596 ------EIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGK 652
Cdd:cd03256 158 almqqpKLILADEPVASLDPASSRQVMDLLKRinREEGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
479-658 |
8.99e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 91.34 E-value: 8.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 479 AIRIRNVTKEYK-GKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKL---SEMADLE 554
Cdd:PRK13649 2 GINLQNVSYTYQaGTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstSKNKDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 555 NLSKLTGVC---PQSNVqFDfLTV----------------------RENLR-------LFAK--------------IKGI 588
Cdd:PRK13649 82 QIRKKVGLVfqfPESQL-FE-ETVlkdvafgpqnfgvsqeeaealaREKLAlvgisesLFEKnpfelsggqmrrvaIAGI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6005701 589 LPQEVDkeIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS 658
Cdd:PRK13649 160 LAMEPK--ILVLDEPTAGLDPKGRKELMTLFKKlHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGK 228
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
481-654 |
1.04e-19 |
|
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: 89.24 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 481 RIRNVTKEYKgkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMAdlenLSKLT 560
Cdd:cd03226 1 RIENISFSYK---KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE----RRKSI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 561 GVCPQ-SNVQFDFLTVRENLRLFAKIKGILPQEV------------------------------------DKEIFLLDEP 603
Cdd:cd03226 74 GYVMQdVDYQLFTDSVREELLLGLKELDAGNEQAetvlkdldlyalkerhplslsggqkqrlaiaaallsGKDLLIFDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6005701 604 TAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKLK 654
Cdd:cd03226 154 TSGLDYKNMERVGELIRElAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1236-1460 |
1.82e-19 |
|
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: 90.01 E-value: 1.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1236 EKPVIIASCLRKEYAGKRKGCFskrknkIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsGGG 1315
Cdd:cd03294 16 KAFKLLAKGKSKEEILKKTGQT------VGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLI---DGQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1316 DALEF------------LGYCPQENALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIK 1383
Cdd:cd03294 87 DIAAMsrkelrelrrkkISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQ 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6005701 1384 RKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1460
Cdd:cd03294 167 QRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVG 243
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
457-653 |
1.94e-19 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 94.46 E-value: 1.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 457 MDADPSFHDSfEQAPPEFQGKEAIRIRNVTKEYkgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPT 536
Cdd:COG1132 318 LDEPPEIPDP-PGAVPLPPVRGEIEFENVSFSY---PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPT 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 537 KGSVTIYNNKLSEMaDLENLSKLTGVCPQSNVQFDfLTVRENLRLF------------AKIKGI------LPQ----EV- 593
Cdd:COG1132 394 SGRILIDGVDIRDL-TLESLRRQIGVVPQDTFLFS-GTIRENIRYGrpdatdeeveeaAKAAQAhefieaLPDgydtVVg 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 594 ----------------------DKEIFLLDEPTAGLDPFSRHQVWNLLKERKTDR-VIL----FSTqfmdeadIL-ADRK 645
Cdd:COG1132 472 ergvnlsggqrqriaiarallkDPPILILDEATSALDTETEALIQEALERLMKGRtTIViahrLST-------IRnADRI 544
|
....*...
gi 6005701 646 VFLSQGKL 653
Cdd:COG1132 545 LVLDDGRI 552
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1265-1461 |
2.55e-19 |
|
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: 88.94 E-value: 2.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1265 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsGGGDALEF------LGYCPQENALWPNLTVRQ 1338
Cdd:cd03296 17 ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILF---GGEDATDVpvqernVGFVFQHYALFRHMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1339 HLEVYAAVKGLRKGDAEVAITRLVDAL-------KLQDQLKSpvkTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1411
Cdd:cd03296 94 NVAFGLRVKPRSERPPEAEIRAKVHELlklvqldWLADRYPA---QLSGGQRQRVALARALAVEPKVLLLDEPFGALDAK 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6005701 1412 GQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1461
Cdd:cd03296 171 VRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1267-1455 |
2.80e-19 |
|
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: 86.67 E-value: 2.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1267 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsGGGDALEF--------LGYCPQENALWpNLTVRQ 1338
Cdd:cd03228 19 KDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILI---DGVDLRDLdleslrknIAYVPQDPFLF-SGTIRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1339 HLevyaavkglrkgdaevaitrlvdalklqdqlkspvktLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQ 1418
Cdd:cd03228 95 NI-------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILE 137
|
170 180 190
....*....|....*....|....*....|....*..
gi 6005701 1419 AIRATFRNteRGALLTTHYMAEAEAvCDRVAIMVSGR 1455
Cdd:cd03228 138 ALRALAKG--KTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
480-674 |
4.14e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 89.69 E-value: 4.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGK-PDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLS---EMADLEN 555
Cdd:PRK13634 3 ITFQKVEHRYQYKtPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 556 LSKLTGVCPQ--------SNVQFD-------FLTVRENLRLFAK--IKGI-LPQEV------------------------ 593
Cdd:PRK13634 83 LRKKVGIVFQfpehqlfeETVEKDicfgpmnFGVSEEDAKQKARemIELVgLPEELlarspfelsggqmrrvaiagvlam 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 594 DKEIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS--SLFLKKKWGIG 669
Cdd:PRK13634 163 EPEVLVLDEPTAGLDPKGRKEMMEMFYKlhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTprEIFADPDELEA 242
|
....*
gi 6005701 670 YHLSL 674
Cdd:PRK13634 243 IGLDL 247
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1267-1456 |
7.23e-19 |
|
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: 86.81 E-value: 7.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1267 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG---SGGGDALEFL----GYCPQENALWPNLTVRQH 1339
Cdd:cd03262 17 KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGlklTDDKKNINELrqkvGMVFQQFNLFPHLTVLEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1340 L-EVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEG------IKRKLCFvlsilgNPSVVLLDEPSTGMDPEG 1412
Cdd:cd03262 97 ItLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGqqqrvaIARALAM------NPKVMLFDEPTSALDPEL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6005701 1413 QQQMWQAIRatfRNTERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1456
Cdd:cd03262 171 VGEVLDVMK---DLAEEGMtmVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
480-653 |
7.57e-19 |
|
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: 88.47 E-value: 7.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGKP-----------DKIE---------ALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGS 539
Cdd:cd03294 1 IKIKGLYKIFGKNPqkafkllakgkSKEEilkktgqtvGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 540 VTIYNNKLSEM--ADLENL-SKLTGVCPQSNVQFDFLTVRENLRLFAKIKGILPQE------------------------ 592
Cdd:cd03294 81 VLIDGQDIAAMsrKELRELrRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEreeraaealelvglegwehkypde 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6005701 593 ----------------VDKEIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKL 653
Cdd:cd03294 161 lsggmqqrvglaralaVDPDILLMDEAFSALDPLIRREMQDELLRlqAELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1265-1490 |
9.44e-19 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 89.79 E-value: 9.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1265 ATRNVSFCVRKGEVLGLLGHNGAGKSTSiKVITGDTKPTAGQvllkgsgggDALEFLGYCPQENALW------------- 1331
Cdd:NF000106 28 AVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGR---------RPWRF*TWCANRRALRrtig*hrpvr*gr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1332 -PNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDP 1410
Cdd:NF000106 98 rESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1411 EGQQQMWQAIRATFRNTERgALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFGKDYLlemkvknlaQVEPLHA 1490
Cdd:NF000106 178 RTRNEVWDEVRSMVRDGAT-VLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGGRTL---------QIRPAHA 247
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
480-653 |
1.00e-18 |
|
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: 86.43 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGKpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLS-EMADLENLSK 558
Cdd:cd03262 1 IEIKNLHKSFGDF----HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTdDKKNINELRQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 559 LTGVCPQSNVQFDFLTVRENLRLfAKIK--------------------GILPQE----------------------VDKE 596
Cdd:cd03262 77 KVGMVFQQFNLFPHLTVLENITL-APIKvkgmskaeaeeralellekvGLADKAdaypaqlsggqqqrvaiaralaMNPK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6005701 597 IFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKL 653
Cdd:cd03262 156 VMLFDEPTSALDPELVGEVLDVMKDlAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
480-652 |
1.07e-18 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 86.73 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGKPdkiealkdLVFD--IYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIyNNklsemadlENLS 557
Cdd:COG3840 2 LRLDDLTYRYGDFP--------LRFDltIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILW-NG--------QDLT 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 558 KLTgvcP---------QSNVQFDFLTVREN--------LRLFA----KIKGIL------------PQEV----------- 593
Cdd:COG3840 65 ALP---PaerpvsmlfQENNLFPHLTVAQNiglglrpgLKLTAeqraQVEQALervglaglldrlPGQLsggqrqrvala 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6005701 594 -----DKEIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGK 652
Cdd:COG3840 142 rclvrKRPILLLDEPFSALDPALRQEMLDLVDElcRERGLTVLMVTHDPEDAARIADRVLLVADGR 207
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1267-1461 |
1.22e-18 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 89.36 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1267 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsGGGDALEF------LGYCPQENALWPNLTVRQHL 1340
Cdd:COG3839 20 KDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILI---GGRDVTDLppkdrnIAMVFQSYALYPHMTVYENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1341 EVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEG------IKRklcfvlSILGNPSVVLLDEPSTGMDPEGQQ 1414
Cdd:COG3839 97 AFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGqrqrvaLGR------ALVREPKVFLLDEPLSNLDAKLRV 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6005701 1415 QMWQAIRATFRntERGA--LLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1461
Cdd:COG3839 171 EMRAEIKRLHR--RLGTttIYVTHDQVEAMTLADRIAVMNDGRIQQVGT 217
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1263-1456 |
1.86e-18 |
|
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: 84.79 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1263 KIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-----SGGGDALEF-LGYCP---QENALWPN 1333
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGkpvtrRSPRDAIRAgIAYVPedrKREGLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1334 LTVRQHLevyaavkglrkgdaevAITRLvdalklqdqlkspvktLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQ 1413
Cdd:cd03215 93 LSVAENI----------------ALSSL----------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 6005701 1414 QQMWQAIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1456
Cdd:cd03215 141 AEIYRLIRE-LADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1237-1404 |
2.19e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.51 E-value: 2.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1237 KPVIIASCLRKEYAGKrkgcfskrknKIAtRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsggGD 1316
Cdd:COG0488 313 KKVLELEGLSKSYGDK----------TLL-DDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-----GE 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1317 ALEfLGYCPQENA-LWPNLTVRQHLevyaavKGLRKGDAEVAITRLVDALKL-QDQLKSPVKTLSEGIKRKLCFVLSILG 1394
Cdd:COG0488 377 TVK-IGYFDQHQEeLDPDKTVLDEL------RDGAPGGTEQEVRGYLGRFLFsGDDAFKPVGVLSGGEKARLALAKLLLS 449
|
170
....*....|
gi 6005701 1395 NPSVVLLDEP 1404
Cdd:COG0488 450 PPNVLLLDEP 459
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
483-620 |
2.24e-18 |
|
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: 84.99 E-value: 2.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 483 RNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSG--LSVPTKGSVTIYNNKLSemadlENLSKLT 560
Cdd:cd03232 7 KNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLD-----KNFQRST 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6005701 561 GVCPQSNVQFDFLTVRENLRLFAKIKGILPQE-----------VDKEIFLLDEPTAGLDPFSRHQVWNLLK 620
Cdd:cd03232 82 GYVEQQDVHSPNLTVREALRFSALLRGLSVEQrkrltigvelaAKPSILFLDEPTSGLDSQAAYNIVRFLK 152
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
481-659 |
2.42e-18 |
|
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: 85.80 E-value: 2.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 481 RIRNVTKEYkgkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIynnklsemaDLENLSKLT 560
Cdd:COG0410 5 EVENLHAGY----GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRF---------DGEDITGLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 561 ---------GVCPQS-NVqFDFLTVRENLRLFA---KIKGILPQEVDK--EIF--------------------------- 598
Cdd:COG0410 72 phriarlgiGYVPEGrRI-FPSLTVEENLLLGAyarRDRAEVRADLERvyELFprlkerrrqragtlsggeqqmlaigra 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 599 --------LLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGSS 659
Cdd:COG0410 151 lmsrpkllLLDEPSLGLAPLIVEEIFEIIRRlNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTA 220
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1259-1463 |
2.80e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 86.36 E-value: 2.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1259 KRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGD--ALEF---LGYCPQENALWPN 1333
Cdd:PRK13548 11 RLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwsPAELarrRAVLPQHSSLSFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1334 LTVRQHLEVYAAVKGLRKGDAEVAIT---RLVDALKLQDqlkSPVKTLSEGIK------RKLCFVLSILGNPSVVLLDEP 1404
Cdd:PRK13548 91 FTVEEVVAMGRAPHGLSRAEDDALVAaalAQVDLAHLAG---RDYPQLSGGEQqrvqlaRVLAQLWEPDGPPRWLLLDEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6005701 1405 STGMDPEGQQQMWQAIRAtfRNTERGA--------L-LTTHYmaeaeavCDRVAIMVSGRLRCIGSIQ 1463
Cdd:PRK13548 168 TSALDLAHQHHVLRLARQ--LAHERGLavivvlhdLnLAARY-------ADRIVLLHQGRLVADGTPA 226
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
480-653 |
4.00e-18 |
|
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: 84.61 E-value: 4.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNklsEMADLENLSKL 559
Cdd:cd03301 1 VELENVTKRFGNVT----ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGR---DVTDLPPKDRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 560 TGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDK----------------------------------------EIFL 599
Cdd:cd03301 74 IAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDErvrevaellqiehlldrkpkqlsggqrqrvalgraivrepKVFL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6005701 600 LDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKL 653
Cdd:cd03301 154 MDEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
480-658 |
4.17e-18 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 85.94 E-value: 4.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLEnLSKL 559
Cdd:COG4559 2 LEAENLSVRLGGRT----LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWE-LARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 560 TGVCPQ-SNVQFDFlTVRENLRLfAKIKGILPQEVDKEI----------------------------------------- 597
Cdd:COG4559 77 RAVLPQhSSLAFPF-TVEEVVAL-GRAPHGSSAAQDRQIvrealalvglahlagrsyqtlsggeqqrvqlarvlaqlwep 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6005701 598 -------FLLDEPTAGLDPFSRHQVWNLLKERkTDR-----VIL----FSTQFmdeadilADRKVFLSQGKLKCAGS 658
Cdd:COG4559 155 vdggprwLFLDEPTSALDLAHQHAVLRLARQL-ARRgggvvAVLhdlnLAAQY-------ADRILLLHQGRLVAQGT 223
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1267-1456 |
5.91e-18 |
|
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: 83.03 E-value: 5.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1267 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDAL-EFLGYCPQENALWPNlTVRQHLe 1341
Cdd:cd03246 19 RNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGadisQWDPNELgDHVGYLPQDDELFSG-SIAENI- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1342 vyaavkglrkgdaevaitrlvdalklqdqlkspvktLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIR 1421
Cdd:cd03246 97 ------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIA 140
|
170 180 190
....*....|....*....|....*....|....*..
gi 6005701 1422 ATfrnTERGA--LLTTHYMaEAEAVCDRVAIMVSGRL 1456
Cdd:cd03246 141 AL---KAAGAtrIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
479-658 |
6.58e-18 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 89.19 E-value: 6.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 479 AIRIRNVTKEYKGkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPT---KGSVTIYNNKLSEMaDLEN 555
Cdd:COG1123 4 LLEVRDLSVRYPG--GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLEL-SEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 556 LSKLTGVCPQS-NVQFDFLTVRENLRLFAKIKGILPQEVDK--------------------------------------- 595
Cdd:COG1123 81 RGRRIGMVFQDpMTQLNPVTVGDQIAEALENLGLSRAEARArvlelleavglerrldryphqlsggqrqrvaiamalald 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6005701 596 -EIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS 658
Cdd:COG1123 161 pDLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGP 226
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1265-1474 |
6.73e-18 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 87.58 E-value: 6.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1265 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGggdalefLGYCP----------QENALWPNL 1334
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVD-------LSHVPpyqrpinmmfQSYALFPHM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1335 TVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQ 1414
Cdd:PRK11607 107 TVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6005701 1415 QMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS----IQHLKSKFGKDYL 1474
Cdd:PRK11607 187 RMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEpeeiYEHPTTRYSAEFI 250
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
479-653 |
1.15e-17 |
|
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: 83.41 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 479 AIRIRNVTKEYKgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMaDLENLSK 558
Cdd:cd03245 2 RIEFRNVSFSYP--NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQL-DPADLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 559 LTGVCPQSNVQFdFLTVRENLRLF------------AKIKGILP-------------------------QEV-------- 593
Cdd:cd03245 79 NIGYVPQDVTLF-YGTLRDNITLGapladderilraAELAGVTDfvnkhpngldlqigergrglsggqrQAValaralln 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 594 DKEIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEADiLADRKVFLSQGKL 653
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLD-LVDRIIVMDSGRI 216
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1258-1411 |
1.35e-17 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 83.56 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1258 SKR--KNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDALEFL----GYCPQE 1327
Cdd:COG2884 8 SKRypGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdlsRLKRREIPYLrrriGVVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1328 NALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTG 1407
Cdd:COG2884 88 FRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGN 167
|
....
gi 6005701 1408 MDPE 1411
Cdd:COG2884 168 LDPE 171
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
481-657 |
1.70e-17 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 82.97 E-value: 1.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 481 RIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMadlenlSKLT 560
Cdd:cd03235 1 EVEDLTVSYGGHP----VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE------RKRI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 561 GVCPQS-NVQFDF-LTVRE--NLRLFAKIKGILP----------------------------------QEV--------D 594
Cdd:cd03235 71 GYVPQRrSIDRDFpISVRDvvLMGLYGHKGLFRRlskadkakvdealervglseladrqigelsggqqQRVllaralvqD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6005701 595 KEIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRkVFLSQGKLKCAG 657
Cdd:cd03235 151 PDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYFDR-VLLLNRTVVASG 213
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
480-674 |
1.74e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 84.83 E-value: 1.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEY-KGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIynNKLSEMAD-----L 553
Cdd:PRK13646 3 IRFDNVSYTYqKGTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTV--DDITITHKtkdkyI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 554 ENLSKLTGVC---PQS----------------NVQFDFLTVRE--------------------------NLRLFAkIKGI 588
Cdd:PRK13646 81 RPVRKRIGMVfqfPESqlfedtvereiifgpkNFKMNLDEVKNyahrllmdlgfsrdvmsqspfqmsggQMRKIA-IVSI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 589 LPqeVDKEIFLLDEPTAGLDPFSRHQVWNLLKERKTD--RVILFSTQFMDEADILADRKVFLSQGKL--KCAGSSLFLKK 664
Cdd:PRK13646 160 LA--MNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDenKTIILVSHDMNEVARYADEVIVMKEGSIvsQTSPKELFKDK 237
|
250
....*....|
gi 6005701 665 KWGIGYHLSL 674
Cdd:PRK13646 238 KKLADWHIGL 247
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1257-1461 |
1.74e-17 |
|
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: 83.50 E-value: 1.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1257 FSKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsGGGDALEF--------LGYCPQEN 1328
Cdd:cd03295 8 KRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFI---DGEDIREQdpvelrrkIGYVIQQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1329 ALWPNLTVRQHLevyAAVKGLRKGDAEVAITRLVDALKLQDQlkSPVK-------TLSEGIKRKLCFVLSILGNPSVVLL 1401
Cdd:cd03295 85 GLFPHMTVEENI---ALVPKLLKWPKEKIRERADELLALVGL--DPAEfadryphELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1402 DEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1461
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGT 219
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
480-653 |
3.00e-17 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 83.12 E-value: 3.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYkgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEM--ADLENLS 557
Cdd:TIGR02315 2 LEVENLSKVY---PNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLrgKKLRKLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 558 KLTGVCPQSNVQFDFLTVRENL---RLFAK--IKGILPQ--EVDKE---------------------------------- 596
Cdd:TIGR02315 79 RRIGMIFQHYNLIERLTVLENVlhgRLGYKptWRSLLGRfsEEDKEralsalervgladkayqradqlsggqqqrvaiar 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6005701 597 -------IFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKL 653
Cdd:TIGR02315 159 alaqqpdLILADEPIASLDPKTSKQVMDYLKRinKEDGITVIINLHQVDLAKKYADRIVGLKAGEI 224
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1265-1456 |
3.19e-17 |
|
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: 84.72 E-value: 3.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1265 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKP---TAGQVLLKG----SGGGDALE-----FLGYCPQE--NAL 1330
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGedllKLSEKELRkirgrEIQMIFQDpmTSL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1331 WPNLTVRQHL-EVYAAVKGLRKGDAEvaiTRLVDALKLQdQLKSPVKT-------LSEGIKRKLCFVLSILGNPSVVLLD 1402
Cdd:COG0444 100 NPVMTVGDQIaEPLRIHGGLSKAEAR---ERAIELLERV-GLPDPERRldrypheLSGGMRQRVMIARALALEPKLLIAD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6005701 1403 EPSTGMDPEGQQQmwqaIRATFR--NTERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1456
Cdd:COG0444 176 EPTTALDVTIQAQ----ILNLLKdlQRELGLaiLFITHDLGVVAEIADRVAVMYAGRI 229
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1269-1460 |
3.87e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 85.66 E-value: 3.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1269 VSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsgGGDALEFL---------GYCPQENALWPNLTVRQ- 1338
Cdd:PRK09536 22 VDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLV----AGDDVEALsaraasrrvASVPQDTSLSFEFDVRQv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1339 -------HLEVYAAVKGLRKGDAEVAITRlVDALKLQDQlksPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1411
Cdd:PRK09536 98 vemgrtpHRSRFDTWTETDRAAVERAMER-TGVAQFADR---PVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDIN 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6005701 1412 GQQQMWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1460
Cdd:PRK09536 174 HQVRTLELVR-RLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
476-658 |
4.60e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 83.21 E-value: 4.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 476 GKEAIRIRNVTKEYK--GKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADL 553
Cdd:PRK13633 1 MNEMIKCKNVSYKYEsnEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 554 ENLSKLTGVCPQSN--------VQFDFLTVRENLrlfakikGILPQEVDK------------------------------ 595
Cdd:PRK13633 81 WDIRNKAGMVFQNPdnqivatiVEEDVAFGPENL-------GIPPEEIRErvdeslkkvgmyeyrrhaphllsggqkqrv 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6005701 596 ----------EIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEAdILADRKVFLSQGKLKCAGS 658
Cdd:PRK13633 154 aiagilamrpECIIFDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGT 227
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
225-418 |
5.17e-17 |
|
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: 84.36 E-value: 5.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 225 YLFSCIISFSSFIYYASV--NVTRER-KRMKALMTMMGLRDSAFWLSWGLLYAGFIFIMALFLALVIRSTqFIILSGFMV 301
Cdd:pfam12698 162 YLVGLILMIIILIGAAIIavSIVEEKeSRIKERLLVSGVSPLQYWLGKILGDFLVGLLQLLIILLLLFGI-GIPFGNLGL 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 302 VFSLFLLYGLSLVALAFLMSILVKKSFLTGLVVFLLT-VFWGCLGFTSLYRHLPASLEWILSLLSPFAFMLGMAQLLHld 380
Cdd:pfam12698 241 LLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVIlLLSGFFGGLFPLEDPPSFLQWIFSIIPFFSPIDGLLRLIY-- 318
|
170 180 190
....*....|....*....|....*....|....*...
gi 6005701 381 YDLNSNAFPhpsdgsNLIvatnfMLAFDTCLYLALAIY 418
Cdd:pfam12698 319 GDSLWEIAP------SLI-----ILLLFAVVLLLLALL 345
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
480-658 |
5.56e-17 |
|
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: 81.90 E-value: 5.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNklsEMADLENLSKL 559
Cdd:cd03300 1 IELENVSKFYGGFV----ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGK---DITNLPPHKRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 560 TGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEI----------------------------------------FL 599
Cdd:cd03300 74 VNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVaealdlvqlegyanrkpsqlsggqqqrvaiaralvnepkvLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6005701 600 LDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS 658
Cdd:cd03300 154 LDEPLGALDLKLRKDMQLELKRlqKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1229-1454 |
5.61e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 86.26 E-value: 5.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1229 LNSTNFDEKPVIIASCLRKEYAGKR--KGcfskrknkiatrnVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQ 1306
Cdd:PRK15439 1 MQTSDTTAPPLLCARSISKQYSGVEvlKG-------------IDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1307 VLLKGS-----GGGDALEFLGY-CPQENALWPNLTVRQHLEVyaavkGL-RKGDAEVAITRLVDALKLQDQLKSPVKTLs 1379
Cdd:PRK15439 68 LEIGGNpcarlTPAKAHQLGIYlVPQEPLLFPNLSVKENILF-----GLpKRQASMQKMKQLLAALGCQLDLDSSAGSL- 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6005701 1380 EGIKRKLCFVL-SILGNPSVVLLDEPSTGMDPEGQQQMWQAIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSG 1454
Cdd:PRK15439 142 EVADRQIVEILrGLMRDSRILILDEPTASLTPAETERLFSRIRE-LLAQGVGIVFISHKLPEIRQLADRISVMRDG 216
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
479-658 |
6.38e-17 |
|
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: 82.00 E-value: 6.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 479 AIRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLEnlsK 558
Cdd:cd03296 2 SIEVRNVSKRFGDFV----ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE---R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 559 LTGVCPQSNVQFDFLTVRENL----------------RLFAKIKGIL------------PQE----------------VD 594
Cdd:cd03296 75 NVGFVFQHYALFRHMTVFDNVafglrvkprserppeaEIRAKVHELLklvqldwladryPAQlsggqrqrvalaralaVE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6005701 595 KEIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS 658
Cdd:cd03296 155 PKVLLLDEPFGALDAKVRKELRRWLRRlhDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1267-1456 |
6.38e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 85.84 E-value: 6.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1267 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-----SGGGDALEF-LGYCP---QENALWPNLTVR 1337
Cdd:COG1129 269 RDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpvriRSPRDAIRAgIAYVPedrKGEGLVLDLSIR 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1338 Q-----HLEVYAAVKGLRKGDAEVAITRLVDALKL----QDQlksPVKTLSEGIKRKLcfVLS--ILGNPSVVLLDEPST 1406
Cdd:COG1129 349 EnitlaSLDRLSRGGLLDRRRERALAEEYIKRLRIktpsPEQ---PVGNLSGGNQQKV--VLAkwLATDPKVLILDEPTR 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6005701 1407 GMDPEGQQQMWQAIRatfRNTERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1456
Cdd:COG1129 424 GIDVGAKAEIYRLIR---ELAAEGKavIVISSELPELLGLSDRILVMREGRI 472
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
480-658 |
6.73e-17 |
|
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: 81.71 E-value: 6.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGkpdkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVtIYNNKlsemadlenlsKL 559
Cdd:cd03219 1 LEVRGLTKRFGG----LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSV-LFDGE-----------DI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 560 TGVCP------------QsNVQ-FDFLTVRENLRL-----------FAKIKGILPQEVDK-------------------- 595
Cdd:cd03219 65 TGLPPheiarlgigrtfQ-IPRlFPELTVLENVMVaaqartgsgllLARARREEREARERaeellervgladladrpage 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 596 -------------------EIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILfstqfMDEADI-----LADRKVFLSQ 650
Cdd:cd03219 144 lsygqqrrleiaralatdpKLLLLDEPAAGLNPEETEELAELIRElRERGITVL-----LVEHDMdvvmsLADRVTVLDQ 218
|
....*...
gi 6005701 651 GKLKCAGS 658
Cdd:cd03219 219 GRVIAEGT 226
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1273-1448 |
1.04e-16 |
|
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: 81.69 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1273 VRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsgggdALEFLGYCPQENALWPNLTVRQHLevYAAVKGlrKG 1352
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI-------ELDTVSYKPQYIKADYEGTVRDLL--SSITKD--FY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1353 DAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGAL 1432
Cdd:cd03237 91 THPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAF 170
|
170
....*....|....*.
gi 6005701 1433 LTTHYMAEAEAVCDRV 1448
Cdd:cd03237 171 VVEHDIIMIDYLADRL 186
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1265-1456 |
1.21e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 84.96 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1265 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-----SGGGDALEfLG----YcpQENALWPNLT 1335
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGqemrfASTTAALA-AGvaiiY--QELHLVPEMT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1336 VRQ-----HLEVYAAVkgLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDP 1410
Cdd:PRK11288 96 VAEnlylgQLPHKGGI--VNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6005701 1411 EGQQQMWQAIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1456
Cdd:PRK11288 174 REIEQLFRVIRE-LRAEGRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
480-653 |
1.24e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 82.05 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYkgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTI------YNNKlsemaDL 553
Cdd:PRK13639 2 LETRDLKYSY---PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIkgepikYDKK-----SL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 554 ENLSKLTGVCPQS------------NVQFDFLT-----------VRENLRL-----FAK---------------IKGILP 590
Cdd:PRK13639 74 LEVRKTVGIVFQNpddqlfaptveeDVAFGPLNlglskeevekrVKEALKAvgmegFENkpphhlsggqkkrvaIAGILA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6005701 591 QEvdKEIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKL 653
Cdd:PRK13639 154 MK--PEIIVLDEPTSGLDPMGASQIMKLLYDlNKEGITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
480-664 |
1.29e-16 |
|
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: 80.73 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEY-KGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMaDLENLSK 558
Cdd:cd03254 3 IEFENVNFSYdEKKP----VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDI-SRKSLRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 559 LTGVCPQSnvqfDFL---TVRENLRLF------------AKIKGI------LPQEVDKE--------------------- 596
Cdd:cd03254 78 MIGVVLQD----TFLfsgTIMENIRLGrpnatdeevieaAKEAGAhdfimkLPNGYDTVlgenggnlsqgerqllaiara 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 597 ------IFLLDEPTAGLDPFSRHQVWN---LLKERKTDRVI---LFSTQFmdeadilADRKVFLSQGKLKCAGS--SLFL 662
Cdd:cd03254 154 mlrdpkILILDEATSNIDTETEKLIQEaleKLMKGRTSIIIahrLSTIKN-------ADKILVLDDGKIIEEGThdELLA 226
|
..
gi 6005701 663 KK 664
Cdd:cd03254 227 KK 228
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
455-648 |
1.36e-16 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 85.03 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 455 DEMDADPSFHDSF---EQAPPEFQGKE--------AIRIRNVTKEYkgkPDKIEALKDLVFDIYEGQITAILGHSGAGKS 523
Cdd:TIGR02857 286 ARADGVAAAEALFavlDAAPRPLAGKApvtaapasSLEFSGVSVAY---PGRRPALRPVSFTVPPGERVALVGPSGAGKS 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 524 TLLNILSGLSVPTKGSVTIYNNKLSEmADLENLSKLTGVCPQSNVQFDfLTVRENLRLF------AKIKGI--------- 588
Cdd:TIGR02857 363 TLLNLLLGFVDPTEGSIAVNGVPLAD-ADADSWRDQIAWVPQHPFLFA-GTIAENIRLArpdasdAEIREAleragldef 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 589 ---LPQEVDKEI---------------------------FLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQfmDEA 638
Cdd:TIGR02857 441 vaaLPQGLDTPIgeggaglsggqaqrlalaraflrdaplLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTH--RLA 518
|
250
....*....|.
gi 6005701 639 DI-LADRKVFL 648
Cdd:TIGR02857 519 LAaLADRIVVL 529
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1263-1462 |
1.39e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 82.02 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1263 KIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG---SGGGDALEFL----GYCPQ--ENALWPN 1333
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvdiTDKKVKLSDIrkkvGLVFQypEYQLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1334 lTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQL---KSPVKtLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDP 1410
Cdd:PRK13637 100 -TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEDykdKSPFE-LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6005701 1411 EGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSI 1462
Cdd:PRK13637 178 KGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1269-1436 |
1.43e-16 |
|
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: 79.84 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1269 VSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDAL----EFLGYCPQENALWPNLTVRQHLEVYA 1344
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRdsiaRGLLYLGHAPGIKTTLSVLENLRFWH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1345 AV---KGLRKGDAEVAITRLVDAlklqdqlksPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIR 1421
Cdd:cd03231 99 ADhsdEQVEEALARVGLNGFEDR---------PVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMA 169
|
170
....*....|....*..
gi 6005701 1422 AtfrNTERG--ALLTTH 1436
Cdd:cd03231 170 G---HCARGgmVVLTTH 183
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1259-1463 |
1.46e-16 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 81.32 E-value: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1259 KRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsgGGDALEflGYCPQENALwpNLTV-R 1337
Cdd:COG4559 10 RLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRL----NGRPLA--AWSPWELAR--RRAVlP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1338 QH---------LEVYA--AVKGLRKGDAEVAITR----LVDALKLQDQLkspVKTLSEGIK------RKLCFVL-SILGN 1395
Cdd:COG4559 82 QHsslafpftvEEVVAlgRAPHGSSAAQDRQIVRealaLVGLAHLAGRS---YQTLSGGEQqrvqlaRVLAQLWePVDGG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6005701 1396 PSVVLLDEPSTGMDPEGQQQMWQAIRatfRNTERGA--------L-LTTHYmaeaeavCDRVAIMVSGRLRCIGSIQ 1463
Cdd:COG4559 159 PRWLFLDEPTSALDLAHQHAVLRLAR---QLARRGGgvvavlhdLnLAAQY-------ADRILLLHQGRLVAQGTPE 225
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
484-653 |
1.53e-16 |
|
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: 80.39 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 484 NVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLsVP----TKGSVTIYNNKLSEMADLENLSKL 559
Cdd:cd03234 8 DVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGR-VEgggtTSGQILFNGQPRKPDQFQKCVAYV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 560 tgvcPQSNVQFDFLTVRENLRLFA---------------------------------KIKGILPQE-----------VDK 595
Cdd:cd03234 87 ----RQDDILLPGLTVRETLTYTAilrlprkssdairkkrvedvllrdlaltriggnLVKGISGGErrrvsiavqllWDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6005701 596 EIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQfMDEADI--LADRKVFLSQGKL 653
Cdd:cd03234 163 KVLILDEPTSGLDSFTALNLVSTLSQlARRNRIVILTIH-QPRSDLfrLFDRILLLSSGEI 222
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1260-1456 |
2.40e-16 |
|
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: 79.92 E-value: 2.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1260 RKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITG-----DTKPTAGQVLLKG----SGGGDALEF---LGYCPQE 1327
Cdd:cd03260 10 YGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGkdiyDLDVDVLELrrrVGMVFQK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1328 NALWPnLTVRQHLEVYAAVKGLRKGDAEVAITRlvDALK---LQDQLKSPVK--TLSEGIKRKLCFVLSILGNPSVVLLD 1402
Cdd:cd03260 90 PNPFP-GSIYDNVAYGLRLHGIKLKEELDERVE--EALRkaaLWDEVKDRLHalGLSGGQQQRLCLARALANEPEVLLLD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 6005701 1403 EPSTGMDPEGQQQMWQAIRATfrNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1456
Cdd:cd03260 167 EPTSALDPISTAKIEELIAEL--KKEYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
480-653 |
2.47e-16 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 82.16 E-value: 2.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEM--ADLENLS 557
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALseKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 558 KLTGVCPQsnvQFDFL---TVRENLRLFAKIKGILPQEVDK--------------------------------------- 595
Cdd:PRK11153 82 RQIGMIFQ---HFNLLssrTVFDNVALPLELAGTPKAEIKArvtellelvglsdkadrypaqlsggqkqrvaiaralasn 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6005701 596 -EIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKL 653
Cdd:PRK11153 159 pKVLLCDEATSALDPATTRSILELLKDinRELGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1268-1454 |
2.80e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 80.54 E-value: 2.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1268 NVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKgsgggDALEfLGYCPQENALWPN--LTVRQHLEVYAA 1345
Cdd:PRK09544 22 DVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRN-----GKLR-IGYVPQKLYLDTTlpLTVNRFLRLRPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1346 VKglrKGDAEVAITRlVDALKLQDQlksPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFR 1425
Cdd:PRK09544 96 TK---KEDILPALKR-VQAGHLIDA---PMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRR 168
|
170 180 190
....*....|....*....|....*....|....
gi 6005701 1426 NTERGALLTTH----YMAEA-EAVCDRVAIMVSG 1454
Cdd:PRK09544 169 ELDCAVLMVSHdlhlVMAKTdEVLCLNHHICCSG 202
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1273-1456 |
2.99e-16 |
|
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: 79.07 E-value: 2.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1273 VRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDA--------LEFlgycpQENALWPNLTVRQHLEVyA 1344
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAppadrpvsMLF-----QENNLFAHLTVEQNVGL-G 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1345 AVKGLR-----KGDAEVAITRLvdalKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQA 1419
Cdd:cd03298 95 LSPGLKltaedRQAIEVALARV----GLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 6005701 1420 IRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1456
Cdd:cd03298 171 VLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
480-658 |
3.08e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 80.86 E-value: 3.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEY-KGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYN-NKLSEMADLENLS 557
Cdd:PRK13637 3 IKIENLTHIYmEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvDITDKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 558 KLTGVCPQ-------------------SN------------------VQFDFLTVRE---------NLRLFAkIKGILPQ 591
Cdd:PRK13637 83 KKVGLVFQypeyqlfeetiekdiafgpINlglseeeienrvkramniVGLDYEDYKDkspfelsggQKRRVA-IAGVVAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6005701 592 EvdKEIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS 658
Cdd:PRK13637 162 E--PKILILDEPTAGLDPKGRDEILNKIKElhKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGT 228
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
470-653 |
3.24e-16 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 80.47 E-value: 3.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 470 APPEFQGKEAIRIRNVTKEYKGKpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLS--VP---TKGSVT--- 541
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGDK----QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlIPgarVEGEILldg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 542 --IYNNKLsemaDLENLSKLTG-VCPQSNVqfdF-LTVRENLRLFAKIKGI------------------LPQEV-DK--- 595
Cdd:COG1117 78 edIYDPDV----DVVELRRRVGmVFQKPNP---FpKSIYDNVAYGLRLHGIkskseldeiveeslrkaaLWDEVkDRlkk 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 596 -----------------------EIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEADILADRKVFLSQGK 652
Cdd:COG1117 151 salglsggqqqrlciaralavepEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARVSDYTAFFYLGE 230
|
.
gi 6005701 653 L 653
Cdd:COG1117 231 L 231
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1267-1436 |
3.74e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 78.69 E-value: 3.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1267 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDALEFLGYCPQENALWPNLTVRQHLEV 1342
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGepirRQRDEYHQDLLYLGHQPGIKTELTALENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1343 YAAVKGLrkGDAEVAITRLvDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRA 1422
Cdd:PRK13538 98 YQRLHGP--GDDEALWEAL-AQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQ 174
|
170
....*....|....*.
gi 6005701 1423 tfrNTERG--ALLTTH 1436
Cdd:PRK13538 175 ---HAEQGgmVILTTH 187
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1267-1404 |
4.04e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 83.58 E-value: 4.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1267 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSgggdalEFLGYCPQENALWPNLTVRQ-----HLE 1341
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG------LRIGYLPQEPPLDDDLTVLDtvldgDAE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1342 VYAAVKGLRKG---------------------------DAEVAITRLVDALKL-QDQLKSPVKTLSEGIKRK--LCFVLs 1391
Cdd:COG0488 89 LRALEAELEELeaklaepdedlerlaelqeefealggwEAEARAEEILSGLGFpEEDLDRPVSELSGGWRRRvaLARAL- 167
|
170
....*....|...
gi 6005701 1392 iLGNPSVVLLDEP 1404
Cdd:COG0488 168 -LSEPDLLLLDEP 179
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1265-1411 |
4.13e-16 |
|
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: 78.99 E-value: 4.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1265 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSG----GGDALEFL----GYCPQENALWPNLTV 1336
Cdd:cd03292 16 ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDvsdlRGRAIPYLrrkiGVVFQDFRLLPDRNV 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6005701 1337 RQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1411
Cdd:cd03292 96 YENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPD 170
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
479-673 |
5.47e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 80.26 E-value: 5.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 479 AIRIRNVTKEYK-GKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLS 557
Cdd:PRK13641 2 SIKFENVDYIYSpGTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 558 KL---TGVCPQ-SNVQFDFLTVRENLRL----F------AKIKGI-------LPQEV----------------------- 593
Cdd:PRK13641 82 KLrkkVSLVFQfPEAQLFENTVLKDVEFgpknFgfsedeAKEKALkwlkkvgLSEDLiskspfelsggqmrrvaiagvma 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 594 -DKEIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKL--KCAGSSLFLKKKWGIG 669
Cdd:PRK13641 162 yEPEILCLDEPAAGLDPEGRKEMMQLFKDyQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLikHASPKEIFSDKEWLKK 241
|
....
gi 6005701 670 YHLS 673
Cdd:PRK13641 242 HYLD 245
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
480-654 |
6.07e-16 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 78.59 E-value: 6.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGKpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEmADLENLskl 559
Cdd:TIGR03740 1 LETKNLSKRFGKQ----TAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTR-KDLHKI--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 560 tGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDK------------------------------------EIFLLDEP 603
Cdd:TIGR03740 73 -GSLIESPPLYENLTARENLKVHTTLLGLPDSRIDEvlnivdltntgkkkakqfslgmkqrlgiaiallnhpKLLILDEP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6005701 604 TAGLDPFSRHQVWNLLKERKTDRV-ILFSTQFMDEADILADRKVFLSQGKLK 654
Cdd:TIGR03740 152 TNGLDPIGIQELRELIRSFPEQGItVILSSHILSEVQQLADHIGIISEGVLG 203
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1270-1465 |
1.01e-15 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 78.26 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1270 SFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSgggdalEFLGYCP---------QENALWPNLTVRQHl 1340
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQ------DLTALPPaerpvsmlfQENNLFPHLTVAQN- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1341 eVYAAVK-GLRKGDAEVAitRLVDALK---LQDQLKSPVKTLSEG------IKRklCFVLsilGNPsVVLLDEPSTGMDP 1410
Cdd:COG3840 92 -IGLGLRpGLKLTAEQRA--QVEQALErvgLAGLLDRLPGQLSGGqrqrvaLAR--CLVR---KRP-ILLLDEPFSALDP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6005701 1411 EGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL 1465
Cdd:COG3840 163 ALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAAL 217
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1268-1468 |
1.07e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 79.39 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1268 NVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGsgggDALeflgycpQENALWpnlTVRQHLE------ 1341
Cdd:PRK13650 25 DVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG----DLL-------TEENVW---DIRHKIGmvfqnp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1342 ----VYAAVK-----GLR-KG-DAEVAITRLVDALKL---QD-QLKSPVKtLSEGIKRKLCFVLSILGNPSVVLLDEPST 1406
Cdd:PRK13650 91 dnqfVGATVEddvafGLEnKGiPHEEMKERVNEALELvgmQDfKEREPAR-LSGGQKQRVAIAGAVAMRPKIIILDEATS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6005701 1407 GMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAeAVCDRVAIMVSGRLRCIGSIQHLKSK 1468
Cdd:PRK13650 170 MLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
477-657 |
1.11e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 79.29 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 477 KEAIRIRNVTKEYKGkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSE------- 549
Cdd:PRK13635 3 EEIIRVEHISFRYPD--AATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEetvwdvr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 550 ------------------MAD-----LEN--------LSKLTGVCPQSNVQfDFLTvRENLRLFA------KIKGILPQE 592
Cdd:PRK13635 81 rqvgmvfqnpdnqfvgatVQDdvafgLENigvpreemVERVDQALRQVGME-DFLN-REPHRLSGgqkqrvAIAGVLALQ 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6005701 593 VDkeIFLLDEPTAGLDPFSRHQVWN---LLKERKTDRVILFsTQFMDEAdILADRKVFLSQGKLKCAG 657
Cdd:PRK13635 159 PD--IIILDEATSMLDPRGRREVLEtvrQLKEQKGITVLSI-THDLDEA-AQADRVIVMNKGEILEEG 222
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1257-1470 |
1.18e-15 |
|
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: 78.04 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1257 FSKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDA-----LEFLGYCPQENALW 1331
Cdd:cd03254 10 FSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIsrkslRSMIGVVLQDTFLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1332 PNlTVRQHL----------EVYAAVKglrkgdaEVAITRLVDALK--LQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVV 1399
Cdd:cd03254 90 SG-TIMENIrlgrpnatdeEVIEAAK-------EAGAHDFIMKLPngYDTVLGENGGNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6005701 1400 LLDEPSTGMDPEGQQQMWQAIRATFRNteRGALLTTHYMAEAEAVcDRVAIMVSGRLRCIGSIQHLKSKFG 1470
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKLMKG--RTSIIIAHRLSTIKNA-DKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1261-1456 |
1.29e-15 |
|
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: 76.58 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1261 KNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG---SGGGDAL-EFLGYCPQENALWpNLTV 1336
Cdd:cd03247 13 QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGvpvSDLEKALsSLISVLNQRPYLF-DTTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1337 RQHLevyaavkGLRkgdaevaitrlvdalklqdqlkspvktLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQM 1416
Cdd:cd03247 92 RNNL-------GRR---------------------------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQL 137
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 6005701 1417 WQAIRATFRNteRGALLTTHYMAEAEAVcDRVAIMVSGRL 1456
Cdd:cd03247 138 LSLIFEVLKD--KTLIWITHHLTGIEHM-DKILFLENGKI 174
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1261-1456 |
1.36e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 78.98 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1261 KNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDaleflgycpqENALWpnlTVRQHL 1340
Cdd:PRK13633 21 TEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSD----------EENLW---DIRNKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1341 ---------EVYAAVKglrkgDAEVAI-------------TRLVDALK---LQDQLKSPVKTLSEGIKRKLCFVLSILGN 1395
Cdd:PRK13633 88 gmvfqnpdnQIVATIV-----EEDVAFgpenlgippeeirERVDESLKkvgMYEYRRHAPHLLSGGQKQRVAIAGILAMR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6005701 1396 PSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAeAVCDRVAIMVSGRL 1456
Cdd:PRK13633 163 PECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEA-VEADRIIVMDSGKV 222
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1265-1474 |
1.42e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 82.48 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1265 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQ--VLlkgsgGGD--------------AleflgYCPQ-- 1326
Cdd:NF033858 16 ALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRveVL-----GGDmadarhrravcpriA-----YMPQgl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1327 -ENaLWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRK--LCFVLsiLGNPSVVLLDE 1403
Cdd:NF033858 86 gKN-LYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKlgLCCAL--IHDPDLLILDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6005701 1404 PSTGMDPEGQQQMWQ---AIRAtfrntERGA---LLTTHYMAEAEAvCDRVAIMVSGRLRCIGSIQHLKSKFGKDYL 1474
Cdd:NF033858 163 PTTGVDPLSRRQFWElidRIRA-----ERPGmsvLVATAYMEEAER-FDWLVAMDAGRVLATGTPAELLARTGADTL 233
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1268-1456 |
1.43e-15 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 78.13 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1268 NVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGS--------GGGDALEF---LGYCPQENALWPNLTV 1336
Cdd:COG4161 20 DINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdfsqkpSEKAIRLLrqkVGMVFQQYNLWPHLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1337 RQHL-EVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQ 1415
Cdd:COG4161 100 MENLiEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQ 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 6005701 1416 MWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1456
Cdd:COG4161 180 VVEIIR-ELSQTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1252-1508 |
1.45e-15 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 81.86 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1252 KRKGCFSKRKN---KIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDALeflgycpqEN 1328
Cdd:PRK13545 23 KLKDLFFRSKDgeyHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAI--------SS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1329 ALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGM 1408
Cdd:PRK13545 95 GLNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1409 DPEGQQQMWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFGkDYLLEMKVKNLAQVEPL 1488
Cdd:PRK13545 175 DQTFTKKCLDKMN-EFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYD-EFLKKYNQMSVEERKDF 252
|
250 260
....*....|....*....|
gi 6005701 1489 HAEILRLFPQAARQERYSSL 1508
Cdd:PRK13545 253 REEQISQFQHGLLQEDQTGR 272
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1262-1455 |
1.55e-15 |
|
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: 77.99 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1262 NKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDALEFL----GYCPQENALWPN 1333
Cdd:cd03256 13 GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGtdinKLKGKALRQLrrqiGMIFQQFNLIER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1334 LTVRQH-----LEVYAAVKGLR----KGDAEVAItRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEP 1404
Cdd:cd03256 93 LSVLENvlsgrLGRRSTWRSLFglfpKEEKQRAL-AALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6005701 1405 STGMDPEGQQQMWQAIRATfrNTERG--ALLTTHYMAEAEAVCDRVAIMVSGR 1455
Cdd:cd03256 172 VASLDPASSRQVMDLLKRI--NREEGitVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
478-657 |
2.41e-15 |
|
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: 77.43 E-value: 2.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 478 EAIRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKG-SVTIYNNKLSEmADLENL 556
Cdd:COG1119 2 PLLELRNVTVRRGGKT----ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGG-EDVWEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 557 SKLTGVCpqSNVQFDFLTVRENLR------LFAKIkGiLPQEVDK----------------------------------- 595
Cdd:COG1119 77 RKRIGLV--SPALQLRFPRDETVLdvvlsgFFDSI-G-LYREPTDeqrerarellellglahladrpfgtlsqgeqrrvl 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6005701 596 ---------EIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEadILA--DRKVFLSQGKLKCAG 657
Cdd:COG1119 153 iaralvkdpELLILDEPTAGLDLGARELLLALLDKlaAEGAPTLVLVTHHVEE--IPPgiTHVLLLKDGRVVAAG 225
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
480-665 |
2.98e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 77.97 E-value: 2.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYkgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKG--------------------- 538
Cdd:PRK13636 6 LKVEELNYNY---SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGrilfdgkpidysrkglmklre 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 539 --------------SVTIY--------NNKLSE---MADLENLSKLTGVCPQSNVQFDFLTVRENLRlfAKIKGILPQEv 593
Cdd:PRK13636 83 svgmvfqdpdnqlfSASVYqdvsfgavNLKLPEdevRKRVDNALKRTGIEHLKDKPTHCLSFGQKKR--VAIAGVLVME- 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6005701 594 dKEIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAG--SSLFLKKK 665
Cdd:PRK13636 160 -PKVLVLDEPTAGLDPMGVSEIMKLLVEmqKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGnpKEVFAEKE 234
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1229-1461 |
2.99e-15 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 79.61 E-value: 2.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1229 LNSTNFDEKPVIIASCLRKEYAGKrkgcfskrknkIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVL 1308
Cdd:PRK09452 4 LNKQPSSLSPLVELRGISKSFDGK-----------EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1309 LKGsgggdalEFLGYCPQEN----------ALWPNLTVRQHLEVyaavkGLR---KGDAEVAiTRLVDALK---LQDQLK 1372
Cdd:PRK09452 73 LDG-------QDITHVPAENrhvntvfqsyALFPHMTVFENVAF-----GLRmqkTPAAEIT-PRVMEALRmvqLEEFAQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1373 SPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMV 1452
Cdd:PRK09452 140 RKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMR 219
|
....*....
gi 6005701 1453 SGRLRCIGS 1461
Cdd:PRK09452 220 DGRIEQDGT 228
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1263-1468 |
4.08e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 77.56 E-value: 4.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1263 KIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-----SGGGDALEFL----GYCPQ--ENALW 1331
Cdd:PRK13641 20 KKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpETGNKNLKKLrkkvSLVFQfpEAQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1332 PNlTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQL--KSPVKtLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMD 1409
Cdd:PRK13641 100 EN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLisKSPFE-LSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6005701 1410 PEGQQQMWQairaTFRNTERGA---LLTTHYMAEAEAVCDRVAIMVSGRLrcigsIQHLKSK 1468
Cdd:PRK13641 178 PEGRKEMMQ----LFKDYQKAGhtvILVTHNMDDVAEYADDVLVLEHGKL-----IKHASPK 230
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1264-1455 |
4.36e-15 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 76.95 E-value: 4.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1264 IATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSgggdalEFLGYCPQENA-------------- 1329
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQ------HIEGLPGHQIArmgvvrtfqhvrlf 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1330 ----LWPNLTVRQHLEVYAAV-------KGLRKGDAEvAITRL---VDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGN 1395
Cdd:PRK11300 93 remtVIENLLVAQHQQLKTGLfsgllktPAFRRAESE-ALDRAatwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQ 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1396 PSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1455
Cdd:PRK11300 172 PEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1265-1463 |
5.47e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 79.83 E-value: 5.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1265 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSG-----GGDALEF-LGYCPQENALWPNLTVRQ 1338
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINynkldHKLAAQLgIGIIYQELSVIDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1339 HLEV----YAAVKGLRKGD---AEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1411
Cdd:PRK09700 100 NLYIgrhlTKKVCGVNIIDwreMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6005701 1412 GQQQMWqAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQ 1463
Cdd:PRK09700 180 EVDYLF-LIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVS 230
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
480-653 |
7.17e-15 |
|
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: 75.14 E-value: 7.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYkgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMAD--LENLS 557
Cdd:cd03292 1 IEFINVTKTY---PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGraIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 558 KLTGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKE----------------------------------------I 597
Cdd:cd03292 78 RKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRvpaalelvglshkhralpaelsggeqqrvaiaraivnsptI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 6005701 598 FLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKL 653
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKiNKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
495-653 |
8.41e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 75.97 E-value: 8.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 495 KIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLS-----VPTKGSVtIYN--NKLSEMADLENLSKLTGVCPQSN 567
Cdd:PRK14239 17 KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNdlnpeVTITGSI-VYNghNIYSPRTDTVDLRKEIGMVFQQP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 568 VQFDFlTVREN----LRLFA-KIKGILPQEVDK----------------------------------------EIFLLDE 602
Cdd:PRK14239 96 NPFPM-SIYENvvygLRLKGiKDKQVLDEAVEKslkgasiwdevkdrlhdsalglsggqqqrvciarvlatspKIILLDE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6005701 603 PTAGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEADILADRKVFLSQGKL 653
Cdd:PRK14239 175 PTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDL 225
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1265-1451 |
9.30e-15 |
|
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: 79.25 E-value: 9.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1265 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsGGGDALEF--------LGYCPQENALWPNlTV 1336
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAV---NGVPLADAdadswrdqIAWVPQHPFLFAG-TI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1337 RQHLEVY---AAVKGLRKGDAEVAITRLVDALK--LQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1411
Cdd:TIGR02857 413 AENIRLArpdASDAEIREALERAGLDEFVAALPqgLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAE 492
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 6005701 1412 GQQQMWQAIRATFRNteRGALLTTHYMAEAEAvCDRVAIM 1451
Cdd:TIGR02857 493 TEAEVLEALRALAQG--RTVLLVTHRLALAAL-ADRIVVL 529
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
480-652 |
9.75e-15 |
|
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: 72.87 E-value: 9.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNklSEMADLENLSKl 559
Cdd:cd03221 1 IELENLSKTYGGKL----LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST--VKIGYFEQLSG- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 560 tGvcpqsnvqfdfltvrENLRL-FAKikgILPQEVDkeIFLLDEPTAGLDPFSRHQVWNLLKE-RKTdrVILFS--TQFM 635
Cdd:cd03221 74 -G---------------EKMRLaLAK---LLLENPN--LLLLDEPTNHLDLESIEALEEALKEyPGT--VILVShdRYFL 130
|
170
....*....|....*..
gi 6005701 636 DEadiLADRKVFLSQGK 652
Cdd:cd03221 131 DQ---VATKIIELEDGK 144
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1245-1456 |
1.07e-14 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 77.53 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1245 LRKEYAGKRKGcfskrknKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsgGGDALEFLGyc 1324
Cdd:PRK11153 7 ISKVFPQGGRT-------IHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLV----DGQDLTALS-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1325 pqENALwpNLTVR------QHLE------VYAAV------KGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKL 1386
Cdd:PRK11153 74 --EKEL--RKARRqigmifQHFNllssrtVFDNValplelAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6005701 1387 CFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATfrNTERG--ALLTTHYMAEAEAVCDRVAIMVSGRL 1456
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALDPATTRSILELLKDI--NRELGltIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
480-577 |
1.52e-14 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 75.12 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADlENLSKL 559
Cdd:COG4604 2 IEIKNVSKRYGGKV----VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPS-RELAKR 76
|
90
....*....|....*...
gi 6005701 560 TGVCPQSNVQFDFLTVRE 577
Cdd:COG4604 77 LAILRQENHINSRLTVRE 94
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1253-1475 |
1.58e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 75.61 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1253 RKGCFSKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-----SGGGDALEFLGYC--- 1324
Cdd:PRK13652 7 RDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGepitkENIREVRKFVGLVfqn 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1325 PQENALWPnlTVRQHLEVYAAVKGLrkgDAEVAITRLVDALK---LQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLL 1401
Cdd:PRK13652 87 PDDQIFSP--TVEQDIAFGPINLGL---DEETVAHRVSSALHmlgLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6005701 1402 DEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLkskFGKDYLL 1475
Cdd:PRK13652 162 DEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI---FLQPDLL 232
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
480-628 |
1.63e-14 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 73.02 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEmADLENLSKL 559
Cdd:cd03246 1 LEVENVSFRYPG--AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQ-WDPNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 560 TGVCPQSNVQFDFlTVRENlrlfakikgILP----QEV--------DKEIFLLDEPTAGLDPFSRHQVWNL---LKERKT 624
Cdd:cd03246 78 VGYLPQDDELFSG-SIAEN---------ILSggqrQRLglaralygNPRILVLDEPNSHLDVEGERALNQAiaaLKAAGA 147
|
....
gi 6005701 625 DRVI 628
Cdd:cd03246 148 TRIV 151
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
480-648 |
1.83e-14 |
|
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: 74.50 E-value: 1.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLSKL 559
Cdd:cd03218 1 LRAENLSKRYGKRK----VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 560 TGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEI----------------------------------------FL 599
Cdd:cd03218 77 IGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLeelleefhithlrkskasslsggerrrveiaralatnpkfLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6005701 600 LDEPTAGLDPFSRHQVWNL---LKERK----------------TDRV-ILFSTQFMDE---ADILAD---RKVFL 648
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIikiLKDRGigvlitdhnvretlsiTDRAyIIYEGKVLAEgtpEEIAANelvRKVYL 231
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1246-1471 |
1.88e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 78.55 E-value: 1.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1246 RKEYAGKRKGCFSKRKN-KIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKP---TAGQVLLKGSGGGdaLEFL 1321
Cdd:TIGR00955 20 WKQLVSRLRGCFCRERPrKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPID--AKEM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1322 ----GYCPQENALWPNLTVRQHLEVYAAVKGLRKGDAEVAITR---LVDALKLQD------QLKSPVKTLSEGIKRKLCF 1388
Cdd:TIGR00955 98 raisAYVQQDDLFIPTLTVREHLMFQAHLRMPRRVTKKEKRERvdeVLQALGLRKcantriGVPGRVKGLSGGERKRLAF 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1389 VLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRAtFRNTERGALLTTHyMAEAEAVC--DRVAIMVSGRLRCIGSIQHLK 1466
Cdd:TIGR00955 178 ASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKG-LAQKGKTIICTIH-QPSSELFElfDKIILMAEGRVAYLGSPDQAV 255
|
....*
gi 6005701 1467 SKFGK 1471
Cdd:TIGR00955 256 PFFSD 260
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1265-1468 |
2.22e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 75.27 E-value: 2.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1265 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGS-------GGGDALEFLGYCPQ--ENALWpNLT 1335
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpidysrkGLMKLRESVGMVFQdpDNQLF-SAS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1336 VRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQ 1415
Cdd:PRK13636 100 VYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6005701 1416 MWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSK 1468
Cdd:PRK13636 180 IMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
480-652 |
2.26e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 75.12 E-value: 2.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKE-YKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLE---N 555
Cdd:COG1101 2 LELKNLSKTfNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKrakY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 556 LSK-----LTGVCPQsnvqfdfLTVRENLRLFAK-------IKGILPQEVDK---------------------------- 595
Cdd:COG1101 82 IGRvfqdpMMGTAPS-------MTIEENLALAYRrgkrrglRRGLTKKRRELfrellatlglglenrldtkvgllsggqr 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6005701 596 -------------EIFLLDEPTAGLDPFSRHQVWNLlkerkTDRVI-------LFSTQFMDEADILADRKVFLSQGK 652
Cdd:COG1101 155 qalsllmatltkpKLLLLDEHTAALDPKTAALVLEL-----TEKIVeennlttLMVTHNMEQALDYGNRLIMMHEGR 226
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1267-1461 |
2.46e-14 |
|
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: 73.33 E-value: 2.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1267 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITG--DTKPTAGQVLLKGSgggDALEFLgycPQENAlwpnltvrqhlevya 1344
Cdd:cd03217 17 KGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGE---DITDLP---PEERA--------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1345 avkglRKG-----DAEVAITrlvdALKLQDQLKSPVKTLSEGiKRKLCFVLSILG-NPSVVLLDEPSTGMDPEGQQQMWQ 1418
Cdd:cd03217 76 -----RLGiflafQYPPEIP----GVKNADFLRYVNEGFSGG-EKKRNEILQLLLlEPDLAILDEPDSGLDIDALRLVAE 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 6005701 1419 AIRaTFRNTERGALLTTHYMAEAEAV-CDRVAIMVSGRLRCIGS 1461
Cdd:cd03217 146 VIN-KLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGD 188
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
499-651 |
2.48e-14 |
|
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: 74.04 E-value: 2.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 499 LKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSE-----MADLENLSKL-------------T 560
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEpgpdrMVVFQNYSLLpwltvrenialavD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 561 GVCPQSNVQFDFLTVRENLRLF----------AKIKGILPQEV--------DKEIFLLDEPTAGLDPFSRHQVWN-LLKE 621
Cdd:TIGR01184 81 RVLPDLSKSERRAIVEEHIALVglteaadkrpGQLSGGMKQRVaiaralsiRPKVLLLDEPFGALDALTRGNLQEeLMQI 160
|
170 180 190
....*....|....*....|....*....|.
gi 6005701 622 RKTDRV-ILFSTQFMDEADILADRKVFLSQG 651
Cdd:TIGR01184 161 WEEHRVtVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1267-1475 |
2.87e-14 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 74.06 E-value: 2.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1267 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDA-LEFL----GYCPQENALWpNLTVRQHLE 1341
Cdd:cd03252 19 DNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALAdPAWLrrqvGVVLQENVLF-NRSIRDNIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1342 VYAAVKGLRKgdaEVAITRLVDALKLQDQLKSPVKT--------LSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQ 1413
Cdd:cd03252 98 LADPGMSMER---VIEAAKLAGAHDFISELPEGYDTivgeqgagLSGGQRQRIAIARALIHNPRILIFDEATSALDYESE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6005701 1414 QQMWQAIRATFRNteRGALLTTHYMAEAEAVcDRVAIMVSGRLRCIGSIQHLKSKFGKDYLL 1475
Cdd:cd03252 175 HAIMRNMHDICAG--RTVIIIAHRLSTVKNA-DRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
479-657 |
2.99e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 74.77 E-value: 2.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 479 AIRIRNVTKEYKgkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLSK 558
Cdd:PRK13647 4 IIEVEDLHFRYK---DGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 559 LTGVCPQSNVQFDFLTVRE-------NLRLFAK-----------------------------------IKGILPqeVDKE 596
Cdd:PRK13647 81 VGLVFQDPDDQVFSSTVWDdvafgpvNMGLDKDeverrveealkavrmwdfrdkppyhlsygqkkrvaIAGVLA--MDPD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6005701 597 IFLLDEPTAGLDPFSRHQV----WNLLKERKTdrvILFSTQFMDEADILADRKVFLSQGKLKCAG 657
Cdd:PRK13647 159 VIVLDEPMAYLDPRGQETLmeilDRLHNQGKT---VIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
480-658 |
3.82e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 74.77 E-value: 3.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYK-GKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYN---NKLSEMADLEN 555
Cdd:PRK13643 2 IKFEKVNYTYQpNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 556 LSKLTGVC---PQS---------NVQF---DFLTVRENLRLFA-----------------------------KIKGILPQ 591
Cdd:PRK13643 82 VRKKVGVVfqfPESqlfeetvlkDVAFgpqNFGIPKEKAEKIAaeklemvgladefwekspfelsggqmrrvAIAGILAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6005701 592 EvdKEIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS 658
Cdd:PRK13643 162 E--PEVLVLDEPTAGLDPKARIEMMQLFESiHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGT 227
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1265-1456 |
3.91e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 74.34 E-value: 3.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1265 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGS----GGGDALEF---LGYC---PQENALWPnl 1334
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpikyDKKSLLEVrktVGIVfqnPDDQLFAP-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1335 TVRQHLEVYAAVKGLRKGDAEvaiTRLVDALK---LQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1411
Cdd:PRK13639 95 TVEEDVAFGPLNLGLSKEEVE---KRVKEALKavgMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPM 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 6005701 1412 GQQQMwqaIRATFRNTERG--ALLTTHYMAEAEAVCDRVAIMVSGRL 1456
Cdd:PRK13639 172 GASQI---MKLLYDLNKEGitIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1264-1474 |
8.54e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 75.45 E-value: 8.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1264 IATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG---SGGGDA------LEFLGYCPQENALWPNL 1334
Cdd:PRK10070 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAelrevrRKKIAMVFQSFALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1335 TVRQHLEVYAAVKGLrkgDAEVAITRLVDALK---LQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1411
Cdd:PRK10070 122 TVLDNTAFGMELAGI---NAEERREKALDALRqvgLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6005701 1412 GQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFGKDYL 1474
Cdd:PRK10070 199 IRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYV 261
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1259-1484 |
9.90e-14 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 73.31 E-value: 9.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1259 KRKNK--IATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDALeflgycpqeNA-LWPNLT 1335
Cdd:PRK13546 31 KHKNKtfFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAI---------SAgLSGQLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1336 VRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQ 1415
Cdd:PRK13546 102 GIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQK 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6005701 1416 MWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFgKDYLLEMKVKNLAQ 1484
Cdd:PRK13546 182 CLDKIY-EFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKY-EAFLNDFKKKSKAE 248
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1260-1459 |
1.06e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.59 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1260 RKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-----SGGGDALE----FLGYCPQENAL 1330
Cdd:PRK09700 273 SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGkdispRSPLDAVKkgmaYITESRRDNGF 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1331 WPNLTVRQHLEVYAAVKGLRKGDA-----EVAITRLVDALKLQDQLKSP-----VKTLSEGIKRKLCFVLSILGNPSVVL 1400
Cdd:PRK09700 353 FPNFSIAQNMAISRSLKDGGYKGAmglfhEVDEQRTAENQRELLALKCHsvnqnITELSGGNQQKVLISKWLCCCPEVII 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6005701 1401 LDEPSTGMDPEGQQQMWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCI 1459
Cdd:PRK09700 433 FDEPTRGIDVGAKAEIYKVMR-QLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
480-658 |
1.24e-13 |
|
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: 71.76 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMaDLENLSKL 559
Cdd:cd03244 3 IEFKNVSLRYR--PNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKI-GLHDLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 560 TGVCPQSNVQFDFlTVRENLRLF--------------AKIKGILPQEVDK------------------------------ 595
Cdd:cd03244 80 ISIIPQDPVLFSG-TIRSNLDPFgeysdeelwqalerVGLKEFVESLPGGldtvveeggenlsvgqrqllclarallrks 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6005701 596 EIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQ----FMDeadilADRKVFLSQGKLKCAGS 658
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHrldtIID-----SDRILVLDKGRVVEFDS 220
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
480-579 |
1.31e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.59 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGkpdkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIyNNKLSEMADLENLSKL 559
Cdd:PRK09700 6 ISMAGIGKSFGP----VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITI-NNINYNKLDHKLAAQL 80
|
90 100
....*....|....*....|.
gi 6005701 560 -TGVCPQSNVQFDFLTVRENL 579
Cdd:PRK09700 81 gIGIIYQELSVIDELTVLENL 101
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
480-658 |
1.84e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.09 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGkpdkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMAdlENLSKL 559
Cdd:PRK15439 12 LCARSISKQYSG----VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT--PAKAHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 560 TGV--CPQSNVQFDFLTVRENLrLF---------AKIKGILPQ--------------EV--------------DKEIFLL 600
Cdd:PRK15439 86 LGIylVPQEPLLFPNLSVKENI-LFglpkrqasmQKMKQLLAAlgcqldldssagslEVadrqiveilrglmrDSRILIL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6005701 601 DEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS 658
Cdd:PRK15439 165 DEPTASLTPAETERLFSRIRElLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGK 223
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
480-672 |
1.89e-13 |
|
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: 71.80 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGKPDkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMAdLENLSKL 559
Cdd:cd03249 1 IEFKNVSFRYPSRPD-VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLN-LRWLRSQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 560 TGVCPQSNVQFDfLTVRENLRL------------FAKIKGI------LPQEVDKE------------------------- 596
Cdd:cd03249 79 IGLVSQEPVLFD-GTIAENIRYgkpdatdeeveeAAKKANIhdfimsLPDGYDTLvgergsqlsggqkqriaiarallrn 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 597 --IFLLDEPTAGLDPFSRHQVWNLLKERKTDRVIL-----FSTqfmdeadIL-ADRKVFLSQGKLKCAGSSLFLKKKWGI 668
Cdd:cd03249 158 pkILLLDEATSALDAESEKLVQEALDRAMKGRTTIviahrLST-------IRnADLIAVLQNGQVVEQGTHDELMAQKGV 230
|
....
gi 6005701 669 GYHL 672
Cdd:cd03249 231 YAKL 234
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
511-667 |
1.98e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 73.76 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 511 ITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLS---KLTGVCPQSNVQFDFLTVRENLR------- 580
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLPpekRRIGYVFQDARLFPHYKVRGNLRygmaksm 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 581 --LFAKIKGIL---------P--------QEV--------DKEIFLLDEPTAGLDPFSRHQVWNLLkERKTDRV---ILF 630
Cdd:PRK11144 106 vaQFDKIVALLgieplldryPgslsggekQRVaigralltAPELLLMDEPLASLDLPRKRELLPYL-ERLAREInipILY 184
|
170 180 190
....*....|....*....|....*....|....*..
gi 6005701 631 STQFMDEADILADRKVFLSQGKLKCAGSslfLKKKWG 667
Cdd:PRK11144 185 VSHSLDEILRLADRVVVLEQGKVKAFGP---LEEVWA 218
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
480-657 |
2.03e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 72.48 E-value: 2.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVtIYNNKLSEMADLENLSKL 559
Cdd:PRK13648 8 IVFKNVSFQYQS--DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEI-FYNNQAITDDNFEKLRKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 560 TGVCPQ--------SNVQFDFLTVRENLRL-FAKIKGILPQ---EVD-----------------------------KEIF 598
Cdd:PRK13648 85 IGIVFQnpdnqfvgSIVKYDVAFGLENHAVpYDEMHRRVSEalkQVDmleradyepnalsggqkqrvaiagvlalnPSVI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6005701 599 LLDEPTAGLDPFSRHQVWNLLKERKTDR--VILFSTQFMDEAdILADRKVFLSQGKLKCAG 657
Cdd:PRK13648 165 ILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEA-MEADHVIVMNKGTVYKEG 224
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
883-1128 |
2.19e-13 |
|
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: 73.58 E-value: 2.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 883 ASIDDFIQSVEHQNI--ALEVDAFGTRNGTDDPSYNgaITVCCNEKNYSFSLACNAKRLNCFPVLMDIVSNGLLGMVKPS 960
Cdd:pfam12698 65 DSEEEAKEALKNGKIdgLLVIPKGFSKDLLKGESAT--VTVYINSSNLLVSKLILNALQSLLQQLNASALVLLLEALSTS 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 961 VHIRTErSTFLENGQDNPIGFLAYIMFWLVLTSSCPpYIAMSSIDDYKNRARSQLRISGLSPSAYWFGQALVDVSLYFLV 1040
Cdd:pfam12698 143 APIPVE-STPLFNPQSGYAYYLVGLILMIIILIGAA-IIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFLVGLLQ 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1041 FVFIYLMSYISNFEDMLLTIIHIIQIPcavgYSFSLIFMTYVISFIFRKGRKNSGIWSFCFYVVTVFSVAGFAFSIFESD 1120
Cdd:pfam12698 221 LLIILLLLFGIGIPFGNLGLLLLLFLL----YGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLFPLEDPPSF 296
|
....*...
gi 6005701 1121 IPFIFTFL 1128
Cdd:pfam12698 297 LQWIFSII 304
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1262-1436 |
2.25e-13 |
|
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: 74.70 E-value: 2.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1262 NKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDALEFL-GYCPQENALWpNLTV 1336
Cdd:TIGR02868 347 APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGvpvsSLDQDEVRRRvSVCAQDAHLF-DTTV 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1337 RQHL----------EVYAAVKGLRKGDaevaitrLVDAlkLQDQLKSPV----KTLSEGIKRKLCFVLSILGNPSVVLLD 1402
Cdd:TIGR02868 426 RENLrlarpdatdeELWAALERVGLAD-------WLRA--LPDGLDTVLgeggARLSGGERQRLALARALLADAPILLLD 496
|
170 180 190
....*....|....*....|....*....|....
gi 6005701 1403 EPSTGMDPEGQQQMWQAIRATfrNTERGALLTTH 1436
Cdd:TIGR02868 497 EPTEHLDAETADELLEDLLAA--LSGRTVVLITH 528
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1267-1461 |
2.31e-13 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 74.82 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1267 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsgGG--------DAL-EFLGYCPQENALWpNLTVR 1337
Cdd:COG1132 357 KDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILI----DGvdirdltlESLrRQIGVVPQDTFLF-SGTIR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1338 QHL----------EVYAAVKglrkgdaEVAITRLVDALKlqDQLKSPV----KTLSEGIKRKLCFVLSILGNPSVVLLDE 1403
Cdd:COG1132 432 ENIrygrpdatdeEVEEAAK-------AAQAHEFIEALP--DGYDTVVgergVNLSGGQRQRIAIARALLKDPPILILDE 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6005701 1404 PSTGMDPEGQQQMWQAIRATFRNteRGALLTTHYMAEAEAvCDRVAIMVSGRLRCIGS 1461
Cdd:COG1132 503 ATSALDTETEALIQEALERLMKG--RTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGT 557
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1257-1456 |
2.51e-13 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 73.19 E-value: 2.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1257 FSKRKNKI-ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDAL-EF---LGYCPQE 1327
Cdd:COG1135 11 FPTKGGPVtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGvdltALSERELrAArrkIGMIFQH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1328 NALWPNLTVRQH----LEvyaaVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEG------IKRKLCfvlsilGNPS 1397
Cdd:COG1135 91 FNLLSSRTVAENvalpLE----IAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGqkqrvgIARALA------NNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6005701 1398 VVLLDEPSTGMDPEGQQQmwqaIRATFR--NTERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1456
Cdd:COG1135 161 VLLCDEATSALDPETTRS----ILDLLKdiNRELGLtiVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
479-644 |
2.52e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 74.28 E-value: 2.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 479 AIRIRNVTKEYKGkpdkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLSK 558
Cdd:COG1129 4 LLEMRGISKSFGG----VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 559 LTGVCPQSNVQFDFLTVRENL----------------------RLFAKIkGI----------LP----QEV--------D 594
Cdd:COG1129 80 GIAIIHQELNLVPNLSVAENIflgreprrgglidwramrrrarELLARL-GLdidpdtpvgdLSvaqqQLVeiaralsrD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6005701 595 KEIFLLDEPTAGLDPFSRHQVWNLLKERKTDRV-ILFSTQFMDEADILADR 644
Cdd:COG1129 159 ARVLILDEPTASLTEREVERLFRIIRRLKAQGVaIIYISHRLDEVFEIADR 209
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1267-1455 |
2.77e-13 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 71.18 E-value: 2.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1267 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDALEF---LGYCPQENALWPNLTVRQH 1339
Cdd:COG1126 18 KGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGedltDSKKDINKLrrkVGMVFQQFNLFPHLTVLEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1340 LeVYA--AVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEG------IKRKLCFvlsilgNPSVVLLDEPSTGMDPE 1411
Cdd:COG1126 98 V-TLApiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGqqqrvaIARALAM------EPKVMLFDEPTSALDPE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 6005701 1412 gqqqMWQAIRATFRN-TERGA--LLTTHYMAEAEAVCDRVAIMVSGR 1455
Cdd:COG1126 171 ----LVGEVLDVMRDlAKEGMtmVVVTHEMGFAREVADRVVFMDGGR 213
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
480-581 |
2.94e-13 |
|
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: 70.98 E-value: 2.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSeMADLENLSKL 559
Cdd:cd03252 1 ITFEHVRFRYK--PDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLA-LADPAWLRRQ 77
|
90 100
....*....|....*....|..
gi 6005701 560 TGVCPQSNVQFDfLTVRENLRL 581
Cdd:cd03252 78 VGVVLQENVLFN-RSIRDNIAL 98
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
501-657 |
2.97e-13 |
|
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: 70.40 E-value: 2.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 501 DLVFDIyEGQITAILGHSGAGKSTLLNILSGLSVPTKGSV----TIYNNKLSEMaDLENLSKLTGVCPQSNVQFDFLTVR 576
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngTVLFDSRKKI-NLPPQQRKIGLVFQQYALFPHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 577 ENL-----RLFAKIKGILPQEV---------------------------------DKEIFLLDEPTAGLDPFSRHQVWNL 618
Cdd:cd03297 94 ENLafglkRKRNREDRISVDELldllgldhllnrypaqlsggekqrvalaralaaQPELLLLDEPFSALDRALRLQLLPE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 6005701 619 LKERKTDRVI--LFSTQFMDEADILADRKVFLSQGKLKCAG 657
Cdd:cd03297 174 LKQIKKNLNIpvIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1268-1474 |
4.17e-13 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 70.81 E-value: 4.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1268 NVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-----SGGGDALEFL------GYCPQENALWPNLTV 1336
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfSKTPSDKAIRelrrnvGMVFQQYNLWPHLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1337 RQHL-EVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQ 1415
Cdd:PRK11124 100 QQNLiEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQ 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6005701 1416 MWQAIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLK----SKFgKDYL 1474
Cdd:PRK11124 180 IVSIIRE-LAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASCFTqpqtEAF-KNYL 240
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1267-1461 |
4.46e-13 |
|
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: 69.75 E-value: 4.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1267 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGS-----GGGDALEFLGYCPQENALWPNlTVRQHLE 1341
Cdd:cd03369 25 KNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIdistiPLEDLRSSLTIIPQDPTLFSG-TIRSNLD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1342 VYAavkglRKGDAEvaitrLVDALKlqdqLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIR 1421
Cdd:cd03369 104 PFD-----EYSDEE-----IYGALR----VSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 6005701 1422 ATFRNTergALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1461
Cdd:cd03369 170 EEFTNS---TILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
479-653 |
4.52e-13 |
|
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: 70.54 E-value: 4.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 479 AIRIRNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMaDLENLSK 558
Cdd:COG4181 8 IIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAL-DEDARAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 559 LTGvcpqSNVQFDF--------LTVRENLRL----------FAKIKGIL------------P--------QEV------- 593
Cdd:COG4181 87 LRA----RHVGFVFqsfqllptLTALENVMLplelagrrdaRARARALLervglghrldhyPaqlsggeqQRValarafa 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6005701 594 -DKEIFLLDEPTAGLDPFSRHQVWNLL----KERKTDRVILfsTQfmDEAdiLA---DRKVFLSQGKL 653
Cdd:COG4181 163 tEPAILFADEPTGNLDAATGEQIIDLLfelnRERGTTLVLV--TH--DPA--LAarcDRVLRLRAGRL 224
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
481-653 |
4.66e-13 |
|
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: 70.84 E-value: 4.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 481 RIRNVTKEYKGkpdkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTiYNNKlsemadlenlsKLT 560
Cdd:COG0411 6 EVRGLTKRFGG----LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRIL-FDGR-----------DIT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 561 GVCP------------QsNVQ-FDFLTVRENLRL---------FAKIKGILPQEVDKE---------------------- 596
Cdd:COG0411 70 GLPPhriarlgiartfQ-NPRlFPELTVLENVLVaaharlgrgLLAALLRLPRARREEreareraeellervgladrade 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 597 ------------------------IFLLDEPTAGLDPFSRHQVWNLLKERKTDRVIlfsTQFMDEADI-----LADRKVF 647
Cdd:COG0411 149 pagnlsygqqrrleiaralatepkLLLLDEPAAGLNPEETEELAELIRRLRDERGI---TILLIEHDMdlvmgLADRIVV 225
|
....*.
gi 6005701 648 LSQGKL 653
Cdd:COG0411 226 LDFGRV 231
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1265-1474 |
4.70e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 71.17 E-value: 4.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1265 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGD------------------ALEFLGYCPQ 1326
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDfsklqgirklvgivfqnpETQFVGRTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1327 -------ENALWPNLTVRQHLEVYAAVKGLRKGdaevaitrlvdalklqdQLKSPvKTLSEGIKRKLCFVLSILGNPSVV 1399
Cdd:PRK13644 97 edlafgpENLCLPPIEIRKRVDRALAEIGLEKY-----------------RHRSP-KTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6005701 1400 LLDEPSTGMDPEGQQQMWQAIRatfRNTERGALL--TTHYMAEAEAVcDRVAIMVSGRLRCIGSIQHLKSKFGKDYL 1474
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIK---KLHEKGKTIvyITHNLEELHDA-DRIIVMDRGKIVLEGEPENVLSDVSLQTL 231
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
504-658 |
5.04e-13 |
|
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: 72.44 E-value: 5.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 504 FDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLS----KLtGVCPQSNVQFDFLTVRENL 579
Cdd:COG4148 20 FTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFLPphrrRI-GYVFQEARLFPHLSVRGNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 580 -----RLFAKIKGILPQEV---------------------------------DKEIFLLDEPTAGLDPFSRHQVWNLLkE 621
Cdd:COG4148 99 lygrkRAPRAERRISFDEVvellgighlldrrpatlsggerqrvaigrallsSPRLLLMDEPLAALDLARKAEILPYL-E 177
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 6005701 622 RKTDRV---ILFSTQFMDEADILADRKVFLSQGKLKCAGS 658
Cdd:COG4148 178 RLRDELdipILYVSHSLDEVARLADHVVLLEQGRVVASGP 217
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
466-609 |
5.27e-13 |
|
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: 73.55 E-value: 5.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 466 SFEQAPPEFQGKEAIRIRNVTKEYKGKPdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNN 545
Cdd:TIGR02868 321 SAPAAGAVGLGKPTLELRDLSAGYPGAP---PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGV 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 546 KLSEmADLENLSKLTGVCPQSNVQFDfLTVRENLRL-------------FAKIK-GILPQEV------------------ 593
Cdd:TIGR02868 398 PVSS-LDQDEVRRRVSVCAQDAHLFD-TTVRENLRLarpdatdeelwaaLERVGlADWLRALpdgldtvlgeggarlsgg 475
|
170 180
....*....|....*....|....*....
gi 6005701 594 -------------DKEIFLLDEPTAGLDP 609
Cdd:TIGR02868 476 erqrlalarallaDAPILLLDEPTEHLDA 504
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1268-1421 |
6.23e-13 |
|
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: 69.19 E-value: 6.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1268 NVSFCVRKGEVLGLLGHNGAGKSTSIKVITG--DTKPTAGQVLLKGSGGGDALE-FLGYCPQENALWPNLTVRQHLEVYA 1344
Cdd:cd03232 25 NISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLDKNFQrSTGYVEQQDVHSPNLTVREALRFSA 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6005701 1345 AVKGLrkgdaevaitrlvdalklqdqlkspvkTLSEgiKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIR 1421
Cdd:cd03232 105 LLRGL---------------------------SVEQ--RKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLK 152
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
479-639 |
7.75e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 73.62 E-value: 7.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 479 AIRIRNVTKEYKgkpdKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNnklsemADLENLSK 558
Cdd:NF033858 1 VARLEGVSHRYG----KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLG------GDMADARH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 559 LTGVCPQ---------SNVQFDfLTVRENL----RLF--------AKIK------GILP--------------QEV---- 593
Cdd:NF033858 71 RRAVCPRiaympqglgKNLYPT-LSVFENLdffgRLFgqdaaerrRRIDellratGLAPfadrpagklsggmkQKLglcc 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6005701 594 ----DKEIFLLDEPTAGLDPFSRHQVWNLLKERKTDRV---ILFSTQFMDEAD 639
Cdd:NF033858 150 alihDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERPgmsVLVATAYMEEAE 202
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1271-1436 |
7.80e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 69.49 E-value: 7.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1271 FCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG--SGGGDALEFLGYCPQENALWPNLTVRQHLEVYAAVKG 1348
Cdd:PRK13543 32 FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGktATRGDRSRFMAYLGHLPGLKADLSTLENLHFLCGLHG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1349 LRK----GDAeVAITRLVDalkLQDQLkspVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATF 1424
Cdd:PRK13543 112 RRAkqmpGSA-LAIVGLAG---YEDTL---VRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHL 184
|
170
....*....|..
gi 6005701 1425 RnTERGALLTTH 1436
Cdd:PRK13543 185 R-GGGAALVTTH 195
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1256-1468 |
7.81e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 70.40 E-value: 7.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1256 CFSKRKN-KIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-----SGGGDALEFLGYCPQEna 1329
Cdd:PRK13632 14 SFSYPNSeNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGitiskENLKEIRKKIGIIFQN-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1330 lwPN-----LTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCfVLSILG-NPSVVLLDE 1403
Cdd:PRK13632 92 --PDnqfigATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVA-IASVLAlNPEIIIFDE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6005701 1404 pSTGM-DPEGQQQMWQAIRATFRNTERGALLTTHYMAEAeAVCDRVAIMVSGRLRCIGSIQH-LKSK 1468
Cdd:PRK13632 169 -STSMlDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEiLNNK 233
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
476-653 |
8.53e-13 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 68.23 E-value: 8.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 476 GKEAIRIRNVTKEYkgkpdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLEN 555
Cdd:cd03215 1 GEPVLEVRGLSVKG--------AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 556 LS----------KLTGVCPQsnvqfdfLTVRENLRLFAKIKG------ILPQEV--DKEIFLLDEPTAGLDPFSRHQVWN 617
Cdd:cd03215 73 IRagiayvpedrKREGLVLD-------LSVAENIALSSLLSGgnqqkvVLARWLarDPRVLILDEPTRGVDVGAKAEIYR 145
|
170 180 190
....*....|....*....|....*....|....*....
gi 6005701 618 LLKErKTDR---VILFSTQfMDEADILADRKVFLSQGKL 653
Cdd:cd03215 146 LIRE-LADAgkaVLLISSE-LDELLGLCDRILVMYEGRI 182
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
480-658 |
8.74e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 70.40 E-value: 8.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYkgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLSKL 559
Cdd:PRK13644 2 IRLENVSYSY---PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 560 TGVCPQS-NVQFDFLTVRENL-------------------RLFAKIK-----------------------GILPQEVDKE 596
Cdd:PRK13644 79 VGIVFQNpETQFVGRTVEEDLafgpenlclppieirkrvdRALAEIGlekyrhrspktlsggqgqcvalaGILTMEPECL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6005701 597 IFllDEPTAGLDPFSRHQVW-NLLKERKTDRVILFSTQFMDEADIlADRKVFLSQGKLKCAGS 658
Cdd:PRK13644 159 IF--DEVTSMLDPDSGIAVLeRIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGE 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
453-654 |
9.80e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.79 E-value: 9.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 453 LEDEMDADPSFHDSFEQAPPefQGKEAIRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGL 532
Cdd:COG0488 291 REEPPRRDKTVEIRFPPPER--LGKKVLELEGLSKSYGDKT----LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 533 SVPTKGSVTIYnnklsemadlENLSklTGVCPQSNVQFDF-LTVRENLRLFA------KIKGIL------PQEVDKEI-- 597
Cdd:COG0488 365 LEPDSGTVKLG----------ETVK--IGYFDQHQEELDPdKTVLDELRDGApggteqEVRGYLgrflfsGDDAFKPVgv 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 598 --------------------FL-LDEPTAGLDPFSRHQVWNLLKERK-TdrVILFS--TQFMDEadiLADRKVFLSQGKL 653
Cdd:COG0488 433 lsggekarlalaklllsppnVLlLDEPTNHLDIETLEALEEALDDFPgT--VLLVShdRYFLDR---VATRILEFEDGGV 507
|
.
gi 6005701 654 K 654
Cdd:COG0488 508 R 508
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
470-653 |
9.85e-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: 69.42 E-value: 9.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 470 APPEFQGKeaIRIRNVTKEYKGKPDKiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVtIYNNKLSE 549
Cdd:cd03248 4 APDHLKGI--VKFQNVTFAYPTRPDT-LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQV-LLDGKPIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 550 MADLENLSKLTGVCPQSNVQFDfLTVRENLRL------FAKIKGI------------LPQEVDKE--------------- 596
Cdd:cd03248 80 QYEHKYLHSKVSLVGQEPVLFA-RSLQDNIAYglqscsFECVKEAaqkahahsfiseLASGYDTEvgekgsqlsggqkqr 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6005701 597 ------------IFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEADiLADRKVFLSQGKL 653
Cdd:cd03248 159 vaiaralirnpqVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVE-RADQILVLDGGRI 226
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1247-1456 |
1.01e-12 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 69.13 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1247 KEYAGKRKgcfskrknkiATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSG----GGDALEFL- 1321
Cdd:PRK10908 9 KAYLGGRQ----------ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDitrlKNREVPFLr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1322 ---GYCPQENALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSV 1398
Cdd:PRK10908 79 rqiGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6005701 1399 VLLDEPSTGMDPEgqqqMWQAIRATFRNTER---GALLTTHYMAEAEAVCDRVAIMVSGRL 1456
Cdd:PRK10908 159 LLADEPTGNLDDA----LSEGILRLFEEFNRvgvTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1267-1461 |
1.02e-12 |
|
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: 69.06 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1267 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG---SGGG--DALEFLGYCPQEnalwPNL---TVRQ 1338
Cdd:cd03244 21 KNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiSKIGlhDLRSRISIIPQD----PVLfsgTIRS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1339 HL---------EVYAAVKglrkgdaEVAITRLVDAL--KLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTG 1407
Cdd:cd03244 97 NLdpfgeysdeELWQALE-------RVGLKEFVESLpgGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATAS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 6005701 1408 MDPEGQQQMWQAIRATFRNTergALLT-THYMaeaEAV--CDRVAIMVSGRLRCIGS 1461
Cdd:cd03244 170 VDPETDALIQKTIREAFKDC---TVLTiAHRL---DTIidSDRILVLDKGRVVEFDS 220
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1235-1455 |
1.21e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 69.57 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1235 DEKPVIIASCLRKEYaGKRKGCfskrknkiatRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGG 1314
Cdd:PRK11701 2 MDQPLLSVRGLTKLY-GPRKGC----------RDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1315 GDA-LEFLGYcPQENAL----WPnlTVRQHlevyaAVKGLRKG---DAEVAiTRL-----------------------VD 1363
Cdd:PRK11701 71 QLRdLYALSE-AERRRLlrteWG--FVHQH-----PRDGLRMQvsaGGNIG-ERLmavgarhygdiratagdwlerveID 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1364 ALKLQDQlksPvKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEA 1443
Cdd:PRK11701 142 AARIDDL---P-TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARL 217
|
250
....*....|..
gi 6005701 1444 VCDRVAIMVSGR 1455
Cdd:PRK11701 218 LAHRLLVMKQGR 229
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1269-1464 |
1.50e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 71.87 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1269 VSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-----SGGGDALEF-LGYCPQ---ENALWPNLTVRQH 1339
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpidiRSPRDAIRAgIMLCPEdrkAEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1340 LEVYAAVKGLRKG----------DAEVAITRLvdALKLQDQlKSPVKTLSEGIKRKlcfvlSILG-----NPSVVLLDEP 1404
Cdd:PRK11288 352 INISARRHHLRAGclinnrweaeNADRFIRSL--NIKTPSR-EQLIMNLSGGNQQK-----AILGrwlseDMKVILLDEP 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6005701 1405 STGMDPEGQQQMWQAIratFRNTERG--ALLTTHYMAEAEAVCDRVAIMVSGRLRciGSIQH 1464
Cdd:PRK11288 424 TRGIDVGAKHEIYNVI---YELAAQGvaVLFVSSDLPEVLGVADRIVVMREGRIA--GELAR 480
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
480-658 |
1.57e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 69.27 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLEnLSKL 559
Cdd:PRK11231 3 LRTENLTVGYGTKR----ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ-LARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 560 TGVCPQSNVQFDFLTVRE--------NLRLFAKIKG--------------------------------------ILPQev 593
Cdd:PRK11231 78 LALLPQHHLTPEGITVRElvaygrspWLSLWGRLSAednarvnqameqtrinhladrrltdlsggqrqraflamVLAQ-- 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6005701 594 DKEIFLLDEPTAGLDpfSRHQV--WNLLKER----KTDRVILFStqfMDEADILADRKVFLSQGKLKCAGS 658
Cdd:PRK11231 156 DTPVVLLDEPTTYLD--INHQVelMRLMRELntqgKTVVTVLHD---LNQASRYCDHLVVLANGHVMAQGT 221
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
480-672 |
2.10e-12 |
|
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: 68.41 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMaDLENLSKL 559
Cdd:cd03251 1 VEFKNVTFRYPG--DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDY-TLASLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 560 TGVCPQSNVQFDFlTVRENLR-----------LFA--------------------------KIKGILPQEV--------D 594
Cdd:cd03251 78 IGLVSQDVFLFND-TVAENIAygrpgatreevEEAaraanahefimelpegydtvigergvKLSGGQRQRIaiarallkD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 595 KEIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVIL-----FSTqFMDeadilADRKVFLSQGKLKCAGSSLFLKKKWGIG 669
Cdd:cd03251 157 PPILILDEATSALDTESERLVQAALERLMKNRTTFviahrLST-IEN-----ADRIVVLEDGKIVERGTHEELLAQGGVY 230
|
...
gi 6005701 670 YHL 672
Cdd:cd03251 231 AKL 233
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1265-1465 |
2.15e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 69.27 E-value: 2.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1265 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsgGGDALEflgycpqENALWpnlTVRQHLE--- 1341
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITV----GGMVLS-------EETVW---DVRRQVGmvf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1342 -------VYAAVK-----GL--RKGDAEVAITRLVDALKL---QDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEP 1404
Cdd:PRK13635 88 qnpdnqfVGATVQddvafGLenIGVPREEMVERVDQALRQvgmEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6005701 1405 STGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAeAVCDRVAIMVSGRLRCIGSIQHL 1465
Cdd:PRK13635 168 TSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEEGTPEEI 227
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1267-1456 |
2.24e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 68.30 E-value: 2.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1267 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG------SGGGDAL---EFLGYCPQENALWPNLTVR 1337
Cdd:PRK11629 26 HNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpmsklSSAAKAElrnQKLGFIYQFHHLLPDFTAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1338 QHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMW 1417
Cdd:PRK11629 106 ENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIF 185
|
170 180 190
....*....|....*....|....*....|....*....
gi 6005701 1418 QAIRATFRNTERGALLTTHYMAEAEAVcDRVAIMVSGRL 1456
Cdd:PRK11629 186 QLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRL 223
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1267-1455 |
2.60e-12 |
|
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: 67.67 E-value: 2.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1267 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGqvlLKGS---GGGDALEF-------LGYCPQENALWPNLTV 1336
Cdd:cd03233 24 KDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVS---VEGDihyNGIPYKEFaekypgeIIYVSEEDVHFPTLTV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1337 RQHLEVYAAVKGlrkgdaevaitrlvdalklqDQLkspVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQM 1416
Cdd:cd03233 101 RETLDFALRCKG--------------------NEF---VRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 6005701 1417 WQAIRaTFRNTERGALLTTHYMA--EAEAVCDRVAIMVSGR 1455
Cdd:cd03233 158 LKCIR-TMADVLKTTTFVSLYQAsdEIYDLFDKVLVLYEGR 197
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
480-580 |
2.94e-12 |
|
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: 68.03 E-value: 2.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKgkPDKiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMaDLENLSKL 559
Cdd:cd03253 1 IEFENVTFAYD--PGR-PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREV-TLDSLRRA 76
|
90 100
....*....|....*....|.
gi 6005701 560 TGVCPQSNVQFDfLTVRENLR 580
Cdd:cd03253 77 IGVVPQDTVLFN-DTIGYNIR 96
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1268-1465 |
3.04e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 70.13 E-value: 3.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1268 NVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGD-ALEFLGYCP--QENALWPNLTVRQHleVYA 1344
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHrSIQQRDICMvfQSYALFPHMSLGEN--VGY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1345 AVKGLRKGDAEVAiTRLVDALKLQDQL---KSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIR 1421
Cdd:PRK11432 102 GLKMLGVPKEERK-QRVKEALELVDLAgfeDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIR 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 6005701 1422 ATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL 1465
Cdd:PRK11432 181 ELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
480-657 |
3.21e-12 |
|
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: 68.13 E-value: 3.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGKpdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVtiynnkLSEMADLENLS-- 557
Cdd:cd03299 1 LKVENLSKDWKEF-----KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKI------LLNGKDITNLPpe 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 558 -KLTGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDK----------------------------------------E 596
Cdd:cd03299 70 kRDISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERkvleiaemlgidhllnrkpetlsggeqqrvaiaralvvnpK 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6005701 597 IFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAG 657
Cdd:cd03299 150 ILLLDEPFSALDVRTKEKLREELKKirKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVG 212
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1269-1409 |
3.32e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 68.42 E-value: 3.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1269 VSFCVRKGEVLGLLGHNGAGKSTSIKVITGdTKPTAGQVLLkgsgGGDALEFL---------GYCPQENALWPNLTVRQH 1339
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQF----AGQPLEAWsaaelarhrAYLSQQQTPPFAMPVFQY 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6005701 1340 LEVYAAVkGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSIL-----GNPS--VVLLDEPSTGMD 1409
Cdd:PRK03695 90 LTLHQPD-KTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLqvwpdINPAgqLLLLDEPMNSLD 165
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
467-653 |
4.00e-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: 70.60 E-value: 4.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 467 FEQAPPEFQGKEAIRIRNVTKEY----KGKpdkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTI 542
Cdd:TIGR03269 267 VEKECEVEVGEPIIKVRNVSKRYisvdRGV---VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNV 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 543 -YNNKLSEMADLENL-----SKLTGVCPQSNVQFDFLTVRENL---------RLFAKIKGI------------------- 588
Cdd:TIGR03269 344 rVGDEWVDMTKPGPDgrgraKRYIGILHQEYDLYPHRTVLDNLteaiglelpDELARMKAVitlkmvgfdeekaeeildk 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 589 --------------LPQEVDKE--IFLLDEPTAGLDPFSRHQVWN-LLKERKT-DRVILFSTQFMDEADILADRKVFLSQ 650
Cdd:TIGR03269 424 ypdelsegerhrvaLAQVLIKEprIVILDEPTGTMDPITKVDVTHsILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRD 503
|
...
gi 6005701 651 GKL 653
Cdd:TIGR03269 504 GKI 506
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
479-653 |
4.31e-12 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 67.73 E-value: 4.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 479 AIRIRNVTKEYKGKpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNK--LSEMADLENL 556
Cdd:PRK11124 2 SIQLNGINCFYGAH----QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdFSKTPSDKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 557 SKLtgvcpQSNVQFDF--------LTVRENL------------------------RL----FA-----KIKGILPQEV-- 593
Cdd:PRK11124 78 REL-----RRNVGMVFqqynlwphLTVQQNLieapcrvlglskdqalaraeklleRLrlkpYAdrfplHLSGGQQQRVai 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6005701 594 ------DKEIFLLDEPTAGLDPFSRHQVWNLLKE-RKT--DRVILfsTQFMDEADILADRKVFLSQGKL 653
Cdd:PRK11124 153 aralmmEPQVLLFDEPTAALDPEITAQIVSIIRElAETgiTQVIV--THEVEVARKTASRVVYMENGHI 219
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1273-1452 |
4.39e-12 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 70.97 E-value: 4.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1273 VRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSgggdalefLGYCPQEnalwpnLTVRQHLEVYAAVKGLRKG 1352
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK--------ISYKPQY------ISPDYDGTVEEFLRSANTD 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1353 DAEVAI--TRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERG 1430
Cdd:COG1245 429 DFGSSYykTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKT 508
|
170 180
....*....|....*....|..
gi 6005701 1431 ALLTTHYMAEAEAVCDRvaIMV 1452
Cdd:COG1245 509 AMVVDHDIYLIDYISDR--LMV 528
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1267-1436 |
4.56e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 66.90 E-value: 4.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1267 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDAL----EFLGYCPQENALWPNLTVRQHlev 1342
Cdd:PRK13540 18 QQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLctyqKQLCFVGHRSGINPYLTLREN--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1343 yaAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRA 1422
Cdd:PRK13540 95 --CLYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQE 172
|
170
....*....|....
gi 6005701 1423 tFRNTERGALLTTH 1436
Cdd:PRK13540 173 -HRAKGGAVLLTSH 185
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1263-1455 |
4.60e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 68.19 E-value: 4.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1263 KIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGsgggdalEFLGYCPQEN-ALW---------- 1331
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDG-------KDVTKLPEYKrAKYigrvfqdpmm 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1332 ---PNLTVRQHLEVyAAVKGLRKG------DAEVAITRlvDALK-----LQDQLKSPVKTLSEGIKRKLCFVLSILGNPS 1397
Cdd:COG1101 92 gtaPSMTIEENLAL-AYRRGKRRGlrrgltKKRRELFR--ELLAtlglgLENRLDTKVGLLSGGQRQALSLLMATLTKPK 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6005701 1398 VVLLDEPSTGMDPEGQQQMwqaIRATFRNTERG---ALLTTHYMAEAEAVCDRVAIMVSGR 1455
Cdd:COG1101 169 LLLLDEHTAALDPKTAALV---LELTEKIVEENnltTLMVTHNMEQALDYGNRLIMMHEGR 226
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
475-658 |
6.36e-12 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 69.21 E-value: 6.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 475 QGKEAIRIRNVTKEYKGKpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIynnklsemadle 554
Cdd:PRK09452 10 SLSPLVELRGISKSFDGK----EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIML------------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 555 NLSKLTGVCP---------QSNVQFDFLTVREN----LRL----FAKIK------------------------------- 586
Cdd:PRK09452 74 DGQDITHVPAenrhvntvfQSYALFPHMTVFENvafgLRMqktpAAEITprvmealrmvqleefaqrkphqlsggqqqrv 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6005701 587 GILPQEVDK-EIFLLDEPTAGLDPFSRHQVWNLLK--ERKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS 658
Cdd:PRK09452 154 AIARAVVNKpKVLLLDESLSALDYKLRKQMQNELKalQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
479-542 |
7.12e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 69.67 E-value: 7.12e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6005701 479 AIRIRNVTKEYKGkpdkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTI 542
Cdd:COG3845 5 ALELRGITKRFGG----VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILI 64
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1267-1436 |
7.43e-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: 64.39 E-value: 7.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1267 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsggGDALEFlGYCPQenalwpnltvrqhlevyaav 1346
Cdd:cd03221 17 KDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-----GSTVKI-GYFEQ-------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1347 kglrkgdaevaitrlvdalklqdqlkspvktLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQqqmwQAIRATFRN 1426
Cdd:cd03221 71 -------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESI----EALEEALKE 115
|
170
....*....|
gi 6005701 1427 TERGALLTTH 1436
Cdd:cd03221 116 YPGTVILVSH 125
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1278-1461 |
7.64e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 67.72 E-value: 7.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1278 VLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGsgggDALEFlgycpQENALwpnLTVRQHLEV----------YAAVK 1347
Cdd:PRK13638 29 VTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQG----KPLDY-----SKRGL---LALRQQVATvfqdpeqqifYTDID 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1348 G-----LRK-GDAEVAITRLVD-ALKLQDQL---KSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMW 1417
Cdd:PRK13638 97 SdiafsLRNlGVPEAEITRRVDeALTLVDAQhfrHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 6005701 1418 QAIRATFRNTERgALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1461
Cdd:PRK13638 177 AIIRRIVAQGNH-VIISSHDIDLIYEISDAVYVLRQGQILTHGA 219
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1260-1454 |
7.99e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.60 E-value: 7.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1260 RKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDALE--FLGYCPQ-ENALWPNLTV 1336
Cdd:PRK15056 17 RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQknLVAYVPQsEEVDWSFPVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1337 RQHLEV---YAAVKGLRKGDA------EVAITRlVDALKLQDQlksPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTG 1407
Cdd:PRK15056 97 VEDVVMmgrYGHMGWLRRAKKrdrqivTAALAR-VDMVEFRHR---QIGELSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 6005701 1408 MDPEGQQQMWQAIRaTFRNTERGALLTTHYMAEAEAVCDrVAIMVSG 1454
Cdd:PRK15056 173 VDVKTEARIISLLR-ELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKG 217
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
470-658 |
8.27e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 68.34 E-value: 8.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 470 APPEFQGKEAIRIRNVTKEYKGK-PDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVT---IYNN 545
Cdd:PRK13631 12 VPNPLSDDIILRVKNLYCVFDEKqENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQvgdIYIG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 546 ------------KLSEMADLENLSKLTGVCPQ--------SNVQFDFL-------TVRENLRLFAK-------------- 584
Cdd:PRK13631 92 dkknnhelitnpYSKKIKNFKELRRRVSMVFQfpeyqlfkDTIEKDIMfgpvalgVKKSEAKKLAKfylnkmglddsyle 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 585 ---------------IKGILPqeVDKEIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFL 648
Cdd:PRK13631 172 rspfglsggqkrrvaIAGILA--IQPEILIFDEPTAGLDPKGEHEMMQLILDaKANNKTVFVITHTMEHVLEVADEVIVM 249
|
250
....*....|
gi 6005701 649 SQGKLKCAGS 658
Cdd:PRK13631 250 DKGKILKTGT 259
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
457-672 |
8.28e-12 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 70.14 E-value: 8.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 457 MDADPSFHDSFEQAPPEFQGKeaIRIRNVTKEYKGKPDKiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPT 536
Cdd:TIGR00958 458 LDRKPNIPLTGTLAPLNLEGL--IEFQDVSFSYPNRPDV-PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPT 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 537 KGSVTIYNNKLSEMaDLENLSKLTGVCPQSNVQFDfLTVRENL------------RLFAKIKGI------LPQEVDKEI- 597
Cdd:TIGR00958 535 GGQVLLDGVPLVQY-DHHYLHRQVALVGQEPVLFS-GSVRENIaygltdtpdeeiMAAAKAANAhdfimeFPNGYDTEVg 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 598 --------------------------FLLDEPTAGLDPFSRHQVWNlLKERKtDRVILFSTQFMDEADiLADRKVFLSQG 651
Cdd:TIGR00958 613 ekgsqlsggqkqriaiaralvrkprvLILDEATSALDAECEQLLQE-SRSRA-SRTVLLIAHRLSTVE-RADQILVLKKG 689
|
250 260
....*....|....*....|.
gi 6005701 652 KLKCAGSSLFLKKKWGIGYHL 672
Cdd:TIGR00958 690 SVVEMGTHKQLMEDQGCYKHL 710
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1267-1456 |
9.25e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 69.65 E-value: 9.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1267 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG------------SGG---------GDALeFLGYCP 1325
Cdd:PRK10762 269 NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGhevvtrspqdglANGivyisedrkRDGL-VLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1326 QENAlwpNLTVRQHLEvYAAVKgLRKGDAEVAITRLVDALKL----QDQlksPVKTLSEGIKRKLCFVLSILGNPSVVLL 1401
Cdd:PRK10762 348 KENM---SLTALRYFS-RAGGS-LKHADEQQAVSDFIRLFNIktpsMEQ---AIGLLSGGNQQKVAIARGLMTRPKVLIL 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6005701 1402 DEPSTGMDPEGQQQMWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1456
Cdd:PRK10762 420 DEPTRGVDVGAKKEIYQLIN-QFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
480-652 |
1.09e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 68.71 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLEnlsKL 559
Cdd:PRK11607 20 LEIRNLTKSFDGQH----AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ---RP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 560 TGVCPQSNVQFDFLTVRENL-------RL--------------------FAKIK-----GILPQEV--------DKEIFL 599
Cdd:PRK11607 93 INMMFQSYALFPHMTVEQNIafglkqdKLpkaeiasrvnemlglvhmqeFAKRKphqlsGGQRQRValarslakRPKLLL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 6005701 600 LDEPTAGLDPFSR----HQVWNLLKERKTDRVILFSTQfmDEADILADRKVFLSQGK 652
Cdd:PRK11607 173 LDEPMGALDKKLRdrmqLEVVDILERVGVTCVMVTHDQ--EEAMTMAGRIAIMNRGK 227
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1273-1452 |
1.17e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 69.45 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1273 VRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVL--LKGSgggdaleflgYCPQENALWPNLTVRQHLEvyAAVKGLr 1350
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDpeLKIS----------YKPQYIKPDYDGTVEDLLR--SITDDL- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1351 kgDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERG 1430
Cdd:PRK13409 429 --GSSYYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREAT 506
|
170 180
....*....|....*....|..
gi 6005701 1431 ALLTTHYMAEAEAVCDRvaIMV 1452
Cdd:PRK13409 507 ALVVDHDIYMIDYISDR--LMV 526
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1260-1456 |
1.26e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 68.90 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1260 RKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGS--GGGDALEF----LGYCPQE---NAL 1330
Cdd:COG3845 268 DRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEdiTGLSPRERrrlgVAYIPEDrlgRGL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1331 WPNLTVRQHL-----EVYAAVKG--LRKGDAEVAITRLVDALKLQ-DQLKSPVKTLSEGIKRKlcFVLS--ILGNPSVVL 1400
Cdd:COG3845 348 VPDMSVAENLilgryRRPPFSRGgfLDRKAIRAFAEELIEEFDVRtPGPDTPARSLSGGNQQK--VILAreLSRDPKLLI 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6005701 1401 LDEPSTGMDPEGQQQMWQAIRATfRNteRGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1456
Cdd:COG3845 426 AAQPTRGLDVGAIEFIHQRLLEL-RD--AGAavLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
479-658 |
1.26e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 69.08 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 479 AIRIRNVTKEYKGKPDKieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADlENLSK 558
Cdd:PRK11160 338 SLTLNNVSFTYPDQPQP--VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSE-AALRQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 559 LTGVCPQSnVQFDFLTVRENLRLFA------KIKGILpQEV--------------------------------------- 593
Cdd:PRK11160 415 AISVVSQR-VHLFSATLRDNLLLAApnasdeALIEVL-QQVgleklleddkglnawlgeggrqlsggeqrrlgiarallh 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6005701 594 DKEIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFST-------QFmdeadilaDRKVFLSQGKLKCAGS 658
Cdd:PRK11160 493 DAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMIThrltgleQF--------DRICVMDNGQIIEQGT 556
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
499-608 |
1.33e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 65.67 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 499 LKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTiYNNKLSEMADLENLSKLTGvcpQSNVQFDFLTVREN 578
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIK-LDGGDIDDPDVAEACHYLG---HRNAMKPALTVAEN 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6005701 579 LRLFAKIKGILPQEVD------------------------------------KEIFLLDEPTAGLD 608
Cdd:PRK13539 94 LEFWAAFLGGEELDIAaaleavglaplahlpfgylsagqkrrvalarllvsnRPIWILDEPTAALD 159
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
479-651 |
1.37e-11 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 66.65 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 479 AIRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLS-EMADLENLS 557
Cdd:PRK11248 1 MLQISHLYADYGGKP----ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEgPGAERGVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 558 KLTGVCP----QSNVQFDF-----------LTVRENL----------RLFAKIKGILPQEV--------DKEIFLLDEPT 604
Cdd:PRK11248 77 QNEGLLPwrnvQDNVAFGLqlagvekmqrlEIAHQMLkkvglegaekRYIWQLSGGQRQRVgiaralaaNPQLLLLDEPF 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6005701 605 AGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQG 651
Cdd:PRK11248 157 GALDAFTREQMQTLLLKlwQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
504-653 |
1.47e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 66.14 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 504 FDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLEN-LSKLTgvcpQSNVQFDFLTVREN---- 578
Cdd:PRK10771 20 LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRpVSMLF----QENNLFSHLTVAQNiglg 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 579 ----LRLFAKIK----------GI------LPQEV----------------DKEIFLLDEPTAGLDPFSRHQVWNLLKER 622
Cdd:PRK10771 96 lnpgLKLNAAQReklhaiarqmGIedllarLPGQLsggqrqrvalarclvrEQPILLLDEPFSALDPALRQEMLTLVSQV 175
|
170 180 190
....*....|....*....|....*....|...
gi 6005701 623 KTDRVI--LFSTQFMDEADILADRKVFLSQGKL 653
Cdd:PRK10771 176 CQERQLtlLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
480-692 |
1.54e-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: 68.68 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGKpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLS--VPTKGSVtIYNNKLSEMAD-LENL 556
Cdd:TIGR03269 1 IEVKNLTKKFDGK----EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRI-IYHVALCEKCGyVERP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 557 SKLTGVCPQSNVQF-----DFL----TVRENL---------RLFA----------------------------------- 583
Cdd:TIGR03269 76 SKVGEPCPVCGGTLepeevDFWnlsdKLRRRIrkriaimlqRTFAlygddtvldnvlealeeigyegkeavgravdliem 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 584 ------------------KIKGILPQEVDKE--IFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADIL 641
Cdd:TIGR03269 156 vqlshrithiardlsggeKQRVVLARQLAKEpfLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTSHWPEVIEDL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 6005701 642 ADRKVFLSQGKLKCAGSSLFLKKKWGIGYHLSLQLNEICVEENITSL--VKQH 692
Cdd:TIGR03269 236 SDKAIWLENGEIKEEGTPDEVVAVFMEGVSEVEKECEVEVGEPIIKVrnVSKR 288
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
480-661 |
1.55e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 66.06 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYkgkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLSKL 559
Cdd:PRK11614 6 LSFDKVSAHY----GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 560 TGVCPQSNVQFDFLTVRENLRL---FA----------KIKGILPQEVDKEI--------------------------FLL 600
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLAMggfFAerdqfqerikWVYELFPRLHERRIqragtmsggeqqmlaigralmsqprlLLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6005701 601 DEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGK--LKCAGSSLF 661
Cdd:PRK11614 162 DEPSLGLAPIIIQQIFDTIEQlREQGMTIFLVEQNANQALKLADRGYVLENGHvvLEDTGDALL 225
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1265-1465 |
1.61e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.11 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1265 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQV-----------------------LLKGSGGGD-ALEF 1320
Cdd:PRK10261 31 AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqvielseqsaaQMRHVRGADmAMIF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1321 lgycpQE--NALWPNLTV-RQHLEVYAAVKGLRKGDAEVAITRLVDALKL---QDQLKSPVKTLSEGIKRKLCFVLSILG 1394
Cdd:PRK10261 111 -----QEpmTSLNPVFTVgEQIAESIRLHQGASREEAMVEAKRMLDQVRIpeaQTILSRYPHQLSGGMRQRVMIAMALSC 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6005701 1395 NPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL 1465
Cdd:PRK10261 186 RPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
481-644 |
2.11e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.40 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 481 RIRNVTKEYKGkpdkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTI------YNNK-------- 546
Cdd:PRK11288 6 SFDGIGKTFPG----VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIdgqemrFASTtaalaagv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 547 ---------LSEMADLENLskLTGVCPQSnvqFDFL-------TVRENL-RLFAKIKGILP---------QEV------- 593
Cdd:PRK11288 82 aiiyqelhlVPEMTVAENL--YLGQLPHK---GGIVnrrllnyEAREQLeHLGVDIDPDTPlkylsigqrQMVeiakala 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6005701 594 -DKEIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADR 644
Cdd:PRK11288 157 rNARVIAFDEPTSSLSAREIEQLFRVIRElRAEGRVILYVSHRMEEIFALCDA 209
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
479-653 |
2.41e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 65.93 E-value: 2.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 479 AIRIRNVTKEYKGKpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTI------YNNKLSEMAD 552
Cdd:PRK11264 3 AIEVKNLVKKFHGQ----TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidTARSLSQQKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 553 L-ENLSKLTGVCPQSNVQFDFLTVRENL--------------------RLFAKI-------------KGILPQEV----- 593
Cdd:PRK11264 79 LiRQLRQHVGFVFQNFNLFPHRTVLENIiegpvivkgepkeeatararELLAKVglagketsyprrlSGGQQQRVaiara 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6005701 594 ---DKEIFLLDEPTAGLDPFSRHQVWNL---LKERKTDRVILfsTQFMDEADILADRKVFLSQGKL 653
Cdd:PRK11264 159 lamRPEVILFDEPTSALDPELVGEVLNTirqLAQEKRTMVIV--THEMSFARDVADRAIFMDQGRI 222
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1273-1456 |
3.39e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 65.16 E-value: 3.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1273 VRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLL--------KGSGGGDAL-----EFLGYCPQENALWPNLTVRQH 1339
Cdd:PRK11264 26 VKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidtaRSLSQQKGLirqlrQHVGFVFQNFNLFPHRTVLEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1340 -LEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQ 1418
Cdd:PRK11264 106 iIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLN 185
|
170 180 190
....*....|....*....|....*....|....*...
gi 6005701 1419 AIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1456
Cdd:PRK11264 186 TIRQ-LAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1256-1470 |
3.83e-11 |
|
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: 64.94 E-value: 3.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1256 CFSKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsGGGD----ALEFL----GYCPQE 1327
Cdd:cd03253 7 TFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILI---DGQDirevTLDSLrraiGVVPQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1328 NALWpNLTVRQHL----------EVYAAVKglrKGDAEVAITRLVDA---------LKlqdqlkspvktLSEGIKRKLCF 1388
Cdd:cd03253 84 TVLF-NDTIGYNIrygrpdatdeEVIEAAK---AAQIHDKIMRFPDGydtivgergLK-----------LSGGEKQRVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1389 VLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNteRGALLTTHYMAEAeAVCDRVAIMVSGRLRCIGSIQHLKSK 1468
Cdd:cd03253 149 ARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKG--RTTIVIAHRLSTI-VNADKIIVLKDGRIVERGTHEELLAK 225
|
..
gi 6005701 1469 FG 1470
Cdd:cd03253 226 GG 227
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1267-1411 |
5.00e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 67.22 E-value: 5.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1267 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVllKGSGGGDalefLGYCPQENALW--PNLTVRQHLEVYA 1344
Cdd:PRK15064 336 KNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV--KWSENAN----IGYYAQDHAYDfeNDLTLFDWMSQWR 409
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6005701 1345 avkglRKGDAEVAIT----RLvdaLKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1411
Cdd:PRK15064 410 -----QEGDDEQAVRgtlgRL---LFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDME 472
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1235-1311 |
5.10e-11 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 65.91 E-value: 5.10e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6005701 1235 DEKPVIIASCLRKEYAgKRKGCFSKRKNKI-ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG 1311
Cdd:COG4608 3 MAEPLLEVRDLKKHFP-VRGGLFGRTVGVVkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDG 79
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
480-671 |
5.96e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 66.21 E-value: 5.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYkgkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKlseMADLENLSKL 559
Cdd:PRK11000 4 VTLRNVTKAY----GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKR---MNDVPPAERG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 560 TGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDK----------------------------------------EIFL 599
Cdd:PRK11000 77 VGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQrvnqvaevlqlahlldrkpkalsggqrqrvaigrtlvaepSVFL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6005701 600 LDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGSSLFLkkkwgigYH 671
Cdd:PRK11000 157 LDEPLSNLDAALRVQMRIEISRlhKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL-------YH 223
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1267-1456 |
6.62e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 64.34 E-value: 6.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1267 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKP----TAGQVLLKG------SGGGDALEFLGYCPQeNALWPNLTV 1336
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGkpvapcALRGRKIATIMQNPR-SAFNPLHTM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1337 RQHLEVYAAVKGLRKGDAevAITRLVDALKLQDQ---LKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQ 1413
Cdd:PRK10418 99 HTHARETCLALGKPADDA--TLTAALEAVGLENAarvLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQ 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 6005701 1414 QQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1456
Cdd:PRK10418 177 ARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1276-1465 |
6.78e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 64.81 E-value: 6.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1276 GEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGS--GGGDALEF---LGYCPQENALWPNLTVRQHLEV-----YAA 1345
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQplESWSSKAFarkVAYLPQQLPAAEGMTVRELVAIgrypwHGA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1346 VKGLRKGD---AEVAITrLVDALKLQDQLkspVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRA 1422
Cdd:PRK10575 117 LGRFGAADrekVEEAIS-LVGLKPLAHRL---VDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHR 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 6005701 1423 TFRntERGALLTT--HYMAEAEAVCDRVAIMVSGRLRCIGSIQHL 1465
Cdd:PRK10575 193 LSQ--ERGLTVIAvlHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1261-1469 |
6.80e-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: 66.75 E-value: 6.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1261 KNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITG--DTKPTAGQVLLKGS-----GGGDALEFLGY-CP------- 1325
Cdd:TIGR03269 11 DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYHVAlcekcGYVERPSKVGEpCPvcggtle 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1326 -QENALW-PNLTVRQHLEVYAAVKGLRK----GD-----------------AEVAITR---LVDALKLQDQLKSPVKTLS 1379
Cdd:TIGR03269 91 pEEVDFWnLSDKLRRRIRKRIAIMLQRTfalyGDdtvldnvlealeeigyeGKEAVGRavdLIEMVQLSHRITHIARDLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1380 EGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCI 1459
Cdd:TIGR03269 171 GGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIKEE 250
|
250
....*....|
gi 6005701 1460 GSIQHLKSKF 1469
Cdd:TIGR03269 251 GTPDEVVAVF 260
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1242-1471 |
6.82e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 64.71 E-value: 6.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1242 ASCLRKEYAGKrkGCFSKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGS-----GGGD 1316
Cdd:PRK10419 6 VSGLSHHYAHG--GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEplaklNRAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1317 ALEF-----LGYCPQENALWPNLTVRQHL-EVYAAVKGLRKGDAEVAITRLVDALKLQDQL--KSPvKTLSEGIKRKLCF 1388
Cdd:PRK10419 84 RKAFrrdiqMVFQDSISAVNPRKTVREIIrEPLRHLLSLDKAERLARASEMLRAVDLDDSVldKRP-PQLSGGQLQRVCL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1389 VLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL---RCIGSIQHL 1465
Cdd:PRK10419 163 ARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIvetQPVGDKLTF 242
|
....*.
gi 6005701 1466 KSKFGK 1471
Cdd:PRK10419 243 SSPAGR 248
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1267-1508 |
8.58e-11 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 64.49 E-value: 8.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1267 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITgDTKPTAGQVLLKG-SGGGDALE----FLGYCPQENALWPNlTVRQHLE 1341
Cdd:cd03289 21 ENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGvSWNSVPLQkwrkAFGVIPQKVFIFSG-TFRKNLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1342 VYAAVKG--LRKGDAEVAITRLVDAL--KLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPegqqQMW 1417
Cdd:cd03289 99 PYGKWSDeeIWKVAEEVGLKSVIEQFpgQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP----ITY 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1418 QAIRATFRNTERGA--LLTTHYMaEAEAVCDRVAIMVSGRLRCIGSIQHLKSKfgkdyllemkvKNLAQVEPLHAEILRL 1495
Cdd:cd03289 175 QVIRKTLKQAFADCtvILSEHRI-EAMLECQRFLVIEENKVRQYDSIQKLLNE-----------KSHFKQAISPSDRLKL 242
|
250
....*....|...
gi 6005701 1496 FPQAARQERYSSL 1508
Cdd:cd03289 243 FPRRNSSKSKRKP 255
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
504-638 |
9.52e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 66.69 E-value: 9.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 504 FDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLsemaDLENLS--KLTGVCPQSnvqfdF-----LTVR 576
Cdd:NF033858 287 FRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV----DAGDIAtrRRVGYMSQA-----FslygeLTVR 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 577 ENLRLFAKIKGILPQEVDK----------------------------------------EIFLLDEPTAGLDPFSRHQVW 616
Cdd:NF033858 358 QNLELHARLFHLPAAEIAArvaemlerfdladvadalpdslplgirqrlslavavihkpELLILDEPTSGVDPVARDMFW 437
|
170 180
....*....|....*....|....*
gi 6005701 617 NLLKE--RKtDRVILF-STQFMDEA 638
Cdd:NF033858 438 RLLIElsRE-DGVTIFiSTHFMNEA 461
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
483-555 |
9.54e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 63.68 E-value: 9.54e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6005701 483 RNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEM-----ADLEN 555
Cdd:PRK11629 9 DNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaakAELRN 86
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
1264-1409 |
1.29e-10 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 63.32 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1264 IATR--NVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTkPTAGQVLLkgsgGGDALE---------FLGYCPQENALWP 1332
Cdd:COG4138 8 VAGRlgPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILL----NGRPLSdwsaaelarHRAYLSQQQSPPF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1333 NLTVRQHLEVYAAvKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSIL-----GNPS--VVLLDEPS 1405
Cdd:COG4138 83 AMPVFQYLALHQP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptINPEgqLLLLDEPM 161
|
....
gi 6005701 1406 TGMD 1409
Cdd:COG4138 162 NSLD 165
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
481-557 |
1.43e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 63.41 E-value: 1.43e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6005701 481 RIRNVTKEYKGkpdkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVtIYNNKLSEMADLENLS 557
Cdd:PRK11701 8 SVRGLTKLYGP----RKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV-HYRMRDGQLRDLYALS 79
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
479-658 |
1.47e-10 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 64.72 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 479 AIRIRNVTKEYkgkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLEnlsK 558
Cdd:PRK10851 2 SIEIANIKKSF----GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD---R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 559 LTGVCPQSNVQFDFLTVRENL------------------------------------RLFAKIKGILPQEV--------D 594
Cdd:PRK10851 75 KVGFVFQHYALFRHMTVFDNIafgltvlprrerpnaaaikakvtqllemvqlahladRYPAQLSGGQKQRValaralavE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6005701 595 KEIFLLDEPTAGLDPFSRHQV--W--NLLKERKTDRVilFSTQFMDEADILADRKVFLSQGKLKCAGS 658
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKELrrWlrQLHEELKFTSV--FVTHDQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1270-1467 |
1.86e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 62.68 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1270 SFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDA--------LEFlgycpQENALWPNLTVRQH-- 1339
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTppsrrpvsMLF-----QENNLFSHLTVAQNig 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1340 ------LEVYAAVKGLRKGDAE-VAITRLVDALKLQdqlkspvktLSEGIKRKL----CFVLSilgNPsVVLLDEPSTGM 1408
Cdd:PRK10771 94 lglnpgLKLNAAQREKLHAIARqMGIEDLLARLPGQ---------LSGGQRQRValarCLVRE---QP-ILLLDEPFSAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6005701 1409 DPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKS 1467
Cdd:PRK10771 161 DPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1278-1467 |
1.91e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 63.58 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1278 VLGLLGHNGAGKSTSIKVITGDTKPTAG-----QVLLKGSG---GGDALEF---LGYCPQENALWPnLTVRQHleVYAAV 1346
Cdd:PRK14271 49 VTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSifnYRDVLEFrrrVGMLFQRPNPFP-MSIMDN--VLAGV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1347 KGLR-------KGDAEVAITR--LVDALKlqDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMW 1417
Cdd:PRK14271 126 RAHKlvprkefRGVAQARLTEvgLWDAVK--DRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIE 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6005701 1418 QAIRATFRNTErgALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKS 1467
Cdd:PRK14271 204 EFIRSLADRLT--VIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
479-658 |
2.42e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 63.28 E-value: 2.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 479 AIRIRNVTKEYkgkPD-KIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVP---TKGSVTIYNNKLSEMADLE 554
Cdd:PRK13640 5 IVEFKHVSFTY---PDsKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 555 NLSKLTGVCPQSNVQFDFLTVR-------EN--------LRLFAK---------------------------IKGILPqe 592
Cdd:PRK13640 82 IREKVGIVFQNPDNQFVGATVGddvafglENravprpemIKIVRDvladvgmldyidsepanlsggqkqrvaIAGILA-- 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6005701 593 VDKEIFLLDEPTAGLDPFSRHQVWNLLKERKTDR-VILFS-TQFMDEADiLADRKVFLSQGKLKCAGS 658
Cdd:PRK13640 160 VEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnLTVISiTHDIDEAN-MADQVLVLDDGKLLAQGS 226
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1265-1502 |
2.70e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 62.83 E-value: 2.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1265 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGggdaleflgyCPQENALWpnltVRQHL---- 1340
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGRE----------VNAENEKW----VRSKVglvf 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1341 -----EVYAAV-----------KGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEP 1404
Cdd:PRK13647 86 qdpddQVFSSTvwddvafgpvnMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1405 STGMDPEGQQQMwQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGsiqhlkskfGKDYLLEMKVKNLAQ 1484
Cdd:PRK13647 166 MAYLDPRGQETL-MEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG---------DKSLLTDEDIVEQAG 235
|
250
....*....|....*....
gi 6005701 1485 VE-PLHAEILRLFPQAARQ 1502
Cdd:PRK13647 236 LRlPLVAQIFEDLPELGQS 254
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1239-1411 |
2.98e-10 |
|
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: 64.96 E-value: 2.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1239 VIIASCLRKEYAGKrkgcfskrknkIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsggGDAL 1318
Cdd:TIGR03719 322 VIEAENLTKAFGDK-----------LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-----GETV 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1319 EfLGYCPQE-NALWPNLTVRQhlEVYAAVKGLRKGDAEVAITRLVDA--LKLQDQLKsPVKTLSEGIKRKLCFVLSILGN 1395
Cdd:TIGR03719 386 K-LAYVDQSrDALDPNKTVWE--EISGGLDIIKLGKREIPSRAYVGRfnFKGSDQQK-KVGQLSGGERNRVHLAKTLKSG 461
|
170
....*....|....*.
gi 6005701 1396 PSVVLLDEPSTGMDPE 1411
Cdd:TIGR03719 462 GNVLLLDEPTNDLDVE 477
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1265-1456 |
3.52e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 62.20 E-value: 3.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1265 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGD------ALEFLGYCPQENALWPNLTVRQ 1338
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwqtakiMREAVAIVPEGRRVFSRMTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1339 HLevyaAVKGL--RKGDAEVAITRLVDAL-KLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQ 1415
Cdd:PRK11614 100 NL----AMGGFfaERDQFQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQ 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 6005701 1416 MWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1456
Cdd:PRK11614 176 IFDTIE-QLREQGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1245-1441 |
3.66e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 62.41 E-value: 3.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1245 LRKEYAGKRkgcfskrknkiATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLL-----KGSGGGDALE 1319
Cdd:PRK11248 7 LYADYGGKP-----------ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLdgkpvEGPGAERGVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1320 FlgycpQENALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVV 1399
Cdd:PRK11248 76 F-----QNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 6005701 1400 LLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEA 1441
Cdd:PRK11248 151 LLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEA 192
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
480-653 |
3.87e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 62.80 E-value: 3.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEY-KGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVT-IYNN-------KLSEM 550
Cdd:PRK13651 3 IKVKNIVKIFnKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwIFKDeknkkktKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 551 ADLENLSKLT---------GVCPQSNVQFDF----------------------LTVRENLRLFAK--------------- 584
Cdd:PRK13651 83 VLEKLVIQKTrfkkikkikEIRRRVGVVFQFaeyqlfeqtiekdiifgpvsmgVSKEEAKKRAAKyielvgldesylqrs 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 585 -------------IKGILPQEVDkeIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQ 650
Cdd:PRK13651 163 pfelsggqkrrvaLAGILAMEPD--FLVFDEPTAGLDPQGVKEILEIFDNlNKQGKTIILVTHDLDNVLEWTKRTIFFKD 240
|
...
gi 6005701 651 GKL 653
Cdd:PRK13651 241 GKI 243
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
489-648 |
4.21e-10 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 60.71 E-value: 4.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 489 YKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTI-------YNNKLSEMAD--------- 552
Cdd:NF040873 2 YGGRP----VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRaggarvaYVPQRSEVPDslpltvrdl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 553 --------LENLSKLT--------------GVCPQSNVQFDFLTVRENLR-LFAKIkgiLPQEVDkeIFLLDEPTAGLDP 609
Cdd:NF040873 78 vamgrwarRGLWRRLTrddraavddalervGLADLAGRQLGELSGGQRQRaLLAQG---LAQEAD--LLLLDEPTTGLDA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 6005701 610 FSRHQVWNLLKE-RKTDRVILFSTQFMDEAdILADRKVFL 648
Cdd:NF040873 153 ESRERIIALLAEeHARGATVVVVTHDLELV-RRADPCVLL 191
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1268-1461 |
4.98e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 62.44 E-value: 4.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1268 NVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsggGDAL--------------EFLGYCPQ--ENALW 1331
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-----GDIVvsstskqkeikpvrKKVGVVFQfpESQLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1332 PNlTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQL--KSPVKtLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMD 1409
Cdd:PRK13643 99 EE-TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFweKSPFE-LSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6005701 1410 PEGQQQMWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1461
Cdd:PRK13643 177 PKARIEMMQLFE-SIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGT 227
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1267-1456 |
7.26e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 61.47 E-value: 7.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1267 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITG--DTKPTA---GQVLLKGSG--GGDALEF---LGYCPQENALWPNLTV 1336
Cdd:PRK14247 20 DGVNLEIPDNTITALMGPSGSGKSTLLRVFNRliELYPEArvsGEVYLDGQDifKMDVIELrrrVQMVFQIPNPIPNLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1337 RQHLEVYAAVKGLRKGDAEVAiTRLVDALK-------LQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMD 1409
Cdd:PRK14247 100 FENVALGLKLNRLVKSKKELQ-ERVRWALEkaqlwdeVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLD 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6005701 1410 PEGQQQmwqaIRATF--RNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1456
Cdd:PRK14247 179 PENTAK----IESLFleLKKDMTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1263-1468 |
7.72e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 61.96 E-value: 7.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1263 KIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQV-----LLKGSGGGDALEFL----GYCPQ--ENALW 1331
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVtigerVITAGKKNKKLKPLrkkvGIVFQfpEHQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1332 PNlTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQL--KSPVKtLSEGIKRKLCF--VLSIlgNPSVVLLDEPSTG 1407
Cdd:PRK13634 100 EE-TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELlaRSPFE-LSGGQMRRVAIagVLAM--EPEVLVLDEPTAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6005701 1408 MDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSK 1468
Cdd:PRK13634 176 LDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFAD 236
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1257-1456 |
1.09e-09 |
|
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: 60.56 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1257 FSKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG---------------SGGGDALEFL 1321
Cdd:cd03248 21 YPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGkpisqyehkylhskvSLVGQEPVLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1322 GYCPQENALWpNLTVRQHLEVYAAVKglrKGDAEVAITRLvdALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLL 1401
Cdd:cd03248 101 ARSLQDNIAY-GLQSCSFECVKEAAQ---KAHAHSFISEL--ASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLIL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6005701 1402 DEPSTGMDPEGQQQMWQAIRATfrNTERGALLTTHYMAEAEAVcDRVAIMVSGRL 1456
Cdd:cd03248 175 DEATSALDAESEQQVQQALYDW--PERRTVLVIAHRLSTVERA-DQILVLDGGRI 226
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1265-1481 |
1.33e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 61.18 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1265 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLL---KGSGGGDALEFLGYCPQENAL---WPNL---- 1334
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgdyAIPANLKKIKEVKRLRKEIGLvfqFPEYqlfq 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1335 -TVRQHLEVYAAVKGLRKGDAEVAITRLVDALKL-QDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEG 1412
Cdd:PRK13645 106 eTIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKG 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6005701 1413 QQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSI------QHLKSKFGKD----YLLEMKVKN 1481
Cdd:PRK13645 186 EEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPfeifsnQELLTKIEIDppklYQLMYKLKN 264
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1267-1475 |
1.42e-09 |
|
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: 60.32 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1267 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSgggDALEF--------LGYCPQENALWpNLTVRQ 1338
Cdd:cd03251 19 RDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGH---DVRDYtlaslrrqIGLVSQDVFLF-NDTVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1339 HLeVYAAvkgLRKGDAEV-AITRLVDAL----KLQDQLKSPVK----TLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMD 1409
Cdd:cd03251 95 NI-AYGR---PGATREEVeEAARAANAHefimELPEGYDTVIGergvKLSGGQRQRIAIARALLKDPPILILDEATSALD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6005701 1410 PEGQQQMWQAIRATFRNteRGALLTTHYMAEAEAVcDRVAIMVSGRLRCIGSIQHLKSKFGKDYLL 1475
Cdd:cd03251 171 TESERLVQAALERLMKN--RTTFVIAHRLSTIENA-DRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1267-1436 |
1.51e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.97 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1267 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITG--DTKPTAGQVLLkgsgggdaleflgycpQENALWPNLTVRQHLevya 1344
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDV----------------PDNQFGREASLIDAI---- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1345 avkgLRKGDAEVAITRLVDAlKLQDQ--LKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRA 1422
Cdd:COG2401 107 ----GRKGDFKDAVELLNAV-GLSDAvlWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQK 181
|
170
....*....|....
gi 6005701 1423 TFRNTERGALLTTH 1436
Cdd:COG2401 182 LARRAGITLVVATH 195
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1267-1501 |
1.68e-09 |
|
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: 63.01 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1267 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITgDTKPTAGQVLLKG-SGGGDALE----FLGYCPQENALWPNlTVRQHLE 1341
Cdd:TIGR01271 1236 QDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDGvSWNSVTLQtwrkAFGVIPQKVFIFSG-TFRKNLD 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1342 VYA--AVKGLRKGDAEVAITRLVDAL--KLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMW 1417
Cdd:TIGR01271 1314 PYEqwSDEEIWKVAEEVGLKSVIEQFpdKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIR 1393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1418 QAIRATFRNTErgALLTTHYMaEAEAVCDRVAIMVSGRLRCIGSIQ-------HLKSKFGkdyllemkvknlaqveplHA 1490
Cdd:TIGR01271 1394 KTLKQSFSNCT--VILSEHRV-EALLECQQFLVIEGSSVKQYDSIQkllnetsLFKQAMS------------------AA 1452
|
250
....*....|.
gi 6005701 1491 EILRLFPQAAR 1501
Cdd:TIGR01271 1453 DRLKLFPLHRR 1463
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1267-1456 |
1.87e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 60.37 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1267 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGS-------GGGDALEF-----------LGYCPQEN 1328
Cdd:PRK10619 22 KGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQtinlvrdKDGQLKVAdknqlrllrtrLTMVFQHF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1329 ALWPNLTVRQH-LEVYAAVKGLRKGDAEVAITRLVDALKLQD--QLKSPVKtLSEGIKRKLCFVLSILGNPSVVLLDEPS 1405
Cdd:PRK10619 102 NLWSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIDEraQGKYPVH-LSGGQQQRVSIARALAMEPEVLLFDEPT 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6005701 1406 TGMDPEgqqQMWQAIRATFRNTERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1456
Cdd:PRK10619 181 SALDPE---LVGEVLRIMQQLAEEGKtmVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1265-1465 |
1.93e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 60.41 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1265 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIK----VITGDTKPTAGQVLL------KGSGGGD---ALEFLGYCPQENALW 1331
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGSHIELLgrtvqrEGRLARDirkSRANTGYIFQQFNLV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1332 PNLTVRQHLEVYAA------------VKGLRKGDAEVAITRlVDALKLQDQlksPVKTLSEGIKRKLCFVLSILGNPSVV 1399
Cdd:PRK09984 99 NRLSVLENVLIGALgstpfwrtcfswFTREQKQRALQALTR-VGMVHFAHQ---RVSTLSGGQQQRVAIARALMQQAKVI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6005701 1400 LLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL 1465
Cdd:PRK09984 175 LADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1262-1494 |
2.31e-09 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 60.03 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1262 NKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG---SGGGD-----ALEFLgycPQENALWPN 1333
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpiSMLSSrqlarRLALL---PQHHLTPEG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1334 LTVRQHLEV----YAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGiKRKLCFVLSILG-NPSVVLLDEPSTGM 1408
Cdd:PRK11231 91 ITVRELVAYgrspWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGG-QRQRAFLAMVLAqDTPVVLLDEPTTYL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1409 DPEGQQQMWQAIRAtfRNTERGALLTT-HYMAEAEAVCDRVAIMVSGRLRCIGSIQHLkskfgkdylleMKVKNLAQVEP 1487
Cdd:PRK11231 170 DINHQVELMRLMRE--LNTQGKTVVTVlHDLNQASRYCDHLVVLANGHVMAQGTPEEV-----------MTPGLLRTVFD 236
|
....*..
gi 6005701 1488 LHAEILR 1494
Cdd:PRK11231 237 VEAEIHP 243
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1268-1492 |
2.45e-09 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 60.87 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1268 NVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGS--GGGDALE-FLGYCPQENALWPNLTVRQHLEVYA 1344
Cdd:PRK10851 20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvSRLHARDrKVGFVFQHYALFRHMTVFDNIAFGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1345 AVKGLRKGDAEVAI----TRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAI 1420
Cdd:PRK10851 100 TVLPRRERPNAAAIkakvTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6005701 1421 RATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFGKDYLLEMkvknLAQVEPLHAEI 1492
Cdd:PRK10851 180 RQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEF----MGEVNRLQGTI 247
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
492-621 |
2.49e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 61.78 E-value: 2.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 492 KPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLsVPTKGSVTIYNNKLSEMaDLE----NLSKLtGVCPQsn 567
Cdd:PRK11174 359 SPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELREL-DPEswrkHLSWV-GQNPQ-- 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 568 vqfdfL---TVRENLRL---------------FAKIKGI---LPQEVDKEI---------------------------FL 599
Cdd:PRK11174 434 -----LphgTLRDNVLLgnpdasdeqlqqaleNAWVSEFlplLPQGLDTPIgdqaaglsvgqaqrlalarallqpcqlLL 508
|
170 180
....*....|....*....|..
gi 6005701 600 LDEPTAGLDPFSRHQVWNLLKE 621
Cdd:PRK11174 509 LDEPTASLDAHSEQLVMQALNA 530
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1265-1470 |
2.99e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 61.76 E-value: 2.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1265 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsGGGDALEFlgycpQENALWPNLT-VRQHLEVY 1343
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILL---NGQPIADY-----SEAALRQAISvVSQRVHLF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1344 AAV--KGLRKGDAEVAITRLVDALK---LQDQLKSPV----------KTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGM 1408
Cdd:PRK11160 427 SATlrDNLLLAAPNASDEALIEVLQqvgLEKLLEDDKglnawlgeggRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGL 506
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6005701 1409 DPEGQQQMWQAIRATFRNteRGALLTTHYMAEAEAVcDRVAIMVSGRLRCIGSIQHLKSKFG 1470
Cdd:PRK11160 507 DAETERQILELLAEHAQN--KTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQELLAQQG 565
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1265-1465 |
3.57e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 60.12 E-value: 3.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1265 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGdtkptagqvLLKGSG--GGDAL----EFLGYCPQE----------- 1327
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMG---------LLAANGriGGSATfngrEILNLPEKElnklraeqism 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1328 ------NALWPNLTV-RQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKS----PvKTLSEGIKRKLCFVLSILGNP 1396
Cdd:PRK09473 102 ifqdpmTSLNPYMRVgEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRmkmyP-HEFSGGMRQRVMIAMALLCRP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6005701 1397 SVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL 1465
Cdd:PRK09473 181 KLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
480-639 |
3.91e-09 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 58.25 E-value: 3.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGKPDKIE-ALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNklsemadlenlsk 558
Cdd:cd03250 1 ISVEDASFTWDSGEQETSfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 559 lTGVCPQSN-VQFDflTVRENLrLFAK----------IKG--------ILPQ----EV---------------------- 593
Cdd:cd03250 68 -IAYVSQEPwIQNG--TIRENI-LFGKpfdeeryekvIKAcalepdleILPDgdltEIgekginlsggqkqrislaravy 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 6005701 594 -DKEIFLLDEPTAGLDPFSRHQVWN-----LLKERKTdrVILF--STQFMDEAD 639
Cdd:cd03250 144 sDADIYLLDDPLSAVDAHVGRHIFEncilgLLLNNKT--RILVthQLQLLPHAD 195
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1245-1411 |
3.99e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 61.10 E-value: 3.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1245 LRKEYAGKRKgcfskrknkiATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgSGGGDalefLGYC 1324
Cdd:TIGR03719 10 VSKVVPPKKE----------ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP--QPGIK----VGYL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1325 PQENALWPNLTVRQHLEvyAAVKGLRKgdaevAITRL-------------VDAL-----KLQDQLKS------------- 1373
Cdd:TIGR03719 74 PQEPQLDPTKTVRENVE--EGVAEIKD-----ALDRFneisakyaepdadFDKLaaeqaELQEIIDAadawdldsqleia 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6005701 1374 -----------PVKTLSEGIKRK--LCFVLsiLGNPSVVLLDEPSTGMDPE 1411
Cdd:TIGR03719 147 mdalrcppwdaDVTKLSGGERRRvaLCRLL--LSKPDMLLLDEPTNHLDAE 195
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
483-651 |
4.04e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 61.66 E-value: 4.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 483 RNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSG---LSVPTKGSVTIYNNKLSemadlENLSKL 559
Cdd:TIGR00956 763 RNLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAErvtTGVITGGDRLVNGRPLD-----SSFQRS 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 560 TGVCPQSNVQFDFLTVRENLRLFAKIKgiLPQEVDKE------------------------------------------- 596
Cdd:TIGR00956 838 IGYVQQQDLHLPTSTVRESLRFSAYLR--QPKSVSKSekmeyveevikllemesyadavvgvpgeglnveqrkrltigve 915
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6005701 597 -------IFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILfSTQFMDEADILA--DRKVFLSQG 651
Cdd:TIGR00956 916 lvakpklLLFLDEPTSGLDSQTAWSICKLMRKlADHGQAIL-CTIHQPSAILFEefDRLLLLQKG 979
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
480-658 |
4.16e-09 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 57.92 E-value: 4.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGKpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLS--VPTKGSVTIYNNKLSEMADLENLS 557
Cdd:cd03217 1 LEIKDLHVSVGGK----EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 558 KLTGVCPQSNVQFDFLTVRENLR-LFAKIKG----------ILPQEVDkeIFLLDEPTAGLDPFSRHQVWNLLKE-RKTD 625
Cdd:cd03217 77 LGIFLAFQYPPEIPGVKNADFLRyVNEGFSGgekkrneilqLLLLEPD--LAILDEPDSGLDIDALRLVAEVINKlREEG 154
|
170 180 190
....*....|....*....|....*....|....
gi 6005701 626 RVILFSTQFMDEAD-ILADRKVFLSQGKLKCAGS 658
Cdd:cd03217 155 KSVLIITHYQRLLDyIKPDRVHVLYDGRIVKSGD 188
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1260-1420 |
4.75e-09 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 58.71 E-value: 4.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1260 RKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGD-ALEFL----GYCPQENALWPNl 1334
Cdd:cd03249 13 RPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlNLRWLrsqiGLVSQEPVLFDG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1335 TVRQHLEvYaavkGLRKGDAEVAITRLVDA------LKLQDQLKSPV----KTLSEGIKRKLCFVLSILGNPSVVLLDEP 1404
Cdd:cd03249 92 TIAENIR-Y----GKPDATDEEVEEAAKKAnihdfiMSLPDGYDTLVgergSQLSGGQKQRIAIARALLRNPKILLLDEA 166
|
170
....*....|....*.
gi 6005701 1405 STGMDPEGQQQMWQAI 1420
Cdd:cd03249 167 TSALDAESEKLVQEAL 182
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1262-1461 |
4.93e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 58.91 E-value: 4.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1262 NKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITG-----DTK-PTAGQVLLKGSG--GGDALEF---LGYCPQENAL 1330
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRlieiyDSKiKVDGKVLYFGKDifQIDAIKLrkeVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1331 WPNLTVRQHLEVYAAVKGLR-----KGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPS 1405
Cdd:PRK14246 102 FPHLSIYDNIAYPLKSHGIKekreiKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6005701 1406 TGMDPEGQQQMWQAIraTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1461
Cdd:PRK14246 182 SMIDIVNSQAIEKLI--TELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGS 235
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
478-651 |
5.33e-09 |
|
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: 58.21 E-value: 5.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 478 EAIRIRNVTKEYK-----GKpdKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTI-YNNKLSEMA 551
Cdd:COG4778 3 TLLEVENLSKTFTlhlqgGK--RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrHDGGWVDLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 552 DLE-----NLSKLT-GVCPQsnvqfdFLTVR----------ENLR---------------LFAKIKgiLPQE-------- 592
Cdd:COG4778 81 QASpreilALRRRTiGYVSQ------FLRVIprvsaldvvaEPLLergvdreeararareLLARLN--LPERlwdlppat 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6005701 593 ----------------VDKEIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTqFMDEA--DILADRKVFLSQG 651
Cdd:COG4778 153 fsggeqqrvniargfiADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGI-FHDEEvrEAVADRVVDVTPF 228
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1269-1461 |
5.62e-09 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 58.66 E-value: 5.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1269 VSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsgGGDALEF----------------------LGYCPQ 1326
Cdd:COG4598 27 VSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRV----GGEEIRLkpdrdgelvpadrrqlqrirtrLGMVFQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1327 ENALWPNLTVRQHL-EVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEG------IKRKLCFvlsilgNPSVV 1399
Cdd:COG4598 103 SFNLWSHMTVLENViEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGqqqraaIARALAM------EPEVM 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6005701 1400 LLDEPSTGMDPEGQQQMWQAIRATfrnTERGA--LLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1461
Cdd:COG4598 177 LFDEPTSALDPELVGEVLKVMRDL---AEEGRtmLVVTHEMGFARDVSSHVVFLHQGRIEEQGP 237
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1267-1455 |
6.13e-09 |
|
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: 58.21 E-value: 6.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1267 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGG----DALEF---------LGYCPQenalwpN 1333
Cdd:COG4778 28 DGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWvdlaQASPReilalrrrtIGYVSQ------F 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1334 LTV--RQH-LEVYAAVkGLRKG-DAEVAITR---LVDALKLQDQLKS-PVKTLSEGIKRKLCFVLSILGNPSVVLLDEPS 1405
Cdd:COG4778 102 LRVipRVSaLDVVAEP-LLERGvDREEARARareLLARLNLPERLWDlPPATFSGGEQQRVNIARGFIADPPLLLLDEPT 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6005701 1406 TGMDPEGQQ---QMWQAIRAtfrnteRG-ALLT-THYMAEAEAVCDRVAIMVSGR 1455
Cdd:COG4778 181 ASLDAANRAvvvELIEEAKA------RGtAIIGiFHDEEVREAVADRVVDVTPFS 229
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1260-1456 |
6.72e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 58.68 E-value: 6.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1260 RKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGD-TKPTA-------GQVLLKGS--GGGDALEFL---GYCPQ 1326
Cdd:PRK13547 11 RRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDlTGGGAprgarvtGDVTLNGEplAAIDAPRLArlrAVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1327 ENALWPNLTVRQ--------HLEVYAAVKGLRKGDAEVAITRL-VDALKLQDqlkspVKTLSEGIKRKLCF--VLSIL-- 1393
Cdd:PRK13547 91 AAQPAFAFSAREivllgrypHARRAGALTHRDGEIAWQALALAgATALVGRD-----VTTLSGGELARVQFarVLAQLwp 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6005701 1394 -----GNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1456
Cdd:PRK13547 166 phdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAI 233
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
480-658 |
6.88e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 58.87 E-value: 6.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGK-PDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNK----LSEMADLE 554
Cdd:PRK13645 7 IILDNVSYTYAKKtPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAipanLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 555 NLSKLTGVCPQ------------SNVQFDFLTVRENLR-LFAKIKGIL-----PQE------------------------ 592
Cdd:PRK13645 87 RLRKEIGLVFQfpeyqlfqetieKDIAFGPVNLGENKQeAYKKVPELLklvqlPEDyvkrspfelsggqkrrvalagiia 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6005701 593 VDKEIFLLDEPTAGLDPFSRHQVWNL---LKERKTDRVILFsTQFMDEADILADRKVFLSQGKLKCAGS 658
Cdd:PRK13645 167 MDGNTLVLDEPTGGLDPKGEEDFINLferLNKEYKKRIIMV-THNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
479-542 |
7.02e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 59.47 E-value: 7.02e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6005701 479 AIRIRNVTKEYKGKpdkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTI 542
Cdd:PRK11650 3 GLKLQAVRKSYDGK---TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWI 63
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1257-1456 |
7.26e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 58.25 E-value: 7.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1257 FSKRKnkiATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVIT--GDTKP---TAGQVLLKG----SGGGDALEF---LGYC 1324
Cdd:PRK14239 15 YNKKK---ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPevtITGSIVYNGhniySPRTDTVDLrkeIGMV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1325 PQENALWPnltvrqhLEVYA-AVKGLR-KG--DAEVAITRLVDALK-------LQDQLKSPVKTLSEGIKRKLCFVLSIL 1393
Cdd:PRK14239 92 FQQPNPFP-------MSIYEnVVYGLRlKGikDKQVLDEAVEKSLKgasiwdeVKDRLHDSALGLSGGQQQRVCIARVLA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6005701 1394 GNPSVVLLDEPSTGMDPEGQQQmwqaIRATFRNTERG--ALLTTHYMAEAEAVCDRVAIMVSGRL 1456
Cdd:PRK14239 165 TSPKIILLDEPTSALDPISAGK----IEETLLGLKDDytMLLVTRSMQQASRISDRTGFFLDGDL 225
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
469-580 |
7.68e-09 |
|
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: 60.22 E-value: 7.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 469 QAPPEFQGKEAIRIRNVTKEYKgkPDKiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIynnkls 548
Cdd:COG5265 347 DAPPLVVGGGEVRFENVSFGYD--PER-PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILI------ 417
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 6005701 549 emaDLENLSKLT--------GVCPQSNVQF-DflTVRENLR 580
Cdd:COG5265 418 ---DGQDIRDVTqaslraaiGIVPQDTVLFnD--TIAYNIA 453
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
480-638 |
7.84e-09 |
|
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: 57.42 E-value: 7.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMaDLENLSKL 559
Cdd:cd03369 7 IEVENLSVRYA--PDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTI-PLEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 560 TGVCPQSNVQFDFlTVRENLRLFAKIKgilpqevDKEIFLLDEPTAGLDPFSRHQVWNLLKER---KTDRVILfstqfMD 636
Cdd:cd03369 84 LTIIPQDPTLFSG-TIRSNLDPFDEYS-------DEEIYGALRVSEGGLNLSQGQRQLLCLARallKRPRVLV-----LD 150
|
..
gi 6005701 637 EA 638
Cdd:cd03369 151 EA 152
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
482-559 |
8.14e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 60.12 E-value: 8.14e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6005701 482 IRNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMaDLENLSKL 559
Cdd:PRK10535 7 LKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATL-DADALAQL 83
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1268-1456 |
9.13e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 57.80 E-value: 9.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1268 NVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSG--GGDALEFL-----GYCPQENALWPNLTVrqhL 1340
Cdd:PRK09493 19 NIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKvnDPKVDERLirqeaGMVFQQFYLFPHLTA---L 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1341 EVYA----AVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQM 1416
Cdd:PRK09493 96 ENVMfgplRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEV 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 6005701 1417 WQAIRATfrnTERG--ALLTTHYMAEAEAVCDRVAIMVSGRL 1456
Cdd:PRK09493 176 LKVMQDL---AEEGmtMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1268-1455 |
9.68e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 59.72 E-value: 9.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1268 NVSFCVRKGEVLGLLGHNGAGKS-TSIKVI-----------TGDTKpTAGQVLLKGS--------GGGDALEFlgycpQE 1327
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSvTALSILrllpsppvvypSGDIR-FHGESLLHASeqtlrgvrGNKIAMIF-----QE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1328 N--ALWPNLTVRQHL-EVYAAVKGLRKGDAEVAITRLVDALKLQD---QLKSPVKTLSEGIKRKLCFVLSILGNPSVVLL 1401
Cdd:PRK15134 101 PmvSLNPLHTLEKQLyEVLSLHRGMRREAARGEILNCLDRVGIRQaakRLTDYPHQLSGGERQRVMIAMALLTRPELLIA 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 6005701 1402 DEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1455
Cdd:PRK15134 181 DEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1263-1482 |
9.95e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 58.27 E-value: 9.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1263 KIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGdtkptagqVLLKGSGGGDALEFLGYCPQENALWpnlTVRQHLE- 1341
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLING--------LLLPDDNPNSKITVDGITLTAKTVW---DIREKVGi 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1342 ---------VYAAV----------KGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCfVLSILG-NPSVVLL 1401
Cdd:PRK13640 89 vfqnpdnqfVGATVgddvafglenRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVA-IAGILAvEPKIIIL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1402 DEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEA-----VCDRVAIMVSGRLRCIGSIQHLKSKFGKDYLLE 1476
Cdd:PRK13640 168 DESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMadqvlVLDDGKLLAQGSPVEIFSKVEMLKEIGLDIPFV 247
|
....*.
gi 6005701 1477 MKVKNL 1482
Cdd:PRK13640 248 YKLKNK 253
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1276-1456 |
1.20e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 57.77 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1276 GEVLGLLGHNGAGKSTSIKVITGDTKPTAGQvLLKGSGG-GDALEFLGYCPQENALWPNLTVRQHLEVyaavkGLrKGDA 1354
Cdd:PRK11247 38 GQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-LLAGTAPlAEAREDTRLMFQDARLLPWKKVIDNVGL-----GL-KGQW 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1355 EVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLT 1434
Cdd:PRK11247 111 RDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLV 190
|
170 180
....*....|....*....|..
gi 6005701 1435 THYMAEAEAVCDRVAIMVSGRL 1456
Cdd:PRK11247 191 THDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1276-1420 |
1.20e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 59.80 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1276 GEVLGLLGHNGAGKSTSIKVITGDTKPTAGQV-LLKGSGGG----DALEFLGycPQENALwpnltvrQHLEVYAavkglr 1350
Cdd:PRK10636 338 GSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGyfaqHQLEFLR--ADESPL-------QHLARLA------ 402
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6005701 1351 KGDAEVAITRLVDALKLQ-DQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAI 1420
Cdd:PRK10636 403 PQELEQKLRDYLGGFGFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEAL 473
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1267-1436 |
1.22e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 60.24 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1267 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGdtKPTAGQVL--LKGSGGGDALEFL----GYCPQENALWPNLTVRQHL 1340
Cdd:PLN03140 897 REVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEgdIRISGFPKKQETFarisGYCEQNDIHSPQVTVRESL 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1341 eVYAAVKGLRKGDAEVAITRLVDA---LKLQDQLKSP------VKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1411
Cdd:PLN03140 975 -IYSAFLRLPKEVSKEEKMMFVDEvmeLVELDNLKDAivglpgVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDAR 1053
|
170 180
....*....|....*....|....*
gi 6005701 1412 GQQQMWQAIRATFrNTERGALLTTH 1436
Cdd:PLN03140 1054 AAAIVMRTVRNTV-DTGRTVVCTIH 1077
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1280-1411 |
1.25e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 59.36 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1280 GLLGHNGAGKSTSIKVITGDTKPTAGQ-VLLKGSGggdalefLGYCPQENALWPNLTVRQHLEvyAAVkglrkGDAEVAI 1358
Cdd:PRK11819 37 GVLGLNGAGKSTLLRIMAGVDKEFEGEaRPAPGIK-------VGYLPQEPQLDPEKTVRENVE--EGV-----AEVKAAL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1359 TRL-------------VDAL-----KLQDQLKS------------------------PVKTLSEGIKRK--LCFVLsiLG 1394
Cdd:PRK11819 103 DRFneiyaayaepdadFDALaaeqgELQEIIDAadawdldsqleiamdalrcppwdaKVTKLSGGERRRvaLCRLL--LE 180
|
170
....*....|....*..
gi 6005701 1395 NPSVVLLDEPSTGMDPE 1411
Cdd:PRK11819 181 KPDMLLLDEPTNHLDAE 197
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1269-1457 |
1.34e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 57.10 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1269 VSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSG-------GGDAL--EFLGYCPQENALWPNLTVRQH 1339
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPlhqmdeeARAKLraKHVGFVFQSFMLIPTLNALEN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1340 LEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQA 1419
Cdd:PRK10584 109 VELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADL 188
|
170 180 190
....*....|....*....|....*....|....*...
gi 6005701 1420 IRATFRNTERGALLTTHYMAEAeAVCDRVAIMVSGRLR 1457
Cdd:PRK10584 189 LFSLNREHGTTLILVTHDLQLA-ARCDRRLRLVNGQLQ 225
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
483-652 |
1.42e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 59.29 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 483 RNVTKEYKGKPDKIeALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVP-TKGSVTIYNNklSEMADLENLSKLTG 561
Cdd:TIGR00955 26 RLRGCFCRERPRKH-LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgVKGSGSVLLN--GMPIDAKEMRAISA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 562 VCPQSNVQFDFLTVRENL----------RLFAKIKGILPQEV-------------------------------------- 593
Cdd:TIGR00955 103 YVQQDDLFIPTLTVREHLmfqahlrmprRVTKKEKRERVDEVlqalglrkcantrigvpgrvkglsggerkrlafasell 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6005701 594 -DKEIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEADI--LADRKVFLSQGK 652
Cdd:TIGR00955 183 tDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELfeLFDKIILMAEGR 244
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
498-658 |
1.43e-08 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 58.89 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 498 ALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLS---KLTGVCPQSNVQFDFLT 574
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 575 VRENLRLFAKIKGILPQE----------------------------------------VDKEIFLLDEPTAGLDPFSRHQ 614
Cdd:PRK10070 123 VLDNTAFGMELAGINAEErrekaldalrqvglenyahsypdelsggmrqrvglaralaINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6005701 615 VWN-LLK-ERKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS 658
Cdd:PRK10070 203 MQDeLVKlQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGT 248
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1267-1456 |
1.44e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 59.29 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1267 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGS-----GGGDALEF-LGYCPQEnalwpnltvRQ-- 1338
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKeinalSTAQRLARgLVYLPED---------RQss 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1339 --HLE------VYAAVKGLR----KGDAEVAI-TRLVDALKLQ-DQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEP 1404
Cdd:PRK15439 351 glYLDaplawnVCALTHNRRgfwiKPARENAVlERYRRALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6005701 1405 STGMDPEGQQQMWQAIRA-TFRNTerGALLTTHYMAEAEAVCDRVAIMVSGRL 1456
Cdd:PRK15439 431 TRGVDVSARNDIYQLIRSiAAQNV--AVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
480-658 |
1.49e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 57.89 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGKpdkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEmADLENLSKL 559
Cdd:PRK13652 4 IETRDLCYSYSGS---KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITK-ENIREVRKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 560 TGVCPQS-------------------NVQFDFLTVR----ENLRLFA--------------------KIKGILPQEvdKE 596
Cdd:PRK13652 80 VGLVFQNpddqifsptveqdiafgpiNLGLDEETVAhrvsSALHMLGleelrdrvphhlsggekkrvAIAGVIAME--PQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6005701 597 IFLLDEPTAGLDPFSRHQVW---NLLKERKTDRVIlFSTQFMDEADILADRKVFLSQGKLKCAGS 658
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIdflNDLPETYGMTVI-FSTHQLDLVPEMADYIYVMDKGRIVAYGT 221
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1268-1454 |
1.61e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 57.45 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1268 NVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLlkgsgggdaleFLGYCPQENalwpNLT-VRQHLEV---- 1342
Cdd:PRK13648 27 DVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIF-----------YNNQAITDD----NFEkLRKHIGIvfqn 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1343 -----------YAAVKGLRK-----GDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPST 1406
Cdd:PRK13648 92 pdnqfvgsivkYDVAFGLENhavpyDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATS 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 6005701 1407 GMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAeAVCDRVAIMVSG 1454
Cdd:PRK13648 172 MLDPDARQNLLDLVRKVKSEHNITIISITHDLSEA-MEADHVIVMNKG 218
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
436-581 |
1.79e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 59.20 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 436 FLKSSFWSQTQKTDHVALEDEMdadPSFHDSfEQAPPEFQGKEAIRIRNVTKEYKGKPdkiEALKDLVFDIYEGQITAIL 515
Cdd:PRK13657 295 FINQVFMAAPKLEEFFEVEDAV---PDVRDP-PGAIDLGRVKGAVEFDDVSFSYDNSR---QGVEDVSFEAKPGQTVAIV 367
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6005701 516 GHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMAdLENLSKLTGVCPQSNVQFDfLTVRENLRL 581
Cdd:PRK13657 368 GPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT-RASLRRNIAVVFQDAGLFN-RSIEDNIRV 431
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1265-1479 |
1.80e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.86 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1265 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-----SGGGDALEF-LGYCPQENALWPNLTVRQ 1338
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGkevtfNGPKSSQEAgIGIIHQELNLIPQLTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1339 HL----EVYAAVKGL--RKGDAEVaiTRLVDALKLQDQLKSPVKTLSEG------IKRKLCFvlsilgNPSVVLLDEPST 1406
Cdd:PRK10762 99 NIflgrEFVNRFGRIdwKKMYAEA--DKLLARLNLRFSSDKLVGELSIGeqqmveIAKVLSF------ESKVIIMDEPTD 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6005701 1407 GMDPEGQQQMWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLrcIGsiQHLKSKFGKDYLLEMKV 1479
Cdd:PRK10762 171 ALTDTETESLFRVIR-ELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQF--IA--EREVADLTEDSLIEMMV 238
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1269-1456 |
1.87e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 57.41 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1269 VSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGS-----GGGDALEFLGYCPQE-NALWPNLTVRQHLEV 1342
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGElltaeNVWNLRRKIGMVFQNpDNQFVGATVEDDVAF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1343 YAAVKGLRKgdaEVAITRLVDAL----KLQDQLKSPVKtLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQ 1418
Cdd:PRK13642 106 GMENQGIPR---EEMIKRVDEALlavnMLDFKTREPAR-LSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMR 181
|
170 180 190
....*....|....*....|....*....|....*...
gi 6005701 1419 AIRATFRNTERGALLTTHYMAEAeAVCDRVAIMVSGRL 1456
Cdd:PRK13642 182 VIHEIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEI 218
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
482-552 |
1.94e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 56.99 E-value: 1.94e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6005701 482 IRNVTKEYKGKpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMAD 552
Cdd:PRK11247 15 LNAVSKRYGER----TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARE 81
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1267-1460 |
2.06e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 57.16 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1267 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITG--DTKPTA---GQVLLKG----SGGGDALEF---LGYCPQENALWPNL 1334
Cdd:PRK14267 21 KGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRllELNEEArveGEVRLFGrniySPDVDPIEVrreVGMVFQYPNPFPHL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1335 TVRQHLEVYAAVKGLRKGDAEVAiTRLVDALK-------LQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTG 1407
Cdd:PRK14267 101 TIYDNVAIGVKLNGLVKSKKELD-ERVEWALKkaalwdeVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTAN 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6005701 1408 MDPEGQQQMWQAIRATfrNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1460
Cdd:PRK14267 180 IDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVG 230
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
483-652 |
2.18e-08 |
|
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: 56.12 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 483 RNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPT---KGSVTiYNNKLSemadLENLSKL 559
Cdd:cd03233 7 RNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIH-YNGIPY----KEFAEKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 560 TG---VCPQSNVQFDFLTVRENLRLFAK------IKGI---------LPQEVDKE--IFLLDEPTAGLDPFSRHQVWNLL 619
Cdd:cd03233 82 PGeiiYVSEEDVHFPTLTVRETLDFALRckgnefVRGIsggerkrvsIAEALVSRasVLCWDNSTRGLDSSTALEILKCI 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 6005701 620 KE--RKTDRVILFS-TQFMDEADILADRKVFLSQGK 652
Cdd:cd03233 162 RTmaDVLKTTTFVSlYQASDEIYDLFDKVLVLYEGR 197
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1265-1456 |
2.23e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 57.48 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1265 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsgggDALEF---------------LGYCPQ--E 1327
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTV------DDITIthktkdkyirpvrkrIGMVFQfpE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1328 NALWPNLTVRqhlEVYAAVKGLRKGDAEVAitrlVDALKLQDQL--------KSPVKtLSEGIKRKLCFVlSILG-NPSV 1398
Cdd:PRK13646 96 SQLFEDTVER---EIIFGPKNFKMNLDEVK----NYAHRLLMDLgfsrdvmsQSPFQ-MSGGQMRKIAIV-SILAmNPDI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6005701 1399 VLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1456
Cdd:PRK13646 167 IVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1266-1460 |
2.25e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 58.12 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1266 TRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGD---ALEFLGYCPQENALWPNLTVRQHLEV 1342
Cdd:PRK11000 19 SKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDvppAERGVGMVFQSYALYPHLSVAENMSF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1343 YAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRA 1422
Cdd:PRK11000 99 GLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISR 178
|
170 180 190
....*....|....*....|....*....|....*...
gi 6005701 1423 TFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1460
Cdd:PRK11000 179 LHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1258-1456 |
2.64e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 57.55 E-value: 2.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1258 SKRKNKI-ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDALEFLGYCPQENA------- 1329
Cdd:PRK13631 33 EKQENELvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELITNPYSkkiknfk 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1330 ----------LWPNL-----TVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQL--KSPVKtLSEGIKRKLCF--VL 1390
Cdd:PRK13631 113 elrrrvsmvfQFPEYqlfkdTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSYleRSPFG-LSGGQKRRVAIagIL 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6005701 1391 SIlgNPSVVLLDEPSTGMDPEGQQQMWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1456
Cdd:PRK13631 192 AI--QPEILIFDEPTAGLDPKGEHEMMQLIL-DAKANNKTVFVITHTMEHVLEVADEVIVMDKGKI 254
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
477-653 |
2.87e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 56.77 E-value: 2.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 477 KEAIRIRNVTKEYKGKpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGL-----SVPTKGSVTIYN-NKLSEM 550
Cdd:PRK14267 2 KFAIETVNLRVYYGSN----HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGrNIYSPD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 551 ADLENLSKLTGVCPQSNVQFDFLTVRENLRLFAKIKGILP--QEVDK--------------------------------- 595
Cdd:PRK14267 78 VDPIEVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKskKELDErvewalkkaalwdevkdrlndypsnlsggqrqr 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6005701 596 -----------EIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEADILADRKVFLSQGKL 653
Cdd:PRK14267 158 lviaralamkpKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
479-648 |
3.05e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 56.58 E-value: 3.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 479 AIRIRNVTKEYkgkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLS-----VPTKGSVTIYNNKLSE-MAD 552
Cdd:PRK14258 7 AIKVNNLSFYY----DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNeleseVRVEGRVEFFNQNIYErRVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 553 LENLSK-LTGVCPQSNVqFDfLTVRENLRLFAKIKGILPQ-EVD------------------------------------ 594
Cdd:PRK14258 83 LNRLRRqVSMVHPKPNL-FP-MSVYDNVAYGVKIVGWRPKlEIDdivesalkdadlwdeikhkihksaldlsggqqqrlc 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6005701 595 --------KEIFLLDEPTAGLDPFSRHQVWNLLKER--KTDRVILFSTQFMDEADILADRKVFL 648
Cdd:PRK14258 161 iaralavkPKVLLMDEPCFGLDPIASMKVESLIQSLrlRSELTMVIVSHNLHQVSRLSDFTAFF 224
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
498-649 |
3.07e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 56.71 E-value: 3.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 498 ALKDLVFDIYEGQITAILGHSGAGKSTLL---NILSGL--SVPTKGSVTIYNNKL--SEMADLENLSKLTGVC------P 564
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILrcfNRLNDLipGFRVEGKVTFHGKNLyaPDVDPVEVRRRIGMVFqkpnpfP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 565 QS---NVQF-----------DFLtVRENLR---LFAKIKGILPQE-------------------VDKEIFLLDEPTAGLD 608
Cdd:PRK14243 105 KSiydNIAYgaringykgdmDEL-VERSLRqaaLWDEVKDKLKQSglslsggqqqrlciaraiaVQPEVILMDEPCSALD 183
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 6005701 609 PFSRHQVWNLLKERKTDRVILFSTQFMDEADILADRKVFLS 649
Cdd:PRK14243 184 PISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFN 224
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
480-554 |
3.68e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 57.98 E-value: 3.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGKPDKIEALKDLV----------------FDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTI- 542
Cdd:PRK13545 5 VKFEHVTKKYKMYNKPFDKLKDLFfrskdgeyhyalnnisFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIk 84
|
90 100
....*....|....*....|...
gi 6005701 543 -----------YNNKLSEMADLE 554
Cdd:PRK13545 85 gsaaliaissgLNGQLTGIENIE 107
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
484-658 |
3.74e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 56.06 E-value: 3.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 484 NVTKEYKGKpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLSKLTGVC 563
Cdd:PRK10895 8 NLAKAYKGR----RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 564 PQSNVQFDFLTVRENLRLFAKIKGILPQEVDKE-----------------------------------------IFLLDE 602
Cdd:PRK10895 84 PQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDranelmeefhiehlrdsmgqslsggerrrveiaralaanpkFILLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 6005701 603 PTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS 658
Cdd:PRK10895 164 PFAGVDPISVIDIKRIIEHlRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
480-658 |
4.19e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 56.28 E-value: 4.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGKPDKIeALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLSKL 559
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKY-TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 560 TGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEV-----------------DKE-----------------------IFL 599
Cdd:PRK13650 84 GMVFQNPDNQFVGATVEDDVAFGLENKGIPHEEMkervnealelvgmqdfkEREparlsggqkqrvaiagavamrpkIII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6005701 600 LDEPTAGLDPFSRHQVWNLLKERKTDR--VILFSTQFMDEAdILADRKVFLSQGKLKCAGS 658
Cdd:PRK13650 164 LDEATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDEV-ALSDRVLVMKNGQVESTST 223
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1273-1421 |
5.12e-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: 55.84 E-value: 5.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1273 VRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDALEFLGYCPQ-------ENALWPNLTVRQHLEVYAA 1345
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDEILDEFRGSELQnyftkllEGDVKVIVKPQYVDLIPKA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1346 VKG-----LRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAI 1420
Cdd:cd03236 103 VKGkvgelLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLI 182
|
.
gi 6005701 1421 R 1421
Cdd:cd03236 183 R 183
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
471-542 |
5.27e-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: 5.27e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6005701 471 PPEFQGKEAIRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTI 542
Cdd:TIGR03719 314 PGPRLGDKVIEAENLTKAFGDKL----LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI 381
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
501-592 |
5.65e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 54.81 E-value: 5.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 501 DLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEM-----ADLENLSKLTGVCPQsnvqfdfLTV 575
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQrdeyhQDLLYLGHQPGIKTE-------LTA 91
|
90
....*....|....*..
gi 6005701 576 RENLRLFAKIKGILPQE 592
Cdd:PRK13538 92 LENLRFYQRLHGPGDDE 108
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1253-1460 |
5.82e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.56 E-value: 5.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1253 RKGCFSKRKNKI-ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG------SGGG-----DALEF 1320
Cdd:PRK10261 326 RSGLLNRVTREVhAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqridtlSPGKlqalrRDIQF 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1321 LGYCPQEnALWPNLTVRQHLEVYAAVKGLRKGDAEVA-ITRLVD--ALKLQDQLKSPvKTLSEGIKRKLCFVLSILGNPS 1397
Cdd:PRK10261 406 IFQDPYA-SLDPRQTVGDSIMEPLRVHGLLPGKAAAArVAWLLErvGLLPEHAWRYP-HEFSGGQRQRICIARALALNPK 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6005701 1398 VVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1460
Cdd:PRK10261 484 VIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
480-548 |
6.20e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 55.95 E-value: 6.20e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6005701 480 IRIRNVTKEYKGKP-----DKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLS 548
Cdd:PRK15112 5 LEVRNLSKTFRYRTgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH 78
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1273-1450 |
7.58e-08 |
|
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: 54.12 E-value: 7.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1273 VRKGEVLGLLGHNGAGKSTSIKVITGDTKPTagqvllkgsgggdaleflgycpQENALWPNLTVrqhleVYaavkglrkg 1352
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPN----------------------GDNDEWDGITP-----VY--------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1353 daevaitrlvdalklqdqlKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGAL 1432
Cdd:cd03222 66 -------------------KPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTAL 126
|
170
....*....|....*...
gi 6005701 1433 LTTHYMAEAEAVCDRVAI 1450
Cdd:cd03222 127 VVEHDLAVLDYLSDRIHV 144
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1267-1455 |
7.63e-08 |
|
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: 54.40 E-value: 7.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1267 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSgggdalefLGYCPQENalW-PNLTVRQHL----- 1340
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--------IAYVSQEP--WiQNGTIRENIlfgkp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1341 ---EVYAAVkglrkgdaevaitrlVDALKLQDQLKSPVK-----------TLSEGIKRKLCFVLSILGNPSVVLLDEPST 1406
Cdd:cd03250 92 fdeERYEKV---------------IKACALEPDLEILPDgdlteigekgiNLSGGQKQRISLARAVYSDADIYLLDDPLS 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6005701 1407 GMDPE-GQQQMWQAIRATFRNtERGALLTTHYMAEAEAvCDRVAIMVSGR 1455
Cdd:cd03250 157 AVDAHvGRHIFENCILGLLLN-NKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1267-1474 |
7.80e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 55.42 E-value: 7.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1267 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITG--DTKPTAGQVLLKGSgggDALEFLgycPQEnalwpnltvRQHLEVYA 1344
Cdd:CHL00131 24 KGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGE---SILDLE---PEE---------RAHLGIFL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1345 A------VKGLRKGDaevaITRLVDALKLQDQLKSPVKTLS--EGIKRKLCFV------LS------------------- 1391
Cdd:CHL00131 89 AfqypieIPGVSNAD----FLRLAYNSKRKFQGLPELDPLEflEIINEKLKLVgmdpsfLSrnvnegfsggekkrneilq 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1392 -ILGNPSVVLLDEPSTGMDPEGQQQMWQAIRaTFRNTERGALLTTHYMAEAEAVC-DRVAIMVSGRLRCIGSIQ--HLKS 1467
Cdd:CHL00131 165 mALLDSELAILDETDSGLDIDALKIIAEGIN-KLMTSENSIILITHYQRLLDYIKpDYVHVMQNGKIIKTGDAElaKELE 243
|
....*..
gi 6005701 1468 KFGKDYL 1474
Cdd:CHL00131 244 KKGYDWL 250
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1268-1457 |
8.00e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 56.76 E-value: 8.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1268 NVSFCVRKGEVLGLLGHNGAGKSTSIKVITG------------DTKPTAGQVLLKGSGGGDALeflgyCPQE---NALWP 1332
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGaypgkfegnvfiNGKPVDIRNPAQAIRAGIAM-----VPEDrkrHGIVP 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1333 NLTVRQH--LEVYAAVKGLRKGDAEV---AITRLVDALKLQDQLKS-PVKTLSEGIKRKLCFVLSILGNPSVVLLDEPST 1406
Cdd:TIGR02633 353 ILGVGKNitLSVLKSFCFKMRIDAAAelqIIGSAIQRLKVKTASPFlPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6005701 1407 GMDPEGQQQMWQAIRATFRnteRGA--LLTTHYMAEAEAVCDRVAIMVSGRLR 1457
Cdd:TIGR02633 433 GVDVGAKYEIYKLINQLAQ---EGVaiIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
496-653 |
8.03e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 55.30 E-value: 8.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 496 IEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGL-----SVPTKGSVTIYNNKLSEMaDLENLSKLTGVCPQSNVQF 570
Cdd:PRK14247 16 VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKM-DVIELRRRVQMVFQIPNPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 571 DFLTVRENLRLFAKI-------------------KGILPQEV---------------------------DKEIFLLDEPT 604
Cdd:PRK14247 95 PNLSIFENVALGLKLnrlvkskkelqervrwaleKAQLWDEVkdrldapagklsggqqqrlciaralafQPEVLLADEPT 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6005701 605 AGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEADILADRKVFLSQGKL 653
Cdd:PRK14247 175 ANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1267-1444 |
8.65e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 57.04 E-value: 8.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1267 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSG----GGDAL-----EFLGYCPQENALWPNLTVR 1337
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDvatlDADALaqlrrEHFGFIFQRYHLLSHLTAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1338 QHLEVYAAVKGL----RKGDAEVAITRlvdaLKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPE-G 1412
Cdd:PRK10535 105 QNVEVPAVYAGLerkqRLLRAQELLQR----LGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHsG 180
|
170 180 190
....*....|....*....|....*....|....*
gi 6005701 1413 QQQMwqAIRATFRNTERGALLTTH---YMAEAEAV 1444
Cdd:PRK10535 181 EEVM--AILHQLRDRGHTVIIVTHdpqVAAQAERV 213
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1267-1471 |
8.86e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.43 E-value: 8.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1267 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDT----KPTAGQVLLKGSGGGDALEF----LGYCPQENALWPNLTVRQ 1338
Cdd:TIGR00956 78 KPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTdgfhIGVEGVITYDGITPEEIKKHyrgdVVYNAETDVHFPHLTVGE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1339 HLEVYAAVKGlrKGDAEVAITRLVDALKLQDQLKSP---------------VKTLSEGIKRKLCFVLSILGNPSVVLLDE 1403
Cdd:TIGR00956 158 TLDFAARCKT--PQNRPDGVSREEYAKHIADVYMATyglshtrntkvgndfVRGVSGGERKRVSIAEASLGGAKIQCWDN 235
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1404 PSTGMDPEGQQQMWQAIRATFRNTERGALLTThYMAEAEA--VCDRVAIMVSGRLRCIGSIQHLKSKFGK 1471
Cdd:TIGR00956 236 ATRGLDSATALEFIRALKTSANILDTTPLVAI-YQCSQDAyeLFDKVIVLYEGYQIYFGPADKAKQYFEK 304
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1276-1409 |
9.61e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 56.81 E-value: 9.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1276 GEVLGLLGHNGAGKSTSIKVITGDTKPT--AGQVLLKGSG-GGDALEFLGYCPQENALWPNLTVRQHLeVYAAVKGLRKG 1352
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKpTKQILKRTGFVTQDDILYPHLTVRETL-VFCSLLRLPKS 172
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6005701 1353 DAEVAITRLVDAL-------KLQDQL--KSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMD 1409
Cdd:PLN03211 173 LTKQEKILVAESViselgltKCENTIigNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
482-542 |
1.07e-07 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 56.61 E-value: 1.07e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6005701 482 IRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTI 542
Cdd:COG0488 1 LENLSKSFGGRP----LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI 57
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
471-582 |
1.67e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 56.28 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 471 PPEFQGKEAIRIRNVTKEYKgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEM 550
Cdd:PLN03130 1229 PPGWPSSGSIKFEDVVLRYR--PELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKF 1306
|
90 100 110
....*....|....*....|....*....|..
gi 6005701 551 AdLENLSKLTGVCPQSNVQFDFlTVRENLRLF 582
Cdd:PLN03130 1307 G-LMDLRKVLGIIPQAPVLFSG-TVRFNLDPF 1336
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1257-1457 |
2.08e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 54.27 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1257 FSKRKNKIaTRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITgDTKPTAGQVLLKGSgggdaLEFLGYCPQENALWPNLTV 1336
Cdd:PRK14258 15 FYYDTQKI-LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLN-RMNELESEVRVEGR-----VEFFNQNIYERRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1337 RQ-----------HLEVYAAVK-GLR------KGDAEVAITRLVDALKLQDQLKSPVKT----LSEGIKRKLCFVLSILG 1394
Cdd:PRK14258 88 RQvsmvhpkpnlfPMSVYDNVAyGVKivgwrpKLEIDDIVESALKDADLWDEIKHKIHKsaldLSGGQQQRLCIARALAV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6005701 1395 NPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLR 1457
Cdd:PRK14258 168 KPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENR 230
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
509-651 |
2.12e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 51.99 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 509 GQITAILGHSGAGKSTLLNILSGLSVPTKGSVtIYNNKLSEMADLENLSKLTGVCPQSNVQFDFLTVRenlRLFAKIKgi 588
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV-IYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLR---LALALAR-- 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6005701 589 lpqEVDKEIFLLDEPTAGLDPFSRHQVWNLL-------KERKTDRVILFSTQFMDEAD-----ILADRKVFLSQG 651
Cdd:smart00382 76 ---KLKPDVLILDEITSLLDAEQEALLLLLEelrllllLKSEKNLTVILTTNDEKDLGpallrRRFDRRIVLLLI 147
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1268-1436 |
2.36e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 53.56 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1268 NVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSgggDALEF--------LGYCPQENALWPNlTVRQH 1339
Cdd:PRK10247 25 NISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGE---DISTLkpeiyrqqVSYCAQTPTLFGD-TVYDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1340 LEVYAAVKGlrKGDAEVAITRLVDALKLQDQ-LKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQ 1418
Cdd:PRK10247 101 LIFPWQIRN--QQPDPAIFLDDLERFALPDTiLTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNE 178
|
170
....*....|....*...
gi 6005701 1419 AIRATFRNTERGALLTTH 1436
Cdd:PRK10247 179 IIHRYVREQNIAVLWVTH 196
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
480-653 |
3.02e-07 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 53.17 E-value: 3.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYkgkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNK-LSEMADLENLSK 558
Cdd:PRK09493 2 IEFKNVSKHF----GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKvNDPKVDERLIRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 559 LTGVC-------PQ----SNVQFDFLTVRENLR---------LFAKI-----KGILPQE----------------VDKEI 597
Cdd:PRK09493 78 EAGMVfqqfylfPHltalENVMFGPLRVRGASKeeaekqareLLAKVglaerAHHYPSElsggqqqrvaiaralaVKPKL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6005701 598 FLLDEPTAGLDPFSRHQVWNLLK---ERKTDRVILfsTQFMDEADILADRKVFLSQGKL 653
Cdd:PRK09493 158 MLFDEPTSALDPELRHEVLKVMQdlaEEGMTMVIV--THEIGFAEKVASRLIFIDKGRI 214
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
476-653 |
3.27e-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: 3.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 476 GKEAIRIRNVTkeYKGkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNnklsemADLEN 555
Cdd:COG3845 254 GEVVLEVENLS--VRD-DRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDG------EDITG 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 556 LS-----KL-----------TGVCPQsnvqfdfLTVRENL---------------------RLFAK-------IKG---- 587
Cdd:COG3845 325 LSprerrRLgvayipedrlgRGLVPD-------MSVAENLilgryrrppfsrggfldrkaiRAFAEelieefdVRTpgpd 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 588 --------------ILPQEVDKE--IFLLDEPTAGLDPFSRHQVWNLLKERKtDR---VILFSTQfMDEADILADRKVFL 648
Cdd:COG3845 398 tparslsggnqqkvILARELSRDpkLLIAAQPTRGLDVGAIEFIHQRLLELR-DAgaaVLLISED-LDEILALSDRIAVM 475
|
....*
gi 6005701 649 SQGKL 653
Cdd:COG3845 476 YEGRI 480
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1261-1459 |
3.31e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.74 E-value: 3.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1261 KNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGS--GGGDALEFL----------------- 1321
Cdd:PRK10982 259 LRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKkiNNHNANEAInhgfalvteerrstgiy 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1322 GYCPQE-NALWPNltVRQHLEVYAAVKGLR-KGDAEVAItrlvDALKLQD-QLKSPVKTLSEGIKRKLCFVLSILGNPSV 1398
Cdd:PRK10982 339 AYLDIGfNSLISN--IRNYKNKVGLLDNSRmKSDTQWVI----DSMRVKTpGHRTQIGSLSGGNQQKVIIGRWLLTQPEI 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6005701 1399 VLLDEPSTGMDPEGQQQMWQAIrATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCI 1459
Cdd:PRK10982 413 LMLDEPTRGIDVGAKFEIYQLI-AELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGI 472
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1268-1411 |
4.48e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.35 E-value: 4.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1268 NVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsggGDALEfLGYCPQE-NALWPNLTvrqhleVYAAV 1346
Cdd:PRK11819 342 DLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-----GETVK-LAYVDQSrDALDPNKT------VWEEI 409
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6005701 1347 KG----LRKGDAEVAITRLVDA--LKLQDQLKsPVKTLSEGiKRK---LCFVLSILGNpsVVLLDEPSTGMDPE 1411
Cdd:PRK11819 410 SGgldiIKVGNREIPSRAYVGRfnFKGGDQQK-KVGVLSGG-ERNrlhLAKTLKQGGN--VLLLDEPTNDLDVE 479
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
481-531 |
4.62e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 54.41 E-value: 4.62e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 6005701 481 RIRNVTKEYKGkpdkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSG 531
Cdd:NF040905 3 EMRGITKTFPG----VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
597-667 |
4.79e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 53.97 E-value: 4.79e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6005701 597 IFLLDEPTAGLDPFSRHQVWNLLKERKTD-RVILFSTQFMDEADILADRKVFLSQGKLKCAGSSLFLKKKWG 667
Cdd:NF000106 165 VLYLDEPTTGLDPRTRNEVWDEVRSMVRDgATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG 236
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1260-1470 |
4.86e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 54.73 E-value: 4.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1260 RKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSgggDALEF--------LGYCPQENALW 1331
Cdd:TIGR00958 491 RPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGV---PLVQYdhhylhrqVALVGQEPVLF 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1332 pNLTVRQHLevyaaVKGLRKG-DAEV-AITRLVDALKLQDQLKSPVKT--------LSEGIKRKLCFVLSILGNPSVVLL 1401
Cdd:TIGR00958 568 -SGSVRENI-----AYGLTDTpDEEImAAAKAANAHDFIMEFPNGYDTevgekgsqLSGGQKQRIAIARALVRKPRVLIL 641
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6005701 1402 DEPSTGMDPEGQQQMWQAIRAtfrnTERGALLTTHYMAEAEAvCDRVAIMVSGRLRCIGSIQHLKSKFG 1470
Cdd:TIGR00958 642 DEATSALDAECEQLLQESRSR----ASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQG 705
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1274-1409 |
6.07e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 54.02 E-value: 6.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1274 RKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQ---------VL--LKGSGGGDALEFLgycpQENalwpNLTVR---QH 1339
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDydeepswdeVLkrFRGTELQDYFKKL----ANG----EIKVAhkpQY 168
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6005701 1340 LEVYA-AVKG-----LRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMD 1409
Cdd:COG1245 169 VDLIPkVFKGtvrelLEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
478-594 |
6.54e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 52.51 E-value: 6.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 478 EAIRIRNVTKEY----------------KGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVT 541
Cdd:PRK13546 3 VSVNIKNVTKEYriyrtnkermkdalipKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 6005701 542 iYNNKLSEMADLENLS-KLTGVcpqSNVQFDFLTVRENLRlfaKIKGILPQEVD 594
Cdd:PRK13546 83 -RNGEVSVIAISAGLSgQLTGI---ENIEFKMLCMGFKRK---EIKAMTPKIIE 129
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
480-661 |
7.69e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 52.40 E-value: 7.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGKPDkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEmADLENLSKL 559
Cdd:PRK13642 5 LEVENLVFKYEKESD-VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTA-ENVWNLRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 560 TGVCPQS-NVQFDFLTVRENLRLFAKIKGILPQEVDK----------------------------------------EIF 598
Cdd:PRK13642 83 IGMVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKrvdeallavnmldfktreparlsggqkqrvavagiialrpEII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6005701 599 LLDEPTAGLDPFSRHQVWNLLKERKTDR--VILFSTQFMDEAdILADRKVFLSQGKL--KCAGSSLF 661
Cdd:PRK13642 163 ILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEA-ASSDRILVMKAGEIikEAAPSELF 228
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1265-1455 |
7.95e-07 |
|
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: 53.68 E-value: 7.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1265 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGdTKPTA---GQVL-----LKGSGGGDALEF-LGYCPQENALWPNLT 1335
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHGtwdGEIYwsgspLKASNIRDTERAgIVIIHQELTLVPELS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1336 VRQHL----EVyaAVKGLRKGDAevAITRLVDALKLQDQLKS-----PVKTLSEGIKRKLCFVLSILGNPSVVLLDEPST 1406
Cdd:TIGR02633 95 VAENIflgnEI--TLPGGRMAYN--AMYLRAKNLLRELQLDAdnvtrPVGDYGGGQQQLVEIAKALNKQARLLILDEPSS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6005701 1407 GMDPEGQQQMWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1455
Cdd:TIGR02633 171 SLTEKETEILLDIIR-DLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
497-657 |
8.08e-07 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 52.28 E-value: 8.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 497 EALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLS---------EMADLENL----SKLTGVC 563
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlKVADKNQLrllrTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 564 PQSNVqFDFLTVREN--------------------LRLFAKI------KGILP--------QEV--------DKEIFLLD 601
Cdd:PRK10619 99 QHFNL-WSHMTVLENvmeapiqvlglskqeareraVKYLAKVgideraQGKYPvhlsggqqQRVsiaralamEPEVLLFD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 602 EPTAGLDPFSRHQVWNLLK----ERKTDRVIlfsTQFMDEADILADRKVFLSQGKLKCAG 657
Cdd:PRK10619 178 EPTSALDPELVGEVLRIMQqlaeEGKTMVVV---THEMGFARHVSSHVIFLHQGKIEEEG 234
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1253-1311 |
8.20e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 52.48 E-value: 8.20e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 6005701 1253 RKGCFsKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG 1311
Cdd:PRK15112 17 RTGWF-RRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDD 74
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
499-657 |
8.47e-07 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 53.31 E-value: 8.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 499 LKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLsEMADLENLSKLTGVCPQ-SNVQFDFlTVRE 577
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDV-EALSARAASRRVASVPQdTSLSFEF-DVRQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 578 NLRL--------FAKI-------------KGILPQEVDKEI-----------------------FLLDEPTAGLDpfSRH 613
Cdd:PRK09536 97 VVEMgrtphrsrFDTWtetdraaverameRTGVAQFADRPVtslsggerqrvllaralaqatpvLLLDEPTASLD--INH 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 6005701 614 QVWNLLKERK---TDRVILFSTQFMDEADILADRKVFLSQGKLKCAG 657
Cdd:PRK09536 175 QVRTLELVRRlvdDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1262-1449 |
9.46e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 52.09 E-value: 9.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1262 NKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVI--TGDTKPTA---GQVLLKGS----GGGDALEF---LGYCPQENA 1329
Cdd:PRK14243 22 SFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPGFrveGKVTFHGKnlyaPDVDPVEVrrrIGMVFQKPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1330 LWPNlTVRQHLEVYAAVKGLrKGDAEVAITRLVDALKLQDQLKSPVKT----LSEGIKRKLCFVLSILGNPSVVLLDEPS 1405
Cdd:PRK14243 102 PFPK-SIYDNIAYGARINGY-KGDMDELVERSLRQAALWDEVKDKLKQsglsLSGGQQQRLCIARAIAVQPEVILMDEPC 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 6005701 1406 TGMDPEGQQQMWQAIRATFRntERGALLTTHYMAEAEAVCDRVA 1449
Cdd:PRK14243 180 SALDPISTLRIEELMHELKE--QYTIIIVTHNMQQAARVSDMTA 221
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
480-560 |
1.00e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 51.50 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGKPD-------------------KIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSG--LSVPTKG 538
Cdd:COG2401 8 FVLMRVTKVYSSVLDlservaivleafgvelrvvERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAG 87
|
90 100
....*....|....*....|...
gi 6005701 539 SVTIYNNKL-SEMADLENLSKLT 560
Cdd:COG2401 88 CVDVPDNQFgREASLIDAIGRKG 110
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1273-1409 |
1.15e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.27 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1273 VRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQ---------VL--LKGSGGGDALEFL-------GYCPQENALWPNl 1334
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDyeeepswdeVLkrFRGTELQNYFKKLyngeikvVHKPQYVDLIPK- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1335 tvrqhlevyaAVKG-----LRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMD 1409
Cdd:PRK13409 175 ----------VFKGkvrelLKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1262-1413 |
1.17e-06 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 51.91 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1262 NKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGS-----GGGDALEFLGYCPQeNALWP-NLT 1335
Cdd:PRK10253 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEhiqhyASKEVARRIGLLAQ-NATTPgDIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1336 VRQ--------HLEVYAAvkgLRKGDAEvAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTG 1407
Cdd:PRK10253 98 VQElvargrypHQPLFTR---WRKEDEE-AVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
....*.
gi 6005701 1408 MDPEGQ 1413
Cdd:PRK10253 174 LDISHQ 179
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
476-659 |
1.45e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 51.59 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 476 GKEAIRIRNVTKEYKGKPDKiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGL------SVPTKGSVTIYNNKLSE 549
Cdd:PRK14246 4 GKSAEDVFNISRLYLYINDK-AILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydsKIKVDGKVLYFGKDIFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 550 MaDLENLSKLTGVCPQSNVQFDFLTVRENLRLFAK---------IKGILPQEVDK------------------------- 595
Cdd:PRK14246 83 I-DAIKLRKEVGMVFQQPNPFPHLSIYDNIAYPLKshgikekreIKKIVEECLRKvglwkevydrlnspasqlsggqqqr 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6005701 596 -----------EIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGSS 659
Cdd:PRK14246 162 ltiaralalkpKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSS 236
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1263-1411 |
1.75e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 52.65 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1263 KIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsggGDALEfLGYCPQENA-LWPNLTVrqhle 1341
Cdd:PRK11147 332 KQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-----GTKLE-VAYFDQHRAeLDPEKTV----- 400
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6005701 1342 vyaaVKGLRKGDAEVAIT-RLVDALK-LQDQL------KSPVKTLSEGIKRKLcFVLSILGNPSVVL-LDEPSTGMDPE 1411
Cdd:PRK11147 401 ----MDNLAEGKQEVMVNgRPRHVLGyLQDFLfhpkraMTPVKALSGGERNRL-LLARLFLKPSNLLiLDEPTNDLDVE 474
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1245-1461 |
1.89e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 51.77 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1245 LRKEYAGKRKgcfskrknkiATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGD-------- 1316
Cdd:PRK11650 9 VRKSYDGKTQ----------VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNElepadrdi 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1317 ALEFLGYcpqenALWPNLTVRQHLEvYA-AVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGN 1395
Cdd:PRK11650 79 AMVFQNY-----ALYPHMSVRENMA-YGlKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVRE 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6005701 1396 PSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1461
Cdd:PRK11650 153 PAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGT 218
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1283-1411 |
2.48e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 49.87 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1283 GHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGD-ALEFLGYCPQENALWPNLTVRQHLEVYAAVKglrkgDAEVAITRL 1361
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNiAKPYCTYIGHNLGLKLEMTVFENLKFWSEIY-----NSAETLYAA 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 6005701 1362 VDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1411
Cdd:PRK13541 108 IHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKE 157
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
486-587 |
2.53e-06 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 49.80 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 486 TKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADlENLSKLTGVCPQ 565
Cdd:cd03231 3 ADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD-SIARGLLYLGHA 81
|
90 100
....*....|....*....|..
gi 6005701 566 SNVQfDFLTVRENLRLFAKIKG 587
Cdd:cd03231 82 PGIK-TTLSVLENLRFWHADHS 102
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
480-542 |
2.70e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 52.34 E-value: 2.70e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6005701 480 IRIRNVTKEYKGKPDkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTI 542
Cdd:PTZ00265 383 IQFKNVRFHYDTRKD-VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIII 444
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
1269-1403 |
2.99e-06 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 51.72 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1269 VSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsgGGDALEflgycpQENALWpnltVRQHlevYAAV-- 1346
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILL----DGQPVT------ADNREA----YRQL---FSAVfs 413
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6005701 1347 --------KGLRKGDAEVAITRLVDALKLQDQLK------SPVKtLSEGIKRKLCFVLSILGNPSVVLLDE 1403
Cdd:COG4615 414 dfhlfdrlLGLDGEADPARARELLERLELDHKVSvedgrfSTTD-LSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
480-554 |
3.17e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 49.87 E-value: 3.17e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6005701 480 IRIRNVTKEYKGKPdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLE 554
Cdd:PRK10908 2 IRFEHVSKAYLGGR---QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRE 73
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
493-531 |
3.41e-06 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 49.70 E-value: 3.41e-06
10 20 30
....*....|....*....|....*....|....*....
gi 6005701 493 PDKIEALKDLVfdiyEGQITAILGHSGAGKSTLLNILSG 531
Cdd:cd01854 73 GEGLDELRELL----KGKTSVLVGQSGVGKSTLLNALLP 107
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1265-1298 |
3.65e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.47 E-value: 3.65e-06
10 20 30
....*....|....*....|....*....|....
gi 6005701 1265 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITG 1298
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG 53
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
494-596 |
3.66e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 52.16 E-value: 3.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 494 DKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVP--TKGSVTIYNNKLSEmadlENLSKLTGVCPQSNVQFD 571
Cdd:PLN03140 891 DRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISGFPKKQ----ETFARISGYCEQNDIHSP 966
|
90 100
....*....|....*....|....*
gi 6005701 572 FLTVRENLRLFAKIKgiLPQEVDKE 596
Cdd:PLN03140 967 QVTVRESLIYSAFLR--LPKEVSKE 989
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1268-1456 |
3.90e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 50.51 E-value: 3.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1268 NVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG------SGGGDALEF---LGYCPQ--ENALWPNlTV 1336
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtlitstSKNKDIKQIrkkVGLVFQfpESQLFEE-TV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1337 RQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQL--KSPVKtLSEGIKRKLCfVLSILG-NPSVVLLDEPSTGMDPEGQ 1413
Cdd:PRK13649 104 LKDVAFGPQNFGVSQEEAEALAREKLALVGISESLfeKNPFE-LSGGQMRRVA-IAGILAmEPKILVLDEPTAGLDPKGR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6005701 1414 QQMWQairaTFRNTERGAL---LTTHYMAEAEAVCDRVAIMVSGRL 1456
Cdd:PRK13649 182 KELMT----LFKKLHQSGMtivLVTHLMDDVANYADFVYVLEKGKL 223
|
|
| RsgA |
COG1162 |
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis]; |
496-531 |
4.48e-06 |
|
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440776 [Multi-domain] Cd Length: 300 Bit Score: 50.50 E-value: 4.48e-06
10 20 30
....*....|....*....|....*....|....*.
gi 6005701 496 IEALKDLVfdiyEGQITAILGHSGAGKSTLLNILSG 531
Cdd:COG1162 157 LDELRELL----KGKTSVLVGQSGVGKSTLINALLP 188
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
505-644 |
4.78e-06 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 49.71 E-value: 4.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 505 DIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLS----------EMADLENLSKLT-GVCPQSNVQFDFL 573
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqyikadyEGTVRDLLSSITkDFYTHPYFKTEIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 574 TVrenlrlfAKIKGILPQEV-------------------DKEIFLLDEPTAGLDPFSRhqvwnLLKERKTDRVILF--ST 632
Cdd:cd03237 101 KP-------LQIEQILDREVpelsggelqrvaiaaclskDADIYLLDEPSAYLDVEQR-----LMASKVIRRFAENneKT 168
|
170
....*....|....*..
gi 6005701 633 QFMDEADI-----LADR 644
Cdd:cd03237 169 AFVVEHDIimidyLADR 185
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
509-587 |
7.30e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 49.01 E-value: 7.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 509 GQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMaDLENLSKL----TGVCPQSNVQFDFLTVRENLRLFAK 584
Cdd:PRK10584 36 GETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQM-DEEARAKLrakhVGFVFQSFMLIPTLNALENVELPAL 114
|
...
gi 6005701 585 IKG 587
Cdd:PRK10584 115 LRG 117
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1235-1311 |
9.05e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 49.58 E-value: 9.05e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6005701 1235 DEKPVIIASCLRKEYAGKRkGCFSKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG 1311
Cdd:PRK11308 1 SQQPLLQAIDLKKHYPVKR-GLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQG 76
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
478-548 |
9.25e-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: 50.17 E-value: 9.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 478 EAIRIRNVtkeykgkPDKIEalKDLV-------FDIY------EGQITAILGHSGAGKSTLLNILSGLSVPTKGsvtIYN 544
Cdd:COG1245 64 DAISIVNL-------PEELE--EDPVhrygengFRLYglpvpkKGKVTGILGPNGIGKSTALKILSGELKPNLG---DYD 131
|
....
gi 6005701 545 NKLS 548
Cdd:COG1245 132 EEPS 135
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1268-1436 |
1.10e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.49 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1268 NVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKP---TAGQVLLKGSGGGDALE-FLGYCPQENALWPNLTVRQHLEVY 1343
Cdd:TIGR00956 781 NVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLDSSFQrSIGYVQQQDLHLPTSTVRESLRFS 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1344 AAvkgLRKgDAEVAIT---RLVDA----LKLQDQLKSPVKTLSEGI----KRKLCFVLSILGNP-SVVLLDEPSTGMDPE 1411
Cdd:TIGR00956 861 AY---LRQ-PKSVSKSekmEYVEEviklLEMESYADAVVGVPGEGLnveqRKRLTIGVELVAKPkLLLFLDEPTSGLDSQ 936
|
170 180
....*....|....*....|....*
gi 6005701 1412 GQQQMWQAIRATfRNTERGALLTTH 1436
Cdd:TIGR00956 937 TAWSICKLMRKL-ADHGQAILCTIH 960
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
480-631 |
1.48e-05 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 48.70 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGKPDKIeaLKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLsVPTKGSVTIYNNKLSEMAdLENLSKL 559
Cdd:cd03289 3 MTVKDLTAKYTEGGNAV--LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWNSVP-LQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 560 TGVCPQSNVQFDFlTVRENLRLFAK--------------IKGILPQEVDK------------------------------ 595
Cdd:cd03289 79 FGVIPQKVFIFSG-TFRKNLDPYGKwsdeeiwkvaeevgLKSVIEQFPGQldfvlvdggcvlshghkqlmclarsvlska 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 6005701 596 EIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFS 631
Cdd:cd03289 158 KILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILS 193
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
482-631 |
1.60e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 49.91 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 482 IRNVTKEYKGKPDKIeaLKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLsVPTKGSVTIYNNKLSEMAdLENLSKLTG 561
Cdd:TIGR01271 1220 VQGLTAKYTEAGRAV--LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSVT-LQTWRKAFG 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 562 VCPQSNVQFDFlTVRENLRLFAK--------------IKGILPQEVDK------------------------------EI 597
Cdd:TIGR01271 1296 VIPQKVFIFSG-TFRKNLDPYEQwsdeeiwkvaeevgLKSVIEQFPDKldfvlvdggyvlsnghkqlmclarsilskaKI 1374
|
170 180 190
....*....|....*....|....*....|....
gi 6005701 598 FLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFS 631
Cdd:TIGR01271 1375 LLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILS 1408
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
471-542 |
1.78e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 49.35 E-value: 1.78e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6005701 471 PPEFQGKEAIRIRNVTKEYKgkpDKIeALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTI 542
Cdd:PRK11819 316 PGPRLGDKVIEAENLSKSFG---DRL-LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
477-530 |
1.96e-05 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 49.25 E-value: 1.96e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 6005701 477 KEAIRIRNVTKEYKGKpdKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILS 530
Cdd:PRK11176 339 KGDIEFRNVTFTYPGK--EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLT 390
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1253-1470 |
2.09e-05 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 49.56 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1253 RKGCFSKRKNKIATRN-VSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSgggdalefLGYCPQEnALW 1331
Cdd:TIGR00957 640 HNATFTWARDLPPTLNgITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--------VAYVPQQ-AWI 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1332 PNLTVRQHLEVYAAVKGLRKGDAEVAITRLVD--ALKLQDQLKSPVK--TLSEGIKRKLCFVLSILGNPSVVLLDEPSTG 1407
Cdd:TIGR00957 711 QNDSLRENILFGKALNEKYYQQVLEACALLPDleILPSGDRTEIGEKgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSA 790
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6005701 1408 MDPEGQQQMWQAI---RATFRNTERgaLLTTHYMAEAEAVcDRVAIMVSGRLRCIGSIQHLKSKFG 1470
Cdd:TIGR00957 791 VDAHVGKHIFEHVigpEGVLKNKTR--ILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQRDG 853
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1267-1409 |
2.65e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 49.14 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1267 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVllKGSGGgdalefLGYCPQENALWPNlTVRQHLevyaaV 1346
Cdd:TIGR01271 443 KNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI--KHSGR------ISFSPQTSWIMPG-TIKDNI-----I 508
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6005701 1347 KGLRKGdaEVAITRLVDALKLQDQL-KSPVK----------TLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMD 1409
Cdd:TIGR01271 509 FGLSYD--EYRYTSVIKACQLEEDIaLFPEKdktvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
493-531 |
2.68e-05 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 46.38 E-value: 2.68e-05
10 20 30
....*....|....*....|....*....|....*....
gi 6005701 493 PDKIEALKDLVfdiyEGQITAILGHSGAGKSTLLNILSG 531
Cdd:pfam03193 94 GEGIEALKELL----KGKTTVLAGQSGVGKSTLLNALLP 128
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
492-621 |
3.18e-05 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 47.78 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 492 KPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLSK-----------LT 560
Cdd:PRK15079 30 PPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVrsdiqmifqdpLA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 561 GVCPQSNV-------------QFDFLTVRENLRLFAKIKGILPQEVDK-----------------------EIFLLDEPT 604
Cdd:PRK15079 110 SLNPRMTIgeiiaeplrtyhpKLSRQEVKDRVKAMMLKVGLLPNLINRyphefsggqcqrigiaralilepKLIICDEPV 189
|
170
....*....|....*..
gi 6005701 605 AGLDPFSRHQVWNLLKE 621
Cdd:PRK15079 190 SALDVSIQAQVVNLLQQ 206
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
478-535 |
3.56e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 48.27 E-value: 3.56e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6005701 478 EAIRIRNVtkeykgkPDKIEalKDLV-------FDIY------EGQITAILGHSGAGKSTLLNILSGLSVP 535
Cdd:PRK13409 64 DAISIVNL-------PEELE--EEPVhrygvngFKLYglpipkEGKVTGILGPNGIGKTTAVKILSGELIP 125
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
509-600 |
3.90e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 48.34 E-value: 3.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 509 GQITAILGHSGAGKSTLLNILSGL--SVPTKGSVTIYNNKLSemadlENLSKLTGVCPQSNVQFDFLTVRENLRLFAKIK 586
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRiqGNNFTGTILANNRKPT-----KQILKRTGFVTQDDILYPHLTVRETLVFCSLLR 168
|
90
....*....|....
gi 6005701 587 giLPQEVDKEIFLL 600
Cdd:PLN03211 169 --LPKSLTKQEKIL 180
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
499-592 |
4.01e-05 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 46.63 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 499 LKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADlENLSKLTGVCPQSNVQF-DflTVRE 577
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP-EIYRQQVSYCAQTPTLFgD--TVYD 99
|
90
....*....|....*
gi 6005701 578 NLRLFAKIKGILPQE 592
Cdd:PRK10247 100 NLIFPWQIRNQQPDP 114
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
504-579 |
4.41e-05 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 46.91 E-value: 4.41e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6005701 504 FDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADlENLSKLTGVCPQSNVQ-FDFLTVRENL 579
Cdd:PRK11300 26 LEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPG-HQIARMGVVRTFQHVRlFREMTVIENL 101
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1267-1419 |
4.77e-05 |
|
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: 47.16 E-value: 4.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1267 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVllKGSGGgdalefLGYCPQENALWPNlTVRQHLEVYAAV 1346
Cdd:cd03291 54 KNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI--KHSGR------ISFSSQFSWIMPG-TIKENIIFGVSY 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6005701 1347 KGLRKGDAEVAITRLVDALKLQDQLKSPVK----TLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQA 1419
Cdd:cd03291 125 DEYRYKSVVKACQLEEDITKFPEKDNTVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFES 201
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1265-1298 |
4.89e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.86 E-value: 4.89e-05
10 20 30
....*....|....*....|....*....|....
gi 6005701 1265 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITG 1298
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1235-1291 |
5.64e-05 |
|
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: 47.76 E-value: 5.64e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 6005701 1235 DEKPVIIASCLRKEYAGKRkGCFSKRKNKI-ATRNVSFCVRKGEVLGLLGHNGAGKST 1291
Cdd:COG4172 271 DAPPLLEARDLKVWFPIKR-GLFRRTVGHVkAVDGVSLTLRRGETLGLVGESGSGKST 327
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1256-1410 |
5.86e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 47.66 E-value: 5.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1256 CFSKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSgggdaleflgycPQENALWPNLt 1335
Cdd:PRK10522 329 TFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK------------PVTAEQPEDY- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1336 vRQHlevYAAV-------KGLRKGDAEVAITRLVDA----LKLQDQLK------SPVKtLSEGIKRKLCFVLSILGNPSV 1398
Cdd:PRK10522 396 -RKL---FSAVftdfhlfDQLLGPEGKPANPALVEKwlerLKMAHKLEledgriSNLK-LSKGQKKRLALLLALAEERDI 470
|
170
....*....|..
gi 6005701 1399 VLLDEPSTGMDP 1410
Cdd:PRK10522 471 LLLDEWAADQDP 482
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
499-643 |
6.80e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 46.36 E-value: 6.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 499 LKDLVFDIYEGQITAILGHSGAGKSTLLNILSG--------LSVPTKGSVTIYNNKLSEMaDLENLSKLTGVCPQ-SNVQ 569
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltgggapRGARVTGDVTLNGEPLAAI-DAPRLARLRAVLPQaAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 570 FDFlTVRENLRL-------------------------------------------------FAKIKGIL-PQE---VDKE 596
Cdd:PRK13547 96 FAF-SAREIVLLgrypharragalthrdgeiawqalalagatalvgrdvttlsggelarvqFARVLAQLwPPHdaaQPPR 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6005701 597 IFLLDEPTAGLDPFSRHQV----------WNL----------LKERKTDRVILFStqfmdEADILAD 643
Cdd:PRK13547 175 YLLLDEPTAALDLAHQHRLldtvrrlardWNLgvlaivhdpnLAARHADRIAMLA-----DGAIVAH 236
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
480-540 |
7.30e-05 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 46.22 E-value: 7.30e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6005701 480 IRIRNVTKEYK-----GKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSV 540
Cdd:PRK10419 4 LNVSGLSHHYAhgglsGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNV 69
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1248-1471 |
9.29e-05 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 46.88 E-value: 9.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1248 EYAGKRKGCFskrknkiatrNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGD-ALEFL----G 1322
Cdd:PRK13657 343 SYDNSRQGVE----------DVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTvTRASLrrniA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1323 YCPQENALWpNLTVRQHLEVyaavkGlrKGDAEVAitRLVDALKLQDQL----KSPVK----------TLSEGIKRKLCF 1388
Cdd:PRK13657 413 VVFQDAGLF-NRSIEDNIRV-----G--RPDATDE--EMRAAAERAQAHdfieRKPDGydtvvgergrQLSGGERQRLAI 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1389 VLSILGNPSVVLLDEPSTGMDPEGQQQMWQAI------RATFRNTERgalLTThyMAEAeavcDRVAIMVSGRLRCIGSI 1462
Cdd:PRK13657 483 ARALLKDPPILILDEATSALDVETEAKVKAALdelmkgRTTFIIAHR---LST--VRNA----DRILVFDNGRVVESGSF 553
|
....*....
gi 6005701 1463 QHLKSKFGK 1471
Cdd:PRK13657 554 DELVARGGR 562
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
496-536 |
9.95e-05 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 46.35 E-value: 9.95e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 6005701 496 IEALKDLVfdiyEGQITAILGHSGAGKSTLLN-ILSGLSVPT 536
Cdd:PRK00098 155 LDELKPLL----AGKVTVLAGQSGVGKSTLLNaLAPDLELKT 192
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
498-643 |
1.04e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 44.62 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 498 ALKDLVFDIYEGQITAILGHSGAGKSTLLN----------ILSGLSVPTKgSVTIYNNKLSEMADLeNLSKLTGVCPQSN 567
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLVNeglyasgkarLISFLPKFSR-NKLIFIDQLQFLIDV-GLGYLTLGQKLST 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 568 vqfdfLTVRENLRLfaKIKGILPQEVDKEIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILF--STQFMDEADILAD 643
Cdd:cd03238 88 -----LSGGELQRV--KLASELFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGliDLGNTVILIehNLDVLSSADWIID 160
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
500-577 |
1.13e-04 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 45.75 E-value: 1.13e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6005701 500 KDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLEnLSKLTGVCPQSNVQFDFLTVRE 577
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKE-VARRIGLLAQNATTPGDITVQE 100
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
482-542 |
1.44e-04 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 45.87 E-value: 1.44e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6005701 482 IRNVTKEYkGKPDKIEalkDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTI 542
Cdd:PRK11432 9 LKNITKRF-GSNTVID---NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFI 65
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1267-1421 |
1.55e-04 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 45.07 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1267 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDAL-EFLGYCPQENALWPNLTVRQhLe 1341
Cdd:COG4604 18 DDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGldvaTTPSRELaKRLAILRQENHINSRLTVRE-L- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1342 V----YAAVKG-LRKGDaEVAITRLVDALKLQDQLKSPVKTLSEGiKRKLCFVLSILG-NPSVVLLDEPSTGMDPEGQQQ 1415
Cdd:COG4604 96 VafgrFPYSKGrLTAED-REIIDEAIAYLDLEDLADRYLDELSGG-QRQRAFIAMVLAqDTDYVLLDEPLNNLDMKHSVQ 173
|
....*.
gi 6005701 1416 MWQAIR 1421
Cdd:COG4604 174 MMKLLR 179
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
479-551 |
1.61e-04 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 46.25 E-value: 1.61e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6005701 479 AIRIRNVTKEYKGkpDKIeALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMA 551
Cdd:PRK10790 340 RIDIDNVSFAYRD--DNL-VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLS 409
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
479-584 |
1.94e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.51 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 479 AIRIRNVTKEYKgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMAdLENLSK 558
Cdd:PLN03232 1234 SIKFEDVHLRYR--PGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFG-LTDLRR 1310
|
90 100
....*....|....*....|....*.
gi 6005701 559 LTGVCPQSNVQFDFlTVRENLRLFAK 584
Cdd:PLN03232 1311 VLSIIPQSPVLFSG-TVRFNIDPFSE 1335
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
1263-1461 |
2.12e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 46.31 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1263 KIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSgggdalefLGYCPQEnALWPNLTVRQHLEV 1342
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERS--------IAYVPQQ-AWIMNATVRGNILF 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1343 YaavkglrkgDAEVAiTRLVDALKLQD------QLKSPVKT--------LSEGIKRKLCFVLSILGNPSVVLLDEPSTGM 1408
Cdd:PTZ00243 744 F---------DEEDA-ARLADAVRVSQleadlaQLGGGLETeigekgvnLSGGQKARVSLARAVYANRDVYLLDDPLSAL 813
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 6005701 1409 DPE-GQQQMWQAIRATFRNTERgaLLTTHYMaEAEAVCDRVAIMVSGRLRCIGS 1461
Cdd:PTZ00243 814 DAHvGERVVEECFLGALAGKTR--VLATHQV-HVVPRADYVVALGDGRVEFSGS 864
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1268-1309 |
2.25e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.65 E-value: 2.25e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 6005701 1268 NVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLL 1309
Cdd:PRK15064 19 NISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSL 60
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1269-1468 |
2.29e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.12 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1269 VSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGS-----GGGDALEFLGYCPQENALWPNlTVRQHLEVY 1343
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCdvakfGLTDLRRVLSIIPQSPVLFSG-TVRFNIDPF 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1344 AA------VKGLRKGDAEVAITRlvDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMW 1417
Cdd:PLN03232 1334 SEhndadlWEALERAHIKDVIDR--NPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQ 1411
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6005701 1418 QAIRATFRNTergALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSK 1468
Cdd:PLN03232 1412 RTIREEFKSC---TMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSR 1459
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
509-583 |
2.51e-04 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 44.45 E-value: 2.51e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6005701 509 GQITAILGHSGAGKSTLLNILSGLSvPTKGSVTIYNNKLSEMaDLENLSKLTGVCPQSNVQFDFLTVRENLRLFA 583
Cdd:COG4138 22 GELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDW-SAAELARHRAYLSQQQSPPFAMPVFQYLALHQ 94
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1278-1404 |
2.63e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 45.25 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 1278 VLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDALE--FL-------GYCPQENALWPNLTVRQHLEvYaavkG 1348
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKgiCLppekrriGYVFQDARLFPHYKVRGNLR-Y----G 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 6005701 1349 LRKGDAEvAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEP 1404
Cdd:PRK11144 101 MAKSMVA-QFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEP 155
|
|
| GAAP_like |
cd10429 |
Golgi antiapoptotic protein; GAAP (or transmembrane BAX inhibitor motif containing 4) is a ... |
266-373 |
3.03e-04 |
|
Golgi antiapoptotic protein; GAAP (or transmembrane BAX inhibitor motif containing 4) is a regulator of apoptosis that is related to the BAX inhibitor (BI)-1 like family of small transmembrane proteins, which have been shown to have an antiapoptotic effect either by stimulating the antiapoptotic function of Bcl-2, a well-characterized oncogene, or by inhibiting the proapoptotic effect of Bax, another member of the Bcl-2 family. Human GAAP has been linked to the modulation of intracellular fluxes of Ca(2+), by suppressing influx from the extracellular medium and reducing release from intracellular stores. A viral homolog (vaccinia virus vGAAP) acts similar to its human counterpart in inhibiting apoptosis.
Pssm-ID: 198411 Cd Length: 233 Bit Score: 44.13 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 266 WLSWGLLYAGFIFIMALFLALVIRSTQFIILSGFmvvfSLFLLYGLSLVALAFLMSILVKKSFLTGLVVFLLTV--FWGC 343
Cdd:cd10429 67 WLFLISLIGSLILLIALYWKRHSHPVNLILLSLF----TLCEAYTVGLVVSFYDGKIVLQALILTLGVFVGLTAytFQTK 142
|
90 100 110
....*....|....*....|....*....|
gi 6005701 344 LGFTSLYRHLPASLeWILSLLSPFAFMLGM 373
Cdd:cd10429 143 RDFSSFGALLFILL-WALILLALIFQFFPY 171
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1253-1292 |
3.09e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 45.47 E-value: 3.09e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 6005701 1253 RKGCFsKRK--NKIATRNVSFCVRKGEVLGLLGHNGAGKSTS 1292
Cdd:PRK15134 288 RKGIL-KRTvdHNVVVKNISFTLRPGETLGLVGESGSGKSTT 328
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
467-565 |
3.12e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.27 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 467 FEQAPPEFqgKEAIRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVtiynnK 546
Cdd:PRK15064 309 FEQDKKLH--RNALEVENLTKGFDNGP----LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-----K 377
|
90
....*....|....*....
gi 6005701 547 LSEMADLenlskltGVCPQ 565
Cdd:PRK15064 378 WSENANI-------GYYAQ 389
|
|
| NosY |
COG1277 |
ABC-type transport system involved in multi-copper enzyme maturation, permease component ... |
213-340 |
3.71e-04 |
|
ABC-type transport system involved in multi-copper enzyme maturation, permease component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440888 [Multi-domain] Cd Length: 201 Bit Score: 43.27 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 213 SFIGQSGVITDLYLFSCIISFSSFIYY------ASVNVTRERKR--MKALMTMmGLRDSAF--------WLSWGLLYAgF 276
Cdd:COG1277 36 GGAASGFLGLGLALLASLFSLLSLLLPllapalGMDAISGERESgtLELLLTL-PISRWEIvlgkflgaLLVLLLALL-I 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6005701 277 IFIMALFLALVIRSTQFIILSGFMVVFSLFLLYGLSLVALAFLMSILVKK---SFLTGLVVFLLTVF 340
Cdd:COG1277 114 TFLLALLLGLLLFGSPPPDLGAILGFYLGLLLLGLAFLAIGLFISALTRNqivAAILAIALWLLLVI 180
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
467-608 |
4.68e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 44.78 E-value: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 467 FEQAPP--EFQGKEAIRIRNVTKEYKGKPDKIEAlkdlvFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIyN 544
Cdd:COG1245 327 FEVHAPrrEKEEETLVEYPDLTKSYGGFSLEVEG-----GEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDE-D 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 545 NKLSemadlenlSKltgvcPQSnVQFDF-LTVRENLRLFAK-----------------IKGILPQEV------------- 593
Cdd:COG1245 401 LKIS--------YK-----PQY-ISPDYdGTVEEFLRSANTddfgssyykteiikplgLEKLLDKNVkdlsggelqrvai 466
|
170 180
....*....|....*....|.
gi 6005701 594 ------DKEIFLLDEPTAGLD 608
Cdd:COG1245 467 aaclsrDADLYLLDEPSAHLD 487
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
509-577 |
5.43e-04 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 43.62 E-value: 5.43e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6005701 509 GQITAILGHSGAGKSTLLNILSGLSVPTKGSVtIYNNKLSEMADLENLSKLTGVCPQSNVQFDFLTVRE 577
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEI-LLDAQPLESWSSKAFARKVAYLPQQLPAAEGMTVRE 104
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
499-585 |
6.38e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 42.55 E-value: 6.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 499 LKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSemadleNLSK--LTGVCPQSNVQFDfLTVR 576
Cdd:PRK13541 16 LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNIN------NIAKpyCTYIGHNLGLKLE-MTVF 88
|
....*....
gi 6005701 577 ENLRLFAKI 585
Cdd:PRK13541 89 ENLKFWSEI 97
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
480-659 |
6.41e-04 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 43.46 E-value: 6.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 480 IRIRNVTKEYKGKpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGS---VTIYNNKLSEMA----D 552
Cdd:PRK09984 5 IRVEKLAKTFNQH----QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAgshIELLGRTVQREGrlarD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 553 LENLSKLTGVCPQsnvQFDF---LTVREN---------------LRLFAKIK-------------------------GIL 589
Cdd:PRK09984 81 IRKSRANTGYIFQ---QFNLvnrLSVLENvligalgstpfwrtcFSWFTREQkqralqaltrvgmvhfahqrvstlsGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 590 PQEV--------DKEIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFST-QFMDEADILADRKVFLSQGKLKCAGSS 659
Cdd:PRK09984 158 QQRVaiaralmqQAKVILADEPIASLDPESARIVMDTLRDiNQNDGITVVVTlHQVDYALRYCERIVALRQGHVFYDGSS 237
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
483-542 |
6.64e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 43.80 E-value: 6.64e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6005701 483 RNVTKEY---KG---KPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTI 542
Cdd:PRK11308 9 IDLKKHYpvkRGlfkPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYY 74
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
458-540 |
7.03e-04 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 44.29 E-value: 7.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 458 DADPSFhdsfEQAPPEFQGKEAIRIRNVTKEYKGK-------PDKIEALKDLVFDIYEGQITAILGHSGAGKSTL-LNIL 529
Cdd:COG4172 258 AAEPRG----DPRPVPPDAPPLLEARDLKVWFPIKrglfrrtVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALL 333
|
90
....*....|.
gi 6005701 530 sGLsVPTKGSV 540
Cdd:COG4172 334 -RL-IPSEGEI 342
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
483-532 |
7.88e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 43.76 E-value: 7.88e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 6005701 483 RNVTKEYKGkpdkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGL 532
Cdd:PRK13549 9 KNITKTFGG----VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV 54
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
480-546 |
1.15e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 43.45 E-value: 1.15e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6005701 480 IRIRNVTKEYKGkpdkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVtIYNNK 546
Cdd:PRK10762 5 LQLKGIDKAFPG----VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSI-LYLGK 66
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
480-540 |
1.38e-03 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 42.41 E-value: 1.38e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6005701 480 IRIRNVTKEYKGKpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSV 540
Cdd:PRK09544 5 VSLENVSVSFGQR----RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI 61
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
494-531 |
1.47e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 42.32 E-value: 1.47e-03
10 20 30
....*....|....*....|....*....|....*...
gi 6005701 494 DKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSG 531
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG 55
|
|
| 7TMR-DISM_7TM |
pfam07695 |
7TM diverse intracellular signalling; This entry represents the transmembrane region of the ... |
267-421 |
1.95e-03 |
|
7TM diverse intracellular signalling; This entry represents the transmembrane region of the 7TM-DISM (7TM Receptors with Diverse Intracellular Signalling Modules).
Pssm-ID: 429600 [Multi-domain] Cd Length: 207 Bit Score: 41.49 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 267 LSWGLLYaGFIFIMA---LFLALVIRSTQFIILSGFMVVFSLFLLYGLSLVALAFLMSILVKKSFLTGLVVFLLTVFWGC 343
Cdd:pfam07695 3 LLLGLFY-GILLALAlynLFLFFSLRDRSYLYYVLYLLSFLLYQLSLNGLGFQYLWPNAPPWLNNKLLYLSLLLLLPFFA 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6005701 344 LGFTSLYRHLPASLEWILSLLSPFAFMLGMAQLLhldydlnsnAFPHPSDGSNLIVATNFMLAFDTCLYLALAIYFEK 421
Cdd:pfam07695 82 LLFARSFLELKKYLPRLLRLLLGLALLLALLLLL---------LPLFPYTLSLPLAQLLALLFILFLLLLGIIAWRKG 150
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
477-633 |
2.96e-03 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 41.41 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 477 KEAIRIRNVTKEYKgkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEmADLENl 556
Cdd:PRK15056 4 QAGIVVNDVTVTWR---NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ-ALQKN- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 557 skLTGVCPQS-NVQFDFLTVRENLRLFAKI--KGIL--PQEVDKEI---------------------------------- 597
Cdd:PRK15056 79 --LVAYVPQSeEVDWSFPVLVEDVVMMGRYghMGWLrrAKKRDRQIvtaalarvdmvefrhrqigelsggqkkrvflara 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 6005701 598 -------FLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQ 633
Cdd:PRK15056 157 iaqqgqvILLDEPFTGVDVKTEARIISLLRElRDEGKTMLVSTH 200
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1257-1311 |
3.41e-03 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 41.62 E-value: 3.41e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 6005701 1257 FSKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG 1311
Cdd:PRK15079 28 WQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLG 82
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
469-559 |
3.50e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 41.88 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 469 QAPPEFQgkeAIRIRNVTKEYkgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLS 548
Cdd:PRK10522 315 QAFPDWQ---TLELRNVTFAY---QDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT 388
|
90
....*....|.
gi 6005701 549 eMADLENLSKL 559
Cdd:PRK10522 389 -AEQPEDYRKL 398
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1265-1311 |
3.75e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 41.64 E-value: 3.75e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 6005701 1265 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG 1311
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQG 59
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
502-550 |
3.83e-03 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 40.69 E-value: 3.83e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 6005701 502 LVFDIYEGQITAILGHSGAGKSTLLNILSGLSvPTKGSVTIYNNKLSEM 550
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAW 62
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
501-579 |
4.32e-03 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 40.90 E-value: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 501 DLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMA--DLENLSKLTGVCPQSNVQFDFLTVREN 578
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsRLYTVRKRMSMLFQSGALFTDMNVFDN 104
|
.
gi 6005701 579 L 579
Cdd:PRK11831 105 V 105
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
499-532 |
4.73e-03 |
|
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: 39.44 E-value: 4.73e-03
10 20 30
....*....|....*....|....*....|....
gi 6005701 499 LKDLVFDIYEGQITAILGHSGAGKSTLLNILSGL 532
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGL 50
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
465-584 |
4.75e-03 |
|
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: 41.85 E-value: 4.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005701 465 DSFEQAPPEFQGKEAIRIRNVTKEY-KGKPdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILsglsvptkgsvtiy 543
Cdd:TIGR00957 622 DSIERRTIKPGEGNSITVHNATFTWaRDLP---PTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL-------------- 684
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 6005701 544 nnkLSEMADLENLSKLTG----VCPQSNVQFDflTVRENLrLFAK 584
Cdd:TIGR00957 685 ---LAEMDKVEGHVHMKGsvayVPQQAWIQND--SLRENI-LFGK 723
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
499-540 |
6.81e-03 |
|
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: 41.43 E-value: 6.81e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 6005701 499 LKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSV 540
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI 483
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
482-532 |
7.91e-03 |
|
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: 40.69 E-value: 7.91e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 6005701 482 IRNVTKEYkgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGL 532
Cdd:TIGR03719 7 MNRVSKVV---PPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV 54
|
|
| ABC_MutS2 |
cd03280 |
ATP-binding cassette domain of MutS2; MutS2 homologs in bacteria and eukaryotes. The MutS ... |
1377-1437 |
7.92e-03 |
|
ATP-binding cassette domain of MutS2; MutS2 homologs in bacteria and eukaryotes. The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family also possess a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213247 [Multi-domain] Cd Length: 200 Bit Score: 39.54 E-value: 7.92e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6005701 1377 TLSEGIKRkLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHY 1437
Cdd:cd03280 91 TFSSHMKN-IARILQHADPDSLVLLDELGSGTDPVEGAALAIAILEELLERGALVIATTHY 150
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
480-541 |
8.03e-03 |
|
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: 40.82 E-value: 8.03e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6005701 480 IRIRNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKS-TLLNIL----SGLSVPTkGSVT 541
Cdd:COG4172 7 LSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILrllpDPAAHPS-GSIL 72
|
|
| |
