|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
419-642 |
2.71e-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: 277.85 E-value: 2.71e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKPDKieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIynNKLSEMADLENLSKL 498
Cdd:cd03263 1 LQIRNLTKTYKKGTKP--AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYI--NGYSIRTDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 TGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFL 578
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1771853535 579 LDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGSSLFLK 642
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1224-1445 |
8.88e-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: 276.31 E-value: 8.88e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1224 LRKEYagkrkgcfsKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDALEF 1299
Cdd:cd03263 6 LTKTY---------KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirTDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1300 LGYCPQENALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVL 1379
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1771853535 1380 LDEPSTGMDPEGQQQMWQAIRATFRNteRGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLK 1445
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVRKG--RSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
174-729 |
3.84e-78 |
|
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: 287.29 E-value: 3.84e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 174 SFIYYASVNVT----RERKRMKALMTMMGLRDSAFWLSWgLLYAGFIFIMALFL-ALVIRSTQFIILSGFMVVFSLFLLY 248
Cdd:TIGR01257 662 AWIYSVSMTVKsivlEKELRLKETLKNQGVSNAVIWCTW-FLDSFSIMSMSIFLlTIFIMHGRILHYSDPFILFLFLLAF 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 249 GLSLVALAFLMSILVKKSFL----TGLVVFLLTV-FWGCLGFTSlyrHLPASLEWILSLLSPFAFMLGMAQLLHLDYD-- 321
Cdd:TIGR01257 741 STATIMQCFLLSTFFSKASLaaacSGVIYFTLYLpHILCFAWQD---RMTADLKTAVSLLSPVAFGFGTEYLVRFEEQgl 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 322 ----LNSNAFPHPSDGSNLIVATNFMLaFDTCLYLALAIYFEKILPNEYGHRRPPLFFLKSSFW-----------SQTQK 386
Cdd:TIGR01257 818 glqwSNIGNSPLEGDEFSFLLSMKMML-LDAALYGLLAWYLDQVFPGDYGTPLPWYFLLQESYWlggegcstreeRALEK 896
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 387 TDHVALEDEMDADPS-FHDSF-EQAPPEFQgkEAIRIRNVTK--EYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKS 462
Cdd:TIGR01257 897 TEPLTEEMEDPEHPEgINDSFfERELPGLV--PGVCVKNLVKifEPSGRP----AVDRLNITFYENQITAFLGHNGAGKT 970
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 463 TLLNILSGLSVPTKGSVTIYNNKLSemADLENLSKLTGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLE 542
Cdd:TIGR01257 971 TTLSILTGLLPPTSGTVLVGGKDIE--TNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLED 1048
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 543 LEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEADILAD 622
Cdd:TIGR01257 1049 TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGD 1128
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 623 RKVFLSQGKLKCAGSSLFLKKKWGIGYHLSL--QLNEI------------------------CVEE------------NI 664
Cdd:TIGR01257 1129 RIAIISQGRLYCSGTPLFLKNCFGTGFYLTLvrKMKNIqsqrggcegtcsctskgfstrcpaRVDEitpeqvldgdvnEL 1208
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1771853535 665 TSLVKQHIPDAKLSAKSEGKLIYTLPLE--RTNKFPELYKDL-DSYPDLGIENYGVSMTTLNEVFLKL 729
Cdd:TIGR01257 1209 MDLVYHHVPEAKLVECIGQELIFLLPNKnfKQRAYASLFRELeETLADLGLSSFGISDTPLEEIFLKV 1276
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1237-1448 |
5.46e-73 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 243.43 E-value: 5.46e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1237 SKR-KNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDALEFLGYCPQENALWP 1311
Cdd:COG1131 7 TKRyGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGedvaRDPAEVRRRIGYVPQEPALYP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1312 NLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEG 1391
Cdd:COG1131 87 DLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1771853535 1392 QQQMWQAIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKF 1448
Cdd:COG1131 167 RRELWELLRE-LAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
419-637 |
2.27e-69 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 233.03 E-value: 2.27e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEmaDLENLSKL 498
Cdd:COG1131 1 IEVRGLTKRYGDKT----ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR--DPAEVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 TGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFL 578
Cdd:COG1131 75 IGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 579 LDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS 637
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRElAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGT 214
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
972-1537 |
3.04e-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: 3.04e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 972 SSCPPYIAMSSIDDYKNRARSQLRISGLSPSAYWFGQALVDVSLY-----FLVFVFIYLMSYISNFEDMLLTIIHIIQIp 1046
Cdd:TIGR01257 1691 SFVPASFVLYLIQERVNKAKHLQFISGVSPTTYWLTNFLWDIMNYavsagLVVGIFIGFQKKAYTSPENLPALVALLML- 1769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1047 cavgYSFSLIFMTYVISFIFRKGRKNSGIWSFCFYVVTVFSVA-GFAFSIFESD------------IPFIFTFLIPPATM 1113
Cdd:TIGR01257 1770 ----YGWAVIPMMYPASFLFDVPSTAYVALSCANLFIGINSSAiTFVLELFENNrtllrfnamlrkLLIVFPHFCLGRGL 1845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1114 IGCLFLSSHLLFSSLFSEERmDVQPFL-------VFLIPFLHFIIFLFTLRCLEWKFGKKSMRKDPFFRISPRSSDVCQn 1186
Cdd:TIGR01257 1846 IDLALSQAVTDVYAQFGEEH-SANPFQwdligknLVAMAVEGVVYFLLTLLIQHHFFLSRWIAEPAKEPIFDEDDDVAE- 1923
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1187 peepegededvqmERVRTANALNSTNfdekpVIIASCLRKEYAGKrkgcfskrkNKIATRNVSFCVRKGEVLGLLGHNGA 1266
Cdd:TIGR01257 1924 -------------ERQRIISGGNKTD-----ILRLNELTKVYSGT---------SSPAVDRLCVGVRPGECFGLLGVNGA 1976
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1267 GKSTSIKVITGDTKPTAGQVLLKG----SGGGDALEFLGYCPQENALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVD 1342
Cdd:TIGR01257 1977 GKTTTFKMLTGDTTVTSGDATVAGksilTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQ 2056
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1343 ALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNtERGALLTTHYMAEAEA 1422
Cdd:TIGR01257 2057 SLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEA 2135
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1423 VCDRVAIMVSGRLRCIGSIQHLKSKFGKDYLLEMKVKN-----LAQVEPLHAEILRLFPQAARQERYSSLMVYKLPVEDv 1497
Cdd:TIGR01257 2136 LCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMKIKSpkddlLPDLNPVEQFFQGNFPGSVQRERHYNMLQFQVSSSS- 2214
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1771853535 1498 qpLAQAFFKLEKVKQSFDLEEYSLSQSTLEQVFLELSKEQ 1537
Cdd:TIGR01257 2215 --LARIFQLLISHKDSLLIEEYSVTQTTLDQVFVNFAKQQ 2252
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
419-637 |
1.35e-59 |
|
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: 205.09 E-value: 1.35e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIyNNKLSEMADLENLSKL 498
Cdd:COG4555 2 IEVENLSKKYGKVP----ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILI-DGEDVRKEPREARRQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 tGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFL 578
Cdd:COG4555 77 -GVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 579 LDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS 637
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRAlKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGS 215
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1240-1468 |
5.79e-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: 194.69 E-value: 5.79e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1240 KNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGD----ALEFLGYCPQENALWPNLTV 1315
Cdd:COG4555 12 GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKepreARRQIGVLPDERGLYDRLTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1316 RQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQM 1395
Cdd:COG4555 92 RENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1771853535 1396 WQAIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFGKDYLLEMKVKNLAQVEPLH 1468
Cdd:COG4555 172 REILRA-LKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEENLEDAFVALIGSEEGEA 243
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1237-1435 |
2.65e-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: 189.92 E-value: 2.65e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1237 SKR-KNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDALEFLGYCPQENALWP 1311
Cdd:cd03230 7 SKRyGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGkdikKEPEEVKRRIGYLPEEPSLYE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1312 NLTVRQHLEvyaavkglrkgdaevaitrlvdalklqdqlkspvktLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEG 1391
Cdd:cd03230 87 NLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPES 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1771853535 1392 QQQMWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1435
Cdd:cd03230 131 RREFWELLR-ELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
419-632 |
9.71e-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: 188.38 E-value: 9.71e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEmaDLENLSKL 498
Cdd:cd03230 1 IEVRNLSKRYGKKT----ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK--EPEEVKRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 TGVCPQSNVQFDFLTVRENLRlfakikgilpqevdkeiqrvllelemkniqdvlaqnLSGGQKRKLTFGIAILGDPQIFL 578
Cdd:cd03230 75 IGYLPEEPSLYENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1771853535 579 LDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKL 632
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1237-1538 |
1.22e-54 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 193.02 E-value: 1.22e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1237 SKR-KNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSG-GGDALEFLGYCPQENALWPNLT 1314
Cdd:COG4152 8 TKRfGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPlDPEDRRRIGYLPEERGLYPKMK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1315 VRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQ 1394
Cdd:COG4152 88 VGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVEL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1395 MWQAIRATfrnTERGA--LLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFGkdyllemkvKNLAQVEPLH-AEI 1471
Cdd:COG4152 168 LKDVIREL---AAKGTtvIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFG---------RNTLRLEADGdAGW 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1771853535 1472 LRLFPQAARQERYSSLMVYKLP-VEDVQPLaqaffkLEKVKQSFDLEEYSLSQSTLEQVFLELSKEQE 1538
Cdd:COG4152 236 LRALPGVTVVEEDGDGAELKLEdGADAQEL------LRALLARGPVREFEEVRPSLNEIFIEVVGEKA 297
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
1238-1533 |
6.49e-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: 6.49e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1238 KRKNKI-ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDALEFLGYCPQENALWPN 1312
Cdd:TIGR01188 1 KVYGDFkAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGydvvREPRKVRRSIGIVPQYASVDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1313 LTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQ 1392
Cdd:TIGR01188 81 LTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1393 QQMWQAIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFGKDYlLEMKVKNLAQVEPLHAEIL 1472
Cdd:TIGR01188 161 RAIWDYIRA-LKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGKDT-LESRPRDIQSLKVEVSMLI 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1771853535 1473 RLFP--QAARQERYSSLMVYKLPVEDVQPLAQAFFKlEKVKQSFDLEEYSLSQSTLEQVFLEL 1533
Cdd:TIGR01188 239 AELGetGLGLLAVTVDSDRIKILVPDGDETVPEIVE-AAIRNGIRIRSISTERPSLDDVFLKL 300
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1219-1445 |
1.26e-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: 1.26e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1219 IIASCLRKEYAGKRkgcfskrknkiATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGG 1294
Cdd:cd03265 1 IEVENLVKKYGDFE-----------AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvREPR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1295 DALEFLGYCPQENALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGN 1374
Cdd:cd03265 70 EVRRRIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1771853535 1375 PSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLK 1445
Cdd:cd03265 150 PEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
419-632 |
5.54e-48 |
|
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: 170.75 E-value: 5.54e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLEnLSKL 498
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKE-LAAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 ----TGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDP 574
Cdd:cd03255 80 rrrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 575 QIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADiLADRKVFLSQGKL 632
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
419-633 |
3.65e-47 |
|
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: 168.14 E-value: 3.65e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKpdkiEALKDLVFDIYEGqITAILGHSGAGKSTLLNILSGLSVPTKGSVTIynNKLSEMADLENLSKL 498
Cdd:cd03264 1 LQLENLTKRYGKK----RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRI--DGQDVLKQPQKLRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 TGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFL 578
Cdd:cd03264 74 IGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1771853535 579 LDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEADILADRKVFLSQGKLK 633
Cdd:cd03264 154 VDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1236-1439 |
6.12e-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: 167.46 E-value: 6.12e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1236 FSKR-KNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDAL-EFLGYCPQENALWPNL 1313
Cdd:cd03269 6 VTKRfGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAArNRIGYLPEERGLYPKM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1314 TVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQ 1393
Cdd:cd03269 86 KVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1771853535 1394 QMWQAIRATFRNtERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1439
Cdd:cd03269 166 LLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
419-637 |
7.16e-47 |
|
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: 168.28 E-value: 7.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYkgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEmADLENLSKL 498
Cdd:COG1122 1 IELENLSFSY---PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITK-KNLRELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 TGVCPQ-SNVQFDFLTVRENLrLFA-KIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLtfgiAILG---- 572
Cdd:COG1122 77 VGLVFQnPDDQLFAPTVEEDV-AFGpENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRV----AIAGvlam 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1771853535 573 DPQIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS 637
Cdd:COG1122 152 EPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGT 217
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
433-731 |
3.31e-46 |
|
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: 168.72 E-value: 3.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 433 DKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLenLSKLTGVCPQSNVQFDFL 512
Cdd:TIGR01188 4 GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRK--VRRSIGIVPQYASVDEDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 513 TVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRH 592
Cdd:TIGR01188 82 TGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 593 QVWNLLKERKTDRV-ILFSTQFMDEADILADRKVFLSQGKLKCAGSSLFLKKKWGiGYHLSLQLNEICVEENITSLVKQH 671
Cdd:TIGR01188 162 AIWDYIRALKEEGVtILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLG-KDTLESRPRDIQSLKVEVSMLIAE 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1771853535 672 IPDAKLSAK-----SEGKLIYTLPLERTnkFPELYKDLDSYpdlGIENYGVSMT--TLNEVFLKLEG 731
Cdd:TIGR01188 241 LGETGLGLLavtvdSDRIKILVPDGDET--VPEIVEAAIRN---GIRIRSISTErpSLDDVFLKLTG 302
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
420-631 |
2.98e-45 |
|
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: 162.64 E-value: 2.98e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 420 RIRNVTKEYKGKpdKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMaDLENLSKLT 499
Cdd:cd03225 1 ELKNLSFSYPDG--ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKL-SLKELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 500 GVCPQ-SNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFL 578
Cdd:cd03225 78 GLVFQnPDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1771853535 579 LDEPTAGLDPFSRHQVWNLLKERKTDRV-ILFSTQFMDEADILADRKVFLSQGK 631
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAEGKtIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1237-1436 |
3.04e-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: 162.75 E-value: 3.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1237 SKR-KNKIATRNVSFCVRKGeVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG---SGGGDAL-EFLGYCPQENALWP 1311
Cdd:cd03264 7 TKRyGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqdvLKQPQKLrRRIGYLPQEFGVYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1312 NLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEg 1391
Cdd:cd03264 86 NFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPE- 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1771853535 1392 qqqmwQAIRatFRN------TERGALLTTHYMAEAEAVCDRVAIMVSGRLR 1436
Cdd:cd03264 165 -----ERIR--FRNllselgEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1218-1497 |
4.68e-45 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 166.03 E-value: 4.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1218 VIIASCLRKEY---------AGKRKGCFSKRKNKI-ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVl 1287
Cdd:COG4586 1 IIEVENLSKTYrvyekepglKGALKGLFRREYREVeAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1288 lkgsgggdalEFLGYCP----------------QENALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLK 1351
Cdd:COG4586 80 ----------RVLGYVPfkrrkefarrigvvfgQRSQLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1352 SPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRAtfRNTERGA--LLTTHYMAEAEAVCDRVAI 1429
Cdd:COG4586 150 TPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKE--YNRERGTtiLLTSHDMDDIEALCDRVIV 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1771853535 1430 MVSGRLRCIGSIQHLKSKFGKDYLLEMKVKNLAQVEPL--HAEILRLFPQAAR-----QERYSSLMVY---KLPVEDV 1497
Cdd:COG4586 228 IDHGRIIYDGSLEELKERFGPYKTIVLELAEPVPPLELprGGEVIEREGNRVRlevdpRESLAEVLARllaRYPVRDL 305
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
419-632 |
4.96e-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: 162.00 E-value: 4.96e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIynnKLSEMADLENLSKL 498
Cdd:cd03268 1 LKTNDLTKTYGKKR----VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITF---DGKSYQKNIEALRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 TGVCPQSNVQFDFLTVRENLRLFAKIKGILpqevDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFL 578
Cdd:cd03268 74 IGALIEAPGFYPNLTARENLRLLARLLGIR----KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1771853535 579 LDEPTAGLDPFSRHQVWNLL-KERKTDRVILFSTQFMDEADILADRKVFLSQGKL 632
Cdd:cd03268 150 LDEPTNGLDPDGIKELRELIlSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1235-1436 |
8.77e-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: 161.23 E-value: 8.77e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1235 CFSKR-KNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGD---ALEFLGYCPQENALW 1310
Cdd:cd03268 5 DLTKTyGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKnieALRRIGALIEAPGFY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1311 PNLTVRQHLEVYAAVKGLRKGDAEvaitRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1390
Cdd:cd03268 85 PNLTARENLRLLARLLGIRKKRID----EVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1771853535 1391 GQQQMWQAIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLR 1436
Cdd:cd03268 161 GIKELRELILS-LRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
419-642 |
1.48e-43 |
|
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: 158.30 E-value: 1.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYkgkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIynNKLSEMADLENLSKL 498
Cdd:cd03265 1 IEVENLVKKY----GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATV--AGHDVVREPREVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 TGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFL 578
Cdd:cd03265 75 IGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1771853535 579 LDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGSSLFLK 642
Cdd:cd03265 155 LDEPTIGLDPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
416-632 |
5.70e-42 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 154.05 E-value: 5.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 416 KEAIRIRNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADlENL 495
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSE-REL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 496 SKL----TGVCPQS-NVqFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQK------Rkl 564
Cdd:COG1136 81 ARLrrrhIGFVFQFfNL-LPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQqrvaiaR-- 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 565 tfgiAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADIlADRKVFLSQGKL 632
Cdd:COG1136 158 ----ALVNRPKLILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTHDPELAAR-ADRVIRLRDGRI 222
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
419-628 |
9.57e-42 |
|
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: 153.01 E-value: 9.57e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEmadlenLSKL 498
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG------PGPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 TGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFL 578
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1771853535 579 LDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLS 628
Cdd:cd03293 155 LDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDEAVFLADRVVVLS 206
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
419-632 |
1.18e-41 |
|
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: 153.43 E-value: 1.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEM--ADLENLS 496
Cdd:cd03261 1 IELRGLTKSFGGRT----VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLseAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 497 KLTGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIqrVLLELEM---KNIQDVLAQNLSGGQKRKLTFGIAILGD 573
Cdd:cd03261 77 RRMGMLFQSGALFDSLTVFENVAFPLREHTRLSEEEIREI--VLEKLEAvglRGAEDLYPAELSGGMKKRVALARALALD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1771853535 574 PQIFLLDEPTAGLDPFSRHQVWNL---LKERKTDRVILFSTQfMDEADILADRKVFLSQGKL 632
Cdd:cd03261 155 PELLLYDEPTAGLDPIASGVIDDLirsLKKELGLTSIMVTHD-LDTAFAIADRIAVLYDGKI 215
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
419-636 |
8.85e-41 |
|
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: 150.21 E-value: 8.85e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEmADLENLSKL 498
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 tGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFL 578
Cdd:cd03266 81 -GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1771853535 579 LDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAG 636
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRQlRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1242-1534 |
1.33e-40 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 152.65 E-value: 1.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1242 KIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDALEFLGYCPQENALWPNLTVRQ 1317
Cdd:PRK13537 20 KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGepvpSRARHARQRVGVVPQFDNLDPDFTVRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1318 HLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQ 1397
Cdd:PRK13537 100 NLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1398 AIRATFrntERGA--LLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL-KSKFGKDyLLEMKVKNLAQVEPLhaeilrL 1474
Cdd:PRK13537 180 RLRSLL---ARGKtiLLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALiESEIGCD-VIEIYGPDPVALRDE------L 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1771853535 1475 FPQAARQE-RYSSLMVYklpVEDVQPLAQAffklekVKQSFDLeEYSLSQSTLEQVFLELS 1534
Cdd:PRK13537 250 APLAERTEiSGETLFCY---VRDPEPLHAR------LKGRAGL-RYLHRPANLEDVFLRLT 300
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
418-630 |
2.46e-40 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 150.24 E-value: 2.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 418 AIRIRNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEmadlenLSK 497
Cdd:COG1116 7 ALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG------PGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 498 LTGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLtfGIA--ILGDPQ 575
Cdd:COG1116 81 DRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRV--AIAraLANDPE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 576 IFLLDEPTAGLDPFSRHQVWNLL-----KERKTdrvILFSTQFMDEADILADRKVFLSQG 630
Cdd:COG1116 159 VLLMDEPFGALDALTRERLQDELlrlwqETGKT---VLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
419-631 |
1.00e-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: 146.86 E-value: 1.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTiYNNKLSEMADLENLSKL 498
Cdd:COG4133 3 LEAENLSCRRGERL----LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVL-WNGEPIRDAREDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 TGVCPQSNVqFDFLTVRENLRLFAKIKGILPQEVDkeIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFL 578
Cdd:COG4133 78 AYLGHADGL-KPELTVRENLRFWAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1771853535 579 LDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQfmDEADILADRKVFLSQGK 631
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAhLARGGAVLLTTH--QPLELAAARVLDLGDFK 206
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1238-1439 |
1.30e-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: 1.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1238 KRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDALEFLGYCPQENALWPNL 1313
Cdd:cd03266 14 VKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvKEPAEARRRLGFVSDSTGLYDRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1314 TVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQ 1393
Cdd:cd03266 94 TARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATR 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1771853535 1394 QMWQAIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1439
Cdd:cd03266 174 ALREFIRQ-LRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1246-1415 |
2.79e-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: 2.79e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1246 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDALEF----LGYCPQENALWPNLTVRQHLEV 1321
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDyrrrLAYLGHADGLKPELTVRENLRF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1322 YAAVKGLRKGDAevAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRA 1401
Cdd:COG4133 99 WAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAA 176
|
170
....*....|....
gi 1771853535 1402 tFRNTERGALLTTH 1415
Cdd:COG4133 177 -HLARGGAVLLTTH 189
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
438-584 |
2.92e-39 |
|
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: 143.17 E-value: 2.92e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 438 LKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIyNNKLSEMADLENLSKLTGVCPQSNVQFDFLTVREN 517
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILL-DGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1771853535 518 LRLFAKIKGILPQEVDKEIQRVLLELEM----KNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTA 584
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARAEEALEKLGLgdlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1247-1540 |
1.16e-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: 1.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1247 NVSFcvRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDALEF----LGYCPQENALWPNLTVRQHLEVY 1322
Cdd:TIGR01257 950 NITF--YENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAvrqsLGMCPQHNILFHHLTVAEHILFY 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1323 AAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIrAT 1402
Cdd:TIGR01257 1028 AQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL-LK 1106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1403 FRnTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFGKDYLLEM--KVKNL------------------- 1461
Cdd:TIGR01257 1107 YR-SGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLvrKMKNIqsqrggcegtcsctskgfs 1185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1462 ----AQVEPLHAE-------------ILRLFPQAARQERYSSLMVYKLPVEDVQPLAQA--FFKLEKVKQSFDLEEYSLS 1522
Cdd:TIGR01257 1186 trcpARVDEITPEqvldgdvnelmdlVYHHVPEAKLVECIGQELIFLLPNKNFKQRAYAslFRELEETLADLGLSSFGIS 1265
|
330
....*....|....*...
gi 1771853535 1523 QSTLEQVFLELSKEQELG 1540
Cdd:TIGR01257 1266 DTPLEEIFLKVTEDADSG 1283
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
419-631 |
2.66e-38 |
|
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: 141.37 E-value: 2.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKPDKIeaLKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMaDLENLSKL 498
Cdd:cd03228 1 IEFKNVSFSYPGRPKPV--LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDL-DLESLRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 TGVCPQSNVQFDFlTVRENLrlfakikgilpqevdkeiqrvllelemkniqdvlaqnLSGGQKRKLTFGIAILGDPQIFL 578
Cdd:cd03228 78 IAYVPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1771853535 579 LDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEADiLADRKVFLSQGK 631
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
419-670 |
2.67e-38 |
|
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: 144.88 E-value: 2.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLSKL 498
Cdd:TIGR04520 1 IEVENVSFSYPE--SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWEIRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 TGVCPQS--NvQFDFLTVR-------ENLrlfakikGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKltfgIA 569
Cdd:TIGR04520 79 VGMVFQNpdN-QFVGATVEddvafglENL-------GVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQR----VA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 570 ILG----DPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEAdILADRKVFLSQGKLKCAGS--SLFL 641
Cdd:TIGR04520 147 IAGvlamRPDIIILDEATSMLDPKGRKEVLETIRKlnKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTprEIFS 225
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1771853535 642 K----KKWGIG----YHLSLQLNE--ICVEENITS---LVKQ 670
Cdd:TIGR04520 226 QvellKEIGLDvpfiTELAKALKKrgIPLPPDILTeeeLVDE 267
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
419-632 |
5.84e-38 |
|
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: 142.32 E-value: 5.84e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYkgkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGL-----SVPTKGSVTIYN-NKLSEMADL 492
Cdd:cd03260 1 IELRDLNVYY----GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGkDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 493 ENLSKLTGVCPQSNVQFDfLTVRENLRLFAKIKGILPQEVDKEIQRVLLEL-----EMKNIQDVLAqnLSGGQKRKLTFG 567
Cdd:cd03260 77 LELRRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEEALRKaalwdEVKDRLHALG--LSGGQQQRLCLA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1771853535 568 IAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEADILADRKVFLSQGKL 632
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
418-631 |
6.08e-38 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 146.13 E-value: 6.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 418 AIRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENlsK 497
Cdd:PRK13536 41 AIDLAGVSKSYGDKA----VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLAR--A 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 498 LTGVCPQ-SNVQFDFlTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQI 576
Cdd:PRK13536 115 RIGVVPQfDNLDLEF-TVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1771853535 577 FLLDEPTAGLDPFSRHQVW----NLLKERKTdrvILFSTQFMDEADILADRKVFLSQGK 631
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIWerlrSLLARGKT---ILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
392-651 |
8.75e-38 |
|
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: 151.07 E-value: 8.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 392 LEDEMDADPSfhDSFEQAPPEFQGKEAIRIRNVTKEYKGKPDkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGL 471
Cdd:COG4987 309 LNELLDAPPA--VTEPAEPAPAPGGPSLELEDVSFRYPGAGR--PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRF 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 472 SVPTKGSVTIYNNKLSEMaDLENLSKLTGVCPQSNVQFDfLTVRENLRLfAKikgilPQEVDKEIQRVLlelEMKNIQDV 551
Cdd:COG4987 385 LDPQSGSITLGGVDLRDL-DEDDLRRRIAVVPQRPHLFD-TTLRENLRL-AR-----PDATDEELWAAL---ERVGLGDW 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 552 LAQ--------------NLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEA 617
Cdd:COG4987 454 LAAlpdgldtwlgeggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGL 533
|
250 260 270
....*....|....*....|....*....|....
gi 1771853535 618 DiLADRKVFLSQGKLKCAGSSLFLKKKWGIGYHL 651
Cdd:COG4987 534 E-RMDRILVLEDGRIVEQGTHEELLAQNGRYRQL 566
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
420-631 |
9.24e-38 |
|
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: 139.30 E-value: 9.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 420 RIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMaDLENLSKLT 499
Cdd:cd00267 1 EIENLSFRYGGRT----ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKL-PLEELRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 500 GVCPQsnvqfdfltvrenlrlfakikgilpqevdkeiqrvllelemkniqdvlaqnLSGGQKRKLTFGIAILGDPQIFLL 579
Cdd:cd00267 76 GYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1771853535 580 DEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGK 631
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
418-637 |
2.08e-37 |
|
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: 141.72 E-value: 2.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 418 AIRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLEnLSK 497
Cdd:COG1120 1 MLEAENLSVGYGGRP----VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRE-LAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 498 LTGVCPQSNVQFDFLTVRE--------NLRLFAKikgilPQEVDKEI-QRVLLELEMKNIQDVLAQNLSGGQKRKLTFGI 568
Cdd:COG1120 76 RIAYVPQEPPAPFGLTVRElvalgrypHLGLFGR-----PSAEDREAvEEALERTGLEHLADRPVDELSGGERQRVLIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1771853535 569 AILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS 637
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
168-734 |
3.36e-37 |
|
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: 154.02 E-value: 3.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 168 CII---SF--SSFIYYasvnVTRER-KRMKALMTMMGLRDSAFWLS---WGLLyaGFIFIMALFLALVI--RSTQFIILS 236
Cdd:TIGR01257 1685 CVIfamSFvpASFVLY----LIQERvNKAKHLQFISGVSPTTYWLTnflWDIM--NYAVSAGLVVGIFIgfQKKAYTSPE 1758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 237 GFMVVFSLFLLYGLSLVALAFLMSILVK-----------KSFLTGL----VVFLLTVFWG---CLGFTSLYRHLpaslew 298
Cdd:TIGR01257 1759 NLPALVALLMLYGWAVIPMMYPASFLFDvpstayvalscANLFIGInssaITFVLELFENnrtLLRFNAMLRKL------ 1832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 299 iLSLLSPFAFMLGMAQLL----------HLDYDLNSNAFPHPSDGSNLivatnFMLAFDTCLYLALAIYFEKilpneygh 368
Cdd:TIGR01257 1833 -LIVFPHFCLGRGLIDLAlsqavtdvyaQFGEEHSANPFQWDLIGKNL-----VAMAVEGVVYFLLTLLIQH-------- 1898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 369 rrppLFFLkssfwsqTQKTDHVALEDEMDADPSFHDSFEQAPPEFQGKEAIRIRNVTKEYKGKPDKieALKDLVFDIYEG 448
Cdd:TIGR01257 1899 ----HFFL-------SRWIAEPAKEPIFDEDDDVAEERQRIISGGNKTDILRLNELTKVYSGTSSP--AVDRLCVGVRPG 1965
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 449 QITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLseMADLENLSKLTGVCPQSNVQFDFLTVRENLRLFAKIKGIL 528
Cdd:TIGR01257 1966 ECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI--LTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVP 2043
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 529 PQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWN-LLKERKTDRVI 607
Cdd:TIGR01257 2044 AEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNtIVSIIREGRAV 2123
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 608 LFSTQFMDEADILADRKVFLSQGKLKCAGSSLFLKKKWGIGYHLSLQL----NEICVEEN-ITSLVKQHIPDAKLSAKSE 682
Cdd:TIGR01257 2124 VLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMKIkspkDDLLPDLNpVEQFFQGNFPGSVQRERHY 2203
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 1771853535 683 GKLIYTLPlerTNKFPELYKDLDSYPD-LGIENYGVSMTTLNEVFLKLEGKST 734
Cdd:TIGR01257 2204 NMLQFQVS---SSSLARIFQLLISHKDsLLIEEYSVTQTTLDQVFVNFAKQQT 2253
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
419-632 |
7.18e-37 |
|
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: 139.64 E-value: 7.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEM--ADLENLS 496
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLsgKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 497 KLTGVCPQsnvQFDFL---TVRENLRLFAKIKGILPQEVDKEIQRvLLEL-EMKNIQDVLAQNLSGGQKRKLTFGIAILG 572
Cdd:cd03258 82 RRIGMIFQ---HFNLLssrTVFENVALPLEIAGVPKAEIEERVLE-LLELvGLEDKADAYPAQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1771853535 573 DPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKL 632
Cdd:cd03258 158 NPKVLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1241-1434 |
1.04e-36 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 142.66 E-value: 1.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1241 NKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDALEFLGYCPQENALWPNLTVR 1316
Cdd:PRK13536 53 DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGvpvpARARLARARIGVVPQFDNLDLEFTVR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1317 QHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMW 1396
Cdd:PRK13536 133 ENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIW 212
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1771853535 1397 QAIRATFrntERGA--LLTTHYMAEAEAVCDRVAIMVSGR 1434
Cdd:PRK13536 213 ERLRSLL---ARGKtiLLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
418-637 |
1.17e-36 |
|
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: 138.96 E-value: 1.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 418 AIRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEM--ADLENL 495
Cdd:COG1127 5 MIEVRNLTKSFGDRV----VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLseKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 496 SKLTGVCPQSNVQFDFLTVRENLRLFAKIKGILPqevDKEI-QRVLLELEMKNIQDVLAQN---LSGGQKRKLtfGIA-- 569
Cdd:COG1127 81 RRRIGMLFQGGALFDSLTVFENVAFPLREHTDLS---EAEIrELVLEKLELVGLPGAADKMpseLSGGMRKRV--ALAra 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1771853535 570 ILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDR---VILFSTQfMDEADILADRKVFLSQGKLKCAGS 637
Cdd:COG1127 156 LALDPEILLYDEPTAGLDPITSAVIDELIRELRDELgltSVVVTHD-LDSAFAIADRVAVLADGKIIAEGT 225
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
422-632 |
1.40e-36 |
|
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: 137.30 E-value: 1.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 422 RNVTKEYKGKPDKIEA--LKDLVFDIYEGQITAILGHSGAGKSTLLNILSGL--SVPTKGSVTIyNNKlseMADLENLSK 497
Cdd:cd03213 7 RNLTVTVKSSPSKSGKqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLI-NGR---PLDKRSFRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 498 LTGVCPQSNVQFDFLTVRENLRLFAKIKGIlpqevdkeiqrvllelemkniqdvlaqnlSGGQKRKLTFGIAILGDPQIF 577
Cdd:cd03213 83 IIGYVPQDDILHPTLTVRETLMFAAKLRGL-----------------------------SGGERKRVSIALELVSNPSLL 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1771853535 578 LLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFST-QFMDEADILADRKVFLSQGKL 632
Cdd:cd03213 134 FLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIhQPSSEIFELFDKLLLLSQGRV 190
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
408-637 |
1.46e-36 |
|
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: 147.21 E-value: 1.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 408 QAPPEFQGKEAIRIRNVTKEYkgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLS 487
Cdd:COG4988 326 TAPLPAAGPPSIELEDVSFSY---PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLS 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 488 EMaDLENLSKLTGVCPQSNVQFDfLTVRENLRLFAkikgilPQEVDKEIQRVlleLEMKNIQDVLAQ------------- 554
Cdd:COG4988 403 DL-DPASWRRQIAWVPQNPYLFA-GTIRENLRLGR------PDASDEELEAA---LEAAGLDEFVAAlpdgldtplgegg 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 555 -NLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQfmDEADI-LADRKVFLSQGKL 632
Cdd:COG4988 472 rGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITH--RLALLaQADRILVLDDGRI 549
|
....*
gi 1771853535 633 KCAGS 637
Cdd:COG4988 550 VEQGT 554
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1219-1435 |
1.59e-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: 1.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1219 IIASCLRKEYAGKRKGCF----------SKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVll 1288
Cdd:cd03267 1 IEVSNLSKSYRVYSKEPGligslkslfkRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1289 kgsgggdalEFLGYCP----------------QENALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKS 1352
Cdd:cd03267 79 ---------RVAGLVPwkrrkkflrrigvvfgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1353 PVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVS 1432
Cdd:cd03267 150 PVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDK 229
|
...
gi 1771853535 1433 GRL 1435
Cdd:cd03267 230 GRL 232
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
419-631 |
4.84e-36 |
|
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: 136.80 E-value: 4.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYkgkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLSKL 498
Cdd:cd03224 1 LEVENLNAGY----GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 TGVCPQSNVQFDFLTVRENLRLFAKIKGilPQEVDKEIQRVlLEL--EMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQI 576
Cdd:cd03224 77 IGYVPEGRRIFPELTVEENLLLGAYARR--RAKRKARLERV-YELfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1771853535 577 FLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGK 631
Cdd:cd03224 154 LLLDEPSEGLAPKIVEEIFEAIRElRDEGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
418-670 |
3.82e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 135.89 E-value: 3.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 418 AIRIRNVTKEYKgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEmADLENLSK 497
Cdd:PRK13632 7 MIKVENVSFSYP--NSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISK-ENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 498 LTGVCPQS-NVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQI 576
Cdd:PRK13632 84 KIGIIFQNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 577 FLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEAdILADRKVFLSQGKLKCAGS-SLFLKKKWGIG----- 648
Cdd:PRK13632 164 IIFDESTSMLDPKGKREIKKIMVDlrKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKpKEILNNKEILEkakid 242
|
250 260
....*....|....*....|....*.
gi 1771853535 649 ----YHLSLQLNEICVEENITSLVKQ 670
Cdd:PRK13632 243 spfiYKLSKKLKGIDPTYNEEELIEQ 268
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
388-651 |
4.41e-35 |
|
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: 144.59 E-value: 4.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 388 DHVALEDEMDADPSFhdsfeQAPPEFQGkeAIRIRNVTKEYKgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNI 467
Cdd:COG2274 450 DILDLPPEREEGRSK-----LSLPRLKG--DIELENVSFRYP--GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKL 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 468 LSGLSVPTKGSVTIYNNKLSEMaDLENLSKLTGVCPQSNVQFdFLTVRENLRLFAkikgilPQEVDKEIQRVlleLEMKN 547
Cdd:COG2274 521 LLGLYEPTSGRILIDGIDLRQI-DPASLRRQIGVVLQDVFLF-SGTIRENITLGD------PDATDEEIIEA---ARLAG 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 548 IQDVLAQ--------------NLSGGQKRKLtfGIA--ILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFST 611
Cdd:COG2274 590 LHDFIEAlpmgydtvvgeggsNLSGGQRQRL--AIAraLLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIA 667
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1771853535 612 QfmDEADI-LADRKVFLSQGKLKCAGSSLFLKKKWGIGYHL 651
Cdd:COG2274 668 H--RLSTIrLADRIIVLDKGRIVEDGTHEELLARKGLYAEL 706
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
419-636 |
8.05e-35 |
|
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: 132.79 E-value: 8.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMAdlenlSKL 498
Cdd:cd03269 1 LEVENVTKRFGRV----TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA-----RNR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 TGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFL 578
Cdd:cd03269 72 IGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1771853535 579 LDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAG 636
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRElARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
418-631 |
1.09e-34 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 135.70 E-value: 1.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 418 AIRIRNVTKEYKgkpDKIeALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLSk 497
Cdd:PRK13537 7 PIDFRNVEKRYG---DKL-VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 498 lTGVCPQ-SNVQFDFlTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQI 576
Cdd:PRK13537 82 -VGVVPQfDNLDPDF-TVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1771853535 577 FLLDEPTAGLDPFSRHQVW----NLLKERKTdrvILFSTQFMDEADILADRKVFLSQGK 631
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWerlrSLLARGKT---ILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
419-653 |
1.72e-34 |
|
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: 134.12 E-value: 1.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEY-KGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTI--YNNKLSEMADLENL 495
Cdd:TIGR04521 1 IKLKNVSYIYqPGTPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIdgRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 496 SKLTGVcpqsnVqFDF-------LTVRE-------NLrlfakikGILPQEVDkeiQRVLLELEMKNI-QDVLAQN---LS 557
Cdd:TIGR04521 81 RKKVGL-----V-FQFpehqlfeETVYKdiafgpkNL-------GLSEEEAE---ERVKEALELVGLdEEYLERSpfeLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 558 GGQKRKltfgIAILG----DPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGK 631
Cdd:TIGR04521 145 GGQMRR----VAIAGvlamEPEVLILDEPTAGLDPKGRKEILDLFKRlhKEKGLTVILVTHSMEDVAEYADRVIVMHKGK 220
|
250 260
....*....|....*....|....
gi 1771853535 632 LKCAGSS--LFLKKKWGIGYHLSL 653
Cdd:TIGR04521 221 IVLDGTPreVFSDVDELEKIGLDV 244
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1246-1385 |
2.39e-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: 129.30 E-value: 2.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1246 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-SGGGDALEFL----GYCPQENALWPNLTVRQHLE 1320
Cdd:pfam00005 2 KNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGqDLTDDERKSLrkeiGYVFQDPQLFPRLTVRENLR 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1771853535 1321 VYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPV----KTLSEGIKRKLCFVLSILGNPSVVLLDEPST 1385
Cdd:pfam00005 82 LGLLLKGLSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
419-632 |
3.30e-34 |
|
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: 131.10 E-value: 3.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIynnklsemaDLENLSKL 498
Cdd:cd03259 1 LELKGLSKTYGSVR----ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILI---------DGRDVTGV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 ------TGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILG 572
Cdd:cd03259 68 pperrnIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1771853535 573 DPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKL 632
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 ... |
1244-1434 |
3.80e-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: 3.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1244 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-------------SGggdalefLGYCPQENALW 1310
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGrditglppherarAG-------IGYVPEGRRIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1311 PNLTVRQHLEVYAAVKGLRKGDAEVAitRLVDAL-KLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDP 1389
Cdd:cd03224 88 PELTVEENLLLGAYARRRAKRKARLE--RVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1771853535 1390 EGQQQMWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1434
Cdd:cd03224 166 KIVEEIFEAIR-ELRDEGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
419-632 |
1.06e-33 |
|
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: 130.53 E-value: 1.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEY-----------------KGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTI 481
Cdd:cd03267 1 IEVSNLSKSYrvyskepgligslkslfKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 482 YNNKLSEMADlENLSKLTGVCPQSN-VQFDfLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQ 560
Cdd:cd03267 81 AGLVPWKRRK-KFLRRIGVVFGQKTqLWWD-LPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1771853535 561 KRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKL 632
Cdd:cd03267 159 RMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEynRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
419-631 |
1.91e-33 |
|
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: 127.69 E-value: 1.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMAD-LENLSK 497
Cdd:cd03229 1 LELKNVSKRYGQKT----VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDeLPPLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 498 LTGVCPQSNVQFDFLTVRENLRLfakikgilpqevdkeiqrvllelemkniqdvlaqNLSGGQKRKLTFGIAILGDPQIF 577
Cdd:cd03229 77 RIGMVFQDFALFPHLTVLENIAL----------------------------------GLSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1771853535 578 LLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGK 631
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSlqAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
419-637 |
1.93e-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: 129.86 E-value: 1.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGkpdkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVtIYNNKlsemadlenlsKL 498
Cdd:cd03219 1 LEVRGLTKRFGG----LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSV-LFDGE-----------DI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 TGVCP------------QsNVQ-FDFLTVRENLRL---FAKIKGILP-------QEVDKEIQRVLLELEMKNIQDVLAQN 555
Cdd:cd03219 65 TGLPPheiarlgigrtfQ-IPRlFPELTVLENVMVaaqARTGSGLLLararreeREARERAEELLERVGLADLADRPAGE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 556 LSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILfstqfMDEADI-----LADRKVFLSQ 629
Cdd:cd03219 144 LSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRElRERGITVL-----LVEHDMdvvmsLADRVTVLDQ 218
|
....*...
gi 1771853535 630 GKLKCAGS 637
Cdd:cd03219 219 GRVIAEGT 226
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1244-1435 |
3.37e-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: 3.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1244 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-----------SGGGDALEFlgycpQENALWPN 1312
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGeditglppheiARLGIGRTF-----QIPRLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1313 LTVRQHLEV--------YAAVKGLRKGDAEV--AITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDE 1382
Cdd:cd03219 90 LTVLENVMVaaqartgsGLLLARARREEREAreRAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1771853535 1383 PSTGMDPEGQQQMWQAIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1435
Cdd:cd03219 170 PAAGLNPEETEELAELIRE-LRERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
418-637 |
5.60e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 130.23 E-value: 5.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 418 AIRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIyNNKLSEMADLENLSK 497
Cdd:COG4152 1 MLELKGLTKRFGDKT----AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLW-DGEPLDPEDRRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 498 L---TGVCPQsnvqfdfLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDP 574
Cdd:COG4152 76 LpeeRGLYPK-------MKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1771853535 575 QIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS 637
Cdd:COG4152 149 ELLILDEPFSGLDPVNVELLKDVIRElAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGS 212
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
394-638 |
7.38e-33 |
|
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: 135.03 E-value: 7.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 394 DEMDADPSFHDSFEQAPPEFQGKE-AIRIRNVTKEYKGK-PDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGL 471
Cdd:COG1123 235 QALAAVPRLGAARGRAAPAAAAAEpLLEVRNLSKRYPVRgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 472 SVPTKGSVTIYNNKLSEM--ADLENLSKLTGVCPQS-NVQFD-FLTVRENLRLFAKIKGILP-QEVDKEIQRVL----LE 542
Cdd:COG1123 315 LRPTSGSILFDGKDLTKLsrRSLRELRRRVQMVFQDpYSSLNpRMTVGDIIAEPLRLHGLLSrAERRERVAELLervgLP 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 543 LEMKniqDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADIL 620
Cdd:COG1123 395 PDLA---DRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDlqRELGLTYLFISHDLAVVRYI 471
|
250
....*....|....*...
gi 1771853535 621 ADRKVFLSQGKLKCAGSS 638
Cdd:COG1123 472 ADRVAVMYDGRIVEDGPT 489
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
418-632 |
7.57e-33 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 128.25 E-value: 7.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 418 AIRIRNVTKEYkgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEM--ADLENL 495
Cdd:COG3638 2 MLELRNLSKRY---PGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALrgRALRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 496 SKLTGVCPQsnvQFDF---LTVREN--------LRLFAKIKGILPQEvdkEIQRVLLELEMKNIQDVLAQ---NLSGGQK 561
Cdd:COG3638 79 RRRIGMIFQ---QFNLvprLSVLTNvlagrlgrTSTWRSLLGLFPPE---DRERALEALERVGLADKAYQradQLSGGQQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1771853535 562 RKLtfGIA--ILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKL 632
Cdd:COG3638 153 QRV--AIAraLVQEPKLILADEPVASLDPKTARQVMDLLRRiaREDGITVVVNLHQVDLARRYADRIIGLRDGRV 225
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
419-632 |
9.90e-33 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 126.85 E-value: 9.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKPDkieaLKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMaDLENLSKL 498
Cdd:COG4619 1 LELEGLSFRVGGKPI----LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAM-PPPEWRRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 TGVCPQSNVQFDfLTVRENLRLFAKIKGilpQEVDKEIQRVLLE-LEMKniQDVL---AQNLSGGQKRKLTFGIAILGDP 574
Cdd:COG4619 76 VAYVPQEPALWG-GTVRDNLPFPFQLRE---RKFDRERALELLErLGLP--PDILdkpVERLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 575 QIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKL 632
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
419-632 |
2.08e-32 |
|
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: 126.47 E-value: 2.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMadLENLSKL 498
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKL--SRRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 TGvcpqSNVQFDF----------LTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVL---AQNLSGGQKRKLT 565
Cdd:cd03257 80 RR----KEIQMVFqdpmsslnprMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLnryPHELSGGQRQRVA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1771853535 566 FGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKL 632
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKKlqEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1238-1434 |
2.52e-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: 125.66 E-value: 2.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1238 KRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-----SGGGDALEFLGYCPQEnalwP- 1311
Cdd:cd03225 10 PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGkdltkLSLKELRRKVGLVFQN----Pd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1312 ----NLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCfVLSIL-GNPSVVLLDEPSTG 1386
Cdd:cd03225 86 dqffGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVA-IAGVLaMDPDILLLDEPTAG 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1771853535 1387 MDPEGQQQMWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1434
Cdd:cd03225 165 LDPAGRRELLELLK-KLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
418-637 |
3.44e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 126.36 E-value: 3.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 418 AIRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNnklsemADLENLSK 497
Cdd:COG1121 6 AIELENLTVSYGGRP----VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG------KPPRRARR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 498 LTGVCPQ-SNVQFDF-LTVRE--------NLRLFakikGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFG 567
Cdd:COG1121 76 RIGYVPQrAEVDWDFpITVRDvvlmgrygRRGLF----RRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1771853535 568 IAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKLkCAGS 637
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREYFDRVLLLNRGLV-AHGP 221
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
420-636 |
3.60e-32 |
|
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: 124.08 E-value: 3.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 420 RIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMadlenlsklt 499
Cdd:cd03214 1 EVENLSVGYGGRT----VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASL---------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 500 gvcpqsnvqfdfltvreNLRLFAKIKGILPQevdkEIQRV-LLELEMKNIQDvlaqnLSGGQKRKLTFGIAILGDPQIFL 578
Cdd:cd03214 67 -----------------SPKELARKIAYVPQ----ALELLgLAHLADRPFNE-----LSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 579 LDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAG 636
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRlaRERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
419-632 |
3.82e-32 |
|
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: 125.06 E-value: 3.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNklsEMADLENLSKL 498
Cdd:cd03301 1 VELENVTKRFGNVT----ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGR---DVTDLPPKDRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 TGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFL 578
Cdd:cd03301 74 IAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1771853535 579 LDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKL 632
Cdd:cd03301 154 MDEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
418-632 |
5.21e-32 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 129.04 E-value: 5.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 418 AIRIRNVTKEYkgkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIyNNKLseMADLEnlsk 497
Cdd:COG3839 3 SLELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILI-GGRD--VTDLP---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 498 ltgvcP---------QSNVQFDFLTVRENLrLFA-KIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFG 567
Cdd:COG3839 72 -----PkdrniamvfQSYALYPHMTVYENI-AFPlKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALG 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1771853535 568 IAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKL 632
Cdd:COG3839 146 RALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRlhRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRI 212
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
419-600 |
6.61e-32 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 124.78 E-value: 6.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYkgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEM--ADLENLS 496
Cdd:COG2884 2 IRFENVSKRY---PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrREIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 497 KLTGVCPQsnvqfDF-----LTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLtfGI--A 569
Cdd:COG2884 79 RRIGVVFQ-----DFrllpdRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRV--AIarA 151
|
170 180 190
....*....|....*....|....*....|.
gi 1771853535 570 ILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE 600
Cdd:COG2884 152 LVNRPELLLADEPTGNLDPETSWEIMELLEE 182
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
420-633 |
7.47e-32 |
|
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: 123.91 E-value: 7.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 420 RIRNVTKEYKgkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMAdlenLSKLT 499
Cdd:cd03226 1 RIENISFSYK---KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE----RRKSI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 500 GVCPQ-SNVQFDFLTVRENLRLFAKIKGILPQEVDKeiqrVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFL 578
Cdd:cd03226 74 GYVMQdVDYQLFTDSVREELLLGLKELDAGNEQAET----VLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1771853535 579 LDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKLK 633
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRElAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1236-1439 |
1.03e-31 |
|
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: 123.78 E-value: 1.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1236 FSKR-KNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG---SGGGDALEFLGYCPQENALWP 1311
Cdd:cd03259 6 LSKTyGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGrdvTGVPPERRNIGMVFQDYALFP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1312 NLTVRQHLeVYA-AVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1390
Cdd:cd03259 86 HLTVAENI-AFGlKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1771853535 1391 GQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1439
Cdd:cd03259 165 LREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
418-632 |
1.93e-31 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 124.15 E-value: 1.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 418 AIRIRNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLSK 497
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 498 ltgvcpqsnVQFDF----------LTVRENLRLFAKIKGILpqEVDKEIQRVLLELEMKniQDVL----AQnLSGGQKRK 563
Cdd:COG1124 81 ---------VQMVFqdpyaslhprHTVDRILAEPLRIHGLP--DREERIAELLEQVGLP--PSFLdrypHQ-LSGGQRQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1771853535 564 LTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDR--VILFSTQFMDEADILADRKVFLSQGKL 632
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1244-1435 |
2.36e-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: 2.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1244 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-----------SGGGDALEFlgycpQENALWPN 1312
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGrditglpphriARLGIARTF-----QNPRLFPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1313 LTVRQHLEV----------YAAVKGLRKGDAEVAITR-----LVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSV 1377
Cdd:COG0411 94 LTVLENVLVaaharlgrglLAALLRLPRARREEREAReraeeLLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1378 VLLDEPSTGMDPEGQQQMWQAIRATfrNTERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1435
Cdd:COG0411 174 LLLDEPAAGLNPEETEELAELIRRL--RDERGItiLLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
419-632 |
2.69e-31 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 126.73 E-value: 2.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYN---NKLSEmADLENL 495
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGvdlTALSE-RELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 496 SKLTGVCPQsnvQFDFL---TVRENLRLFAKIKGILPQEVDKeiqRV--LLEL-EMKNIQDVLAQNLSGGQKRKLtfGIA 569
Cdd:COG1135 81 RRKIGMIFQ---HFNLLssrTVAENVALPLEIAGVPKAEIRK---RVaeLLELvGLSDKADAYPSQLSGGQKQRV--GIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1771853535 570 --ILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKL 632
Cdd:COG1135 153 raLANNPKVLLCDEATSALDPETTRSILDLLKDinRELGLTIVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1235-1455 |
3.22e-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: 123.21 E-value: 3.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1235 CFSKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-----SGGGDALEFLGYCPQ--EN 1307
Cdd:COG1122 7 SFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGkditkKNLRELRRKVGLVFQnpDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1308 ALWpNLTVRQhlEV-YAAV-KGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCF--VLSIlgNPSVVLLDEP 1383
Cdd:COG1122 87 QLF-APTVEE--DVaFGPEnLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIagVLAM--EPEVLVLDEP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1771853535 1384 STGMDPEGQQQMWQAIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLkskFGKDYLLE 1455
Cdd:COG1122 162 TAGLDPRGRRELLELLKR-LNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV---FSDYELLE 229
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
420-636 |
4.84e-31 |
|
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: 121.87 E-value: 4.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 420 RIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMadlenlSKLT 499
Cdd:cd03235 1 EVEDLTVSYGGHP----VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE------RKRI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 500 GVCPQS-NVQFDF-LTVRE--NLRLFAKIK--GILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGD 573
Cdd:cd03235 71 GYVPQRrSIDRDFpISVRDvvLMGLYGHKGlfRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1771853535 574 PQIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRkVFLSQGKLKCAG 636
Cdd:cd03235 151 PDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYFDR-VLLLNRTVVASG 213
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
419-632 |
6.60e-31 |
|
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: 121.87 E-value: 6.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEY------------------KGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVT 480
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 481 IyNNKLSEMADLEnlsklTGVCPQsnvqfdfLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQ 560
Cdd:cd03220 81 V-RGRVSSLLGLG-----GGFNPE-------LTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGM 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1771853535 561 KRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKL 632
Cdd:cd03220 148 KARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRElLKQGKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
418-669 |
7.54e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 124.81 E-value: 7.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 418 AIRIRNVTKEYK------G---------KPDK--IEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVT 480
Cdd:COG4586 1 IIEVENLSKTYRvyekepGlkgalkglfRREYreVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 481 I-----YNNKLsemadlENLSKLTGVCPQ-SNVQFDfLTVRENLRLFAKIKGIlPqevDKEIQRVLLEL-EMKNIQDVLA 553
Cdd:COG4586 81 VlgyvpFKRRK------EFARRIGVVFGQrSQLWWD-LPAIDSFRLLKAIYRI-P---DAEYKKRLDELvELLDLGELLD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 554 Q---NLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDeaDI--LADRKVF 626
Cdd:COG4586 150 TpvrQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEynRERGTTILLTSHDMD--DIeaLCDRVIV 227
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1771853535 627 LSQGKLKCAGSSLFLKKKWGIGYHLSLQLNEICVEENITSLVK 669
Cdd:COG4586 228 IDHGRIIYDGSLEELKERFGPYKTIVLELAEPVPPLELPRGGE 270
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
419-632 |
8.78e-31 |
|
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: 122.41 E-value: 8.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKPdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMaDLENLSKL 498
Cdd:cd03295 1 IEFENVTKRYGGGK---KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQ-DPVELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 TGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRV--LLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQI 576
Cdd:cd03295 77 IGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELlaLVGLDPAEFADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1771853535 577 FLLDEPTAGLDPFSRHQVWNLLK--ERKTDRVILFSTQFMDEADILADRKVFLSQGKL 632
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKrlQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEI 214
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
418-637 |
9.12e-31 |
|
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: 128.87 E-value: 9.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 418 AIRIRNVTKEYKGkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPT---KGSVTIYNNKLSEMaDLEN 494
Cdd:COG1123 4 LLEVRDLSVRYPG--GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLEL-SEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 495 LSKLTGVCPQS-NVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGD 573
Cdd:COG1123 81 RGRRIGMVFQDpMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1771853535 574 PQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS 637
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGP 226
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
420-638 |
1.05e-30 |
|
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: 121.63 E-value: 1.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 420 RIRNVTKEYkgkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIynnklsemaDLENLSKLT 499
Cdd:COG0410 5 EVENLHAGY----GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRF---------DGEDITGLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 500 ---------GVCPQS-NVqFDFLTVRENLRLFAKIKGIlPQEVDKEIQRVlLEL-----EMKNiqdVLAQNLSGGQKRKL 564
Cdd:COG0410 72 phriarlgiGYVPEGrRI-FPSLTVEENLLLGAYARRD-RAEVRADLERV-YELfprlkERRR---QRAGTLSGGEQQML 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1771853535 565 TFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGSS 638
Cdd:COG0410 146 AIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRlNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTA 220
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1241-1443 |
1.93e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 121.35 E-value: 1.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1241 NKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDALEFLGYCPQENALWPN--LTVRqh 1318
Cdd:COG1121 18 GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIGYVPQRAEVDWDfpITVR-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1319 lEV-----YAAV---KGLRKGDAEvAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1390
Cdd:COG1121 96 -DVvlmgrYGRRglfRRPSRADRE-AVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1771853535 1391 GQQQMWQAIRAtFRNTERGALLTTHYMAEAEAVCDRVaIMVSGRLRCIGSIQH 1443
Cdd:COG1121 174 TEEALYELLRE-LRREGKTILVVTHDLGAVREYFDRV-LLLNRGLVAHGPPEE 224
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1237-1440 |
2.29e-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: 120.73 E-value: 2.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1237 SKR-KNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsGGGD---------ALEFLGYCPQE 1306
Cdd:cd03218 7 SKRyGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILL---DGQDitklpmhkrARLGIGYLPQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1307 NALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTG 1386
Cdd:cd03218 84 ASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAG 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1771853535 1387 MDPEGQQQMwQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1440
Cdd:cd03218 164 VDPIAVQDI-QKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGT 216
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1238-1434 |
4.43e-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: 117.35 E-value: 4.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1238 KRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGD-----ALEFLGYCPQenalwpn 1312
Cdd:cd00267 8 RYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKlpleeLRRRIGYVPQ------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1313 ltvrqhlevyaavkglrkgdaevaitrlvdalklqdqlkspvktLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQ 1392
Cdd:cd00267 81 --------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASR 116
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1771853535 1393 QQMWQAIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1434
Cdd:cd00267 117 ERLLELLRE-LAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
418-632 |
7.87e-30 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 122.51 E-value: 7.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 418 AIRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIynnklsemaDLENLSK 497
Cdd:COG3842 5 ALELENVSKRYGDVT----ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILL---------DGRDVTG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 498 L------TGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQK------Rklt 565
Cdd:COG3842 72 LppekrnVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQqrvalaR--- 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1771853535 566 fgiAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFST--QfmDEADILADRKVFLSQGKL 632
Cdd:COG3842 149 ---ALAPEPRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVThdQ--EEALALADRIAVMNDGRI 214
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
423-632 |
8.73e-30 |
|
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: 118.91 E-value: 8.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 423 NVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLsVP----TKGSVTIYNNKLSEMADLENLSKL 498
Cdd:cd03234 8 DVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGR-VEgggtTSGQILFNGQPRKPDQFQKCVAYV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 tgvcPQSNVQFDFLTVRENLRLFAKIKG--ILPQEVDKEI--QRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDP 574
Cdd:cd03234 87 ----RQDDILLPGLTVRETLTYTAILRLprKSSDAIRKKRveDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1771853535 575 QIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQfMDEADI--LADRKVFLSQGKL 632
Cdd:cd03234 163 KVLILDEPTSGLDSFTALNLVSTLSQlARRNRIVILTIH-QPRSDLfrLFDRILLLSSGEI 222
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
419-632 |
9.19e-30 |
|
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: 119.33 E-value: 9.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYkgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEM--ADLENLS 496
Cdd:TIGR02315 2 LEVENLSKVY---PNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLrgKKLRKLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 497 KLTGVCPQSNVQFDFLTVRENL---RLFAK--IKGILPQEVDKEIQRVLLELEMKNIQDVLAQ---NLSGGQKRKLTFGI 568
Cdd:TIGR02315 79 RRIGMIFQHYNLIERLTVLENVlhgRLGYKptWRSLLGRFSEEDKERALSALERVGLADKAYQradQLSGGQQQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1771853535 569 AILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKL 632
Cdd:TIGR02315 159 ALAQQPDLILADEPIASLDPKTSKQVMDYLKRinKEDGITVIINLHQVDLAKKYADRIVGLKAGEI 224
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1238-1439 |
1.68e-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: 118.02 E-value: 1.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1238 KRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVllKGSGGGDALEFLGYcpqenALWPNLTVRQ 1317
Cdd:cd03220 31 EVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV--TVRGRVSSLLGLGG-----GFNPELTGRE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1318 HLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEP-STGmDPEGQQQMW 1396
Cdd:cd03220 104 NIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVlAVG-DAAFQEKCQ 182
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1771853535 1397 QAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1439
Cdd:cd03220 183 RRLR-ELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
396-632 |
1.76e-29 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 125.66 E-value: 1.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 396 MDADPSFHDSfEQAPPEFQGKEAIRIRNVTKEYkgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPT 475
Cdd:COG1132 318 LDEPPEIPDP-PGAVPLPPVRGEIEFENVSFSY---PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPT 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 476 KGSVTIYNNKLSEMaDLENLSKLTGVCPQSNVQFDfLTVRENLRLFAkikgilPQEVDKEIQRVlleLEMKNIQDVLAQ- 554
Cdd:COG1132 394 SGRILIDGVDIRDL-TLESLRRQIGVVPQDTFLFS-GTIRENIRYGR------PDATDEEVEEA---AKAAQAHEFIEAl 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 555 -------------NLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDR-VIL----FSTqfmde 616
Cdd:COG1132 463 pdgydtvvgergvNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRtTIViahrLST----- 537
|
250
....*....|....*..
gi 1771853535 617 adIL-ADRKVFLSQGKL 632
Cdd:COG1132 538 --IRnADRILVLDDGRI 552
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1245-1439 |
2.90e-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: 117.01 E-value: 2.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1245 TRNVSFCVrKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDALEFL---------GYCPQENALWPNLTV 1315
Cdd:cd03297 14 TLKIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKInlppqqrkiGLVFQQYALFPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1316 RQHLEVyaAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQM 1395
Cdd:cd03297 93 RENLAF--GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1771853535 1396 WQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1439
Cdd:cd03297 171 LPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
417-637 |
2.91e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 118.34 E-value: 2.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 417 EAIRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLEnLS 496
Cdd:PRK13548 1 AMLEARNLSVRLGGRT----LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAE-LA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 497 KLTGVCPQ-SNVQFDFlTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQK------RKLTFGIA 569
Cdd:PRK13548 76 RRRAVLPQhSSLSFPF-TVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQqrvqlaRVLAQLWE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1771853535 570 ILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDR-----VIL----FSTQFmdeadilADRKVFLSQGKLKCAGS 637
Cdd:PRK13548 155 PDGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERglaviVVLhdlnLAARY-------ADRIVLLHQGRLVADGT 224
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
419-631 |
3.22e-29 |
|
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: 117.67 E-value: 3.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYkgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEM--ADLENLS 496
Cdd:cd03256 1 IEVENLSKTY---PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLkgKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 497 KLTGVCPQSNVQFDFLTVRENL---RLFAK--IKGILPQEVDKEIQRVLLELEMKNIQDVL---AQNLSGGQKRKLtfGI 568
Cdd:cd03256 78 RQIGMIFQQFNLIERLSVLENVlsgRLGRRstWRSLFGLFPKEEKQRALAALERVGLLDKAyqrADQLSGGQQQRV--AI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1771853535 569 A--ILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGK 631
Cdd:cd03256 156 AraLMQQPKLILADEPVASLDPASSRQVMDLLKRinREEGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1246-1434 |
4.81e-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: 117.01 E-value: 4.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1246 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-------------SGggdalefLGYCPQENALWPN 1312
Cdd:COG0410 20 HGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGeditglpphriarLG-------IGYVPEGRRIFPS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1313 LTVRQHLEVYAAVKGLRKGDAEvaitRL--VDAL--KLQDQLKSPVKTLSEG------IKRKLcfvlsiLGNPSVVLLDE 1382
Cdd:COG0410 93 LTVEENLLLGAYARRDRAEVRA----DLerVYELfpRLKERRRQRAGTLSGGeqqmlaIGRAL------MSRPKLLLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1771853535 1383 PSTGMDPEGQQQMWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1434
Cdd:COG0410 163 PSLGLAPLIVEEIFEIIR-RLNREGVTILLVEQNARFALEIADRAYVLERGR 213
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
420-632 |
5.31e-29 |
|
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: 117.45 E-value: 5.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 420 RIRNVTKEYKGkpdkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTiYNNKlsemadlenlsKLT 499
Cdd:COG0411 6 EVRGLTKRFGG----LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRIL-FDGR-----------DIT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 500 GVCP------------QsNVQ-FDFLTVRENLRL---------FAKIKGILP------QEVDKEIQRVLLELEMKNIQDV 551
Cdd:COG0411 70 GLPPhriarlgiartfQ-NPRlFPELTVLENVLVaaharlgrgLLAALLRLPrarreeREARERAEELLERVGLADRADE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 552 LAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVIlfsTQFMDEADI-----LADRKVF 626
Cdd:COG0411 149 PAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGI---TILLIEHDMdlvmgLADRIVV 225
|
....*.
gi 1771853535 627 LSQGKL 632
Cdd:COG0411 226 LDFGRV 231
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1226-1441 |
5.49e-29 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 117.10 E-value: 5.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1226 KEYAGKRKGcfSKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGS-------GGGdale 1298
Cdd:COG1134 25 KELLLRRRR--TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRvsallelGAG---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1299 FLgycpqenalwPNLTVRQHLEVYAAVKGLRKGDaevaITRLVDALK----LQDQLKSPVKTLSEGIKRKLCFVLSILGN 1374
Cdd:COG1134 99 FH----------PELTGRENIYLNGRLLGLSRKE----IDEKFDEIVefaeLGDFIDQPVKTYSSGMRARLAFAVATAVD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1771853535 1375 PSVVLLDEP-STGmDPEGQQQMWQAIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSI 1441
Cdd:COG1134 165 PDILLVDEVlAVG-DAAFQKKCLARIRE-LRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDP 230
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1241-1439 |
6.00e-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: 116.09 E-value: 6.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1241 NKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDALEFLGYCPQ-ENALW--PnLTVRQ 1317
Cdd:cd03235 11 GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGYVPQrRSIDRdfP-ISVRD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1318 --------HLEVYAAVKGLRKGDAEVAITRlVDALKLQDQlksPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDP 1389
Cdd:cd03235 90 vvlmglygHKGLFRRLSKADKAKVDEALER-VGLSELADR---QIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1390 EGQQQMWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVaIMVSGRLRCIG 1439
Cdd:cd03235 166 KTQEDIYELLR-ELRREGMTILVVTHDLGLVLEYFDRV-LLLNRTVVASG 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
419-637 |
6.80e-29 |
|
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: 116.57 E-value: 6.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNklsEMADLENLSKL 498
Cdd:cd03300 1 IELENVSKFYGGFV----ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGK---DITNLPPHKRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 TGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFL 578
Cdd:cd03300 74 VNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1771853535 579 LDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS 637
Cdd:cd03300 154 LDEPLGALDLKLRKDMQLELKRlqKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1246-1440 |
1.48e-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: 1.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1246 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsgGGDALE---------FLGYCPQENALWPNLTVR 1316
Cdd:COG1120 18 DDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLL----DGRDLAslsrrelarRIAYVPQEPPAPFGLTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1317 Q--------HLevyAAVKGLRKGDAEVAIT--RLVDALKLQDQlksPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTG 1386
Cdd:COG1120 94 ElvalgrypHL---GLFGRPSAEDREAVEEalERTGLEHLADR---PVDELSGGERQRVLIARALAQEPPLLLLDEPTSH 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1771853535 1387 MDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1440
Cdd:COG1120 168 LDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
419-627 |
1.50e-28 |
|
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: 115.33 E-value: 1.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLSKL 498
Cdd:cd03218 1 LRAENLSKRYGKRK----VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 TGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFL 578
Cdd:cd03218 77 IGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1771853535 579 LDEPTAGLDPFSRHQVWNL---LKERK----------------TDRV-ILFSTQFMDE---ADILAD---RKVFL 627
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIikiLKDRGigvlitdhnvretlsiTDRAyIIYEGKVLAEgtpEEIAANelvRKVYL 231
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
418-632 |
3.50e-28 |
|
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: 113.84 E-value: 3.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 418 AIRIRNVTKEYKgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMaDLENLSK 497
Cdd:cd03245 2 RIEFRNVSFSYP--NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQL-DPADLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 498 LTGVCPQSNVQFdFLTVRENLRLFAkikgilpQEVDKEiqRVLLELEMKNIQDVLA--------------QNLSGGQKRK 563
Cdd:cd03245 79 NIGYVPQDVTLF-YGTLRDNITLGA-------PLADDE--RILRAAELAGVTDFVNkhpngldlqigergRGLSGGQRQA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1771853535 564 LTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEADiLADRKVFLSQGKL 632
Cdd:cd03245 149 VALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLD-LVDRIIVMDSGRI 216
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
448-636 |
4.05e-28 |
|
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: 113.74 E-value: 4.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 448 GQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNnklSEMADLENLSKLTGVCPQSNVQFDFLTVRENLRLfAKIKGI 527
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING---VDVTAAPPADRPVSMLFQENNLFAHLTVEQNVGL-GLSPGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 528 LPQEVDKE-IQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTD 604
Cdd:cd03298 100 KLTAEDRQaIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDlhAETK 179
|
170 180 190
....*....|....*....|....*....|..
gi 1771853535 605 RVILFSTQFMDEADILADRKVFLSQGKLKCAG 636
Cdd:cd03298 180 MTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
418-637 |
4.10e-28 |
|
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: 114.36 E-value: 4.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 418 AIRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLEnlsK 497
Cdd:cd03296 2 SIEVRNVSKRFGDFV----ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE---R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 498 LTGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEI-QRV--LLEL-EMKNIQDVLAQNLSGGQKRKLTFGIAILGD 573
Cdd:cd03296 75 NVGFVFQHYALFRHMTVFDNVAFGLRVKPRSERPPEAEIrAKVheLLKLvQLDWLADRYPAQLSGGQRQRVALARALAVE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1771853535 574 PQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS 637
Cdd:cd03296 155 PKVLLLDEPFGALDAKVRKELRRWLRRlhDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
419-653 |
4.85e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 115.65 E-value: 4.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEY-KGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIynNKLSEMAD-----L 492
Cdd:PRK13646 3 IRFDNVSYTYqKGTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTV--DDITITHKtkdkyI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 493 ENLSKLTGVC---PQSNVQFDflTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKniQDVLAQN---LSGGQKRKLTF 566
Cdd:PRK13646 81 RPVRKRIGMVfqfPESQLFED--TVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFS--RDVMSQSpfqMSGGQMRKIAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 567 gIAILG-DPQIFLLDEPTAGLDPFSRHQVWNLLKERKTD--RVILFSTQFMDEADILADRKVFLSQGKL--KCAGSSLFL 641
Cdd:PRK13646 157 -VSILAmNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDenKTIILVSHDMNEVARYADEVIVMKEGSIvsQTSPKELFK 235
|
250
....*....|..
gi 1771853535 642 KKKWGIGYHLSL 653
Cdd:PRK13646 236 DKKKLADWHIGL 247
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
419-632 |
6.40e-28 |
|
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: 113.27 E-value: 6.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYkgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMAD--LENLS 496
Cdd:cd03292 1 IEFINVTKTY---PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGraIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 497 KLTGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQI 576
Cdd:cd03292 78 RKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1771853535 577 FLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKL 632
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKiNKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
419-632 |
1.22e-27 |
|
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: 112.24 E-value: 1.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLS-EMADLENLSK 497
Cdd:cd03262 1 IEIKNLHKSFGDF----HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTdDKKNINELRQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 498 LTGVCPQSNVQFDFLTVRENLRL-FAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQI 576
Cdd:cd03262 77 KVGMVFQQFNLFPHLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1771853535 577 FLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKL 632
Cdd:cd03262 157 MLFDEPTSALDPELVGEVLDVMKDlAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
417-637 |
1.27e-27 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 113.25 E-value: 1.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 417 EAIRIRNVTKEY------------------KGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGS 478
Cdd:COG1134 3 SMIEVENVSKSYrlyhepsrslkelllrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 479 VTIyNNKLSEMADLEnlsklTGVCPQsnvqfdfLTVRENLRLFAKIKGILPQEVDKEIQRVL--------LELEMKniqd 550
Cdd:COG1134 83 VEV-NGRVSALLELG-----AGFHPE-------LTGRENIYLNGRLLGLSRKEIDEKFDEIVefaelgdfIDQPVK---- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 551 vlaqNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTD-RVILFSTQFMDEADILADRKVFLSQ 629
Cdd:COG1134 146 ----TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESgRTVIFVSHSMGAVRRLCDRAIWLEK 221
|
....*...
gi 1771853535 630 GKLKCAGS 637
Cdd:COG1134 222 GRLVMDGD 229
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1217-1440 |
1.42e-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: 1.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1217 PVIIASCLRKEYaGKRKgcfskrknkiATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSgggD- 1295
Cdd:COG1137 2 MTLEAENLVKSY-GKRT----------VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGE---Di 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1296 --------ALEFLGYCPQENALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCF 1367
Cdd:COG1137 68 thlpmhkrARLGIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1771853535 1368 VLSILGNPSVVLLDEPSTGMDP---EGQQQMwqaIRatfRNTERGA--LLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1440
Cdd:COG1137 148 ARALATNPKFILLDEPFAGVDPiavADIQKI---IR---HLKERGIgvLITDHNVRETLGICDRAYIISEGKVLAEGT 219
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
421-637 |
1.46e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 113.29 E-value: 1.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 421 IRNVTKEYKGkpdkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEM--ADLENLskl 498
Cdd:COG4674 13 VEDLTVSFDG----FKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLdeHEIARL--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 tGVC-----PqsNVqFDFLTVRENLRL--------FAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLT 565
Cdd:COG4674 86 -GIGrkfqkP--TV-FEELTVFENLELalkgdrgvFASLFARLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1771853535 566 FGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDR---VILFSTQFMDEadiLADRKVFLSQGKLKCAGS 637
Cdd:COG4674 162 IGMLLAQDPKLLLLDEPVAGMTDAETERTAELLKSLAGKHsvvVVEHDMEFVRQ---IARKVTVLHQGSVLAEGS 233
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
420-637 |
2.97e-27 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 111.46 E-value: 2.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 420 RIRNVTKEYKGKpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLSKLT 499
Cdd:TIGR03410 2 EVSNLNVYYGQS----HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 500 GVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIqrvlLEL-----EMKNIQdvlAQNLSGGQKRKLTFGIAILGDP 574
Cdd:TIGR03410 78 AYVPQGREIFPRLTVEENLLTGLAALPRRSRKIPDEI----YELfpvlkEMLGRR---GGDLSGGQQQQLAIARALVTRP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1771853535 575 QIFLLDEPTAGLDPfS----RHQVWNLLKERKtDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS 637
Cdd:TIGR03410 151 KLLLLDEPTEGIQP-SiikdIGRVIRRLRAEG-GMAILLVEQYLDFARELADRYYVMERGRVVASGA 215
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
419-632 |
3.74e-27 |
|
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: 112.74 E-value: 3.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKP-----------DKIE---------ALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGS 478
Cdd:cd03294 1 IKIKGLYKIFGKNPqkafkllakgkSKEEilkktgqtvGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 479 VTIYNNKLSEM--ADLENL-SKLTGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQN 555
Cdd:cd03294 81 VLIDGQDIAAMsrKELRELrRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1771853535 556 LSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKL 632
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRlqAELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1236-1434 |
5.25e-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: 109.20 E-value: 5.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1236 FSKR-KNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDALEF---LGYCPQEN 1307
Cdd:cd03229 6 VSKRyGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedltDLEDELPPLrrrIGMVFQDF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1308 ALWPNLTVRQHLeVYAavkglrkgdaevaitrlvdalklqdqlkspvktLSEGIKRKLCFVLSILGNPSVVLLDEPSTGM 1387
Cdd:cd03229 86 ALFPHLTVLENI-ALG---------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSAL 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1771853535 1388 DPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1434
Cdd:cd03229 132 DPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
419-633 |
5.30e-27 |
|
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: 110.57 E-value: 5.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEmADLENLskl 498
Cdd:TIGR03740 1 LETKNLSKRFGKQ----TAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTR-KDLHKI--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 tGVCPQSNVQFDFLTVRENLRLFAKIKGiLPqevDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFL 578
Cdd:TIGR03740 73 -GSLIESPPLYENLTARENLKVHTTLLG-LP---DSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLI 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1771853535 579 LDEPTAGLDPFSRHQVWNLLKERKTDRV-ILFSTQFMDEADILADRKVFLSQGKLK 633
Cdd:TIGR03740 148 LDEPTNGLDPIGIQELRELIRSFPEQGItVILSSHILSEVQQLADHIGIISEGVLG 203
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1244-1444 |
6.07e-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: 6.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1244 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTA---GQVLLKGSGGGDALEFL-----GYCPQE--NALWPnL 1313
Cdd:COG1123 21 AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALrgrriGMVFQDpmTQLNP-V 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1314 TVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQ 1393
Cdd:COG1123 100 TVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1771853535 1394 QMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL 1444
Cdd:COG1123 180 EILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
415-637 |
8.12e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 112.10 E-value: 8.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 415 GKEAIRIRNVTKEYK--GKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADL 492
Cdd:PRK13633 1 MNEMIKCKNVSYKYEsnEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 493 ENLSKLTGVCPQSN--------VQFDFLTVRENLrlfakikGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKl 564
Cdd:PRK13633 81 WDIRNKAGMVFQNPdnqivatiVEEDVAFGPENL-------GIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQR- 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1771853535 565 tfgIAILG----DPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEAdILADRKVFLSQGKLKCAGS 637
Cdd:PRK13633 153 ---VAIAGilamRPECIIFDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGT 227
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
417-630 |
8.58e-27 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 111.49 E-value: 8.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 417 EAIRIRNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLS-EMADlenl 495
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTgPGAD---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 496 sklTGVCPQSNVQFDFLTVRENLRLFAKIKGILPQE----VDKEIQRV-LLELEMKNIQDvlaqnLSGGQKRKLtfGIA- 569
Cdd:COG4525 78 ---RGVVFQKDALLPWLNVLDNVAFGLRLRGVPKAErrarAEELLALVgLADFARRRIWQ-----LSGGMRQRV--GIAr 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1771853535 570 -ILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQG 630
Cdd:COG4525 148 aLAADPRFLLMDEPFGALDALTREQMQELLLDvwQRTGKGVFLITHSVEEALFLATRLVVMSPG 211
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
410-632 |
9.16e-27 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 118.04 E-value: 9.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 410 PPEFQGKeaIRIRNVTKEYKGkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEM 489
Cdd:TIGR03375 457 RPRLQGE--IEFRNVSFAYPG--QETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQI 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 490 aDLENLSKLTGVCPQSNVQFdFLTVRENLRLFAkikgilPQEVDKEIQRVLlelEMKNIQDVLA--------------QN 555
Cdd:TIGR03375 533 -DPADLRRNIGYVPQDPRLF-YGTLRDNIALGA------PYADDEEILRAA---ELAGVTEFVRrhpdgldmqigergRS 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 556 LSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFST---QFMDeadiLADRKVFLSQGKL 632
Cdd:TIGR03375 602 LSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGKTLVLVThrtSLLD----LVDRIIVMDNGRI 677
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1219-1434 |
9.85e-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: 9.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1219 IIASCLRKEYAGKRKGcfskrknKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG---SGGGD 1295
Cdd:cd03293 1 LEVRNVSKTYGGGGGA-------VTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGepvTGPGP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1296 AlefLGYCPQENALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNP 1375
Cdd:cd03293 74 D---RGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDP 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1771853535 1376 SVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMvSGR 1434
Cdd:cd03293 151 DVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL-SAR 208
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
419-632 |
1.01e-26 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 113.36 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEM--ADLENLS 496
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALseKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 497 KLTGVCPQsnvQFDFL---TVRENLRLFAKIKGILPQEVDKeiqRV--LLEL-EMKNIQDVLAQNLSGGQKRKLtfGIA- 569
Cdd:PRK11153 82 RQIGMIFQ---HFNLLssrTVFDNVALPLELAGTPKAEIKA---RVteLLELvGLSDKADRYPAQLSGGQKQRV--AIAr 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1771853535 570 -ILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKL 632
Cdd:PRK11153 154 aLASNPKVLLCDEATSALDPATTRSILELLKDinRELGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
419-653 |
1.95e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 111.27 E-value: 1.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGK-PDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLS---EMADLEN 494
Cdd:PRK13634 3 ITFQKVEHRYQYKtPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 495 LSKLTGVC---PQSnvQFDFLTVRENLrLFAKIKGILPQEVDKEIQRVLLELEMKNiQDVLAQN---LSGGQKRKltfgI 568
Cdd:PRK13634 83 LRKKVGIVfqfPEH--QLFEETVEKDI-CFGPMNFGVSEEDAKQKAREMIELVGLP-EELLARSpfeLSGGQMRR----V 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 569 AILG----DPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS--SLF 640
Cdd:PRK13634 155 AIAGvlamEPEVLVLDEPTAGLDPKGRKEMMEMFYKlhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTprEIF 234
|
250
....*....|...
gi 1771853535 641 LKKKWGIGYHLSL 653
Cdd:PRK13634 235 ADPDELEAIGLDL 247
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
417-636 |
3.66e-26 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 109.02 E-value: 3.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 417 EAIRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKG-SVTIYNNKLSEmADLENL 495
Cdd:COG1119 2 PLLELRNVTVRRGGKT----ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGG-EDVWEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 496 SKLTGVCpqSNVQFDFLTVRENLR------LFAKIkGiLPQEVDKE----IQRVLLELEMKNIQDVLAQNLSGGQKRKLT 565
Cdd:COG1119 77 RKRIGLV--SPALQLRFPRDETVLdvvlsgFFDSI-G-LYREPTDEqrerARELLELLGLAHLADRPFGTLSQGEQRRVL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1771853535 566 FGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEadILA--DRKVFLSQGKLKCAG 636
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKlaAEGAPTLVLVTHHVEE--IPPgiTHVLLLKDGRVVAAG 225
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
419-636 |
3.69e-26 |
|
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: 106.63 E-value: 3.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKPDKIeaLKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADleNLSKL 498
Cdd:cd03247 1 LSINNVSFSYPEQEQQV--LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK--ALSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 TGVCPQSNVQFDfLTVRENlrlfakikgilpqevdkeiqrvllelemkniqdvLAQNLSGGQKRKLTFGIAILGDPQIFL 578
Cdd:cd03247 77 ISVLNQRPYLFD-TTLRNN----------------------------------LGRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1771853535 579 LDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEADiLADRKVFLSQGKLKCAG 636
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIE-HMDKILFLENGKIIMQG 178
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
419-643 |
3.73e-26 |
|
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: 108.47 E-value: 3.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEY-KGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMaDLENLSK 497
Cdd:cd03254 3 IEFENVNFSYdEKKP----VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDI-SRKSLRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 498 LTGVCPQSNVQFDFlTVRENLRLFAkikgilPQEVDKEIQRVLLELEMKNIQDVL-----------AQNLSGGQKRKLTF 566
Cdd:cd03254 78 MIGVVLQDTFLFSG-TIMENIRLGR------PNATDEEVIEAAKEAGAHDFIMKLpngydtvlgenGGNLSQGERQLLAI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 567 GIAILGDPQIFLLDEPTAGLDPFSRHQVWN---LLKERKTDRVI---LFSTQFmdeadilADRKVFLSQGKLKCAGS--S 638
Cdd:cd03254 151 ARAMLRDPKILILDEATSNIDTETEKLIQEaleKLMKGRTSIIIahrLSTIKN-------ADKILVLDDGKIIEEGThdE 223
|
....*
gi 1771853535 639 LFLKK 643
Cdd:cd03254 224 LLAKK 228
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
419-637 |
5.04e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 109.75 E-value: 5.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEY-KGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYN-NKLSEMADLENLS 496
Cdd:PRK13637 3 IKIENLTHIYmEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvDITDKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 497 KLTGVCPQ-SNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRV--LLELEMKNIQDVLAQNLSGGQKRKltfgIAILG- 572
Cdd:PRK13637 83 KKVGLVFQyPEYQLFEETIEKDIAFGPINLGLSEEEIENRVKRAmnIVGLDYEDYKDKSPFELSGGQKRR----VAIAGv 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 573 ---DPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS 637
Cdd:PRK13637 159 vamEPKILILDEPTAGLDPKGRDEILNKIKElhKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGT 228
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1237-1440 |
6.51e-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: 6.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1237 SKR-KNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsgGGDALEFL-------GYCPQENA 1308
Cdd:COG3842 12 SKRyGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILL----DGRDVTGLppekrnvGMVFQDYA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1309 LWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEG------IKRKLCFvlsilgNPSVVLLDE 1382
Cdd:COG3842 88 LFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGqqqrvaLARALAP------EPRVLLLDE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1771853535 1383 PSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1440
Cdd:COG3842 162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGT 219
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
419-632 |
7.72e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 109.01 E-value: 7.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYkgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTI------YNNKlsemaDL 492
Cdd:PRK13639 2 LETRDLKYSY---PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIkgepikYDKK-----SL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 493 ENLSKLTGVCPQ-SNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKltfgIAIL 571
Cdd:PRK13639 74 LEVRKTVGIVFQnPDDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKR----VAIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1771853535 572 G----DPQIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKL 632
Cdd:PRK13639 150 GilamKPEIIVLDEPTSGLDPMGASQIMKLLYDlNKEGITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
419-631 |
8.84e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 108.25 E-value: 8.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKE-YKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLE---N 494
Cdd:COG1101 2 LELKNLSKTfNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKrakY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 495 LSK-----LTGVCPQsnvqfdfLTVRENLRLFAK-------IKGILPQEVDKEIQRV-LLELEMKNIQDVLAQNLSGGQK 561
Cdd:COG1101 82 IGRvfqdpMMGTAPS-------MTIEENLALAYRrgkrrglRRGLTKKRRELFRELLaTLGLGLENRLDTKVGLLSGGQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1771853535 562 RKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLlkerkTDRVI-------LFSTQFMDEADILADRKVFLSQGK 631
Cdd:COG1101 155 QALSLLMATLTKPKLLLLDEHTAALDPKTAALVLEL-----TEKIVeennlttLMVTHNMEQALDYGNRLIMMHEGR 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1224-1435 |
1.84e-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: 1.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1224 LRKEYAGKRKgcfskrkNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG---SGGGDA---- 1296
Cdd:cd03255 6 LSKTYGGGGE-------KVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGtdiSKLSEKelaa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1297 --LEFLGYCPQENALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEG------IKRklcfv 1368
Cdd:cd03255 79 frRRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGqqqrvaIAR----- 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1771853535 1369 lSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAvCDRVAIMVSGRL 1435
Cdd:cd03255 154 -ALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1236-1435 |
2.07e-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: 106.44 E-value: 2.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1236 FSKRKNKI-ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG---SGGGDALEFL-----GYCPQE 1306
Cdd:cd03257 11 FPTGGGSVkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdlLKLSRRLRKIrrkeiQMVFQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1307 --NALWPNLTVRQHLEvyAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKT-----LSEGIKRKLCFVLSILGNPSVVL 1379
Cdd:cd03257 91 pmSSLNPRMTIGEQIA--EPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNrypheLSGGQRQRVAIARALALNPKLLI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1380 LDEPSTGMDPEGQQQmwqaIRATFRN--TERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1435
Cdd:cd03257 169 ADEPTSALDVSVQAQ----ILDLLKKlqEELGLtlLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
418-637 |
4.53e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 106.81 E-value: 4.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 418 AIRIRNVTKEYkgkPD-KIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVP---TKGSVTIYNNKLSEMADLE 493
Cdd:PRK13640 5 IVEFKHVSFTY---PDsKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 494 NLSKLTGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKltfgIAILG- 572
Cdd:PRK13640 82 IREKVGIVFQNPDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQR----VAIAGi 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 573 ---DPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDR-VILFS-TQFMDEADiLADRKVFLSQGKLKCAGS 637
Cdd:PRK13640 158 lavEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnLTVISiTHDIDEAN-MADQVLVLDDGKLLAQGS 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1214-1444 |
4.71e-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: 4.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1214 DEKPVIIASCLRKEYAGKRKGCFskrknkIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG--- 1290
Cdd:COG1123 256 AAEPLLEVRNLSKRYPVRGKGGV------RAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGkdl 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1291 --SGGGDALEF---LGYCPQ--ENALWPNLTVRQHL-EVYAAVKGLRKGDAEVAITRLVDALKLQDQL--KSPvKTLSEG 1360
Cdd:COG1123 330 tkLSRRSLRELrrrVQMVFQdpYSSLNPRMTVGDIIaEPLRLHGLLSRAERRERVAELLERVGLPPDLadRYP-HELSGG 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1361 IKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1440
Cdd:COG1123 409 QRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGP 488
|
....
gi 1771853535 1441 IQHL 1444
Cdd:COG1123 489 TEEV 492
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
418-632 |
4.92e-25 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 105.48 E-value: 4.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 418 AIRIRNVTKEYKGKpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNN------KLSEMAD 491
Cdd:COG4161 2 SIQLKNINCFYGSH----QALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdfsqKPSEKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 492 LENLSKLTGVCPQSNVqFDFLTVRENLrLFAKIK--GILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIA 569
Cdd:COG4161 78 RLLRQKVGMVFQQYNL-WPHLTVMENL-IEAPCKvlGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1771853535 570 ILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKT---DRVILfsTQFMDEADILADRKVFLSQGKL 632
Cdd:COG4161 156 LMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtgiTQVIV--THEVEFARKVASQVVYMEKGRI 219
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
419-632 |
5.23e-25 |
|
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: 102.89 E-value: 5.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGkpdkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIyNNKlsemadlenlskl 498
Cdd:cd03216 1 LELRGITKRFGG----VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILV-DGK------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 tgvcpqsnvQFDFLTVRENLRLfakikGIlpqevdkeiqrvllelemkniqdVLAQNLSGGQKRKLTFGIAILGDPQIFL 578
Cdd:cd03216 63 ---------EVSFASPRDARRA-----GI-----------------------AMVYQLSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1771853535 579 LDEPTAGLDPFSRHQVWNLLKERKTDRV-ILFSTQFMDEADILADRKVFLSQGKL 632
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRRLRAQGVaVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1214-1453 |
6.10e-25 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 112.91 E-value: 6.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1214 DEKPVIIASCLRKeyagkRKGCFskrknkIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG--- 1290
Cdd:NF033858 262 DDEPAIEARGLTM-----RFGDF------TAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGqpv 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1291 -SGGGDALEFLGYCPQENALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVL 1369
Cdd:NF033858 331 dAGDIATRRRVGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAV 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1370 SILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAvCDRVAIMVSGRLRCIGSIQHLKSKFG 1449
Cdd:NF033858 411 AVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAER-CDRISLMHAGRVLASDTPAALVAARG 489
|
....
gi 1771853535 1450 KDYL 1453
Cdd:NF033858 490 AATL 493
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
419-633 |
1.05e-24 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 103.79 E-value: 1.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKPDKIEalkdlvFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLEN-LSK 497
Cdd:TIGR01277 1 LALDKVRYEYEHLPMEFD------LNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRpVSM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 498 LTgvcpQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIF 577
Cdd:TIGR01277 75 LF----QENNLFAHLTVRQNIGLGLHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1771853535 578 LLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKLK 633
Cdd:TIGR01277 151 LLDEPFSALDPLLREEMLALVKQlcSERQRTLLMVTHHLSDARAIASQIAVVSQGKIK 208
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
419-637 |
1.36e-24 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 104.81 E-value: 1.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLEnLSKL 498
Cdd:COG4559 2 LEAENLSVRLGGRT----LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWE-LARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 TGVCPQ-SNVQFDFlTVRENLRLfakikGILP-----QEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAIL- 571
Cdd:COG4559 77 RAVLPQhSSLAFPF-TVEEVVAL-----GRAPhgssaAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAq 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 572 ------GDPQIFLLDEPTAGLDPFSRHQVWNLLKERkTDR-----VIL----FSTQFmdeadilADRKVFLSQGKLKCAG 636
Cdd:COG4559 151 lwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQL-ARRgggvvAVLhdlnLAAQY-------ADRILLLHQGRLVAQG 222
|
.
gi 1771853535 637 S 637
Cdd:COG4559 223 T 223
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1244-1435 |
1.53e-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: 1.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1244 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSgggdaleflgycpqenalwpnltvrqhlevya 1323
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK-------------------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1324 avkglrkgdaEVAITRLVDALKL------QdqlkspvktLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQ 1397
Cdd:cd03216 63 ----------EVSFASPRDARRAgiamvyQ---------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFK 123
|
170 180 190
....*....|....*....|....*....|....*...
gi 1771853535 1398 AIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1435
Cdd:cd03216 124 VIRR-LRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
418-637 |
1.75e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 105.21 E-value: 1.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 418 AIRIRNVTKEYK-GKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKL---SEMADLE 493
Cdd:PRK13649 2 GINLQNVSYTYQaGTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstSKNKDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 494 NLSKLTGVC---PQSNVqFDfLTVRENLRLFAKIKGILPQEVDKeiqRVLLELEMKNI-QDVLAQN---LSGGQKRKltf 566
Cdd:PRK13649 82 QIRKKVGLVfqfPESQL-FE-ETVLKDVAFGPQNFGVSQEEAEA---LAREKLALVGIsESLFEKNpfeLSGGQMRR--- 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1771853535 567 gIAILG----DPQIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS 637
Cdd:PRK13649 154 -VAIAGilamEPKILVLDEPTAGLDPKGRKELMTLFKKlHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGK 228
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
418-636 |
1.91e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 104.82 E-value: 1.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 418 AIRIRNVTKEYKgkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLSK 497
Cdd:PRK13647 4 IIEVEDLHFRYK---DGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 498 LTGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKltfgIAILG----D 573
Cdd:PRK13647 81 VGLVFQDPDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKR----VAIAGvlamD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1771853535 574 PQIFLLDEPTAGLDPFSRHQV----WNLLKERKTdrvILFSTQFMDEADILADRKVFLSQGKLKCAG 636
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLmeilDRLHNQGKT---VIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1239-1415 |
2.11e-24 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 102.64 E-value: 2.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1239 RKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGD-----ALEFLGYcpqENALWPNL 1313
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDpdvaeACHYLGH---RNAMKPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1314 TVRQHLEVYAAVKGLRKGDAEVAItrlvDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQ 1393
Cdd:PRK13539 89 TVAENLEFWAAFLGGEELDIAAAL----EAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVA 164
|
170 180
....*....|....*....|....
gi 1771853535 1394 QMWQAIRAtfrNTERG--ALLTTH 1415
Cdd:PRK13539 165 LFAELIRA---HLAQGgiVIAATH 185
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
409-632 |
2.34e-24 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 103.96 E-value: 2.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 409 APPEFQGKEAIRIRNVTKEYKGKpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLS--VP---TKGSVT--- 480
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGDK----QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlIPgarVEGEILldg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 481 --IYNNKLsemaDLENLSKLTG-VCPQSNVqfdF-LTVRENLRLFAKIKGILP-QEVDKEIQRVLLEL----EMKNIQDV 551
Cdd:COG1117 78 edIYDPDV----DVVELRRRVGmVFQKPNP---FpKSIYDNVAYGLRLHGIKSkSELDEIVEESLRKAalwdEVKDRLKK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 552 LAQNLSGGQKRKLTfgIA--ILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEADILADRKVFLSQ 629
Cdd:COG1117 151 SALGLSGGQQQRLC--IAraLAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARVSDYTAFFYL 228
|
...
gi 1771853535 630 GKL 632
Cdd:COG1117 229 GEL 231
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
432-617 |
2.47e-24 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 102.12 E-value: 2.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 432 PDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKL--SEMADLENLSKLTGVCPQSNVQF 509
Cdd:TIGR01166 2 PGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLdySRKGLLERRQRVGLVFQDPDDQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 510 DFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPF 589
Cdd:TIGR01166 82 FAADVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPA 161
|
170 180
....*....|....*....|....*....
gi 1771853535 590 SRHQVWNLLKE-RKTDRVILFSTQFMDEA 617
Cdd:TIGR01166 162 GREQMLAILRRlRAEGMTVVISTHDVDLA 190
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
418-632 |
2.47e-24 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 103.56 E-value: 2.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 418 AIRIRNVTKEYKGKpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNK--LSEMADLENL 495
Cdd:PRK11124 2 SIQLNGINCFYGAH----QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdFSKTPSDKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 496 SKLtgvcpQSNVQFDF--------LTVRENL-RLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTF 566
Cdd:PRK11124 78 REL-----RRNVGMVFqqynlwphLTVQQNLiEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1771853535 567 GIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE-RKT--DRVILfsTQFMDEADILADRKVFLSQGKL 632
Cdd:PRK11124 153 ARALMMEPQVLLFDEPTAALDPEITAQIVSIIRElAETgiTQVIV--THEVEVARKTASRVVYMENGHI 219
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
394-627 |
2.76e-24 |
|
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: 109.30 E-value: 2.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 394 DEMDADPSFHDSF---EQAPPEFQGKE--------AIRIRNVTKEYkgkPDKIEALKDLVFDIYEGQITAILGHSGAGKS 462
Cdd:TIGR02857 286 ARADGVAAAEALFavlDAAPRPLAGKApvtaapasSLEFSGVSVAY---PGRRPALRPVSFTVPPGERVALVGPSGAGKS 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 463 TLLNILSGLSVPTKGSVTIYNNKLSEmADLENLSKLTGVCPQSNVQFDfLTVRENLRLFAkiKGILPQEVDKEIQRV-LL 541
Cdd:TIGR02857 363 TLLNLLLGFVDPTEGSIAVNGVPLAD-ADADSWRDQIAWVPQHPFLFA-GTIAENIRLAR--PDASDAEIREALERAgLD 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 542 ELEM---KNIQDVLAQN---LSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQfmD 615
Cdd:TIGR02857 439 EFVAalpQGLDTPIGEGgagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTH--R 516
|
250
....*....|...
gi 1771853535 616 EADI-LADRKVFL 627
Cdd:TIGR02857 517 LALAaLADRIVVL 529
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
419-651 |
2.95e-24 |
|
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: 103.08 E-value: 2.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMaDLENLSKL 498
Cdd:cd03251 1 VEFKNVTFRYPG--DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDY-TLASLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 TGVCPQSNVQFDFlTVRENLRlFAKikgilPQEVDKEIQRVlleLEMKNIQDVLAQ--------------NLSGGQKRKL 564
Cdd:cd03251 78 IGLVSQDVFLFND-TVAENIA-YGR-----PGATREEVEEA---ARAANAHEFIMElpegydtvigergvKLSGGQRQRI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 565 TFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVIL-----FSTqFMDeadilADRKVFLSQGKLKCAGSSL 639
Cdd:cd03251 148 AIARALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFviahrLST-IEN-----ADRIVVLEDGKIVERGTHE 221
|
250
....*....|..
gi 1771853535 640 FLKKKWGIGYHL 651
Cdd:cd03251 222 ELLAQGGVYAKL 233
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
440-636 |
3.15e-24 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 102.37 E-value: 3.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 440 DLVFDIyEGQITAILGHSGAGKSTLLNILSGLSVPTKGSV----TIYNNKLSEMaDLENLSKLTGVCPQSNVQFDFLTVR 515
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngTVLFDSRKKI-NLPPQQRKIGLVFQQYALFPHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 516 ENLRLFAKIKGILPQEVDKEIQRVLLELEmkNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVW 595
Cdd:cd03297 94 ENLAFGLKRKRNREDRISVDELLDLLGLD--HLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1771853535 596 NLLKERKTDRVI--LFSTQFMDEADILADRKVFLSQGKLKCAG 636
Cdd:cd03297 172 PELKQIKKNLNIpvIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1246-1435 |
3.15e-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: 3.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1246 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-----SGGGDALEfLG----YcpQENALWPNLTVR 1316
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepvrfRSPRDAQA-AGiaiiH--QELNLVPNLSVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1317 Q--HLEVYAAVKGLRKGDAEVAITR-LVDALKLQDQLKSPVKTLSEGiKRKLcfVL---SILGNPSVVLLDEPSTGMDPE 1390
Cdd:COG1129 98 EniFLGREPRRGGLIDWRAMRRRAReLLARLGLDIDPDTPVGDLSVA-QQQL--VEiarALSRDARVLILDEPTASLTER 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1771853535 1391 GQQQMWQAIRaTFRntERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1435
Cdd:COG1129 175 EVERLFRIIR-RLK--AQGVaiIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
418-652 |
3.34e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 104.53 E-value: 3.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 418 AIRIRNVTKEYK-GKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLS 496
Cdd:PRK13641 2 SIKFENVDYIYSpGTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 497 KL---TGVCPQ-SNVQFDFLTVRENLRLFAKIKGILPQEVD----KEIQRVLLELEMKNIQDVlaqNLSGGQKRKLTFGI 568
Cdd:PRK13641 82 KLrkkVSLVFQfPEAQLFENTVLKDVEFGPKNFGFSEDEAKekalKWLKKVGLSEDLISKSPF---ELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 569 AILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKL--KCAGSSLFLKKKW 645
Cdd:PRK13641 159 VMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDyQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLikHASPKEIFSDKEW 238
|
....*..
gi 1771853535 646 GIGYHLS 652
Cdd:PRK13641 239 LKKHYLD 245
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
419-631 |
5.15e-24 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 102.14 E-value: 5.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKPdkiealkdLVFD--IYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIyNNklsemadlENLS 496
Cdd:COG3840 2 LRLDDLTYRYGDFP--------LRFDltIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILW-NG--------QDLT 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 497 KLTgvcP---------QSNVQFDFLTVRENLRLfakikGILP---------QEVDKEIQRVLLElemkNIQDVLAQNLSG 558
Cdd:COG3840 65 ALP---PaerpvsmlfQENNLFPHLTVAQNIGL-----GLRPglkltaeqrAQVEQALERVGLA----GLLDRLPGQLSG 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1771853535 559 GQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGK 631
Cdd:COG3840 133 GQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDElcRERGLTVLMVTHDPEDAARIADRVLLVADGR 207
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
434-632 |
5.66e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 102.93 E-value: 5.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 434 KIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLS-----VPTKGSVtIYN--NKLSEMADLENLSKLTGVCPQSN 506
Cdd:PRK14239 17 KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNdlnpeVTITGSI-VYNghNIYSPRTDTVDLRKEIGMVFQQP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 507 VQFDFlTVRENLRLFAKIKGI-----LPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDE 581
Cdd:PRK14239 96 NPFPM-SIYENVVYGLRLKGIkdkqvLDEAVEKSLKGASIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1771853535 582 PTAGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEADILADRKVFLSQGKL 632
Cdd:PRK14239 175 PTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDL 225
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
405-588 |
5.95e-24 |
|
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: 108.22 E-value: 5.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 405 SFEQAPPEFQGKEAIRIRNVTKEYKGKPdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNN 484
Cdd:TIGR02868 321 SAPAAGAVGLGKPTLELRDLSAGYPGAP---PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGV 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 485 KLSEmADLENLSKLTGVCPQSNVQFDfLTVRENLRLFAkiKGILPQEVDKEIQRVLLELEMKNIQDVL-------AQNLS 557
Cdd:TIGR02868 398 PVSS-LDQDEVRRRVSVCAQDAHLFD-TTVRENLRLAR--PDATDEELWAALERVGLADWLRALPDGLdtvlgegGARLS 473
|
170 180 190
....*....|....*....|....*....|.
gi 1771853535 558 GGQKRKLTFGIAILGDPQIFLLDEPTAGLDP 588
Cdd:TIGR02868 474 GGERQRLALARALLADAPILLLDEPTEHLDA 504
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
416-636 |
9.03e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 103.17 E-value: 9.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 416 KEAIRIRNVTKEYKGkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENL 495
Cdd:PRK13635 3 EEIIRVEHISFRYPD--AATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 496 SKLTGVCPQSNVQFDFLTVRENLRLFAKIKGIlpqEVDKEIQRVLLELEMKNIQDVLAQ---NLSGGQKRKltfgIAILG 572
Cdd:PRK13635 81 RQVGMVFQNPDNQFVGATVQDDVAFGLENIGV---PREEMVERVDQALRQVGMEDFLNRephRLSGGQKQR----VAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1771853535 573 ----DPQIFLLDEPTAGLDPFSRHQVWN---LLKERKTDRVILFsTQFMDEAdILADRKVFLSQGKLKCAG 636
Cdd:PRK13635 154 vlalQPDIIILDEATSMLDPRGRREVLEtvrQLKEQKGITVLSI-THDLDEA-AQADRVIVMNKGEILEEG 222
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
419-644 |
1.08e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 103.00 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYkgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVtIYNNKLSEMA--DLENLS 496
Cdd:PRK13636 6 LKVEELNYNY---SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRI-LFDGKPIDYSrkGLMKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 497 KLTGVCPQS-NVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQ 575
Cdd:PRK13636 82 ESVGMVFQDpDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPK 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1771853535 576 IFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAG--SSLFLKKK 644
Cdd:PRK13636 162 VLVLDEPTAGLDPMGVSEIMKLLVEmqKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGnpKEVFAEKE 234
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
440-637 |
1.32e-23 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 104.42 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 440 DLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMA---DLENLSKLTGVCPQSNVQFDFLTVRE 516
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRkgiFLPPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 517 NLRLfaKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWN 596
Cdd:TIGR02142 95 NLRY--GMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1771853535 597 LLkERKTDRV---ILFSTQFMDEADILADRKVFLSQGKLKCAGS 637
Cdd:TIGR02142 173 YL-ERLHAEFgipILYVSHSLQEVLRLADRVVVLEDGRVAAAGP 215
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
419-627 |
2.35e-23 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 100.49 E-value: 2.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIynnklsemaDLENLSKL 498
Cdd:COG1137 4 LEAENLVKSYGKRT----VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFL---------DGEDITHL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 T---------GVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIA 569
Cdd:COG1137 71 PmhkrarlgiGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 570 ILGDPQIFLLDEPTAGLDPFSRHQVWNL---LKERK----------------TDRV-ILFSTQFMDE---ADILAD---R 623
Cdd:COG1137 151 LATNPKFILLDEPFAGVDPIAVADIQKIirhLKERGigvlitdhnvretlgiCDRAyIISEGKVLAEgtpEEILNNplvR 230
|
....
gi 1771853535 624 KVFL 627
Cdd:COG1137 231 KVYL 234
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
419-588 |
3.14e-23 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 100.07 E-value: 3.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEM-ADLENLSK 497
Cdd:COG1126 2 IEIENLHKSFGDL----EVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSkKDINKLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 498 LTGVCPQS-NVqFDFLTVRENLRLfA--KIKGILPQEVdKEIQRVLLE-LEMKNIQDVLAQNLSGGQK-RkltfgIAI-- 570
Cdd:COG1126 78 KVGMVFQQfNL-FPHLTVLENVTL-ApiKVKKMSKAEA-EERAMELLErVGLADKADAYPAQLSGGQQqR-----VAIar 149
|
170 180
....*....|....*....|
gi 1771853535 571 -LG-DPQIFLLDEPTAGLDP 588
Cdd:COG1126 150 aLAmEPKVMLFDEPTSALDP 169
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1237-1439 |
4.17e-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: 99.25 E-value: 4.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1237 SKR-KNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGD--------ALEFLGYcpqen 1307
Cdd:cd03301 7 TKRfGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDlppkdrdiAMVFQNY----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1308 ALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGM 1387
Cdd:cd03301 82 ALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1771853535 1388 DPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1439
Cdd:cd03301 162 DAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
419-637 |
4.68e-23 |
|
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: 99.11 E-value: 4.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMaDLENLSKL 498
Cdd:cd03244 3 IEFKNVSLRYR--PNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKI-GLHDLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 TGVCPQSNVQFDFlTVRENLRLFAkikgilpQEVDKEIQRVLLELEMKNIQDVLA-----------QNLSGGQKRKLTFG 567
Cdd:cd03244 80 ISIIPQDPVLFSG-TIRSNLDPFG-------EYSDEELWQALERVGLKEFVESLPggldtvveeggENLSVGQRQLLCLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1771853535 568 IAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQ----FMDeadilADRKVFLSQGKLKCAGS 637
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHrldtIID-----SDRILVLDKGRVVEFDS 220
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
419-651 |
7.49e-23 |
|
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: 99.15 E-value: 7.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKPDkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMAdLENLSKL 498
Cdd:cd03249 1 IEFKNVSFRYPSRPD-VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLN-LRWLRSQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 TGVCPQSNVQFDfLTVRENLRLfakikGiLPQEVDKEIQRVlleLEMKNIQDVLAQ--------------NLSGGQKRKL 564
Cdd:cd03249 79 IGLVSQEPVLFD-GTIAENIRY-----G-KPDATDEEVEEA---AKKANIHDFIMSlpdgydtlvgergsQLSGGQKQRI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 565 TFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVIL-----FSTqfmdeadIL-ADRKVFLSQGKLKCAGSS 638
Cdd:cd03249 149 AIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIviahrLST-------IRnADLIAVLQNGQVVEQGTH 221
|
250
....*....|...
gi 1771853535 639 LFLKKKWGIGYHL 651
Cdd:cd03249 222 DELMAQKGVYAKL 234
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
419-636 |
9.92e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 99.83 E-value: 9.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVtIYNNKLSEMADLENLSKL 498
Cdd:PRK13648 8 IVFKNVSFQYQS--DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEI-FYNNQAITDDNFEKLRKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 TGVCPQ--------SNVQFDFLTVRENLRL-FAKIKGILPQevdkeiqrVLLELEMKNIQDVLAQNLSGGQKRKltfgIA 569
Cdd:PRK13648 85 IGIVFQnpdnqfvgSIVKYDVAFGLENHAVpYDEMHRRVSE--------ALKQVDMLERADYEPNALSGGQKQR----VA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1771853535 570 ILG----DPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDR--VILFSTQFMDEAdILADRKVFLSQGKLKCAG 636
Cdd:PRK13648 153 IAGvlalNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEA-MEADHVIVMNKGTVYKEG 224
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1246-1453 |
1.01e-22 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 98.56 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1246 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSgggDALEF------LGYCPQENALWPNLTVRQHL 1319
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGK---DITNLppekrdISYVPQNYALFPHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1320 EVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAI 1399
Cdd:cd03299 93 AYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREEL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1771853535 1400 RATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQ----HLKSKFGKDYL 1453
Cdd:cd03299 173 KKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEevfkKPKNEFVAEFL 230
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
438-630 |
1.14e-22 |
|
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: 98.31 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 438 LKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSE-----MADLENLSKLTgvcpqsnvqfdFL 512
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEpgpdrMVVFQNYSLLP-----------WL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 513 TVRENLRLfaKIKGILPQEVDKEIQRVLLE-LEMKNI---QDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDP 588
Cdd:TIGR01184 70 TVRENIAL--AVDRVLPDLSKSERRAIVEEhIALVGLteaADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1771853535 589 FSRHQVWN-LLKERKTDRV-ILFSTQFMDEADILADRKVFLSQG 630
Cdd:TIGR01184 148 LTRGNLQEeLMQIWEEHRVtVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1224-1444 |
1.36e-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: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1224 LRKEYAGKRKgcfskrkNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDAL-E 1298
Cdd:cd03258 7 VSKVFGDTGG-------KVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGtdltLLSGKELrK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1299 F---LGYCPQENALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNP 1375
Cdd:cd03258 80 ArrrIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1771853535 1376 SVVLLDEPSTGMDPEGQQQMWQAIRATfrNTERG--ALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL 1444
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDI--NRELGltIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
422-631 |
1.96e-22 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 103.97 E-value: 1.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 422 RNVTKEYKGKPDKIeALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVP-TKGSVTIYNNklSEMADLENLSKLTG 500
Cdd:TIGR00955 26 RLRGCFCRERPRKH-LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgVKGSGSVLLN--GMPIDAKEMRAISA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 501 VCPQSNVQFDFLTVRENLRLFAKIKgiLPQEVDKE-----IQRVLLELEMKNIQDVLAQ------NLSGGQKRKLTFGIA 569
Cdd:TIGR00955 103 YVQQDDLFIPTLTVREHLMFQAHLR--MPRRVTKKekrerVDEVLQALGLRKCANTRIGvpgrvkGLSGGERKRLAFASE 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1771853535 570 ILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEADI--LADRKVFLSQGK 631
Cdd:TIGR00955 181 LLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELfeLFDKIILMAEGR 244
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
443-637 |
2.22e-22 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 100.56 E-value: 2.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 443 FDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLS----KLtGVCPQSNVQFDFLTVRENL 518
Cdd:COG4148 20 FTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFLPphrrRI-GYVFQEARLFPHLSVRGNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 519 RlFAkIKGILPQEvdkeiQRVLLE--LEMKNIQDVLA---QNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQ 593
Cdd:COG4148 99 L-YG-RKRAPRAE-----RRISFDevVELLGIGHLLDrrpATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1771853535 594 VWNLLkERKTDRV---ILFSTQFMDEADILADRKVFLSQGKLKCAGS 637
Cdd:COG4148 172 ILPYL-ERLRDELdipILYVSHSLDEVARLADHVVLLEQGRVVASGP 217
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
414-637 |
2.35e-22 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 101.18 E-value: 2.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 414 QGKEAIRIRNVTKEYKGKpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIynnklsemadle 493
Cdd:PRK09452 10 SLSPLVELRGISKSFDGK----EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIML------------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 494 NLSKLTGVCP---------QSNVQFDFLTVRENLRLFAKIKGILPQEVDKeiqRVLLELEMKNIQDvLAQ----NLSGGQ 560
Cdd:PRK09452 74 DGQDITHVPAenrhvntvfQSYALFPHMTVFENVAFGLRMQKTPAAEITP---RVMEALRMVQLEE-FAQrkphQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1771853535 561 KRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLK--ERKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS 637
Cdd:PRK09452 150 QQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKalQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1236-1439 |
2.45e-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: 95.97 E-value: 2.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1236 FSKRKNKIAtRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGsgggdaleflgycpQENALWPNLTV 1315
Cdd:cd03214 7 VGYGGRTVL-DDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDG--------------KDLASLSPKEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1316 RQHLEVyaavkglrkgdaevaITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQM 1395
Cdd:cd03214 72 ARKIAY---------------VPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIEL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1771853535 1396 WQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1439
Cdd:cd03214 137 LELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
423-637 |
4.41e-22 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 96.89 E-value: 4.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 423 NVTKEYKGKpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLSKLTGVC 502
Cdd:PRK10895 8 NLAKAYKGR----RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 503 PQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLL-ELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDE 581
Cdd:PRK10895 84 PQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMeEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1771853535 582 PTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS 637
Cdd:PRK10895 164 PFAGVDPISVIDIKRIIEHlRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
418-618 |
4.47e-22 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 103.67 E-value: 4.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 418 AIRIRNVTKEYKgkpdKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNnklsemADLENLSK 497
Cdd:NF033858 1 VARLEGVSHRYG----KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLG------GDMADARH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 498 LTGVCPQ---------SNVQFDfLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGI 568
Cdd:NF033858 71 RRAVCPRiaympqglgKNLYPT-LSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCC 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1771853535 569 AILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRV---ILFSTQFMDEAD 618
Cdd:NF033858 150 ALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERPgmsVLVATAYMEEAE 202
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
419-636 |
4.80e-22 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 96.64 E-value: 4.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKpdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVtiynnkLSEMADLENLS-- 496
Cdd:cd03299 1 LKVENLSKDWKEF-----KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKI------LLNGKDITNLPpe 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 497 -KLTGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLlelEMKNIQDVLAQN---LSGGQKRKLTFGIAILG 572
Cdd:cd03299 70 kRDISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIA---EMLGIDHLLNRKpetLSGGEQQRVAIARALVV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1771853535 573 DPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAG 636
Cdd:cd03299 147 NPKILLLDEPFSALDVRTKEKLREELKKirKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVG 212
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1246-1434 |
5.06e-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: 97.08 E-value: 5.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1246 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVL-LKGS--GGGDALE---FLGYCPQENALW--PNLTVRq 1317
Cdd:COG1119 20 DDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrLFGErrGGEDVWElrkRIGLVSPALQLRfpRDETVL- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1318 hlEV-----YAAVkGLRK--GDAEVAITR-LVDALKLQDQLKSPVKTLSEGIKRKlcfVL---SILGNPSVVLLDEPSTG 1386
Cdd:COG1119 99 --DVvlsgfFDSI-GLYRepTDEQRERAReLLELLGLAHLADRPFGTLSQGEQRR---VLiarALVKDPELLILDEPTAG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1771853535 1387 MDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1434
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 ... |
1235-1433 |
5.83e-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: 95.40 E-value: 5.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1235 CFSKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGS--GGGDALEFLGYCPQEnalwpn 1312
Cdd:cd03226 6 SFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKpiKAKERRKSIGYVMQD------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1313 ltVRQHL-------EVYAAVKGLRKGDAEVA-ITRLVDALKLQDQLksPvKTLSEGIKRKLCFVLSILGNPSVVLLDEPS 1384
Cdd:cd03226 80 --VDYQLftdsvreELLLGLKELDAGNEQAEtVLKDLDLYALKERH--P-LSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1771853535 1385 TGMDPEGQQQMWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSG 1433
Cdd:cd03226 155 SGLDYKNMERVGELIR-ELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
419-637 |
6.21e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 97.37 E-value: 6.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYkgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLSKL 498
Cdd:PRK13644 2 IRLENVSYSY---PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 TGVCPQS-NVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIF 577
Cdd:PRK13644 79 VGIVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1771853535 578 LLDEPTAGLDPFSRHQVW-NLLKERKTDRVILFSTQFMDEADIlADRKVFLSQGKLKCAGS 637
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLeRIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGE 218
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1243-1435 |
7.27e-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: 7.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1243 IATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-----SGGGDALEF-LGYCPQENALWPNLTVR 1316
Cdd:COG3845 19 VANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpvriRSPRDAIALgIGMVHQHFMLVPNLTVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1317 QHLeVYAAVKG----LRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQ 1392
Cdd:COG3845 99 ENI-VLGLEPTkggrLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1771853535 1393 QQMWQAIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1435
Cdd:COG3845 178 DELFEILRR-LAAEGKSIIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
419-650 |
9.88e-22 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 98.95 E-value: 9.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYkgkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKlseMADLENLSKL 498
Cdd:PRK11000 4 VTLRNVTKAY----GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKR---MNDVPPAERG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 TGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFL 578
Cdd:PRK11000 77 VGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1771853535 579 LDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGSSLFLkkkwgigYH 650
Cdd:PRK11000 157 LDEPLSNLDAALRVQMRIEISRlhKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL-------YH 223
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1246-1435 |
1.16e-21 |
|
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: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1246 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTA--GQVLLKGSGGgDALEF---LGYCPQENALWPNLTVRQHLE 1320
Cdd:cd03213 26 KNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPL-DKRSFrkiIGYVPQDDILHPTLTVRETLM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1321 VYAAVKGLrkgdaevaitrlvdalklqdqlkspvktlSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIR 1400
Cdd:cd03213 105 FAAKLRGL-----------------------------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLR 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 1771853535 1401 AtFRNTERGALLTTHYM-AEAEAVCDRVAIMVSGRL 1435
Cdd:cd03213 156 R-LADTGRTIICSIHQPsSEIFELFDKLLLLSQGRV 190
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
422-599 |
1.37e-21 |
|
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: 94.23 E-value: 1.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 422 RNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSG--LSVPTKGSVTIYNNKLSemadlENLSKLT 499
Cdd:cd03232 7 KNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLD-----KNFQRST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 500 GVCPQSNVQFDFLTVRENLRLFAKIKGilpqevdkeiqrvllelemkniqdvlaqnLSGGQKRKLTFGIAILGDPQIFLL 579
Cdd:cd03232 82 GYVEQQDVHSPNLTVREALRFSALLRG-----------------------------LSVEQRKRLTIGVELAAKPSILFL 132
|
170 180
....*....|....*....|
gi 1771853535 580 DEPTAGLDPFSRHQVWNLLK 599
Cdd:cd03232 133 DEPTSGLDSQAAYNIVRFLK 152
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
419-671 |
1.40e-21 |
|
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: 100.65 E-value: 1.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLS--VPTKGSVtIYNNKLSEMAD-LENL 495
Cdd:TIGR03269 1 IEVKNLTKKFDGK----EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRI-IYHVALCEKCGyVERP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 496 SKLTGVCPQSNVQF-----DFL----TVRENL---------RLFA---------KIKGILPQ---EVDKEIQRVLLELEM 545
Cdd:TIGR03269 76 SKVGEPCPVCGGTLepeevDFWnlsdKLRRRIrkriaimlqRTFAlygddtvldNVLEALEEigyEGKEAVGRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 546 KNIQDV---LAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADIL 620
Cdd:TIGR03269 156 VQLSHRithIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTSHWPEVIEDL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1771853535 621 ADRKVFLSQGKLKCAGSSLFLKKKWGIGYHLSLQLNEICVEENITSL--VKQH 671
Cdd:TIGR03269 236 SDKAIWLENGEIKEEGTPDEVVAVFMEGVSEVEKECEVEVGEPIIKVrnVSKR 288
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1246-1445 |
1.45e-21 |
|
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: 95.26 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1246 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDALEFL----GYCPQENALWPNLTVRQ 1317
Cdd:cd03261 17 KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGedisGLSEAELYRLrrrmGMLFQSGALFDSLTVFE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1318 HLEVYaavkgLR---KGDAEVaITRLVdALKLQ------DQLKSPVKtLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMD 1388
Cdd:cd03261 97 NVAFP-----LRehtRLSEEE-IREIV-LEKLEavglrgAEDLYPAE-LSGGMKKRVALARALALDPELLLYDEPTAGLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1771853535 1389 PEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLK 1445
Cdd:cd03261 169 PIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELR 225
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1241-1440 |
1.54e-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: 95.00 E-value: 1.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1241 NKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsGGGDALEFLGYCPQEN------ALWPNLT 1314
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILL---DGKDITNLPPHKRPVNtvfqnyALFPHLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1315 VRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQ 1394
Cdd:cd03300 89 VFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1771853535 1395 MWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1440
Cdd:cd03300 169 MQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
409-632 |
1.68e-21 |
|
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: 94.85 E-value: 1.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 409 APPEFQGKeaIRIRNVTKEYKGKPDKiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVtIYNNKLSE 488
Cdd:cd03248 4 APDHLKGI--VKFQNVTFAYPTRPDT-LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQV-LLDGKPIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 489 MADLENLSKLTGVCPQSNVQFDfLTVRENlrlfakIKGILPQEVDKEIQRV-----------LLELEMKNIQDVLAQNLS 557
Cdd:cd03248 80 QYEHKYLHSKVSLVGQEPVLFA-RSLQDN------IAYGLQSCSFECVKEAaqkahahsfisELASGYDTEVGEKGSQLS 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1771853535 558 GGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEADiLADRKVFLSQGKL 632
Cdd:cd03248 153 GGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVE-RADQILVLDGGRI 226
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
419-640 |
1.77e-21 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 95.33 E-value: 1.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYkgkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLSKL 498
Cdd:PRK11614 6 LSFDKVSAHY----GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 TGVCPQSNVQFDFLTVRENLRL---FAKikgilPQEVDKEIQRV---LLELEMKNIQDvlAQNLSGGQKRKLTFGIAILG 572
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLAMggfFAE-----RDQFQERIKWVyelFPRLHERRIQR--AGTMSGGEQQMLAIGRALMS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1771853535 573 DPQIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGK--LKCAGSSLF 640
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPIIIQQIFDTIEQlREQGMTIFLVEQNANQALKLADRGYVLENGHvvLEDTGDALL 225
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
419-637 |
1.85e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 96.34 E-value: 1.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYK-GKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYN---NKLSEMADLEN 494
Cdd:PRK13643 2 IKFEKVNYTYQpNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 495 LSKLTGVC---PQSnvQFDFLTVRENLRLFAKIKGILPQEVDKEIQRvllELEMKNIQDVLAQN----LSGGQKRKLTFG 567
Cdd:PRK13643 82 VRKKVGVVfqfPES--QLFEETVLKDVAFGPQNFGIPKEKAEKIAAE---KLEMVGLADEFWEKspfeLSGGQMRRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1771853535 568 IAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS 637
Cdd:PRK13643 157 GILAMEPEVLVLDEPTAGLDPKARIEMMQLFESiHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGT 227
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
438-587 |
2.33e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 93.79 E-value: 2.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 438 LKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTiYNNKLSEMADLENLSKLTGvcpQSNVQFDFLTVREN 517
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIK-LDGGDIDDPDVAEACHYLG---HRNAMKPALTVAEN 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1771853535 518 LRLFAKIKGILPQEVDKEIQRVllelEMKNIQDVLAQNLSGGQKRKLtfGIAIL---GDPqIFLLDEPTAGLD 587
Cdd:PRK13539 94 LEFWAAFLGGEELDIAAALEAV----GLAPLAHLPFGYLSAGQKRRV--ALARLlvsNRP-IWILDEPTAALD 159
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1246-1441 |
3.35e-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: 3.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1246 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDALEFLgycpQENALWPNLTVRQH--L 1319
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGkqitEPGPDRMVVF----QNYSLLPWLTVRENiaL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1320 EVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDP-------EGQ 1392
Cdd:TIGR01184 78 AVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAltrgnlqEEL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1771853535 1393 QQMWQAIRATfrntergALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSI 1441
Cdd:TIGR01184 158 MQIWEEHRVT-------VLMVTHDVDEALLLSDRVVMLTNGPAANIGQI 199
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
418-630 |
3.40e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 94.77 E-value: 3.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 418 AIRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLsemadlENLSK 497
Cdd:PRK11248 1 MLQISHLYADYGGKP----ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV------EGPGA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 498 LTGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIF 577
Cdd:PRK11248 71 ERGVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1771853535 578 LLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQG 630
Cdd:PRK11248 151 LLDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
419-650 |
4.56e-21 |
|
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: 93.83 E-value: 4.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKgkPDKiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMaDLENLSKL 498
Cdd:cd03253 1 IEFENVTFAYD--PGR-PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREV-TLDSLRRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 TGVCPQSNVQFDfLTVRENLRlFAKikgilPQEVDKEIQRVlleLEMKNIQDVLAQ--------------NLSGGQKRKL 564
Cdd:cd03253 77 IGVVPQDTVLFN-DTIGYNIR-YGR-----PDATDEEVIEA---AKAAQIHDKIMRfpdgydtivgerglKLSGGEKQRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 565 TFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILF-----STqFMDeadilADRKVFLSQGKLKCAGSSL 639
Cdd:cd03253 147 AIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIViahrlST-IVN-----ADKIIVLKDGRIVERGTHE 220
|
250
....*....|.
gi 1771853535 640 FLKKKWGIgYH 650
Cdd:cd03253 221 ELLAKGGL-YA 230
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
419-631 |
6.96e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 96.44 E-value: 6.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLEnlsKL 498
Cdd:PRK11607 20 LEIRNLTKSFDGQH----AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ---RP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 TGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFL 578
Cdd:PRK11607 93 INMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1771853535 579 LDEPTAGLDPFSR----HQVWNLLKERKTDRVILFSTQfmDEADILADRKVFLSQGK 631
Cdd:PRK11607 173 LDEPMGALDKKLRdrmqLEVVDILERVGVTCVMVTHDQ--EEAMTMAGRIAIMNRGK 227
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
450-646 |
7.21e-21 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 96.10 E-value: 7.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 450 ITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLS---KLTGVCPQSNVQFDFLTVRENLRLfaKIKG 526
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLPpekRRIGYVFQDARLFPHYKVRGNLRY--GMAK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 527 ILPQEVDKEIQrvLLELEmkNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLkERKTDRV 606
Cdd:PRK11144 104 SMVAQFDKIVA--LLGIE--PLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYL-ERLAREI 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1771853535 607 ---ILFSTQFMDEADILADRKVFLSQGKLKCAGSslfLKKKWG 646
Cdd:PRK11144 179 nipILYVSHSLDEILRLADRVVVLEQGKVKAFGP---LEEVWA 218
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
419-594 |
8.17e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 93.61 E-value: 8.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADlENLSKL 498
Cdd:COG4604 2 IEIKNVSKRYGGKV----VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPS-RELAKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 TGVCPQSNVQFDFLTVREnLRLFAKI---KGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQkRKLTFgIA--ILGD 573
Cdd:COG4604 77 LAILRQENHINSRLTVRE-LVAFGRFpysKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQ-RQRAF-IAmvLAQD 153
|
170 180
....*....|....*....|.
gi 1771853535 574 PQIFLLDEPTAGLDPfsRHQV 594
Cdd:COG4604 154 TDYVLLDEPLNNLDM--KHSV 172
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
409-632 |
1.04e-20 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 98.25 E-value: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 409 APPEFQGKeaIRIRNVTKEYKGkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSE 488
Cdd:TIGR02203 323 AIERARGD--VEFRNVTFRYPG--RDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLAD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 489 MAdLENLSKLTGVCPQSNVQFDFlTVRENLRLfakikGILPQEVDKEIQRVLlelEMKNIQDVLAQ-------------- 554
Cdd:TIGR02203 399 YT-LASLRRQVALVSQDVVLFND-TIANNIAY-----GRTEQADRAEIERAL---AAAYAQDFVDKlplgldtpigengv 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 555 NLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVW----NLLKERkTDRVILFSTQFMDEadilADRKVFLSQG 630
Cdd:TIGR02203 469 LLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQaaleRLMQGR-TTLVIAHRLSTIEK----ADRIVVMDDG 543
|
..
gi 1771853535 631 KL 632
Cdd:TIGR02203 544 RI 545
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1242-1457 |
1.23e-20 |
|
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: 93.65 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1242 KIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSgggDALEflgycpqENALWpnlTVRQHLE- 1320
Cdd:TIGR04520 15 KPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGL---DTLD-------EENLW---EIRKKVGm 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1321 ---------VYAAVK-----GL--RKGDAEVAITRLVDALK---LQDQLKSPVKTLSEGIKRKLCfVLSILG-NPSVVLL 1380
Cdd:TIGR04520 82 vfqnpdnqfVGATVEddvafGLenLGVPREEMRKRVDEALKlvgMEDFRDREPHLLSGGQKQRVA-IAGVLAmRPDIIIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1381 DEPsTGM-DPEGQQQMWQAIRATfrNTERGA--LLTTHYMAEAeAVCDRVAIMVSGRLRCIGSIQHLKSKfgKDYLLEMK 1457
Cdd:TIGR04520 161 DEA-TSMlDPKGRKEVLETIRKL--NKEEGItvISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIFSQ--VELLKEIG 234
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
435-632 |
1.47e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 93.05 E-value: 1.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 435 IEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGL-----SVPTKGSVTIYNNKLSEMaDLENLSKLTGVCPQSNVQF 509
Cdd:PRK14247 16 VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKM-DVIELRRRVQMVFQIPNPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 510 DFLTVRENLRL------FAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPT 583
Cdd:PRK14247 95 PNLSIFENVALglklnrLVKSKKELQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPT 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1771853535 584 AGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEADILADRKVFLSQGKL 632
Cdd:PRK14247 175 ANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
419-636 |
1.66e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 97.16 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGkpdkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIyNNKLSEMADLENLSKL 498
Cdd:PRK09700 6 ISMAGIGKSFGP----VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITI-NNINYNKLDHKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 -TGVCPQSNVQFDFLTVRENL---RLFAK----IKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAI 570
Cdd:PRK09700 81 gIGIIYQELSVIDELTVLENLyigRHLTKkvcgVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1771853535 571 LGDPQIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAG 636
Cdd:PRK09700 161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQlRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
418-637 |
1.96e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 94.77 E-value: 1.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 418 AIRIRNVTKEYkgkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLEnlsK 497
Cdd:PRK10851 2 SIEIANIKKSF----GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD---R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 498 LTGVCPQSNVQFDFLTVRENLRLFAKikgILPQ-------EVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAI 570
Cdd:PRK10851 75 KVGFVFQHYALFRHMTVFDNIAFGLT---VLPRrerpnaaAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1771853535 571 LGDPQIFLLDEPTAGLDPFSRHQV--W--NLLKERKTDRVilFSTQFMDEADILADRKVFLSQGKLKCAGS 637
Cdd:PRK10851 152 AVEPQILLLDEPFGALDAQVRKELrrWlrQLHEELKFTSV--FVTHDQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
419-637 |
2.29e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 92.38 E-value: 2.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLEnLSKL 498
Cdd:PRK11231 3 LRTENLTVGYGTKR----ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ-LARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 TGVCPQSNVQFDFLTVRE--------NLRLFakikGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAI 570
Cdd:PRK11231 78 LALLPQHHLTPEGITVRElvaygrspWLSLW----GRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1771853535 571 LGDPQIFLLDEPTAGLDpfSRHQV--WNLLKER----KTDRVILFStqfMDEADILADRKVFLSQGKLKCAGS 637
Cdd:PRK11231 154 AQDTPVVLLDEPTTYLD--INHQVelMRLMRELntqgKTVVTVLHD---LNQASRYCDHLVVLANGHVMAQGT 221
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1246-1454 |
2.37e-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: 97.60 E-value: 2.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1246 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsGGGDALEF--------LGYCPQENALWP-----N 1312
Cdd:COG2274 492 DNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILI---DGIDLRQIdpaslrrqIGVVLQDVFLFSgtireN 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1313 LTVrqhlevyaavkglrkGDAEVAITRLVDALK----------LQDQLKSPV----KTLSEGIKRKLCFVLSILGNPSVV 1378
Cdd:COG2274 569 ITL---------------GDPDATDEEIIEAARlaglhdfieaLPMGYDTVVgeggSNLSGGQRQRLAIARALLRNPRIL 633
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1771853535 1379 LLDEPSTGMDPEGQQQMWQAIRATFRNteRGALLTTHYMAEAEAvCDRVAIMVSGRLRCIGSIQHLKSKFGKDYLL 1454
Cdd:COG2274 634 ILDEATSALDAETEAIILENLRRLLKG--RTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEELLARKGLYAEL 706
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1218-1440 |
2.78e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 91.88 E-value: 2.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1218 VIIASCLRKEYAGKRkgcfskrknkiATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSG----- 1292
Cdd:PRK10895 3 TLTAKNLAKAYKGRR-----------VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDisllp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1293 -GGDALEFLGYCPQENALWPNLTVRQHL-EVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLS 1370
Cdd:PRK10895 72 lHARARRGIGYLPQEASIFRRLSVYDNLmAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1371 ILGNPSVVLLDEPSTGMDPEGQQQMWQAIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1440
Cdd:PRK10895 152 LAANPKFILLDEPFAGVDPISVIDIKRIIEH-LRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1215-1439 |
3.10e-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: 3.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1215 EKPVIIASCLRKEYAGKRKGCFSkrknkiATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLK----- 1289
Cdd:TIGR03269 276 GEPIIKVRNVSKRYISVDRGVVK------AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgdew 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1290 -------GSGGGDALEFLGYCPQENALWPNLTVrqhLEVYAAVKGLRKGDaEVAITRLVDALKL----QDQLKSPVK--- 1355
Cdd:TIGR03269 350 vdmtkpgPDGRGRAKRYIGILHQEYDLYPHRTV---LDNLTEAIGLELPD-ELARMKAVITLKMvgfdEEKAEEILDkyp 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1356 -TLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1434
Cdd:TIGR03269 426 dELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGK 505
|
....*
gi 1771853535 1435 LRCIG 1439
Cdd:TIGR03269 506 IVKIG 510
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
416-632 |
3.38e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 91.83 E-value: 3.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 416 KEAIRIRNVTKEYKGKpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGL-----SVPTKGSVTIYN-NKLSEM 489
Cdd:PRK14267 2 KFAIETVNLRVYYGSN----HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGrNIYSPD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 490 ADLENLSKLTGVCPQSNVQFDFLTVRENLRLFAKIKGI------LPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRK 563
Cdd:PRK14267 78 VDPIEVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLvkskkeLDERVEWALKKAALWDEVKDRLNDYPSNLSGGQRQR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1771853535 564 LTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEADILADRKVFLSQGKL 632
Cdd:PRK14267 158 LVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1244-1435 |
4.32e-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: 4.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1244 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsGGGDALEF--------LGYCPQENALWpNLTV 1315
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLL---DGTDIRQLdpadlrrnIGYVPQDVTLF-YGTL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1316 RQHLEVyaavkglrkGDAEVAITRLVDALKLQ--DQL--KSPV----------KTLSEGIKRKLCFVLSILGNPSVVLLD 1381
Cdd:cd03245 95 RDNITL---------GAPLADDERILRAAELAgvTDFvnKHPNgldlqigergRGLSGGQRQAVALARALLNDPPILLLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1771853535 1382 EPSTGMDPEGQQQMWQAIRATFRntERGALLTTHYMAeAEAVCDRVAIMVSGRL 1435
Cdd:cd03245 166 EPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPS-LLDLVDRIIVMDSGRI 216
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1244-1447 |
4.90e-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: 95.98 E-value: 4.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1244 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsGGGDALEF--------LGYCPQeNALWPNLTV 1315
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILI---NGVDLSDLdpaswrrqIAWVPQ-NPYLFAGTI 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1316 RQHL----------EVYAAVKglrkgdaEVAITRLVDAlkLQDQLKSPV----KTLSEGIKRKLCFVLSILGNPSVVLLD 1381
Cdd:COG4988 428 RENLrlgrpdasdeELEAALE-------AAGLDEFVAA--LPDGLDTPLgeggRGLSGGQAQRLALARALLRDAPLLLLD 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1771853535 1382 EPSTGMDPEGQQQMWQAIRATFRNteRGALLTTHYMAEAEAvCDRVAIMVSGRLRCIGSIQHLKSK 1447
Cdd:COG4988 499 EPTAHLDAETEAEILQALRRLAKG--RTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
419-651 |
5.01e-20 |
|
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: 91.01 E-value: 5.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSeMADLENLSKL 498
Cdd:cd03252 1 ITFEHVRFRYK--PDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLA-LADPAWLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 TGVCPQSNVQFDfLTVRENLRLfakikgilpQEVDKEIQRVLLELEMKNIQDVLAQ--------------NLSGGQKRKL 564
Cdd:cd03252 78 VGVVLQENVLFN-RSIRDNIAL---------ADPGMSMERVIEAAKLAGAHDFISElpegydtivgeqgaGLSGGQRQRI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 565 TFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQFMdEADILADRKVFLSQGKLKCAGSSLFLKKK 644
Cdd:cd03252 148 AIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHDELLAE 226
|
....*..
gi 1771853535 645 WGIGYHL 651
Cdd:cd03252 227 NGLYAYL 233
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1230-1435 |
5.35e-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: 90.41 E-value: 5.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1230 GKRKGCF-SKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITG---DTKPTAGQVLLKGSgGGDALEFL---GY 1302
Cdd:cd03234 7 WDVGLKAkNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQ-PRKPDQFQkcvAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1303 CPQENALWPNLTVRQHLeVYAAVKGLRKGDAEVAITRLVDALKLQD----QLKSP-VKTLSEGIKRKLCFVLSILGNPSV 1377
Cdd:cd03234 86 VRQDDILLPGLTVRETL-TYTAILRLPRKSSDAIRKKRVEDVLLRDlaltRIGGNlVKGISGGERRRVSIAVQLLWDPKV 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1771853535 1378 VLLDEPSTGMDPEGQQQMWQAIRATFRnTERGALLTTHY-MAEAEAVCDRVAIMVSGRL 1435
Cdd:cd03234 165 LILDEPTSGLDSFTALNLVSTLSQLAR-RNRIVILTIHQpRSDLFRLFDRILLLSSGEI 222
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
433-588 |
7.04e-20 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 89.34 E-value: 7.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 433 DKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADL--EN---LSKLTGVCPQsnv 507
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEphENilyLGHLPGLKPE--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 508 qfdfLTVRENLRLFAKIKGilpqEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLD 587
Cdd:TIGR01189 88 ----LSALENLHFWAAIHG----GAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
.
gi 1771853535 588 P 588
Cdd:TIGR01189 160 K 160
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
443-617 |
7.30e-20 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 96.73 E-value: 7.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 443 FDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLsemaDLENLS--KLTGVCPQSnvqfdF-----LTVR 515
Cdd:NF033858 287 FRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV----DAGDIAtrRRVGYMSQA-----FslygeLTVR 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 516 ENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVW 595
Cdd:NF033858 358 QNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFW 437
|
170 180
....*....|....*....|....*
gi 1771853535 596 NLLKE--RKtDRVILF-STQFMDEA 617
Cdd:NF033858 438 RLLIElsRE-DGVTIFiSTHFMNEA 461
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
419-607 |
8.74e-20 |
|
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: 88.43 E-value: 8.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEmADLENLSKL 498
Cdd:cd03246 1 LEVENVSFRYPG--AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQ-WDPNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 TGVCPQsnvqfdfltvreNLRLFAkikgilpqevdkeiqrvllelemkniqDVLAQN-LSGGQKRKLTFGIAILGDPQIF 577
Cdd:cd03246 78 VGYLPQ------------DDELFS---------------------------GSIAENiLSGGQRQRLGLARALYGNPRIL 118
|
170 180 190
....*....|....*....|....*....|...
gi 1771853535 578 LLDEPTAGLDPFSRHQVWNL---LKERKTDRVI 607
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAiaaLKAAGATRIV 151
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
418-632 |
1.08e-19 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 90.19 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 418 AIRIRNVTKEYKGKpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTI------YNNKLSEMAD 491
Cdd:PRK11264 3 AIEVKNLVKKFHGQ----TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidTARSLSQQKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 492 L-ENLSKLTGVCPQSNVQFDFLTVRENLRLFAKI-KGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIA 569
Cdd:PRK11264 79 LiRQLRQHVGFVFQNFNLFPHRTVLENIIEGPVIvKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1771853535 570 ILGDPQIFLLDEPTAGLDPFSRHQVWNL---LKERKTDRVILfsTQFMDEADILADRKVFLSQGKL 632
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPELVGEVLNTirqLAQEKRTMVIV--THEMSFARDVADRAIFMDQGRI 222
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
418-627 |
1.18e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 90.48 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 418 AIRIRNVTKEYkgkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLS-----VPTKGSVTIYNNKLSEM-AD 491
Cdd:PRK14258 7 AIKVNNLSFYY----DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNeleseVRVEGRVEFFNQNIYERrVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 492 LENLSK-LTGVCPQSNVqFDfLTVRENLRLFAKIKGILPQ-EVDKEIQRVL----LELEMKNIQDVLAQNLSGGQKRKLT 565
Cdd:PRK14258 83 LNRLRRqVSMVHPKPNL-FP-MSVYDNVAYGVKIVGWRPKlEIDDIVESALkdadLWDEIKHKIHKSALDLSGGQQQRLC 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1771853535 566 FGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKER--KTDRVILFSTQFMDEADILADRKVFL 627
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrlRSELTMVIVSHNLHQVSRLSDFTAFF 224
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
422-600 |
1.49e-19 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 89.49 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 422 RNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEM-----ADLENlS 496
Cdd:PRK11629 9 DNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaakAELRN-Q 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 497 KLTGVCPQSNVQFDFlTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQI 576
Cdd:PRK11629 88 KLGFIYQFHHLLPDF-TALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRL 166
|
170 180
....*....|....*....|....
gi 1771853535 577 FLLDEPTAGLDPFSRHQVWNLLKE 600
Cdd:PRK11629 167 VLADEPTGNLDARNADSIFQLLGE 190
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
396-651 |
2.39e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 94.40 E-value: 2.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 396 MDADPSFHDSFEQAPPEFQGKeaIRIRNVTKEYKGKPDKiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPT 475
Cdd:TIGR00958 458 LDRKPNIPLTGTLAPLNLEGL--IEFQDVSFSYPNRPDV-PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPT 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 476 KGSVTIYNNKLSEMaDLENLSKLTGVCPQSNVQFDfLTVRENlrlfakIKGILPQEVDKEIQRVLLE-------LEMKNI 548
Cdd:TIGR00958 535 GGQVLLDGVPLVQY-DHHYLHRQVALVGQEPVLFS-GSVREN------IAYGLTDTPDEEIMAAAKAanahdfiMEFPNG 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 549 QDVL----AQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNlLKERKtDRVILFSTQFMDEADiLADRK 624
Cdd:TIGR00958 607 YDTEvgekGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE-SRSRA-SRTVLLIAHRLSTVE-RADQI 683
|
250 260
....*....|....*....|....*..
gi 1771853535 625 VFLSQGKLKCAGSSLFLKKKWGIGYHL 651
Cdd:TIGR00958 684 LVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1244-1440 |
2.51e-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: 2.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1244 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsGGGDALEF------LGYCPQENALWPNLTVRQ 1317
Cdd:cd03296 17 ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILF---GGEDATDVpvqernVGFVFQHYALFRHMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1318 HLEVYAAVKGLRKGDAEVAITRLVDAL-------KLQDQLKSpvkTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1390
Cdd:cd03296 94 NVAFGLRVKPRSERPPEAEIRAKVHELlklvqldWLADRYPA---QLSGGQRQRVALARALAVEPKVLLLDEPFGALDAK 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1391 GQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1440
Cdd:cd03296 171 VRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1215-1439 |
2.54e-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: 89.63 E-value: 2.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1215 EKPVIIASCLRKEYAGKRKGCFskrknkIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsGGG 1294
Cdd:cd03294 16 KAFKLLAKGKSKEEILKKTGQT------VGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLI---DGQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1295 DALEF------------LGYCPQENALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIK 1362
Cdd:cd03294 87 DIAAMsrkelrelrrkkISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQ 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1771853535 1363 RKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1439
Cdd:cd03294 167 QRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVG 243
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
418-637 |
2.84e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 93.74 E-value: 2.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 418 AIRIRNVTKEYKGKPDKieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADlENLSK 497
Cdd:PRK11160 338 SLTLNNVSFTYPDQPQP--VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSE-AALRQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 498 LTGVCPQSnVQFDFLTVRENLRLfAKikgilPQEVDKEIQRVLLELEMKNiqdvLAQN--------------LSGGQKRK 563
Cdd:PRK11160 415 AISVVSQR-VHLFSATLRDNLLL-AA-----PNASDEALIEVLQQVGLEK----LLEDdkglnawlgeggrqLSGGEQRR 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 564 LTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFST-------QFmdeadilaDRKVFLSQGKLKCAG 636
Cdd:PRK11160 484 LGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMIThrltgleQF--------DRICVMDNGQIIEQG 555
|
.
gi 1771853535 637 S 637
Cdd:PRK11160 556 T 556
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
419-637 |
3.67e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 89.41 E-value: 3.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKPDKIEaLKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLSKL 498
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYT-LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 TGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFL 578
Cdd:PRK13650 84 GMVFQNPDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1771853535 579 LDEPTAGLDPFSRHQVWNLLKERKTDR--VILFSTQFMDEAdILADRKVFLSQGKLKCAGS 637
Cdd:PRK13650 164 LDEATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDEV-ALSDRVLVMKNGQVESTST 223
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1246-1434 |
3.98e-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: 86.28 E-value: 3.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1246 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsGGGDALEF--------LGYCPQENALWpNLTVRQ 1317
Cdd:cd03228 19 KDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILI---DGVDLRDLdleslrknIAYVPQDPFLF-SGTIRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1318 HLevyaavkglrkgdaevaitrlvdalklqdqlkspvktLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQ 1397
Cdd:cd03228 95 NI-------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILE 137
|
170 180 190
....*....|....*....|....*....|....*..
gi 1771853535 1398 AIRATFRNteRGALLTTHYMAEAEAvCDRVAIMVSGR 1434
Cdd:cd03228 138 ALRALAKG--KTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
418-623 |
5.20e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 92.39 E-value: 5.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 418 AIRIRNVTKEYKGkpdkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLSK 497
Cdd:COG1129 4 LLEMRGISKSFGG----VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 498 LTGVCPQSNVQFDFLTVRENLRL--FAKIKGIL-PQEVDKEIQRVLLELEMkNIQ-DVLAQNLSGGQK------Rkltfg 567
Cdd:COG1129 80 GIAIIHQELNLVPNLSVAENIFLgrEPRRGGLIdWRAMRRRARELLARLGL-DIDpDTPVGDLSVAQQqlveiaR----- 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1771853535 568 iAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRV-ILFSTQFMDEADILADR 623
Cdd:COG1129 154 -ALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVaIIYISHRLDEVFEIADR 209
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
419-609 |
5.24e-19 |
|
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: 89.73 E-value: 5.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGL---SVPTKGSVTIYNNKLSEMADlENL 495
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLlppPGITSGEILFDGEDLLKLSE-KEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 496 SKLTGvcpqSNVQFDF----------LTVRENLRLFAKIKGILP-QEVDKEIQRVLLELEMKNIQDVLAQ---NLSGGQK 561
Cdd:COG0444 81 RKIRG----REIQMIFqdpmtslnpvMTVGDQIAEPLRIHGGLSkAEARERAIELLERVGLPDPERRLDRyphELSGGMR 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1771853535 562 RKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILF 609
Cdd:COG0444 157 QRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDlqRELGLAILF 206
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
406-632 |
5.56e-19 |
|
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: 92.56 E-value: 5.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 406 FEQAPPEFQGKEAIRIRNVTKEY----KGKpdkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTI 481
Cdd:TIGR03269 267 VEKECEVEVGEPIIKVRNVSKRYisvdRGV---VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNV 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 482 -YNNKLSEMADLENL-----SKLTGVCPQSNVQFDFLTVRENLrlfAKIKGI-LPQEVDKEIQRVLL------ELEMKNI 548
Cdd:TIGR03269 344 rVGDEWVDMTKPGPDgrgraKRYIGILHQEYDLYPHRTVLDNL---TEAIGLeLPDELARMKAVITLkmvgfdEEKAEEI 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 549 QDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWN-LLKERKT-DRVILFSTQFMDEADILADRKVF 626
Cdd:TIGR03269 421 LDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHsILKAREEmEQTFIIVSHDMDFVLDVCDRAAL 500
|
....*.
gi 1771853535 627 LSQGKL 632
Cdd:TIGR03269 501 MRDGKI 506
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
409-637 |
6.12e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 89.91 E-value: 6.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 409 APPEFQGKEAIRIRNVTKEYKGK-PDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVT---IYNN 484
Cdd:PRK13631 12 VPNPLSDDIILRVKNLYCVFDEKqENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQvgdIYIG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 485 ------------KLSEMADLENLSKLTGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLElEMKNIQDVL 552
Cdd:PRK13631 92 dkknnhelitnpYSKKIKNFKELRRRVSMVFQFPEYQLFKDTIEKDIMFGPVALGVKKSEAKKLAKFYLN-KMGLDDSYL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 553 AQN---LSGGQKRKltfgIAILG----DPQIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRK 624
Cdd:PRK13631 171 ERSpfgLSGGQKRR----VAIAGilaiQPEILIFDEPTAGLDPKGEHEMMQLILDaKANNKTVFVITHTMEHVLEVADEV 246
|
250
....*....|...
gi 1771853535 625 VFLSQGKLKCAGS 637
Cdd:PRK13631 247 IVMDKGKILKTGT 259
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
428-627 |
6.66e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 86.13 E-value: 6.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 428 YKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKlsEMADLENLSKLTGVCPqsnv 507
Cdd:NF040873 2 YGGRP----VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA--RVAYVPQRSEVPDSLP---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 508 qfdfLTVRE--NLRLFAKIKGILP------QEVDKEIQRV-LLELEMKNIQDvlaqnLSGGQKRKLTFGIAILGDPQIFL 578
Cdd:NF040873 72 ----LTVRDlvAMGRWARRGLWRRltrddrAAVDDALERVgLADLAGRQLGE-----LSGGQRQRALLAQGLAQEADLLL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1771853535 579 LDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEAdILADRKVFL 627
Cdd:NF040873 143 LDEPTTGLDAESRERIIALLAEeHARGATVVVVTHDLELV-RRADPCVLL 191
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
415-638 |
9.26e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 87.80 E-value: 9.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 415 GKEAIRIRNVTKEYKGKPDKiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGL------SVPTKGSVTIYNNKLSE 488
Cdd:PRK14246 4 GKSAEDVFNISRLYLYINDK-AILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydsKIKVDGKVLYFGKDIFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 489 MaDLENLSKLTGVCPQSNVQFDFLTVRENLRLFAKIKGILPQ-EVDKEIQRVLLELEM-KNIQDVL---AQNLSGGQKRK 563
Cdd:PRK14246 83 I-DAIKLRKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKrEIKKIVEECLRKVGLwKEVYDRLnspASQLSGGQQQR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1771853535 564 LTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGSS 638
Cdd:PRK14246 162 LTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSS 236
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1244-1469 |
9.29e-19 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 89.79 E-value: 9.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1244 ATRNVSFCVRKGEVLGLLGHNGAGKSTSiKVITGDTKPTAGQvllkgsgggDALEFLGYCPQENALW------------- 1310
Cdd:NF000106 28 AVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGR---------RPWRF*TWCANRRALRrtig*hrpvr*gr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1311 -PNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDP 1389
Cdd:NF000106 98 rESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1390 EGQQQMWQAIRATFRNTERgALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFGKDYLlemkvknlaQVEPLHA 1469
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 ... |
1246-1435 |
9.59e-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: 86.43 E-value: 9.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1246 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG---SGGGDALEFL----GYCPQENALWPNLTVRQH 1318
Cdd:cd03262 17 KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGlklTDDKKNINELrqkvGMVFQQFNLFPHLTVLEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1319 L-EVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEG------IKRKLCFvlsilgNPSVVLLDEPSTGMDPEG 1391
Cdd:cd03262 97 ItLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGqqqrvaIARALAM------NPKVMLFDEPTSALDPEL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1771853535 1392 QQQMWQAIRatfRNTERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1435
Cdd:cd03262 171 VGEVLDVMK---DLAEEGMtmVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
453-638 |
1.08e-18 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 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. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 89.09 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 453 ILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADlENLSklTGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEV 532
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPP-HLRH--INMVFQSYALFPHMTVEENVAFGLKMRKVPRAEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 533 DkeiQRVLLELEMKNIQDVLAQ---NLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLK--ERKTDRVI 607
Cdd:TIGR01187 78 K---PRVLEALRLVQLEEFADRkphQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKtiQEQLGITF 154
|
170 180 190
....*....|....*....|....*....|.
gi 1771853535 608 LFSTQFMDEADILADRKVFLSQGKLKCAGSS 638
Cdd:TIGR01187 155 VFVTHDQEEAMTMSDRIAIMRKGKIAQIGTP 185
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1246-1440 |
1.20e-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: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1246 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsGGGDALEF------LGYCPQENALWPNLTVRQHL 1319
Cdd:COG3839 20 KDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILI---GGRDVTDLppkdrnIAMVFQSYALYPHMTVYENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1320 EVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEG------IKRklcfvlSILGNPSVVLLDEPSTGMDPEGQQ 1393
Cdd:COG3839 97 AFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGqrqrvaLGR------ALVREPKVFLLDEPLSNLDAKLRV 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1771853535 1394 QMWQAIRATFRntERGA--LLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1440
Cdd:COG3839 171 EMRAEIKRLHR--RLGTttIYVTHDQVEAMTLADRIAVMNDGRIQQVGT 217
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
419-632 |
1.29e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 88.60 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEY-KGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVT-IYNN-------KLSEM 489
Cdd:PRK13651 3 IKVKNIVKIFnKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwIFKDeknkkktKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 490 ADLENLSKLT---------GVCPQSNVQFDFL-------TVRENLRLFAKIKGILPQEVDKeiqRVLLELEMKNIQDVLA 553
Cdd:PRK13651 83 VLEKLVIQKTrfkkikkikEIRRRVGVVFQFAeyqlfeqTIEKDIIFGPVSMGVSKEEAKK---RAAKYIELVGLDESYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 554 Q----NLSGGQKRKltfgIAILG----DPQIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRK 624
Cdd:PRK13651 160 QrspfELSGGQKRR----VALAGilamEPDFLVFDEPTAGLDPQGVKEILEIFDNlNKQGKTIILVTHDLDNVLEWTKRT 235
|
....*...
gi 1771853535 625 VFLSQGKL 632
Cdd:PRK13651 236 IFFKDGKI 243
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
418-630 |
1.49e-18 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 89.13 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 418 AIRIRNVTKEYKGKpdkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYN---NKLsEMADlen 494
Cdd:PRK11650 3 GLKLQAVRKSYDGK---TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGrvvNEL-EPAD--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 495 lskltgvcpqSNVQFDF--------LTVRENLRLFAKIKGILPQEVDKEIQRV--LLELEmkniqDVLA---QNLSGGQK 561
Cdd:PRK11650 76 ----------RDIAMVFqnyalyphMSVRENMAYGLKIRGMPKAEIEERVAEAarILELE-----PLLDrkpRELSGGQR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1771853535 562 RKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVwnLLKERKTDRVI----LFSTQFMDEADILADRKVFLSQG 630
Cdd:PRK11650 141 QRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQM--RLEIQRLHRRLkttsLYVTHDQVEAMTLADRVVVMNGG 211
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
419-631 |
1.56e-18 |
|
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: 83.65 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNklsemadlenlskl 498
Cdd:cd03221 1 IELENLSKTYGGKL----LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST-------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 tgvcpqsnvqfdfltvrenlrlfAKIkGILPQevdkeiqrvllelemkniqdvlaqnLSGGQKRKLTFGIAILGDPQIFL 578
Cdd:cd03221 63 -----------------------VKI-GYFEQ-------------------------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1771853535 579 LDEPTAGLDPFSRHQVWNLLKE-RKTdrVILFS--TQFMDEadiLADRKVFLSQGK 631
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKEyPGT--VILVShdRYFLDQ---VATKIIELEDGK 144
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
437-628 |
1.63e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 87.14 E-value: 1.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 437 ALKDLVFDIYEGQITAILGHSGAGKSTLL---NILSGL--SVPTKGSVTIYNNKL-SEMADLENLSKLTGVCPQSNVQFD 510
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILrcfNRLNDLipGFRVEGKVTFHGKNLyAPDVDPVEVRRRIGMVFQKPNPFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 511 fLTVRENLRLFAKI---KGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLD 587
Cdd:PRK14243 105 -KSIYDNIAYGARIngyKGDMDELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALD 183
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1771853535 588 PFSRHQVWNLLKERKTDRVILFSTQFMDEADILADRKVFLS 628
Cdd:PRK14243 184 PISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFN 224
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1242-1435 |
1.83e-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: 1.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1242 KIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-----SGGGDALEF-LGYCP---QENALWPN 1312
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGkpvtrRSPRDAIRAgIAYVPedrKREGLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1313 LTVRQHLevyaavkglrkgdaevAITRLvdalklqdqlkspvktLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQ 1392
Cdd:cd03215 93 LSVAENI----------------ALSSL----------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1771853535 1393 QQMWQAIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1435
Cdd:cd03215 141 AEIYRLIRE-LADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1216-1383 |
2.71e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.12 E-value: 2.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1216 KPVIIASCLRKEYAGKrkgcfskrknKIAtRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsggGD 1295
Cdd:COG0488 313 KKVLELEGLSKSYGDK----------TLL-DDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-----GE 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1296 ALEfLGYCPQENA-LWPNLTVRQHLevyaavKGLRKGDAEVAITRLVDALKL-QDQLKSPVKTLSEGIKRKLCFVLSILG 1373
Cdd:COG0488 377 TVK-IGYFDQHQEeLDPDKTVLDEL------RDGAPGGTEQEVRGYLGRFLFsGDDAFKPVGVLSGGEKARLALAKLLLS 449
|
170
....*....|
gi 1771853535 1374 NPSVVLLDEP 1383
Cdd:COG0488 450 PPNVLLLDEP 459
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1238-1442 |
2.76e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 86.36 E-value: 2.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1238 KRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGD--ALEF---LGYCPQENALWPN 1312
Cdd:PRK13548 11 RLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwsPAELarrRAVLPQHSSLSFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1313 LTVRQHLEVYAAVKGLRKGDAEVAIT---RLVDALKLQDqlkSPVKTLSEGIK------RKLCFVLSILGNPSVVLLDEP 1383
Cdd:PRK13548 91 FTVEEVVAMGRAPHGLSRAEDDALVAaalAQVDLAHLAG---RDYPQLSGGEQqrvqlaRVLAQLWEPDGPPRWLLLDEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1771853535 1384 STGMDPEGQQQMWQAIRAtfRNTERGA--------L-LTTHYmaeaeavCDRVAIMVSGRLRCIGSIQ 1442
Cdd:PRK13548 168 TSALDLAHQHHVLRLARQ--LAHERGLavivvlhdLnLAARY-------ADRIVLLHQGRLVADGTPA 226
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
420-623 |
3.04e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 89.97 E-value: 3.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 420 RIRNVTKEYKGkpdkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKL---SEMADLEnls 496
Cdd:PRK11288 6 SFDGIGKTFPG----VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfaSTTAALA--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 497 klTGVC---------PQsnvqfdfLTVRENLRLfakikGILPQE---VDKE--IQRVLLELE---MKNIQDVLAQNLSGG 559
Cdd:PRK11288 79 --AGVAiiyqelhlvPE-------MTVAENLYL-----GQLPHKggiVNRRllNYEAREQLEhlgVDIDPDTPLKYLSIG 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1771853535 560 QKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADR 623
Cdd:PRK11288 145 QRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRElRAEGRVILYVSHRMEEIFALCDA 209
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
418-632 |
3.11e-18 |
|
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: 85.56 E-value: 3.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 418 AIRIRNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMaDLENLSK 497
Cdd:COG4181 8 IIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAL-DEDARAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 498 LTGvcpqSNVQFDF--------LTVRENlrlfakikgilpqevdkeiqrVLLELEMKNIQDVLAQ--------------- 554
Cdd:COG4181 87 LRA----RHVGFVFqsfqllptLTALEN---------------------VMLPLELAGRRDARARarallervglghrld 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 555 ----NLSGG-QKRkltfgIAI----LGDPQIFLLDEPTAGLDPFSRHQVWNLL----KERKTDRVILfsTQfmDEAdiLA 621
Cdd:COG4181 142 hypaQLSGGeQQR-----VALarafATEPAILFADEPTGNLDAATGEQIIDLLfelnRERGTTLVLV--TH--DPA--LA 210
|
250
....*....|....
gi 1771853535 622 ---DRKVFLSQGKL 632
Cdd:COG4181 211 arcDRVLRLRAGRL 224
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
419-640 |
3.45e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 86.69 E-value: 3.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKPDkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEmADLENLSKL 498
Cdd:PRK13642 5 LEVENLVFKYEKESD-VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTA-ENVWNLRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 TGVCPQS-NVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIF 577
Cdd:PRK13642 83 IGMVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1771853535 578 LLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEAdILADRKVFLSQGKL--KCAGSSLF 640
Cdd:PRK13642 163 ILDESTSMLDPTGRQEIMRVIHEikEKYQLTVLSITHDLDEA-ASSDRILVMKAGEIikEAAPSELF 228
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
392-633 |
5.29e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.35 E-value: 5.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 392 LEDEMDADPSFHDSFEQAPPefQGKEAIRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGL 471
Cdd:COG0488 291 REEPPRRDKTVEIRFPPPER--LGKKVLELEGLSKSYGDKT----LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 472 SVPTKGSVTIYnnklsemadlENLSklTGVCPQSNVQFDF-LTVRENLRLFA------KIKGIL------PQEVDKEIQR 538
Cdd:COG0488 365 LEPDSGTVKLG----------ETVK--IGYFDQHQEELDPdKTVLDELRDGApggteqEVRGYLgrflfsGDDAFKPVGV 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 539 vllelemkniqdvlaqnLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERK-TdrVILFS--TQFMD 615
Cdd:COG0488 433 -----------------LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPgT--VLLVShdRYFLD 493
|
250
....*....|....*...
gi 1771853535 616 EadiLADRKVFLSQGKLK 633
Cdd:COG0488 494 R---VATRILEFEDGGVR 508
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
415-632 |
5.38e-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: 83.25 E-value: 5.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 415 GKEAIRIRNVTKEYkgkpdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSemadlen 494
Cdd:cd03215 1 GEPVLEVRGLSVKG--------AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVT------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 495 lskltgvcpqsnvqfdFLTVRENLRLfakikGI--LPqevdKEIQRVLLELEM---KNIqdVLAQNLSGGQKRKLTFGIA 569
Cdd:cd03215 66 ----------------RRSPRDAIRA-----GIayVP----EDRKREGLVLDLsvaENI--ALSSLLSGGNQQKVVLARW 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1771853535 570 ILGDPQIFLLDEPTAGLDPFSRHQVWNLLKErKTDR---VILFSTQfMDEADILADRKVFLSQGKL 632
Cdd:cd03215 119 LARDPRVLILDEPTRGVDVGAKAEIYRLIRE-LADAgkaVLLISSE-LDELLGLCDRILVMYEGRI 182
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1246-1435 |
5.83e-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: 5.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1246 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDAL-EFLGYCPQENALWPNlTVRQHLe 1320
Cdd:cd03246 19 RNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGadisQWDPNELgDHVGYLPQDDELFSG-SIAENI- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1321 vyaavkglrkgdaevaitrlvdalklqdqlkspvktLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIR 1400
Cdd:cd03246 97 ------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIA 140
|
170 180 190
....*....|....*....|....*....|....*..
gi 1771853535 1401 ATfrnTERGA--LLTTHYMaEAEAVCDRVAIMVSGRL 1435
Cdd:cd03246 141 AL---KAAGAtrIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1244-1453 |
6.62e-18 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 87.58 E-value: 6.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1244 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGggdalefLGYCP----------QENALWPNL 1313
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVD-------LSHVPpyqrpinmmfQSYALFPHM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1314 TVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQ 1393
Cdd:PRK11607 107 TVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1771853535 1394 QMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS----IQHLKSKFGKDYL 1453
Cdd:PRK11607 187 RMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEpeeiYEHPTTRYSAEFI 250
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
422-630 |
1.07e-17 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 89.78 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 422 RNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSG---LSVPTKGSVTIYNNKLSemadlENLSKL 498
Cdd:TIGR00956 763 RNLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAErvtTGVITGGDRLVNGRPLD-----SSFQRS 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 TGVCPQSNVQFDFLTVRENLRLFAKIKgiLPQEVDKE-----IQRVLLELEMKNIQD----VLAQNLSGGQKRKLTFGIA 569
Cdd:TIGR00956 838 IGYVQQQDLHLPTSTVRESLRFSAYLR--QPKSVSKSekmeyVEEVIKLLEMESYADavvgVPGEGLNVEQRKRLTIGVE 915
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1771853535 570 ILGDPQIFL-LDEPTAGLDPFSRHQVWNLLKE-RKTDRVILfSTQFMDEADILA--DRKVFLSQG 630
Cdd:TIGR00956 916 LVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKlADHGQAIL-CTIHQPSAILFEefDRLLLLQKG 979
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
419-637 |
1.34e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 84.85 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKpdkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEmADLENLSKL 498
Cdd:PRK13652 4 IETRDLCYSYSGS---KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITK-ENIREVRKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 TGVCPQSNVQFDFLTVRENLRLFAKIK-GILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIF 577
Cdd:PRK13652 80 VGLVFQNPDDQIFSPTVEQDIAFGPINlGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1771853535 578 LLDEPTAGLDPFSRHQVW---NLLKERKTDRVIlFSTQFMDEADILADRKVFLSQGKLKCAGS 637
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIdflNDLPETYGMTVI-FSTHQLDLVPEMADYIYVMDKGRIVAYGT 221
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1237-1390 |
1.41e-17 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 83.18 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1237 SKR--KNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDALEFL----GYCPQE 1306
Cdd:COG2884 8 SKRypGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdlsRLKRREIPYLrrriGVVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1307 NALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTG 1386
Cdd:COG2884 88 FRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGN 167
|
....
gi 1771853535 1387 MDPE 1390
Cdd:COG2884 168 LDPE 171
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1236-1440 |
1.72e-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: 1.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1236 FSKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsGGGDALEF--------LGYCPQEN 1307
Cdd:cd03295 8 KRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFI---DGEDIREQdpvelrrkIGYVIQQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1308 ALWPNLTVRQHLevyAAVKGLRKGDAEVAITRLVDALKLQDQlkSPVK-------TLSEGIKRKLCFVLSILGNPSVVLL 1380
Cdd:cd03295 85 GLFPHMTVEENI---ALVPKLLKWPKEKIRERADELLALVGL--DPAEfadryphELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1381 DEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1440
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGT 219
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1244-1435 |
3.14e-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: 3.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1244 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKP---TAGQVLLKG----SGGGDALE-----FLGYCPQE--NAL 1309
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGedllKLSEKELRkirgrEIQMIFQDpmTSL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1310 WPNLTVRQHL-EVYAAVKGLRKGDAEvaiTRLVDALKLQdQLKSPVKT-------LSEGIKRKLCFVLSILGNPSVVLLD 1381
Cdd:COG0444 100 NPVMTVGDQIaEPLRIHGGLSKAEAR---ERAIELLERV-GLPDPERRldrypheLSGGMRQRVMIARALALEPKLLIAD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1771853535 1382 EPSTGMDPEGQQQmwqaIRATFR--NTERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1435
Cdd:COG0444 176 EPTTALDVTIQAQ----ILNLLKdlQRELGLaiLFITHDLGVVAEIADRVAVMYAGRI 229
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
437-637 |
3.64e-17 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 85.86 E-value: 3.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 437 ALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLS---KLTGVCPQSNVQFDFLT 513
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 514 VRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQ 593
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1771853535 594 VWN-LLK-ERKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS 637
Cdd:PRK10070 203 MQDeLVKlQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGT 248
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1248-1439 |
3.80e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 85.66 E-value: 3.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1248 VSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsgGGDALEFL---------GYCPQENALWPNLTVRQ- 1317
Cdd:PRK09536 22 VDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLV----AGDDVEALsaraasrrvASVPQDTSLSFEFDVRQv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1318 -------HLEVYAAVKGLRKGDAEVAITRlVDALKLQDQlksPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1390
Cdd:PRK09536 98 vemgrtpHRSRFDTWTETDRAAVERAMER-TGVAQFADR---PVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDIN 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1771853535 1391 GQQQMWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1439
Cdd:PRK09536 174 HQVRTLELVR-RLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1208-1433 |
5.52e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 86.26 E-value: 5.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1208 LNSTNFDEKPVIIASCLRKEYAGKR--KGcfskrknkiatrnVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQ 1285
Cdd:PRK15439 1 MQTSDTTAPPLLCARSISKQYSGVEvlKG-------------IDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1286 VLLKGS-----GGGDALEFLGY-CPQENALWPNLTVRQHLEVyaavkGL-RKGDAEVAITRLVDALKLQDQLKSPVKTLs 1358
Cdd:PRK15439 68 LEIGGNpcarlTPAKAHQLGIYlVPQEPLLFPNLSVKENILF-----GLpKRQASMQKMKQLLAALGCQLDLDSSAGSL- 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1771853535 1359 EGIKRKLCFVL-SILGNPSVVLLDEPSTGMDPEGQQQMWQAIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSG 1433
Cdd:PRK15439 142 EVADRQIVEILrGLMRDSRILILDEPTASLTPAETERLFSRIRE-LLAQGVGIVFISHKLPEIRQLADRISVMRDG 216
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
421-600 |
5.67e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 86.70 E-value: 5.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 421 IRNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMaDLENLSKLT- 499
Cdd:PRK10535 7 LKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATL-DADALAQLRr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 500 ---GVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQI 576
Cdd:PRK10535 86 ehfGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQV 165
|
170 180
....*....|....*....|....
gi 1771853535 577 FLLDEPTAGLDPFSRHQVWNLLKE 600
Cdd:PRK10535 166 ILADEPTGALDSHSGEEVMAILHQ 189
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1246-1435 |
6.28e-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: 6.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1246 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-----SGGGDALEF-LGYCP---QENALWPNLTVR 1316
Cdd:COG1129 269 RDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpvriRSPRDAIRAgIAYVPedrKGEGLVLDLSIR 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1317 Q-----HLEVYAAVKGLRKGDAEVAITRLVDALKL----QDQlksPVKTLSEGIKRKLcfVLS--ILGNPSVVLLDEPST 1385
Cdd:COG1129 349 EnitlaSLDRLSRGGLLDRRRERALAEEYIKRLRIktpsPEQ---PVGNLSGGNQQKV--VLAkwLATDPKVLILDEPTR 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1771853535 1386 GMDPEGQQQMWQAIRatfRNTERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1435
Cdd:COG1129 424 GIDVGAKAEIYRLIR---ELAAEGKavIVISSELPELLGLSDRILVMREGRI 472
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
164-357 |
7.35e-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: 83.98 E-value: 7.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 164 YLFSCIISFSSFIYYASV--NVTRER-KRMKALMTMMGLRDSAFWLSWGLLYAGFIFIMALFLALVIRSTqFIILSGFMV 240
Cdd:pfam12698 162 YLVGLILMIIILIGAAIIavSIVEEKeSRIKERLLVSGVSPLQYWLGKILGDFLVGLLQLLIILLLLFGI-GIPFGNLGL 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 241 VFSLFLLYGLSLVALAFLMSILVKKSFLTGLVVFLLT-VFWGCLGFTSLYRHLPASLEWILSLLSPFAFMLGMAQLLHld 319
Cdd:pfam12698 241 LLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVIlLLSGFFGGLFPLEDPPSFLQWIFSIIPFFSPIDGLLRLIY-- 318
|
170 180 190
....*....|....*....|....*....|....*...
gi 1771853535 320 YDLNSNAFPhpsdgsNLIvatnfMLAFDTCLYLALAIY 357
Cdd:pfam12698 319 GDSLWEIAP------SLI-----ILLLFAVVLLLLALL 345
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
419-608 |
9.43e-17 |
|
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: 80.53 E-value: 9.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMaDLENLSKL 498
Cdd:cd03369 7 IEVENLSVRYA--PDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTI-PLEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 TGVCPQSNVQFDFlTVRENLRLFAKIKgilpqevDKEIQRVLLELEMKNiqdvlaqNLSGGQKRKLTFGIAILGDPQIFL 578
Cdd:cd03369 84 LTIIPQDPTLFSG-TIRSNLDPFDEYS-------DEEIYGALRVSEGGL-------NLSQGQRQLLCLARALLKRPRVLV 148
|
170 180 190
....*....|....*....|....*....|
gi 1771853535 579 LDEPTAGLDPFSRHQVWNLLKERKTDRVIL 608
Cdd:cd03369 149 LDEATASIDYATDALIQKTIREEFTNSTIL 178
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1252-1427 |
1.02e-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: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1252 VRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsgggdALEFLGYCPQENALWPNLTVRQHLevYAAVKGlrKG 1331
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI-------ELDTVSYKPQYIKADYEGTVRDLL--SSITKD--FY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1332 DAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGAL 1411
Cdd:cd03237 91 THPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAF 170
|
170
....*....|....*.
gi 1771853535 1412 LTTHYMAEAEAVCDRV 1427
Cdd:cd03237 171 VVEHDIIMIDYLADRL 186
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
425-587 |
1.08e-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: 80.23 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 425 TKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADlENLSKLTGVCPQ 504
Cdd:cd03231 3 ADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD-SIARGLLYLGHA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 505 SNVQfDFLTVRENLRLFAKIKGilpqevDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTA 584
Cdd:cd03231 82 PGIK-TTLSVLENLRFWHADHS------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
...
gi 1771853535 585 GLD 587
Cdd:cd03231 155 ALD 157
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1244-1435 |
1.19e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 84.96 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1244 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-----SGGGDALEfLG----YcpQENALWPNLT 1314
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGqemrfASTTAALA-AGvaiiY--QELHLVPEMT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1315 VRQ-----HLEVYAAVkgLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDP 1389
Cdd:PRK11288 96 VAEnlylgQLPHKGGI--VNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1771853535 1390 EGQQQMWQAIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1435
Cdd:PRK11288 174 REIEQLFRVIRE-LRAEGRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
419-618 |
1.22e-16 |
|
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: 80.21 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKPDKIE-ALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNklsemadlenlsk 497
Cdd:cd03250 1 ISVEDASFTWDSGEQETSfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 498 lTGVCPQSN-VQFDflTVRENLrLFAKikgilpqEVDKE-IQRVL----LELEMKN----IQDVLAQ---NLSGGQKRKL 564
Cdd:cd03250 68 -IAYVSQEPwIQNG--TIRENI-LFGK-------PFDEErYEKVIkacaLEPDLEIlpdgDLTEIGEkgiNLSGGQKQRI 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1771853535 565 TFGIAILGDPQIFLLDEPTAGLDPFSRHQVWN-----LLKERKTdrVILF--STQFMDEAD 618
Cdd:cd03250 137 SLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncilgLLLNNKT--RILVthQLQLLPHAD 195
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
421-632 |
1.39e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 81.26 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 421 IRNVTKEYKGKpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVtiynnklsemadlenlskLTG 500
Cdd:PRK11247 15 LNAVSKRYGER----TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL------------------LAG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 501 VCPQSNvqfdfltVRENLRLFAKIKGILPQEvdKEIQRVLLELEMK---NIQDVLAQ------------NLSGGQKRKLT 565
Cdd:PRK11247 73 TAPLAE-------AREDTRLMFQDARLLPWK--KVIDNVGLGLKGQwrdAALQALAAvgladranewpaALSGGQKQRVA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1771853535 566 FGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKL 632
Cdd:PRK11247 144 LARALIHRPGLLLLDEPLGALDALTRIEMQDLIESlwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1248-1415 |
1.41e-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: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1248 VSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDAL----EFLGYCPQENALWPNLTVRQHLEVYA 1323
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRdsiaRGLLYLGHAPGIKTTLSVLENLRFWH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1324 AV---KGLRKGDAEVAITRLVDAlklqdqlksPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIR 1400
Cdd:cd03231 99 ADhsdEQVEEALARVGLNGFEDR---------PVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMA 169
|
170
....*....|....*..
gi 1771853535 1401 AtfrNTERG--ALLTTH 1415
Cdd:cd03231 170 G---HCARGgmVVLTTH 183
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1238-1442 |
1.44e-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: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1238 KRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsgGGDALEflGYCPQENALwpNLTV-R 1316
Cdd:COG4559 10 RLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRL----NGRPLA--AWSPWELAR--RRAVlP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1317 QH---------LEVYA--AVKGLRKGDAEVAITR----LVDALKLQDQLkspVKTLSEGIK------RKLCFVL-SILGN 1374
Cdd:COG4559 82 QHsslafpftvEEVVAlgRAPHGSSAAQDRQIVRealaLVGLAHLAGRS---YQTLSGGEQqrvqlaRVLAQLWePVDGG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1771853535 1375 PSVVLLDEPSTGMDPEGQQQMWQAIRatfRNTERGA--------L-LTTHYmaeaeavCDRVAIMVSGRLRCIGSIQ 1442
Cdd:COG4559 159 PRWLFLDEPTSALDLAHQHAVLRLAR---QLARRGGgvvavlhdLnLAAQY-------ADRILLLHQGRLVAQGTPE 225
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1242-1441 |
1.73e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 81.63 E-value: 1.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1242 KIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG---SGGGDALEFL----GYCPQ--ENALWPN 1312
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvdiTDKKVKLSDIrkkvGLVFQypEYQLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1313 lTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQL---KSPVKtLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDP 1389
Cdd:PRK13637 100 -TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEDykdKSPFE-LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1771853535 1390 EGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSI 1441
Cdd:PRK13637 178 KGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1239-1435 |
2.37e-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: 2.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1239 RKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITG-----DTKPTAGQVLLKG----SGGGDALEF---LGYCPQE 1306
Cdd:cd03260 10 YGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGkdiyDLDVDVLELrrrVGMVFQK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1307 NALWPnLTVRQHLEVYAAVKGLRKGDAEVAITRlvDALK---LQDQLKSPVK--TLSEGIKRKLCFVLSILGNPSVVLLD 1381
Cdd:cd03260 90 PNPFP-GSIYDNVAYGLRLHGIKLKEELDERVE--EALRkaaLWDEVKDRLHalGLSGGQQQRLCLARALANEPEVLLLD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1771853535 1382 EPSTGMDPEGQQQMWQAIRATfrNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1435
Cdd:cd03260 167 EPTSALDPISTAKIEELIAEL--KKEYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
443-632 |
2.39e-16 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 80.01 E-value: 2.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 443 FDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLEN-LSKLTgvcpQSNVQFDFLTVRENLRLf 521
Cdd:PRK10771 20 LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRpVSMLF----QENNLFSHLTVAQNIGL- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 522 akikGILP---------QEVDKEIQRVLLElemkNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRH 592
Cdd:PRK10771 95 ----GLNPglklnaaqrEKLHAIARQMGIE----DLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQ 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1771853535 593 QVWNLLKERKTDRVI--LFSTQFMDEADILADRKVFLSQGKL 632
Cdd:PRK10771 167 EMLTLVSQVCQERQLtlLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
436-651 |
2.46e-16 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 84.79 E-value: 2.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 436 EALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMaDLENLSKLTGVCPQSNVQFDFlTVR 515
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI-DRHTLRQFINYLPQEPYIFSG-SIL 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 516 ENLRLFAKiKGILPQEVDKEIQRVLLELEMKNIQ-------DVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDP 588
Cdd:TIGR01193 566 ENLLLGAK-ENVSQDEIWAACEIAEIKDDIENMPlgyqtelSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDT 644
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1771853535 589 FSRHQ-VWNLLKerKTDRVILFSTQFMDEADiLADRKVFLSQGKLKCAGSSLFLKKKWGIGYHL 651
Cdd:TIGR01193 645 ITEKKiVNNLLN--LQDKTIIFVAHRLSVAK-QSDKIIVLDHGKIIEQGSHDELLDRNGFYASL 705
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
431-600 |
2.49e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 84.51 E-value: 2.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 431 KPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLsVPTKGSVTIYNNKLSEMaDLE----NLSKLtGVCPQsn 506
Cdd:PRK11174 359 SPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELREL-DPEswrkHLSWV-GQNPQ-- 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 507 vqfdfL---TVRENLRLfAKikgilPQEVDKEIQRVLlelEMKNIQDVLAQ--------------NLSGGQKRKLTFGIA 569
Cdd:PRK11174 434 -----LphgTLRDNVLL-GN-----PDASDEQLQQAL---ENAWVSEFLPLlpqgldtpigdqaaGLSVGQAQRLALARA 499
|
170 180 190
....*....|....*....|....*....|.
gi 1771853535 570 ILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE 600
Cdd:PRK11174 500 LLQPCQLLLLDEPTASLDAHSEQLVMQALNA 530
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1252-1435 |
2.94e-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: 2.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1252 VRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDA--------LEFlgycpQENALWPNLTVRQHLEVyA 1323
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAppadrpvsMLF-----QENNLFAHLTVEQNVGL-G 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1324 AVKGLR-----KGDAEVAITRLvdalKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQA 1398
Cdd:cd03298 95 LSPGLKltaedRQAIEVALARV----GLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 1771853535 1399 IRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1435
Cdd:cd03298 171 VLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
419-637 |
3.14e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 81.21 E-value: 3.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGK-PDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNK----LSEMADLE 493
Cdd:PRK13645 7 IILDNVSYTYAKKtPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAipanLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 494 NLSKLTGVCPQ-SNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKniQDVLAQN---LSGGQKRKLTFGIA 569
Cdd:PRK13645 87 RLRKEIGLVFQfPEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLP--EDYVKRSpfeLSGGQKRRVALAGI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1771853535 570 ILGDPQIFLLDEPTAGLDPFSRHQVWNL---LKERKTDRVILFsTQFMDEADILADRKVFLSQGKLKCAGS 637
Cdd:PRK13645 165 IAMDGNTLVLDEPTGGLDPKGEEDFINLferLNKEYKKRIIMV-THNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1247-1433 |
3.39e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 80.16 E-value: 3.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1247 NVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKgsgggDALEfLGYCPQENALWPN--LTVRQHLEVYAA 1324
Cdd:PRK09544 22 DVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRN-----GKLR-IGYVPQKLYLDTTlpLTVNRFLRLRPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1325 VKglrKGDAEVAITRlVDALKLQDQlksPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFR 1404
Cdd:PRK09544 96 TK---KEDILPALKR-VQAGHLIDA---PMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRR 168
|
170 180 190
....*....|....*....|....*....|....
gi 1771853535 1405 NTERGALLTTH----YMAEA-EAVCDRVAIMVSG 1433
Cdd:PRK09544 169 ELDCAVLMVSHdlhlVMAKTdEVLCLNHHICCSG 202
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1246-1415 |
3.69e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 78.69 E-value: 3.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1246 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDALEFLGYCPQENALWPNLTVRQHLEV 1321
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGepirRQRDEYHQDLLYLGHQPGIKTELTALENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1322 YAAVKGLrkGDAEVAITRLvDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRA 1401
Cdd:PRK13538 98 YQRLHGP--GDDEALWEAL-AQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQ 174
|
170
....*....|....*.
gi 1771853535 1402 tfrNTERG--ALLTTH 1415
Cdd:PRK13538 175 ---HAEQGgmVILTTH 187
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1244-1390 |
4.07e-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: 4.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1244 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSG----GGDALEFL----GYCPQENALWPNLTV 1315
Cdd:cd03292 16 ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDvsdlRGRAIPYLrrkiGVVFQDFRLLPDRNV 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1771853535 1316 RQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1390
Cdd:cd03292 96 YENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPD 170
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1246-1383 |
5.12e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 83.19 E-value: 5.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1246 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSgggdalEFLGYCPQENALWPNLTVRQ-----HLE 1320
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG------LRIGYLPQEPPLDDDLTVLDtvldgDAE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1321 VYAAVKGLRKG---------------------------DAEVAITRLVDALKL-QDQLKSPVKTLSEGIKRK--LCFVLs 1370
Cdd:COG0488 89 LRALEAELEELeaklaepdedlerlaelqeefealggwEAEARAEEILSGLGFpEEDLDRPVSELSGGWRRRvaLARAL- 167
|
170
....*....|...
gi 1771853535 1371 iLGNPSVVLLDEP 1383
Cdd:COG0488 168 -LSEPDLLLLDEP 179
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
419-637 |
6.41e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.79 E-value: 6.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGkpdkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMAdlENLSKL 498
Cdd:PRK15439 12 LCARSISKQYSG----VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT--PAKAHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 TGV--CPQSNVQFDFLTVRENLrLFAKIKgilPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQI 576
Cdd:PRK15439 86 LGIylVPQEPLLFPNLSVKENI-LFGLPK---RQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1771853535 577 FLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS 637
Cdd:PRK15439 162 LILDEPTASLTPAETERLFSRIRElLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGK 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
421-633 |
8.72e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 82.42 E-value: 8.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 421 IRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKlsemadlenlsKLtG 500
Cdd:COG0488 1 LENLSKSFGGRP----LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL-----------RI-G 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 501 VCPQSNVQFDFLTVREN-LRLFAKIKGIL------------PQEVDKEIQRVLLELEMKN-------IQDVLAQ------ 554
Cdd:COG0488 65 YLPQEPPLDDDLTVLDTvLDGDAELRALEaeleeleaklaePDEDLERLAELQEEFEALGgweaearAEEILSGlgfpee 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 555 -------NLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHqvW--NLLKERKT-------DRVilfstqFMDEad 618
Cdd:COG0488 145 dldrpvsELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIE--WleEFLKNYPGtvlvvshDRY------FLDR-- 214
|
250
....*....|....*
gi 1771853535 619 iLADRKVFLSQGKLK 633
Cdd:COG0488 215 -VATRILELDRGKLT 228
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1249-1444 |
1.16e-15 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 77.87 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1249 SFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSgggdalEFLGYCP---------QENALWPNLTVRQHl 1319
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQ------DLTALPPaerpvsmlfQENNLFPHLTVAQN- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1320 eVYAAVK-GLRKGDAEVAitRLVDALK---LQDQLKSPVKTLSEG------IKRklCFVLsilGNPsVVLLDEPSTGMDP 1389
Cdd:COG3840 92 -IGLGLRpGLKLTAEQRA--QVEQALErvgLAGLLDRLPGQLSGGqrqrvaLAR--CLVR---KRP-ILLLDEPFSALDP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1771853535 1390 EGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL 1444
Cdd:COG3840 163 ALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAAL 217
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1240-1435 |
1.34e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 78.98 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1240 KNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDaleflgycpqENALWpnlTVRQHL 1319
Cdd:PRK13633 21 TEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSD----------EENLW---DIRNKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1320 ---------EVYAAVKglrkgDAEVAI-------------TRLVDALK---LQDQLKSPVKTLSEGIKRKLCFVLSILGN 1374
Cdd:PRK13633 88 gmvfqnpdnQIVATIV-----EEDVAFgpenlgippeeirERVDESLKkvgMYEYRRHAPHLLSGGQKQRVAIAGILAMR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1771853535 1375 PSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAeAVCDRVAIMVSGRL 1435
Cdd:PRK13633 163 PECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEA-VEADRIIVMDSGKV 222
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1244-1453 |
1.40e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 82.48 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1244 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQ--VLlkgsgGGD--------------AleflgYCPQ-- 1305
Cdd:NF033858 16 ALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRveVL-----GGDmadarhrravcpriA-----YMPQgl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1306 -ENaLWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRK--LCFVLsiLGNPSVVLLDE 1382
Cdd:NF033858 86 gKN-LYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKlgLCCAL--IHDPDLLILDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1771853535 1383 PSTGMDPEGQQQMWQ---AIRAtfrntERGA---LLTTHYMAEAEAvCDRVAIMVSGRLRCIGSIQHLKSKFGKDYL 1453
Cdd:NF033858 163 PTTGVDPLSRRQFWElidRIRA-----ERPGmsvLVATAYMEEAER-FDWLVAMDAGRVLATGTPAELLARTGADTL 233
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1247-1447 |
1.43e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 79.01 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1247 NVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGsgggDALeflgycpQENALWpnlTVRQHLE------ 1320
Cdd:PRK13650 25 DVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG----DLL-------TEENVW---DIRHKIGmvfqnp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1321 ----VYAAVK-----GLR-KG-DAEVAITRLVDALKL---QD-QLKSPVKtLSEGIKRKLCFVLSILGNPSVVLLDEPST 1385
Cdd:PRK13650 91 dnqfVGATVEddvafGLEnKGiPHEEMKERVNEALELvgmQDfKEREPAR-LSGGQKQRVAIAGAVAMRPKIIILDEATS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1771853535 1386 GMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAeAVCDRVAIMVSGRLRCIGSIQHLKSK 1447
Cdd:PRK13650 170 MLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1247-1435 |
1.53e-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: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1247 NVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGS--------GGGDALEF---LGYCPQENALWPNLTV 1315
Cdd:COG4161 20 DINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdfsqkpSEKAIRLLrqkVGMVFQQYNLWPHLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1316 RQHL-EVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQ 1394
Cdd:COG4161 100 MENLiEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQ 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1771853535 1395 MWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1435
Cdd:COG4161 180 VVEIIR-ELSQTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
418-632 |
1.53e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 81.61 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 418 AIRIRNVTKEYKGkpdkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLsemadlenlsK 497
Cdd:COG3845 5 ALELRGITKRFGG----VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV----------R 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 498 LT----------GVCPQSNVQFDFLTVRENLRLFAKIKGIL---PQEVDKEIQRVL----LELEMkniqDVLAQNLSGGQ 560
Cdd:COG3845 71 IRsprdaialgiGMVHQHFMLVPNLTVAENIVLGLEPTKGGrldRKAARARIRELSerygLDVDP----DAKVEDLSVGE 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1771853535 561 KRKLTfgI--AILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKL 632
Cdd:COG3845 147 QQRVE--IlkALYRGARILILDEPTAVLTPQEADELFEILRRlAAEGKSIIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
433-587 |
1.72e-15 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 82.59 E-value: 1.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 433 DKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVP--TKGSVTIYNNKLSEmadlENLSKLTGVCPQSNVQFD 510
Cdd:PLN03140 891 DRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISGFPKKQ----ETFARISGYCEQNDIHSP 966
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 511 FLTVRENLRLFAKIKgiLPQEVDKE-----IQRVLLELEMKNIQDVLA-----QNLSGGQKRKLTFGIAILGDPQIFLLD 580
Cdd:PLN03140 967 QVTVRESLIYSAFLR--LPKEVSKEekmmfVDEVMELVELDNLKDAIVglpgvTGLSTEQRKRLTIAVELVANPSIIFMD 1044
|
....*..
gi 1771853535 581 EPTAGLD 587
Cdd:PLN03140 1045 EPTSGLD 1051
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1231-1487 |
1.77e-15 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 81.48 E-value: 1.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1231 KRKGCFSKRKN---KIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDALeflgycpqEN 1307
Cdd:PRK13545 23 KLKDLFFRSKDgeyHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAI--------SS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1308 ALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGM 1387
Cdd:PRK13545 95 GLNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1388 DPEGQQQMWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFGkDYLLEMKVKNLAQVEPL 1467
Cdd:PRK13545 175 DQTFTKKCLDKMN-EFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYD-EFLKKYNQMSVEERKDF 252
|
250 260
....*....|....*....|
gi 1771853535 1468 HAEILRLFPQAARQERYSSL 1487
Cdd:PRK13545 253 REEQISQFQHGLLQEDQTGR 272
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1240-1435 |
1.90e-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: 75.81 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1240 KNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG---SGGGDAL-EFLGYCPQENALWpNLTV 1315
Cdd:cd03247 13 QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGvpvSDLEKALsSLISVLNQRPYLF-DTTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1316 RQHLevyaavkGLRkgdaevaitrlvdalklqdqlkspvktLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQM 1395
Cdd:cd03247 92 RNNL-------GRR---------------------------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQL 137
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1771853535 1396 WQAIRATFRNteRGALLTTHYMAEAEAVcDRVAIMVSGRL 1435
Cdd:cd03247 138 LSLIFEVLKD--KTLIWITHHLTGIEHM-DKILFLENGKI 174
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1236-1449 |
1.98e-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: 77.27 E-value: 1.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1236 FSKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDA-----LEFLGYCPQENALW 1310
Cdd:cd03254 10 FSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIsrkslRSMIGVVLQDTFLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1311 PNlTVRQHL----------EVYAAVKglrkgdaEVAITRLVDALK--LQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVV 1378
Cdd:cd03254 90 SG-TIMENIrlgrpnatdeEVIEAAK-------EAGAHDFIMKLPngYDTVLGENGGNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1771853535 1379 LLDEPSTGMDPEGQQQMWQAIRATFRNteRGALLTTHYMAEAEAVcDRVAIMVSGRLRCIGSIQHLKSKFG 1449
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKLMKG--RTSIIIAHRLSTIKNA-DKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1241-1434 |
2.30e-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: 77.22 E-value: 2.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1241 NKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDALEFL----GYCPQENALWPN 1312
Cdd:cd03256 13 GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGtdinKLKGKALRQLrrqiGMIFQQFNLIER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1313 LTVRQH-----LEVYAAVKGLR----KGDAEVAItRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEP 1383
Cdd:cd03256 93 LSVLENvlsgrLGRRSTWRSLFglfpKEEKQRAL-AALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1771853535 1384 STGMDPEGQQQMWQAIRATfrNTERG--ALLTTHYMAEAEAVCDRVAIMVSGR 1434
Cdd:cd03256 172 VASLDPASSRQVMDLLKRI--NREEGitVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
436-636 |
2.47e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 77.70 E-value: 2.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 436 EALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLS---------EMADLENL----SKLTGVC 502
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlKVADKNQLrllrTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 503 PQSNVqFDFLTVREN-LRLFAKIKGILPQEVDKEIQRVLLELEM-KNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLD 580
Cdd:PRK10619 99 QHFNL-WSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIdERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 581 EPTAGLDPFSRHQVWNLLK----ERKTDRVIlfsTQFMDEADILADRKVFLSQGKLKCAG 636
Cdd:PRK10619 178 EPTSALDPELVGEVLRIMQqlaeEGKTMVVV---THEMGFARHVSSHVIFLHQGKIEEEG 234
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
419-632 |
2.55e-15 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 77.92 E-value: 2.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYK-----GKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMA--- 490
Cdd:TIGR02769 3 LEVRDVTHTYRtgglfGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 491 ------DLENLSK--LTGVCPQSNVQFdflTVRENLRLFAKIKgilPQEVDKEIQRVLLELEMK-NIQDVLAQNLSGGQK 561
Cdd:TIGR02769 83 rrafrrDVQLVFQdsPSAVNPRMTVRQ---IIGEPLRHLTSLD---ESEQKARIAELLDMVGLRsEDADKLPRQLSGGQL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1771853535 562 RKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVI--LFSTQFMDEADILADRKVFLSQGKL 632
Cdd:TIGR02769 157 QRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTayLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
396-637 |
3.52e-15 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 80.78 E-value: 3.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 396 MDADPSFHDSfEQAPPEFQGKEAIRIRNVTKEYKGKPdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPT 475
Cdd:PRK13657 313 EDAVPDVRDP-PGAIDLGRVKGAVEFDDVSFSYDNSR---QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQ 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 476 KGSVTIYNNKLSEMAdLENLSKLTGVCPQSNVQFDfLTVRENLRLfAKikgilPQEVDKEIQRVL-----LELEMKNIQ- 549
Cdd:PRK13657 389 SGRILIDGTDIRTVT-RASLRRNIAVVFQDAGLFN-RSIEDNIRV-GR-----PDATDEEMRAAAeraqaHDFIERKPDg 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 550 -DVLA----QNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRvilfsTQFMDeADIL---- 620
Cdd:PRK13657 461 yDTVVgergRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGR-----TTFII-AHRLstvr 534
|
250
....*....|....*...
gi 1771853535 621 -ADRKVFLSQGKLKCAGS 637
Cdd:PRK13657 535 nADRILVFDNGRVVESGS 552
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1208-1440 |
3.97e-15 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 79.22 E-value: 3.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1208 LNSTNFDEKPVIIASCLRKEYAGKrkgcfskrknkIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVL 1287
Cdd:PRK09452 4 LNKQPSSLSPLVELRGISKSFDGK-----------EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1288 LKGsgggdalEFLGYCPQEN----------ALWPNLTVRQHLEVyaavkGLR---KGDAEVAiTRLVDALK---LQDQLK 1351
Cdd:PRK09452 73 LDG-------QDITHVPAENrhvntvfqsyALFPHMTVFENVAF-----GLRmqkTPAAEIT-PRVMEALRmvqLEEFAQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1352 SPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMV 1431
Cdd:PRK09452 140 RKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMR 219
|
....*....
gi 1771853535 1432 SGRLRCIGS 1440
Cdd:PRK09452 220 DGRIEQDGT 228
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1243-1434 |
4.30e-15 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 76.95 E-value: 4.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1243 IATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSgggdalEFLGYCPQENA-------------- 1308
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQ------HIEGLPGHQIArmgvvrtfqhvrlf 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1309 ----LWPNLTVRQHLEVYAAV-------KGLRKGDAEvAITRL---VDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGN 1374
Cdd:PRK11300 93 remtVIENLLVAQHQQLKTGLfsgllktPAFRRAESE-ALDRAatwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQ 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1375 PSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1434
Cdd:PRK11300 172 PEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
422-631 |
4.87e-15 |
|
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: 75.38 E-value: 4.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 422 RNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPT---KGSVTiYNNKLSemadLENLSKL 498
Cdd:cd03233 7 RNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIH-YNGIPY----KEFAEKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 TG---VCPQSNVQFDFLTVRENLRLFAKIKGilpqevdKEIQRVllelemkniqdvlaqnLSGGQKRKLTFGIAILGDPQ 575
Cdd:cd03233 82 PGeiiYVSEEDVHFPTLTVRETLDFALRCKG-------NEFVRG----------------ISGGERKRVSIAEALVSRAS 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1771853535 576 IFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFS-TQFMDEADILADRKVFLSQGK 631
Cdd:cd03233 139 VLCWDNSTRGLDSSTALEILKCIRTmaDVLKTTTFVSlYQASDEIYDLFDKVLVLYEGR 197
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1242-1447 |
4.93e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 77.56 E-value: 4.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1242 KIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-----SGGGDALEFL----GYCPQ--ENALW 1310
Cdd:PRK13641 20 KKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpETGNKNLKKLrkkvSLVFQfpEAQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1311 PNlTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQL--KSPVKtLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMD 1388
Cdd:PRK13641 100 EN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLisKSPFE-LSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1771853535 1389 PEGQQQMWQairaTFRNTERGA---LLTTHYMAEAEAVCDRVAIMVSGRLrcigsIQHLKSK 1447
Cdd:PRK13641 178 PEGRKEMMQ----LFKDYQKAGhtvILVTHNMDDVAEYADDVLVLEHGKL-----IKHASPK 230
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1244-1442 |
6.25e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 79.44 E-value: 6.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1244 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSG-----GGDALEF-LGYCPQENALWPNLTVRQ 1317
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINynkldHKLAAQLgIGIIYQELSVIDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1318 HLEV----YAAVKGLRKGD---AEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1390
Cdd:PRK09700 100 NLYIgrhlTKKVCGVNIIDwreMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1771853535 1391 GQQQMWqAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQ 1442
Cdd:PRK09700 180 EVDYLF-LIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVS 230
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
415-646 |
8.00e-15 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 77.85 E-value: 8.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 415 GKEAIRIRNVTKEYkgkpDKIEALKDLVFDIYEGQITAILGHSGAG--KSTLLNILSGlsvPTKGSVTIynNKLSEMADL 492
Cdd:NF000106 10 ARNAVEVRGLVKHF----GEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPW--RF*TWCANR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 493 ENLSKLTGVC-PQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAIL 571
Cdd:NF000106 81 RALRRTIG*HrPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1771853535 572 GDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTD-RVILFSTQFMDEADILADRKVFLSQGKLKCAGSSLFLKKKWG 646
Cdd:NF000106 161 GRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDgATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG 236
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1244-1430 |
9.47e-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: 9.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1244 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsGGGDALEF--------LGYCPQENALWPNlTV 1315
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAV---NGVPLADAdadswrdqIAWVPQHPFLFAG-TI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1316 RQHLEVY---AAVKGLRKGDAEVAITRLVDALK--LQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1390
Cdd:TIGR02857 413 AENIRLArpdASDAEIREALERAGLDEFVAALPqgLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAE 492
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1771853535 1391 GQQQMWQAIRATFRNteRGALLTTHYMAEAEAvCDRVAIM 1430
Cdd:TIGR02857 493 TEAEVLEALRALAQG--RTVLLVTHRLALAAL-ADRIVVL 529
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
411-636 |
9.60e-15 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 79.31 E-value: 9.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 411 PEFQGKeaIRIRNVTkeYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMa 490
Cdd:TIGR01842 311 PEPEGH--LSVENVT--IVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQW- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 491 DLENLSKLTGVCPQsNVQFDFLTVRENLRLF------------AKIKGI------LPQEVDKEIqrvllelemkniqDVL 552
Cdd:TIGR01842 386 DRETFGKHIGYLPQ-DVELFPGTVAENIARFgenadpekiieaAKLAGVhelilrLPDGYDTVI-------------GPG 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 553 AQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEADILADRKVFLSQGKL 632
Cdd:TIGR01842 452 GATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPSLLGCVDKILVLQDGRI 531
|
....
gi 1771853535 633 KCAG 636
Cdd:TIGR01842 532 ARFG 535
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
440-587 |
1.13e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 74.46 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 440 DLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEM-----ADLENLSKLTGVCPQsnvqfdfLTV 514
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQrdeyhQDLLYLGHQPGIKTE-------LTA 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1771853535 515 RENLRLFAKIKGILPQEvdkEIQRVLLELEMKNIQDVLAQNLSGGQKRKltfgIAI----LGDPQIFLLDEPTAGLD 587
Cdd:PRK13538 92 LENLRFYQRLHGPGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRR----VALarlwLTRAPLWILDEPFTAID 161
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
417-630 |
1.49e-14 |
|
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: 74.78 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 417 EAIRIRNVTKEYK-----GKpdKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTI-YNNKLSEMA 490
Cdd:COG4778 3 TLLEVENLSKTFTlhlqgGK--RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrHDGGWVDLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 491 DLE-----NLSKLT-GVCPQsnvqfdFLTVR----------ENLRLfakiKGILPQEVDKEIQRVLLELemkNIQDVLAQ 554
Cdd:COG4778 81 QASpreilALRRRTiGYVSQ------FLRVIprvsaldvvaEPLLE----RGVDREEARARARELLARL---NLPERLWD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 555 ----NLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTqFMDEA--DILADRKVFLS 628
Cdd:COG4778 148 lppaTFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGI-FHDEEvrEAVADRVVDVT 226
|
..
gi 1771853535 629 QG 630
Cdd:COG4778 227 PF 228
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1224-1435 |
1.49e-14 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 76.76 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1224 LRKEYAGKRKGcfskrknKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsgGGDALEFLGyc 1303
Cdd:PRK11153 7 ISKVFPQGGRT-------IHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLV----DGQDLTALS-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1304 pqENALwpNLTVR------QHLE------VYAAV------KGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKL 1365
Cdd:PRK11153 74 --EKEL--RKARRqigmifQHFNllssrtVFDNValplelAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1771853535 1366 CFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATfrNTERG--ALLTTHYMAEAEAVCDRVAIMVSGRL 1435
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALDPATTRSILELLKDI--NRELGltIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
436-671 |
1.78e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 75.43 E-value: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 436 EALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKL--SEMADLENLSKLTGVCPQSNVQFDFLT 513
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdySKRGLLALRQQVATVFQDPEQQIFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 514 VRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQ 593
Cdd:PRK13638 95 IDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 594 VWNLLKE--RKTDRVILfSTQFMDEADILADRKVFLSQGKLKCAGS--SLF----------LKKKWGIGYHLSLQLNEIC 659
Cdd:PRK13638 175 MIAIIRRivAQGNHVII-SSHDIDLIYEISDAVYVLRQGQILTHGApgEVFacteameqagLTQPWLVKLHTQLGLPLCK 253
|
250
....*....|..
gi 1771853535 660 VEENITSLVKQH 671
Cdd:PRK13638 254 TETEFFHRMQKC 265
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1225-1450 |
1.85e-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: 1.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1225 RKEYAGKRKGCFSKRKN-KIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKP---TAGQVLLKGSGGGdaLEFL 1300
Cdd:TIGR00955 20 WKQLVSRLRGCFCRERPrKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPID--AKEM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1301 ----GYCPQENALWPNLTVRQHLEVYAAVKGLRKGDAEVAITR---LVDALKLQD------QLKSPVKTLSEGIKRKLCF 1367
Cdd:TIGR00955 98 raisAYVQQDDLFIPTLTVREHLMFQAHLRMPRRVTKKEKRERvdeVLQALGLRKcantriGVPGRVKGLSGGERKRLAF 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1368 VLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRAtFRNTERGALLTTHyMAEAEAVC--DRVAIMVSGRLRCIGSIQHLK 1445
Cdd:TIGR00955 178 ASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKG-LAQKGKTIICTIH-QPSSELFElfDKIILMAEGRVAYLGSPDQAV 255
|
....*
gi 1771853535 1446 SKFGK 1450
Cdd:TIGR00955 256 PFFSD 260
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
419-632 |
1.88e-14 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 74.74 E-value: 1.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYkgkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNK-LSEMADLENLSK 497
Cdd:PRK09493 2 IEFKNVSKHF----GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKvNDPKVDERLIRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 498 LTGVCPQSNVQFDFLTVRENLrLFA--KIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQ 575
Cdd:PRK09493 78 EAGMVFQQFYLFPHLTALENV-MFGplRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 576 IFLLDEPTAGLDPFSRHQVWNLLK---ERKTDRVILfsTQFMDEADILADRKVFLSQGKL 632
Cdd:PRK09493 157 LMLFDEPTSALDPELRHEVLKVMQdlaEEGMTMVIV--THEIGFAEKVASRLIFIDKGRI 214
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1232-1454 |
2.10e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 75.22 E-value: 2.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1232 RKGCFSKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-----SGGGDALEFLGYC--- 1303
Cdd:PRK13652 7 RDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGepitkENIREVRKFVGLVfqn 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1304 PQENALWPnlTVRQHLEVYAAVKGLrkgDAEVAITRLVDALK---LQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLL 1380
Cdd:PRK13652 87 PDDQIFSP--TVEQDIAFGPINLGL---DEETVAHRVSSALHmlgLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1771853535 1381 DEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLkskFGKDYLL 1454
Cdd:PRK13652 162 DEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI---FLQPDLL 232
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
448-610 |
2.75e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 74.05 E-value: 2.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 448 GQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMaDLENLSKL----TGVCPQSNVQFDFLTVRENLRLFAK 523
Cdd:PRK10584 36 GETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQM-DEEARAKLrakhVGFVFQSFMLIPTLNALENVELPAL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 524 IKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDpfsrhqvwnllkeRKT 603
Cdd:PRK10584 115 LRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD-------------RQT 181
|
170
....*....|
gi 1771853535 604 -DRV--ILFS 610
Cdd:PRK10584 182 gDKIadLLFS 191
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1244-1447 |
2.81e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 75.27 E-value: 2.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1244 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGS-------GGGDALEFLGYCPQ--ENALWpNLT 1314
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpidysrkGLMKLRESVGMVFQdpDNQLF-SAS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1315 VRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQ 1394
Cdd:PRK13636 100 VYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1771853535 1395 MWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSK 1447
Cdd:PRK13636 180 IMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1246-1454 |
2.82e-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: 2.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1246 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDA-LEFL----GYCPQENALWpNLTVRQHLE 1320
Cdd:cd03252 19 DNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALAdPAWLrrqvGVVLQENVLF-NRSIRDNIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1321 VYAAVKGLRKgdaEVAITRLVDALKLQDQLKSPVKT--------LSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQ 1392
Cdd:cd03252 98 LADPGMSMER---VIEAAKLAGAHDFISELPEGYDTivgeqgagLSGGQRQRIAIARALIHNPRILIFDEATSALDYESE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1771853535 1393 QQMWQAIRATFRNteRGALLTTHYMAEAEAVcDRVAIMVSGRLRCIGSIQHLKSKFGKDYLL 1454
Cdd:cd03252 175 HAIMRNMHDICAG--RTVIIIAHRLSTVKNA-DRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
408-587 |
3.63e-14 |
|
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: 77.55 E-value: 3.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 408 QAPPEFQGKEAIRIRNVTKEYKgkPDKiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIynnkls 487
Cdd:COG5265 347 DAPPLVVGGGEVRFENVSFGYD--PER-PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILI------ 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 488 emaDLENLSKLT--------GVCPQSNVQF-DflTVRENLRlFAKikgilPQEVDKEIQRVlleLEMKNIQDVLAQ---- 554
Cdd:COG5265 418 ---DGQDIRDVTqaslraaiGIVPQDTVLFnD--TIAYNIA-YGR-----PDASEEEVEAA---ARAAQIHDFIESlpdg 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1771853535 555 ----------NLSGGQKRKLtfGIA--ILGDPQIFLLDEPTAGLD 587
Cdd:COG5265 484 ydtrvgerglKLSGGEKQRV--AIArtLLKNPPILIFDEATSALD 526
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1246-1440 |
3.91e-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: 72.56 E-value: 3.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1246 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITG--DTKPTAGQVLLKGSgggDALEFLgycPQENAlwpnltvrqhlevya 1323
Cdd:cd03217 17 KGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGE---DITDLP---PEERA--------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1324 avkglRKG-----DAEVAITrlvdALKLQDQLKSPVKTLSEGiKRKLCFVLSILG-NPSVVLLDEPSTGMDPEGQQQMWQ 1397
Cdd:cd03217 76 -----RLGiflafQYPPEIP----GVKNADFLRYVNEGFSGG-EKKRNEILQLLLlEPDLAILDEPDSGLDIDALRLVAE 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1771853535 1398 AIRaTFRNTERGALLTTHYMAEAEAV-CDRVAIMVSGRLRCIGS 1440
Cdd:cd03217 146 VIN-KLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGD 188
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1244-1435 |
5.48e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 73.96 E-value: 5.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1244 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGS----GGGDALEF---LGYC---PQENALWPnl 1313
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpikyDKKSLLEVrktVGIVfqnPDDQLFAP-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1314 TVRQHLEVYAAVKGLRKGDAEvaiTRLVDALK---LQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1390
Cdd:PRK13639 95 TVEEDVAFGPLNLGLSKEEVE---KRVKEALKavgMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPM 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1771853535 1391 GQQQMwqaIRATFRNTERG--ALLTTHYMAEAEAVCDRVAIMVSGRL 1435
Cdd:PRK13639 172 GASQI---MKLLYDLNKEGitIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
415-632 |
6.15e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 76.22 E-value: 6.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 415 GKEAIRIRNVTkeYKGkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNnklsemADLEN 494
Cdd:COG3845 254 GEVVLEVENLS--VRD-DRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDG------EDITG 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 495 LS-----KL-----------TGVCPQsnvqfdfLTVRENLRL-------FAKiKGIL-PQEVDKEIQRVLLELEMK--NI 548
Cdd:COG3845 325 LSprerrRLgvayipedrlgRGLVPD-------MSVAENLILgryrrppFSR-GGFLdRKAIRAFAEELIEEFDVRtpGP 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 549 qDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKtDR---VILFSTQfMDEADILADRKV 625
Cdd:COG3845 397 -DTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELR-DAgaaVLLISED-LDEILALSDRIA 473
|
....*..
gi 1771853535 626 FLSQGKL 632
Cdd:COG3845 474 VMYEGRI 480
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
419-632 |
6.27e-14 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 72.60 E-value: 6.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKPdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLEN--LS 496
Cdd:PRK10908 2 IRFEHVSKAYLGGR---QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVpfLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 497 KLTGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQI 576
Cdd:PRK10908 79 RQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1771853535 577 FLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKL 632
Cdd:PRK10908 159 LLADEPTGNLDDALSEGILRLFEEfNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
416-612 |
1.03e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 73.38 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 416 KEAIRIRNVTKEYKgkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEmADLENL 495
Cdd:PRK15056 4 QAGIVVNDVTVTWR---NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ-ALQKNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 496 sklTGVCPQSN-VQFDFLTVRENLRLFAKI--KGIL--PQEVDKEI-QRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIA 569
Cdd:PRK15056 80 ---VAYVPQSEeVDWSFPVLVEDVVMMGRYghMGWLrrAKKRDRQIvTAALARVDMVEFRHRQIGELSGGQKKRVFLARA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1771853535 570 ILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQ 612
Cdd:PRK15056 157 IAQQGQVILLDEPFTGVDVKTEARIISLLRElRDEGKTMLVSTH 200
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1238-1463 |
1.29e-13 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 72.93 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1238 KRKNK--IATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDALeflgycpqeNA-LWPNLT 1314
Cdd:PRK13546 31 KHKNKtfFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAI---------SAgLSGQLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1315 VRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQ 1394
Cdd:PRK13546 102 GIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQK 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1771853535 1395 MWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFgKDYLLEMKVKNLAQ 1463
Cdd:PRK13546 182 CLDKIY-EFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKY-EAFLNDFKKKSKAE 248
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1239-1438 |
1.33e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.21 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1239 RKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-----SGGGDALE----FLGYCPQENAL 1309
Cdd:PRK09700 273 SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGkdispRSPLDAVKkgmaYITESRRDNGF 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1310 WPNLTVRQHLEVYAAVKGLRKGDA-----EVAITRLVDALKLQDQLKSP-----VKTLSEGIKRKLCFVLSILGNPSVVL 1379
Cdd:PRK09700 353 FPNFSIAQNMAISRSLKDGGYKGAmglfhEVDEQRTAENQRELLALKCHsvnqnITELSGGNQQKVLISKWLCCCPEVII 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1771853535 1380 LDEPSTGMDPEGQQQMWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCI 1438
Cdd:PRK09700 433 FDEPTRGIDVGAKAEIYKVMR-QLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1243-1453 |
1.40e-13 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 74.68 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1243 IATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG---SGGGDA------LEFLGYCPQENALWPNL 1313
Cdd:PRK10070 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAelrevrRKKIAMVFQSFALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1314 TVRQHLEVYAAVKGLrkgDAEVAITRLVDALK---LQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1390
Cdd:PRK10070 122 TVLDNTAFGMELAGI---NAEERREKALDALRqvgLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1771853535 1391 GQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFGKDYL 1453
Cdd:PRK10070 199 IRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYV 261
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1241-1415 |
2.22e-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: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1241 NKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDALEFL-GYCPQENALWpNLTV 1315
Cdd:TIGR02868 347 APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGvpvsSLDQDEVRRRvSVCAQDAHLF-DTTV 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1316 RQHL----------EVYAAVKGLRKGDaevaitrLVDAlkLQDQLKSPV----KTLSEGIKRKLCFVLSILGNPSVVLLD 1381
Cdd:TIGR02868 426 RENLrlarpdatdeELWAALERVGLAD-------WLRA--LPDGLDTVLgeggARLSGGERQRLALARALLADAPILLLD 496
|
170 180 190
....*....|....*....|....*....|....
gi 1771853535 1382 EPSTGMDPEGQQQMWQAIRATfrNTERGALLTTH 1415
Cdd:TIGR02868 497 EPTEHLDAETADELLEDLLAA--LSGRTVVLITH 528
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1236-1435 |
2.47e-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: 2.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1236 FSKRKNKI-ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDAL-EF---LGYCPQE 1306
Cdd:COG1135 11 FPTKGGPVtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGvdltALSERELrAArrkIGMIFQH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1307 NALWPNLTVRQH----LEvyaaVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEG------IKRKLCfvlsilGNPS 1376
Cdd:COG1135 91 FNLLSSRTVAENvalpLE----IAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGqkqrvgIARALA------NNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1771853535 1377 VVLLDEPSTGMDPEGQQQmwqaIRATFR--NTERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1435
Cdd:COG1135 161 VLLCDEATSALDPETTRS----ILDLLKdiNRELGLtiVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
862-1107 |
3.18e-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: 72.81 E-value: 3.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 862 ASIDDFIQSVEHQNI--ALEVDAFGTRNGTDDPSYNgaITVCCNEKNYSFSLACNAKRLNCFPVLMDIVSNGLLGMVKPS 939
Cdd:pfam12698 65 DSEEEAKEALKNGKIdgLLVIPKGFSKDLLKGESAT--VTVYINSSNLLVSKLILNALQSLLQQLNASALVLLLEALSTS 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 940 VHIRTErSTFLENGQDNPIGFLAYIMFWLVLTSSCPpYIAMSSIDDYKNRARSQLRISGLSPSAYWFGQALVDVSLYFLV 1019
Cdd:pfam12698 143 APIPVE-STPLFNPQSGYAYYLVGLILMIIILIGAA-IIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFLVGLLQ 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1020 FVFIYLMSYISNFEDMLLTIIHIIQIPcavgYSFSLIFMTYVISFIFRKGRKNSGIWSFCFYVVTVFSVAGFAFSIFESD 1099
Cdd:pfam12698 221 LLIILLLLFGIGIPFGNLGLLLLLFLL----YGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLFPLEDPPSF 296
|
....*...
gi 1771853535 1100 IPFIFTFL 1107
Cdd:pfam12698 297 LQWIFSII 304
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1246-1440 |
3.29e-13 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 74.43 E-value: 3.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1246 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsgGG--------DAL-EFLGYCPQENALWpNLTVR 1316
Cdd:COG1132 357 KDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILI----DGvdirdltlESLrRQIGVVPQDTFLF-SGTIR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1317 QHL----------EVYAAVKglrkgdaEVAITRLVDALKlqDQLKSPV----KTLSEGIKRKLCFVLSILGNPSVVLLDE 1382
Cdd:COG1132 432 ENIrygrpdatdeEVEEAAK-------AAQAHEFIEALP--DGYDTVVgergVNLSGGQRQRIAIARALLKDPPILILDE 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1771853535 1383 PSTGMDPEGQQQMWQAIRATFRNteRGALLTTHYMAEAEAvCDRVAIMVSGRLRCIGS 1440
Cdd:COG1132 503 ATSALDTETEALIQEALERLMKG--RTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGT 557
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1246-1434 |
3.48e-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: 70.79 E-value: 3.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1246 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDALEF---LGYCPQENALWPNLTVRQH 1318
Cdd:COG1126 18 KGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGedltDSKKDINKLrrkVGMVFQQFNLFPHLTVLEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1319 LeVYA--AVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEG------IKRKLCFvlsilgNPSVVLLDEPSTGMDPE 1390
Cdd:COG1126 98 V-TLApiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGqqqrvaIARALAM------EPKVMLFDEPTSALDPE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1771853535 1391 gqqqMWQAIRATFRN-TERGA--LLTTHYMAEAEAVCDRVAIMVSGR 1434
Cdd:COG1126 171 ----LVGEVLDVMRDlAKEGMtmVVVTHEMGFAREVADRVVFMDGGR 213
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1247-1453 |
4.11e-13 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 70.81 E-value: 4.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1247 NVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-----SGGGDALEFL------GYCPQENALWPNLTV 1315
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfSKTPSDKAIRelrrnvGMVFQQYNLWPHLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1316 RQHL-EVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQ 1394
Cdd:PRK11124 100 QQNLiEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQ 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1771853535 1395 MWQAIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLK----SKFgKDYL 1453
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 ... |
1246-1440 |
4.40e-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: 4.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1246 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGS-----GGGDALEFLGYCPQENALWPNlTVRQHLE 1320
Cdd:cd03369 25 KNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIdistiPLEDLRSSLTIIPQDPTLFSG-TIRSNLD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1321 VYAavkglRKGDAEvaitrLVDALKlqdqLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIR 1400
Cdd:cd03369 104 PFD-----EYSDEE-----IYGALR----VSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1771853535 1401 ATFRNTergALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1440
Cdd:cd03369 170 EEFTNS---TILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1244-1453 |
4.63e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 71.17 E-value: 4.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1244 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGD------------------ALEFLGYCPQ 1305
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDfsklqgirklvgivfqnpETQFVGRTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1306 -------ENALWPNLTVRQHLEVYAAVKGLRKGdaevaitrlvdalklqdQLKSPvKTLSEGIKRKLCFVLSILGNPSVV 1378
Cdd:PRK13644 97 edlafgpENLCLPPIEIRKRVDRALAEIGLEKY-----------------RHRSP-KTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1771853535 1379 LLDEPSTGMDPEGQQQMWQAIRatfRNTERGALL--TTHYMAEAEAVcDRVAIMVSGRLRCIGSIQHLKSKFGKDYL 1453
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIK---KLHEKGKTIvyITHNLEELHDA-DRIIVMDRGKIVLEGEPENVLSDVSLQTL 231
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
438-594 |
4.68e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 70.13 E-value: 4.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 438 LKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADlENLSKLTGVCPQSNVQF-DflTVRE 516
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP-EIYRQQVSYCAQTPTLFgD--TVYD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 517 NLRLFAKIKGILPQE--VDKEIQRVLLELEM--KNIQDvlaqnLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRH 592
Cdd:PRK10247 100 NLIFPWQIRNQQPDPaiFLDDLERFALPDTIltKNIAE-----LSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKH 174
|
..
gi 1771853535 593 QV 594
Cdd:PRK10247 175 NV 176
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
443-588 |
5.78e-13 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 70.79 E-value: 5.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 443 FDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADlENLSKLTGVCPQSNVQ-FDFLTVRENL--- 518
Cdd:PRK11300 26 LEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPG-HQIARMGVVRTFQHVRlFREMTVIENLlva 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 519 -------RLFA---KIKGILPQEVDKeIQRVLLELEMKNIQDVL---AQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAG 585
Cdd:PRK11300 105 qhqqlktGLFSgllKTPAFRRAESEA-LDRAATWLERVGLLEHAnrqAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAG 183
|
...
gi 1771853535 586 LDP 588
Cdd:PRK11300 184 LNP 186
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
406-587 |
6.88e-13 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 73.24 E-value: 6.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 406 FEQAPPEFQG------KEAIRIRNVTKEYKGKPDKIeaLKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSV 479
Cdd:COG4618 312 LAAVPAEPERmplprpKGRLSVENLTVVPPGSKRPI--LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSV 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 480 TIynnklsEMADL-----ENLSKLTGVCPQsNVQ-FDFlTVRENLRLF-----------AKIKGI------LPQEVDKEI 536
Cdd:COG4618 390 RL------DGADLsqwdrEELGRHIGYLPQ-DVElFDG-TIAENIARFgdadpekvvaaAKLAGVhemilrLPDGYDTRI 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1771853535 537 qrvllelemkniqDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLD 587
Cdd:COG4618 462 -------------GEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLD 499
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1250-1415 |
7.69e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 69.49 E-value: 7.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1250 FCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG--SGGGDALEFLGYCPQENALWPNLTVRQHLEVYAAVKG 1327
Cdd:PRK13543 32 FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGktATRGDRSRFMAYLGHLPGLKADLSTLENLHFLCGLHG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1328 LRK----GDAeVAITRLVDalkLQDQLkspVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATF 1403
Cdd:PRK13543 112 RRAkqmpGSA-LAIVGLAG---YEDTL---VRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHL 184
|
170
....*....|..
gi 1771853535 1404 RnTERGALLTTH 1415
Cdd:PRK13543 185 R-GGGAALVTTH 195
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1247-1400 |
8.58e-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: 68.81 E-value: 8.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1247 NVSFCVRKGEVLGLLGHNGAGKSTSIKVITG--DTKPTAGQVLLKGSGGGDALE-FLGYCPQENALWPNLTVRQHLEVYA 1323
Cdd:cd03232 25 NISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLDKNFQrSTGYVEQQDVHSPNLTVREALRFSA 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1771853535 1324 AVKGLrkgdaevaitrlvdalklqdqlkspvkTLSEgiKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIR 1400
Cdd:cd03232 105 LLRGL---------------------------SVEQ--RKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLK 152
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
448-587 |
9.32e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 72.99 E-value: 9.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 448 GQITAILGHSGAGKSTLLNILSGL--SVPTKGSVTIYNNKLSemadlENLSKLTGVCPQSNVQFDFLTVRENLRLFAKIK 525
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRiqGNNFTGTILANNRKPT-----KQILKRTGFVTQDDILYPHLTVRETLVFCSLLR 168
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1771853535 526 giLPQEVDKEI-----QRVLLELEMKNIQDVLAQN-----LSGGQKRKLTFGIAILGDPQIFLLDEPTAGLD 587
Cdd:PLN03211 169 --LPKSLTKQEkilvaESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1226-1435 |
9.91e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 69.13 E-value: 9.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1226 KEYAGKRKgcfskrknkiATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSG----GGDALEFL- 1300
Cdd:PRK10908 9 KAYLGGRQ----------ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDitrlKNREVPFLr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1301 ---GYCPQENALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSV 1377
Cdd:PRK10908 79 rqiGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1771853535 1378 VLLDEPSTGMDPEgqqqMWQAIRATFRNTER---GALLTTHYMAEAEAVCDRVAIMVSGRL 1435
Cdd:PRK10908 159 LLADEPTGNLDDA----LSEGILRLFEEFNRvgvTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
419-638 |
1.00e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 70.04 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGS---VTIYNNKLSEMA----D 491
Cdd:PRK09984 5 IRVEKLAKTFNQH----QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAgshIELLGRTVQREGrlarD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 492 LENLSKLTGVCPQsnvQFDF---LTVRENLRLFAKikGILP----------QEVDKEIQRVLLELEMKNIQDVLAQNLSG 558
Cdd:PRK09984 81 IRKSRANTGYIFQ---QFNLvnrLSVLENVLIGAL--GSTPfwrtcfswftREQKQRALQALTRVGMVHFAHQRVSTLSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 559 GQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFST-QFMDEADILADRKVFLSQGKLKCAG 636
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDiNQNDGITVVVTlHQVDYALRYCERIVALRQGHVFYDG 235
|
..
gi 1771853535 637 SS 638
Cdd:PRK09984 236 SS 237
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1235-1447 |
1.09e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 70.02 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1235 CFSKRKN-KIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-----SGGGDALEFLGYCPQEna 1308
Cdd:PRK13632 14 SFSYPNSeNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGitiskENLKEIRKKIGIIFQN-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1309 lwPN-----LTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCfVLSILG-NPSVVLLDE 1382
Cdd:PRK13632 92 --PDnqfigATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVA-IASVLAlNPEIIIFDE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1771853535 1383 pSTGM-DPEGQQQMWQAIRATFRNTERGALLTTHYMAEAeAVCDRVAIMVSGRLRCIGSIQH-LKSK 1447
Cdd:PRK13632 169 -STSMlDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEiLNNK 233
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
444-623 |
1.11e-12 |
|
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: 69.74 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 444 DIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMadlenlskltgvcPQSnVQFDF-LTVRENLRLFA 522
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYK-------------PQY-IKADYeGTVRDLLSSIT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 523 KIKGILPQ-EVDkeiqrVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRhqvwnLLKER 601
Cdd:cd03237 87 KDFYTHPYfKTE-----IAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQR-----LMASK 156
|
170 180
....*....|....*....|....*....
gi 1771853535 602 KTDRVILF--STQFMDEADI-----LADR 623
Cdd:cd03237 157 VIRRFAENneKTAFVVEHDIimidyLADR 185
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1214-1434 |
1.19e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 69.57 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1214 DEKPVIIASCLRKEYaGKRKGCfskrknkiatRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGG 1293
Cdd:PRK11701 2 MDQPLLSVRGLTKLY-GPRKGC----------RDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1294 GDA-LEFLGYcPQENAL----WPnlTVRQHlevyaAVKGLRKG---DAEVAiTRL-----------------------VD 1342
Cdd:PRK11701 71 QLRdLYALSE-AERRRLlrteWG--FVHQH-----PRDGLRMQvsaGGNIG-ERLmavgarhygdiratagdwlerveID 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1343 ALKLQDQlksPvKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEA 1422
Cdd:PRK11701 142 AARIDDL---P-TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARL 217
|
250
....*....|..
gi 1771853535 1423 VCDRVAIMVSGR 1434
Cdd:PRK11701 218 LAHRLLVMKQGR 229
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
419-610 |
1.36e-12 |
|
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: 69.88 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKPDKIeaLKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLsVPTKGSVTIYNNKLSEMAdLENLSKL 498
Cdd:cd03289 3 MTVKDLTAKYTEGGNAV--LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWNSVP-LQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 TGVCPQSNVQFDFlTVRENLRLFAKIKgilpqevDKEIQRVLLELEMKNIQD--------VLAQN---LSGGQKRKLTFG 567
Cdd:cd03289 79 FGVIPQKVFIFSG-TFRKNLDPYGKWS-------DEEIWKVAEEVGLKSVIEqfpgqldfVLVDGgcvLSHGHKQLMCLA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1771853535 568 IAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFS 610
Cdd:cd03289 151 RSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILS 193
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1246-1440 |
1.47e-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: 68.67 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1246 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG---SGGG--DALEFLGYCPQEnalwPNL---TVRQ 1317
Cdd:cd03244 21 KNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiSKIGlhDLRSRISIIPQD----PVLfsgTIRS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1318 HL---------EVYAAVKglrkgdaEVAITRLVDAL--KLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTG 1386
Cdd:cd03244 97 NLdpfgeysdeELWQALE-------RVGLKEFVESLpgGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATAS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1771853535 1387 MDPEGQQQMWQAIRATFRNTergALLT-THYMaeaEAV--CDRVAIMVSGRLRCIGS 1440
Cdd:cd03244 170 VDPETDALIQKTIREAFKDC---TVLTiAHRL---DTIidSDRILVLDKGRVVEFDS 220
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1248-1443 |
1.48e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 71.87 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1248 VSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-----SGGGDALEF-LGYCPQ---ENALWPNLTVRQH 1318
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpidiRSPRDAIRAgIMLCPEdrkAEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1319 LEVYAAVKGLRKG----------DAEVAITRLvdALKLQDQlKSPVKTLSEGIKRKlcfvlSILG-----NPSVVLLDEP 1383
Cdd:PRK11288 352 INISARRHHLRAGclinnrweaeNADRFIRSL--NIKTPSR-EQLIMNLSGGNQQK-----AILGrwlseDMKVILLDEP 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1771853535 1384 STGMDPEGQQQMWQAIratFRNTERG--ALLTTHYMAEAEAVCDRVAIMVSGRLRciGSIQH 1443
Cdd:PRK11288 424 TRGIDVGAKHEIYNVI---YELAAQGvaVLFVSSDLPEVLGVADRIVVMREGRIA--GELAR 480
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
438-636 |
1.84e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 71.03 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 438 LKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLsEMADLENLSKLTGVCPQ-SNVQFDFlTVRE 516
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDV-EALSARAASRRVASVPQdTSLSFEF-DVRQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 517 NLRL--------FAKIKGILPQEVDKEIQRVllelEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDp 588
Cdd:PRK09536 97 VVEMgrtphrsrFDTWTETDRAAVERAMERT----GVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD- 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1771853535 589 fSRHQVWNLLKERK---TDRVILFSTQFMDEADILADRKVFLSQGKLKCAG 636
Cdd:PRK09536 172 -INHQVRTLELVRRlvdDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
421-641 |
1.89e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 70.52 E-value: 1.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 421 IRNVTKEYkGKPDKIEalkDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIynnklsemaDLENLSKLT- 499
Cdd:PRK11432 9 LKNITKRF-GSNTVID---NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFI---------DGEDVTHRSi 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 500 ---GVCP--QSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDP 574
Cdd:PRK11432 76 qqrDICMvfQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1771853535 575 QIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVI--LFSTQFMDEADILADRKVFLSQGKLKCAGS---------SLFL 641
Cdd:PRK11432 156 KVLLFDEPLSNLDANLRRSMREKIRELQQQFNItsLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSpqelyrqpaSRFM 233
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1244-1444 |
2.12e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 69.27 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1244 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsgGGDALEflgycpqENALWpnlTVRQHLE--- 1320
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITV----GGMVLS-------EETVW---DVRRQVGmvf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1321 -------VYAAVK-----GL--RKGDAEVAITRLVDALKL---QDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEP 1383
Cdd:PRK13635 88 qnpdnqfVGATVQddvafGLenIGVPREEMVERVDQALRQvgmEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1771853535 1384 STGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAeAVCDRVAIMVSGRLRCIGSIQHL 1444
Cdd:PRK13635 168 TSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEEGTPEEI 227
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1246-1435 |
2.21e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 68.30 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1246 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG------SGGGDAL---EFLGYCPQENALWPNLTVR 1316
Cdd:PRK11629 26 HNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpmsklSSAAKAElrnQKLGFIYQFHHLLPDFTAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1317 QHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMW 1396
Cdd:PRK11629 106 ENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIF 185
|
170 180 190
....*....|....*....|....*....|....*....
gi 1771853535 1397 QAIRATFRNTERGALLTTHYMAEAEAVcDRVAIMVSGRL 1435
Cdd:PRK11629 186 QLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRL 223
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1247-1444 |
2.99e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 70.13 E-value: 2.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1247 NVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGD-ALEFLGYCP--QENALWPNLTVRQHleVYA 1323
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHrSIQQRDICMvfQSYALFPHMSLGEN--VGY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1324 AVKGLRKGDAEVAiTRLVDALKLQDQL---KSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIR 1400
Cdd:PRK11432 102 GLKMLGVPKEERK-QRVKEALELVDLAgfeDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIR 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1771853535 1401 ATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL 1444
Cdd:PRK11432 181 ELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
417-608 |
3.16e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 71.38 E-value: 3.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 417 EAIRIRNVtkeykgkPDKIEalKDLV-------FDIY------EGQITAILGHSGAGKSTLLNILSGLSVPTKGSvtiYN 483
Cdd:PRK13409 64 DAISIVNL-------PEELE--EEPVhrygvngFKLYglpipkEGKVTGILGPNGIGKTTAVKILSGELIPNLGD---YE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 484 NKLSemADlENLSKLTGvcpqSNVQFDFLTVRENlrlfaKIKGIL-PQEVDKeIQRV-------LLE------------- 542
Cdd:PRK13409 132 EEPS--WD-EVLKRFRG----TELQNYFKKLYNG-----EIKVVHkPQYVDL-IPKVfkgkvreLLKkvdergkldevve 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1771853535 543 -LEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVIL 608
Cdd:PRK13409 199 rLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVL 265
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1246-1434 |
3.19e-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: 67.29 E-value: 3.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1246 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGqvlLKGS---GGGDALEF-------LGYCPQENALWPNLTV 1315
Cdd:cd03233 24 KDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVS---VEGDihyNGIPYKEFaekypgeIIYVSEEDVHFPTLTV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1316 RQHLEVYAAVKGlrkgdaevaitrlvdalklqDQLkspVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQM 1395
Cdd:cd03233 101 RETLDFALRCKG--------------------NEF---VRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1771853535 1396 WQAIRaTFRNTERGALLTTHYMA--EAEAVCDRVAIMVSGR 1434
Cdd:cd03233 158 LKCIR-TMADVLKTTTFVSLYQAsdEIYDLFDKVLVLYEGR 197
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1248-1388 |
3.52e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 68.04 E-value: 3.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1248 VSFCVRKGEVLGLLGHNGAGKSTSIKVITGdTKPTAGQVLLkgsgGGDALEFL---------GYCPQENALWPNLTVRQH 1318
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQF----AGQPLEAWsaaelarhrAYLSQQQTPPFAMPVFQY 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1771853535 1319 LEVYAAVkGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSIL-----GNPS--VVLLDEPSTGMD 1388
Cdd:PRK03695 90 LTLHQPD-KTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLqvwpdINPAgqLLLLDEPMNSLD 165
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
419-581 |
4.28e-12 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 70.69 E-value: 4.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKPDKIEALKDLV----------------FDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVtiy 482
Cdd:PRK13545 5 VKFEHVTKKYKMYNKPFDKLKDLFfrskdgeyhyalnnisFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 483 nnklsemaDLENLSKLTGVCPQSNVQfdfLTVRENLRLFAKIKGILPQEVDKEIQRVlleLEMKNIQDVLAQ---NLSGG 559
Cdd:PRK13545 82 --------DIKGSAALIAISSGLNGQ---LTGIENIELKGLMMGLTKEKIKEIIPEI---IEFADIGKFIYQpvkTYSSG 147
|
170 180
....*....|....*....|..
gi 1771853535 560 QKRKLTFGIAILGDPQIFLLDE 581
Cdd:PRK13545 148 MKSRLGFAISVHINPDILVIDE 169
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1246-1415 |
4.49e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 66.90 E-value: 4.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1246 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDAL----EFLGYCPQENALWPNLTVRQHlev 1321
Cdd:PRK13540 18 QQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLctyqKQLCFVGHRSGINPYLTLREN--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1322 yaAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRA 1401
Cdd:PRK13540 95 --CLYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQE 172
|
170
....*....|....
gi 1771853535 1402 tFRNTERGALLTTH 1415
Cdd:PRK13540 173 -HRAKGGAVLLTSH 185
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
408-632 |
4.66e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 70.39 E-value: 4.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 408 QAPPEFQgkeAIRIRNVTKEYkgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLS 487
Cdd:PRK10522 315 QAFPDWQ---TLELRNVTFAY---QDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 488 eMADLENLSKLtgvcpqsnvqfdFLTVRENLRLFAKIKGILPQEVDKEIQRVLLE-LEMKN---IQD--VLAQNLSGGQK 561
Cdd:PRK10522 389 -AEQPEDYRKL------------FSAVFTDFHLFDQLLGPEGKPANPALVEKWLErLKMAHkleLEDgrISNLKLSKGQK 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1771853535 562 RKLTFGIAILGDPQIFLLDEPTAGLDP-FSR---HQVWNLLKER-KTdrviLFSTQFMDEADILADRKVFLSQGKL 632
Cdd:PRK10522 456 KRLALLLALAEERDILLLDEWAADQDPhFRRefyQVLLPLLQEMgKT----IFAISHDDHYFIHADRLLEMRNGQL 527
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
391-632 |
5.08e-12 |
|
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: 70.60 E-value: 5.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 391 ALEDEMDADPSfHDSFEQAPPEFQGKEAIRIRNVTKEYKG-KPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILS 469
Cdd:COG4615 301 ELELALAAAEP-AAADAAAPPAPADFQTLELRGVTYRYPGeDGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLT 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 470 GLSVPTKGSVTIyNNKLSEMADLENLSKLTgvcpqSNVQFDFltvrenlRLFAKIKGILPQEVDKEIQRVLLELEMKN-- 547
Cdd:COG4615 380 GLYRPESGEILL-DGQPVTADNREAYRQLF-----SAVFSDF-------HLFDRLLGLDGEADPARARELLERLELDHkv 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 548 -IQD--VLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDP-FSR---HQVWNLLKER-KTdrVILFS--TQFMDea 617
Cdd:COG4615 447 sVEDgrFSTTDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPeFRRvfyTELLPELKARgKT--VIAIShdDRYFD-- 522
|
250
....*....|....*
gi 1771853535 618 diLADRKVFLSQGKL 632
Cdd:COG4615 523 --LADRVLKMDYGKL 535
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
417-600 |
5.09e-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: 70.58 E-value: 5.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 417 EAIRIRNVtkeykgkPDKIEalKDLV-------FDIY------EGQITAILGHSGAGKSTLLNILSGLSVPTKGsvtIYN 483
Cdd:COG1245 64 DAISIVNL-------PEELE--EDPVhrygengFRLYglpvpkKGKVTGILGPNGIGKSTALKILSGELKPNLG---DYD 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 484 NKLSEmaDlENLSKLTGvcpqSNVQFDFLTVRENlrlfaKIKGIL-PQEVDKeIQRV-------LLE------------- 542
Cdd:COG1245 132 EEPSW--D-EVLKRFRG----TELQDYFKKLANG-----EIKVAHkPQYVDL-IPKVfkgtvreLLEkvdergkldelae 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1771853535 543 -LEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE 600
Cdd:COG1245 199 kLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRE 257
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
420-587 |
5.20e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 68.03 E-value: 5.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 420 RIRNVTKEYKGkpdkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVtIYNNKLSEMADLENLSklt 499
Cdd:PRK11701 8 SVRGLTKLYGP----RKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV-HYRMRDGQLRDLYALS--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 500 gvcpQSNVQFDFLT----VRENL----------------RLFA---KIKGILPQEVDKEIQRVllELEMKNIQDvLAQNL 556
Cdd:PRK11701 80 ----EAERRRLLRTewgfVHQHPrdglrmqvsaggnigeRLMAvgaRHYGDIRATAGDWLERV--EIDAARIDD-LPTTF 152
|
170 180 190
....*....|....*....|....*....|.
gi 1771853535 557 SGGQKRKLTFGIAILGDPQIFLLDEPTAGLD 587
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLD 183
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1252-1431 |
5.22e-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: 70.58 E-value: 5.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1252 VRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSgggdalefLGYCPQEnalwpnLTVRQHLEVYAAVKGLRKG 1331
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK--------ISYKPQY------ISPDYDGTVEEFLRSANTD 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1332 DAEVAI--TRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERG 1409
Cdd:COG1245 429 DFGSSYykTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKT 508
|
170 180
....*....|....*....|..
gi 1771853535 1410 ALLTTHYMAEAEAVCDRvaIMV 1431
Cdd:COG1245 509 AMVVDHDIYLIDYISDR--LMV 528
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
417-633 |
5.81e-12 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 67.92 E-value: 5.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 417 EAIRIRNVTKEY----------------KGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVT 480
Cdd:PRK13546 3 VSVNIKNVTKEYriyrtnkermkdalipKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 481 iYNNKLSEMADLENLS-KLTGVcpqSNVQFDFLTVrenlrlfakikGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGG 559
Cdd:PRK13546 83 -RNGEVSVIAISAGLSgQLTGI---ENIEFKMLCM-----------GFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1771853535 560 QKRKLTFGIAILGDPQIFLLDEP-TAGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEADILADRKVFLSQGKLK 633
Cdd:PRK13546 148 MRAKLGFSINITVNPDILVIDEAlSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLK 222
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
421-610 |
5.86e-12 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 71.09 E-value: 5.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 421 IRNVTKEYKGKPDKIeaLKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLsVPTKGSVTIYNNKLSEMAdLENLSKLTG 500
Cdd:TIGR01271 1220 VQGLTAKYTEAGRAV--LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSVT-LQTWRKAFG 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 501 VCPQSNVQFDFlTVRENLRLFAkikgilpQEVDKEIQRVLLELEMKNIQD--------VLAQN---LSGGQKRKLTFGIA 569
Cdd:TIGR01271 1296 VIPQKVFIFSG-TFRKNLDPYE-------QWSDEEIWKVAEEVGLKSVIEqfpdkldfVLVDGgyvLSNGHKQLMCLARS 1367
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1771853535 570 ILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFS 610
Cdd:TIGR01271 1368 ILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILS 1408
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1242-1434 |
5.88e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 67.80 E-value: 5.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1242 KIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGsgggdalEFLGYCPQEN-ALW---------- 1310
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDG-------KDVTKLPEYKrAKYigrvfqdpmm 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1311 ---PNLTVRQHLEVyAAVKGLRKG------DAEVAITRlvDALK-----LQDQLKSPVKTLSEGIKRKLCFVLSILGNPS 1376
Cdd:COG1101 92 gtaPSMTIEENLAL-AYRRGKRRGlrrgltKKRRELFR--ELLAtlglgLENRLDTKVGLLSGGQRQALSLLMATLTKPK 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1771853535 1377 VVLLDEPSTGMDPEGQQQMwqaIRATFRNTERG---ALLTTHYMAEAEAVCDRVAIMVSGR 1434
Cdd:COG1101 169 LLLLDEHTAALDPKTAALV---LELTEKIVEENnltTLMVTHNMEQALDYGNRLIMMHEGR 226
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
440-588 |
6.15e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 67.87 E-value: 6.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 440 DLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMA--DLENLSKLTGVCPQSNVQFDFLTVREN 517
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsRLYTVRKRMSMLFQSGALFTDMNVFDN 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1771853535 518 LRLFAKIKGILPQEVDKEIqrVLLELE---MKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDP 588
Cdd:PRK11831 105 VAYPLREHTQLPAPLLHST--VMMKLEavgLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDP 176
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
416-608 |
6.48e-12 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 70.05 E-value: 6.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 416 KEAIRIRNVTKEYKGKpdKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMAdLENL 495
Cdd:PRK11176 339 KGDIEFRNVTFTYPGK--EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYT-LASL 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 496 SKLTGVCPQsNVQFDFLTVRENLrLFAKiKGILPQEVDKEIQRVLLELE----MKNIQD-VLAQN---LSGGQKRKLTFG 567
Cdd:PRK11176 416 RNQVALVSQ-NVHLFNDTIANNI-AYAR-TEQYSREQIEEAARMAYAMDfinkMDNGLDtVIGENgvlLSGGQRQRIAIA 492
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1771853535 568 IAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVIL 608
Cdd:PRK11176 493 RALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSL 533
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1257-1440 |
7.53e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 67.72 E-value: 7.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1257 VLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGsgggDALEFlgycpQENALwpnLTVRQHLEV----------YAAVK 1326
Cdd:PRK13638 29 VTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQG----KPLDY-----SKRGL---LALRQQVATvfqdpeqqifYTDID 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1327 G-----LRK-GDAEVAITRLVD-ALKLQDQL---KSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMW 1396
Cdd:PRK13638 97 SdiafsLRNlGVPEAEITRRVDeALTLVDAQhfrHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1771853535 1397 QAIRATFRNTERgALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1440
Cdd:PRK13638 177 AIIRRIVAQGNH-VIISSHDIDLIYEISDAVYVLRQGQILTHGA 219
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
419-638 |
7.63e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 67.51 E-value: 7.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKP-----DKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLsEMADLE 493
Cdd:PRK15112 5 LEVRNLSKTFRYRTgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 494 NLSKL---------TGVCPQSNVQ--FDFltvreNLRLFAKIKgilPQEVDKEIQRVLLELEMKNIQ-DVLAQNLSGGQK 561
Cdd:PRK15112 84 YRSQRirmifqdpsTSLNPRQRISqiLDF-----PLRLNTDLE---PEQREKQIIETLRQVGLLPDHaSYYPHMLAPGQK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1771853535 562 RKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVI--LFSTQFMDEADILADRKVFLSQGKLKCAGSS 638
Cdd:PRK15112 156 QRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHLGMMKHISDQVLVMHQGEVVERGST 234
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1239-1433 |
7.87e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.60 E-value: 7.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1239 RKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDALE--FLGYCPQ-ENALWPNLTV 1315
Cdd:PRK15056 17 RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQknLVAYVPQsEEVDWSFPVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1316 RQHLEV---YAAVKGLRKGDA------EVAITRlVDALKLQDQlksPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTG 1386
Cdd:PRK15056 97 VEDVVMmgrYGHMGWLRRAKKrdrqivTAALAR-VDMVEFRHR---QIGELSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1771853535 1387 MDPEGQQQMWQAIRaTFRNTERGALLTTHYMAEAEAVCDrVAIMVSG 1433
Cdd:PRK15056 173 VDVKTEARIISLLR-ELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKG 217
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1246-1435 |
9.10e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 69.65 E-value: 9.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1246 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG------------SGG---------GDALeFLGYCP 1304
Cdd:PRK10762 269 NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGhevvtrspqdglANGivyisedrkRDGL-VLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1305 QENAlwpNLTVRQHLEvYAAVKgLRKGDAEVAITRLVDALKL----QDQlksPVKTLSEGIKRKLCFVLSILGNPSVVLL 1380
Cdd:PRK10762 348 KENM---SLTALRYFS-RAGGS-LKHADEQQAVSDFIRLFNIktpsMEQ---AIGLLSGGNQQKVAIARGLMTRPKVLIL 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1771853535 1381 DEPSTGMDPEGQQQMWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1435
Cdd:PRK10762 420 DEPTRGVDVGAKKEIYQLIN-QFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1246-1415 |
9.33e-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: 9.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1246 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsggGDALEFlGYCPQenalwpnltvrqhlevyaav 1325
Cdd:cd03221 17 KDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-----GSTVKI-GYFEQ-------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1326 kglrkgdaevaitrlvdalklqdqlkspvktLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQqqmwQAIRATFRN 1405
Cdd:cd03221 71 -------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESI----EALEEALKE 115
|
170
....*....|
gi 1771853535 1406 TERGALLTTH 1415
Cdd:cd03221 116 YPGTVILVSH 125
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1252-1431 |
1.24e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 69.45 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1252 VRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVL--LKGSgggdaleflgYCPQENALWPNLTVRQHLEvyAAVKGLr 1329
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDpeLKIS----------YKPQYIKPDYDGTVEDLLR--SITDDL- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1330 kgDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERG 1409
Cdd:PRK13409 429 --GSSYYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREAT 506
|
170 180
....*....|....*....|..
gi 1771853535 1410 ALLTTHYMAEAEAVCDRvaIMV 1431
Cdd:PRK13409 507 ALVVDHDIYMIDYISDR--LMV 526
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1239-1435 |
1.24e-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: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1239 RKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGS--GGGDALEF----LGYCPQE---NAL 1309
Cdd:COG3845 268 DRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEdiTGLSPRERrrlgVAYIPEDrlgRGL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1310 WPNLTVRQHL-----EVYAAVKG--LRKGDAEVAITRLVDALKLQ-DQLKSPVKTLSEGIKRKlcFVLS--ILGNPSVVL 1379
Cdd:COG3845 348 VPDMSVAENLilgryRRPPFSRGgfLDRKAIRAFAEELIEEFDVRtPGPDTPARSLSGGNQQK--VILAreLSRDPKLLI 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1771853535 1380 LDEPSTGMDPEGQQQMWQAIRATfRNteRGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1435
Cdd:COG3845 426 AAQPTRGLDVGAIEFIHQRLLEL-RD--AGAavLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
406-587 |
1.57e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 68.77 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 406 FEQAPPEFqgKEAIRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVtiynnK 485
Cdd:PRK15064 309 FEQDKKLH--RNALEVENLTKGFDNGP----LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-----K 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 486 LSEMADLenlskltGVCPQSNVQfDF---LTVRENLRLFAKikgilPQEVDKEIQRVLLELEMKNiQDVL--AQNLSGGQ 560
Cdd:PRK15064 378 WSENANI-------GYYAQDHAY-DFendLTLFDWMSQWRQ-----EGDDEQAVRGTLGRLLFSQ-DDIKksVKVLSGGE 443
|
170 180
....*....|....*....|....*..
gi 1771853535 561 KRKLTFGIAILGDPQIFLLDEPTAGLD 587
Cdd:PRK15064 444 KGRMLFGKLMMQKPNVLVMDEPTNHMD 470
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
419-587 |
1.60e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 66.29 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVtiynnklsemadlENLSKL 498
Cdd:PRK09544 5 VSLENVSVSFGQR----RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-------------KRNGKL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 -TGVCPQsNVQFDF---LTVRENLRLFAKIKG--ILPQevdkeIQRV----LLELEMkniqdvlaQNLSGGQKRKLTFGI 568
Cdd:PRK09544 68 rIGYVPQ-KLYLDTtlpLTVNRFLRLRPGTKKedILPA-----LKRVqaghLIDAPM--------QKLSGGETQRVLLAR 133
|
170
....*....|....*....
gi 1771853535 569 AILGDPQIFLLDEPTAGLD 587
Cdd:PRK09544 134 ALLNRPQLLVLDEPTQGVD 152
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1244-1444 |
1.89e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 68.73 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1244 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQV-----------------------LLKGSGGGD-ALEF 1299
Cdd:PRK10261 31 AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqvielseqsaaQMRHVRGADmAMIF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1300 lgycpQE--NALWPNLTV-RQHLEVYAAVKGLRKGDAEVAITRLVDALKL---QDQLKSPVKTLSEGIKRKLCFVLSILG 1373
Cdd:PRK10261 111 -----QEpmTSLNPVFTVgEQIAESIRLHQGASREEAMVEAKRMLDQVRIpeaQTILSRYPHQLSGGMRQRVMIAMALSC 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1771853535 1374 NPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL 1444
Cdd:PRK10261 186 RPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
411-633 |
2.06e-11 |
|
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: 68.31 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 411 PEFQGKEAIRIRNVTKEYKGKPdKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGlSVPTK--GSVTIYNNKLSE 488
Cdd:TIGR02633 250 PHEIGDVILEARNLTCWDVINP-HRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFG-AYPGKfeGNVFINGKPVDI 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 489 MADLENLS----------KLTGVCPQsnvqfdfLTVRENLRL-----FAKIKGILPQEVDKEIQRVLLELEMKNIQDVLA 553
Cdd:TIGR02633 328 RNPAQAIRagiamvpedrKRHGIVPI-------LGVGKNITLsvlksFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLP 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 554 -QNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQfMDEADILADRKVFLSQG 630
Cdd:TIGR02633 401 iGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlaQEGVAIIVVSSE-LAEVLGLSDRVLVIGEG 479
|
...
gi 1771853535 631 KLK 633
Cdd:TIGR02633 480 KLK 482
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
415-632 |
2.39e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 68.27 E-value: 2.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 415 GKEAIRIRNVTKEYKGKpdkieaLKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLEN 494
Cdd:PRK09700 262 HETVFEVRNVTSRDRKK------VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 495 LSKLTGVCPQS---NVQFDFLTVRENLRLFAKIK--------GILPQEVDKEI---QRVLLELEMKNIQdvlaQN---LS 557
Cdd:PRK09700 336 VKKGMAYITESrrdNGFFPNFSIAQNMAISRSLKdggykgamGLFHEVDEQRTaenQRELLALKCHSVN----QNiteLS 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1771853535 558 GGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTD-RVILFSTQFMDEADILADRKVFLSQGKL 632
Cdd:PRK09700 412 GGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
448-587 |
2.80e-11 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 65.63 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 448 GQITAILGHSGAGKSTLLNILSGLSvPTKGSVTIYNNKLSEMaDLENLSKLTGVCPQSNVQFDFLTVRENLRLFAKikgi 527
Cdd:COG4138 22 GELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDW-SAAELARHRAYLSQQQSPPFAMPVFQYLALHQP---- 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1771853535 528 lPQEVDKEIQRVLLEL-EMKNIQDVLAQN---LSGG--QKRKLTfgiAIL--------GDPQIFLLDEPTAGLD 587
Cdd:COG4138 96 -AGASSEAVEQLLAQLaEALGLEDKLSRPltqLSGGewQRVRLA---AVLlqvwptinPEGQLLLLDEPMNSLD 165
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
410-587 |
3.07e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 68.61 E-value: 3.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 410 PPEFQGKEAIRIRNVTKEYKgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEM 489
Cdd:PLN03130 1229 PPGWPSSGSIKFEDVVLRYR--PELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKF 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 490 AdLENLSKLTGVCPQSNVQFDFlTVRENLRLFAKIKgilpqEVDkeiqrvLLE-LEMKNIQDVL--------------AQ 554
Cdd:PLN03130 1307 G-LMDLRKVLGIIPQAPVLFSG-TVRFNLDPFNEHN-----DAD------LWEsLERAHLKDVIrrnslgldaevseaGE 1373
|
170 180 190
....*....|....*....|....*....|...
gi 1771853535 555 NLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLD 587
Cdd:PLN03130 1374 NFSVGQRQLLSLARALLRRSKILVLDEATAAVD 1406
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1252-1435 |
3.47e-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: 3.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1252 VRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLL--------KGSGGGDAL-----EFLGYCPQENALWPNLTVRQH 1318
Cdd:PRK11264 26 VKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidtaRSLSQQKGLirqlrQHVGFVFQNFNLFPHRTVLEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1319 -LEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQ 1397
Cdd:PRK11264 106 iIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLN 185
|
170 180 190
....*....|....*....|....*....|....*...
gi 1771853535 1398 AIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1435
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 ... |
1235-1449 |
3.78e-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: 3.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1235 CFSKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsGGGD----ALEFL----GYCPQE 1306
Cdd:cd03253 7 TFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILI---DGQDirevTLDSLrraiGVVPQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1307 NALWpNLTVRQHL----------EVYAAVKglrKGDAEVAITRLVDA---------LKlqdqlkspvktLSEGIKRKLCF 1367
Cdd:cd03253 84 TVLF-NDTIGYNIrygrpdatdeEVIEAAK---AAQIHDKIMRFPDGydtivgergLK-----------LSGGEKQRVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1368 VLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNteRGALLTTHYMAEAeAVCDRVAIMVSGRLRCIGSIQHLKSK 1447
Cdd:cd03253 149 ARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKG--RTTIVIAHRLSTI-VNADKIIVLKDGRIVERGTHEELLAK 225
|
..
gi 1771853535 1448 FG 1449
Cdd:cd03253 226 GG 227
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
419-625 |
3.86e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 65.48 E-value: 3.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYK-----GKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNnklsemADLE 493
Cdd:PRK10419 4 LNVSGLSHHYAhgglsGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRG------EPLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 494 NLSK-----------------LTGVCPQSNVQFdflTVRENLRlfaKIKGILPQEVDKEIQRVLLELEMK-NIQDVLAQN 555
Cdd:PRK10419 78 KLNRaqrkafrrdiqmvfqdsISAVNPRKTVRE---IIREPLR---HLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 556 LSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQ-------------FMDEADIL 620
Cdd:PRK10419 152 LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKlqQQFGTACLFITHdlrlverfcqrvmVMDNGQIV 231
|
....*
gi 1771853535 621 ADRKV 625
Cdd:PRK10419 232 ETQPV 236
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
438-622 |
4.40e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 65.23 E-value: 4.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 438 LKDLVFDIYEGQITAILGHSGAGKSTLLNILSG--------LSVPTKGSVTIYNNKLSEMaDLENLSKLTGVCPQ-SNVQ 508
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltgggapRGARVTGDVTLNGEPLAAI-DAPRLARLRAVLPQaAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 509 FDFlTVRENLRL----FAKIKGILPQEvDKEIQRVLLEL---EMKNIQDVlaQNLSGGQKRKLTFGIAI---------LG 572
Cdd:PRK13547 96 FAF-SAREIVLLgrypHARRAGALTHR-DGEIAWQALALagaTALVGRDV--TTLSGGELARVQFARVLaqlwpphdaAQ 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 573 DPQIFLLDEPTAGLDPFSRHQV----------WNL----------LKERKTDRVILFStqfmdEADILAD 622
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLldtvrrlardWNLgvlaivhdpnLAARHADRIAMLA-----DGAIVAH 236
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1214-1290 |
5.02e-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: 5.02e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1771853535 1214 DEKPVIIASCLRKEYAgKRKGCFSKRKNKI-ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG 1290
Cdd:COG4608 3 MAEPLLEVRDLKKHFP-VRGGLFGRTVGVVkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDG 79
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1246-1390 |
5.13e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 67.22 E-value: 5.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1246 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVllKGSGGGDalefLGYCPQENALW--PNLTVRQHLEVYA 1323
Cdd:PRK15064 336 KNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV--KWSENAN----IGYYAQDHAYDfeNDLTLFDWMSQWR 409
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1771853535 1324 avkglRKGDAEVAIT----RLvdaLKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1390
Cdd:PRK15064 410 -----QEGDDEQAVRgtlgRL---LFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDME 472
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1246-1435 |
6.53e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 64.34 E-value: 6.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1246 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKP----TAGQVLLKG------SGGGDALEFLGYCPQeNALWPNLTV 1315
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGkpvapcALRGRKIATIMQNPR-SAFNPLHTM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1316 RQHLEVYAAVKGLRKGDAevAITRLVDALKLQDQ---LKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQ 1392
Cdd:PRK10418 99 HTHARETCLALGKPADDA--TLTAALEAVGLENAarvLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQ 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1771853535 1393 QQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1435
Cdd:PRK10418 177 ARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1255-1444 |
6.67e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 64.81 E-value: 6.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1255 GEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGS--GGGDALEF---LGYCPQENALWPNLTVRQHLEV-----YAA 1324
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQplESWSSKAFarkVAYLPQQLPAAEGMTVRELVAIgrypwHGA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1325 VKGLRKGD---AEVAITrLVDALKLQDQLkspVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRA 1401
Cdd:PRK10575 117 LGRFGAADrekVEEAIS-LVGLKPLAHRL---VDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHR 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1771853535 1402 TFRntERGALLTT--HYMAEAEAVCDRVAIMVSGRLRCIGSIQHL 1444
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 ... |
1240-1448 |
6.69e-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: 6.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1240 KNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITG--DTKPTAGQVLLKGS-----GGGDALEFLGY-CP------- 1304
Cdd:TIGR03269 11 DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYHVAlcekcGYVERPSKVGEpCPvcggtle 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1305 -QENALW-PNLTVRQHLEVYAAVKGLRK----GD-----------------AEVAITR---LVDALKLQDQLKSPVKTLS 1358
Cdd:TIGR03269 91 pEEVDFWnLSDKLRRRIRKRIAIMLQRTfalyGDdtvldnvlealeeigyeGKEAVGRavdLIEMVQLSHRITHIARDLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1359 EGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCI 1438
Cdd:TIGR03269 171 GGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIKEE 250
|
250
....*....|
gi 1771853535 1439 GSIQHLKSKF 1448
Cdd:TIGR03269 251 GTPDEVVAVF 260
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1221-1450 |
6.72e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 64.71 E-value: 6.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1221 ASCLRKEYAGKrkGCFSKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGS-----GGGD 1295
Cdd:PRK10419 6 VSGLSHHYAHG--GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEplaklNRAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1296 ALEF-----LGYCPQENALWPNLTVRQHL-EVYAAVKGLRKGDAEVAITRLVDALKLQDQL--KSPvKTLSEGIKRKLCF 1367
Cdd:PRK10419 84 RKAFrrdiqMVFQDSISAVNPRKTVREIIrEPLRHLLSLDKAERLARASEMLRAVDLDDSVldKRP-PQLSGGQLQRVCL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1368 VLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL---RCIGSIQHL 1444
Cdd:PRK10419 163 ARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIvetQPVGDKLTF 242
|
....*.
gi 1771853535 1445 KSKFGK 1450
Cdd:PRK10419 243 SSPAGR 248
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
441-588 |
7.11e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 63.71 E-value: 7.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 441 LVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIyNNKLSEMAD----LENLSKLTGVCPQsnvqfdfLTVRE 516
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQI-DGKTATRGDrsrfMAYLGHLPGLKAD-------LSTLE 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1771853535 517 NLRLFAKIKGILPQEVDKEiqrVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDP 588
Cdd:PRK13543 102 NLHFLCGLHGRRAKQMPGS---ALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
439-600 |
7.89e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 64.62 E-value: 7.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 439 KDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLEnLSKLTGVCPQSNVQFDFLTVREnl 518
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKE-VARRIGLLAQNATTPGDITVQE-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 519 rLFAkiKGILPQEV------DKEIQRVLLELEMKNIQDVLAQN---LSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPF 589
Cdd:PRK10253 101 -LVA--RGRYPHQPlftrwrKEDEEAVTKAMQATGITHLADQSvdtLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS 177
|
170
....*....|.
gi 1771853535 590 SRHQVWNLLKE 600
Cdd:PRK10253 178 HQIDLLELLSE 188
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
419-637 |
9.06e-11 |
|
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: 62.93 E-value: 9.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLS--VPTKGSVTIYNNKLSEMADLENLS 496
Cdd:cd03217 1 LEIKDLHVSVGGK----EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 497 KLTGVCPQSNVQFDFLTVRENLRlfakikgilpqEVDKeiqrvllelemkniqdvlaqNLSGGQKRKLTFGIAILGDPQI 576
Cdd:cd03217 77 LGIFLAFQYPPEIPGVKNADFLR-----------YVNE--------------------GFSGGEKKRNEILQLLLLEPDL 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1771853535 577 FLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEAD-ILADRKVFLSQGKLKCAGS 637
Cdd:cd03217 126 AILDEPDSGLDIDALRLVAEVINKlREEGKSVLIITHYQRLLDyIKPDRVHVLYDGRIVKSGD 188
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1246-1487 |
9.53e-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: 9.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1246 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITgDTKPTAGQVLLKG-SGGGDALE----FLGYCPQENALWPNlTVRQHLE 1320
Cdd:cd03289 21 ENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGvSWNSVPLQkwrkAFGVIPQKVFIFSG-TFRKNLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1321 VYAAVKG--LRKGDAEVAITRLVDAL--KLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPegqqQMW 1396
Cdd:cd03289 99 PYGKWSDeeIWKVAEEVGLKSVIEQFpgQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP----ITY 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1397 QAIRATFRNTERGA--LLTTHYMaEAEAVCDRVAIMVSGRLRCIGSIQHLKSKfgkdyllemkvKNLAQVEPLHAEILRL 1474
Cdd:cd03289 175 QVIRKTLKQAFADCtvILSEHRI-EAMLECQRFLVIEENKVRQYDSIQKLLNE-----------KSHFKQAISPSDRLKL 242
|
250
....*....|...
gi 1771853535 1475 FPQAARQERYSSL 1487
Cdd:cd03289 243 FPRRNSSKSKRKP 255
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
401-632 |
1.01e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 66.20 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 401 SFHDSFEQAPPEfQGKEAIRIRNVTKEykgkpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVT 480
Cdd:COG1129 240 ELEDLFPKRAAA-PGEVVLEVEGLSVG--------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIR 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 481 IyNNKlsemaDLENLS----------------KLTGVCPQsnvqfdfLTVREN-----LRLFAKIKGILPQEVDKEIQRV 539
Cdd:COG1129 311 L-DGK-----PVRIRSprdairagiayvpedrKGEGLVLD-------LSIRENitlasLDRLSRGGLLDRRRERALAEEY 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 540 LLELEMK--NIqDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERkTDR---VILFSTQfM 614
Cdd:COG1129 378 IKRLRIKtpSP-EQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIREL-AAEgkaVIVISSE-L 454
|
250
....*....|....*...
gi 1771853535 615 DEADILADRKVFLSQGKL 632
Cdd:COG1129 455 PELLGLSDRILVMREGRI 472
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
419-594 |
1.17e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.59 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKPDkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSV------------------- 479
Cdd:PTZ00265 383 IQFKNVRFHYDTRKD-VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIiindshnlkdinlkwwrsk 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 480 -------------TIYNN---KLSEMADLENLSKLTGvcPQSNVQFDFLTVRENLRlfAKIKGILPQEVDKEIQRVLLEL 543
Cdd:PTZ00265 462 igvvsqdpllfsnSIKNNikySLYSLKDLEALSNYYN--EDGNDSQENKNKRNSCR--AKCAGDLNDMSNTTDSNELIEM 537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 544 --EMKNIQD---------VL-------------------AQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQ 593
Cdd:PTZ00265 538 rkNYQTIKDsevvdvskkVLihdfvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYL 617
|
.
gi 1771853535 594 V 594
Cdd:PTZ00265 618 V 618
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
1243-1388 |
1.28e-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: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1243 IATR--NVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTkPTAGQVLLkgsgGGDALE---------FLGYCPQENALWP 1311
Cdd:COG4138 8 VAGRlgPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILL----NGRPLSdwsaaelarHRAYLSQQQSPPF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1312 NLTVRQHLEVYAAvKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSIL-----GNPS--VVLLDEPS 1384
Cdd:COG4138 83 AMPVFQYLALHQP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptINPEgqLLLLDEPM 161
|
....
gi 1771853535 1385 TGMD 1388
Cdd:COG4138 162 NSLD 165
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
404-637 |
1.31e-10 |
|
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: 66.51 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 404 DSFEQAPPEFQGKEAIRIRNVTKEY-KGKPdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILsglsvptkgsvtiy 482
Cdd:TIGR00957 622 DSIERRTIKPGEGNSITVHNATFTWaRDLP---PTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL-------------- 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 483 nnkLSEMADLENLSKLTG----VCPQSNVQFDflTVRENLrLFAKikGILPQEVDKEIQR--VLLELEMKNIQDVL---- 552
Cdd:TIGR00957 685 ---LAEMDKVEGHVHMKGsvayVPQQAWIQND--SLRENI-LFGK--ALNEKYYQQVLEAcaLLPDLEILPSGDRTeige 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 553 -AQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWN-------LLKErKTDRVILFSTQFMDEADILadrk 624
Cdd:TIGR00957 757 kGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEhvigpegVLKN-KTRILVTHGISYLPQVDVI---- 831
|
250
....*....|...
gi 1771853535 625 VFLSQGKLKCAGS 637
Cdd:TIGR00957 832 IVMSGGKISEMGS 844
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
431-600 |
1.52e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 64.34 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 431 KPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLSKltgvcpQSNVQFD 510
Cdd:PRK15079 30 PPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAV------RSDIQMI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 511 F----------LTV----RENLRLF-AKIKGilpQEVDKEIQRVLLELEM-KNIQDVLAQNLSGGQKRKLtfGIA---IL 571
Cdd:PRK15079 104 FqdplaslnprMTIgeiiAEPLRTYhPKLSR---QEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRI--GIAralIL 178
|
170 180
....*....|....*....|....*....
gi 1771853535 572 gDPQIFLLDEPTAGLDPFSRHQVWNLLKE 600
Cdd:PRK15079 179 -EPKLIICDEPVSALDVSIQAQVVNLLQQ 206
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1249-1446 |
1.84e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 62.68 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1249 SFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDA--------LEFlgycpQENALWPNLTVRQH-- 1318
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTppsrrpvsMLF-----QENNLFSHLTVAQNig 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1319 ------LEVYAAVKGLRKGDAE-VAITRLVDALKLQdqlkspvktLSEGIKRKL----CFVLSilgNPsVVLLDEPSTGM 1387
Cdd:PRK10771 94 lglnpgLKLNAAQREKLHAIARqMGIEDLLARLPGQ---------LSGGQRQRValarCLVRE---QP-ILLLDEPFSAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1771853535 1388 DPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKS 1446
Cdd:PRK10771 161 DPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1257-1446 |
1.88e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 63.58 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1257 VLGLLGHNGAGKSTSIKVITGDTKPTAG-----QVLLKGSG---GGDALEF---LGYCPQENALWPnLTVRQHleVYAAV 1325
Cdd:PRK14271 49 VTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSifnYRDVLEFrrrVGMLFQRPNPFP-MSIMDN--VLAGV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1326 KGLR-------KGDAEVAITR--LVDALKlqDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMW 1396
Cdd:PRK14271 126 RAHKlvprkefRGVAQARLTEvgLWDAVK--DRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIE 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1397 QAIRATFRNTErgALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKS 1446
Cdd:PRK14271 204 EFIRSLADRLT--VIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
408-684 |
2.01e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.15 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 408 QAPPEFQGKEAIRIRNVTKEYKGKPDKiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSG-LSVPTKGSVTIYNNkl 486
Cdd:PLN03232 604 QNPPLQPGAPAISIKNGYFSWDSKTSK-PTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRGS-- 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 487 semadlenlsklTGVCPQSNVQFDfLTVRENLRLFAKI------KGI----LPQEVDKEIQRVLLELEMKNIqdvlaqNL 556
Cdd:PLN03232 681 ------------VAYVPQVSWIFN-ATVRENILFGSDFeserywRAIdvtaLQHDLDLLPGRDLTEIGERGV------NI 741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 557 SGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWN-LLKER---KTDRVILFSTQFMDeadiLADRKVFLSQGKL 632
Cdd:PLN03232 742 SGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDsCMKDElkgKTRVLVTNQLHFLP----LMDRIILVSEGMI 817
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1771853535 633 KCAG-------SSLFLKKKWGIGYHLSLQLNEICVEENITSL---VKQHIPDAKLSAKSEGK 684
Cdd:PLN03232 818 KEEGtfaelskSGSLFKKLMENAGKMDATQEVNTNDENILKLgptVTIDVSERNLGSTKQGK 879
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1244-1481 |
2.66e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 62.83 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1244 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGggdaleflgyCPQENALWpnltVRQHL---- 1319
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGRE----------VNAENEKW----VRSKVglvf 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1320 -----EVYAAV-----------KGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEP 1383
Cdd:PRK13647 86 qdpddQVFSSTvwddvafgpvnMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1384 STGMDPEGQQQMwQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGsiqhlkskfGKDYLLEMKVKNLAQ 1463
Cdd:PRK13647 166 MAYLDPRGQETL-MEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG---------DKSLLTDEDIVEQAG 235
|
250
....*....|....*....
gi 1771853535 1464 VE-PLHAEILRLFPQAARQ 1481
Cdd:PRK13647 236 LRlPLVAQIFEDLPELGQS 254
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
421-587 |
2.69e-10 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 62.39 E-value: 2.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 421 IRNVTKEYKGKPdkIeaLKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSV--PTKGSVTIYNNKLSEMaDLENLSKL 498
Cdd:COG0396 3 IKNLHVSVEGKE--I--LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILEL-SPDERARA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 tGV--CPQSNVQFDFLTVRENLRLFAKIKG---ILPQEVDKEIQRVLLELEMKniQDVLAQNL----SGGQKRKL-TFGI 568
Cdd:COG0396 78 -GIflAFQYPVEIPGVSVSNFLRTALNARRgeeLSAREFLKLLKEKMKELGLD--EDFLDRYVnegfSGGEKKRNeILQM 154
|
170
....*....|....*....
gi 1771853535 569 AILgDPQIFLLDEPTAGLD 587
Cdd:COG0396 155 LLL-EPKLAILDETDSGLD 172
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1218-1390 |
2.93e-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: 2.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1218 VIIASCLRKEYAGKrkgcfskrknkIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsggGDAL 1297
Cdd:TIGR03719 322 VIEAENLTKAFGDK-----------LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-----GETV 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1298 EfLGYCPQE-NALWPNLTVRQhlEVYAAVKGLRKGDAEVAITRLVDA--LKLQDQLKsPVKTLSEGIKRKLCFVLSILGN 1374
Cdd:TIGR03719 386 K-LAYVDQSrDALDPNKTVWE--EISGGLDIIKLGKREIPSRAYVGRfnFKGSDQQK-KVGQLSGGERNRVHLAKTLKSG 461
|
170
....*....|....*.
gi 1771853535 1375 PSVVLLDEPSTGMDPE 1390
Cdd:TIGR03719 462 GNVLLLDEPTNDLDVE 477
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1244-1435 |
3.47e-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: 3.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1244 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGD------ALEFLGYCPQENALWPNLTVRQ 1317
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwqtakiMREAVAIVPEGRRVFSRMTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1318 HLevyaAVKGL--RKGDAEVAITRLVDAL-KLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQ 1394
Cdd:PRK11614 100 NL----AMGGFfaERDQFQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQ 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1771853535 1395 MWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1435
Cdd:PRK11614 176 IFDTIE-QLREQGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
438-632 |
4.06e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 64.25 E-value: 4.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 438 LKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLSklTGVCPQS-NVQFDFL---- 512
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLA--NGIVYISeDRKRDGLvlgm 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 513 TVREN-----LRLFAKIKGILPQevDKEIQRVLLELEMKNI----QDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPT 583
Cdd:PRK10762 346 SVKENmsltaLRYFSRAGGSLKH--ADEQQAVSDFIRLFNIktpsMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPT 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1771853535 584 AGLDPFSRHQVWNLLKERKTD--RVILFSTQfMDEADILADRKVFLSQGKL 632
Cdd:PRK10762 424 RGVDVGAKKEIYQLINQFKAEglSIILVSSE-MPEVLGMSDRILVMHEGRI 473
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1224-1420 |
4.38e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 62.02 E-value: 4.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1224 LRKEYAGKRkgcfskrknkiATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLL-----KGSGGGDALE 1298
Cdd:PRK11248 7 LYADYGGKP-----------ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLdgkpvEGPGAERGVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1299 FlgycpQENALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVV 1378
Cdd:PRK11248 76 F-----QNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1771853535 1379 LLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEA 1420
Cdd:PRK11248 151 LLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEA 192
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1247-1440 |
6.05e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 62.06 E-value: 6.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1247 NVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsggGDAL--------------EFLGYCPQ--ENALW 1310
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-----GDIVvsstskqkeikpvrKKVGVVFQfpESQLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1311 PNlTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQL--KSPVKtLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMD 1388
Cdd:PRK13643 99 EE-TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFweKSPFE-LSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1771853535 1389 PEGQQQMWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1440
Cdd:PRK13643 177 PKARIEMMQLFE-SIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGT 227
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1246-1435 |
7.16e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 61.47 E-value: 7.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1246 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITG--DTKPTA---GQVLLKGSG--GGDALEF---LGYCPQENALWPNLTV 1315
Cdd:PRK14247 20 DGVNLEIPDNTITALMGPSGSGKSTLLRVFNRliELYPEArvsGEVYLDGQDifKMDVIELrrrVQMVFQIPNPIPNLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1316 RQHLEVYAAVKGLRKGDAEVAiTRLVDALK-------LQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMD 1388
Cdd:PRK14247 100 FENVALGLKLNRLVKSKKELQ-ERVRWALEkaqlwdeVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLD 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1771853535 1389 PEGQQQmwqaIRATF--RNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1435
Cdd:PRK14247 179 PENTAK----IESLFleLKKDMTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1242-1447 |
7.60e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 61.96 E-value: 7.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1242 KIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQV-----LLKGSGGGDALEFL----GYCPQ--ENALW 1310
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVtigerVITAGKKNKKLKPLrkkvGIVFQfpEHQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1311 PNlTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQL--KSPVKtLSEGIKRKLCF--VLSIlgNPSVVLLDEPSTG 1386
Cdd:PRK13634 100 EE-TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELlaRSPFE-LSGGQMRRVAIagVLAM--EPEVLVLDEPTAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1771853535 1387 MDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSK 1447
Cdd:PRK13634 176 LDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFAD 236
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
448-594 |
1.02e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 60.96 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 448 GQITAILGHSGAGKSTLLNILSGLSVPTKGSVtIYNNKLSEMADLENLSKLTGVCPQSNVQFDFLTVRENLRLfakikGI 527
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEI-LLDAQPLESWSSKAFARKVAYLPQQLPAAEGMTVRELVAI-----GR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 528 LP-------------QEVDKEIQRVLLelemKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDpfSRHQV 594
Cdd:PRK10575 111 YPwhgalgrfgaadrEKVEEAISLVGL----KPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD--IAHQV 184
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1236-1435 |
1.07e-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: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1236 FSKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG---------------SGGGDALEFL 1300
Cdd:cd03248 21 YPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGkpisqyehkylhskvSLVGQEPVLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1301 GYCPQENALWpNLTVRQHLEVYAAVKglrKGDAEVAITRLvdALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLL 1380
Cdd:cd03248 101 ARSLQDNIAY-GLQSCSFECVKEAAQ---KAHAHSFISEL--ASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLIL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1771853535 1381 DEPSTGMDPEGQQQMWQAIRATfrNTERGALLTTHYMAEAEAVcDRVAIMVSGRL 1435
Cdd:cd03248 175 DEATSALDAESEQQVQQALYDW--PERRTVLVIAHRLSTVERA-DQILVLDGGRI 226
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
414-632 |
1.09e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 62.76 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 414 QGKEAIRIRNVTKEykgkpdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLE 493
Cdd:PRK15439 264 AGAPVLTVEDLTGE---------GFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 494 NLSK----------LTGVCPQSNVQFDFLTVRENLRLFAkikgILPQEVDKEIQRVLLELEMK-NIQDVLAQNLSGGQKR 562
Cdd:PRK15439 335 RLARglvylpedrqSSGLYLDAPLAWNVCALTHNRRGFW----IKPARENAVLERYRRALNIKfNHAEQAARTLSGGNQQ 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1771853535 563 KLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRV-ILFSTQFMDEADILADRKVFLSQGKL 632
Cdd:PRK15439 411 KVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVaVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1244-1460 |
1.31e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 61.18 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1244 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLL---KGSGGGDALEFLGYCPQENAL---WPNL---- 1313
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgdyAIPANLKKIKEVKRLRKEIGLvfqFPEYqlfq 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1314 -TVRQHLEVYAAVKGLRKGDAEVAITRLVDALKL-QDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEG 1391
Cdd:PRK13645 106 eTIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKG 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1771853535 1392 QQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSI------QHLKSKFGKD----YLLEMKVKN 1460
Cdd:PRK13645 186 EEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPfeifsnQELLTKIEIDppklYQLMYKLKN 264
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1246-1454 |
1.40e-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: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1246 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSgggDALEF--------LGYCPQENALWpNLTVRQ 1317
Cdd:cd03251 19 RDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGH---DVRDYtlaslrrqIGLVSQDVFLF-NDTVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1318 HLeVYAAvkgLRKGDAEV-AITRLVDAL----KLQDQLKSPVK----TLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMD 1388
Cdd:cd03251 95 NI-AYGR---PGATREEVeEAARAANAHefimELPEGYDTVIGergvKLSGGQRQRIAIARALLKDPPILILDEATSALD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1771853535 1389 PEGQQQMWQAIRATFRNteRGALLTTHYMAEAEAVcDRVAIMVSGRLRCIGSIQHLKSKFGKDYLL 1454
Cdd:cd03251 171 TESERLVQAALERLMKN--RTTFVIAHRLSTIENA-DRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
412-637 |
1.42e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 62.57 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 412 EFQGKEAIRIRNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKS-TLLNIL-----SGLSVPTKGSVTIYNNK 485
Cdd:PRK10261 6 ELDARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMrlleqAGGLVQCDKMLLRRRSR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 486 ----LSEM----------ADL-----ENLSKLTGVCPQSNvqfdflTVRENLRLFakiKGILPQEVDKEIQRVLLELEMK 546
Cdd:PRK10261 86 qvieLSEQsaaqmrhvrgADMamifqEPMTSLNPVFTVGE------QIAESIRLH---QGASREEAMVEAKRMLDQVRIP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 547 NIQDVLAQ---NLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLK--ERKTDRVILFSTQFMDEADILA 621
Cdd:PRK10261 157 EAQTILSRyphQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKvlQKEMSMGVIFITHDMGVVAEIA 236
|
250
....*....|....*.
gi 1771853535 622 DRKVFLSQGKLKCAGS 637
Cdd:PRK10261 237 DRVLVMYQGEAVETGS 252
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
437-632 |
1.58e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.44 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 437 ALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLS----------KLTGVcpQSN 506
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINhgfalvteerRSTGI--YAY 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 507 VQFDFLTVRENLRLFAKIKGILPQE-VDKEIQRVLLELEMKN-IQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTA 584
Cdd:PRK10982 341 LDIGFNSLISNIRNYKNKVGLLDNSrMKSDTQWVIDSMRVKTpGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTR 420
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1771853535 585 GLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKL 632
Cdd:PRK10982 421 GIDVGAKFEIYQLIAElAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1246-1480 |
1.66e-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: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1246 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITgDTKPTAGQVLLKG-SGGGDALE----FLGYCPQENALWPNlTVRQHLE 1320
Cdd:TIGR01271 1236 QDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDGvSWNSVTLQtwrkAFGVIPQKVFIFSG-TFRKNLD 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1321 VYA--AVKGLRKGDAEVAITRLVDAL--KLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMW 1396
Cdd:TIGR01271 1314 PYEqwSDEEIWKVAEEVGLKSVIEQFpdKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIR 1393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1397 QAIRATFRNTErgALLTTHYMaEAEAVCDRVAIMVSGRLRCIGSIQ-------HLKSKFGkdyllemkvknlaqveplHA 1469
Cdd:TIGR01271 1394 KTLKQSFSNCT--VILSEHRV-EALLECQQFLVIEGSSVKQYDSIQkllnetsLFKQAMS------------------AA 1452
|
250
....*....|.
gi 1771853535 1470 EILRLFPQAAR 1480
Cdd:TIGR01271 1453 DRLKLFPLHRR 1463
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1246-1415 |
1.87e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.59 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1246 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITG--DTKPTAGQVLLkgsgggdaleflgycpQENALWPNLTVRQHLevya 1323
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDV----------------PDNQFGREASLIDAI---- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1324 avkgLRKGDAEVAITRLVDAlKLQDQ--LKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRA 1401
Cdd:COG2401 107 ----GRKGDFKDAVELLNAV-GLSDAvlWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQK 181
|
170
....*....|....
gi 1771853535 1402 TFRNTERGALLTTH 1415
Cdd:COG2401 182 LARRAGITLVVATH 195
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1244-1444 |
1.90e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 60.41 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1244 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIK----VITGDTKPTAGQVLL------KGSGGGD---ALEFLGYCPQENALW 1310
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGSHIELLgrtvqrEGRLARDirkSRANTGYIFQQFNLV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1311 PNLTVRQHLEVYAA------------VKGLRKGDAEVAITRlVDALKLQDQlksPVKTLSEGIKRKLCFVLSILGNPSVV 1378
Cdd:PRK09984 99 NRLSVLENVLIGALgstpfwrtcfswFTREQKQRALQALTR-VGMVHFAHQ---RVSTLSGGQQQRVAIARALMQQAKVI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1771853535 1379 LLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL 1444
Cdd:PRK09984 175 LADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1246-1435 |
2.12e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 59.98 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1246 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGS-------GGGDALEF-----------LGYCPQEN 1307
Cdd:PRK10619 22 KGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQtinlvrdKDGQLKVAdknqlrllrtrLTMVFQHF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1308 ALWPNLTVRQH-LEVYAAVKGLRKGDAEVAITRLVDALKLQD--QLKSPVKtLSEGIKRKLCFVLSILGNPSVVLLDEPS 1384
Cdd:PRK10619 102 NLWSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIDEraQGKYPVH-LSGGQQQRVSIARALAMEPEVLLFDEPT 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1771853535 1385 TGMDPEgqqQMWQAIRATFRNTERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1435
Cdd:PRK10619 181 SALDPE---LVGEVLRIMQQLAEEGKtmVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1241-1473 |
2.28e-09 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 60.03 E-value: 2.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1241 NKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG---SGGGD-----ALEFLgycPQENALWPN 1312
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpiSMLSSrqlarRLALL---PQHHLTPEG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1313 LTVRQHLEV----YAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGiKRKLCFVLSILG-NPSVVLLDEPSTGM 1387
Cdd:PRK11231 91 ITVRELVAYgrspWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGG-QRQRAFLAMVLAqDTPVVLLDEPTTYL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1388 DPEGQQQMWQAIRAtfRNTERGALLTT-HYMAEAEAVCDRVAIMVSGRLRCIGSIQHLkskfgkdylleMKVKNLAQVEP 1466
Cdd:PRK11231 170 DINHQVELMRLMRE--LNTQGKTVVTVlHDLNQASRYCDHLVVLANGHVMAQGTPEEV-----------MTPGLLRTVFD 236
|
....*..
gi 1771853535 1467 LHAEILR 1473
Cdd:PRK11231 237 VEAEIHP 243
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1247-1471 |
2.41e-09 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 60.87 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1247 NVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGS--GGGDALE-FLGYCPQENALWPNLTVRQHLEVYA 1323
Cdd:PRK10851 20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvSRLHARDrKVGFVFQHYALFRHMTVFDNIAFGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1324 AVKGLRKGDAEVAI----TRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAI 1399
Cdd:PRK10851 100 TVLPRRERPNAAAIkakvTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1771853535 1400 RATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFGKDYLLEMkvknLAQVEPLHAEI 1471
Cdd:PRK10851 180 RQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEF----MGEVNRLQGTI 247
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1244-1444 |
3.52e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 60.12 E-value: 3.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1244 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGdtkptagqvLLKGSG--GGDAL----EFLGYCPQE----------- 1306
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMG---------LLAANGriGGSATfngrEILNLPEKElnklraeqism 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1307 ------NALWPNLTV-RQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKS----PvKTLSEGIKRKLCFVLSILGNP 1375
Cdd:PRK09473 102 ifqdpmTSLNPYMRVgEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRmkmyP-HEFSGGMRQRVMIAMALLCRP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1771853535 1376 SVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL 1444
Cdd:PRK09473 181 KLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1244-1449 |
3.75e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 61.38 E-value: 3.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1244 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsGGGDALEFlgycpQENALWPNLT-VRQHLEVY 1322
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILL---NGQPIADY-----SEAALRQAISvVSQRVHLF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1323 AAV--KGLRKGDAEVAITRLVDALK---LQDQLKSPV----------KTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGM 1387
Cdd:PRK11160 427 SATlrDNLLLAAPNASDEALIEVLQqvgLEKLLEDDKglnawlgeggRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGL 506
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1771853535 1388 DPEGQQQMWQAIRATFRNteRGALLTTHYMAEAEAVcDRVAIMVSGRLRCIGSIQHLKSKFG 1449
Cdd:PRK11160 507 DAETERQILELLAEHAQN--KTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQELLAQQG 565
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1224-1390 |
3.92e-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: 3.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1224 LRKEYAGKRKgcfskrknkiATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgSGGGDalefLGYC 1303
Cdd:TIGR03719 10 VSKVVPPKKE----------ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP--QPGIK----VGYL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1304 PQENALWPNLTVRQHLEvyAAVKGLRKgdaevAITRL-------------VDAL-----KLQDQLKS------------- 1352
Cdd:TIGR03719 74 PQEPQLDPTKTVRENVE--EGVAEIKD-----ALDRFneisakyaepdadFDKLaaeqaELQEIIDAadawdldsqleia 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1771853535 1353 -----------PVKTLSEGIKRK--LCFVLsiLGNPSVVLLDEPSTGMDPE 1390
Cdd:TIGR03719 147 mdalrcppwdaDVTKLSGGERRRvaLCRLL--LSKPDMLLLDEPTNHLDAE 195
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1241-1440 |
4.64e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 58.91 E-value: 4.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1241 NKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITG-----DTK-PTAGQVLLKGSG--GGDALEF---LGYCPQENAL 1309
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRlieiyDSKiKVDGKVLYFGKDifQIDAIKLrkeVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1310 WPNLTVRQHLEVYAAVKGLR-----KGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPS 1384
Cdd:PRK14246 102 FPHLSIYDNIAYPLKSHGIKekreiKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1771853535 1385 TGMDPEGQQQMWQAIraTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1440
Cdd:PRK14246 182 SMIDIVNSQAIEKLI--TELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGS 235
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
418-587 |
5.34e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.15 E-value: 5.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 418 AIRIRNVTKEYKgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMAdLENLSK 497
Cdd:PLN03232 1234 SIKFEDVHLRYR--PGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFG-LTDLRR 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 498 LTGVCPQSNVQFDFlTVRENLRLFAkikgilpQEVDKEIQRVlleLEMKNIQDVL--------------AQNLSGGQKRK 563
Cdd:PLN03232 1311 VLSIIPQSPVLFSG-TVRFNIDPFS-------EHNDADLWEA---LERAHIKDVIdrnpfgldaevsegGENFSVGQRQL 1379
|
170 180
....*....|....*....|....
gi 1771853535 564 LTFGIAILGDPQIFLLDEPTAGLD 587
Cdd:PLN03232 1380 LSLARALLRRSKILVLDEATASVD 1403
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
443-587 |
5.76e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 60.73 E-value: 5.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 443 FDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVtIYNNKLSeMADLENlskltgvCPQSNVQ---FDFLT-----V 514
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRI-IYEQDLI-VARLQQ-------DPPRNVEgtvYDFVAegieeQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 515 RENLRLFAKIKGILPQEVD----KEIQRVLLELEMKN-------IQDVLAQ----------NLSGGQKRKLTFGIAILGD 573
Cdd:PRK11147 95 AEYLKRYHDISHLVETDPSeknlNELAKLQEQLDHHNlwqlenrINEVLAQlgldpdaalsSLSGGWLRKAALGRALVSN 174
|
170
....*....|....
gi 1771853535 574 PQIFLLDEPTAGLD 587
Cdd:PRK11147 175 PDVLLLDEPTNHLD 188
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1246-1434 |
6.04e-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: 6.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1246 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGG----DALEF---------LGYCPQenalwpN 1312
Cdd:COG4778 28 DGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWvdlaQASPReilalrrrtIGYVSQ------F 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1313 LTV--RQH-LEVYAAVkGLRKG-DAEVAITR---LVDALKLQDQLKS-PVKTLSEGIKRKLCFVLSILGNPSVVLLDEPS 1384
Cdd:COG4778 102 LRVipRVSaLDVVAEP-LLERGvDREEARARareLLARLNLPERLWDlPPATFSGGEQQRVNIARGFIADPPLLLLDEPT 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1771853535 1385 TGMDPEGQQ---QMWQAIRAtfrnteRG-ALLT-THYMAEAEAVCDRVAIMVSGR 1434
Cdd:COG4778 181 ASLDAANRAvvvELIEEAKA------RGtAIIGiFHDEEVREAVADRVVDVTPFS 229
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1239-1399 |
6.12e-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: 58.32 E-value: 6.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1239 RKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGD-ALEFL----GYCPQENALWPNl 1313
Cdd:cd03249 13 RPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlNLRWLrsqiGLVSQEPVLFDG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1314 TVRQHLEvYaavkGLRKGDAEVAITRLVDA------LKLQDQLKSPV----KTLSEGIKRKLCFVLSILGNPSVVLLDEP 1383
Cdd:cd03249 92 TIAENIR-Y----GKPDATDEEVEEAAKKAnihdfiMSLPDGYDTLVgergSQLSGGQKQRIAIARALLRNPKILLLDEA 166
|
170
....*....|....*.
gi 1771853535 1384 STGMDPEGQQQMWQAI 1399
Cdd:cd03249 167 TSALDAESEKLVQEAL 182
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
419-630 |
6.32e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 58.05 E-value: 6.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKPD-------------------KIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSG--LSVPTKG 477
Cdd:COG2401 8 FVLMRVTKVYSSVLDlservaivleafgvelrvvERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 478 SVTIYNNKL-SEMADLENLSKLTgvcpqsnvqfDFLTVRENLR---------LFAKIKgilpqevdkeiqrvllelemkn 547
Cdd:COG2401 88 CVDVPDNQFgREASLIDAIGRKG----------DFKDAVELLNavglsdavlWLRRFK---------------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 548 iqdvlaqNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDP-FSRHQVWNLLKE-RKTDRVILFSTQFMD-EADILADRK 624
Cdd:COG2401 136 -------ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRqTAKRVARNLQKLaRRAGITLVVATHHYDvIDDLQPDLL 208
|
....*.
gi 1771853535 625 VFLSQG 630
Cdd:COG2401 209 IFVGYG 214
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1248-1440 |
6.59e-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: 6.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1248 VSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsgGGDALEF----------------------LGYCPQ 1305
Cdd:COG4598 27 VSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRV----GGEEIRLkpdrdgelvpadrrqlqrirtrLGMVFQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1306 ENALWPNLTVRQHL-EVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEG------IKRKLCFvlsilgNPSVV 1378
Cdd:COG4598 103 SFNLWSHMTVLENViEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGqqqraaIARALAM------EPEVM 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1771853535 1379 LLDEPSTGMDPEGQQQMWQAIRATfrnTERGA--LLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1440
Cdd:COG4598 177 LFDEPTSALDPELVGEVLKVMRDL---AEEGRtmLVVTHEMGFARDVSSHVVFLHQGRIEEQGP 237
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1239-1435 |
6.62e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 58.68 E-value: 6.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1239 RKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGD-TKPTA-------GQVLLKGS--GGGDALEFL---GYCPQ 1305
Cdd:PRK13547 11 RRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDlTGGGAprgarvtGDVTLNGEplAAIDAPRLArlrAVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1306 ENALWPNLTVRQ--------HLEVYAAVKGLRKGDAEVAITRL-VDALKLQDqlkspVKTLSEGIKRKLCF--VLSIL-- 1372
Cdd:PRK13547 91 AAQPAFAFSAREivllgrypHARRAGALTHRDGEIAWQALALAgATALVGRD-----VTTLSGGELARVQFarVLAQLwp 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1771853535 1373 -----GNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1435
Cdd:PRK13547 166 phdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAI 233
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
418-587 |
6.78e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 60.50 E-value: 6.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 418 AIRIRNVTKEYKGkpDKIeALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEM--ADLENl 495
Cdd:PRK10790 340 RIDIDNVSFAYRD--DNL-VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLshSVLRQ- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 496 skltGVcpqSNVQFDFLTVRENlrLFAKI---KGILPQEVDKEIQRVLLELEMKNIQDVL-------AQNLSGGQKRKLT 565
Cdd:PRK10790 416 ----GV---AMVQQDPVVLADT--FLANVtlgRDISEEQVWQALETVQLAELARSLPDGLytplgeqGNNLSVGQKQLLA 486
|
170 180
....*....|....*....|..
gi 1771853535 566 FGIAILGDPQIFLLDEPTAGLD 587
Cdd:PRK10790 487 LARVLVQTPQILILDEATANID 508
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1236-1435 |
7.15e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 58.25 E-value: 7.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1236 FSKRKnkiATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVIT--GDTKP---TAGQVLLKG----SGGGDALEF---LGYC 1303
Cdd:PRK14239 15 YNKKK---ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPevtITGSIVYNGhniySPRTDTVDLrkeIGMV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1304 PQENALWPnltvrqhLEVYA-AVKGLR-KG--DAEVAITRLVDALK-------LQDQLKSPVKTLSEGIKRKLCFVLSIL 1372
Cdd:PRK14239 92 FQQPNPFP-------MSIYEnVVYGLRlKGikDKQVLDEAVEKSLKgasiwdeVKDRLHDSALGLSGGQQQRVCIARVLA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1771853535 1373 GNPSVVLLDEPSTGMDPEGQQQmwqaIRATFRNTERG--ALLTTHYMAEAEAVCDRVAIMVSGRL 1435
Cdd:PRK14239 165 TSPKIILLDEPTSALDPISAGK----IEETLLGLKDDytMLLVTRSMQQASRISDRTGFFLDGDL 225
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
443-632 |
8.86e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 59.92 E-value: 8.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 443 FDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLSKLTGVCPQSNVQ---FDFLTVRENL- 518
Cdd:PRK11288 274 FSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMLCPEDRKAegiIPVHSVADNIn 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 519 ----RLFAKIKGIL--PQE---VDKEIQRVllelemkNIQ----DVLAQNLSGGQKRKltfgiAILG-----DPQIFLLD 580
Cdd:PRK11288 354 isarRHHLRAGCLInnRWEaenADRFIRSL-------NIKtpsrEQLIMNLSGGNQQK-----AILGrwlseDMKVILLD 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1771853535 581 EPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKL 632
Cdd:PRK11288 422 EPTRGIDVGAKHEIYNVIYElAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1247-1435 |
9.00e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 57.80 E-value: 9.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1247 NVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSG--GGDALEFL-----GYCPQENALWPNLTVrqhL 1319
Cdd:PRK09493 19 NIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKvnDPKVDERLirqeaGMVFQQFYLFPHLTA---L 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1320 EVYA----AVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQM 1395
Cdd:PRK09493 96 ENVMfgplRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEV 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1771853535 1396 WQAIRATfrnTERG--ALLTTHYMAEAEAVCDRVAIMVSGRL 1435
Cdd:PRK09493 176 LKVMQDL---AEEGmtMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1242-1461 |
9.80e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 58.27 E-value: 9.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1242 KIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGdtkptagqVLLKGSGGGDALEFLGYCPQENALWpnlTVRQHLE- 1320
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLING--------LLLPDDNPNSKITVDGITLTAKTVW---DIREKVGi 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1321 ---------VYAAV----------KGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCfVLSILG-NPSVVLL 1380
Cdd:PRK13640 89 vfqnpdnqfVGATVgddvafglenRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVA-IAGILAvEPKIIIL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1381 DEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEA-----VCDRVAIMVSGRLRCIGSIQHLKSKFGKDYLLE 1455
Cdd:PRK13640 168 DESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMadqvlVLDDGKLLAQGSPVEIFSKVEMLKEIGLDIPFV 247
|
....*.
gi 1771853535 1456 MKVKNL 1461
Cdd:PRK13640 248 YKLKNK 253
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
450-632 |
1.04e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 58.18 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 450 ITAILGHSGAGKSTLLNILSGLSVPTKG-----SVTIYNNKLSEMADLENLSKLTGVCPQSNVQFDfLTVRENLRLFAKI 524
Cdd:PRK14271 49 VTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVLEFRRRVGMLFQRPNPFP-MSIMDNVLAGVRA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 525 KGILP-QEVDKEIQRVLLELEMKN-IQDVLAQN---LSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLK 599
Cdd:PRK14271 128 HKLVPrKEFRGVAQARLTEVGLWDaVKDRLSDSpfrLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIR 207
|
170 180 190
....*....|....*....|....*....|...
gi 1771853535 600 ERKTDRVILFSTQFMDEADILADRKVFLSQGKL 632
Cdd:PRK14271 208 SLADRLTVIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1255-1435 |
1.18e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 57.77 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1255 GEVLGLLGHNGAGKSTSIKVITGDTKPTAGQvLLKGSGG-GDALEFLGYCPQENALWPNLTVRQHLEVyaavkGLrKGDA 1333
Cdd:PRK11247 38 GQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-LLAGTAPlAEAREDTRLMFQDARLLPWKKVIDNVGL-----GL-KGQW 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1334 EVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLT 1413
Cdd:PRK11247 111 RDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLV 190
|
170 180
....*....|....*....|..
gi 1771853535 1414 THYMAEAEAVCDRVAIMVSGRL 1435
Cdd:PRK11247 191 THDVSEAVAMADRVLLIEEGKI 212
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1246-1415 |
1.20e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 60.24 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1246 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGdtKPTAGQVL--LKGSGGGDALEFL----GYCPQENALWPNLTVRQHL 1319
Cdd:PLN03140 897 REVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEgdIRISGFPKKQETFarisGYCEQNDIHSPQVTVRESL 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1320 eVYAAVKGLRKGDAEVAITRLVDA---LKLQDQLKSP------VKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1390
Cdd:PLN03140 975 -IYSAFLRLPKEVSKEEKMMFVDEvmeLVELDNLKDAivglpgVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDAR 1053
|
170 180
....*....|....*....|....*
gi 1771853535 1391 GQQQMWQAIRATFrNTERGALLTTH 1415
Cdd:PLN03140 1054 AAAIVMRTVRNTV-DTGRTVVCTIH 1077
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1247-1434 |
1.21e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 59.33 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1247 NVSFCVRKGEVLGLLGHNGAGKS-TSIKVI-----------TGDTKpTAGQVLLKGS--------GGGDALEFlgycpQE 1306
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSvTALSILrllpsppvvypSGDIR-FHGESLLHASeqtlrgvrGNKIAMIF-----QE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1307 N--ALWPNLTVRQHL-EVYAAVKGLRKGDAEVAITRLVDALKLQD---QLKSPVKTLSEGIKRKLCFVLSILGNPSVVLL 1380
Cdd:PRK15134 101 PmvSLNPLHTLEKQLyEVLSLHRGMRREAARGEILNCLDRVGIRQaakRLTDYPHQLSGGERQRVMIAMALLTRPELLIA 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1771853535 1381 DEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1434
Cdd:PRK15134 181 DEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1259-1390 |
1.23e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 59.36 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1259 GLLGHNGAGKSTSIKVITGDTKPTAGQ-VLLKGSGggdalefLGYCPQENALWPNLTVRQHLEvyAAVkglrkGDAEVAI 1337
Cdd:PRK11819 37 GVLGLNGAGKSTLLRIMAGVDKEFEGEaRPAPGIK-------VGYLPQEPQLDPEKTVRENVE--EGV-----AEVKAAL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1338 TRL-------------VDAL-----KLQDQLKS------------------------PVKTLSEGIKRK--LCFVLsiLG 1373
Cdd:PRK11819 103 DRFneiyaayaepdadFDALaaeqgELQEIIDAadawdldsqleiamdalrcppwdaKVTKLSGGERRRvaLCRLL--LE 180
|
170
....*....|....*..
gi 1771853535 1374 NPSVVLLDEPSTGMDPE 1390
Cdd:PRK11819 181 KPDMLLLDEPTNHLDAE 197
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1248-1436 |
1.32e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 57.10 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1248 VSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSG-------GGDAL--EFLGYCPQENALWPNLTVRQH 1318
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPlhqmdeeARAKLraKHVGFVFQSFMLIPTLNALEN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1319 LEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQA 1398
Cdd:PRK10584 109 VELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADL 188
|
170 180 190
....*....|....*....|....*....|....*...
gi 1771853535 1399 IRATFRNTERGALLTTHYMAEAeAVCDRVAIMVSGRLR 1436
Cdd:PRK10584 189 LFSLNREHGTTLILVTHDLQLA-ARCDRRLRLVNGQLQ 225
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1246-1435 |
1.42e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 59.29 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1246 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGS-----GGGDALEF-LGYCPQEnalwpnltvRQ-- 1317
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKeinalSTAQRLARgLVYLPED---------RQss 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1318 --HLE------VYAAVKGLR----KGDAEVAI-TRLVDALKLQ-DQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEP 1383
Cdd:PRK15439 351 glYLDaplawnVCALTHNRRgfwiKPARENAVlERYRRALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1771853535 1384 STGMDPEGQQQMWQAIRA-TFRNTerGALLTTHYMAEAEAVCDRVAIMVSGRL 1435
Cdd:PRK15439 431 TRGVDVSARNDIYQLIRSiAAQNV--AVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1255-1399 |
1.43e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 59.41 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1255 GEVLGLLGHNGAGKSTSIKVITGDTKPTAGQV-LLKGSGGG----DALEFLGycPQENALwpnltvrQHLEVYAavkglr 1329
Cdd:PRK10636 338 GSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGyfaqHQLEFLR--ADESPL-------QHLARLA------ 402
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1771853535 1330 KGDAEVAITRLVDALKLQ-DQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAI 1399
Cdd:PRK10636 403 PQELEQKLRDYLGGFGFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEAL 473
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
441-587 |
1.76e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 57.25 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 441 LVFDIYEGQITAILGHSGAGKSTLLNILSGLSvPTKGSVTIYNNKLSEMaDLENLSKLTG-VCPQSNVQFDfLTVRENLR 519
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAW-SAAELARHRAyLSQQQTPPFA-MPVFQYLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 520 LFakikgiLPQEVDK-EIQRVLLEL-EMKNIQDVLA---QNLSGGQKRKLTFGIAIL-----GDP--QIFLLDEPTAGLD 587
Cdd:PRK03695 92 LH------QPDKTRTeAVASALNEVaEALGLDDKLGrsvNQLSGGEWQRVRLAAVVLqvwpdINPagQLLLLDEPMNSLD 165
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1244-1458 |
1.77e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.86 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1244 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-----SGGGDALEF-LGYCPQENALWPNLTVRQ 1317
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGkevtfNGPKSSQEAgIGIIHQELNLIPQLTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1318 HL----EVYAAVKGL--RKGDAEVaiTRLVDALKLQDQLKSPVKTLSEG------IKRKLCFvlsilgNPSVVLLDEPST 1385
Cdd:PRK10762 99 NIflgrEFVNRFGRIdwKKMYAEA--DKLLARLNLRFSSDKLVGELSIGeqqmveIAKVLSF------ESKVIIMDEPTD 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1771853535 1386 GMDPEGQQQMWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLrcIGsiQHLKSKFGKDYLLEMKV 1458
Cdd:PRK10762 171 ALTDTETESLFRVIR-ELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQF--IA--EREVADLTEDSLIEMMV 238
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1246-1439 |
1.96e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 57.16 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1246 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITG--DTKPTA---GQVLLKG----SGGGDALEF---LGYCPQENALWPNL 1313
Cdd:PRK14267 21 KGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRllELNEEArveGEVRLFGrniySPDVDPIEVrreVGMVFQYPNPFPHL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1314 TVRQHLEVYAAVKGLRKGDAEVAiTRLVDALK-------LQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTG 1386
Cdd:PRK14267 101 TIYDNVAIGVKLNGLVKSKKELD-ERVEWALKkaalwdeVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTAN 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1771853535 1387 MDPEGQQQMWQAIRATfrNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1439
Cdd:PRK14267 180 IDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVG 230
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1248-1435 |
2.00e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 57.41 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1248 VSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGS-----GGGDALEFLGYCPQE-NALWPNLTVRQHLEV 1321
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGElltaeNVWNLRRKIGMVFQNpDNQFVGATVEDDVAF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1322 YAAVKGLRKgdaEVAITRLVDAL----KLQDQLKSPVKtLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQ 1397
Cdd:PRK13642 106 GMENQGIPR---EEMIKRVDEALlavnMLDFKTREPAR-LSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMR 181
|
170 180 190
....*....|....*....|....*....|....*...
gi 1771853535 1398 AIRATFRNTERGALLTTHYMAEAeAVCDRVAIMVSGRL 1435
Cdd:PRK13642 182 VIHEIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEI 218
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1247-1433 |
2.08e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 57.07 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1247 NVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLlkgsgggdaleFLGYCPQENalwpNLT-VRQHLEV---- 1321
Cdd:PRK13648 27 DVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIF-----------YNNQAITDD----NFEkLRKHIGIvfqn 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1322 -----------YAAVKGLRK-----GDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPST 1385
Cdd:PRK13648 92 pdnqfvgsivkYDVAFGLENhavpyDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATS 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1771853535 1386 GMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAeAVCDRVAIMVSG 1433
Cdd:PRK13648 172 MLDPDARQNLLDLVRKVKSEHNITIISITHDLSEA-MEADHVIVMNKG 218
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1245-1439 |
2.21e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 58.12 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1245 TRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGD---ALEFLGYCPQENALWPNLTVRQHLEV 1321
Cdd:PRK11000 19 SKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDvppAERGVGMVFQSYALYPHLSVAENMSF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1322 YAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRA 1401
Cdd:PRK11000 99 GLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISR 178
|
170 180 190
....*....|....*....|....*....|....*...
gi 1771853535 1402 TFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1439
Cdd:PRK11000 179 LHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
406-587 |
2.40e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 58.64 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 406 FEQAPP--EFQGKEAIRIRNVTKEYKGKPDKIEAlkdlvFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIyN 483
Cdd:COG1245 327 FEVHAPrrEKEEETLVEYPDLTKSYGGFSLEVEG-----GEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDE-D 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 484 NKLSemadlenlSKltgvcPQSnVQFDF-LTVRENLRlfAKIKGILPqevDKEIQRVLLE-LEMKNIQDVLAQNLSGGQK 561
Cdd:COG1245 401 LKIS--------YK-----PQY-ISPDYdGTVEEFLR--SANTDDFG---SSYYKTEIIKpLGLEKLLDKNVKDLSGGEL 461
|
170 180
....*....|....*....|....*.
gi 1771853535 562 RKLTFGIAILGDPQIFLLDEPTAGLD 587
Cdd:COG1245 462 QRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1237-1435 |
2.82e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 57.55 E-value: 2.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1237 SKRKNKI-ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDALEFLGYCPQENA------- 1308
Cdd:PRK13631 33 EKQENELvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELITNPYSkkiknfk 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1309 ----------LWPNL-----TVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQL--KSPVKtLSEGIKRKLCF--VL 1369
Cdd:PRK13631 113 elrrrvsmvfQFPEYqlfkdTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSYleRSPFG-LSGGQKRRVAIagIL 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1771853535 1370 SIlgNPSVVLLDEPSTGMDPEGQQQMWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1435
Cdd:PRK13631 192 AI--QPEILIFDEPTAGLDPKGEHEMMQLIL-DAKANNKTVFVITHTMEHVLEVADEVIVMDKGKI 254
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1244-1435 |
2.90e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 57.10 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1244 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsgggDALEF---------------LGYCPQ--E 1306
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTV------DDITIthktkdkyirpvrkrIGMVFQfpE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1307 NALWPNLTVRqhlEVYAAVKGLRKGDAEVAitrlVDALKLQDQL--------KSPVKtLSEGIKRKLCFVlSILG-NPSV 1377
Cdd:PRK13646 96 SQLFEDTVER---EIIFGPKNFKMNLDEVK----NYAHRLLMDLgfsrdvmsQSPFQ-MSGGQMRKIAIV-SILAmNPDI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1771853535 1378 VLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1435
Cdd:PRK13646 167 IVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
447-622 |
3.07e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 56.61 E-value: 3.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 447 EGQITAILGHSGAGKSTLLNILSGLSVPtkgsvtiynnklsemadleNLSKLtgvcpQSNVQFDflTVRENLR------L 520
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKP-------------------NLGKF-----DDPPDWD--EILDEFRgselqnY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 521 FAKIKG------ILPQEVDkEIQRV-------LLE--------------LEMKNIQDVLAQNLSGGQKRKLTFGIAILGD 573
Cdd:cd03236 79 FTKLLEgdvkviVKPQYVD-LIPKAvkgkvgeLLKkkdergkldelvdqLELRHVLDRNIDQLSGGELQRVAIAAALARD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1771853535 574 PQIFLLDEPTAGLDPFSRHQVWNLLKER-KTDRVILFSTQFMDEADILAD 622
Cdd:cd03236 158 ADFYFFDEPSSYLDIKQRLNAARLIRELaEDDNYVLVVEHDLAVLDYLSD 207
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
401-601 |
4.34e-08 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 57.89 E-value: 4.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 401 SFHDSFEQAPPEFQGKEAIR--------IRNVTKEykgKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLS 472
Cdd:COG4178 337 GFEEALEAADALPEAASRIEtsedgalaLEDLTLR---TPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLW 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 473 VPTKGSVTIynNKLSEMADLenlskltgvcPQSNvqfdFL---TVRENLrlfakikgILPQEV----DKEIQRVL----L 541
Cdd:COG4178 414 PYGSGRIAR--PAGARVLFL----------PQRP----YLplgTLREAL--------LYPATAeafsDAELREALeavgL 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1771853535 542 E--LEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKER 601
Cdd:COG4178 470 GhlAERLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREE 531
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
415-633 |
4.38e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 57.63 E-value: 4.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 415 GKEAIRIRNVTKEYKGKPdKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGlSVPTK--GSVTIYNNKLSEMADL 492
Cdd:PRK13549 256 GEVILEVRNLTAWDPVNP-HIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFG-AYPGRweGEIFIDGKPVKIRNPQ 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 493 ENLS----------KLTGVCPQSNVQFDFLTVreNLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLA-QNLSGGQK 561
Cdd:PRK13549 334 QAIAqgiamvpedrKRDGIVPVMGVGKNITLA--ALDRFTGGSRIDDAAELKTILESIQRLKVKTASPELAiARLSGGNQ 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1771853535 562 RKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQfMDEADILADRKVFLSQGKLK 633
Cdd:PRK13549 412 QKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQlvQQGVAIIVISSE-LPEVLGLSDRVLVMHEGKLK 484
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
433-587 |
4.39e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 55.80 E-value: 4.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 433 DKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSG---LSVpTKGSVTIYNNKLSEMaDLENLSKL----------- 498
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpaYKI-LEGDILFKGESILDL-EPEERAHLgiflafqypie 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 -TGVcpqSNVqfDFLTVRENLRL-FAKIKGILPQEVDKEIQRVLLELEMKniQDVLAQNL----SGGQKRKLTFGIAILG 572
Cdd:CHL00131 96 iPGV---SNA--DFLRLAYNSKRkFQGLPELDPLEFLEIINEKLKLVGMD--PSFLSRNVnegfSGGEKKRNEILQMALL 168
|
170
....*....|....*
gi 1771853535 573 DPQIFLLDEPTAGLD 587
Cdd:CHL00131 169 DSELAILDETDSGLD 183
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
421-587 |
4.49e-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: 4.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 421 IRNVTKEYkgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGsvtiynnklsEMADLENLSklTG 500
Cdd:TIGR03719 7 MNRVSKVV---PPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG----------EARPQPGIK--VG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 501 VCPQSNVQFDFLTVRENLRL-FAKIKGIL-------------PQEVDK------EIQRVL-----------LELEMKNIQ 549
Cdd:TIGR03719 72 YLPQEPQLDPTKTVRENVEEgVAEIKDALdrfneisakyaepDADFDKlaaeqaELQEIIdaadawdldsqLEIAMDALR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1771853535 550 ----DVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLD 587
Cdd:TIGR03719 152 cppwDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1252-1400 |
5.04e-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: 5.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1252 VRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDALEFLGYCPQ-------ENALWPNLTVRQHLEVYAA 1324
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDEILDEFRGSELQnyftkllEGDVKVIVKPQYVDLIPKA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1325 VKG-----LRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAI 1399
Cdd:cd03236 103 VKGkvgelLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLI 182
|
.
gi 1771853535 1400 R 1400
Cdd:cd03236 183 R 183
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
410-481 |
5.19e-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: 5.19e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1771853535 410 PPEFQGKEAIRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTI 481
Cdd:TIGR03719 314 PGPRLGDKVIEAENLTKAFGDKL----LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI 381
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
431-632 |
5.36e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 57.93 E-value: 5.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 431 KPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGL---SVPTKGSVTIYNNKLSEMADlenlSKLTGVCPQSNV 507
Cdd:PLN03140 174 KKTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKldpSLKVSGEITYNGYRLNEFVP----RKTSAYISQNDV 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 508 QFDFLTVRENLRLFAKIKG-------------------ILPQ-EVDKEIQRVLLELEMKN-------------------I 548
Cdd:PLN03140 250 HVGVMTVKETLDFSARCQGvgtrydllselarrekdagIFPEaEVDLFMKATAMEGVKSSlitdytlkilgldickdtiV 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 549 QDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFS-TQFMDEADILADRKV 625
Cdd:PLN03140 330 GDEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQivHLTEATVLMSlLQPAPETFDLFDDII 409
|
....*..
gi 1771853535 626 FLSQGKL 632
Cdd:PLN03140 410 LLSEGQI 416
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
407-587 |
5.61e-08 |
|
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: 58.03 E-value: 5.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 407 EQAPPE-FQGKEAIRIRNVTKEYKgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNK 485
Cdd:TIGR00957 1272 ETAPPSgWPPRGRVEFRNYCLRYR--EDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLN 1349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 486 LSEMAdLENL-SKLTgVCPQSNVQFDFlTVRENLRLFAkikgilpQEVDKEiqrVLLELEMKNIQDVLA----------- 553
Cdd:TIGR00957 1350 IAKIG-LHDLrFKIT-IIPQDPVLFSG-SLRMNLDPFS-------QYSDEE---VWWALELAHLKTFVSalpdkldheca 1416
|
170 180 190
....*....|....*....|....*....|....*..
gi 1771853535 554 ---QNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLD 587
Cdd:TIGR00957 1417 eggENLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1453
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1232-1439 |
6.52e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.17 E-value: 6.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1232 RKGCFSKRKNKI-ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG------SGGG-----DALEF 1299
Cdd:PRK10261 326 RSGLLNRVTREVhAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqridtlSPGKlqalrRDIQF 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1300 LGYCPQEnALWPNLTVRQHLEVYAAVKGLRKGDAEVA-ITRLVD--ALKLQDQLKSPvKTLSEGIKRKLCFVLSILGNPS 1376
Cdd:PRK10261 406 IFQDPYA-SLDPRQTVGDSIMEPLRVHGLLPGKAAAArVAWLLErvGLLPEHAWRYP-HEFSGGQRQRICIARALALNPK 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1771853535 1377 VVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1439
Cdd:PRK10261 484 VIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1252-1429 |
7.83e-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: 53.73 E-value: 7.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1252 VRKGEVLGLLGHNGAGKSTSIKVITGDTKPTagqvllkgsgggdaleflgycpQENALWPNLTVrqhleVYaavkglrkg 1331
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPN----------------------GDNDEWDGITP-----VY--------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1332 daevaitrlvdalklqdqlKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGAL 1411
Cdd:cd03222 66 -------------------KPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTAL 126
|
170
....*....|....*...
gi 1771853535 1412 LTTHYMAEAEAVCDRVAI 1429
Cdd:cd03222 127 VVEHDLAVLDYLSDRIHV 144
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1247-1436 |
7.88e-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: 7.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1247 NVSFCVRKGEVLGLLGHNGAGKSTSIKVITG------------DTKPTAGQVLLKGSGGGDALeflgyCPQE---NALWP 1311
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGaypgkfegnvfiNGKPVDIRNPAQAIRAGIAM-----VPEDrkrHGIVP 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1312 NLTVRQH--LEVYAAVKGLRKGDAEV---AITRLVDALKLQDQLKS-PVKTLSEGIKRKLCFVLSILGNPSVVLLDEPST 1385
Cdd:TIGR02633 353 ILGVGKNitLSVLKSFCFKMRIDAAAelqIIGSAIQRLKVKTASPFlPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1771853535 1386 GMDPEGQQQMWQAIRATFRnteRGA--LLTTHYMAEAEAVCDRVAIMVSGRLR 1436
Cdd:TIGR02633 433 GVDVGAKYEIYKLINQLAQ---EGVaiIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1246-1450 |
8.09e-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: 8.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1246 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDT----KPTAGQVLLKGSGGGDALEF----LGYCPQENALWPNLTVRQ 1317
Cdd:TIGR00956 78 KPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTdgfhIGVEGVITYDGITPEEIKKHyrgdVVYNAETDVHFPHLTVGE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1318 HLEVYAAVKGlrKGDAEVAITRLVDALKLQDQLKSP---------------VKTLSEGIKRKLCFVLSILGNPSVVLLDE 1382
Cdd:TIGR00956 158 TLDFAARCKT--PQNRPDGVSREEYAKHIADVYMATyglshtrntkvgndfVRGVSGGERKRVSIAEASLGGAKIQCWDN 235
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1383 PSTGMDPEGQQQMWQAIRATFRNTERGALLTThYMAEAEA--VCDRVAIMVSGRLRCIGSIQHLKSKFGK 1450
Cdd:TIGR00956 236 ATRGLDSATALEFIRALKTSANILDTTPLVAI-YQCSQDAyeLFDKVIVLYEGYQIYFGPADKAKQYFEK 304
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1246-1434 |
8.34e-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: 8.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1246 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSgggdalefLGYCPQENalW-PNLTVRQHL----- 1319
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--------IAYVSQEP--WiQNGTIRENIlfgkp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1320 ---EVYAAVkglrkgdaevaitrlVDALKLQDQLKSPVK-----------TLSEGIKRKLCFVLSILGNPSVVLLDEPST 1385
Cdd:cd03250 92 fdeERYEKV---------------IKACALEPDLEILPDgdlteigekgiNLSGGQKQRISLARAVYSDADIYLLDDPLS 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1386 GMDPE-GQQQMWQAIRATFRNtERGALLTTHYMAEAEAvCDRVAIMVSGR 1434
Cdd:cd03250 157 AVDAHvGRHIFENCILGLLLN-NKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
340-612 |
9.35e-08 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 55.47 E-value: 9.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 340 TNFMLAFDTCLYLALAIYFEKILPNEYGHRRPPLFFL-------KSSFWSQTQKTDHVALEDEMDADPSFHDSFEQAPPE 412
Cdd:pfam13304 13 SNLLEALRFLADFDALVIGLTDERSRNGGIGGIPSLLngidpkePIEFEISEFLEDGVRYRYGLDLEREDVEEKLSSKPT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 413 FQGKEAIRIRNVTKEYKGKPDKIEALKDLVFDIYEGQITAIL---GHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEM 489
Cdd:pfam13304 93 LLEKRLLLREDSEEREPKFPPEAEELRLGLDVEERIELSLSElsdLISGLLLLSIISPLSFLLLLDEGLLLEDWAVLDLA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 490 ADLENLSKLTGVCPQSNVQFDFLTVRENLRLFAKIKGILpqEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIA 569
Cdd:pfam13304 173 ADLALFPDLKELLQRLVRGLKLADLNLSDLGEGIEKSLL--VDDRLRERGLILLENGGGGELPAFELSDGTKRLLALLAA 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1771853535 570 ILGDPQ---IFLLDEPTAGLDPFSRHQVWNLLKERKTDRV-ILFSTQ 612
Cdd:pfam13304 251 LLSALPkggLLLIDEPESGLHPKLLRRLLELLKELSRNGAqLILTTH 297
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1246-1423 |
9.35e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 56.66 E-value: 9.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1246 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSG----GGDAL-----EFLGYCPQENALWPNLTVR 1316
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDvatlDADALaqlrrEHFGFIFQRYHLLSHLTAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1317 QHLEVYAAVKGL----RKGDAEVAITRlvdaLKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPE-G 1391
Cdd:PRK10535 105 QNVEVPAVYAGLerkqRLLRAQELLQR----LGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHsG 180
|
170 180 190
....*....|....*....|....*....|....*
gi 1771853535 1392 QQQMwqAIRATFRNTERGALLTTH---YMAEAEAV 1423
Cdd:PRK10535 181 EEVM--AILHQLRDRGHTVIIVTHdpqVAAQAERV 213
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1246-1453 |
9.49e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 55.03 E-value: 9.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1246 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITG--DTKPTAGQVLLKGSgggDALEFLgycPQEnalwpnltvRQHLEVYA 1323
Cdd:CHL00131 24 KGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGE---SILDLE---PEE---------RAHLGIFL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1324 A------VKGLRKGDaevaITRLVDALKLQDQLKSPVKTLS--EGIKRKLCFV------LS------------------- 1370
Cdd:CHL00131 89 AfqypieIPGVSNAD----FLRLAYNSKRKFQGLPELDPLEflEIINEKLKLVgmdpsfLSrnvnegfsggekkrneilq 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1371 -ILGNPSVVLLDEPSTGMDPEGQQQMWQAIRaTFRNTERGALLTTHYMAEAEAVC-DRVAIMVSGRLRCIGSIQ--HLKS 1446
Cdd:CHL00131 165 mALLDSELAILDETDSGLDIDALKIIAEGIN-KLMTSENSIILITHYQRLLDYIKpDYVHVMQNGKIIKTGDAElaKELE 243
|
....*..
gi 1771853535 1447 KFGKDYL 1453
Cdd:CHL00131 244 KKGYDWL 250
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1255-1388 |
9.71e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 56.81 E-value: 9.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1255 GEVLGLLGHNGAGKSTSIKVITGDTKPT--AGQVLLKGSG-GGDALEFLGYCPQENALWPNLTVRQHLeVYAAVKGLRKG 1331
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKpTKQILKRTGFVTQDDILYPHLTVRETL-VFCSLLRLPKS 172
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1771853535 1332 DAEVAITRLVDAL-------KLQDQL--KSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMD 1388
Cdd:PLN03211 173 LTKQEKILVAESViselgltKCENTIigNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
397-600 |
1.15e-07 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 56.23 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 397 DADPSFhdsfEQAPPEFQGKEAIRIRNVTKEYKGK-------PDKIEALKDLVFDIYEGQITAILGHSGAGKSTL-LNIL 468
Cdd:COG4172 258 AAEPRG----DPRPVPPDAPPLLEARDLKVWFPIKrglfrrtVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 469 sGLsVPTKGSVTIYNNKLSEMADLENLSKltgvcpQSNVQFDF----------LTVR----ENLRLFAkiKGILPQEVDK 534
Cdd:COG4172 334 -RL-IPSEGEIRFDGQDLDGLSRRALRPL------RRRMQVVFqdpfgslsprMTVGqiiaEGLRVHG--PGLSAAERRA 403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1771853535 535 EIQRVLLELEMkniqDVLAQN-----LSGGQKRKLtfGIA---ILgDPQIFLLDEPTAGLDPFSRHQVWNLLKE 600
Cdd:COG4172 404 RVAEALEEVGL----DPAARHrypheFSGGQRQRI--AIAralIL-EPKLLVLDEPTSALDVSVQAQILDLLRD 470
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
448-631 |
1.77e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 56.27 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 448 GQITAILGHSGAGKSTLLNILSGLSVPTKGSVT--IYNNKLSEmADLENLSKLTGV-CPQSNVQFDFLTVRENLRLFAKI 524
Cdd:TIGR00956 87 GELTVVLGRPGSGCSTLLKTIASNTDGFHIGVEgvITYDGITP-EEIKKHYRGDVVyNAETDVHFPHLTVGETLDFAARC 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 525 KGilPQE----VDKEIQRV-LLELEMK----------NIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPF 589
Cdd:TIGR00956 166 KT--PQNrpdgVSREEYAKhIADVYMAtyglshtrntKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSA 243
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1771853535 590 SRHQVWNLLkerKTDRVILFSTQFM------DEADILADRKVFLSQGK 631
Cdd:TIGR00956 244 TALEFIRAL---KTSANILDTTPLVaiyqcsQDAYELFDKVIVLYEGY 288
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1236-1436 |
2.05e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 54.27 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1236 FSKRKNKIaTRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITgDTKPTAGQVLLKGSgggdaLEFLGYCPQENALWPNLTV 1315
Cdd:PRK14258 15 FYYDTQKI-LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLN-RMNELESEVRVEGR-----VEFFNQNIYERRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1316 RQ-----------HLEVYAAVK-GLR------KGDAEVAITRLVDALKLQDQLKSPVKT----LSEGIKRKLCFVLSILG 1373
Cdd:PRK14258 88 RQvsmvhpkpnlfPMSVYDNVAyGVKivgwrpKLEIDDIVESALKDADLWDEIKHKIHKsaldLSGGQQQRLCIARALAV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1771853535 1374 NPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLR 1436
Cdd:PRK14258 168 KPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENR 230
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1247-1415 |
2.48e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 53.18 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1247 NVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSgggDALEF--------LGYCPQENALWPNlTVRQH 1318
Cdd:PRK10247 25 NISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGE---DISTLkpeiyrqqVSYCAQTPTLFGD-TVYDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1319 LEVYAAVKGlrKGDAEVAITRLVDALKLQDQ-LKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQ 1397
Cdd:PRK10247 101 LIFPWQIRN--QQPDPAIFLDDLERFALPDTiLTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNE 178
|
170
....*....|....*...
gi 1771853535 1398 AIRATFRNTERGALLTTH 1415
Cdd:PRK10247 179 IIHRYVREQNIAVLWVTH 196
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
438-595 |
2.55e-07 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 54.09 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 438 LKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGsvtiynnKLSEMADLENLSKLTGVCPQsnvqfdflTVREN 517
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEG-------KIKHSGRISFSSQFSWIMPG--------TIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 518 LrlfakIKGILPQEVDKE--IQRVLLELEMKNIQD----VLAQ---NLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDP 588
Cdd:cd03291 118 I-----IFGVSYDEYRYKsvVKACQLEEDITKFPEkdntVLGEggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
....*..
gi 1771853535 589 FSRHQVW 595
Cdd:cd03291 193 FTEKEIF 199
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
422-598 |
2.57e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 54.59 E-value: 2.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 422 RNVTKEY---KG---KPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEmADLENL 495
Cdd:PRK11308 9 IDLKKHYpvkRGlfkPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLK-ADPEAQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 496 SKLtgvcpQSNVQFDFLTVRENLRLFAKIKGILpqEVDKEIQRVLLELEMK-NIQDVLAQ-------------NLSGGQK 561
Cdd:PRK11308 88 KLL-----RQKIQIVFQNPYGSLNPRKKVGQIL--EEPLLINTSLSAAERReKALAMMAKvglrpehydryphMFSGGQR 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 1771853535 562 RKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLL 598
Cdd:PRK11308 161 QRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLM 197
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
416-608 |
2.64e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.81 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 416 KEAIRIRNVTKEYKGKPDkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNIL--------------------------- 468
Cdd:PTZ00265 1163 KGKIEIMDVNFRYISRPN-VPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtndmtneqd 1241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 469 --------------SGLSVPTKGS----VTIYNNKLSEMAD--------LENLSKLTGVCPQSNVQFDfLTVRENLRlFA 522
Cdd:PTZ00265 1242 yqgdeeqnvgmknvNEFSLTKEGGsgedSTVFKNSGKILLDgvdicdynLKDLRNLFSIVSQEPMLFN-MSIYENIK-FG 1319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 523 KIKGILpQEVDK-----EIQRVLLELEMKNIQDV--LAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVW 595
Cdd:PTZ00265 1320 KEDATR-EDVKRackfaAIDEFIESLPNKYDTNVgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIE 1398
|
250
....*....|....*
gi 1771853535 596 NLLKE--RKTDRVIL 608
Cdd:PTZ00265 1399 KTIVDikDKADKTII 1413
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1240-1438 |
3.71e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.74 E-value: 3.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1240 KNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGS--GGGDALEFL----------------- 1300
Cdd:PRK10982 259 LRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKkiNNHNANEAInhgfalvteerrstgiy 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1301 GYCPQE-NALWPNltVRQHLEVYAAVKGLR-KGDAEVAItrlvDALKLQD-QLKSPVKTLSEGIKRKLCFVLSILGNPSV 1377
Cdd:PRK10982 339 AYLDIGfNSLISN--IRNYKNKVGLLDNSRmKSDTQWVI----DSMRVKTpGHRTQIGSLSGGNQQKVIIGRWLLTQPEI 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1771853535 1378 VLLDEPSTGMDPEGQQQMWQAIrATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCI 1438
Cdd:PRK10982 413 LMLDEPTRGIDVGAKFEIYQLI-AELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGI 472
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1247-1390 |
4.41e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.35 E-value: 4.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1247 NVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsggGDALEfLGYCPQE-NALWPNLTvrqhleVYAAV 1325
Cdd:PRK11819 342 DLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-----GETVK-LAYVDQSrDALDPNKT------VWEEI 409
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1771853535 1326 KG----LRKGDAEVAITRLVDA--LKLQDQLKsPVKTLSEGiKRK---LCFVLSILGNpsVVLLDEPSTGMDPE 1390
Cdd:PRK11819 410 SGgldiIKVGNREIPSRAYVGRfnFKGGDQQK-KVGVLSGG-ERNrlhLAKTLKQGGN--VLLLDEPTNDLDVE 479
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
438-612 |
4.60e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 52.26 E-value: 4.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 438 LKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSV-----TIYNNKLSEMADLENLSKLTGVCPqsnvqfdFL 512
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEIlferqSIKKDLCTYQKQLCFVGHRSGINP-------YL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 513 TVRENLrLFakikGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRH 592
Cdd:PRK13540 90 TLRENC-LY----DIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLL 164
|
170 180
....*....|....*....|..
gi 1771853535 593 QVWNLLKE--RKTDRVILFSTQ 612
Cdd:PRK13540 165 TIITKIQEhrAKGGAVLLTSHQ 186
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
434-609 |
4.72e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.48 E-value: 4.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 434 KIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADlenlSKLTGVcpQSNVQFDF-- 511
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSP----GKLQAL--RRDIQFIFqd 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 512 --------LTVRENLRLFAKIKGILPQEVDKEiqRVLLELEMKNIQDVLA----QNLSGGQKRKLTFGIAILGDPQIFLL 579
Cdd:PRK10261 410 pyasldprQTVGDSIMEPLRVHGLLPGKAAAA--RVAWLLERVGLLPEHAwrypHEFSGGQRQRICIARALALNPKVIIA 487
|
170 180 190
....*....|....*....|....*....|
gi 1771853535 580 DEPTAGLDPFSRHQVWNLLKERKTDRVILF 609
Cdd:PRK10261 488 DEAVSALDVSIRGQIINLLLDLQRDFGIAY 517
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
420-470 |
4.83e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 54.41 E-value: 4.83e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1771853535 420 RIRNVTKEYKGkpdkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSG 470
Cdd:NF040905 3 EMRGITKTFPG----VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1239-1449 |
5.12e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 54.34 E-value: 5.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1239 RKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSgggDALEF--------LGYCPQENALW 1310
Cdd:TIGR00958 491 RPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGV---PLVQYdhhylhrqVALVGQEPVLF 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1311 pNLTVRQHLevyaaVKGLRKG-DAEV-AITRLVDALKLQDQLKSPVKT--------LSEGIKRKLCFVLSILGNPSVVLL 1380
Cdd:TIGR00958 568 -SGSVRENI-----AYGLTDTpDEEImAAAKAANAHDFIMEFPNGYDTevgekgsqLSGGQKQRIAIARALVRKPRVLIL 641
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1771853535 1381 DEPSTGMDPEGQQQMWQAIRAtfrnTERGALLTTHYMAEAEAvCDRVAIMVSGRLRCIGSIQHLKSKFG 1449
Cdd:TIGR00958 642 DEATSALDAECEQLLQESRSR----ASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQG 705
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1253-1388 |
6.97e-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: 6.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1253 RKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQ---------VL--LKGSGGGDALEFLgycpQENalwpNLTVR---QH 1318
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDydeepswdeVLkrFRGTELQDYFKKL----ANG----EIKVAhkpQY 168
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1771853535 1319 LEVYA-AVKG-----LRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMD 1388
Cdd:COG1245 169 VDLIPkVFKGtvrelLEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
438-603 |
7.69e-07 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 50.62 E-value: 7.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 438 LKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIynnklsemadlenlskltgvCPQSNVQFdfltvren 517
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM--------------------PEGEDLLF-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 518 lrlfakikgiLPQevdkeiqRVLLELemKNIQDVLA----QNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQ 593
Cdd:cd03223 69 ----------LPQ-------RPYLPL--GTLREQLIypwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDR 129
|
170
....*....|
gi 1771853535 594 VWNLLKERKT 603
Cdd:cd03223 130 LYQLLKELGI 139
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1244-1434 |
7.83e-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: 7.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1244 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGdTKPTA---GQVL-----LKGSGGGDALEF-LGYCPQENALWPNLT 1314
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHGtwdGEIYwsgspLKASNIRDTERAgIVIIHQELTLVPELS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1315 VRQHL----EVyaAVKGLRKGDAevAITRLVDALKLQDQLKS-----PVKTLSEGIKRKLCFVLSILGNPSVVLLDEPST 1385
Cdd:TIGR02633 95 VAENIflgnEI--TLPGGRMAYN--AMYLRAKNLLRELQLDAdnvtrPVGDYGGGQQQLVEIAKALNKQARLLILDEPSS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1771853535 1386 GMDPEGQQQMWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1434
Cdd:TIGR02633 171 SLTEKETEILLDIIR-DLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
443-631 |
7.89e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.48 E-value: 7.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 443 FDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSvtiYNNKLSEMADL--ENLSKLTGVCPQSNvQFDFLTVRENL-- 518
Cdd:PRK10938 24 LTLNAGDSWAFVGANGSGKSALARALAGELPLLSGE---RQSQFSHITRLsfEQLQKLVSDEWQRN-NTDMLSPGEDDtg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 519 RLFAKIkgIlpQEVDKEIQRVLLELEMKNIQDVLAQN---LSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVW 595
Cdd:PRK10938 100 RTTAEI--I--QDEVKDPARCEQLAQQFGITALLDRRfkyLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1771853535 596 NLLKERKTDRVIL------FST--QFMDEADILADRKVFLsQGK 631
Cdd:PRK10938 176 ELLASLHQSGITLvlvlnrFDEipDFVQFAGVLADCTLAE-TGE 218
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1232-1290 |
9.01e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 52.10 E-value: 9.01e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1771853535 1232 RKGCFsKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG 1290
Cdd:PRK15112 17 RTGWF-RRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDD 74
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1241-1428 |
9.32e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 52.09 E-value: 9.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1241 NKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVI--TGDTKPTA---GQVLLKGS----GGGDALEF---LGYCPQENA 1308
Cdd:PRK14243 22 SFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPGFrveGKVTFHGKnlyaPDVDPVEVrrrIGMVFQKPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1309 LWPNlTVRQHLEVYAAVKGLrKGDAEVAITRLVDALKLQDQLKSPVKT----LSEGIKRKLCFVLSILGNPSVVLLDEPS 1384
Cdd:PRK14243 102 PFPK-SIYDNIAYGARINGY-KGDMDELVERSLRQAALWDEVKDKLKQsglsLSGGQQQRLCIARAIAVQPEVILMDEPC 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1771853535 1385 TGMDPEGQQQMWQAIRATFRntERGALLTTHYMAEAEAVCDRVA 1428
Cdd:PRK14243 180 SALDPISTLRIEELMHELKE--QYTIIIVTHNMQQAARVSDMTA 221
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
438-598 |
9.74e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 51.03 E-value: 9.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 438 LKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSemadleNLSK--LTGVCPQSNVQFDfLTVR 515
Cdd:PRK13541 16 LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNIN------NIAKpyCTYIGHNLGLKLE-MTVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 516 ENLRLFAKIkgilpQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVW 595
Cdd:PRK13541 89 ENLKFWSEI-----YNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLN 163
|
...
gi 1771853535 596 NLL 598
Cdd:PRK13541 164 NLI 166
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
410-637 |
1.13e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.59 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 410 PPEFQGKEAIRIRNVTKEYKGKPDKiEALKDLVFDIYEGQITAILGHSGAGKSTLLN-ILSGLSVPTKGSVTIYNNklse 488
Cdd:PLN03130 606 PPLEPGLPAISIKNGYFSWDSKAER-PTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGT---- 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 489 madlenlsklTGVCPQSNVQFDfLTVRENLrLFAkikgiLPQEVDK--------EIQRVLLELEMKNIQDVLAQ--NLSG 558
Cdd:PLN03130 681 ----------VAYVPQVSWIFN-ATVRDNI-LFG-----SPFDPERyeraidvtALQHDLDLLPGGDLTEIGERgvNISG 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 559 GQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWN-LLKE--RKTDRViLFSTQ--FMDEadilADRKVFLSQGKLK 633
Cdd:PLN03130 744 GQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDkCIKDelRGKTRV-LVTNQlhFLSQ----VDRIILVHEGMIK 818
|
....
gi 1771853535 634 CAGS 637
Cdd:PLN03130 819 EEGT 822
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1241-1392 |
1.15e-06 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 51.91 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1241 NKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGS-----GGGDALEFLGYCPQeNALWP-NLT 1314
Cdd:PRK10253 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEhiqhyASKEVARRIGLLAQ-NATTPgDIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1315 VRQ--------HLEVYAAvkgLRKGDAEvAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTG 1386
Cdd:PRK10253 98 VQElvargrypHQPLFTR---WRKEDEE-AVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
....*.
gi 1771853535 1387 MDPEGQ 1392
Cdd:PRK10253 174 LDISHQ 179
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1252-1388 |
1.22e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.27 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1252 VRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQ---------VL--LKGSGGGDALEFL-------GYCPQENALWPNl 1313
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDyeeepswdeVLkrFRGTELQNYFKKLyngeikvVHKPQYVDLIPK- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1314 tvrqhlevyaAVKG-----LRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMD 1388
Cdd:PRK13409 175 ----------VFKGkvrelLKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1242-1390 |
1.72e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 52.65 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1242 KIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsggGDALEfLGYCPQENA-LWPNLTVrqhle 1320
Cdd:PRK11147 332 KQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-----GTKLE-VAYFDQHRAeLDPEKTV----- 400
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1771853535 1321 vyaaVKGLRKGDAEVAIT-RLVDALK-LQDQL------KSPVKTLSEGIKRKLcFVLSILGNPSVVL-LDEPSTGMDPE 1390
Cdd:PRK11147 401 ----MDNLAEGKQEVMVNgRPRHVLGyLQDFLfhpkraMTPVKALSGGERNRL-LLARLFLKPSNLLiLDEPTNDLDVE 474
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1224-1440 |
1.87e-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: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1224 LRKEYAGKRKgcfskrknkiATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGD-------- 1295
Cdd:PRK11650 9 VRKSYDGKTQ----------VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNElepadrdi 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1296 ALEFLGYcpqenALWPNLTVRQHLEvYA-AVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGN 1374
Cdd:PRK11650 79 AMVFQNY-----ALYPHMSVRENMA-YGlKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVRE 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1771853535 1375 PSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1440
Cdd:PRK11650 153 PAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGT 218
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1262-1390 |
2.39e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 49.87 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1262 GHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGD-ALEFLGYCPQENALWPNLTVRQHLEVYAAVKglrkgDAEVAITRL 1340
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNiAKPYCTYIGHNLGLKLEMTVFENLKFWSEIY-----NSAETLYAA 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1341 VDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1390
Cdd:PRK13541 108 IHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKE 157
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1244-1277 |
3.60e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.47 E-value: 3.60e-06
10 20 30
....*....|....*....|....*....|....
gi 1771853535 1244 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITG 1277
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG 53
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
1248-1382 |
3.61e-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: 3.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1248 VSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsgGGDALEflgycpQENALWpnltVRQHlevYAAV-- 1325
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILL----DGQPVT------ADNREA----YRQL---FSAVfs 413
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1771853535 1326 --------KGLRKGDAEVAITRLVDALKLQDQLK------SPVKtLSEGIKRKLCFVLSILGNPSVVLLDE 1382
Cdd:COG4615 414 dfhlfdrlLGLDGEADPARARELLERLELDHKVSvedgrfSTTD-LSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
432-470 |
3.66e-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: 3.66e-06
10 20 30
....*....|....*....|....*....|....*....
gi 1771853535 432 PDKIEALKDLVfdiyEGQITAILGHSGAGKSTLLNILSG 470
Cdd:cd01854 73 GEGLDELRELL----KGKTSVLVGQSGVGKSTLLNALLP 107
|
|
| RsgA |
COG1162 |
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis]; |
435-470 |
4.42e-06 |
|
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440776 [Multi-domain] Cd Length: 300 Bit Score: 50.50 E-value: 4.42e-06
10 20 30
....*....|....*....|....*....|....*.
gi 1771853535 435 IEALKDLVfdiyEGQITAILGHSGAGKSTLLNILSG 470
Cdd:COG1162 157 LDELRELL----KGKTSVLVGQSGVGKSTLINALLP 188
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
419-586 |
5.44e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 50.77 E-value: 5.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGkpdkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGS-------VTIYNNKLSEMAD 491
Cdd:PRK10762 5 LQLKGIDKAFPG----VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSilylgkeVTFNGPKSSQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 492 LENLSKLTGVCPQsnvqfdfLTVRENL---RLFAKIKG-ILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFG 567
Cdd:PRK10762 81 IGIIHQELNLIPQ-------LTIAENIflgREFVNRFGrIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIA 153
|
170
....*....|....*....
gi 1771853535 568 IAILGDPQIFLLDEPTAGL 586
Cdd:PRK10762 154 KVLSFESKVIIMDEPTDAL 172
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1247-1435 |
5.65e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 49.74 E-value: 5.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1247 NVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG------SGGGDALEF---LGYCPQ--ENALWPNlTV 1315
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtlitstSKNKDIKQIrkkVGLVFQfpESQLFEE-TV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1316 RQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQL--KSPVKtLSEGIKRKLCfVLSILG-NPSVVLLDEPSTGMDPEGQ 1392
Cdd:PRK13649 104 LKDVAFGPQNFGVSQEEAEALAREKLALVGISESLfeKNPFE-LSGGQMRRVA-IAGILAmEPKILVLDEPTAGLDPKGR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1771853535 1393 QQMWQairaTFRNTERGAL---LTTHYMAEAEAVCDRVAIMVSGRL 1435
Cdd:PRK13649 182 KELMT----LFKKLHQSGMtivLVTHLMDDVANYADFVYVLEKGKL 223
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1214-1290 |
8.92e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 49.58 E-value: 8.92e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1771853535 1214 DEKPVIIASCLRKEYAGKRkGCFSKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG 1290
Cdd:PRK11308 1 SQQPLLQAIDLKKHYPVKR-GLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQG 76
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1247-1415 |
1.06e-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: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1247 NVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKP---TAGQVLLKGSGGGDALE-FLGYCPQENALWPNLTVRQHLEVY 1322
Cdd:TIGR00956 781 NVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLDSSFQrSIGYVQQQDLHLPTSTVRESLRFS 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1323 AAvkgLRKgDAEVAIT---RLVDA----LKLQDQLKSPVKTLSEGI----KRKLCFVLSILGNP-SVVLLDEPSTGMDPE 1390
Cdd:TIGR00956 861 AY---LRQ-PKSVSKSekmEYVEEviklLEMESYADAVVGVPGEGLnveqRKRLTIGVELVAKPkLLLFLDEPTSGLDSQ 936
|
170 180
....*....|....*....|....*
gi 1771853535 1391 GQQQMWQAIRATfRNTERGALLTTH 1415
Cdd:TIGR00956 937 TAWSICKLMRKL-ADHGQAILCTIH 960
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
410-481 |
1.75e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 49.35 E-value: 1.75e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1771853535 410 PPEFQGKEAIRIRNVTKEYKgkpDKIeALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTI 481
Cdd:PRK11819 316 PGPRLGDKVIEAENLSKSFG---DRL-LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1232-1449 |
1.94e-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: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1232 RKGCFSKRKNKIATRN-VSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSgggdalefLGYCPQEnALW 1310
Cdd:TIGR00957 640 HNATFTWARDLPPTLNgITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--------VAYVPQQ-AWI 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1311 PNLTVRQHLEVYAAVKGLRKGDAEVAITRLVD--ALKLQDQLKSPVK--TLSEGIKRKLCFVLSILGNPSVVLLDEPSTG 1386
Cdd:TIGR00957 711 QNDSLRENILFGKALNEKYYQQVLEACALLPDleILPSGDRTEIGEKgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSA 790
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1771853535 1387 MDPEGQQQMWQAI---RATFRNTERgaLLTTHYMAEAEAVcDRVAIMVSGRLRCIGSIQHLKSKFG 1449
Cdd:TIGR00957 791 VDAHVGKHIFEHVigpEGVLKNKTR--ILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQRDG 853
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
419-611 |
2.44e-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: 48.91 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 419 IRIRNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKS-TLLNIL----SGLSVPTkGSVTiYNNK----LSEm 489
Cdd:COG4172 7 LSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILrllpDPAAHPS-GSIL-FDGQdllgLSE- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 490 ADL-------------ENLSKLTGVcpqsnvqfdfLTV----RENLRLFAKIKGilpqevdKEI-QRVLLELEMKNIQDV 551
Cdd:COG4172 84 RELrrirgnriamifqEPMTSLNPL----------HTIgkqiAEVLRLHRGLSG-------AAArARALELLERVGIPDP 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1771853535 552 ---LAQ---NLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFST 611
Cdd:COG4172 147 errLDAyphQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDlqRELGMALLLIT 214
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1246-1388 |
2.64e-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: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1246 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVllKGSGGgdalefLGYCPQENALWPNlTVRQHLevyaaV 1325
Cdd:TIGR01271 443 KNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI--KHSGR------ISFSPQTSWIMPG-TIKDNI-----I 508
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1771853535 1326 KGLRKGdaEVAITRLVDALKLQDQL-KSPVK----------TLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMD 1388
Cdd:TIGR01271 509 FGLSYD--EYRYTSVIKACQLEEDIaLFPEKdktvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
438-587 |
2.77e-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: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 438 LKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTiYNNKLSemadlenlskltgVCPqsnvQFDFL---TV 514
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK-HSGRIS-------------FSP----QTSWImpgTI 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 515 RENLRLFAKIKGILPQEVDKEIQrvlLELEMKNIQD----VLAQ---NLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLD 587
Cdd:TIGR01271 504 KDNIIFGLSYDEYRYTSVIKACQ---LEEDIALFPEkdktVLGEggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
432-470 |
3.07e-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: 46.00 E-value: 3.07e-05
10 20 30
....*....|....*....|....*....|....*....
gi 1771853535 432 PDKIEALKDLVfdiyEGQITAILGHSGAGKSTLLNILSG 470
Cdd:pfam03193 94 GEGIEALKELL----KGKTTVLAGQSGVGKSTLLNALLP 128
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1244-1277 |
5.03e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.86 E-value: 5.03e-05
10 20 30
....*....|....*....|....*....|....
gi 1771853535 1244 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITG 1277
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1246-1398 |
5.19e-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: 46.77 E-value: 5.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1246 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVllKGSGGgdalefLGYCPQENALWPNlTVRQHLEVYAAV 1325
Cdd:cd03291 54 KNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI--KHSGR------ISFSSQFSWIMPG-TIKENIIFGVSY 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1771853535 1326 KGLRKGDAEVAITRLVDALKLQDQLKSPVK----TLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQA 1398
Cdd:cd03291 125 DEYRYKSVVKACQLEEDITKFPEKDNTVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFES 201
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1214-1270 |
5.56e-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: 5.56e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1771853535 1214 DEKPVIIASCLRKEYAGKRkGCFSKRKNKI-ATRNVSFCVRKGEVLGLLGHNGAGKST 1270
Cdd:COG4172 271 DAPPLLEARDLKVWFPIKR-GLFRRTVGHVkAVDGVSLTLRRGETLGLVGESGSGKST 327
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
422-586 |
5.69e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 47.62 E-value: 5.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 422 RNVTKEYKGkpdkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLsVPT---KGSVTIYNNKL--SEMADLENL- 495
Cdd:PRK13549 9 KNITKTFGG----VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEELqaSNIRDTERAg 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 496 -----SKLTGVcPQsnvqfdfLTVRENLRLFAKI--KGILP-QEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFG 567
Cdd:PRK13549 84 iaiihQELALV-KE-------LSVLENIFLGNEItpGGIMDyDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIA 155
|
170
....*....|....*....
gi 1771853535 568 IAILGDPQIFLLDEPTAGL 586
Cdd:PRK13549 156 KALNKQARLLILDEPTASL 174
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1235-1389 |
5.82e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 47.66 E-value: 5.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1235 CFSKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSgggdaleflgycPQENALWPNLt 1314
Cdd:PRK10522 329 TFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK------------PVTAEQPEDY- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1315 vRQHlevYAAV-------KGLRKGDAEVAITRLVDA----LKLQDQLK------SPVKtLSEGIKRKLCFVLSILGNPSV 1377
Cdd:PRK10522 396 -RKL---FSAVftdfhlfDQLLGPEGKPANPALVEKwlerLKMAHKLEledgriSNLK-LSKGQKKRLALLLALAEERDI 470
|
170
....*....|..
gi 1771853535 1378 VLLDEPSTGMDP 1389
Cdd:PRK10522 471 LLLDEWAADQDP 482
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
440-631 |
6.09e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.39 E-value: 6.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 440 DLVFDIYEGQITAILGHSGAGKS-TLLNILSGLSVP----TKGSVTIYNNKLSEmADLENLSKLTG-------------V 501
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLH-ASEQTLRGVRGnkiamifqepmvsL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 502 CPQSNVQ---FDFLTVRENLRLFAKIKGILpqevdKEIQRVLLELEMKNIQDVLAQnLSGGQKRKLTFGIAILGDPQIFL 578
Cdd:PRK15134 106 NPLHTLEkqlYEVLSLHRGMRREAARGEIL-----NCLDRVGIRQAAKRLTDYPHQ-LSGGERQRVMIAMALLTRPELLI 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1771853535 579 LDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGK 631
Cdd:PRK15134 180 ADEPTTALDVSVQAQILQLLRElqQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
421-631 |
8.66e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.03 E-value: 8.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 421 IRNVTKEYKGkpdkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLSKLTG 500
Cdd:PRK10982 1 MSNISKSFPG----VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGIS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 501 VCPQSNVQFDFLTVRENLRLFA-KIKGILpqeVD-----KEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDP 574
Cdd:PRK10982 77 MVHQELNLVLQRSVMDNMWLGRyPTKGMF---VDqdkmyRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1771853535 575 QIFLLDEPTAGLdpfSRHQVWNL------LKERKTDrvILFSTQFMDEADILADRKVFLSQGK 631
Cdd:PRK10982 154 KIVIMDEPTSSL---TEKEVNHLftiirkLKERGCG--IVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
435-475 |
9.80e-05 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 46.35 E-value: 9.80e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1771853535 435 IEALKDLVfdiyEGQITAILGHSGAGKSTLLN-ILSGLSVPT 475
Cdd:PRK00098 155 LDELKPLL----AGKVTVLAGQSGVGKSTLLNaLAPDLELKT 192
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1227-1450 |
1.06e-04 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 46.88 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1227 EYAGKRKGCFskrknkiatrNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGD-ALEFL----G 1301
Cdd:PRK13657 343 SYDNSRQGVE----------DVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTvTRASLrrniA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1302 YCPQENALWpNLTVRQHLEVyaavkGlrKGDAEVAitRLVDALKLQDQL----KSPVK----------TLSEGIKRKLCF 1367
Cdd:PRK13657 413 VVFQDAGLF-NRSIEDNIRV-----G--RPDATDE--EMRAAAERAQAHdfieRKPDGydtvvgergrQLSGGERQRLAI 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1368 VLSILGNPSVVLLDEPSTGMDPEGQQQMWQAI------RATFRNTERgalLTThyMAEAeavcDRVAIMVSGRLRCIGSI 1441
Cdd:PRK13657 483 ARALLKDPPILILDEATSALDVETEAKVKAALdelmkgRTTFIIAHR---LST--VRNA----DRILVFDNGRVVESGSF 553
|
....*....
gi 1771853535 1442 QHLKSKFGK 1450
Cdd:PRK13657 554 DELVARGGR 562
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
439-606 |
1.39e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 44.91 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 439 KDLVFDIYEGqITAILGHSGAGKSTllnILSGLSVPTKGSVTIYNNKLSEMADL----ENLS--KLTgvcpQSNVQFDFL 512
Cdd:cd03240 14 ERSEIEFFSP-LTLIVGQNGAGKTT---IIEALKYALTGELPPNSKGGAHDPKLiregEVRAqvKLA----FENANGKKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 513 TVRENLRLFAKIKgILPQEvdkEIqRVLLELEMKNiqdvlaqnLSGGQKRKLTFGIAI-----LGDP-QIFLLDEPTAGL 586
Cdd:cd03240 86 TITRSLAILENVI-FCHQG---ES-NWPLLDMRGR--------CSGGEKVLASLIIRLalaetFGSNcGILALDEPTTNL 152
|
170 180
....*....|....*....|.
gi 1771853535 587 DPFSR-HQVWNLLKERKTDRV 606
Cdd:cd03240 153 DEENIeESLAEIIEERKSQKN 173
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
437-599 |
1.47e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 46.24 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 437 ALKDLVFDIYEGQITAILGHSGAGKSTllnilSGLS----VPTKGSVTIYNNKLSEMADLENL--------------SKL 498
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKST-----TGLAllrlINSQGEIWFDGQPLHNLNRRQLLpvrhriqvvfqdpnSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 499 TgvcPQSNVQfdfLTVRENLRLFAKIKGILPQEvdkeiQRVLLELEMKNIQDVLAQ----NLSGGQKRKLTFGIAILGDP 574
Cdd:PRK15134 376 N---PRLNVL---QIIEEGLRVHQPTLSAAQRE-----QQVIAVMEEVGLDPETRHrypaEFSGGQRQRIAIARALILKP 444
|
170 180
....*....|....*....|....*
gi 1771853535 575 QIFLLDEPTAGLDPFSRHQVWNLLK 599
Cdd:PRK15134 445 SLIILDEPTSSLDKTVQAQILALLK 469
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1246-1400 |
1.52e-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: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1246 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDAL-EFLGYCPQENALWPNLTVRQhLe 1320
Cdd:COG4604 18 DDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGldvaTTPSRELaKRLAILRQENHINSRLTVRE-L- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1321 V----YAAVKG-LRKGDaEVAITRLVDALKLQDQLKSPVKTLSEGiKRKLCFVLSILG-NPSVVLLDEPSTGMDPEGQQQ 1394
Cdd:COG4604 96 VafgrFPYSKGrLTAED-REIIDEAIAYLDLEDLADRYLDELSGG-QRQRAFIAMVLAqDTDYVLLDEPLNNLDMKHSVQ 173
|
....*.
gi 1771853535 1395 MWQAIR 1400
Cdd:COG4604 174 MMKLLR 179
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
1242-1440 |
2.09e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 46.31 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1242 KIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSgggdalefLGYCPQEnALWPNLTVRQHLEV 1321
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERS--------IAYVPQQ-AWIMNATVRGNILF 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1322 YaavkglrkgDAEVAiTRLVDALKLQD------QLKSPVKT--------LSEGIKRKLCFVLSILGNPSVVLLDEPSTGM 1387
Cdd:PTZ00243 744 F---------DEEDA-ARLADAVRVSQleadlaQLGGGLETeigekgvnLSGGQKARVSLARAVYANRDVYLLDDPLSAL 813
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1771853535 1388 DPE-GQQQMWQAIRATFRNTERgaLLTTHYMaEAEAVCDRVAIMVSGRLRCIGS 1440
Cdd:PTZ00243 814 DAHvGERVVEECFLGALAGKTR--VLATHQV-HVVPRADYVVALGDGRVEFSGS 864
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1248-1447 |
2.24e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.12 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1248 VSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGS-----GGGDALEFLGYCPQENALWPNlTVRQHLEVY 1322
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCdvakfGLTDLRRVLSIIPQSPVLFSG-TVRFNIDPF 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1323 AA------VKGLRKGDAEVAITRlvDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMW 1396
Cdd:PLN03232 1334 SEhndadlWEALERAHIKDVIDR--NPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQ 1411
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1771853535 1397 QAIRATFRNTergALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSK 1447
Cdd:PLN03232 1412 RTIREEFKSC---TMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSR 1459
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1247-1288 |
2.24e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.65 E-value: 2.24e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1771853535 1247 NVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLL 1288
Cdd:PRK15064 19 NISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSL 60
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
448-630 |
2.42e-04 |
|
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: 43.13 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 448 GQITAILGHSGAGKSTLLNILSGLSVPTKGSVtiynnklsEMADLENlskltgvcpqsnvqfdfltvrenlrlfakikgi 527
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV--------IYIDGED--------------------------------- 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 528 lpqevdkeIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLL-------KE 600
Cdd:smart00382 41 --------ILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrllllLK 112
|
170 180 190
....*....|....*....|....*....|....*
gi 1771853535 601 RKTDRVILFSTQFMDEAD-----ILADRKVFLSQG 630
Cdd:smart00382 113 SEKNLTVILTTNDEKDLGpallrRRFDRRIVLLLI 147
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1257-1383 |
3.03e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 44.87 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 1257 VLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDALE--FL-------GYCPQENALWPNLTVRQHLEvYaavkG 1327
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKgiCLppekrriGYVFQDARLFPHYKVRGNLR-Y----G 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1771853535 1328 LRKGDAEvAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEP 1383
Cdd:PRK11144 101 MAKSMVA-QFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEP 155
|
|
| GAAP_like |
cd10429 |
Golgi antiapoptotic protein; GAAP (or transmembrane BAX inhibitor motif containing 4) is a ... |
205-312 |
3.07e-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: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 205 WLSWGLLYAGFIFIMALFLALVIRSTQFIILSGFmvvfSLFLLYGLSLVALAFLMSILVKKSFLTGLVVFLLTV--FWGC 282
Cdd:cd10429 67 WLFLISLIGSLILLIALYWKRHSHPVNLILLSLF----TLCEAYTVGLVVSFYDGKIVLQALILTLGVFVGLTAytFQTK 142
|
90 100 110
....*....|....*....|....*....|
gi 1771853535 283 LGFTSLYRHLPASLeWILSLLSPFAFMLGM 312
Cdd:cd10429 143 RDFSSFGALLFILL-WALILLALIFQFFPY 171
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1232-1271 |
3.43e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 45.08 E-value: 3.43e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1771853535 1232 RKGCFsKRK--NKIATRNVSFCVRKGEVLGLLGHNGAGKSTS 1271
Cdd:PRK15134 288 RKGIL-KRTvdHNVVVKNISFTLRPGETLGLVGESGSGKSTT 328
|
|
| NosY |
COG1277 |
ABC-type transport system involved in multi-copper enzyme maturation, permease component ... |
152-279 |
4.65e-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: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 152 SFIGQSGVITDLYLFSCIISFSSFIYY------ASVNVTRERKR--MKALMTMmGLRDSAF--------WLSWGLLYAgF 215
Cdd:COG1277 36 GGAASGFLGLGLALLASLFSLLSLLLPllapalGMDAISGERESgtLELLLTL-PISRWEIvlgkflgaLLVLLLALL-I 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1771853535 216 IFIMALFLALVIRSTQFIILSGFMVVFSLFLLYGLSLVALAFLMSILVKK---SFLTGLVVFLLTVF 279
Cdd:COG1277 114 TFLLALLLGLLLFGSPPPDLGAILGFYLGLLLLGLAFLAIGLFISALTRNqivAAILAIALWLLLVI 180
|
|
| 7TMR-DISM_7TM |
pfam07695 |
7TM diverse intracellular signalling; This entry represents the transmembrane region of the ... |
206-360 |
1.98e-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: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 206 LSWGLLYaGFIFIMA---LFLALVIRSTQFIILSGFMVVFSLFLLYGLSLVALAFLMSILVKKSFLTGLVVFLLTVFWGC 282
Cdd:pfam07695 3 LLLGLFY-GILLALAlynLFLFFSLRDRSYLYYVLYLLSFLLYQLSLNGLGFQYLWPNAPPWLNNKLLYLSLLLLLPFFA 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1771853535 283 LGFTSLYRHLPASLEWILSLLSPFAFMLGMAQLLhldydlnsnAFPHPSDGSNLIVATNFMLAFDTCLYLALAIYFEK 360
Cdd:pfam07695 82 LLFARSFLELKKYLPRLLRLLLGLALLLALLLLL---------LPLFPYTLSLPLAQLLALLFILFLLLLGIIAWRKG 150
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1236-1290 |
3.36e-03 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 41.62 E-value: 3.36e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1771853535 1236 FSKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG 1290
Cdd:PRK15079 28 WQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLG 82
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1244-1290 |
3.72e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 41.64 E-value: 3.72e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1771853535 1244 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG 1290
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQG 59
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
438-588 |
4.97e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 41.69 E-value: 4.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853535 438 LKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLsVPTKGSVTIYNNKLSEMADLENLSKLTGVCPQSNVQFDFlTVREN 517
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRM-VEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDG-TVRQN 1403
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1771853535 518 LRLFAKIKgilPQEVDKEIQRVLLE----LEMKNIQD-VL--AQNLSGGQKRKLTFGIAILGDPQIF-LLDEPTAGLDP 588
Cdd:PTZ00243 1404 VDPFLEAS---SAEVWAALELVGLRervaSESEGIDSrVLegGSNYSVGQRQLMCMARALLKKGSGFiLMDEATANIDP 1479
|
|
| ABC_MutS2 |
cd03280 |
ATP-binding cassette domain of MutS2; MutS2 homologs in bacteria and eukaryotes. The MutS ... |
1356-1416 |
8.56e-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: 39.15 E-value: 8.56e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1771853535 1356 TLSEGIKRkLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHY 1416
Cdd:cd03280 91 TFSSHMKN-IARILQHADPDSLVLLDELGSGTDPVEGAALAIAILEELLERGALVIATTHY 150
|
|
| |
