|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
480-703 |
3.02e-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: 3.02e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKPDKieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIynNKLSEMADLENLSKL 559
Cdd:cd03263 1 LQIRNLTKTYKKGTKP--AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYI--NGYSIRTDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 TGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFL 639
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 572882597 640 LDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGSSLFLK 703
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1285-1506 |
1.03e-84 |
|
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: 1.03e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1285 LRKEYagkrkgcfsKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDALEF 1360
Cdd:cd03263 6 LTKTY---------KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirTDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1361 LGYCPQENALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVL 1440
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 572882597 1441 LDEPSTGMDPEGQQQMWQAIRATFRNteRGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLK 1506
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVRKG--RSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
235-790 |
4.78e-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: 4.78e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 235 SFIYYASVNVT----RERKRMKALMTMMGLRDSAFWLSWgLLYAGFIFIMALFL-ALVIRSTQFIILSGFMVVFSLFLLY 309
Cdd:TIGR01257 662 AWIYSVSMTVKsivlEKELRLKETLKNQGVSNAVIWCTW-FLDSFSIMSMSIFLlTIFIMHGRILHYSDPFILFLFLLAF 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 310 GLSLVALAFLMSILVKKSFL----TGLVVFLLTV-FWGCLGFTSlyrHLPASLEWILSLLSPFAFMLGMAQLLHLDYD-- 382
Cdd:TIGR01257 741 STATIMQCFLLSTFFSKASLaaacSGVIYFTLYLpHILCFAWQD---RMTADLKTAVSLLSPVAFGFGTEYLVRFEEQgl 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 383 ----LNSNAFPHPSDGSNLIVATNFMLaFDTCLYLALAIYFEKILPNEYGHRRPPLFFLKSSFW-----------SQTQK 447
Cdd:TIGR01257 818 glqwSNIGNSPLEGDEFSFLLSMKMML-LDAALYGLLAWYLDQVFPGDYGTPLPWYFLLQESYWlggegcstreeRALEK 896
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 448 TDHVALEDEMDADPS-FHDSF-EQAPPEFQgkEAIRIRNVTK--EYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKS 523
Cdd:TIGR01257 897 TEPLTEEMEDPEHPEgINDSFfERELPGLV--PGVCVKNLVKifEPSGRP----AVDRLNITFYENQITAFLGHNGAGKT 970
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 524 TLLNILSGLSVPTKGSVTIYNNKLSemADLENLSKLTGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLE 603
Cdd:TIGR01257 971 TTLSILTGLLPPTSGTVLVGGKDIE--TNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLED 1048
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 604 LEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEADILAD 683
Cdd:TIGR01257 1049 TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGD 1128
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 684 RKVFLSQGKLKCAGSSLFLKKKWGIGYHLSL--QLNEI------------------------CVEE------------NI 725
Cdd:TIGR01257 1129 RIAIISQGRLYCSGTPLFLKNCFGTGFYLTLvrKMKNIqsqrggcegtcsctskgfstrcpaRVDEitpeqvldgdvnEL 1208
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 572882597 726 TSLVKQHIPDAKLSAKSEGKLIYTLPLE--RTNKFPELYKDL-DSYPDLGIENYGVSMTTLNEVFLKL 790
Cdd:TIGR01257 1209 MDLVYHHVPEAKLVECIGQELIFLLPNKnfKQRAYASLFRELeETLADLGLSSFGISDTPLEEIFLKV 1276
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1298-1509 |
3.53e-73 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 243.82 E-value: 3.53e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1298 SKR-KNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDALEFLGYCPQENALWP 1372
Cdd:COG1131 7 TKRyGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGedvaRDPAEVRRRIGYVPQEPALYP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1373 NLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEG 1452
Cdd:COG1131 87 DLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 572882597 1453 QQQMWQAIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKF 1509
Cdd:COG1131 167 RRELWELLRE-LAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
480-698 |
1.52e-69 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 233.42 E-value: 1.52e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEmaDLENLSKL 559
Cdd:COG1131 1 IEVRGLTKRYGDKT----ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR--DPAEVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 TGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFL 639
Cdd:COG1131 75 IGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 640 LDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS 698
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRElAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGT 214
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1033-1598 |
3.41e-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: 3.41e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1033 SSCPPYIAMSSIDDYKNRARSQLRISGLSPSAYWFGQALVDVSLY-----FLVFVFIYLMSYISNFEDMLLTIIHIIQIp 1107
Cdd:TIGR01257 1691 SFVPASFVLYLIQERVNKAKHLQFISGVSPTTYWLTNFLWDIMNYavsagLVVGIFIGFQKKAYTSPENLPALVALLML- 1769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1108 cavgYSFSLIFMTYVISFIFRKGRKNSGIWSFCFYVVTVFSVA-GFAFSIFESD------------IPFIFTFLIPPATM 1174
Cdd:TIGR01257 1770 ----YGWAVIPMMYPASFLFDVPSTAYVALSCANLFIGINSSAiTFVLELFENNrtllrfnamlrkLLIVFPHFCLGRGL 1845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1175 IGCLFLSSHLLFSSLFSEERmDVQPFL-------VFLIPFLHFIIFLFTLRCLEWKFGKKSMRKDPFFRISPRSSDVCQn 1247
Cdd:TIGR01257 1846 IDLALSQAVTDVYAQFGEEH-SANPFQwdligknLVAMAVEGVVYFLLTLLIQHHFFLSRWIAEPAKEPIFDEDDDVAE- 1923
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1248 peepegededvqmERVRTANALNSTNfdekpVIIASCLRKEYAGKrkgcfskrkNKIATRNVSFCVRKGEVLGLLGHNGA 1327
Cdd:TIGR01257 1924 -------------ERQRIISGGNKTD-----ILRLNELTKVYSGT---------SSPAVDRLCVGVRPGECFGLLGVNGA 1976
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1328 GKSTSIKVITGDTKPTAGQVLLKG----SGGGDALEFLGYCPQENALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVD 1403
Cdd:TIGR01257 1977 GKTTTFKMLTGDTTVTSGDATVAGksilTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQ 2056
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1404 ALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNtERGALLTTHYMAEAEA 1483
Cdd:TIGR01257 2057 SLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEA 2135
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1484 VCDRVAIMVSGRLRCIGSIQHLKSKFGKDYLLEMKVKN-----LAQVEPLHAEILRLFPQAARQERYSSLMVYKLPVEDv 1558
Cdd:TIGR01257 2136 LCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMKIKSpkddlLPDLNPVEQFFQGNFPGSVQRERHYNMLQFQVSSSS- 2214
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 572882597 1559 qpLAQAFFKLEKVKQSFDLEEYSLSQSTLEQVFLELSKEQ 1598
Cdd:TIGR01257 2215 --LARIFQLLISHKDSLLIEEYSVTQTTLDQVFVNFAKQQ 2252
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
480-698 |
1.20e-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: 205.48 E-value: 1.20e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIyNNKLSEMADLENLSKL 559
Cdd:COG4555 2 IEVENLSKKYGKVP----ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILI-DGEDVRKEPREARRQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 tGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFL 639
Cdd:COG4555 77 -GVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 640 LDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS 698
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRAlKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGS 215
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1301-1529 |
5.18e-56 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 195.08 E-value: 5.18e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1301 KNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGD----ALEFLGYCPQENALWPNLTV 1376
Cdd:COG4555 12 GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKepreARRQIGVLPDERGLYDRLTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1377 RQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQM 1456
Cdd:COG4555 92 RENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 572882597 1457 WQAIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFGKDYLLEMKVKNLAQVEPLH 1529
Cdd:COG4555 172 REILRA-LKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEENLEDAFVALIGSEEGEA 243
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1298-1496 |
2.03e-55 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 190.30 E-value: 2.03e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1298 SKR-KNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDALEFLGYCPQENALWP 1372
Cdd:cd03230 7 SKRyGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGkdikKEPEEVKRRIGYLPEEPSLYE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1373 NLTVRQHLEvyaavkglrkgdaevaitrlvdalklqdqlkspvktLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEG 1452
Cdd:cd03230 87 NLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPES 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 572882597 1453 QQQMWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1496
Cdd:cd03230 131 RREFWELLR-ELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
480-693 |
7.64e-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: 188.76 E-value: 7.64e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEmaDLENLSKL 559
Cdd:cd03230 1 IEVRNLSKRYGKKT----ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK--EPEEVKRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 TGVCPQSNVQFDFLTVRENLRlfakikgilpqevdkeiqrvllelemkniqdvlaqnLSGGQKRKLTFGIAILGDPQIFL 639
Cdd:cd03230 75 IGYLPEEPSLYENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 572882597 640 LDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKL 693
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1298-1599 |
8.41e-55 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 193.40 E-value: 8.41e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1298 SKR-KNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSG-GGDALEFLGYCPQENALWPNLT 1375
Cdd:COG4152 8 TKRfGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPlDPEDRRRIGYLPEERGLYPKMK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1376 VRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQ 1455
Cdd:COG4152 88 VGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVEL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1456 MWQAIRAtFRntERGA--LLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFGkdyllemkvKNLAQVEPLH-AEI 1532
Cdd:COG4152 168 LKDVIRE-LA--AKGTtvIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFG---------RNTLRLEADGdAGW 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 572882597 1533 LRLFPQAARQERYSSLMVYKLP-VEDVQPLaqaffkLEKVKQSFDLEEYSLSQSTLEQVFLELSKEQE 1599
Cdd:COG4152 236 LRALPGVTVVEEDGDGAELKLEdGADAQEL------LRALLARGPVREFEEVRPSLNEIFIEVVGEKA 297
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
1299-1594 |
6.79e-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: 6.79e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1299 KRKNKI-ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDALEFLGYCPQENALWPN 1373
Cdd:TIGR01188 1 KVYGDFkAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGydvvREPRKVRRSIGIVPQYASVDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1374 LTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQ 1453
Cdd:TIGR01188 81 LTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1454 QQMWQAIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFGKDYlLEMKVKNLAQVEPLHAEIL 1533
Cdd:TIGR01188 161 RAIWDYIRA-LKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGKDT-LESRPRDIQSLKVEVSMLI 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 572882597 1534 RLFP--QAARQERYSSLMVYKLPVEDVQPLAQAFFKlEKVKQSFDLEEYSLSQSTLEQVFLEL 1594
Cdd:TIGR01188 239 AELGetGLGLLAVTVDSDRIKILVPDGDETVPEIVE-AAIRNGIRIRSISTERPSLDDVFLKL 300
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1280-1506 |
1.31e-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: 1.31e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1280 IIASCLRKEYAGKRkgcfskrknkiATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGG 1355
Cdd:cd03265 1 IEVENLVKKYGDFE-----------AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvREPR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1356 DALEFLGYCPQENALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGN 1435
Cdd:cd03265 70 EVRRRIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 572882597 1436 PSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLK 1506
Cdd:cd03265 150 PEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
480-693 |
5.78e-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: 5.78e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLEnLSKL 559
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKE-LAAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 ----TGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDP 635
Cdd:cd03255 80 rrrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 636 QIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADiLADRKVFLSQGKL 693
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
480-694 |
3.02e-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: 168.53 E-value: 3.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKpdkiEALKDLVFDIYEGqITAILGHSGAGKSTLLNILSGLSVPTKGSVTIynNKLSEMADLENLSKL 559
Cdd:cd03264 1 LQLENLTKRYGKK----RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRI--DGQDVLKQPQKLRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 TGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFL 639
Cdd:cd03264 74 IGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 572882597 640 LDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEADILADRKVFLSQGKLK 694
Cdd:cd03264 154 VDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
480-698 |
4.75e-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: 168.66 E-value: 4.75e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYkgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEmADLENLSKL 559
Cdd:COG1122 1 IELENLSFSY---PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITK-KNLRELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 TGVCPQ-SNVQFDFLTVRENLrLFA-KIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLtfgiAILG---- 633
Cdd:COG1122 77 VGLVFQnPDDQLFAPTVEEDV-AFGpENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRV----AIAGvlam 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 572882597 634 DPQIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS 698
Cdd:COG1122 152 EPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGT 217
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1297-1500 |
5.68e-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: 167.84 E-value: 5.68e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1297 FSKR-KNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDAL-EFLGYCPQENALWPNL 1374
Cdd:cd03269 6 VTKRfGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAArNRIGYLPEERGLYPKM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1375 TVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQ 1454
Cdd:cd03269 86 KVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 572882597 1455 QMWQAIRATFRNtERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1500
Cdd:cd03269 166 LLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
494-792 |
3.47e-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: 3.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 494 DKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLenLSKLTGVCPQSNVQFDFL 573
Cdd:TIGR01188 4 GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRK--VRRSIGIVPQYASVDEDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 574 TVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRH 653
Cdd:TIGR01188 82 TGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 654 QVWNLLKERKTDRV-ILFSTQFMDEADILADRKVFLSQGKLKCAGSSLFLKKKWGiGYHLSLQLNEICVEENITSLVKQH 732
Cdd:TIGR01188 162 AIWDYIRALKEEGVtILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLG-KDTLESRPRDIQSLKVEVSMLIAE 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 572882597 733 IPDAKLSAK-----SEGKLIYTLPLERTnkFPELYKDLDSYpdlGIENYGVSMT--TLNEVFLKLEG 792
Cdd:TIGR01188 241 LGETGLGLLavtvdSDRIKILVPDGDET--VPEIVEAAIRN---GIRIRSISTErpSLDDVFLKLTG 302
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1298-1497 |
2.54e-45 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 163.13 E-value: 2.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1298 SKR-KNKIATRNVSFCVRKGeVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG---SGGGDAL-EFLGYCPQENALWP 1372
Cdd:cd03264 7 TKRyGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqdvLKQPQKLrRRIGYLPQEFGVYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1373 NLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEg 1452
Cdd:cd03264 86 NFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPE- 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 572882597 1453 qqqmwQAIRatFRN------TERGALLTTHYMAEAEAVCDRVAIMVSGRLR 1497
Cdd:cd03264 165 -----ERIR--FRNllselgEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
481-692 |
2.61e-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: 163.02 E-value: 2.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 481 RIRNVTKEYKGKpdKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMaDLENLSKLT 560
Cdd:cd03225 1 ELKNLSFSYPDG--ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKL-SLKELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 561 GVCPQ-SNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFL 639
Cdd:cd03225 78 GLVFQnPDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 572882597 640 LDEPTAGLDPFSRHQVWNLLKERKTDRV-ILFSTQFMDEADILADRKVFLSQGK 692
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAEGKtIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
480-693 |
3.95e-45 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 162.39 E-value: 3.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIynnKLSEMADLENLSKL 559
Cdd:cd03268 1 LKTNDLTKTYGKKR----VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITF---DGKSYQKNIEALRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 TGVCPQSNVQFDFLTVRENLRLFAKIKGILpqevDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFL 639
Cdd:cd03268 74 IGALIEAPGFYPNLTARENLRLLARLLGIR----KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 572882597 640 LDEPTAGLDPFSRHQVWNLL-KERKTDRVILFSTQFMDEADILADRKVFLSQGKL 693
Cdd:cd03268 150 LDEPTNGLDPDGIKELRELIlSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1279-1558 |
4.17e-45 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 166.42 E-value: 4.17e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1279 VIIASCLRKEY---------AGKRKGCFSKRKNKI-ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVl 1348
Cdd:COG4586 1 IIEVENLSKTYrvyekepglKGALKGLFRREYREVeAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1349 lkgsgggdalEFLGYCP----------------QENALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLK 1412
Cdd:COG4586 80 ----------RVLGYVPfkrrkefarrigvvfgQRSQLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1413 SPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRAtfRNTERGA--LLTTHYMAEAEAVCDRVAI 1490
Cdd:COG4586 150 TPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKE--YNRERGTtiLLTSHDMDDIEALCDRVIV 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 572882597 1491 MVSGRLRCIGSIQHLKSKFGKDYLLEMKVKNLAQVEPL--HAEILRLFPQAAR-----QERYSSLMVY---KLPVEDV 1558
Cdd:COG4586 228 IDHGRIIYDGSLEELKERFGPYKTIVLELAEPVPPLELprGGEVIEREGNRVRlevdpRESLAEVLARllaRYPVRDL 305
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1296-1497 |
6.72e-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: 161.62 E-value: 6.72e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1296 CFSKR-KNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGD---ALEFLGYCPQENALW 1371
Cdd:cd03268 5 DLTKTyGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKnieALRRIGALIEAPGFY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1372 PNLTVRQHLEVYAAVKGLRKGDAEvaitRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1451
Cdd:cd03268 85 PNLTARENLRLLARLLGIRKKRID----EVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 572882597 1452 GQQQMWQAIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLR 1497
Cdd:cd03268 161 GIKELRELILS-LRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
480-703 |
1.54e-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: 1.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYkgkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIynNKLSEMADLENLSKL 559
Cdd:cd03265 1 IEVENLVKKY----GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATV--AGHDVVREPREVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 TGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFL 639
Cdd:cd03265 75 IGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 572882597 640 LDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGSSLFLK 703
Cdd:cd03265 155 LDEPTIGLDPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
477-693 |
5.95e-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: 5.95e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 477 KEAIRIRNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADlENL 556
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSE-REL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 557 SKL----TGVCPQS-NVqFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQK------Rkl 625
Cdd:COG1136 81 ARLrrrhIGFVFQFfNL-LPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQqrvaiaR-- 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 626 tfgiAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADIlADRKVFLSQGKL 693
Cdd:COG1136 158 ----ALVNRPKLILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTHDPELAAR-ADRVIRLRDGRI 222
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
480-693 |
8.37e-42 |
|
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: 153.81 E-value: 8.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEM--ADLENLS 557
Cdd:cd03261 1 IELRGLTKSFGGRT----VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLseAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 558 KLTGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIqrVLLELEM---KNIQDVLAQNLSGGQKRKLTFGIAILGD 634
Cdd:cd03261 77 RRMGMLFQSGALFDSLTVFENVAFPLREHTRLSEEEIREI--VLEKLEAvglRGAEDLYPAELSGGMKKRVALARALALD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 572882597 635 PQIFLLDEPTAGLDPFSRHQVWNL---LKERKTDRVILFSTQfMDEADILADRKVFLSQGKL 693
Cdd:cd03261 155 PELLLYDEPTAGLDPIASGVIDDLirsLKKELGLTSIMVTHD-LDTAFAIADRIAVLYDGKI 215
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
480-689 |
9.99e-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: 9.99e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEmadlenLSKL 559
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG------PGPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 TGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFL 639
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 572882597 640 LDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLS 689
Cdd:cd03293 155 LDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDEAVFLADRVVVLS 206
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
480-697 |
9.24e-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: 9.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEmADLENLSKL 559
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 tGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFL 639
Cdd:cd03266 81 -GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 572882597 640 LDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAG 697
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRQlRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1303-1595 |
1.39e-40 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 152.65 E-value: 1.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1303 KIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDALEFLGYCPQENALWPNLTVRQ 1378
Cdd:PRK13537 20 KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGepvpSRARHARQRVGVVPQFDNLDPDFTVRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1379 HLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQ 1458
Cdd:PRK13537 100 NLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1459 AIRATFrntERGA--LLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL-KSKFGKDyLLEMKVKNLAQVEPLhaeilrL 1535
Cdd:PRK13537 180 RLRSLL---ARGKtiLLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALiESEIGCD-VIEIYGPDPVALRDE------L 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 572882597 1536 FPQAARQE-RYSSLMVYklpVEDVQPLAQAffklekVKQSFDLeEYSLSQSTLEQVFLELS 1595
Cdd:PRK13537 250 APLAERTEiSGETLFCY---VRDPEPLHAR------LKGRAGL-RYLHRPANLEDVFLRLT 300
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
479-691 |
2.57e-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: 2.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 479 AIRIRNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEmadlenLSK 558
Cdd:COG1116 7 ALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG------PGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 559 LTGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLtfGIA--ILGDPQ 636
Cdd:COG1116 81 DRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRV--AIAraLANDPE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 637 IFLLDEPTAGLDPFSRHQVWNLL-----KERKTdrvILFSTQFMDEADILADRKVFLSQG 691
Cdd:COG1116 159 VLLMDEPFGALDALTRERLQDELlrlwqETGKT---VLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
480-692 |
1.05e-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: 1.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTiYNNKLSEMADLENLSKL 559
Cdd:COG4133 3 LEAENLSCRRGERL----LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVL-WNGEPIRDAREDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 TGVCPQSNVqFDFLTVRENLRLFAKIKGILPQEVDkeIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFL 639
Cdd:COG4133 78 AYLGHADGL-KPELTVRENLRFWAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 572882597 640 LDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQfmDEADILADRKVFLSQGK 692
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 ... |
1299-1500 |
1.36e-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: 1.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1299 KRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDALEFLGYCPQENALWPNL 1374
Cdd:cd03266 14 VKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvKEPAEARRRLGFVSDSTGLYDRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1375 TVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQ 1454
Cdd:cd03266 94 TARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATR 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 572882597 1455 QMWQAIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1500
Cdd:cd03266 174 ALREFIRQ-LRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
499-645 |
2.43e-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: 143.56 E-value: 2.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 499 LKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIyNNKLSEMADLENLSKLTGVCPQSNVQFDFLTVREN 578
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILL-DGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 572882597 579 LRLFAKIKGILPQEVDKEIQRVLLELEM----KNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTA 645
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARAEEALEKLGLgdlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1307-1476 |
2.91e-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: 2.91e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1307 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDALEF----LGYCPQENALWPNLTVRQHLEV 1382
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDyrrrLAYLGHADGLKPELTVRENLRF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1383 YAAVKGLRKGDAevAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRA 1462
Cdd:COG4133 99 WAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAA 176
|
170
....*....|....
gi 572882597 1463 tFRNTERGALLTTH 1476
Cdd:COG4133 177 -HLARGGAVLLTTH 189
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1308-1601 |
1.25e-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: 1.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1308 NVSFcvRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDALEF----LGYCPQENALWPNLTVRQHLEVY 1383
Cdd:TIGR01257 950 NITF--YENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAvrqsLGMCPQHNILFHHLTVAEHILFY 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1384 AAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIrAT 1463
Cdd:TIGR01257 1028 AQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL-LK 1106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1464 FRnTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFGKDYLLEM--KVKNL------------------- 1522
Cdd:TIGR01257 1107 YR-SGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLvrKMKNIqsqrggcegtcsctskgfs 1185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1523 ----AQVEPLHAE-------------ILRLFPQAARQERYSSLMVYKLPVEDVQPLAQA--FFKLEKVKQSFDLEEYSLS 1583
Cdd:TIGR01257 1186 trcpARVDEITPEqvldgdvnelmdlVYHHVPEAKLVECIGQELIFLLPNKNFKQRAYAslFRELEETLADLGLSSFGIS 1265
|
330
....*....|....*...
gi 572882597 1584 QSTLEQVFLELSKEQELG 1601
Cdd:TIGR01257 1266 DTPLEEIFLKVTEDADSG 1283
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
480-692 |
1.98e-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: 141.75 E-value: 1.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKPDKIeaLKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMaDLENLSKL 559
Cdd:cd03228 1 IEFKNVSFSYPGRPKPV--LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDL-DLESLRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 TGVCPQSNVQFDFlTVRENLrlfakikgilpqevdkeiqrvllelemkniqdvlaqnLSGGQKRKLTFGIAILGDPQIFL 639
Cdd:cd03228 78 IAYVPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 572882597 640 LDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEADiLADRKVFLSQGK 692
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
480-731 |
2.15e-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: 145.27 E-value: 2.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLSKL 559
Cdd:TIGR04520 1 IEVENVSFSYPE--SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWEIRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 TGVCPQS--NvQFDFLTVR-------ENLrlfakikGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKltfgIA 630
Cdd:TIGR04520 79 VGMVFQNpdN-QFVGATVEddvafglENL-------GVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQR----VA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 631 ILG----DPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEAdILADRKVFLSQGKLKCAGS--SLFL 702
Cdd:TIGR04520 147 IAGvlamRPDIIILDEATSMLDPKGRKEVLETIRKlnKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTprEIFS 225
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 572882597 703 K----KKWGIG----YHLSLQLNE--ICVEENITS---LVKQ 731
Cdd:TIGR04520 226 QvellKEIGLDvpfiTELAKALKKrgIPLPPDILTeeeLVDE 267
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
480-693 |
6.10e-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: 6.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYkgkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGL-----SVPTKGSVTIYN-NKLSEMADL 553
Cdd:cd03260 1 IELRDLNVYY----GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGkDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 554 ENLSKLTGVCPQSNVQFDfLTVRENLRLFAKIKGILPQEVDKEIQRVLLEL-----EMKNIQDVLAqnLSGGQKRKLTFG 628
Cdd:cd03260 77 LELRRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEEALRKaalwdEVKDRLHALG--LSGGQQQRLCLA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 572882597 629 IAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEADILADRKVFLSQGKL 693
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
479-692 |
6.37e-38 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 146.13 E-value: 6.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 479 AIRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENlsK 558
Cdd:PRK13536 41 AIDLAGVSKSYGDKA----VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLAR--A 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 559 LTGVCPQ-SNVQFDFlTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQI 637
Cdd:PRK13536 115 RIGVVPQfDNLDLEF-TVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 572882597 638 FLLDEPTAGLDPFSRHQVW----NLLKERKTdrvILFSTQFMDEADILADRKVFLSQGK 692
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIWerlrSLLARGKT---ILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
481-692 |
7.20e-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: 139.69 E-value: 7.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 481 RIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMaDLENLSKLT 560
Cdd:cd00267 1 EIENLSFRYGGRT----ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKL-PLEELRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 561 GVCPQsnvqfdfltvrenlrlfakikgilpqevdkeiqrvllelemkniqdvlaqnLSGGQKRKLTFGIAILGDPQIFLL 640
Cdd:cd00267 76 GYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 572882597 641 DEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGK 692
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
453-712 |
9.23e-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: 9.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 453 LEDEMDADPSfhDSFEQAPPEFQGKEAIRIRNVTKEYKGKPDkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGL 532
Cdd:COG4987 309 LNELLDAPPA--VTEPAEPAPAPGGPSLELEDVSFRYPGAGR--PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRF 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 533 SVPTKGSVTIYNNKLSEMaDLENLSKLTGVCPQSNVQFDfLTVRENLRLfAKikgilPQEVDKEIQRVLlelEMKNIQDV 612
Cdd:COG4987 385 LDPQSGSITLGGVDLRDL-DEDDLRRRIAVVPQRPHLFD-TTLRENLRL-AR-----PDATDEELWAAL---ERVGLGDW 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 613 LAQ--------------NLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEA 678
Cdd:COG4987 454 LAAlpdgldtwlgeggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGL 533
|
250 260 270
....*....|....*....|....*....|....
gi 572882597 679 DiLADRKVFLSQGKLKCAGSSLFLKKKWGIGYHL 712
Cdd:COG4987 534 E-RMDRILVLEDGRIVEQGTHEELLAQNGRYRQL 566
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
479-698 |
2.18e-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: 2.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 479 AIRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLEnLSK 558
Cdd:COG1120 1 MLEAENLSVGYGGRP----VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRE-LAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 559 LTGVCPQSNVQFDFLTVRE--------NLRLFAKikgilPQEVDKEI-QRVLLELEMKNIQDVLAQNLSGGQKRKLTFGI 629
Cdd:COG1120 76 RIAYVPQEPPAPFGLTVRElvalgrypHLGLFGR-----PSAEDREAvEEALERTGLEHLADRPVDELSGGERQRVLIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 572882597 630 AILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS 698
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
229-795 |
3.60e-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: 3.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 229 CII---SF--SSFIYYasvnVTRER-KRMKALMTMMGLRDSAFWLS---WGLLyaGFIFIMALFLALVI--RSTQFIILS 297
Cdd:TIGR01257 1685 CVIfamSFvpASFVLY----LIQERvNKAKHLQFISGVSPTTYWLTnflWDIM--NYAVSAGLVVGIFIgfQKKAYTSPE 1758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 298 GFMVVFSLFLLYGLSLVALAFLMSILVK-----------KSFLTGL----VVFLLTVFWG---CLGFTSLYRHLpaslew 359
Cdd:TIGR01257 1759 NLPALVALLMLYGWAVIPMMYPASFLFDvpstayvalscANLFIGInssaITFVLELFENnrtLLRFNAMLRKL------ 1832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 360 iLSLLSPFAFMLGMAQLL----------HLDYDLNSNAFPHPSDGSNLivatnFMLAFDTCLYLALAIYFEKilpneygh 429
Cdd:TIGR01257 1833 -LIVFPHFCLGRGLIDLAlsqavtdvyaQFGEEHSANPFQWDLIGKNL-----VAMAVEGVVYFLLTLLIQH-------- 1898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 430 rrppLFFLkssfwsqTQKTDHVALEDEMDADPSFHDSFEQAPPEFQGKEAIRIRNVTKEYKGKPDKieALKDLVFDIYEG 509
Cdd:TIGR01257 1899 ----HFFL-------SRWIAEPAKEPIFDEDDDVAEERQRIISGGNKTDILRLNELTKVYSGTSSP--AVDRLCVGVRPG 1965
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 510 QITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLseMADLENLSKLTGVCPQSNVQFDFLTVRENLRLFAKIKGIL 589
Cdd:TIGR01257 1966 ECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI--LTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVP 2043
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 590 PQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWN-LLKERKTDRVI 668
Cdd:TIGR01257 2044 AEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNtIVSIIREGRAV 2123
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 669 LFSTQFMDEADILADRKVFLSQGKLKCAGSSLFLKKKWGIGYHLSLQL----NEICVEEN-ITSLVKQHIPDAKLSAKSE 743
Cdd:TIGR01257 2124 VLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMKIkspkDDLLPDLNpVEQFFQGNFPGSVQRERHY 2203
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 572882597 744 GKLIYTLPlerTNKFPELYKDLDSYPD-LGIENYGVSMTTLNEVFLKLEGKST 795
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 ... |
480-693 |
6.12e-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: 6.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEM--ADLENLS 557
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLsgKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 558 KLTGVCPQsnvQFDFL---TVRENLRLFAKIKGILPQEVDKEIQRvLLEL-EMKNIQDVLAQNLSGGQKRKLTFGIAILG 633
Cdd:cd03258 82 RRIGMIFQ---HFNLLssrTVFENVALPLEIAGVPKAEIEERVLE-LLELvGLEDKADAYPAQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 572882597 634 DPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKL 693
Cdd:cd03258 158 NPKVLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
479-698 |
8.79e-37 |
|
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: 139.73 E-value: 8.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 479 AIRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEM--ADLENL 556
Cdd:COG1127 5 MIEVRNLTKSFGDRV----VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLseKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 557 SKLTGVCPQSNVQFDFLTVRENLRLFAKIKGILPqevDKEI-QRVLLELEMKNIQDVLAQN---LSGGQKRKLtfGIA-- 630
Cdd:COG1127 81 RRRIGMLFQGGALFDSLTVFENVAFPLREHTDLS---EAEIrELVLEKLELVGLPGAADKMpseLSGGMRKRV--ALAra 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 572882597 631 ILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDR---VILFSTQfMDEADILADRKVFLSQGKLKCAGS 698
Cdd:COG1127 156 LALDPEILLYDEPTAGLDPITSAVIDELIRELRDELgltSVVVTHD-LDSAFAIADRVAVLADGKIIAEGT 225
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1302-1495 |
1.09e-36 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 142.66 E-value: 1.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1302 NKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDALEFLGYCPQENALWPNLTVR 1377
Cdd:PRK13536 53 DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGvpvpARARLARARIGVVPQFDNLDLEFTVR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1378 QHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMW 1457
Cdd:PRK13536 133 ENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIW 212
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 572882597 1458 QAIRATFrntERGA--LLTTHYMAEAEAVCDRVAIMVSGR 1495
Cdd:PRK13536 213 ERLRSLL---ARGKtiLLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
469-698 |
1.23e-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: 147.60 E-value: 1.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 469 QAPPEFQGKEAIRIRNVTKEYkgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLS 548
Cdd:COG4988 326 TAPLPAAGPPSIELEDVSFSY---PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLS 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 549 EMaDLENLSKLTGVCPQSNVQFDfLTVRENLRLFAkikgilPQEVDKEIQRVlleLEMKNIQDVLAQ------------- 615
Cdd:COG4988 403 DL-DPASWRRQIAWVPQNPYLFA-GTIRENLRLGR------PDASDEELEAA---LEAAGLDEFVAAlpdgldtplgegg 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 616 -NLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQfmDEADI-LADRKVFLSQGKL 693
Cdd:COG4988 472 rGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITH--RLALLaQADRILVLDDGRI 549
|
....*
gi 572882597 694 KCAGS 698
Cdd:COG4988 550 VEQGT 554
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
483-693 |
1.29e-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: 1.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 483 RNVTKEYKGKPDKIEA--LKDLVFDIYEGQITAILGHSGAGKSTLLNILSGL--SVPTKGSVTIyNNKlseMADLENLSK 558
Cdd:cd03213 7 RNLTVTVKSSPSKSGKqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLI-NGR---PLDKRSFRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 559 LTGVCPQSNVQFDFLTVRENLRLFAKIKGIlpqevdkeiqrvllelemkniqdvlaqnlSGGQKRKLTFGIAILGDPQIF 638
Cdd:cd03213 83 IIGYVPQDDILHPTLTVRETLMFAAKLRGL-----------------------------SGGERKRVSIALELVSNPSLL 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 572882597 639 LLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFST-QFMDEADILADRKVFLSQGKL 693
Cdd:cd03213 134 FLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIhQPSSEIFELFDKLLLLSQGRV 190
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1280-1496 |
1.66e-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: 1.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1280 IIASCLRKEYAGKRKGCF----------SKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVll 1349
Cdd:cd03267 1 IEVSNLSKSYRVYSKEPGligslkslfkRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1350 kgsgggdalEFLGYCP----------------QENALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKS 1413
Cdd:cd03267 79 ---------RVAGLVPwkrrkkflrrigvvfgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1414 PVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVS 1493
Cdd:cd03267 150 PVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDK 229
|
...
gi 572882597 1494 GRL 1496
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 ... |
480-692 |
5.05e-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: 5.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYkgkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLSKL 559
Cdd:cd03224 1 LEVENLNAGY----GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 TGVCPQSNVQFDFLTVRENLRLFAKIKGilPQEVDKEIQRVlLEL--EMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQI 637
Cdd:cd03224 77 IGYVPEGRRIFPELTVEENLLLGAYARR--RAKRKARLERV-YELfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 572882597 638 FLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGK 692
Cdd:cd03224 154 LLLDEPSEGLAPKIVEEIFEAIRElRDEGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
479-731 |
3.11e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 136.27 E-value: 3.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 479 AIRIRNVTKEYKgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEmADLENLSK 558
Cdd:PRK13632 7 MIKVENVSFSYP--NSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISK-ENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 559 LTGVCPQS-NVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQI 637
Cdd:PRK13632 84 KIGIIFQNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 638 FLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEAdILADRKVFLSQGKLKCAGS-SLFLKKKWGIG----- 709
Cdd:PRK13632 164 IIFDESTSMLDPKGKREIKKIMVDlrKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKpKEILNNKEILEkakid 242
|
250 260
....*....|....*....|....*.
gi 572882597 710 ----YHLSLQLNEICVEENITSLVKQ 731
Cdd:PRK13632 243 spfiYKLSKKLKGIDPTYNEEELIEQ 268
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
449-712 |
3.61e-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: 144.98 E-value: 3.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 449 DHVALEDEMDADPSFhdsfeQAPPEFQGkeAIRIRNVTKEYKgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNI 528
Cdd:COG2274 450 DILDLPPEREEGRSK-----LSLPRLKG--DIELENVSFRYP--GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKL 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 529 LSGLSVPTKGSVTIYNNKLSEMaDLENLSKLTGVCPQSNVQFdFLTVRENLRLFAkikgilPQEVDKEIQRVlleLEMKN 608
Cdd:COG2274 521 LLGLYEPTSGRILIDGIDLRQI-DPASLRRQIGVVLQDVFLF-SGTIRENITLGD------PDATDEEIIEA---ARLAG 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 609 IQDVLAQ--------------NLSGGQKRKLtfGIA--ILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFST 672
Cdd:COG2274 590 LHDFIEAlpmgydtvvgeggsNLSGGQRQRL--AIAraLLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIA 667
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 572882597 673 QfmDEADI-LADRKVFLSQGKLKCAGSSLFLKKKWGIGYHL 712
Cdd:COG2274 668 H--RLSTIrLADRIIVLDKGRIVEDGTHEELLARKGLYAEL 706
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
480-697 |
8.08e-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: 8.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMAdlenlSKL 559
Cdd:cd03269 1 LEVENVTKRFGRV----TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA-----RNR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 TGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFL 639
Cdd:cd03269 72 IGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 572882597 640 LDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAG 697
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRElARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
479-692 |
1.14e-34 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 135.70 E-value: 1.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 479 AIRIRNVTKEYKgkpDKIeALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLSk 558
Cdd:PRK13537 7 PIDFRNVEKRYG---DKL-VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 559 lTGVCPQ-SNVQFDFlTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQI 637
Cdd:PRK13537 82 -VGVVPQfDNLDPDF-TVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 572882597 638 FLLDEPTAGLDPFSRHQVW----NLLKERKTdrvILFSTQFMDEADILADRKVFLSQGK 692
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWerlrSLLARGKT---ILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
480-714 |
1.45e-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: 134.50 E-value: 1.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEY-KGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTI--YNNKLSEMADLENL 556
Cdd:TIGR04521 1 IKLKNVSYIYqPGTPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIdgRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 557 SKLTGVcpqsnVqFDF-------LTVRE-------NLrlfakikGILPQEVDkeiQRVLLELEMKNI-QDVLAQN---LS 618
Cdd:TIGR04521 81 RKKVGL-----V-FQFpehqlfeETVYKdiafgpkNL-------GLSEEEAE---ERVKEALELVGLdEEYLERSpfeLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 619 GGQKRKltfgIAILG----DPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGK 692
Cdd:TIGR04521 145 GGQMRR----VAIAGvlamEPEVLILDEPTAGLDPKGRKEILDLFKRlhKEKGLTVILVTHSMEDVAEYADRVIVMHKGK 220
|
250 260
....*....|....*....|....
gi 572882597 693 LKCAGSS--LFLKKKWGIGYHLSL 714
Cdd:TIGR04521 221 IVLDGTPreVFSDVDELEKIGLDV 244
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1307-1446 |
1.82e-34 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 129.69 E-value: 1.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1307 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-SGGGDALEFL----GYCPQENALWPNLTVRQHLE 1381
Cdd:pfam00005 2 KNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGqDLTDDERKSLrkeiGYVFQDPQLFPRLTVRENLR 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 572882597 1382 VYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPV----KTLSEGIKRKLCFVLSILGNPSVVLLDEPST 1446
Cdd:pfam00005 82 LGLLLKGLSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
480-693 |
2.98e-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: 131.49 E-value: 2.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIynnklsemaDLENLSKL 559
Cdd:cd03259 1 LELKGLSKTYGSVR----ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILI---------DGRDVTGV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 ------TGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILG 633
Cdd:cd03259 68 pperrnIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 572882597 634 DPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKL 693
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 ... |
1305-1495 |
3.96e-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: 3.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1305 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-------------SGggdalefLGYCPQENALW 1371
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGrditglppherarAG-------IGYVPEGRRIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1372 PNLTVRQHLEVYAAVKGLRKGDAEVAitRLVDAL-KLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDP 1450
Cdd:cd03224 88 PELTVEENLLLGAYARRRAKRKARLE--RVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 572882597 1451 EGQQQMWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1495
Cdd:cd03224 166 KIVEEIFEAIR-ELRDEGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
480-693 |
1.11e-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: 1.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEY-----------------KGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTI 542
Cdd:cd03267 1 IEVSNLSKSYrvyskepgligslkslfKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 543 YNNKLSEMADlENLSKLTGVCPQSN-VQFDfLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQ 621
Cdd:cd03267 81 AGLVPWKRRK-KFLRRIGVVFGQKTqLWWD-LPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 572882597 622 KRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKL 693
Cdd:cd03267 159 RMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEynRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
480-692 |
1.61e-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: 128.07 E-value: 1.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMAD-LENLSK 558
Cdd:cd03229 1 LELKNVSKRYGQKT----VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDeLPPLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 559 LTGVCPQSNVQFDFLTVRENLRLfakikgilpqevdkeiqrvllelemkniqdvlaqNLSGGQKRKLTFGIAILGDPQIF 638
Cdd:cd03229 77 RIGMVFQDFALFPHLTVLENIAL----------------------------------GLSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 572882597 639 LLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGK 692
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSlqAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
480-698 |
1.61e-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: 1.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGkpdkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVtIYNNKlsemadlenlsKL 559
Cdd:cd03219 1 LEVRGLTKRFGG----LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSV-LFDGE-----------DI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 TGVCP------------QsNVQ-FDFLTVRENLRL---FAKIKGILP-------QEVDKEIQRVLLELEMKNIQDVLAQN 616
Cdd:cd03219 65 TGLPPheiarlgigrtfQ-IPRlFPELTVLENVMVaaqARTGSGLLLararreeREARERAEELLERVGLADLADRPAGE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 617 LSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILfstqfMDEADI-----LADRKVFLSQ 690
Cdd:cd03219 144 LSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRElRERGITVL-----LVEHDMdvvmsLADRVTVLDQ 218
|
....*...
gi 572882597 691 GKLKCAGS 698
Cdd:cd03219 219 GRVIAEGT 226
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1305-1496 |
2.84e-33 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 129.09 E-value: 2.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1305 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-----------SGGGDALEFlgycpQENALWPN 1373
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGeditglppheiARLGIGRTF-----QIPRLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1374 LTVRQHLEV--------YAAVKGLRKGDAEV--AITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDE 1443
Cdd:cd03219 90 LTVLENVMVaaqartgsGLLLARARREEREAreRAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 572882597 1444 PSTGMDPEGQQQMWQAIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1496
Cdd:cd03219 170 PAAGLNPEETEELAELIRE-LRERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
479-698 |
4.75e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 130.61 E-value: 4.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 479 AIRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIyNNKLSEMADLENLSK 558
Cdd:COG4152 1 MLELKGLTKRFGDKT----AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLW-DGEPLDPEDRRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 559 L---TGVCPQsnvqfdfLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDP 635
Cdd:COG4152 76 LpeeRGLYPK-------MKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 572882597 636 QIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS 698
Cdd:COG4152 149 ELLILDEPFSGLDPVNVELLKDVIRElAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGS 212
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
455-699 |
7.77e-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: 7.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 455 DEMDADPSFHDSFEQAPPEFQGKE-AIRIRNVTKEYKGK-PDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGL 532
Cdd:COG1123 235 QALAAVPRLGAARGRAAPAAAAAEpLLEVRNLSKRYPVRgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 533 SVPTKGSVTIYNNKLSEM--ADLENLSKLTGVCPQS-NVQFD-FLTVRENLRLFAKIKGILP-QEVDKEIQRVL----LE 603
Cdd:COG1123 315 LRPTSGSILFDGKDLTKLsrRSLRELRRRVQMVFQDpYSSLNpRMTVGDIIAEPLRLHGLLSrAERRERVAELLervgLP 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 604 LEMKniqDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADIL 681
Cdd:COG1123 395 PDLA---DRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDlqRELGLTYLFISHDLAVVRYI 471
|
250
....*....|....*...
gi 572882597 682 ADRKVFLSQGKLKCAGSS 699
Cdd:COG1123 472 ADRVAVMYDGRIVEDGPT 489
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
479-693 |
7.91e-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: 7.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 479 AIRIRNVTKEYkgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEM--ADLENL 556
Cdd:COG3638 2 MLELRNLSKRY---PGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALrgRALRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 557 SKLTGVCPQsnvQFDF---LTVREN--------LRLFAKIKGILPQEvdkEIQRVLLELEMKNIQDVLAQ---NLSGGQK 622
Cdd:COG3638 79 RRRIGMIFQ---QFNLvprLSVLTNvlagrlgrTSTWRSLLGLFPPE---DRERALEALERVGLADKAYQradQLSGGQQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 572882597 623 RKLtfGIA--ILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKL 693
Cdd:COG3638 153 QRV--AIAraLVQEPKLILADEPVASLDPKTARQVMDLLRRiaREDGITVVVNLHQVDLARRYADRIIGLRDGRV 225
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
480-693 |
1.03e-32 |
|
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: 1.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKPDkieaLKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMaDLENLSKL 559
Cdd:COG4619 1 LELEGLSFRVGGKPI----LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAM-PPPEWRRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 TGVCPQSNVQFDfLTVRENLRLFAKIKGilpQEVDKEIQRVLLE-LEMKniQDVL---AQNLSGGQKRKLTFGIAILGDP 635
Cdd:COG4619 76 VAYVPQEPALWG-GTVRDNLPFPFQLRE---RKFDRERALELLErLGLP--PDILdkpVERLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 636 QIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKL 693
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
480-693 |
1.84e-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: 126.85 E-value: 1.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMadLENLSKL 559
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKL--SRRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 TGvcpqSNVQFDF----------LTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVL---AQNLSGGQKRKLT 626
Cdd:cd03257 80 RR----KEIQMVFqdpmsslnprMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLnryPHELSGGQRQRVA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 572882597 627 FGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKL 693
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 ... |
1299-1495 |
2.14e-32 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 126.04 E-value: 2.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1299 KRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-----SGGGDALEFLGYCPQEnalwP- 1372
Cdd:cd03225 10 PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGkdltkLSLKELRRKVGLVFQN----Pd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1373 ----NLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCfVLSIL-GNPSVVLLDEPSTG 1447
Cdd:cd03225 86 dqffGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVA-IAGVLaMDPDILLLDEPTAG 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 572882597 1448 MDPEGQQQMWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1495
Cdd:cd03225 165 LDPAGRRELLELLK-KLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
479-698 |
3.02e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 126.74 E-value: 3.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 479 AIRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNnklsemADLENLSK 558
Cdd:COG1121 6 AIELENLTVSYGGRP----VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG------KPPRRARR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 559 LTGVCPQ-SNVQFDF-LTVRE--------NLRLFakikGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFG 628
Cdd:COG1121 76 RIGYVPQrAEVDWDFpITVRDvvlmgrygRRGLF----RRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 572882597 629 IAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKLkCAGS 698
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 ... |
481-697 |
3.18e-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: 3.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 481 RIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMadlenlsklt 560
Cdd:cd03214 1 EVENLSVGYGGRT----VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASL---------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 561 gvcpqsnvqfdfltvreNLRLFAKIKGILPQevdkEIQRV-LLELEMKNIQDvlaqnLSGGQKRKLTFGIAILGDPQIFL 639
Cdd:cd03214 67 -----------------SPKELARKIAYVPQ----ALELLgLAHLADRPFNE-----LSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 640 LDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAG 697
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRlaRERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
480-693 |
3.38e-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: 125.44 E-value: 3.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNklsEMADLENLSKL 559
Cdd:cd03301 1 VELENVTKRFGNVT----ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGR---DVTDLPPKDRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 TGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFL 639
Cdd:cd03301 74 IAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 572882597 640 LDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKL 693
Cdd:cd03301 154 MDEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
479-693 |
5.46e-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: 5.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 479 AIRIRNVTKEYkgkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIyNNKLseMADLEnlsk 558
Cdd:COG3839 3 SLELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILI-GGRD--VTDLP---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 559 ltgvcP---------QSNVQFDFLTVRENLrLFA-KIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFG 628
Cdd:COG3839 72 -----PkdrniamvfQSYALYPHMTVYENI-AFPlKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALG 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 572882597 629 IAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKL 693
Cdd:COG3839 146 RALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRlhRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRI 212
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
480-661 |
6.08e-32 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 125.16 E-value: 6.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYkgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEM--ADLENLS 557
Cdd:COG2884 2 IRFENVSKRY---PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrREIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 558 KLTGVCPQsnvqfDF-----LTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLtfGI--A 630
Cdd:COG2884 79 RRIGVVFQ-----DFrllpdRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRV--AIarA 151
|
170 180 190
....*....|....*....|....*....|.
gi 572882597 631 ILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE 661
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 ... |
481-694 |
6.61e-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: 124.29 E-value: 6.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 481 RIRNVTKEYKgkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMAdlenLSKLT 560
Cdd:cd03226 1 RIENISFSYK---KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE----RRKSI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 561 GVCPQ-SNVQFDFLTVRENLRLFAKIKGILPQEVDKeiqrVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFL 639
Cdd:cd03226 74 GYVMQdVDYQLFTDSVREELLLGLKELDAGNEQAET----VLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 572882597 640 LDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKLK 694
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRElAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1297-1500 |
9.27e-32 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 124.17 E-value: 9.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1297 FSKR-KNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG---SGGGDALEFLGYCPQENALWP 1372
Cdd:cd03259 6 LSKTyGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGrdvTGVPPERRNIGMVFQDYALFP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1373 NLTVRQHLeVYA-AVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1451
Cdd:cd03259 86 HLTVAENI-AFGlKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 572882597 1452 GQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1500
Cdd:cd03259 165 LREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
479-693 |
2.02e-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: 2.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 479 AIRIRNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLSK 558
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 559 ltgvcpqsnVQFDF----------LTVRENLRLFAKIKGILpqEVDKEIQRVLLELEMKniQDVL----AQnLSGGQKRK 624
Cdd:COG1124 81 ---------VQMVFqdpyaslhprHTVDRILAEPLRIHGLP--DREERIAELLEQVGLP--PSFLdrypHQ-LSGGQRQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 572882597 625 LTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDR--VILFSTQFMDEADILADRKVFLSQGKL 693
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1305-1496 |
2.47e-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: 2.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1305 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-----------SGGGDALEFlgycpQENALWPN 1373
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGrditglpphriARLGIARTF-----QNPRLFPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1374 LTVRQHLEV----------YAAVKGLRKGDAEVAITR-----LVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSV 1438
Cdd:COG0411 94 LTVLENVLVaaharlgrglLAALLRLPRARREEREAReraeeLLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1439 VLLDEPSTGMDPEGQQQMWQAIRATfrNTERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1496
Cdd:COG0411 174 LLLDEPAAGLNPEETEELAELIRRL--RDERGItiLLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1296-1516 |
2.64e-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: 2.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1296 CFSKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-----SGGGDALEFLGYCPQ--EN 1368
Cdd:COG1122 7 SFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGkditkKNLRELRRKVGLVFQnpDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1369 ALWpNLTVRQhlEV-YAAV-KGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCF--VLSIlgNPSVVLLDEP 1444
Cdd:COG1122 87 QLF-APTVEE--DVaFGPEnLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIagVLAM--EPEVLVLDEP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 572882597 1445 STGMDPEGQQQMWQAIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLkskFGKDYLLE 1516
Cdd:COG1122 162 TAGLDPRGRRELLELLKR-LNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV---FSDYELLE 229
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
480-693 |
2.82e-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: 2.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYN---NKLSEmADLENL 556
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGvdlTALSE-RELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 557 SKLTGVCPQsnvQFDFL---TVRENLRLFAKIKGILPQEVDKeiqRV--LLEL-EMKNIQDVLAQNLSGGQKRKLtfGIA 630
Cdd:COG1135 81 RRKIGMIFQ---HFNLLssrTVAENVALPLEIAGVPKAEIRK---RVaeLLELvGLSDKADAYPSQLSGGQKQRV--GIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 572882597 631 --ILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKL 693
Cdd:COG1135 153 raLANNPKVLLCDEATSALDPETTRSILDLLKDinRELGLTIVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
481-697 |
4.12e-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: 122.26 E-value: 4.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 481 RIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMadlenlSKLT 560
Cdd:cd03235 1 EVEDLTVSYGGHP----VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE------RKRI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 561 GVCPQS-NVQFDF-LTVRE--NLRLFAKIK--GILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGD 634
Cdd:cd03235 71 GYVPQRrSIDRDFpISVRDvvLMGLYGHKGlfRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 572882597 635 PQIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRkVFLSQGKLKCAG 697
Cdd:cd03235 151 PDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYFDR-VLLLNRTVVASG 213
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
480-693 |
5.74e-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: 122.26 E-value: 5.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEY------------------KGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVT 541
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 542 IyNNKLSEMADLEnlsklTGVCPQsnvqfdfLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQ 621
Cdd:cd03220 81 V-RGRVSSLLGLG-----GGFNPE-------LTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGM 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 572882597 622 KRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKL 693
Cdd:cd03220 148 KARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRElLKQGKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
479-730 |
6.59e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 125.20 E-value: 6.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 479 AIRIRNVTKEYK------G---------KPDK--IEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVT 541
Cdd:COG4586 1 IIEVENLSKTYRvyekepGlkgalkglfRREYreVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 542 I-----YNNKLsemadlENLSKLTGVCPQ-SNVQFDfLTVRENLRLFAKIKGIlPqevDKEIQRVLLEL-EMKNIQDVLA 614
Cdd:COG4586 81 VlgyvpFKRRK------EFARRIGVVFGQrSQLWWD-LPAIDSFRLLKAIYRI-P---DAEYKKRLDELvELLDLGELLD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 615 Q---NLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDeaDI--LADRKVF 687
Cdd:COG4586 150 TpvrQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEynRERGTTILLTSHDMD--DIeaLCDRVIV 227
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 572882597 688 LSQGKLKCAGSSLFLKKKWGIGYHLSLQLNEICVEENITSLVK 730
Cdd:COG4586 228 IDHGRIIYDGSLEELKERFGPYKTIVLELAEPVPPLELPRGGE 270
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
481-699 |
7.37e-31 |
|
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: 122.40 E-value: 7.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 481 RIRNVTKEYkgkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIynnklsemaDLENLSKLT 560
Cdd:COG0410 5 EVENLHAGY----GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRF---------DGEDITGLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 561 ---------GVCPQS-NVqFDFLTVRENLRLFAKIKGIlPQEVDKEIQRVlLEL-----EMKNiqdVLAQNLSGGQKRKL 625
Cdd:COG0410 72 phriarlgiGYVPEGrRI-FPSLTVEENLLLGAYARRD-RAEVRADLERV-YELfprlkERRR---QRAGTLSGGEQQML 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 572882597 626 TFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGSS 699
Cdd:COG0410 146 AIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRlNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTA 220
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
480-693 |
9.17e-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: 9.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKPdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMaDLENLSKL 559
Cdd:cd03295 1 IEFENVTKRYGGGK---KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQ-DPVELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 TGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRV--LLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQI 637
Cdd:cd03295 77 IGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELlaLVGLDPAEFADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 572882597 638 FLLDEPTAGLDPFSRHQVWNLLK--ERKTDRVILFSTQFMDEADILADRKVFLSQGKL 693
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKrlQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEI 214
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
479-698 |
9.59e-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: 9.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 479 AIRIRNVTKEYKGkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPT---KGSVTIYNNKLSEMaDLEN 555
Cdd:COG1123 4 LLEVRDLSVRYPG--GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLEL-SEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 556 LSKLTGVCPQS-NVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGD 634
Cdd:COG1123 81 RGRRIGMVFQDpMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 572882597 635 PQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS 698
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGP 226
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1302-1504 |
1.69e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 121.73 E-value: 1.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1302 NKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDALEFLGYCPQENAL-W--PnLTVRq 1378
Cdd:COG1121 18 GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIGYVPQRAEVdWdfP-ITVR- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1379 hlEV-----YAAV---KGLRKGDAEvAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDP 1450
Cdd:COG1121 96 --DVvlmgrYGRRglfRRPSRADRE-AVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 572882597 1451 EGQQQMWQAIRAtFRNTERGALLTTHYMAEAEAVCDRVaIMVSGRLRCIGSIQH 1504
Cdd:COG1121 173 ATEEALYELLRE-LRREGKTILVVTHDLGAVREYFDRV-LLLNRGLVAHGPPEE 224
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1298-1501 |
1.86e-30 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 121.11 E-value: 1.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1298 SKR-KNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsGGGD---------ALEFLGYCPQE 1367
Cdd:cd03218 7 SKRyGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILL---DGQDitklpmhkrARLGIGYLPQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1368 NALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTG 1447
Cdd:cd03218 84 ASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAG 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 572882597 1448 MDPEGQQQMwQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1501
Cdd:cd03218 164 VDPIAVQDI-QKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGT 216
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1299-1495 |
3.69e-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: 3.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1299 KRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGD-----ALEFLGYCPQenalwpn 1373
Cdd:cd00267 8 RYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKlpleeLRRRIGYVPQ------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1374 ltvrqhlevyaavkglrkgdaevaitrlvdalklqdqlkspvktLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQ 1453
Cdd:cd00267 81 --------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASR 116
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 572882597 1454 QQMWQAIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1495
Cdd:cd00267 117 ERLLELLRE-LAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
484-693 |
8.11e-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: 8.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 484 NVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLsVP----TKGSVTIYNNKLSEMADLENLSKL 559
Cdd:cd03234 8 DVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGR-VEgggtTSGQILFNGQPRKPDQFQKCVAYV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 tgvcPQSNVQFDFLTVRENLRLFAKIKG--ILPQEVDKEI--QRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDP 635
Cdd:cd03234 87 ----RQDDILLPGLTVRETLTYTAILRLprKSSDAIRKKRveDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 572882597 636 QIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQfMDEADI--LADRKVFLSQGKL 693
Cdd:cd03234 163 KVLILDEPTSGLDSFTALNLVSTLSQlARRNRIVILTIH-QPRSDLfrLFDRILLLSSGEI 222
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
479-693 |
8.25e-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: 8.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 479 AIRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIynnklsemaDLENLSK 558
Cdd:COG3842 5 ALELENVSKRYGDVT----ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILL---------DGRDVTG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 559 L------TGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQK------Rklt 626
Cdd:COG3842 72 LppekrnVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQqrvalaR--- 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 572882597 627 fgiAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFST--QfmDEADILADRKVFLSQGKL 693
Cdd:COG3842 149 ---ALAPEPRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVThdQ--EEALALADRIAVMNDGRI 214
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
480-693 |
9.59e-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: 9.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYkgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEM--ADLENLS 557
Cdd:TIGR02315 2 LEVENLSKVY---PNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLrgKKLRKLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 558 KLTGVCPQSNVQFDFLTVRENL---RLFAK--IKGILPQEVDKEIQRVLLELEMKNIQDVLAQ---NLSGGQKRKLTFGI 629
Cdd:TIGR02315 79 RRIGMIFQHYNLIERLTVLENVlhgRLGYKptWRSLLGRFSEEDKERALSALERVGLADKAYQradQLSGGQQQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 572882597 630 AILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKL 693
Cdd:TIGR02315 159 ALAQQPDLILADEPIASLDPKTSKQVMDYLKRinKEDGITVIINLHQVDLAKKYADRIVGLKAGEI 224
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
457-693 |
1.33e-29 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 126.05 E-value: 1.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 457 MDADPSFHDSfEQAPPEFQGKEAIRIRNVTKEYkgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPT 536
Cdd:COG1132 318 LDEPPEIPDP-PGAVPLPPVRGEIEFENVSFSY---PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPT 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 537 KGSVTIYNNKLSEMaDLENLSKLTGVCPQSNVQFDfLTVRENLRLFAkikgilPQEVDKEIQRVlleLEMKNIQDVLAQ- 615
Cdd:COG1132 394 SGRILIDGVDIRDL-TLESLRRQIGVVPQDTFLFS-GTIRENIRYGR------PDATDEEVEEA---AKAAQAHEFIEAl 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 616 -------------NLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDR-VIL----FSTqfmde 677
Cdd:COG1132 463 pdgydtvvgergvNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRtTIViahrLST----- 537
|
250
....*....|....*..
gi 572882597 678 adIL-ADRKVFLSQGKL 693
Cdd:COG1132 538 --IRnADRILVLDDGRI 552
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1299-1500 |
1.41e-29 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 118.40 E-value: 1.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1299 KRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVllKGSGGGDALEFLGYcpqenALWPNLTVRQ 1378
Cdd:cd03220 31 EVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV--TVRGRVSSLLGLGG-----GFNPELTGRE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1379 HLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEP-STGmDPEGQQQMW 1457
Cdd:cd03220 104 NIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVlAVG-DAAFQEKCQ 182
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 572882597 1458 QAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1500
Cdd:cd03220 183 RRLR-ELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1306-1500 |
2.52e-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: 2.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1306 TRNVSFCVrKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDALEFL---------GYCPQENALWPNLTV 1376
Cdd:cd03297 14 TLKIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKInlppqqrkiGLVFQQYALFPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1377 RQHLEVyaAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQM 1456
Cdd:cd03297 93 RENLAF--GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 572882597 1457 WQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1500
Cdd:cd03297 171 LPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
480-692 |
2.62e-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: 118.05 E-value: 2.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYkgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEM--ADLENLS 557
Cdd:cd03256 1 IEVENLSKTY---PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLkgKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 558 KLTGVCPQSNVQFDFLTVRENL---RLFAK--IKGILPQEVDKEIQRVLLELEMKNIQDVL---AQNLSGGQKRKLtfGI 629
Cdd:cd03256 78 RQIGMIFQQFNLIERLSVLENVlsgRLGRRstWRSLFGLFPKEEKQRALAALERVGLLDKAyqrADQLSGGQQQRV--AI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 572882597 630 A--ILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGK 692
Cdd:cd03256 156 AraLMQQPKLILADEPVASLDPASSRQVMDLLKRinREEGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
478-698 |
3.04e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 118.34 E-value: 3.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 478 EAIRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLEnLS 557
Cdd:PRK13548 1 AMLEARNLSVRLGGRT----LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAE-LA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 558 KLTGVCPQ-SNVQFDFlTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQK------RKLTFGIA 630
Cdd:PRK13548 76 RRRAVLPQhSSLSFPF-TVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQqrvqlaRVLAQLWE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 572882597 631 ILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDR-----VIL----FSTQFmdeadilADRKVFLSQGKLKCAGS 698
Cdd:PRK13548 155 PDGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERglaviVVLhdlnLAARY-------ADRIVLLHQGRLVADGT 224
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1307-1495 |
3.73e-29 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 117.39 E-value: 3.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1307 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-------------SGggdalefLGYCPQENALWPN 1373
Cdd:COG0410 20 HGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGeditglpphriarLG-------IGYVPEGRRIFPS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1374 LTVRQHLEVYAAVKGLRKGDAEvaitRL--VDAL--KLQDQLKSPVKTLSEG------IKRKLcfvlsiLGNPSVVLLDE 1443
Cdd:COG0410 93 LTVEENLLLGAYARRDRAEVRA----DLerVYELfpRLKERRRQRAGTLSGGeqqmlaIGRAL------MSRPKLLLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 572882597 1444 PSTGMDPEGQQQMWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1495
Cdd:COG0410 163 PSLGLAPLIVEEIFEIIR-RLNREGVTILLVEQNARFALEIADRAYVLERGR 213
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1302-1500 |
5.07e-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: 5.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1302 NKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDALEFLGYCPQ-ENALW--PnLTVRQ 1378
Cdd:cd03235 11 GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGYVPQrRSIDRdfP-ISVRD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1379 --------HLEVYAAVKGLRKGDAEVAITRlVDALKLQDQlksPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDP 1450
Cdd:cd03235 90 vvlmglygHKGLFRRLSKADKAKVDEALER-VGLSELADR---QIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 572882597 1451 EGQQQMWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVaIMVSGRLRCIG 1500
Cdd:cd03235 166 KTQEDIYELLR-ELRREGMTILVVTHDLGLVLEYFDRV-LLLNRTVVASG 213
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1287-1502 |
5.11e-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: 5.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1287 KEYAGKRKGcfSKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGS-------GGGdale 1359
Cdd:COG1134 25 KELLLRRRR--TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRvsallelGAG---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1360 FLgycpqenalwPNLTVRQHLEVYAAVKGLRKGDaevaITRLVDALK----LQDQLKSPVKTLSEGIKRKLCFVLSILGN 1435
Cdd:COG1134 99 FH----------PELTGRENIYLNGRLLGLSRKE----IDEKFDEIVefaeLGDFIDQPVKTYSSGMRARLAFAVATAVD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 572882597 1436 PSVVLLDEP-STGmDPEGQQQMWQAIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSI 1502
Cdd:COG1134 165 PDILLVDEVlAVG-DAAFQKKCLARIRE-LRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDP 230
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
481-693 |
5.55e-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: 5.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 481 RIRNVTKEYKGkpdkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTiYNNKlsemadlenlsKLT 560
Cdd:COG0411 6 EVRGLTKRFGG----LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRIL-FDGR-----------DIT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 561 GVCP------------QsNVQ-FDFLTVRENLRL---------FAKIKGILP------QEVDKEIQRVLLELEMKNIQDV 612
Cdd:COG0411 70 GLPPhriarlgiartfQ-NPRlFPELTVLENVLVaaharlgrgLLAALLRLPrarreeREARERAEELLERVGLADRADE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 613 LAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVIlfsTQFMDEADI-----LADRKVF 687
Cdd:COG0411 149 PAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGI---TILLIEHDMdlvmgLADRIVV 225
|
....*.
gi 572882597 688 LSQGKL 693
Cdd:COG0411 226 LDFGRV 231
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
480-698 |
5.97e-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: 5.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNklsEMADLENLSKL 559
Cdd:cd03300 1 IELENVSKFYGGFV----ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGK---DITNLPPHKRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 TGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFL 639
Cdd:cd03300 74 VNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 572882597 640 LDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS 698
Cdd:cd03300 154 LDEPLGALDLKLRKDMQLELKRlqKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
480-688 |
1.24e-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: 115.72 E-value: 1.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLSKL 559
Cdd:cd03218 1 LRAENLSKRYGKRK----VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 TGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFL 639
Cdd:cd03218 77 IGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 572882597 640 LDEPTAGLDPFSRHQVWNL---LKERK----------------TDRV-ILFSTQFMDE---ADILAD---RKVFL 688
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIikiLKDRGigvlitdhnvretlsiTDRAyIIYEGKVLAEgtpEEIAANelvRKVYL 231
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1307-1501 |
1.54e-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: 1.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1307 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsgGGDALE---------FLGYCPQENALWPNLTVR 1377
Cdd:COG1120 18 DDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLL----DGRDLAslsrrelarRIAYVPQEPPAPFGLTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1378 Q--------HLevyAAVKGLRKGDAEVAIT--RLVDALKLQDQlksPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTG 1447
Cdd:COG1120 94 ElvalgrypHL---GLFGRPSAEDREAVEEalERTGLEHLADR---PVDELSGGERQRVLIARALAQEPPLLLLDEPTSH 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 572882597 1448 MDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1501
Cdd:COG1120 168 LDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
479-693 |
3.65e-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: 3.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 479 AIRIRNVTKEYKgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMaDLENLSK 558
Cdd:cd03245 2 RIEFRNVSFSYP--NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQL-DPADLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 559 LTGVCPQSNVQFdFLTVRENLRLFAkikgilpQEVDKEiqRVLLELEMKNIQDVLA--------------QNLSGGQKRK 624
Cdd:cd03245 79 NIGYVPQDVTLF-YGTLRDNITLGA-------PLADDE--RILRAAELAGVTDFVNkhpngldlqigergRGLSGGQRQA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 572882597 625 LTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEADiLADRKVFLSQGKL 693
Cdd:cd03245 149 VALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLD-LVDRIIVMDSGRI 216
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
509-697 |
4.23e-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: 4.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 509 GQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNnklSEMADLENLSKLTGVCPQSNVQFDFLTVRENLRLfAKIKGI 588
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING---VDVTAAPPADRPVSMLFQENNLFAHLTVEQNVGL-GLSPGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 589 LPQEVDKE-IQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTD 665
Cdd:cd03298 100 KLTAEDRQaIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDlhAETK 179
|
170 180 190
....*....|....*....|....*....|..
gi 572882597 666 RVILFSTQFMDEADILADRKVFLSQGKLKCAG 697
Cdd:cd03298 180 MTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
479-698 |
4.28e-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: 4.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 479 AIRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLEnlsK 558
Cdd:cd03296 2 SIEVRNVSKRFGDFV----ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE---R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 559 LTGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEI-QRV--LLEL-EMKNIQDVLAQNLSGGQKRKLTFGIAILGD 634
Cdd:cd03296 75 NVGFVFQHYALFRHMTVFDNVAFGLRVKPRSERPPEAEIrAKVheLLKLvQLDWLADRYPAQLSGGQRQRVALARALAVE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 572882597 635 PQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS 698
Cdd:cd03296 155 PKVLLLDEPFGALDAKVRKELRRWLRRlhDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
480-714 |
5.12e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 115.65 E-value: 5.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEY-KGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIynNKLSEMAD-----L 553
Cdd:PRK13646 3 IRFDNVSYTYqKGTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTV--DDITITHKtkdkyI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 554 ENLSKLTGVC---PQSNVQFDflTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKniQDVLAQN---LSGGQKRKLTF 627
Cdd:PRK13646 81 RPVRKRIGMVfqfPESQLFED--TVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFS--RDVMSQSpfqMSGGQMRKIAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 628 gIAILG-DPQIFLLDEPTAGLDPFSRHQVWNLLKERKTD--RVILFSTQFMDEADILADRKVFLSQGKL--KCAGSSLFL 702
Cdd:PRK13646 157 -VSILAmNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDenKTIILVSHDMNEVARYADEVIVMKEGSIvsQTSPKELFK 235
|
250
....*....|..
gi 572882597 703 KKKWGIGYHLSL 714
Cdd:PRK13646 236 DKKKLADWHIGL 247
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
480-693 |
6.67e-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: 6.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYkgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMAD--LENLS 557
Cdd:cd03292 1 IEFINVTKTY---PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGraIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 558 KLTGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQI 637
Cdd:cd03292 78 RKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 572882597 638 FLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKL 693
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKiNKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
480-693 |
1.09e-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: 1.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLS-EMADLENLSK 558
Cdd:cd03262 1 IEIKNLHKSFGDF----HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTdDKKNINELRQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 559 LTGVCPQSNVQFDFLTVRENLRL-FAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQI 637
Cdd:cd03262 77 KVGMVFQQFNLFPHLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 572882597 638 FLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKL 693
Cdd:cd03262 157 MLFDEPTSALDPELVGEVLDVMKDlAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
478-698 |
1.20e-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: 1.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 478 EAIRIRNVTKEY------------------KGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGS 539
Cdd:COG1134 3 SMIEVENVSKSYrlyhepsrslkelllrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 540 VTIyNNKLSEMADLEnlsklTGVCPQsnvqfdfLTVRENLRLFAKIKGILPQEVDKEIQRVL--------LELEMKniqd 611
Cdd:COG1134 83 VEV-NGRVSALLELG-----AGFHPE-------LTGRENIYLNGRLLGLSRKEIDEKFDEIVefaelgdfIDQPVK---- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 612 vlaqNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTD-RVILFSTQFMDEADILADRKVFLSQ 690
Cdd:COG1134 146 ----TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESgRTVIFVSHSMGAVRRLCDRAIWLEK 221
|
....*...
gi 572882597 691 GKLKCAGS 698
Cdd:COG1134 222 GRLVMDGD 229
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
482-698 |
1.45e-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: 1.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 482 IRNVTKEYKGkpdkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEM--ADLENLskl 559
Cdd:COG4674 13 VEDLTVSFDG----FKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLdeHEIARL--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 tGVC-----PqsNVqFDFLTVRENLRL--------FAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLT 626
Cdd:COG4674 86 -GIGrkfqkP--TV-FEELTVFENLELalkgdrgvFASLFARLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 572882597 627 FGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDR---VILFSTQFMDEadiLADRKVFLSQGKLKCAGS 698
Cdd:COG4674 162 IGMLLAQDPKLLLLDEPVAGMTDAETERTAELLKSLAGKHsvvVVEHDMEFVRQ---IARKVTVLHQGSVLAEGS 233
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1278-1501 |
1.48e-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: 1.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1278 PVIIASCLRKEYaGKRKgcfskrknkiATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSgggD- 1356
Cdd:COG1137 2 MTLEAENLVKSY-GKRT----------VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGE---Di 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1357 --------ALEFLGYCPQENALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCF 1428
Cdd:COG1137 68 thlpmhkrARLGIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 572882597 1429 VLSILGNPSVVLLDEPSTGMDP---EGQQQMwqaIRatfRNTERGA--LLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1501
Cdd:COG1137 148 ARALATNPKFILLDEPFAGVDPiavADIQKI---IR---HLKERGIgvLITDHNVRETLGICDRAYIISEGKVLAEGT 219
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
481-698 |
2.39e-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: 111.85 E-value: 2.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 481 RIRNVTKEYKGKpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLSKLT 560
Cdd:TIGR03410 2 EVSNLNVYYGQS----HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 561 GVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIqrvlLEL-----EMKNIQdvlAQNLSGGQKRKLTFGIAILGDP 635
Cdd:TIGR03410 78 AYVPQGREIFPRLTVEENLLTGLAALPRRSRKIPDEI----YELfpvlkEMLGRR---GGDLSGGQQQQLAIARALVTRP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 572882597 636 QIFLLDEPTAGLDPfS----RHQVWNLLKERKtDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS 698
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 ... |
480-693 |
3.16e-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: 3.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKP-----------DKIE---------ALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGS 539
Cdd:cd03294 1 IKIKGLYKIFGKNPqkafkllakgkSKEEilkktgqtvGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 540 VTIYNNKLSEM--ADLENL-SKLTGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQN 616
Cdd:cd03294 81 VLIDGQDIAAMsrKELRELrRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 572882597 617 LSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKL 693
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRlqAELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1297-1495 |
4.21e-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: 109.58 E-value: 4.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1297 FSKR-KNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDALEF---LGYCPQEN 1368
Cdd:cd03229 6 VSKRyGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedltDLEDELPPLrrrIGMVFQDF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1369 ALWPNLTVRQHLeVYAavkglrkgdaevaitrlvdalklqdqlkspvktLSEGIKRKLCFVLSILGNPSVVLLDEPSTGM 1448
Cdd:cd03229 86 ALFPHLTVLENI-ALG---------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSAL 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 572882597 1449 DPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1495
Cdd:cd03229 132 DPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
480-694 |
4.52e-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: 110.95 E-value: 4.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEmADLENLskl 559
Cdd:TIGR03740 1 LETKNLSKRFGKQ----TAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTR-KDLHKI--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 tGVCPQSNVQFDFLTVRENLRLFAKIKGiLPqevDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFL 639
Cdd:TIGR03740 73 -GSLIESPPLYENLTARENLKVHTTLLG-LP---DSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLI 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 572882597 640 LDEPTAGLDPFSRHQVWNLLKERKTDRV-ILFSTQFMDEADILADRKVFLSQGKLK 694
Cdd:TIGR03740 148 LDEPTNGLDPIGIQELRELIRSFPEQGItVILSSHILSEVQQLADHIGIISEGVLG 203
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1305-1505 |
6.39e-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: 6.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1305 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTA---GQVLLKGSGGGDALEFL-----GYCPQE--NALWPnL 1374
Cdd:COG1123 21 AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALrgrriGMVFQDpmTQLNP-V 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1375 TVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQ 1454
Cdd:COG1123 100 TVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 572882597 1455 QMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL 1505
Cdd:COG1123 180 EILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
480-693 |
7.17e-27 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 113.74 E-value: 7.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEM--ADLENLS 557
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALseKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 558 KLTGVCPQsnvQFDFL---TVRENLRLFAKIKGILPQEVDKeiqRV--LLEL-EMKNIQDVLAQNLSGGQKRKLtfGIA- 630
Cdd:PRK11153 82 RQIGMIFQ---HFNLLssrTVFDNVALPLELAGTPKAEIKA---RVteLLELvGLSDKADRYPAQLSGGQKQRV--AIAr 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 572882597 631 -ILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKL 693
Cdd:PRK11153 154 aLASNPKVLLCDEATSALDPATTRSILELLKDinRELGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
471-693 |
7.99e-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: 118.43 E-value: 7.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 471 PPEFQGKeaIRIRNVTKEYKGkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEM 550
Cdd:TIGR03375 457 RPRLQGE--IEFRNVSFAYPG--QETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQI 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 551 aDLENLSKLTGVCPQSNVQFdFLTVRENLRLFAkikgilPQEVDKEIQRVLlelEMKNIQDVLA--------------QN 616
Cdd:TIGR03375 533 -DPADLRRNIGYVPQDPRLF-YGTLRDNIALGA------PYADDEEILRAA---ELAGVTEFVRrhpdgldmqigergRS 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 617 LSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFST---QFMDeadiLADRKVFLSQGKL 693
Cdd:TIGR03375 602 LSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGKTLVLVThrtSLLD----LVDRIIVMDNGRI 677
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
476-698 |
8.48e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 112.10 E-value: 8.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 476 GKEAIRIRNVTKEYK--GKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADL 553
Cdd:PRK13633 1 MNEMIKCKNVSYKYEsnEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 554 ENLSKLTGVCPQSN--------VQFDFLTVRENLrlfakikGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKl 625
Cdd:PRK13633 81 WDIRNKAGMVFQNPdnqivatiVEEDVAFGPENL-------GIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQR- 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 572882597 626 tfgIAILG----DPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEAdILADRKVFLSQGKLKCAGS 698
Cdd:PRK13633 153 ---VAIAGilamRPECIIFDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGT 227
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
478-691 |
8.96e-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: 8.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 478 EAIRIRNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLS-EMADlenl 556
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTgPGAD---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 557 sklTGVCPQSNVQFDFLTVRENLRLFAKIKGILPQE----VDKEIQRV-LLELEMKNIQDvlaqnLSGGQKRKLtfGIA- 630
Cdd:COG4525 78 ---RGVVFQKDALLPWLNVLDNVAFGLRLRGVPKAErrarAEELLALVgLADFARRRIWQ-----LSGGMRQRV--GIAr 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 572882597 631 -ILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQG 691
Cdd:COG4525 148 aLAADPRFLLMDEPFGALDALTREQMQELLLDvwQRTGKGVFLITHSVEEALFLATRLVVMSPG 211
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1280-1495 |
1.03e-26 |
|
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: 1.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1280 IIASCLRKEYAGKRKGcfskrknKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG---SGGGD 1356
Cdd:cd03293 1 LEVRNVSKTYGGGGGA-------VTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGepvTGPGP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1357 AlefLGYCPQENALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNP 1436
Cdd:cd03293 74 D---RGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDP 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 572882597 1437 SVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMvSGR 1495
Cdd:cd03293 151 DVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL-SAR 208
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
480-714 |
2.04e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 111.27 E-value: 2.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGK-PDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLS---EMADLEN 555
Cdd:PRK13634 3 ITFQKVEHRYQYKtPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 556 LSKLTGVC---PQSnvQFDFLTVRENLrLFAKIKGILPQEVDKEIQRVLLELEMKNiQDVLAQN---LSGGQKRKltfgI 629
Cdd:PRK13634 83 LRKKVGIVfqfPEH--QLFEETVEKDI-CFGPMNFGVSEEDAKQKAREMIELVGLP-EELLARSpfeLSGGQMRR----V 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 630 AILG----DPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS--SLF 701
Cdd:PRK13634 155 AIAGvlamEPEVLVLDEPTAGLDPKGRKEMMEMFYKlhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTprEIF 234
|
250
....*....|...
gi 572882597 702 LKKKWGIGYHLSL 714
Cdd:PRK13634 235 ADPDELEAIGLDL 247
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
480-704 |
2.95e-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: 108.85 E-value: 2.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEY-KGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMaDLENLSK 558
Cdd:cd03254 3 IEFENVNFSYdEKKP----VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDI-SRKSLRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 559 LTGVCPQSNVQFDFlTVRENLRLFAkikgilPQEVDKEIQRVLLELEMKNIQDVL-----------AQNLSGGQKRKLTF 627
Cdd:cd03254 78 MIGVVLQDTFLFSG-TIMENIRLGR------PNATDEEVIEAAKEAGAHDFIMKLpngydtvlgenGGNLSQGERQLLAI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 628 GIAILGDPQIFLLDEPTAGLDPFSRHQVWN---LLKERKTDRVI---LFSTQFmdeadilADRKVFLSQGKLKCAGS--S 699
Cdd:cd03254 151 ARAMLRDPKILILDEATSNIDTETEKLIQEaleKLMKGRTSIIIahrLSTIKN-------ADKILVLDDGKIIEEGThdE 223
|
....*
gi 572882597 700 LFLKK 704
Cdd:cd03254 224 LLAKK 228
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
478-697 |
3.07e-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: 109.40 E-value: 3.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 478 EAIRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKG-SVTIYNNKLSEmADLENL 556
Cdd:COG1119 2 PLLELRNVTVRRGGKT----ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGG-EDVWEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 557 SKLTGVCpqSNVQFDFLTVRENLR------LFAKIkGiLPQEVDKE----IQRVLLELEMKNIQDVLAQNLSGGQKRKLT 626
Cdd:COG1119 77 RKRIGLV--SPALQLRFPRDETVLdvvlsgFFDSI-G-LYREPTDEqrerARELLELLGLAHLADRPFGTLSQGEQRRVL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 572882597 627 FGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEadILA--DRKVFLSQGKLKCAG 697
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKlaAEGAPTLVLVTHHVEE--IPPgiTHVLLLKDGRVVAAG 225
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
480-697 |
3.45e-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: 107.01 E-value: 3.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKPDKIeaLKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADleNLSKL 559
Cdd:cd03247 1 LSINNVSFSYPEQEQQV--LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK--ALSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 TGVCPQSNVQFDfLTVRENlrlfakikgilpqevdkeiqrvllelemkniqdvLAQNLSGGQKRKLTFGIAILGDPQIFL 639
Cdd:cd03247 77 ISVLNQRPYLFD-TTLRNN----------------------------------LGRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 572882597 640 LDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEADiLADRKVFLSQGKLKCAG 697
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIE-HMDKILFLENGKIIMQG 178
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
480-698 |
4.31e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 110.14 E-value: 4.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEY-KGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYN-NKLSEMADLENLS 557
Cdd:PRK13637 3 IKIENLTHIYmEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvDITDKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 558 KLTGVCPQ-SNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRV--LLELEMKNIQDVLAQNLSGGQKRKltfgIAILG- 633
Cdd:PRK13637 83 KKVGLVFQyPEYQLFEETIEKDIAFGPINLGLSEEEIENRVKRAmnIVGLDYEDYKDKSPFELSGGQKRR----VAIAGv 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 634 ---DPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS 698
Cdd:PRK13637 159 vamEPKILILDEPTAGLDPKGRDEILNKIKElhKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGT 228
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
480-693 |
5.57e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 109.40 E-value: 5.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYkgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTI------YNNKlsemaDL 553
Cdd:PRK13639 2 LETRDLKYSY---PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIkgepikYDKK-----SL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 554 ENLSKLTGVCPQ-SNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKltfgIAIL 632
Cdd:PRK13639 74 LEVRKTVGIVFQnPDDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKR----VAIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 572882597 633 G----DPQIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKL 693
Cdd:PRK13639 150 GilamKPEIIVLDEPTSGLDPMGASQIMKLLYDlNKEGITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1298-1501 |
6.81e-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: 6.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1298 SKR-KNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsgGGDALEFL-------GYCPQENA 1369
Cdd:COG3842 12 SKRyGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILL----DGRDVTGLppekrnvGMVFQDYA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1370 LWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEG------IKRKLCFvlsilgNPSVVLLDE 1443
Cdd:COG3842 88 LFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGqqqrvaLARALAP------EPRVLLLDE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 572882597 1444 PSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1501
Cdd:COG3842 162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGT 219
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
480-692 |
7.77e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 108.63 E-value: 7.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKE-YKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLE---N 555
Cdd:COG1101 2 LELKNLSKTfNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKrakY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 556 LSK-----LTGVCPQsnvqfdfLTVRENLRLFAK-------IKGILPQEVDKEIQRV-LLELEMKNIQDVLAQNLSGGQK 622
Cdd:COG1101 82 IGRvfqdpMMGTAPS-------MTIEENLALAYRrgkrrglRRGLTKKRRELFRELLaTLGLGLENRLDTKVGLLSGGQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 572882597 623 RKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLlkerkTDRVI-------LFSTQFMDEADILADRKVFLSQGK 692
Cdd:COG1101 155 QALSLLMATLTKPKLLLLDEHTAALDPKTAALVLEL-----TEKIVeennlttLMVTHNMEQALDYGNRLIMMHEGR 226
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1297-1496 |
1.82e-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: 1.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1297 FSKRKNKI-ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG---SGGGDALEFL-----GYCPQE 1367
Cdd:cd03257 11 FPTGGGSVkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdlLKLSRRLRKIrrkeiQMVFQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1368 --NALWPNLTVRQHLEvyAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKT-----LSEGIKRKLCFVLSILGNPSVVL 1440
Cdd:cd03257 91 pmSSLNPRMTIGEQIA--EPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNrypheLSGGQRQRVAIARALALNPKLLI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1441 LDEPSTGMDPEGQQQmwqaIRATFRN--TERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1496
Cdd:cd03257 169 ADEPTSALDVSVQAQ----ILDLLKKlqEELGLtlLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1285-1496 |
1.92e-25 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 106.03 E-value: 1.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1285 LRKEYAGKRKgcfskrkNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG---SGGGDA---- 1357
Cdd:cd03255 6 LSKTYGGGGE-------KVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGtdiSKLSEKelaa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1358 --LEFLGYCPQENALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEG------IKRklcfv 1429
Cdd:cd03255 79 frRRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGqqqrvaIAR----- 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 572882597 1430 lSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAvCDRVAIMVSGRL 1496
Cdd:cd03255 154 -ALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
479-698 |
4.73e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 106.81 E-value: 4.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 479 AIRIRNVTKEYkgkPD-KIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVP---TKGSVTIYNNKLSEMADLE 554
Cdd:PRK13640 5 IVEFKHVSFTY---PDsKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 555 NLSKLTGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKltfgIAILG- 633
Cdd:PRK13640 82 IREKVGIVFQNPDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQR----VAIAGi 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 634 ---DPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDR-VILFS-TQFMDEADiLADRKVFLSQGKLKCAGS 698
Cdd:PRK13640 158 lavEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnLTVISiTHDIDEAN-MADQVLVLDDGKLLAQGS 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1275-1505 |
4.95e-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: 4.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1275 DEKPVIIASCLRKEYAGKRKGCFskrknkIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG--- 1351
Cdd:COG1123 256 AAEPLLEVRNLSKRYPVRGKGGV------RAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGkdl 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1352 --SGGGDALEF---LGYCPQ--ENALWPNLTVRQHL-EVYAAVKGLRKGDAEVAITRLVDALKLQDQL--KSPvKTLSEG 1421
Cdd:COG1123 330 tkLSRRSLRELrrrVQMVFQdpYSSLNPRMTVGDIIaEPLRLHGLLSRAERRERVAELLERVGLPPDLadRYP-HELSGG 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1422 IKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1501
Cdd:COG1123 409 QRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGP 488
|
....
gi 572882597 1502 IQHL 1505
Cdd:COG1123 489 TEEV 492
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
479-693 |
5.24e-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: 5.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 479 AIRIRNVTKEYKGKpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNN------KLSEMAD 552
Cdd:COG4161 2 SIQLKNINCFYGSH----QALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdfsqKPSEKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 553 LENLSKLTGVCPQSNVqFDFLTVRENLrLFAKIK--GILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIA 630
Cdd:COG4161 78 RLLRQKVGMVFQQYNL-WPHLTVMENL-IEAPCKvlGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 572882597 631 ILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKT---DRVILfsTQFMDEADILADRKVFLSQGKL 693
Cdd:COG4161 156 LMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtgiTQVIV--THEVEFARKVASQVVYMEKGRI 219
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
480-693 |
5.45e-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: 5.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGkpdkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIyNNKlsemadlenlskl 559
Cdd:cd03216 1 LELRGITKRFGG----VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILV-DGK------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 tgvcpqsnvQFDFLTVRENLRLfakikGIlpqevdkeiqrvllelemkniqdVLAQNLSGGQKRKLTFGIAILGDPQIFL 639
Cdd:cd03216 63 ---------EVSFASPRDARRA-----GI-----------------------AMVYQLSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 572882597 640 LDEPTAGLDPFSRHQVWNLLKERKTDRV-ILFSTQFMDEADILADRKVFLSQGKL 693
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRRLRAQGVaVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1275-1514 |
6.44e-25 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 112.91 E-value: 6.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1275 DEKPVIIASCLRKeyagkRKGCFskrknkIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG--- 1351
Cdd:NF033858 262 DDEPAIEARGLTM-----RFGDF------TAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGqpv 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1352 -SGGGDALEFLGYCPQENALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVL 1430
Cdd:NF033858 331 dAGDIATRRRVGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAV 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1431 SILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAvCDRVAIMVSGRLRCIGSIQHLKSKFG 1510
Cdd:NF033858 411 AVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAER-CDRISLMHAGRVLASDTPAALVAARG 489
|
....
gi 572882597 1511 KDYL 1514
Cdd:NF033858 490 AATL 493
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
480-694 |
1.03e-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: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKPDKIEalkdlvFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLEN-LSK 558
Cdd:TIGR01277 1 LALDKVRYEYEHLPMEFD------LNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRpVSM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 559 LTgvcpQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIF 638
Cdd:TIGR01277 75 LF----QENNLFAHLTVRQNIGLGLHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 572882597 639 LLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKLK 694
Cdd:TIGR01277 151 LLDEPFSALDPLLREEMLALVKQlcSERQRTLLMVTHHLSDARAIASQIAVVSQGKIK 208
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
479-698 |
1.18e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 105.60 E-value: 1.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 479 AIRIRNVTKEYK-GKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKL---SEMADLE 554
Cdd:PRK13649 2 GINLQNVSYTYQaGTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstSKNKDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 555 NLSKLTGVC---PQSNVqFDfLTVRENLRLFAKIKGILPQEVDKeiqRVLLELEMKNI-QDVLAQN---LSGGQKRKltf 627
Cdd:PRK13649 82 QIRKKVGLVfqfPESQL-FE-ETVLKDVAFGPQNFGVSQEEAEA---LAREKLALVGIsESLFEKNpfeLSGGQMRR--- 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 572882597 628 gIAILG----DPQIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS 698
Cdd:PRK13649 154 -VAIAGilamEPKILVLDEPTAGLDPKGRKELMTLFKKlHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGK 228
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
480-698 |
1.43e-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: 1.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLEnLSKL 559
Cdd:COG4559 2 LEAENLSVRLGGRT----LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWE-LARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 TGVCPQ-SNVQFDFlTVRENLRLfakikGILP-----QEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAIL- 632
Cdd:COG4559 77 RAVLPQhSSLAFPF-TVEEVVAL-----GRAPhgssaAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAq 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 633 ------GDPQIFLLDEPTAGLDPFSRHQVWNLLKERkTDR-----VIL----FSTQFmdeadilADRKVFLSQGKLKCAG 697
Cdd:COG4559 151 lwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQL-ARRgggvvAVLhdlnLAAQY-------ADRILLLHQGRLVAQG 222
|
.
gi 572882597 698 S 698
Cdd:COG4559 223 T 223
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1305-1496 |
1.59e-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: 1.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1305 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSgggdaleflgycpqenalwpnltvrqhlevya 1384
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK-------------------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1385 avkglrkgdaEVAITRLVDALKL------QdqlkspvktLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQ 1458
Cdd:cd03216 63 ----------EVSFASPRDARRAgiamvyQ---------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFK 123
|
170 180 190
....*....|....*....|....*....|....*...
gi 572882597 1459 AIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1496
Cdd:cd03216 124 VIRR-LRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
479-697 |
1.99e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 104.82 E-value: 1.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 479 AIRIRNVTKEYKgkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLSK 558
Cdd:PRK13647 4 IIEVEDLHFRYK---DGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 559 LTGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKltfgIAILG----D 634
Cdd:PRK13647 81 VGLVFQDPDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKR----VAIAGvlamD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 572882597 635 PQIFLLDEPTAGLDPFSRHQV----WNLLKERKTdrvILFSTQFMDEADILADRKVFLSQGKLKCAG 697
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLmeilDRLHNQGKT---VIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1300-1476 |
2.21e-24 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 102.64 E-value: 2.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1300 RKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGD-----ALEFLGYcpqENALWPNL 1374
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDpdvaeACHYLGH---RNAMKPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1375 TVRQHLEVYAAVKGLRKGDAEVAItrlvDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQ 1454
Cdd:PRK13539 89 TVAENLEFWAAFLGGEELDIAAAL----EAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVA 164
|
170 180
....*....|....*....|....
gi 572882597 1455 QMWQAIRAtfrNTERG--ALLTTH 1476
Cdd:PRK13539 165 LFAELIRA---HLAQGgiVIAATH 185
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
470-693 |
2.45e-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: 2.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 470 APPEFQGKEAIRIRNVTKEYKGKpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLS--VP---TKGSVT--- 541
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGDK----QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlIPgarVEGEILldg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 542 --IYNNKLsemaDLENLSKLTG-VCPQSNVqfdF-LTVRENLRLFAKIKGILP-QEVDKEIQRVLLEL----EMKNIQDV 612
Cdd:COG1117 78 edIYDPDV----DVVELRRRVGmVFQKPNP---FpKSIYDNVAYGLRLHGIKSkSELDEIVEESLRKAalwdEVKDRLKK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 613 LAQNLSGGQKRKLTfgIA--ILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEADILADRKVFLSQ 690
Cdd:COG1117 151 SALGLSGGQQQRLC--IAraLAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARVSDYTAFFYL 228
|
...
gi 572882597 691 GKL 693
Cdd:COG1117 229 GEL 231
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
493-678 |
2.57e-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: 2.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 493 PDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKL--SEMADLENLSKLTGVCPQSNVQF 570
Cdd:TIGR01166 2 PGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLdySRKGLLERRQRVGLVFQDPDDQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 571 DFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPF 650
Cdd:TIGR01166 82 FAADVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPA 161
|
170 180
....*....|....*....|....*....
gi 572882597 651 SRHQVWNLLKE-RKTDRVILFSTQFMDEA 678
Cdd:TIGR01166 162 GREQMLAILRRlRAEGMTVVISTHDVDLA 190
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
479-693 |
2.58e-24 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 103.56 E-value: 2.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 479 AIRIRNVTKEYKGKpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNK--LSEMADLENL 556
Cdd:PRK11124 2 SIQLNGINCFYGAH----QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdFSKTPSDKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 557 SKLtgvcpQSNVQFDF--------LTVRENL-RLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTF 627
Cdd:PRK11124 78 REL-----RRNVGMVFqqynlwphLTVQQNLiEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 572882597 628 GIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE-RKT--DRVILfsTQFMDEADILADRKVFLSQGKL 693
Cdd:PRK11124 153 ARALMMEPQVLLFDEPTAALDPEITAQIVSIIRElAETgiTQVIV--THEVEVARKTASRVVYMENGHI 219
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
501-697 |
2.71e-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: 102.76 E-value: 2.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 501 DLVFDIyEGQITAILGHSGAGKSTLLNILSGLSVPTKGSV----TIYNNKLSEMaDLENLSKLTGVCPQSNVQFDFLTVR 576
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngTVLFDSRKKI-NLPPQQRKIGLVFQQYALFPHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 577 ENLRLFAKIKGILPQEVDKEIQRVLLELEmkNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVW 656
Cdd:cd03297 94 ENLAFGLKRKRNREDRISVDELLDLLGLD--HLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 572882597 657 NLLKERKTDRVI--LFSTQFMDEADILADRKVFLSQGKLKCAG 697
Cdd:cd03297 172 PELKQIKKNLNIpvIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
455-688 |
2.77e-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: 2.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 455 DEMDADPSFHDSF---EQAPPEFQGKE--------AIRIRNVTKEYkgkPDKIEALKDLVFDIYEGQITAILGHSGAGKS 523
Cdd:TIGR02857 286 ARADGVAAAEALFavlDAAPRPLAGKApvtaapasSLEFSGVSVAY---PGRRPALRPVSFTVPPGERVALVGPSGAGKS 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 524 TLLNILSGLSVPTKGSVTIYNNKLSEmADLENLSKLTGVCPQSNVQFDfLTVRENLRLFAkiKGILPQEVDKEIQRV-LL 602
Cdd:TIGR02857 363 TLLNLLLGFVDPTEGSIAVNGVPLAD-ADADSWRDQIAWVPQHPFLFA-GTIAENIRLAR--PDASDAEIREALERAgLD 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 603 ELEM---KNIQDVLAQN---LSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQfmD 676
Cdd:TIGR02857 439 EFVAalpQGLDTPIGEGgagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTH--R 516
|
250
....*....|...
gi 572882597 677 EADI-LADRKVFL 688
Cdd:TIGR02857 517 LALAaLADRIVVL 529
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
480-712 |
3.08e-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: 3.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMaDLENLSKL 559
Cdd:cd03251 1 VEFKNVTFRYPG--DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDY-TLASLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 TGVCPQSNVQFDFlTVRENLRlFAKikgilPQEVDKEIQRVlleLEMKNIQDVLAQ--------------NLSGGQKRKL 625
Cdd:cd03251 78 IGLVSQDVFLFND-TVAENIA-YGR-----PGATREEVEEA---ARAANAHEFIMElpegydtvigergvKLSGGQRQRI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 626 TFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVIL-----FSTqFMDeadilADRKVFLSQGKLKCAGSSL 700
Cdd:cd03251 148 AIARALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFviahrLST-IEN-----ADRIVVLEDGKIVERGTHE 221
|
250
....*....|..
gi 572882597 701 FLKKKWGIGYHL 712
Cdd:cd03251 222 ELLAQGGVYAKL 233
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
479-713 |
3.12e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 104.53 E-value: 3.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 479 AIRIRNVTKEYK-GKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLS 557
Cdd:PRK13641 2 SIKFENVDYIYSpGTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 558 KL---TGVCPQ-SNVQFDFLTVRENLRLFAKIKGILPQEVD----KEIQRVLLELEMKNIQDVlaqNLSGGQKRKLTFGI 629
Cdd:PRK13641 82 KLrkkVSLVFQfPEAQLFENTVLKDVEFGPKNFGFSEDEAKekalKWLKKVGLSEDLISKSPF---ELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 630 AILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKL--KCAGSSLFLKKKW 706
Cdd:PRK13641 159 VMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDyQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLikHASPKEIFSDKEW 238
|
....*..
gi 572882597 707 GIGYHLS 713
Cdd:PRK13641 239 LKKHYLD 245
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1307-1496 |
3.31e-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: 3.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1307 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-----SGGGDALEfLG----YcpQENALWPNLTVR 1377
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepvrfRSPRDAQA-AGiaiiH--QELNLVPNLSVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1378 Q--HLEVYAAVKGLRKGDAEVAITR-LVDALKLQDQLKSPVKTLSEGiKRKLcfVL---SILGNPSVVLLDEPSTGMDPE 1451
Cdd:COG1129 98 EniFLGREPRRGGLIDWRAMRRRAReLLARLGLDIDPDTPVGDLSVA-QQQL--VEiarALSRDARVLILDEPTASLTER 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 572882597 1452 GQQQMWQAIRaTFRntERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1496
Cdd:COG1129 175 EVERLFRIIR-RLK--AQGVaiIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
480-692 |
4.23e-24 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 102.53 E-value: 4.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKPdkiealkdLVFD--IYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIyNNklsemadlENLS 557
Cdd:COG3840 2 LRLDDLTYRYGDFP--------LRFDltIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILW-NG--------QDLT 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 558 KLTgvcP---------QSNVQFDFLTVRENLRLfakikGILP---------QEVDKEIQRVLLElemkNIQDVLAQNLSG 619
Cdd:COG3840 65 ALP---PaerpvsmlfQENNLFPHLTVAQNIGL-----GLRPglkltaeqrAQVEQALERVGLA----GLLDRLPGQLSG 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 572882597 620 GQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGK 692
Cdd:COG3840 133 GQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDElcRERGLTVLMVTHDPEDAARIADRVLLVADGR 207
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
495-693 |
5.91e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 102.93 E-value: 5.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 495 KIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLS-----VPTKGSVtIYN--NKLSEMADLENLSKLTGVCPQSN 567
Cdd:PRK14239 17 KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNdlnpeVTITGSI-VYNghNIYSPRTDTVDLRKEIGMVFQQP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 568 VQFDFlTVRENLRLFAKIKGI-----LPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDE 642
Cdd:PRK14239 96 NPFPM-SIYENVVYGLRLKGIkdkqvLDEAVEKSLKGASIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 572882597 643 PTAGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEADILADRKVFLSQGKL 693
Cdd:PRK14239 175 PTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDL 225
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
466-649 |
6.26e-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: 6.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 466 SFEQAPPEFQGKEAIRIRNVTKEYKGKPdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNN 545
Cdd:TIGR02868 321 SAPAAGAVGLGKPTLELRDLSAGYPGAP---PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGV 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 546 KLSEmADLENLSKLTGVCPQSNVQFDfLTVRENLRLFAkiKGILPQEVDKEIQRVLLELEMKNIQDVL-------AQNLS 618
Cdd:TIGR02868 398 PVSS-LDQDEVRRRVSVCAQDAHLFD-TTVRENLRLAR--PDATDEELWAALERVGLADWLRALPDGLdtvlgegGARLS 473
|
170 180 190
....*....|....*....|....*....|.
gi 572882597 619 GGQKRKLTFGIAILGDPQIFLLDEPTAGLDP 649
Cdd:TIGR02868 474 GGERQRLALARALLADAPILLLDEPTEHLDA 504
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
477-697 |
9.43e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 103.17 E-value: 9.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 477 KEAIRIRNVTKEYKGkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENL 556
Cdd:PRK13635 3 EEIIRVEHISFRYPD--AATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 557 SKLTGVCPQSNVQFDFLTVRENLRLFAKIKGIlpqEVDKEIQRVLLELEMKNIQDVLAQ---NLSGGQKRKltfgIAILG 633
Cdd:PRK13635 81 RQVGMVFQNPDNQFVGATVQDDVAFGLENIGV---PREEMVERVDQALRQVGMEDFLNRephRLSGGQKQR----VAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 572882597 634 ----DPQIFLLDEPTAGLDPFSRHQVWN---LLKERKTDRVILFsTQFMDEAdILADRKVFLSQGKLKCAG 697
Cdd:PRK13635 154 vlalQPDIIILDEATSMLDPRGRREVLEtvrQLKEQKGITVLSI-THDLDEA-AQADRVIVMNKGEILEEG 222
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
480-705 |
9.79e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 103.00 E-value: 9.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYkgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVtIYNNKLSEMA--DLENLS 557
Cdd:PRK13636 6 LKVEELNYNY---SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRI-LFDGKPIDYSrkGLMKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 558 KLTGVCPQS-NVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQ 636
Cdd:PRK13636 82 ESVGMVFQDpDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPK 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 572882597 637 IFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAG--SSLFLKKK 705
Cdd:PRK13636 162 VLVLDEPTAGLDPMGVSEIMKLLVEmqKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGnpKEVFAEKE 234
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
501-698 |
1.38e-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: 1.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 501 DLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMA---DLENLSKLTGVCPQSNVQFDFLTVRE 577
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRkgiFLPPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 578 NLRLfaKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWN 657
Cdd:TIGR02142 95 NLRY--GMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 572882597 658 LLkERKTDRV---ILFSTQFMDEADILADRKVFLSQGKLKCAGS 698
Cdd:TIGR02142 173 YL-ERLHAEFgipILYVSHSLQEVLRLADRVVVLEDGRVAAAGP 215
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
480-688 |
2.46e-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: 2.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIynnklsemaDLENLSKL 559
Cdd:COG1137 4 LEAENLVKSYGKRT----VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFL---------DGEDITHL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 T---------GVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIA 630
Cdd:COG1137 71 PmhkrarlgiGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 631 ILGDPQIFLLDEPTAGLDPFSRHQVWNL---LKERK----------------TDRV-ILFSTQFMDE---ADILAD---R 684
Cdd:COG1137 151 LATNPKFILLDEPFAGVDPIAVADIQKIirhLKERGigvlitdhnvretlgiCDRAyIISEGKVLAEgtpEEILNNplvR 230
|
....
gi 572882597 685 KVFL 688
Cdd:COG1137 231 KVYL 234
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
480-649 |
2.78e-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: 100.45 E-value: 2.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEM-ADLENLSK 558
Cdd:COG1126 2 IEIENLHKSFGDL----EVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSkKDINKLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 559 LTGVCPQS-NVqFDFLTVRENLRLfA--KIKGILPQEVdKEIQRVLLE-LEMKNIQDVLAQNLSGGQK-RkltfgIAI-- 631
Cdd:COG1126 78 KVGMVFQQfNL-FPHLTVLENVTL-ApiKVKKMSKAEA-EERAMELLErVGLADKADAYPAQLSGGQQqR-----VAIar 149
|
170 180
....*....|....*....|
gi 572882597 632 -LG-DPQIFLLDEPTAGLDP 649
Cdd:COG1126 150 aLAmEPKVMLFDEPTSALDP 169
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1298-1500 |
3.80e-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: 3.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1298 SKR-KNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGD--------ALEFLGYcpqen 1368
Cdd:cd03301 7 TKRfGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDlppkdrdiAMVFQNY----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1369 ALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGM 1448
Cdd:cd03301 82 ALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 572882597 1449 DPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1500
Cdd:cd03301 162 DAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
480-698 |
4.40e-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: 99.49 E-value: 4.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMaDLENLSKL 559
Cdd:cd03244 3 IEFKNVSLRYR--PNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKI-GLHDLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 TGVCPQSNVQFDFlTVRENLRLFAkikgilpQEVDKEIQRVLLELEMKNIQDVLA-----------QNLSGGQKRKLTFG 628
Cdd:cd03244 80 ISIIPQDPVLFSG-TIRSNLDPFG-------EYSDEELWQALERVGLKEFVESLPggldtvveeggENLSVGQRQLLCLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 572882597 629 IAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQ----FMDeadilADRKVFLSQGKLKCAGS 698
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHrldtIID-----SDRILVLDKGRVVEFDS 220
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
480-712 |
6.34e-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: 99.54 E-value: 6.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKPDkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMAdLENLSKL 559
Cdd:cd03249 1 IEFKNVSFRYPSRPD-VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLN-LRWLRSQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 TGVCPQSNVQFDfLTVRENLRLfakikGiLPQEVDKEIQRVlleLEMKNIQDVLAQ--------------NLSGGQKRKL 625
Cdd:cd03249 79 IGLVSQEPVLFD-GTIAENIRY-----G-KPDATDEEVEEA---AKKANIHDFIMSlpdgydtlvgergsQLSGGQKQRI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 626 TFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVIL-----FSTqfmdeadIL-ADRKVFLSQGKLKCAGSS 699
Cdd:cd03249 149 AIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIviahrLST-------IRnADLIAVLQNGQVVEQGTH 221
|
250
....*....|...
gi 572882597 700 LFLKKKWGIGYHL 712
Cdd:cd03249 222 DELMAQKGVYAKL 234
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
480-697 |
7.09e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 100.21 E-value: 7.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVtIYNNKLSEMADLENLSKL 559
Cdd:PRK13648 8 IVFKNVSFQYQS--DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEI-FYNNQAITDDNFEKLRKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 TGVCPQ--------SNVQFDFLTVRENLRL-FAKIKGILPQevdkeiqrVLLELEMKNIQDVLAQNLSGGQKRKltfgIA 630
Cdd:PRK13648 85 IGIVFQnpdnqfvgSIVKYDVAFGLENHAVpYDEMHRRVSE--------ALKQVDMLERADYEPNALSGGQKQR----VA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 572882597 631 ILG----DPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDR--VILFSTQFMDEAdILADRKVFLSQGKLKCAG 697
Cdd:PRK13648 153 IAGvlalNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEA-MEADHVIVMNKGTVYKEG 224
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1307-1514 |
8.98e-23 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 98.95 E-value: 8.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1307 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSgggDALEF------LGYCPQENALWPNLTVRQHL 1380
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGK---DITNLppekrdISYVPQNYALFPHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1381 EVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAI 1460
Cdd:cd03299 93 AYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREEL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 572882597 1461 RATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQ----HLKSKFGKDYL 1514
Cdd:cd03299 173 KKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEevfkKPKNEFVAEFL 230
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
499-691 |
1.19e-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: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 499 LKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSE-----MADLENLSKLTgvcpqsnvqfdFL 573
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEpgpdrMVVFQNYSLLP-----------WL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 574 TVRENLRLfaKIKGILPQEVDKEIQRVLLE-LEMKNI---QDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDP 649
Cdd:TIGR01184 70 TVRENIAL--AVDRVLPDLSKSERRAIVEEhIALVGLteaADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 572882597 650 FSRHQVWN-LLKERKTDRV-ILFSTQFMDEADILADRKVFLSQG 691
Cdd:TIGR01184 148 LTRGNLQEeLMQIWEEHRVtVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1285-1505 |
1.19e-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: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1285 LRKEYAGKRKgcfskrkNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDAL-E 1359
Cdd:cd03258 7 VSKVFGDTGG-------KVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGtdltLLSGKELrK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1360 F---LGYCPQENALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNP 1436
Cdd:cd03258 80 ArrrIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 572882597 1437 SVVLLDEPSTGMDPEGQQQMWQAIRATfrNTERG--ALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL 1505
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDI--NRELGltIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
483-692 |
1.84e-22 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 104.36 E-value: 1.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 483 RNVTKEYKGKPDKIeALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVP-TKGSVTIYNNklSEMADLENLSKLTG 561
Cdd:TIGR00955 26 RLRGCFCRERPRKH-LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgVKGSGSVLLN--GMPIDAKEMRAISA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 562 VCPQSNVQFDFLTVRENLRLFAKIKgiLPQEVDKE-----IQRVLLELEMKNIQDVLAQ------NLSGGQKRKLTFGIA 630
Cdd:TIGR00955 103 YVQQDDLFIPTLTVREHLMFQAHLR--MPRRVTKKekrerVDEVLQALGLRKCANTRIGvpgrvkGLSGGERKRLAFASE 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 572882597 631 ILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEADI--LADRKVFLSQGK 692
Cdd:TIGR00955 181 LLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELfeLFDKIILMAEGR 244
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
475-698 |
2.12e-22 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 101.18 E-value: 2.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 475 QGKEAIRIRNVTKEYKGKpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIynnklsemadle 554
Cdd:PRK09452 10 SLSPLVELRGISKSFDGK----EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIML------------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 555 NLSKLTGVCP---------QSNVQFDFLTVRENLRLFAKIKGILPQEVDKeiqRVLLELEMKNIQDvLAQ----NLSGGQ 621
Cdd:PRK09452 74 DGQDITHVPAenrhvntvfQSYALFPHMTVFENVAFGLRMQKTPAAEITP---RVMEALRMVQLEE-FAQrkphQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 572882597 622 KRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLK--ERKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS 698
Cdd:PRK09452 150 QQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKalQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1297-1500 |
2.32e-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: 2.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1297 FSKRKNKIAtRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGsgggdaleflgycpQENALWPNLTV 1376
Cdd:cd03214 7 VGYGGRTVL-DDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDG--------------KDLASLSPKEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1377 RQHLEVyaavkglrkgdaevaITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQM 1456
Cdd:cd03214 72 ARKIAY---------------VPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIEL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 572882597 1457 WQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1500
Cdd:cd03214 137 LELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
504-698 |
2.33e-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: 2.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 504 FDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLS----KLtGVCPQSNVQFDFLTVRENL 579
Cdd:COG4148 20 FTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFLPphrrRI-GYVFQEARLFPHLSVRGNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 580 RlFAkIKGILPQEvdkeiQRVLLE--LEMKNIQDVLA---QNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQ 654
Cdd:COG4148 99 L-YG-RKRAPRAE-----RRISFDevVELLGIGHLLDrrpATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 572882597 655 VWNLLkERKTDRV---ILFSTQFMDEADILADRKVFLSQGKLKCAGS 698
Cdd:COG4148 172 ILPYL-ERLRDELdipILYVSHSLDEVARLADHVVLLEQGRVVASGP 217
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1307-1495 |
4.32e-22 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 97.46 E-value: 4.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1307 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVL-LKGS--GGGDALE---FLGYCPQENALW--PNLTVRq 1378
Cdd:COG1119 20 DDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrLFGErrGGEDVWElrkRIGLVSPALQLRfpRDETVL- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1379 hlEV-----YAAVkGLRK--GDAEVAITR-LVDALKLQDQLKSPVKTLSEGIKRKlcfVL---SILGNPSVVLLDEPSTG 1447
Cdd:COG1119 99 --DVvlsgfFDSI-GLYRepTDEQRERAReLLELLGLAHLADRPFGTLSQGEQRR---VLiarALVKDPELLILDEPTAG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 572882597 1448 MDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1495
Cdd:COG1119 173 LDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGR 220
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
480-697 |
4.51e-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: 97.02 E-value: 4.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKpdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVtiynnkLSEMADLENLS-- 557
Cdd:cd03299 1 LKVENLSKDWKEF-----KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKI------LLNGKDITNLPpe 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 558 -KLTGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLlelEMKNIQDVLAQN---LSGGQKRKLTFGIAILG 633
Cdd:cd03299 70 kRDISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIA---EMLGIDHLLNRKpetLSGGEQQRVAIARALVV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 572882597 634 DPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAG 697
Cdd:cd03299 147 NPKILLLDEPFSALDVRTKEKLREELKKirKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVG 212
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
484-698 |
4.61e-22 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 96.89 E-value: 4.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 484 NVTKEYKGKpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLSKLTGVC 563
Cdd:PRK10895 8 NLAKAYKGR----RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 564 PQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLL-ELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDE 642
Cdd:PRK10895 84 PQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMeEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 572882597 643 PTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS 698
Cdd:PRK10895 164 PFAGVDPISVIDIKRIIEHlRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
479-679 |
4.71e-22 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 103.67 E-value: 4.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 479 AIRIRNVTKEYKgkpdKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNnklsemADLENLSK 558
Cdd:NF033858 1 VARLEGVSHRYG----KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLG------GDMADARH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 559 LTGVCPQ---------SNVQFDfLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGI 629
Cdd:NF033858 71 RRAVCPRiaympqglgKNLYPT-LSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCC 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 572882597 630 AILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRV---ILFSTQFMDEAD 679
Cdd:NF033858 150 ALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERPgmsVLVATAYMEEAE 202
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1296-1494 |
5.17e-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: 95.79 E-value: 5.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1296 CFSKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGS--GGGDALEFLGYCPQEnalwpn 1373
Cdd:cd03226 6 SFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKpiKAKERRKSIGYVMQD------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1374 ltVRQHL-------EVYAAVKGLRKGDAEVA-ITRLVDALKLQDQLksPvKTLSEGIKRKLCFVLSILGNPSVVLLDEPS 1445
Cdd:cd03226 80 --VDYQLftdsvreELLLGLKELDAGNEQAEtVLKDLDLYALKERH--P-LSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 572882597 1446 TGMDPEGQQQMWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSG 1494
Cdd:cd03226 155 SGLDYKNMERVGELIR-ELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
480-698 |
6.49e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 97.37 E-value: 6.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYkgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLSKL 559
Cdd:PRK13644 2 IRLENVSYSY---PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 TGVCPQS-NVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIF 638
Cdd:PRK13644 79 VGIVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 572882597 639 LLDEPTAGLDPFSRHQVW-NLLKERKTDRVILFSTQFMDEADIlADRKVFLSQGKLKCAGS 698
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLeRIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGE 218
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1304-1496 |
7.64e-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: 7.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1304 IATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-----SGGGDALEF-LGYCPQENALWPNLTVR 1377
Cdd:COG3845 19 VANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpvriRSPRDAIALgIGMVHQHFMLVPNLTVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1378 QHLeVYAAVKG----LRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQ 1453
Cdd:COG3845 99 ENI-VLGLEPTkggrLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 572882597 1454 QQMWQAIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1496
Cdd:COG3845 178 DELFEILRR-LAAEGKSIIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
480-711 |
1.04e-21 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 98.95 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYkgkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKlseMADLENLSKL 559
Cdd:PRK11000 4 VTLRNVTKAY----GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKR---MNDVPPAERG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 TGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFL 639
Cdd:PRK11000 77 VGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 572882597 640 LDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGSSLFLkkkwgigYH 711
Cdd:PRK11000 157 LDEPLSNLDAALRVQMRIEISRlhKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL-------YH 223
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1307-1496 |
1.13e-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: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1307 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTA--GQVLLKGSGGgDALEF---LGYCPQENALWPNLTVRQHLE 1381
Cdd:cd03213 26 KNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPL-DKRSFrkiIGYVPQDDILHPTLTVRETLM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1382 VYAAVKGLrkgdaevaitrlvdalklqdqlkspvktlSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIR 1461
Cdd:cd03213 105 FAAKLRGL-----------------------------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLR 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 572882597 1462 AtFRNTERGALLTTHY-MAEAEAVCDRVAIMVSGRL 1496
Cdd:cd03213 156 R-LADTGRTIICSIHQpSSEIFELFDKLLLLSQGRV 190
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1307-1506 |
1.17e-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: 95.65 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1307 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDALEFL----GYCPQENALWPNLTVRQ 1378
Cdd:cd03261 17 KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGedisGLSEAELYRLrrrmGMLFQSGALFDSLTVFE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1379 HLEVYaavkgLR---KGDAEVaITRLVdALKLQ------DQLKSPVKtLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMD 1449
Cdd:cd03261 97 NVAFP-----LRehtRLSEEE-IREIV-LEKLEavglrgAEDLYPAE-LSGGMKKRVALARALALDPELLLYDEPTAGLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 572882597 1450 PEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLK 1506
Cdd:cd03261 169 PIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELR 225
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
483-660 |
1.21e-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: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 483 RNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSG--LSVPTKGSVTIYNNKLSemadlENLSKLT 560
Cdd:cd03232 7 KNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLD-----KNFQRST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 561 GVCPQSNVQFDFLTVRENLRLFAKIKGilpqevdkeiqrvllelemkniqdvlaqnLSGGQKRKLTFGIAILGDPQIFLL 640
Cdd:cd03232 82 GYVEQQDVHSPNLTVREALRFSALLRG-----------------------------LSVEQRKRLTIGVELAAKPSILFL 132
|
170 180
....*....|....*....|
gi 572882597 641 DEPTAGLDPFSRHQVWNLLK 660
Cdd:cd03232 133 DEPTSGLDSQAAYNIVRFLK 152
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1302-1501 |
1.34e-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: 95.38 E-value: 1.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1302 NKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsGGGDALEFLGYCPQEN------ALWPNLT 1375
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILL---DGKDITNLPPHKRPVNtvfqnyALFPHLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1376 VRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQ 1455
Cdd:cd03300 89 VFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 572882597 1456 MWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1501
Cdd:cd03300 169 MQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
480-732 |
1.47e-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: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLS--VPTKGSVtIYNNKLSEMAD-LENL 556
Cdd:TIGR03269 1 IEVKNLTKKFDGK----EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRI-IYHVALCEKCGyVERP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 557 SKLTGVCPQSNVQF-----DFL----TVRENL---------RLFA---------KIKGILPQ---EVDKEIQRVLLELEM 606
Cdd:TIGR03269 76 SKVGEPCPVCGGTLepeevDFWnlsdKLRRRIrkriaimlqRTFAlygddtvldNVLEALEEigyEGKEAVGRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 607 KNIQDV---LAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADIL 681
Cdd:TIGR03269 156 VQLSHRithIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTSHWPEVIEDL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 572882597 682 ADRKVFLSQGKLKCAGSSLFLKKKWGIGYHLSLQLNEICVEENITSL--VKQH 732
Cdd:TIGR03269 236 SDKAIWLENGEIKEEGTPDEVVAVFMEGVSEVEKECEVEVGEPIIKVrnVSKR 288
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
480-698 |
1.57e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 96.73 E-value: 1.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYK-GKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYN---NKLSEMADLEN 555
Cdd:PRK13643 2 IKFEKVNYTYQpNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 556 LSKLTGVC---PQSnvQFDFLTVRENLRLFAKIKGILPQEVDKEIQRvllELEMKNIQDVLAQN----LSGGQKRKLTFG 628
Cdd:PRK13643 82 VRKKVGVVfqfPES--QLFEETVLKDVAFGPQNFGIPKEKAEKIAAE---KLEMVGLADEFWEKspfeLSGGQMRRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 572882597 629 IAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS 698
Cdd:PRK13643 157 GILAMEPEVLVLDEPTAGLDPKARIEMMQLFESiHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGT 227
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
470-693 |
1.75e-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: 1.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 470 APPEFQGKeaIRIRNVTKEYKGKPDKiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVtIYNNKLSE 549
Cdd:cd03248 4 APDHLKGI--VKFQNVTFAYPTRPDT-LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQV-LLDGKPIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 550 MADLENLSKLTGVCPQSNVQFDfLTVRENlrlfakIKGILPQEVDKEIQRV-----------LLELEMKNIQDVLAQNLS 618
Cdd:cd03248 80 QYEHKYLHSKVSLVGQEPVLFA-RSLQDN------IAYGLQSCSFECVKEAaqkahahsfisELASGYDTEVGEKGSQLS 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 572882597 619 GGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEADiLADRKVFLSQGKL 693
Cdd:cd03248 153 GGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVE-RADQILVLDGGRI 226
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
480-701 |
1.84e-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: 1.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYkgkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLSKL 559
Cdd:PRK11614 6 LSFDKVSAHY----GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 TGVCPQSNVQFDFLTVRENLRL---FAKikgilPQEVDKEIQRV---LLELEMKNIQDvlAQNLSGGQKRKLTFGIAILG 633
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLAMggfFAE-----RDQFQERIKWVyelFPRLHERRIQR--AGTMSGGEQQMLAIGRALMS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 572882597 634 DPQIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGK--LKCAGSSLF 701
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPIIIQQIFDTIEQlREQGMTIFLVEQNANQALKLADRGYVLENGHvvLEDTGDALL 225
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
499-648 |
2.43e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 93.79 E-value: 2.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 499 LKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTiYNNKLSEMADLENLSKLTGvcpQSNVQFDFLTVREN 578
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIK-LDGGDIDDPDVAEACHYLG---HRNAMKPALTVAEN 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 572882597 579 LRLFAKIKGILPQEVDKEIQRVllelEMKNIQDVLAQNLSGGQKRKLtfGIAIL---GDPqIFLLDEPTAGLD 648
Cdd:PRK13539 94 LEFWAAFLGGEELDIAAALEAV----GLAPLAHLPFGYLSAGQKRRV--ALARLlvsNRP-IWILDEPTAALD 159
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
479-691 |
3.32e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 94.77 E-value: 3.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 479 AIRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLsemadlENLSK 558
Cdd:PRK11248 1 MLQISHLYADYGGKP----ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV------EGPGA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 559 LTGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIF 638
Cdd:PRK11248 71 ERGVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 572882597 639 LLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQG 691
Cdd:PRK11248 151 LLDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1307-1502 |
3.49e-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: 3.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1307 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDALEFLgycpQENALWPNLTVRQH--L 1380
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGkqitEPGPDRMVVF----QNYSLLPWLTVRENiaL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1381 EVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDP-------EGQ 1453
Cdd:TIGR01184 78 AVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAltrgnlqEEL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 572882597 1454 QQMWQAIRATfrntergALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSI 1502
Cdd:TIGR01184 158 MQIWEEHRVT-------VLMVTHDVDEALLLSDRVVMLTNGPAANIGQI 199
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
480-711 |
4.76e-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: 4.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKgkPDKiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMaDLENLSKL 559
Cdd:cd03253 1 IEFENVTFAYD--PGR-PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREV-TLDSLRRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 TGVCPQSNVQFDfLTVRENLRlFAKikgilPQEVDKEIQRVlleLEMKNIQDVLAQ--------------NLSGGQKRKL 625
Cdd:cd03253 77 IGVVPQDTVLFN-DTIGYNIR-YGR-----PDATDEEVIEA---AKAAQIHDKIMRfpdgydtivgerglKLSGGEKQRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 626 TFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILF-----STqFMDeadilADRKVFLSQGKLKCAGSSL 700
Cdd:cd03253 147 AIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIViahrlST-IVN-----ADKIIVLKDGRIVERGTHE 220
|
250
....*....|.
gi 572882597 701 FLKKKWGIgYH 711
Cdd:cd03253 221 ELLAKGGL-YA 230
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
480-692 |
7.28e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 96.44 E-value: 7.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLEnlsKL 559
Cdd:PRK11607 20 LEIRNLTKSFDGQH----AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ---RP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 TGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFL 639
Cdd:PRK11607 93 INMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 572882597 640 LDEPTAGLDPFSR----HQVWNLLKERKTDRVILFSTQfmDEADILADRKVFLSQGK 692
Cdd:PRK11607 173 LDEPMGALDKKLRdrmqLEVVDILERVGVTCVMVTHDQ--EEAMTMAGRIAIMNRGK 227
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
511-707 |
7.54e-21 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 96.10 E-value: 7.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 511 ITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLS---KLTGVCPQSNVQFDFLTVRENLRLfaKIKG 587
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLPpekRRIGYVFQDARLFPHYKVRGNLRY--GMAK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 588 ILPQEVDKEIQrvLLELEmkNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLkERKTDRV 667
Cdd:PRK11144 104 SMVAQFDKIVA--LLGIE--PLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYL-ERLAREI 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 572882597 668 ---ILFSTQFMDEADILADRKVFLSQGKLKCAGSslfLKKKWG 707
Cdd:PRK11144 179 nipILYVSHSLDEILRLADRVVVLEQGKVKAFGP---LEEVWA 218
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
480-655 |
8.53e-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: 8.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADlENLSKL 559
Cdd:COG4604 2 IEIKNVSKRYGGKV----VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPS-RELAKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 TGVCPQSNVQFDFLTVREnLRLFAKI---KGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQkRKLTFgIA--ILGD 634
Cdd:COG4604 77 LAILRQENHINSRLTVRE-LVAFGRFpysKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQ-RQRAF-IAmvLAQD 153
|
170 180
....*....|....*....|.
gi 572882597 635 PQIFLLDEPTAGLDPfsRHQV 655
Cdd:COG4604 154 TDYVLLDEPLNNLDM--KHSV 172
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1303-1518 |
1.01e-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: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1303 KIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSgggDALEflgycpqENALWpnlTVRQHLE- 1381
Cdd:TIGR04520 15 KPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGL---DTLD-------EENLW---EIRKKVGm 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1382 ---------VYAAVK-----GL--RKGDAEVAITRLVDALK---LQDQLKSPVKTLSEGIKRKLCfVLSILG-NPSVVLL 1441
Cdd:TIGR04520 82 vfqnpdnqfVGATVEddvafGLenLGVPREEMRKRVDEALKlvgMEDFRDREPHLLSGGQKQRVA-IAGVLAmRPDIIIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1442 DEPsTGM-DPEGQQQMWQAIRATfrNTERGA--LLTTHYMAEAeAVCDRVAIMVSGRLRCIGSIQHLKSKfgKDYLLEMK 1518
Cdd:TIGR04520 161 DEA-TSMlDPKGRKEVLETIRKL--NKEEGItvISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIFSQ--VELLKEIG 234
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
470-693 |
1.09e-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: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 470 APPEFQGKeaIRIRNVTKEYKGkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSE 549
Cdd:TIGR02203 323 AIERARGD--VEFRNVTFRYPG--RDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLAD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 550 MAdLENLSKLTGVCPQSNVQFDFlTVRENLRLfakikGILPQEVDKEIQRVLlelEMKNIQDVLAQ-------------- 615
Cdd:TIGR02203 399 YT-LASLRRQVALVSQDVVLFND-TIANNIAY-----GRTEQADRAEIERAL---AAAYAQDFVDKlplgldtpigengv 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 616 NLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVW----NLLKERkTDRVILFSTQFMDEadilADRKVFLSQG 691
Cdd:TIGR02203 469 LLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQaaleRLMQGR-TTLVIAHRLSTIEK----ADRIVVMDDG 543
|
..
gi 572882597 692 KL 693
Cdd:TIGR02203 544 RI 545
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
496-693 |
1.53e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 93.05 E-value: 1.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 496 IEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGL-----SVPTKGSVTIYNNKLSEMaDLENLSKLTGVCPQSNVQF 570
Cdd:PRK14247 16 VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKM-DVIELRRRVQMVFQIPNPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 571 DFLTVRENLRL------FAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPT 644
Cdd:PRK14247 95 PNLSIFENVALglklnrLVKSKKELQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPT 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 572882597 645 AGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEADILADRKVFLSQGKL 693
Cdd:PRK14247 175 ANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
480-697 |
1.71e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 97.16 E-value: 1.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGkpdkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIyNNKLSEMADLENLSKL 559
Cdd:PRK09700 6 ISMAGIGKSFGP----VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITI-NNINYNKLDHKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 -TGVCPQSNVQFDFLTVRENL---RLFAK----IKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAI 631
Cdd:PRK09700 81 gIGIIYQELSVIDELTVLENLyigRHLTKkvcgVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 572882597 632 LGDPQIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAG 697
Cdd:PRK09700 161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQlRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1307-1515 |
2.01e-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: 97.98 E-value: 2.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1307 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsGGGDALEF--------LGYCPQENALWP-----N 1373
Cdd:COG2274 492 DNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILI---DGIDLRQIdpaslrrqIGVVLQDVFLFSgtireN 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1374 LTVrqhlevyaavkglrkGDAEVAITRLVDALK----------LQDQLKSPV----KTLSEGIKRKLCFVLSILGNPSVV 1439
Cdd:COG2274 569 ITL---------------GDPDATDEEIIEAARlaglhdfieaLPMGYDTVVgeggSNLSGGQRQRLAIARALLRNPRIL 633
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 572882597 1440 LLDEPSTGMDPEGQQQMWQAIRATFRNteRGALLTTHYMAEAEAvCDRVAIMVSGRLRCIGSIQHLKSKFGKDYLL 1515
Cdd:COG2274 634 ILDEATSALDAETEAIILENLRRLLKG--RTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEELLARKGLYAEL 706
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
479-698 |
2.05e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 94.77 E-value: 2.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 479 AIRIRNVTKEYkgkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLEnlsK 558
Cdd:PRK10851 2 SIEIANIKKSF----GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD---R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 559 LTGVCPQSNVQFDFLTVRENLRLFAKikgILPQ-------EVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAI 631
Cdd:PRK10851 75 KVGFVFQHYALFRHMTVFDNIAFGLT---VLPRrerpnaaAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 572882597 632 LGDPQIFLLDEPTAGLDPFSRHQV--W--NLLKERKTDRVilFSTQFMDEADILADRKVFLSQGKLKCAGS 698
Cdd:PRK10851 152 AVEPQILLLDEPFGALDAQVRKELrrWlrQLHEELKFTSV--FVTHDQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
480-698 |
2.39e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 92.38 E-value: 2.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLEnLSKL 559
Cdd:PRK11231 3 LRTENLTVGYGTKR----ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ-LARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 TGVCPQSNVQFDFLTVRE--------NLRLFakikGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAI 631
Cdd:PRK11231 78 LALLPQHHLTPEGITVRElvaygrspWLSLW----GRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 572882597 632 LGDPQIFLLDEPTAGLDpfSRHQV--WNLLKER----KTDRVILFStqfMDEADILADRKVFLSQGKLKCAGS 698
Cdd:PRK11231 154 AQDTPVVLLDEPTTYLD--INHQVelMRLMRELntqgKTVVTVLHD---LNQASRYCDHLVVLANGHVMAQGT 221
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1279-1501 |
2.90e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 91.88 E-value: 2.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1279 VIIASCLRKEYAGKRkgcfskrknkiATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSG----- 1353
Cdd:PRK10895 3 TLTAKNLAKAYKGRR-----------VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDisllp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1354 -GGDALEFLGYCPQENALWPNLTVRQHL-EVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLS 1431
Cdd:PRK10895 72 lHARARRGIGYLPQEASIFRRLSVYDNLmAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1432 ILGNPSVVLLDEPSTGMDPEGQQQMWQAIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1501
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 ... |
1276-1500 |
3.26e-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: 3.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1276 EKPVIIASCLRKEYAGKRKGCFSkrknkiATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLK----- 1350
Cdd:TIGR03269 276 GEPIIKVRNVSKRYISVDRGVVK------AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgdew 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1351 -------GSGGGDALEFLGYCPQENALWPNLTVrqhLEVYAAVKGLRKGDaEVAITRLVDALKL----QDQLKSPVK--- 1416
Cdd:TIGR03269 350 vdmtkpgPDGRGRAKRYIGILHQEYDLYPHRTV---LDNLTEAIGLELPD-ELARMKAVITLKMvgfdEEKAEEILDkyp 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1417 -TLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1495
Cdd:TIGR03269 426 dELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGK 505
|
....*
gi 572882597 1496 LRCIG 1500
Cdd:TIGR03269 506 IVKIG 510
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
477-693 |
3.46e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 91.83 E-value: 3.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 477 KEAIRIRNVTKEYKGKpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGL-----SVPTKGSVTIYN-NKLSEM 550
Cdd:PRK14267 2 KFAIETVNLRVYYGSN----HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGrNIYSPD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 551 ADLENLSKLTGVCPQSNVQFDFLTVRENLRLFAKIKGI------LPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRK 624
Cdd:PRK14267 78 VDPIEVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLvkskkeLDERVEWALKKAALWDEVKDRLNDYPSNLSGGQRQR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 572882597 625 LTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEADILADRKVFLSQGKL 693
Cdd:PRK14267 158 LVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1305-1508 |
4.21e-20 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 96.37 E-value: 4.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1305 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsGGGDALEF--------LGYCPQeNALWPNLTV 1376
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILI---NGVDLSDLdpaswrrqIAWVPQ-NPYLFAGTI 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1377 RQHL----------EVYAAVKglrkgdaEVAITRLVDAlkLQDQLKSPV----KTLSEGIKRKLCFVLSILGNPSVVLLD 1442
Cdd:COG4988 428 RENLrlgrpdasdeELEAALE-------AAGLDEFVAA--LPDGLDTPLgeggRGLSGGQAQRLALARALLRDAPLLLLD 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 572882597 1443 EPSTGMDPEGQQQMWQAIRATFRNteRGALLTTHYMAEAEAvCDRVAIMVSGRLRCIGSIQHLKSK 1508
Cdd:COG4988 499 EPTAHLDAETEAEILQALRRLAKG--RTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1305-1496 |
4.50e-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: 4.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1305 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsGGGDALEF--------LGYCPQENALWpNLTV 1376
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLL---DGTDIRQLdpadlrrnIGYVPQDVTLF-YGTL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1377 RQHLEVyaavkglrkGDAEVAITRLVDALKLQ--DQL--KSPV----------KTLSEGIKRKLCFVLSILGNPSVVLLD 1442
Cdd:cd03245 95 RDNITL---------GAPLADDERILRAAELAgvTDFvnKHPNgldlqigergRGLSGGQRQAVALARALLNDPPILLLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 572882597 1443 EPSTGMDPEGQQQMWQAIRATFRntERGALLTTHYMAeAEAVCDRVAIMVSGRL 1496
Cdd:cd03245 166 EPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPS-LLDLVDRIIVMDSGRI 216
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1291-1496 |
4.84e-20 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 90.79 E-value: 4.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1291 GKRKGCF-SKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITG---DTKPTAGQVLLKGSgGGDALEFL---GY 1363
Cdd:cd03234 7 WDVGLKAkNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQ-PRKPDQFQkcvAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1364 CPQENALWPNLTVRQHLeVYAAVKGLRKGDAEVAITRLVDALKLQD----QLKSP-VKTLSEGIKRKLCFVLSILGNPSV 1438
Cdd:cd03234 86 VRQDDILLPGLTVRETL-TYTAILRLPRKSSDAIRKKRVEDVLLRDlaltRIGGNlVKGISGGERRRVSIAVQLLWDPKV 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 572882597 1439 VLLDEPSTGMDPEGQQQMWQAIRATFRnTERGALLTTHY-MAEAEAVCDRVAIMVSGRL 1496
Cdd:cd03234 165 LILDEPTSGLDSFTALNLVSTLSQLAR-RNRIVILTIHQpRSDLFRLFDRILLLSSGEI 222
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
480-712 |
5.23e-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: 5.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSeMADLENLSKL 559
Cdd:cd03252 1 ITFEHVRFRYK--PDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLA-LADPAWLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 TGVCPQSNVQFDfLTVRENLRLfakikgilpQEVDKEIQRVLLELEMKNIQDVLAQ--------------NLSGGQKRKL 625
Cdd:cd03252 78 VGVVLQENVLFN-RSIRDNIAL---------ADPGMSMERVIEAAKLAGAHDFISElpegydtivgeqgaGLSGGQRQRI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 626 TFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQFMdEADILADRKVFLSQGKLKCAGSSLFLKKK 705
Cdd:cd03252 148 AIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHDELLAE 226
|
....*..
gi 572882597 706 WGIGYHL 712
Cdd:cd03252 227 NGLYAYL 233
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
494-649 |
7.34e-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: 7.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 494 DKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADL--EN---LSKLTGVCPQsnv 568
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEphENilyLGHLPGLKPE--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 569 qfdfLTVRENLRLFAKIKGilpqEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLD 648
Cdd:TIGR01189 88 ----LSALENLHFWAAIHG----GAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
.
gi 572882597 649 P 649
Cdd:TIGR01189 160 K 160
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
504-678 |
7.68e-20 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 96.73 E-value: 7.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 504 FDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLsemaDLENLS--KLTGVCPQSnvqfdF-----LTVR 576
Cdd:NF033858 287 FRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV----DAGDIAtrRRVGYMSQA-----FslygeLTVR 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 577 ENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVW 656
Cdd:NF033858 358 QNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFW 437
|
170 180
....*....|....*....|....*
gi 572882597 657 NLLKE--RKtDRVILF-STQFMDEA 678
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 ... |
480-668 |
9.10e-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: 9.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEmADLENLSKL 559
Cdd:cd03246 1 LEVENVSFRYPG--AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQ-WDPNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 TGVCPQsnvqfdfltvreNLRLFAkikgilpqevdkeiqrvllelemkniqDVLAQN-LSGGQKRKLTFGIAILGDPQIF 638
Cdd:cd03246 78 VGYLPQ------------DDELFS---------------------------GSIAENiLSGGQRQRLGLARALYGNPRIL 118
|
170 180 190
....*....|....*....|....*....|...
gi 572882597 639 LLDEPTAGLDPFSRHQVWNL---LKERKTDRVI 668
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAiaaLKAAGATRIV 151
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
479-693 |
1.06e-19 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 90.58 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 479 AIRIRNVTKEYKGKpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTI------YNNKLSEMAD 552
Cdd:PRK11264 3 AIEVKNLVKKFHGQ----TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidTARSLSQQKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 553 L-ENLSKLTGVCPQSNVQFDFLTVRENLRLFAKI-KGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIA 630
Cdd:PRK11264 79 LiRQLRQHVGFVFQNFNLFPHRTVLENIIEGPVIvKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 572882597 631 ILGDPQIFLLDEPTAGLDPFSRHQVWNL---LKERKTDRVILfsTQFMDEADILADRKVFLSQGKL 693
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPELVGEVLNTirqLAQEKRTMVIV--THEMSFARDVADRAIFMDQGRI 222
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
479-688 |
1.23e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 90.48 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 479 AIRIRNVTKEYkgkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLS-----VPTKGSVTIYNNKLSEM-AD 552
Cdd:PRK14258 7 AIKVNNLSFYY----DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNeleseVRVEGRVEFFNQNIYERrVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 553 LENLSK-LTGVCPQSNVqFDfLTVRENLRLFAKIKGILPQ-EVDKEIQRVL----LELEMKNIQDVLAQNLSGGQKRKLT 626
Cdd:PRK14258 83 LNRLRRqVSMVHPKPNL-FP-MSVYDNVAYGVKIVGWRPKlEIDDIVESALkdadLWDEIKHKIHKSALDLSGGQQQRLC 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 572882597 627 FGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKER--KTDRVILFSTQFMDEADILADRKVFL 688
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrlRSELTMVIVSHNLHQVSRLSDFTAFF 224
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
483-661 |
1.55e-19 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 89.49 E-value: 1.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 483 RNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEM-----ADLENlS 557
Cdd:PRK11629 9 DNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaakAELRN-Q 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 558 KLTGVCPQSNVQFDFlTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQI 637
Cdd:PRK11629 88 KLGFIYQFHHLLPDF-TALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRL 166
|
170 180
....*....|....*....|....
gi 572882597 638 FLLDEPTAGLDPFSRHQVWNLLKE 661
Cdd:PRK11629 167 VLADEPTGNLDARNADSIFQLLGE 190
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1276-1500 |
2.22e-19 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 90.01 E-value: 2.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1276 EKPVIIASCLRKEYAGKRKGCFskrknkIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsGGG 1355
Cdd:cd03294 16 KAFKLLAKGKSKEEILKKTGQT------VGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLI---DGQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1356 DALEF------------LGYCPQENALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIK 1423
Cdd:cd03294 87 DIAAMsrkelrelrrkkISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQ 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 572882597 1424 RKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1500
Cdd:cd03294 167 QRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVG 243
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
457-712 |
2.47e-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: 2.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 457 MDADPSFHDSFEQAPPEFQGKeaIRIRNVTKEYKGKPDKiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPT 536
Cdd:TIGR00958 458 LDRKPNIPLTGTLAPLNLEGL--IEFQDVSFSYPNRPDV-PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPT 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 537 KGSVTIYNNKLSEMaDLENLSKLTGVCPQSNVQFDfLTVRENlrlfakIKGILPQEVDKEIQRVLLE-------LEMKNI 609
Cdd:TIGR00958 535 GGQVLLDGVPLVQY-DHHYLHRQVALVGQEPVLFS-GSVREN------IAYGLTDTPDEEIMAAAKAanahdfiMEFPNG 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 610 QDVL----AQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNlLKERKtDRVILFSTQFMDEADiLADRK 685
Cdd:TIGR00958 607 YDTEvgekGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE-SRSRA-SRTVLLIAHRLSTVE-RADQI 683
|
250 260
....*....|....*....|....*..
gi 572882597 686 VFLSQGKLKCAGSSLFLKKKWGIGYHL 712
Cdd:TIGR00958 684 LVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1305-1501 |
2.62e-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: 2.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1305 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsGGGDALEF------LGYCPQENALWPNLTVRQ 1378
Cdd:cd03296 17 ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILF---GGEDATDVpvqernVGFVFQHYALFRHMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1379 HLEVYAAVKGLRKGDAEVAITRLVDAL-------KLQDQLKSpvkTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1451
Cdd:cd03296 94 NVAFGLRVKPRSERPPEAEIRAKVHELlklvqldWLADRYPA---QLSGGQRQRVALARALAVEPKVLLLDEPFGALDAK 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 572882597 1452 GQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1501
Cdd:cd03296 171 VRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
479-698 |
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 572882597 479 AIRIRNVTKEYKGKPDKieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADlENLSK 558
Cdd:PRK11160 338 SLTLNNVSFTYPDQPQP--VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSE-AALRQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 559 LTGVCPQSNVQFDfLTVRENLRLfAKikgilPQEVDKEIQRVLLELEMKNiqdvLAQN--------------LSGGQKRK 624
Cdd:PRK11160 415 AISVVSQRVHLFS-ATLRDNLLL-AA-----PNASDEALIEVLQQVGLEK----LLEDdkglnawlgeggrqLSGGEQRR 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 625 LTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFST-------QFmdeadilaDRKVFLSQGKLKCAG 697
Cdd:PRK11160 484 LGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMIThrltgleQF--------DRICVMDNGQIIEQG 555
|
.
gi 572882597 698 S 698
Cdd:PRK11160 556 T 556
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1307-1495 |
3.49e-19 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 86.67 E-value: 3.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1307 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsGGGDALEF--------LGYCPQENALWpNLTVRQ 1378
Cdd:cd03228 19 KDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILI---DGVDLRDLdleslrknIAYVPQDPFLF-SGTIRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1379 HLevyaavkglrkgdaevaitrlvdalklqdqlkspvktLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQ 1458
Cdd:cd03228 95 NI-------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILE 137
|
170 180 190
....*....|....*....|....*....|....*..
gi 572882597 1459 AIRATFRNteRGALLTTHYMAEAEAvCDRVAIMVSGR 1495
Cdd:cd03228 138 ALRALAKG--KTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
480-698 |
3.55e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 89.41 E-value: 3.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKPDKIEaLKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLSKL 559
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYT-LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 TGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFL 639
Cdd:PRK13650 84 GMVFQNPDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 572882597 640 LDEPTAGLDPFSRHQVWNLLKERKTDR--VILFSTQFMDEAdILADRKVFLSQGKLKCAGS 698
Cdd:PRK13650 164 LDEATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDEV-ALSDRVLVMKNGQVESTST 223
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
479-684 |
5.46e-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: 5.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 479 AIRIRNVTKEYKGkpdkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLSK 558
Cdd:COG1129 4 LLEMRGISKSFGG----VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 559 LTGVCPQSNVQFDFLTVRENLRL--FAKIKGIL-PQEVDKEIQRVLLELEMkNIQ-DVLAQNLSGGQK------Rkltfg 628
Cdd:COG1129 80 GIAIIHQELNLVPNLSVAENIFLgrEPRRGGLIdWRAMRRRARELLARLGL-DIDpDTPVGDLSVAQQqlveiaR----- 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 572882597 629 iAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRV-ILFSTQFMDEADILADR 684
Cdd:COG1129 154 -ALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVaIIYISHRLDEVFEIADR 209
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
480-670 |
5.48e-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: 5.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGL---SVPTKGSVTIYNNKLSEMADlENL 556
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLlppPGITSGEILFDGEDLLKLSE-KEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 557 SKLTGvcpqSNVQFDF----------LTVRENLRLFAKIKGILP-QEVDKEIQRVLLELEMKNIQDVLAQ---NLSGGQK 622
Cdd:COG0444 81 RKIRG----REIQMIFqdpmtslnpvMTVGDQIAEPLRIHGGLSkAEARERAIELLERVGLPDPERRLDRyphELSGGMR 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 572882597 623 RKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILF 670
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 ... |
467-693 |
5.84e-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: 5.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 467 FEQAPPEFQGKEAIRIRNVTKEY----KGKpdkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTI 542
Cdd:TIGR03269 267 VEKECEVEVGEPIIKVRNVSKRYisvdRGV---VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNV 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 543 -YNNKLSEMADLENL-----SKLTGVCPQSNVQFDFLTVRENLrlfAKIKGI-LPQEVDKEIQRVLL------ELEMKNI 609
Cdd:TIGR03269 344 rVGDEWVDMTKPGPDgrgraKRYIGILHQEYDLYPHRTVLDNL---TEAIGLeLPDELARMKAVITLkmvgfdEEKAEEI 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 610 QDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWN-LLKERKT-DRVILFSTQFMDEADILADRKVF 687
Cdd:TIGR03269 421 LDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHsILKAREEmEQTFIIVSHDMDFVLDVCDRAAL 500
|
....*.
gi 572882597 688 LSQGKL 693
Cdd:TIGR03269 501 MRDGKI 506
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
470-698 |
6.40e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 89.91 E-value: 6.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 470 APPEFQGKEAIRIRNVTKEYKGK-PDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVT---IYNN 545
Cdd:PRK13631 12 VPNPLSDDIILRVKNLYCVFDEKqENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQvgdIYIG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 546 ------------KLSEMADLENLSKLTGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLElEMKNIQDVL 613
Cdd:PRK13631 92 dkknnhelitnpYSKKIKNFKELRRRVSMVFQFPEYQLFKDTIEKDIMFGPVALGVKKSEAKKLAKFYLN-KMGLDDSYL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 614 AQN---LSGGQKRKltfgIAILG----DPQIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRK 685
Cdd:PRK13631 171 ERSpfgLSGGQKRR----VAIAGilaiQPEILIFDEPTAGLDPKGEHEMMQLILDaKANNKTVFVITHTMEHVLEVADEV 246
|
250
....*....|...
gi 572882597 686 VFLSQGKLKCAGS 698
Cdd:PRK13631 247 IVMDKGKILKTGT 259
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
489-688 |
6.94e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 86.13 E-value: 6.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 489 YKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKlsEMADLENLSKLTGVCPqsnv 568
Cdd:NF040873 2 YGGRP----VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA--RVAYVPQRSEVPDSLP---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 569 qfdfLTVRE--NLRLFAKIKGILP------QEVDKEIQRV-LLELEMKNIQDvlaqnLSGGQKRKLTFGIAILGDPQIFL 639
Cdd:NF040873 72 ----LTVRDlvAMGRWARRGLWRRltrddrAAVDDALERVgLADLAGRQLGE-----LSGGQRQRALLAQGLAQEADLLL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 572882597 640 LDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEAdILADRKVFL 688
Cdd:NF040873 143 LDEPTTGLDAESRERIIALLAEeHARGATVVVVTHDLELV-RRADPCVLL 191
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1307-1496 |
8.75e-19 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 86.81 E-value: 8.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1307 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG---SGGGDALEFL----GYCPQENALWPNLTVRQH 1379
Cdd:cd03262 17 KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGlklTDDKKNINELrqkvGMVFQQFNLFPHLTVLEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1380 L-EVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEG------IKRKLCFvlsilgNPSVVLLDEPSTGMDPEG 1452
Cdd:cd03262 97 ItLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGqqqrvaIARALAM------NPKVMLFDEPTSALDPEL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 572882597 1453 QQQMWQAIRatfRNTERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1496
Cdd:cd03262 171 VGEVLDVMK---DLAEEGMtmVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1305-1530 |
9.72e-19 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 89.79 E-value: 9.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1305 ATRNVSFCVRKGEVLGLLGHNGAGKSTSiKVITGDTKPTAGQvllkgsgggDALEFLGYCPQENALW------------- 1371
Cdd:NF000106 28 AVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGR---------RPWRF*TWCANRRALRrtig*hrpvr*gr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1372 -PNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDP 1450
Cdd:NF000106 98 rESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1451 EGQQQMWQAIRATFRNTERgALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFGKDYLlemkvknlaQVEPLHA 1530
Cdd:NF000106 178 RTRNEVWDEVRSMVRDGAT-VLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGGRTL---------QIRPAHA 247
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
476-699 |
9.76e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 87.80 E-value: 9.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 476 GKEAIRIRNVTKEYKGKPDKiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGL------SVPTKGSVTIYNNKLSE 549
Cdd:PRK14246 4 GKSAEDVFNISRLYLYINDK-AILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydsKIKVDGKVLYFGKDIFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 550 MaDLENLSKLTGVCPQSNVQFDFLTVRENLRLFAKIKGILPQ-EVDKEIQRVLLELEM-KNIQDVL---AQNLSGGQKRK 624
Cdd:PRK14246 83 I-DAIKLRKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKrEIKKIVEECLRKVGLwKEVYDRLnspASQLSGGQQQR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 572882597 625 LTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGSS 699
Cdd:PRK14246 162 LTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSS 236
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
514-699 |
1.13e-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: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 514 ILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADlENLSklTGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEV 593
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPP-HLRH--INMVFQSYALFPHMTVEENVAFGLKMRKVPRAEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 594 DkeiQRVLLELEMKNIQDVLAQ---NLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLK--ERKTDRVI 668
Cdd:TIGR01187 78 K---PRVLEALRLVQLEEFADRkphQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKtiQEQLGITF 154
|
170 180 190
....*....|....*....|....*....|.
gi 572882597 669 LFSTQFMDEADILADRKVFLSQGKLKCAGSS 699
Cdd:TIGR01187 155 VFVTHDQEEAMTMSDRIAIMRKGKIAQIGTP 185
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
480-693 |
1.21e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 88.60 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEY-KGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVT-IYNN-------KLSEM 550
Cdd:PRK13651 3 IKVKNIVKIFnKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwIFKDeknkkktKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 551 ADLENLSKLT---------GVCPQSNVQFDFL-------TVRENLRLFAKIKGILPQEVDKeiqRVLLELEMKNIQDVLA 614
Cdd:PRK13651 83 VLEKLVIQKTrfkkikkikEIRRRVGVVFQFAeyqlfeqTIEKDIIFGPVSMGVSKEEAKK---RAAKYIELVGLDESYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 615 Q----NLSGGQKRKltfgIAILG----DPQIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRK 685
Cdd:PRK13651 160 QrspfELSGGQKRR----VALAGilamEPDFLVFDEPTAGLDPQGVKEILEIFDNlNKQGKTIILVTHDLDNVLEWTKRT 235
|
....*...
gi 572882597 686 VFLSQGKL 693
Cdd:PRK13651 236 IFFKDGKI 243
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1307-1501 |
1.26e-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: 1.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1307 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsGGGDALEF------LGYCPQENALWPNLTVRQHL 1380
Cdd:COG3839 20 KDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILI---GGRDVTDLppkdrnIAMVFQSYALYPHMTVYENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1381 EVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEG------IKRklcfvlSILGNPSVVLLDEPSTGMDPEGQQ 1454
Cdd:COG3839 97 AFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGqrqrvaLGR------ALVREPKVFLLDEPLSNLDAKLRV 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 572882597 1455 QMWQAIRATFRntERGA--LLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1501
Cdd:COG3839 171 EMRAEIKRLHR--RLGTttIYVTHDQVEAMTLADRIAVMNDGRIQQVGT 217
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
480-692 |
1.34e-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: 84.04 E-value: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNklsemadlenlskl 559
Cdd:cd03221 1 IELENLSKTYGGKL----LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST-------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 tgvcpqsnvqfdfltvrenlrlfAKIkGILPQevdkeiqrvllelemkniqdvlaqnLSGGQKRKLTFGIAILGDPQIFL 639
Cdd:cd03221 63 -----------------------VKI-GYFEQ-------------------------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 572882597 640 LDEPTAGLDPFSRHQVWNLLKE-RKTdrVILFS--TQFMDEadiLADRKVFLSQGK 692
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKEyPGT--VILVShdRYFLDQ---VATKIIELEDGK 144
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
479-691 |
1.56e-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: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 479 AIRIRNVTKEYKGKpdkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYN---NKLsEMADlen 555
Cdd:PRK11650 3 GLKLQAVRKSYDGK---TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGrvvNEL-EPAD--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 556 lskltgvcpqSNVQFDF--------LTVRENLRLFAKIKGILPQEVDKEIQRV--LLELEmkniqDVLA---QNLSGGQK 622
Cdd:PRK11650 76 ----------RDIAMVFqnyalyphMSVRENMAYGLKIRGMPKAEIEERVAEAarILELE-----PLLDrkpRELSGGQR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 572882597 623 RKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVwnLLKERKTDRVI----LFSTQFMDEADILADRKVFLSQG 691
Cdd:PRK11650 141 QRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQM--RLEIQRLHRRLkttsLYVTHDQVEAMTLADRVVVMNGG 211
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
498-689 |
1.70e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 87.14 E-value: 1.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 498 ALKDLVFDIYEGQITAILGHSGAGKSTLL---NILSGL--SVPTKGSVTIYNNKL-SEMADLENLSKLTGVCPQSNVQFD 571
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILrcfNRLNDLipGFRVEGKVTFHGKNLyAPDVDPVEVRRRIGMVFQKPNPFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 572 fLTVRENLRLFAKI---KGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLD 648
Cdd:PRK14243 105 -KSIYDNIAYGARIngyKGDMDELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALD 183
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 572882597 649 PFSRHQVWNLLKERKTDRVILFSTQFMDEADILADRKVFLS 689
Cdd:PRK14243 184 PISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFN 224
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1303-1496 |
1.91e-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: 1.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1303 KIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-----SGGGDALEF-LGYCP---QENALWPN 1373
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGkpvtrRSPRDAIRAgIAYVPedrKREGLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1374 LTVRQHLevyaavkglrkgdaevAITRLvdalklqdqlkspvktLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQ 1453
Cdd:cd03215 93 LSVAENI----------------ALSSL----------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 572882597 1454 QQMWQAIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1496
Cdd:cd03215 141 AEIYRLIRE-LADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1277-1444 |
2.61e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.51 E-value: 2.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1277 KPVIIASCLRKEYAGKrkgcfskrknKIAtRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsggGD 1356
Cdd:COG0488 313 KKVLELEGLSKSYGDK----------TLL-DDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-----GE 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1357 ALEfLGYCPQENA-LWPNLTVRQHLevyaavKGLRKGDAEVAITRLVDALKL-QDQLKSPVKTLSEGIKRKLCFVLSILG 1434
Cdd:COG0488 377 TVK-IGYFDQHQEeLDPDKTVLDEL------RDGAPGGTEQEVRGYLGRFLFsGDDAFKPVGVLSGGEKARLALAKLLLS 449
|
170
....*....|
gi 572882597 1435 NPSVVLLDEP 1444
Cdd:COG0488 450 PPNVLLLDEP 459
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1299-1503 |
2.88e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 86.36 E-value: 2.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1299 KRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGD--ALEF---LGYCPQENALWPN 1373
Cdd:PRK13548 11 RLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwsPAELarrRAVLPQHSSLSFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1374 LTVRQHLEVYAAVKGLRKGDAEVAIT---RLVDALKLQDqlkSPVKTLSEGIK------RKLCFVLSILGNPSVVLLDEP 1444
Cdd:PRK13548 91 FTVEEVVAMGRAPHGLSRAEDDALVAaalAQVDLAHLAG---RDYPQLSGGEQqrvqlaRVLAQLWEPDGPPRWLLLDEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 572882597 1445 STGMDPEGQQQMWQAIRAtfRNTERGA--------L-LTTHYmaeaeavCDRVAIMVSGRLRCIGSIQ 1503
Cdd:PRK13548 168 TSALDLAHQHHVLRLARQ--LAHERGLavivvlhdLnLAARY-------ADRIVLLHQGRLVADGTPA 226
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
480-701 |
3.02e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 86.69 E-value: 3.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKPDkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEmADLENLSKL 559
Cdd:PRK13642 5 LEVENLVFKYEKESD-VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTA-ENVWNLRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 TGVCPQS-NVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIF 638
Cdd:PRK13642 83 IGMVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 572882597 639 LLDEPTAGLDPFSRHQVWNLLKERKTDR--VILFSTQFMDEAdILADRKVFLSQGKL--KCAGSSLF 701
Cdd:PRK13642 163 ILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEA-ASSDRILVMKAGEIikEAAPSELF 228
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
481-684 |
3.19e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 89.97 E-value: 3.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 481 RIRNVTKEYKGkpdkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKL---SEMADLEnls 557
Cdd:PRK11288 6 SFDGIGKTFPG----VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfaSTTAALA--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 558 klTGVC---------PQsnvqfdfLTVRENLRLfakikGILPQE---VDKE--IQRVLLELE---MKNIQDVLAQNLSGG 620
Cdd:PRK11288 79 --AGVAiiyqelhlvPE-------MTVAENLYL-----GQLPHKggiVNRRllNYEAREQLEhlgVDIDPDTPLKYLSIG 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 572882597 621 QKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADR 684
Cdd:PRK11288 145 QRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRElRAEGRVILYVSHRMEEIFALCDA 209
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
479-693 |
3.24e-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: 3.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 479 AIRIRNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMaDLENLSK 558
Cdd:COG4181 8 IIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAL-DEDARAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 559 LTGvcpqSNVQFDF--------LTVRENlrlfakikgilpqevdkeiqrVLLELEMKNIQDVLAQ--------------- 615
Cdd:COG4181 87 LRA----RHVGFVFqsfqllptLTALEN---------------------VMLPLELAGRRDARARarallervglghrld 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 616 ----NLSGG-QKRkltfgIAI----LGDPQIFLLDEPTAGLDPFSRHQVWNLL----KERKTDRVILfsTQfmDEAdiLA 682
Cdd:COG4181 142 hypaQLSGGeQQR-----VALarafATEPAILFADEPTGNLDAATGEQIIDLLfelnRERGTTLVLV--TH--DPA--LA 210
|
250
....*....|....
gi 572882597 683 ---DRKVFLSQGKL 693
Cdd:COG4181 211 arcDRVLRLRAGRL 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
453-694 |
4.82e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.74 E-value: 4.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 453 LEDEMDADPSFHDSFEQAPPefQGKEAIRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGL 532
Cdd:COG0488 291 REEPPRRDKTVEIRFPPPER--LGKKVLELEGLSKSYGDKT----LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 533 SVPTKGSVTIYnnklsemadlENLSklTGVCPQSNVQFDF-LTVRENLRLFA------KIKGIL------PQEVDKEIQR 599
Cdd:COG0488 365 LEPDSGTVKLG----------ETVK--IGYFDQHQEELDPdKTVLDELRDGApggteqEVRGYLgrflfsGDDAFKPVGV 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 600 vllelemkniqdvlaqnLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERK-TdrVILFS--TQFMD 676
Cdd:COG0488 433 -----------------LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPgT--VLLVShdRYFLD 493
|
250
....*....|....*...
gi 572882597 677 EadiLADRKVFLSQGKLK 694
Cdd:COG0488 494 R---VATRILEFEDGGVR 508
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
476-693 |
5.60e-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: 5.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 476 GKEAIRIRNVTKEYkgkpdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSemadlen 555
Cdd:cd03215 1 GEPVLEVRGLSVKG--------AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVT------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 556 lskltgvcpqsnvqfdFLTVRENLRLfakikGI--LPqevdKEIQRVLLELEM---KNIqdVLAQNLSGGQKRKLTFGIA 630
Cdd:cd03215 66 ----------------RRSPRDAIRA-----GIayVP----EDRKREGLVLDLsvaENI--ALSSLLSGGNQQKVVLARW 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 572882597 631 ILGDPQIFLLDEPTAGLDPFSRHQVWNLLKErKTDR---VILFSTQfMDEADILADRKVFLSQGKL 693
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 ... |
1307-1496 |
6.07e-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: 6.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1307 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDAL-EFLGYCPQENALWPNlTVRQHLe 1381
Cdd:cd03246 19 RNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGadisQWDPNELgDHVGYLPQDDELFSG-SIAENI- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1382 vyaavkglrkgdaevaitrlvdalklqdqlkspvktLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIR 1461
Cdd:cd03246 97 ------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIA 140
|
170 180 190
....*....|....*....|....*....|....*..
gi 572882597 1462 ATfrnTERGA--LLTTHYMaEAEAVCDRVAIMVSGRL 1496
Cdd:cd03246 141 AL---KAAGAtrIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1305-1514 |
6.94e-18 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 87.58 E-value: 6.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1305 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGggdalefLGYCP----------QENALWPNL 1374
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVD-------LSHVPpyqrpinmmfQSYALFPHM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1375 TVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQ 1454
Cdd:PRK11607 107 TVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 572882597 1455 QMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS----IQHLKSKFGKDYL 1514
Cdd:PRK11607 187 RMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEpeeiYEHPTTRYSAEFI 250
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
480-698 |
1.09e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 85.24 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKpdkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEmADLENLSKL 559
Cdd:PRK13652 4 IETRDLCYSYSGS---KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITK-ENIREVRKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 TGVCPQSNVQFDFLTVRENLRLFAKIK-GILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIF 638
Cdd:PRK13652 80 VGLVFQNPDDQIFSPTVEQDIAFGPINlGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 572882597 639 LLDEPTAGLDPFSRHQVW---NLLKERKTDRVIlFSTQFMDEADILADRKVFLSQGKLKCAGS 698
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIdflNDLPETYGMTVI-FSTHQLDLVPEMADYIYVMDKGRIVAYGT 221
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
483-691 |
1.16e-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: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 483 RNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSG---LSVPTKGSVTIYNNKLSemadlENLSKL 559
Cdd:TIGR00956 763 RNLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAErvtTGVITGGDRLVNGRPLD-----SSFQRS 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 TGVCPQSNVQFDFLTVRENLRLFAKIKgiLPQEVDKE-----IQRVLLELEMKNIQD----VLAQNLSGGQKRKLTFGIA 630
Cdd:TIGR00956 838 IGYVQQQDLHLPTSTVRESLRFSAYLR--QPKSVSKSekmeyVEEVIKLLEMESYADavvgVPGEGLNVEQRKRLTIGVE 915
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 572882597 631 ILGDPQIFL-LDEPTAGLDPFSRHQVWNLLKE-RKTDRVILfSTQFMDEADILA--DRKVFLSQG 691
Cdd:TIGR00956 916 LVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKlADHGQAIL-CTIHQPSAILFEefDRLLLLQKG 979
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1298-1451 |
1.41e-17 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 83.56 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1298 SKR--KNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDALEFL----GYCPQE 1367
Cdd:COG2884 8 SKRypGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdlsRLKRREIPYLrrriGVVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1368 NALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTG 1447
Cdd:COG2884 88 FRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGN 167
|
....
gi 572882597 1448 MDPE 1451
Cdd:COG2884 168 LDPE 171
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1297-1501 |
1.79e-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: 1.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1297 FSKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsGGGDALEF--------LGYCPQEN 1368
Cdd:cd03295 8 KRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFI---DGEDIREQdpvelrrkIGYVIQQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1369 ALWPNLTVRQHLevyAAVKGLRKGDAEVAITRLVDALKLQDQlkSPVK-------TLSEGIKRKLCFVLSILGNPSVVLL 1441
Cdd:cd03295 85 GLFPHMTVEENI---ALVPKLLKWPKEKIRERADELLALVGL--DPAEfadryphELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1442 DEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1501
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGT 219
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1305-1496 |
3.28e-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: 3.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1305 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKP---TAGQVLLKG----SGGGDALE-----FLGYCPQE--NAL 1370
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGedllKLSEKELRkirgrEIQMIFQDpmTSL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1371 WPNLTVRQHL-EVYAAVKGLRKGDAEvaiTRLVDALKLQdQLKSPVKT-------LSEGIKRKLCFVLSILGNPSVVLLD 1442
Cdd:COG0444 100 NPVMTVGDQIaEPLRIHGGLSKAEAR---ERAIELLERV-GLPDPERRldrypheLSGGMRQRVMIARALALEPKLLIAD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 572882597 1443 EPSTGMDPEGQQQmwqaIRATFR--NTERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1496
Cdd:COG0444 176 EPTTALDVTIQAQ----ILNLLKdlQRELGLaiLFITHDLGVVAEIADRVAVMYAGRI 229
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
498-698 |
3.33e-17 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 85.86 E-value: 3.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 498 ALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLS---KLTGVCPQSNVQFDFLT 574
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 575 VRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQ 654
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 572882597 655 VWN-LLK-ERKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS 698
Cdd:PRK10070 203 MQDeLVKlQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGT 248
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1309-1500 |
3.99e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 85.66 E-value: 3.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1309 VSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsgGGDALEFL---------GYCPQENALWPNLTVRQ- 1378
Cdd:PRK09536 22 VDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLV----AGDDVEALsaraasrrvASVPQDTSLSFEFDVRQv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1379 -------HLEVYAAVKGLRKGDAEVAITRlVDALKLQDQlksPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1451
Cdd:PRK09536 98 vemgrtpHRSRFDTWTETDRAAVERAMER-TGVAQFADR---PVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDIN 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 572882597 1452 GQQQMWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1500
Cdd:PRK09536 174 HQVRTLELVR-RLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
225-418 |
5.38e-17 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.
Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 84.36 E-value: 5.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 225 YLFSCIISFSSFIYYASV--NVTRER-KRMKALMTMMGLRDSAFWLSWGLLYAGFIFIMALFLALVIRSTqFIILSGFMV 301
Cdd:pfam12698 162 YLVGLILMIIILIGAAIIavSIVEEKeSRIKERLLVSGVSPLQYWLGKILGDFLVGLLQLLIILLLLFGI-GIPFGNLGL 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 302 VFSLFLLYGLSLVALAFLMSILVKKSFLTGLVVFLLT-VFWGCLGFTSLYRHLPASLEWILSLLSPFAFMLGMAQLLHld 380
Cdd:pfam12698 241 LLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVIlLLSGFFGGLFPLEDPPSFLQWIFSIIPFFSPIDGLLRLIY-- 318
|
170 180 190
....*....|....*....|....*....|....*...
gi 572882597 381 YDLNSNAFPhpsdgsNLIvatnfMLAFDTCLYLALAIY 418
Cdd:pfam12698 319 GDSLWEIAP------SLI-----ILLLFAVVLLLLALL 345
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
482-661 |
5.56e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 86.70 E-value: 5.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 482 IRNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMaDLENLSKLT- 560
Cdd:PRK10535 7 LKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATL-DADALAQLRr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 561 ---GVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQI 637
Cdd:PRK10535 86 ehfGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQV 165
|
170 180
....*....|....*....|....
gi 572882597 638 FLLDEPTAGLDPFSRHQVWNLLKE 661
Cdd:PRK10535 166 ILADEPTGALDSHSGEEVMAILHQ 189
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1269-1494 |
5.79e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 86.26 E-value: 5.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1269 LNSTNFDEKPVIIASCLRKEYAGKR--KGcfskrknkiatrnVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQ 1346
Cdd:PRK15439 1 MQTSDTTAPPLLCARSISKQYSGVEvlKG-------------IDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1347 VLLKGS-----GGGDALEFLGY-CPQENALWPNLTVRQHLEVyaavkGL-RKGDAEVAITRLVDALKLQDQLKSPVKTLs 1419
Cdd:PRK15439 68 LEIGGNpcarlTPAKAHQLGIYlVPQEPLLFPNLSVKENILF-----GLpKRQASMQKMKQLLAALGCQLDLDSSAGSL- 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 572882597 1420 EGIKRKLCFVL-SILGNPSVVLLDEPSTGMDPEGQQQMWQAIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSG 1494
Cdd:PRK15439 142 EVADRQIVEILrGLMRDSRILILDEPTASLTPAETERLFSRIRE-LLAQGVGIVFISHKLPEIRQLADRISVMRDG 216
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1307-1496 |
6.59e-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: 6.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1307 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-----SGGGDALEF-LGYCP---QENALWPNLTVR 1377
Cdd:COG1129 269 RDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpvriRSPRDAIRAgIAYVPedrKGEGLVLDLSIR 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1378 Q-----HLEVYAAVKGLRKGDAEVAITRLVDALKL----QDQlksPVKTLSEGIKRKLcfVLS--ILGNPSVVLLDEPST 1446
Cdd:COG1129 349 EnitlaSLDRLSRGGLLDRRRERALAEEYIKRLRIktpsPEQ---PVGNLSGGNQQKV--VLAkwLATDPKVLILDEPTR 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 572882597 1447 GMDPEGQQQMWQAIRatfRNTERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1496
Cdd:COG1129 424 GIDVGAKAEIYRLIR---ELAAEGKavIVISSELPELLGLSDRILVMREGRI 472
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
480-669 |
9.83e-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: 9.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMaDLENLSKL 559
Cdd:cd03369 7 IEVENLSVRYA--PDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTI-PLEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 TGVCPQSNVQFDFlTVRENLRLFAKIKgilpqevDKEIQRVLLELEMKNiqdvlaqNLSGGQKRKLTFGIAILGDPQIFL 639
Cdd:cd03369 84 LTIIPQDPTLFSG-TIRSNLDPFDEYS-------DEEIYGALRVSEGGL-------NLSQGQRQLLCLARALLKRPRVLV 148
|
170 180 190
....*....|....*....|....*....|
gi 572882597 640 LDEPTAGLDPFSRHQVWNLLKERKTDRVIL 669
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) ... |
1313-1488 |
1.07e-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: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1313 VRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsgggdALEFLGYCPQENALWPNLTVRQHLevYAAVKGlrKG 1392
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI-------ELDTVSYKPQYIKADYEGTVRDLL--SSITKD--FY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1393 DAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGAL 1472
Cdd:cd03237 91 THPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAF 170
|
170
....*....|....*.
gi 572882597 1473 LTTHYMAEAEAVCDRV 1488
Cdd:cd03237 171 VVEHDIIMIDYLADRL 186
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
486-648 |
1.12e-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: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 486 TKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADlENLSKLTGVCPQ 565
Cdd:cd03231 3 ADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD-SIARGLLYLGHA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 566 SNVQfDFLTVRENLRLFAKIKGilpqevDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTA 645
Cdd:cd03231 82 PGIK-TTLSVLENLRFWHADHS------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
...
gi 572882597 646 GLD 648
Cdd:cd03231 155 ALD 157
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
480-679 |
1.13e-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: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKPDKIE-ALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNklsemadlenlsk 558
Cdd:cd03250 1 ISVEDASFTWDSGEQETSfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 559 lTGVCPQSN-VQFDflTVRENLrLFAKikgilpqEVDKE-IQRVL----LELEMKN----IQDVLAQ---NLSGGQKRKL 625
Cdd:cd03250 68 -IAYVSQEPwIQNG--TIRENI-LFGK-------PFDEErYEKVIkacaLEPDLEIlpdgDLTEIGEkgiNLSGGQKQRI 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 572882597 626 TFGIAILGDPQIFLLDEPTAGLDPFSRHQVWN-----LLKERKTdrVILF--STQFMDEAD 679
Cdd:cd03250 137 SLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncilgLLLNNKT--RILVthQLQLLPHAD 195
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1305-1496 |
1.24e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 84.96 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1305 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-----SGGGDALEfLG----YcpQENALWPNLT 1375
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGqemrfASTTAALA-AGvaiiY--QELHLVPEMT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1376 VRQ-----HLEVYAAVkgLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDP 1450
Cdd:PRK11288 96 VAEnlylgQLPHKGGI--VNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 572882597 1451 EGQQQMWQAIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1496
Cdd:PRK11288 174 REIEQLFRVIRE-LRAEGRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
482-693 |
1.45e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 81.26 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 482 IRNVTKEYKGKpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVtiynnklsemadlenlskLTG 561
Cdd:PRK11247 15 LNAVSKRYGER----TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL------------------LAG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 562 VCPQSNvqfdfltVRENLRLFAKIKGILPQEvdKEIQRVLLELEMK---NIQDVLAQ------------NLSGGQKRKLT 626
Cdd:PRK11247 73 TAPLAE-------AREDTRLMFQDARLLPWK--KVIDNVGLGLKGQwrdAALQALAAvgladranewpaALSGGQKQRVA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 572882597 627 FGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGKL 693
Cdd:PRK11247 144 LARALIHRPGLLLLDEPLGALDALTRIEMQDLIESlwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1309-1476 |
1.47e-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: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1309 VSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDAL----EFLGYCPQENALWPNLTVRQHLEVYA 1384
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRdsiaRGLLYLGHAPGIKTTLSVLENLRFWH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1385 AV---KGLRKGDAEVAITRLVDAlklqdqlksPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIR 1461
Cdd:cd03231 99 ADhsdEQVEEALARVGLNGFEDR---------PVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMA 169
|
170
....*....|....*..
gi 572882597 1462 AtfrNTERG--ALLTTH 1476
Cdd:cd03231 170 G---HCARGgmVVLTTH 183
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1299-1503 |
1.50e-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: 1.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1299 KRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsgGGDALEflGYCPQENALwpNLTV-R 1377
Cdd:COG4559 10 RLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRL----NGRPLA--AWSPWELAR--RRAVlP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1378 QH---------LEVYA--AVKGLRKGDAEVAITR----LVDALKLQDQLkspVKTLSEGIK------RKLCFVL-SILGN 1435
Cdd:COG4559 82 QHsslafpftvEEVVAlgRAPHGSSAAQDRQIVRealaLVGLAHLAGRS---YQTLSGGEQqrvqlaRVLAQLWePVDGG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 572882597 1436 PSVVLLDEPSTGMDPEGQQQMWQAIRatfRNTERGA--------L-LTTHYmaeaeavCDRVAIMVSGRLRCIGSIQ 1503
Cdd:COG4559 159 PRWLFLDEPTSALDLAHQHAVLRLAR---QLARRGGgvvavlhdLnLAAQY-------ADRILLLHQGRLVAQGTPE 225
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1303-1502 |
1.63e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 82.02 E-value: 1.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1303 KIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG---SGGGDALEFL----GYCPQ--ENALWPN 1373
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvdiTDKKVKLSDIrkkvGLVFQypEYQLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1374 lTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQL---KSPVKtLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDP 1450
Cdd:PRK13637 100 -TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEDykdKSPFE-LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 572882597 1451 EGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSI 1502
Cdd:PRK13637 178 KGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
497-712 |
2.35e-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: 2.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 497 EALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIyNNKLSEMADLENLSKLTGVCPQSNVQFDFlTVR 576
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILL-NGFSLKDIDRHTLRQFINYLPQEPYIFSG-SIL 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 577 ENLRLFAKiKGILPQEVDKEIQRVLLELEMKNIQ-------DVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDP 649
Cdd:TIGR01193 566 ENLLLGAK-ENVSQDEIWAACEIAEIKDDIENMPlgyqtelSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDT 644
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 572882597 650 FSRHQ-VWNLLKerKTDRVILFSTQFMDEADiLADRKVFLSQGKLKCAGSSLFLKKKWGIGYHL 712
Cdd:TIGR01193 645 ITEKKiVNNLLN--LQDKTIIFVAHRLSVAK-QSDKIIVLDHGKIIEQGSHDELLDRNGFYASL 705
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
492-661 |
2.39e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 84.51 E-value: 2.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 492 KPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLsVPTKGSVTIYNNKLSEMaDLE----NLSKLtGVCPQsn 567
Cdd:PRK11174 359 SPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELREL-DPEswrkHLSWV-GQNPQ-- 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 568 vqfdfL---TVRENLRLfAKikgilPQEVDKEIQRVLlelEMKNIQDVLAQ--------------NLSGGQKRKLTFGIA 630
Cdd:PRK11174 434 -----LphgTLRDNVLL-GN-----PDASDEQLQQAL---ENAWVSEFLPLlpqgldtpigdqaaGLSVGQAQRLALARA 499
|
170 180 190
....*....|....*....|....*....|.
gi 572882597 631 ILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE 661
Cdd:PRK11174 500 LLQPCQLLLLDEPTASLDAHSEQLVMQALNA 530
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1300-1496 |
2.47e-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: 2.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1300 RKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITG-----DTKPTAGQVLLKG----SGGGDALEF---LGYCPQE 1367
Cdd:cd03260 10 YGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGkdiyDLDVDVLELrrrVGMVFQK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1368 NALWPnLTVRQHLEVYAAVKGLRKGDAEVAITRlvDALK---LQDQLKSPVK--TLSEGIKRKLCFVLSILGNPSVVLLD 1442
Cdd:cd03260 90 PNPFP-GSIYDNVAYGLRLHGIKLKEELDERVE--EALRkaaLWDEVKDRLHalGLSGGQQQRLCLARALANEPEVLLLD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 572882597 1443 EPSTGMDPEGQQQMWQAIRATfrNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1496
Cdd:cd03260 167 EPTSALDPISTAKIEELIAEL--KKEYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
504-693 |
2.49e-16 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 80.01 E-value: 2.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 504 FDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLEN-LSKLTgvcpQSNVQFDFLTVRENLRLf 582
Cdd:PRK10771 20 LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRpVSMLF----QENNLFSHLTVAQNIGL- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 583 akikGILP---------QEVDKEIQRVLLElemkNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRH 653
Cdd:PRK10771 95 ----GLNPglklnaaqrEKLHAIARQMGIE----DLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQ 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 572882597 654 QVWNLLKERKTDRVI--LFSTQFMDEADILADRKVFLSQGKL 693
Cdd:PRK10771 167 EMLTLVSQVCQERQLtlLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1313-1496 |
3.07e-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: 3.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1313 VRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDA--------LEFlgycpQENALWPNLTVRQHLEVyA 1384
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAppadrpvsMLF-----QENNLFAHLTVEQNVGL-G 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1385 AVKGLR-----KGDAEVAITRLvdalKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQA 1459
Cdd:cd03298 95 LSPGLKltaedRQAIEVALARV----GLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 572882597 1460 IRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1496
Cdd:cd03298 171 VLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
480-698 |
3.28e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 81.21 E-value: 3.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGK-PDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNK----LSEMADLE 554
Cdd:PRK13645 7 IILDNVSYTYAKKtPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAipanLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 555 NLSKLTGVCPQ-SNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKniQDVLAQN---LSGGQKRKLTFGIA 630
Cdd:PRK13645 87 RLRKEIGLVFQfPEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLP--EDYVKRSpfeLSGGQKRRVALAGI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 572882597 631 ILGDPQIFLLDEPTAGLDPFSRHQVWNL---LKERKTDRVILFsTQFMDEADILADRKVFLSQGKLKCAGS 698
Cdd:PRK13645 165 IAMDGNTLVLDEPTGGLDPKGEEDFINLferLNKEYKKRIIMV-THNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1308-1494 |
3.28e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 80.16 E-value: 3.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1308 NVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKgsgggDALEfLGYCPQENALWPN--LTVRQHLEVYAA 1385
Cdd:PRK09544 22 DVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRN-----GKLR-IGYVPQKLYLDTTlpLTVNRFLRLRPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1386 VKglrKGDAEVAITRlVDALKLQDQlksPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFR 1465
Cdd:PRK09544 96 TK---KEDILPALKR-VQAGHLIDA---PMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRR 168
|
170 180 190
....*....|....*....|....*....|....
gi 572882597 1466 NTERGALLTTH----YMAEA-EAVCDRVAIMVSG 1494
Cdd:PRK09544 169 ELDCAVLMVSHdlhlVMAKTdEVLCLNHHICCSG 202
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1307-1476 |
3.85e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 78.69 E-value: 3.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1307 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDALEFLGYCPQENALWPNLTVRQHLEV 1382
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGepirRQRDEYHQDLLYLGHQPGIKTELTALENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1383 YAAVKGLrkGDAEVAITRLvDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRA 1462
Cdd:PRK13538 98 YQRLHGP--GDDEALWEAL-AQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQ 174
|
170
....*....|....*.
gi 572882597 1463 tfrNTERG--ALLTTH 1476
Cdd:PRK13538 175 ---HAEQGgmVILTTH 187
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1305-1451 |
4.24e-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: 4.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1305 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSG----GGDALEFL----GYCPQENALWPNLTV 1376
Cdd:cd03292 16 ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDvsdlRGRAIPYLrrkiGVVFQDFRLLPDRNV 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 572882597 1377 RQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1451
Cdd:cd03292 96 YENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPD 170
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1307-1444 |
4.79e-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: 4.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1307 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSgggdalEFLGYCPQENALWPNLTVRQ-----HLE 1381
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG------LRIGYLPQEPPLDDDLTVLDtvldgDAE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1382 VYAAVKGLRKG---------------------------DAEVAITRLVDALKL-QDQLKSPVKTLSEGIKRK--LCFVLs 1431
Cdd:COG0488 89 LRALEAELEELeaklaepdedlerlaelqeefealggwEAEARAEEILSGLGFpEEDLDRPVSELSGGWRRRvaLARAL- 167
|
170
....*....|...
gi 572882597 1432 iLGNPSVVLLDEP 1444
Cdd:COG0488 168 -LSEPDLLLLDEP 179
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
480-698 |
6.73e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.79 E-value: 6.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGkpdkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMAdlENLSKL 559
Cdd:PRK15439 12 LCARSISKQYSG----VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT--PAKAHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 TGV--CPQSNVQFDFLTVRENLrLFAKIKgilPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQI 637
Cdd:PRK15439 86 LGIylVPQEPLLFPNLSVKENI-LFGLPK---RQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 572882597 638 FLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGS 698
Cdd:PRK15439 162 LILDEPTASLTPAETERLFSRIRElLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGK 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
482-694 |
7.95e-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: 7.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 482 IRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKlsemadlenlsKLtG 561
Cdd:COG0488 1 LENLSKSFGGRP----LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL-----------RI-G 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 562 VCPQSNVQFDFLTVREN-LRLFAKIKGIL------------PQEVDKEIQRVLLELEMKN-------IQDVLAQ------ 615
Cdd:COG0488 65 YLPQEPPLDDDLTVLDTvLDGDAELRALEaeleeleaklaePDEDLERLAELQEEFEALGgweaearAEEILSGlgfpee 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 616 -------NLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHqvW--NLLKERKT-------DRVilfstqFMDEad 679
Cdd:COG0488 145 dldrpvsELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIE--WleEFLKNYPGtvlvvshDRY------FLDR-- 214
|
250
....*....|....*
gi 572882597 680 iLADRKVFLSQGKLK 694
Cdd:COG0488 215 -VATRILELDRGKLT 228
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1310-1505 |
1.04e-15 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 78.26 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1310 SFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSgggdalEFLGYCP---------QENALWPNLTVRQHl 1380
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQ------DLTALPPaerpvsmlfQENNLFPHLTVAQN- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1381 eVYAAVK-GLRKGDAEVAitRLVDALK---LQDQLKSPVKTLSEG------IKRklCFVLsilGNPsVVLLDEPSTGMDP 1450
Cdd:COG3840 92 -IGLGLRpGLKLTAEQRA--QVEQALErvgLAGLLDRLPGQLSGGqrqrvaLAR--CLVR---KRP-ILLLDEPFSALDP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 572882597 1451 EGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL 1505
Cdd:COG3840 163 ALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAAL 217
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1301-1496 |
1.40e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 78.98 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1301 KNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDaleflgycpqENALWpnlTVRQHL 1380
Cdd:PRK13633 21 TEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSD----------EENLW---DIRNKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1381 ---------EVYAAVKglrkgDAEVAI-------------TRLVDALK---LQDQLKSPVKTLSEGIKRKLCFVLSILGN 1435
Cdd:PRK13633 88 gmvfqnpdnQIVATIV-----EEDVAFgpenlgippeeirERVDESLKkvgMYEYRRHAPHLLSGGQKQRVAIAGILAMR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 572882597 1436 PSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAeAVCDRVAIMVSGRL 1496
Cdd:PRK13633 163 PECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEA-VEADRIIVMDSGKV 222
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1308-1508 |
1.41e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 79.01 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1308 NVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGsgggDALeflgycpQENALWpnlTVRQHLE------ 1381
Cdd:PRK13650 25 DVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG----DLL-------TEENVW---DIRHKIGmvfqnp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1382 ----VYAAVK-----GLR-KG-DAEVAITRLVDALKL---QD-QLKSPVKtLSEGIKRKLCFVLSILGNPSVVLLDEPST 1446
Cdd:PRK13650 91 dnqfVGATVEddvafGLEnKGiPHEEMKERVNEALELvgmQDfKEREPAR-LSGGQKQRVAIAGAVAMRPKIIILDEATS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 572882597 1447 GMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAeAVCDRVAIMVSGRLRCIGSIQHLKSK 1508
Cdd:PRK13650 170 MLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1305-1514 |
1.47e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 82.48 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1305 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQ--VLlkgsgGGD--------------AleflgYCPQ-- 1366
Cdd:NF033858 16 ALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRveVL-----GGDmadarhrravcpriA-----YMPQgl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1367 -ENaLWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRK--LCFVLsiLGNPSVVLLDE 1443
Cdd:NF033858 86 gKN-LYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKlgLCCAL--IHDPDLLILDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 572882597 1444 PSTGMDPEGQQQMWQ---AIRAtfrntERGA---LLTTHYMAEAEAvCDRVAIMVSGRLRCIGSIQHLKSKFGKDYL 1514
Cdd:NF033858 163 PTTGVDPLSRRQFWElidRIRA-----ERPGmsvLVATAYMEEAER-FDWLVAMDAGRVLATGTPAELLARTGADTL 233
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
479-693 |
1.61e-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: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 479 AIRIRNVTKEYKGkpdkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLsemadlenlsK 558
Cdd:COG3845 5 ALELRGITKRFGG----VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV----------R 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 559 LT----------GVCPQSNVQFDFLTVRENLRLFAKIKGIL---PQEVDKEIQRVL----LELEMkniqDVLAQNLSGGQ 621
Cdd:COG3845 71 IRsprdaialgiGMVHQHFMLVPNLTVAENIVLGLEPTKGGrldRKAARARIRELSerygLDVDP----DAKVEDLSVGE 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 572882597 622 KRKLTfgI--AILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKL 693
Cdd:COG3845 147 QQRVE--IlkALYRGARILILDEPTAVLTPQEADELFEILRRlAAEGKSIIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1308-1496 |
1.61e-15 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 77.75 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1308 NVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGS--------GGGDALEF---LGYCPQENALWPNLTV 1376
Cdd:COG4161 20 DINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdfsqkpSEKAIRLLrqkVGMVFQQYNLWPHLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1377 RQHL-EVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQ 1455
Cdd:COG4161 100 MENLiEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQ 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 572882597 1456 MWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1496
Cdd:COG4161 180 VVEIIR-ELSQTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1301-1496 |
1.80e-15 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 76.20 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1301 KNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG---SGGGDAL-EFLGYCPQENALWpNLTV 1376
Cdd:cd03247 13 QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGvpvSDLEKALsSLISVLNQRPYLF-DTTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1377 RQHLevyaavkGLRkgdaevaitrlvdalklqdqlkspvktLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQM 1456
Cdd:cd03247 92 RNNL-------GRR---------------------------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQL 137
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 572882597 1457 WQAIRATFRNteRGALLTTHYMAEAEAVcDRVAIMVSGRL 1496
Cdd:cd03247 138 LSLIFEVLKD--KTLIWITHHLTGIEHM-DKILFLENGKI 174
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
494-648 |
1.81e-15 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 82.59 E-value: 1.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 494 DKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVP--TKGSVTIYNNKLSEmadlENLSKLTGVCPQSNVQFD 571
Cdd:PLN03140 891 DRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISGFPKKQ----ETFARISGYCEQNDIHSP 966
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 572 FLTVRENLRLFAKIKgiLPQEVDKE-----IQRVLLELEMKNIQDVLA-----QNLSGGQKRKLTFGIAILGDPQIFLLD 641
Cdd:PLN03140 967 QVTVRESLIYSAFLR--LPKEVSKEekmmfVDEVMELVELDNLKDAIVglpgvTGLSTEQRKRLTIAVELVANPSIIFMD 1044
|
....*..
gi 572882597 642 EPTAGLD 648
Cdd:PLN03140 1045 EPTSGLD 1051
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1297-1510 |
1.81e-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: 1.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1297 FSKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDA-----LEFLGYCPQENALW 1371
Cdd:cd03254 10 FSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIsrkslRSMIGVVLQDTFLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1372 PNlTVRQHL----------EVYAAVKglrkgdaEVAITRLVDALK--LQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVV 1439
Cdd:cd03254 90 SG-TIMENIrlgrpnatdeEVIEAAK-------EAGAHDFIMKLPngYDTVLGENGGNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 572882597 1440 LLDEPSTGMDPEGQQQMWQAIRATFRNteRGALLTTHYMAEAEAVcDRVAIMVSGRLRCIGSIQHLKSKFG 1510
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKLMKG--RTSIIIAHRLSTIKNA-DKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1292-1548 |
1.85e-15 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 81.48 E-value: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1292 KRKGCFSKRKN---KIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDALeflgycpqEN 1368
Cdd:PRK13545 23 KLKDLFFRSKDgeyHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAI--------SS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1369 ALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGM 1448
Cdd:PRK13545 95 GLNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1449 DPEGQQQMWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFGkDYLLEMKVKNLAQVEPL 1528
Cdd:PRK13545 175 DQTFTKKCLDKMN-EFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYD-EFLKKYNQMSVEERKDF 252
|
250 260
....*....|....*....|
gi 572882597 1529 HAEILRLFPQAARQERYSSL 1548
Cdd:PRK13545 253 REEQISQFQHGLLQEDQTGR 272
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1302-1495 |
2.04e-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: 77.61 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1302 NKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDALEFL----GYCPQENALWPN 1373
Cdd:cd03256 13 GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGtdinKLKGKALRQLrrqiGMIFQQFNLIER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1374 LTVRQH-----LEVYAAVKGLR----KGDAEVAItRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEP 1444
Cdd:cd03256 93 LSVLENvlsgrLGRRSTWRSLFglfpKEEKQRAL-AALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 572882597 1445 STGMDPEGQQQMWQAIRATfrNTERG--ALLTTHYMAEAEAVCDRVAIMVSGR 1495
Cdd:cd03256 172 VASLDPASSRQVMDLLKRI--NREEGitVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
497-697 |
2.46e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 77.70 E-value: 2.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 497 EALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLS---------EMADLENL----SKLTGVC 563
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlKVADKNQLrllrTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 564 PQSNVqFDFLTVREN-LRLFAKIKGILPQEVDKEIQRVLLELEM-KNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLD 641
Cdd:PRK10619 99 QHFNL-WSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIdERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 642 EPTAGLDPFSRHQVWNLLK----ERKTDRVIlfsTQFMDEADILADRKVFLSQGKLKCAG 697
Cdd:PRK10619 178 EPTSALDPELVGEVLRIMQqlaeEGKTMVVV---THEMGFARHVSSHVIFLHQGKIEEEG 234
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
480-693 |
2.66e-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: 2.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYK-----GKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMA--- 551
Cdd:TIGR02769 3 LEVRDVTHTYRtgglfGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 552 ------DLENLSK--LTGVCPQSNVQFdflTVRENLRLFAKIKgilPQEVDKEIQRVLLELEMK-NIQDVLAQNLSGGQK 622
Cdd:TIGR02769 83 rrafrrDVQLVFQdsPSAVNPRMTVRQ---IIGEPLRHLTSLD---ESEQKARIAELLDMVGLRsEDADKLPRQLSGGQL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 572882597 623 RKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVI--LFSTQFMDEADILADRKVFLSQGKL 693
Cdd:TIGR02769 157 QRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTayLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
436-698 |
3.25e-15 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 80.78 E-value: 3.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 436 FLKSSFWSQTQKTDHVALEDEMdadPSFHDSfEQAPPEFQGKEAIRIRNVTKEYKGKPdkiEALKDLVFDIYEGQITAIL 515
Cdd:PRK13657 295 FINQVFMAAPKLEEFFEVEDAV---PDVRDP-PGAIDLGRVKGAVEFDDVSFSYDNSR---QGVEDVSFEAKPGQTVAIV 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 516 GHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMAdLENLSKLTGVCPQSNVQFDfLTVRENLRLfAKikgilPQEVDK 595
Cdd:PRK13657 368 GPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT-RASLRRNIAVVFQDAGLFN-RSIEDNIRV-GR-----PDATDE 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 596 EIQRVL-----LELEMKNIQ--DVLA----QNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKT 664
Cdd:PRK13657 440 EMRAAAeraqaHDFIERKPDgyDTVVgergRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMK 519
|
250 260 270
....*....|....*....|....*....|....*....
gi 572882597 665 DRvilfsTQFMDeADIL-----ADRKVFLSQGKLKCAGS 698
Cdd:PRK13657 520 GR-----TTFII-AHRLstvrnADRILVFDNGRVVESGS 552
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1269-1501 |
3.56e-15 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 79.22 E-value: 3.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1269 LNSTNFDEKPVIIASCLRKEYAGKrkgcfskrknkIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVL 1348
Cdd:PRK09452 4 LNKQPSSLSPLVELRGISKSFDGK-----------EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1349 LKGsgggdalEFLGYCPQEN----------ALWPNLTVRQHLEVyaavkGLR---KGDAEVAiTRLVDALK---LQDQLK 1412
Cdd:PRK09452 73 LDG-------QDITHVPAENrhvntvfqsyALFPHMTVFENVAF-----GLRmqkTPAAEIT-PRVMEALRmvqLEEFAQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1413 SPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMV 1492
Cdd:PRK09452 140 RKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMR 219
|
....*....
gi 572882597 1493 SGRLRCIGS 1501
Cdd:PRK09452 220 DGRIEQDGT 228
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
483-692 |
4.40e-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: 75.76 E-value: 4.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 483 RNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPT---KGSVTiYNNKLSemadLENLSKL 559
Cdd:cd03233 7 RNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIH-YNGIPY----KEFAEKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 TG---VCPQSNVQFDFLTVRENLRLFAKIKGilpqevdKEIQRVllelemkniqdvlaqnLSGGQKRKLTFGIAILGDPQ 636
Cdd:cd03233 82 PGeiiYVSEEDVHFPTLTVRETLDFALRCKG-------NEFVRG----------------ISGGERKRVSIAEALVSRAS 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 572882597 637 IFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFS-TQFMDEADILADRKVFLSQGK 692
Cdd:cd03233 139 VLCWDNSTRGLDSSTALEILKCIRTmaDVLKTTTFVSlYQASDEIYDLFDKVLVLYEGR 197
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1304-1495 |
4.49e-15 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 76.95 E-value: 4.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1304 IATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSgggdalEFLGYCPQENA-------------- 1369
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQ------HIEGLPGHQIArmgvvrtfqhvrlf 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1370 ----LWPNLTVRQHLEVYAAV-------KGLRKGDAEvAITRL---VDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGN 1435
Cdd:PRK11300 93 remtVIENLLVAQHQQLKTGLfsgllktPAFRRAESE-ALDRAatwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQ 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1436 PSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1495
Cdd:PRK11300 172 PEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1303-1508 |
4.53e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 77.56 E-value: 4.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1303 KIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-----SGGGDALEFL----GYCPQ--ENALW 1371
Cdd:PRK13641 20 KKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpETGNKNLKKLrkkvSLVFQfpEAQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1372 PNlTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQL--KSPVKtLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMD 1449
Cdd:PRK13641 100 EN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLisKSPFE-LSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 572882597 1450 PEGQQQMWQairaTFRNTERGA---LLTTHYMAEAEAVCDRVAIMVSGRLrcigsIQHLKSK 1508
Cdd:PRK13641 178 PEGRKEMMQ----LFKDYQKAGhtvILVTHNMDDVAEYADDVLVLEHGKL-----IKHASPK 230
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1305-1503 |
6.72e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 79.44 E-value: 6.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1305 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSG-----GGDALEF-LGYCPQENALWPNLTVRQ 1378
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINynkldHKLAAQLgIGIIYQELSVIDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1379 HLEV----YAAVKGLRKGD---AEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1451
Cdd:PRK09700 100 NLYIgrhlTKKVCGVNIIDwreMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 572882597 1452 GQQQMWqAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQ 1503
Cdd:PRK09700 180 EVDYLF-LIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVS 230
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
476-707 |
8.37e-15 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 77.85 E-value: 8.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 476 GKEAIRIRNVTKEYkgkpDKIEALKDLVFDIYEGQITAILGHSGAG--KSTLLNILSGlsvPTKGSVTIynNKLSEMADL 553
Cdd:NF000106 10 ARNAVEVRGLVKHF----GEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPW--RF*TWCANR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 554 ENLSKLTGVC-PQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAIL 632
Cdd:NF000106 81 RALRRTIG*HrPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 572882597 633 GDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTD-RVILFSTQFMDEADILADRKVFLSQGKLKCAGSSLFLKKKWG 707
Cdd:NF000106 161 GRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDgATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG 236
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1305-1491 |
9.59e-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: 9.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1305 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsGGGDALEF--------LGYCPQENALWPNlTV 1376
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAV---NGVPLADAdadswrdqIAWVPQHPFLFAG-TI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1377 RQHLEVY---AAVKGLRKGDAEVAITRLVDALK--LQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1451
Cdd:TIGR02857 413 AENIRLArpdASDAEIREALERAGLDEFVAALPqgLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAE 492
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 572882597 1452 GQQQMWQAIRATFRNteRGALLTTHYMAEAEAvCDRVAIM 1491
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 ... |
472-697 |
1.01e-14 |
|
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: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 472 PEFQGKeaIRIRNVTkeYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMa 551
Cdd:TIGR01842 311 PEPEGH--LSVENVT--IVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQW- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 552 DLENLSKLTGVCPQsNVQFDFLTVRENLRLF------------AKIKGI------LPQEVDKEIqrvllelemkniqDVL 613
Cdd:TIGR01842 386 DRETFGKHIGYLPQ-DVELFPGTVAENIARFgenadpekiieaAKLAGVhelilrLPDGYDTVI-------------GPG 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 614 AQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEADILADRKVFLSQGKL 693
Cdd:TIGR01842 452 GATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPSLLGCVDKILVLQDGRI 531
|
....
gi 572882597 694 KCAG 697
Cdd:TIGR01842 532 ARFG 535
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
501-648 |
1.18e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 74.46 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 501 DLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEM-----ADLENLSKLTGVCPQsnvqfdfLTV 575
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQrdeyhQDLLYLGHQPGIKTE-------LTA 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 572882597 576 RENLRLFAKIKGILPQEvdkEIQRVLLELEMKNIQDVLAQNLSGGQKRKltfgIAI----LGDPQIFLLDEPTAGLD 648
Cdd:PRK13538 92 LENLRFYQRLHGPGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRR----VALarlwLTRAPLWILDEPFTAID 161
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1285-1496 |
1.24e-14 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 77.15 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1285 LRKEYAGKRKGcfskrknKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsgGGDALEFLGyc 1364
Cdd:PRK11153 7 ISKVFPQGGRT-------IHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLV----DGQDLTALS-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1365 pqENALwpNLTVR------QHLE------VYAAV------KGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKL 1426
Cdd:PRK11153 74 --EKEL--RKARRqigmifQHFNllssrtVFDNValplelAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 572882597 1427 CFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATfrNTERG--ALLTTHYMAEAEAVCDRVAIMVSGRL 1496
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALDPATTRSILELLKDI--NRELGltIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
478-691 |
1.55e-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: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 478 EAIRIRNVTKEYK-----GKpdKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTI-YNNKLSEMA 551
Cdd:COG4778 3 TLLEVENLSKTFTlhlqgGK--RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrHDGGWVDLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 552 DLE-----NLSKLT-GVCPQsnvqfdFLTVR----------ENLRLfakiKGILPQEVDKEIQRVLLELemkNIQDVLAQ 615
Cdd:COG4778 81 QASpreilALRRRTiGYVSQ------FLRVIprvsaldvvaEPLLE----RGVDREEARARARELLARL---NLPERLWD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 616 ----NLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTqFMDEA--DILADRKVFLS 689
Cdd:COG4778 148 lppaTFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGI-FHDEEvrEAVADRVVDVT 226
|
..
gi 572882597 690 QG 691
Cdd:COG4778 227 PF 228
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1293-1515 |
1.57e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 75.61 E-value: 1.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1293 RKGCFSKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-----SGGGDALEFLGYC--- 1364
Cdd:PRK13652 7 RDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGepitkENIREVRKFVGLVfqn 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1365 PQENALWPnlTVRQHLEVYAAVKGLrkgDAEVAITRLVDALK---LQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLL 1441
Cdd:PRK13652 87 PDDQIFSP--TVEQDIAFGPINLGL---DEETVAHRVSSALHmlgLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 572882597 1442 DEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLkskFGKDYLL 1515
Cdd:PRK13652 162 DEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI---FLQPDLL 232
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1286-1511 |
1.73e-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: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1286 RKEYAGKRKGCFSKRKN-KIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKP---TAGQVLLKGSGGGdaLEFL 1361
Cdd:TIGR00955 20 WKQLVSRLRGCFCRERPrKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPID--AKEM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1362 ----GYCPQENALWPNLTVRQHLEVYAAVKGLRKGDAEVAITR---LVDALKLQD------QLKSPVKTLSEGIKRKLCF 1428
Cdd:TIGR00955 98 raisAYVQQDDLFIPTLTVREHLMFQAHLRMPRRVTKKEKRERvdeVLQALGLRKcantriGVPGRVKGLSGGERKRLAF 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1429 VLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRAtFRNTERGALLTTHyMAEAEAVC--DRVAIMVSGRLRCIGSIQHLK 1506
Cdd:TIGR00955 178 ASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKG-LAQKGKTIICTIH-QPSSELFElfDKIILMAEGRVAYLGSPDQAV 255
|
....*
gi 572882597 1507 SKFGK 1511
Cdd:TIGR00955 256 PFFSD 260
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
497-732 |
1.85e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 75.43 E-value: 1.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 497 EALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKL--SEMADLENLSKLTGVCPQSNVQFDFLT 574
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdySKRGLLALRQQVATVFQDPEQQIFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 575 VRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQ 654
Cdd:PRK13638 95 IDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 655 VWNLLKE--RKTDRVILfSTQFMDEADILADRKVFLSQGKLKCAGS--SLF----------LKKKWGIGYHLSLQLNEIC 720
Cdd:PRK13638 175 MIAIIRRivAQGNHVII-SSHDIDLIYEISDAVYVLRQGQILTHGApgEVFacteameqagLTQPWLVKLHTQLGLPLCK 253
|
250
....*....|..
gi 572882597 721 VEENITSLVKQH 732
Cdd:PRK13638 254 TETEFFHRMQKC 265
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
480-693 |
1.97e-14 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 74.74 E-value: 1.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYkgkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNK-LSEMADLENLSK 558
Cdd:PRK09493 2 IEFKNVSKHF----GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKvNDPKVDERLIRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 559 LTGVCPQSNVQFDFLTVRENLrLFA--KIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQ 636
Cdd:PRK09493 78 EAGMVFQQFYLFPHLTALENV-MFGplRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 637 IFLLDEPTAGLDPFSRHQVWNLLK---ERKTDRVILfsTQFMDEADILADRKVFLSQGKL 693
Cdd:PRK09493 157 LMLFDEPTSALDPELRHEVLKVMQdlaEEGMTMVIV--THEIGFAEKVASRLIFIDKGRI 214
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1305-1508 |
2.68e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 75.27 E-value: 2.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1305 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGS-------GGGDALEFLGYCPQ--ENALWpNLT 1375
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpidysrkGLMKLRESVGMVFQdpDNQLF-SAS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1376 VRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQ 1455
Cdd:PRK13636 100 VYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 572882597 1456 MWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSK 1508
Cdd:PRK13636 180 IMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
509-671 |
2.87e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 74.05 E-value: 2.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 509 GQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMaDLENLSKL----TGVCPQSNVQFDFLTVRENLRLFAK 584
Cdd:PRK10584 36 GETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQM-DEEARAKLrakhVGFVFQSFMLIPTLNALENVELPAL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 585 IKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDpfsrhqvwnllkeRKT 664
Cdd:PRK10584 115 LRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD-------------RQT 181
|
170
....*....|
gi 572882597 665 -DRV--ILFS 671
Cdd:PRK10584 182 gDKIadLLFS 191
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1307-1515 |
2.95e-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: 2.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1307 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDA-LEFL----GYCPQENALWpNLTVRQHLE 1381
Cdd:cd03252 19 DNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALAdPAWLrrqvGVVLQENVLF-NRSIRDNIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1382 VYAAVKGLRKgdaEVAITRLVDALKLQDQLKSPVKT--------LSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQ 1453
Cdd:cd03252 98 LADPGMSMER---VIEAAKLAGAHDFISELPEGYDTivgeqgagLSGGQRQRIAIARALIHNPRILIFDEATSALDYESE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 572882597 1454 QQMWQAIRATFRNteRGALLTTHYMAEAEAVcDRVAIMVSGRLRCIGSIQHLKSKFGKDYLL 1515
Cdd:cd03252 175 HAIMRNMHDICAG--RTVIIIAHRLSTVKNA-DRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1307-1501 |
3.09e-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: 72.94 E-value: 3.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1307 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITG--DTKPTAGQVLLKGSgggDALEFLgycPQENAlwpnltvrqhlevya 1384
Cdd:cd03217 17 KGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGE---DITDLP---PEERA--------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1385 avkglRKG-----DAEVAITrlvdALKLQDQLKSPVKTLSEGiKRKLCFVLSILG-NPSVVLLDEPSTGMDPEGQQQMWQ 1458
Cdd:cd03217 76 -----RLGiflafQYPPEIP----GVKNADFLRYVNEGFSGG-EKKRNEILQLLLlEPDLAILDEPDSGLDIDALRLVAE 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 572882597 1459 AIRaTFRNTERGALLTTHYMAEAEAV-CDRVAIMVSGRLRCIGS 1501
Cdd:cd03217 146 VIN-KLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGD 188
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
469-648 |
3.15e-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: 77.94 E-value: 3.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 469 QAPPEFQGKEAIRIRNVTKEYKgkPDKiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIynnkls 548
Cdd:COG5265 347 DAPPLVVGGGEVRFENVSFGYD--PER-PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILI------ 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 549 emaDLENLSKLT--------GVCPQSNVQF-DflTVRENLRlFAKikgilPQEVDKEIQRVlleLEMKNIQDVLAQ---- 615
Cdd:COG5265 418 ---DGQDIRDVTqaslraaiGIVPQDTVLFnD--TIAYNIA-YGR-----PDASEEEVEAA---ARAAQIHDFIESlpdg 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 572882597 616 ----------NLSGGQKRKLtfGIA--ILGDPQIFLLDEPTAGLD 648
Cdd:COG5265 484 ydtrvgerglKLSGGEKQRV--AIArtLLKNPPILIFDEATSALD 526
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1305-1496 |
4.67e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 74.34 E-value: 4.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1305 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGS----GGGDALEF---LGYC---PQENALWPnl 1374
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpikyDKKSLLEVrktVGIVfqnPDDQLFAP-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1375 TVRQHLEVYAAVKGLRKGDAEvaiTRLVDALK---LQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1451
Cdd:PRK13639 95 TVEEDVAFGPLNLGLSKEEVE---KRVKEALKavgMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPM 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 572882597 1452 GQQQMwqaIRATFRNTERG--ALLTTHYMAEAEAVCDRVAIMVSGRL 1496
Cdd:PRK13639 172 GASQI---MKLLYDLNKEGitIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
476-693 |
6.45e-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: 6.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 476 GKEAIRIRNVTkeYKGkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNnklsemADLEN 555
Cdd:COG3845 254 GEVVLEVENLS--VRD-DRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDG------EDITG 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 556 LS-----KL-----------TGVCPQsnvqfdfLTVRENLRL-------FAKiKGIL-PQEVDKEIQRVLLELEMK--NI 609
Cdd:COG3845 325 LSprerrRLgvayipedrlgRGLVPD-------MSVAENLILgryrrppFSR-GGFLdRKAIRAFAEELIEEFDVRtpGP 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 610 qDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKtDR---VILFSTQfMDEADILADRKV 686
Cdd:COG3845 397 -DTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELR-DAgaaVLLISED-LDEILALSDRIA 473
|
....*..
gi 572882597 687 FLSQGKL 693
Cdd:COG3845 474 VMYEGRI 480
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
480-693 |
6.54e-14 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 72.60 E-value: 6.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKPdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLEN--LS 557
Cdd:PRK10908 2 IRFEHVSKAYLGGR---QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVpfLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 558 KLTGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQI 637
Cdd:PRK10908 79 RQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 572882597 638 FLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKL 693
Cdd:PRK10908 159 LLADEPTGNLDDALSEGILRLFEEfNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
477-673 |
1.08e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 73.38 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 477 KEAIRIRNVTKEYKgkpDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEmADLENL 556
Cdd:PRK15056 4 QAGIVVNDVTVTWR---NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ-ALQKNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 557 sklTGVCPQSN-VQFDFLTVRENLRLFAKI--KGIL--PQEVDKEI-QRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIA 630
Cdd:PRK15056 80 ---VAYVPQSEeVDWSFPVLVEDVVMMGRYghMGWLrrAKKRDRQIvTAALARVDMVEFRHRQIGELSGGQKKRVFLARA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 572882597 631 ILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQ 673
Cdd:PRK15056 157 IAQQGQVILLDEPFTGVDVKTEARIISLLRElRDEGKTMLVSTH 200
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1304-1514 |
1.20e-13 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 74.68 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1304 IATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG---SGGGDA------LEFLGYCPQENALWPNL 1374
Cdd:PRK10070 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAelrevrRKKIAMVFQSFALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1375 TVRQHLEVYAAVKGLrkgDAEVAITRLVDALK---LQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1451
Cdd:PRK10070 122 TVLDNTAFGMELAGI---NAEERREKALDALRqvgLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 572882597 1452 GQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFGKDYL 1514
Cdd:PRK10070 199 IRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYV 261
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1299-1524 |
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 572882597 1299 KRKNK--IATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDALeflgycpqeNA-LWPNLT 1375
Cdd:PRK13546 31 KHKNKtfFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAI---------SAgLSGQLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1376 VRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQ 1455
Cdd:PRK13546 102 GIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQK 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 572882597 1456 MWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFgKDYLLEMKVKNLAQ 1524
Cdd:PRK13546 182 CLDKIY-EFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKY-EAFLNDFKKKSKAE 248
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1300-1499 |
1.37e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.59 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1300 RKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-----SGGGDALE----FLGYCPQENAL 1370
Cdd:PRK09700 273 SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGkdispRSPLDAVKkgmaYITESRRDNGF 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1371 WPNLTVRQHLEVYAAVKGLRKGDA-----EVAITRLVDALKLQDQLKSP-----VKTLSEGIKRKLCFVLSILGNPSVVL 1440
Cdd:PRK09700 353 FPNFSIAQNMAISRSLKDGGYKGAmglfhEVDEQRTAENQRELLALKCHsvnqnITELSGGNQQKVLISKWLCCCPEVII 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 572882597 1441 LDEPSTGMDPEGQQQMWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCI 1499
Cdd:PRK09700 433 FDEPTRGIDVGAKAEIYKVMR-QLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
923-1168 |
2.27e-13 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.
Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 73.58 E-value: 2.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 923 ASIDDFIQSVEHQNI--ALEVDAFGTRNGTDDPSYNgaITVCCNEKNYSFSLACNAKRLNCFPVLMDIVSNGLLGMVKPS 1000
Cdd:pfam12698 65 DSEEEAKEALKNGKIdgLLVIPKGFSKDLLKGESAT--VTVYINSSNLLVSKLILNALQSLLQQLNASALVLLLEALSTS 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1001 VHIRTErSTFLENGQDNPIGFLAYIMFWLVLTSSCPpYIAMSSIDDYKNRARSQLRISGLSPSAYWFGQALVDVSLYFLV 1080
Cdd:pfam12698 143 APIPVE-STPLFNPQSGYAYYLVGLILMIIILIGAA-IIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFLVGLLQ 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1081 FVFIYLMSYISNFEDMLLTIIHIIQIPcavgYSFSLIFMTYVISFIFRKGRKNSGIWSFCFYVVTVFSVAGFAFSIFESD 1160
Cdd:pfam12698 221 LLIILLLLFGIGIPFGNLGLLLLLFLL----YGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLFPLEDPPSF 296
|
....*...
gi 572882597 1161 IPFIFTFL 1168
Cdd:pfam12698 297 LQWIFSII 304
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1302-1476 |
2.32e-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: 2.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1302 NKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDALEFL-GYCPQENALWpNLTV 1376
Cdd:TIGR02868 347 APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGvpvsSLDQDEVRRRvSVCAQDAHLF-DTTV 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1377 RQHL----------EVYAAVKGLRKGDaevaitrLVDAlkLQDQLKSPV----KTLSEGIKRKLCFVLSILGNPSVVLLD 1442
Cdd:TIGR02868 426 RENLrlarpdatdeELWAALERVGLAD-------WLRA--LPDGLDTVLgeggARLSGGERQRLALARALLADAPILLLD 496
|
170 180 190
....*....|....*....|....*....|....
gi 572882597 1443 EPSTGMDPEGQQQMWQAIRATfrNTERGALLTTH 1476
Cdd:TIGR02868 497 EPTEHLDAETADELLEDLLAA--LSGRTVVLITH 528
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1297-1496 |
2.58e-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: 2.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1297 FSKRKNKI-ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDAL-EF---LGYCPQE 1367
Cdd:COG1135 11 FPTKGGPVtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGvdltALSERELrAArrkIGMIFQH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1368 NALWPNLTVRQH----LEvyaaVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEG------IKRKLCfvlsilGNPS 1437
Cdd:COG1135 91 FNLLSSRTVAENvalpLE----IAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGqkqrvgIARALA------NNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 572882597 1438 VVLLDEPSTGMDPEGQQQmwqaIRATFR--NTERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1496
Cdd:COG1135 161 VLLCDEATSALDPETTRS----ILDLLKdiNRELGLtiVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1307-1501 |
2.76e-13 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 74.82 E-value: 2.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1307 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsgGG--------DAL-EFLGYCPQENALWpNLTVR 1377
Cdd:COG1132 357 KDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILI----DGvdirdltlESLrRQIGVVPQDTFLF-SGTIR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1378 QHL----------EVYAAVKglrkgdaEVAITRLVDALKlqDQLKSPV----KTLSEGIKRKLCFVLSILGNPSVVLLDE 1443
Cdd:COG1132 432 ENIrygrpdatdeEVEEAAK-------AAQAHEFIEALP--DGYDTVVgergVNLSGGQRQRIAIARALLKDPPILILDE 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 572882597 1444 PSTGMDPEGQQQMWQAIRATFRNteRGALLTTHYMAEAEAvCDRVAIMVSGRLRCIGS 1501
Cdd:COG1132 503 ATSALDTETEALIQEALERLMKG--RTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGT 557
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1307-1495 |
3.12e-13 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 71.18 E-value: 3.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1307 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDALEF---LGYCPQENALWPNLTVRQH 1379
Cdd:COG1126 18 KGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGedltDSKKDINKLrrkVGMVFQQFNLFPHLTVLEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1380 LeVYA--AVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEG------IKRKLCFvlsilgNPSVVLLDEPSTGMDPE 1451
Cdd:COG1126 98 V-TLApiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGqqqrvaIARALAM------EPKVMLFDEPTSALDPE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 572882597 1452 gqqqMWQAIRATFRN-TERGA--LLTTHYMAEAEAVCDRVAIMVSGR 1495
Cdd:COG1126 171 ----LVGEVLDVMRDlAKEGMtmVVVTHEMGFAREVADRVVFMDGGR 213
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1308-1514 |
4.28e-13 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 70.81 E-value: 4.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1308 NVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-----SGGGDALEFL------GYCPQENALWPNLTV 1376
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfSKTPSDKAIRelrrnvGMVFQQYNLWPHLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1377 RQHL-EVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQ 1455
Cdd:PRK11124 100 QQNLiEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQ 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 572882597 1456 MWQAIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLK----SKFgKDYL 1514
Cdd:PRK11124 180 IVSIIRE-LAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASCFTqpqtEAF-KNYL 240
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
499-655 |
4.53e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 70.51 E-value: 4.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 499 LKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADlENLSKLTGVCPQSNVQF-DflTVRE 577
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP-EIYRQQVSYCAQTPTLFgD--TVYD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 578 NLRLFAKIKGILPQE--VDKEIQRVLLELEM--KNIQDvlaqnLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRH 653
Cdd:PRK10247 100 NLIFPWQIRNQQPDPaiFLDDLERFALPDTIltKNIAE-----LSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKH 174
|
..
gi 572882597 654 QV 655
Cdd:PRK10247 175 NV 176
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1307-1501 |
4.59e-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: 4.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1307 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGS-----GGGDALEFLGYCPQENALWPNlTVRQHLE 1381
Cdd:cd03369 25 KNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIdistiPLEDLRSSLTIIPQDPTLFSG-TIRSNLD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1382 VYAavkglRKGDAEvaitrLVDALKlqdqLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIR 1461
Cdd:cd03369 104 PFD-----EYSDEE-----IYGALR----VSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 572882597 1462 ATFRNTergALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1501
Cdd:cd03369 170 EEFTNS---TILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1305-1514 |
4.83e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 71.17 E-value: 4.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1305 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGD------------------ALEFLGYCPQ 1366
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDfsklqgirklvgivfqnpETQFVGRTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1367 -------ENALWPNLTVRQHLEVYAAVKGLRKGdaevaitrlvdalklqdQLKSPvKTLSEGIKRKLCFVLSILGNPSVV 1439
Cdd:PRK13644 97 edlafgpENLCLPPIEIRKRVDRALAEIGLEKY-----------------RHRSP-KTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 572882597 1440 LLDEPSTGMDPEGQQQMWQAIRatfRNTERGALL--TTHYMAEAEAVcDRVAIMVSGRLRCIGSIQHLKSKFGKDYL 1514
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIK---KLHEKGKTIvyITHNLEELHDA-DRIIVMDRGKIVLEGEPENVLSDVSLQTL 231
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
504-649 |
6.03e-13 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 70.79 E-value: 6.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 504 FDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADlENLSKLTGVCPQSNVQ-FDFLTVRENL--- 579
Cdd:PRK11300 26 LEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPG-HQIARMGVVRTFQHVRlFREMTVIENLlva 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 580 -------RLFA---KIKGILPQEVDKeIQRVLLELEMKNIQDVL---AQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAG 646
Cdd:PRK11300 105 qhqqlktGLFSgllKTPAFRRAESEA-LDRAATWLERVGLLEHAnrqAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAG 183
|
...
gi 572882597 647 LDP 649
Cdd:PRK11300 184 LNP 186
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
467-648 |
6.73e-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: 6.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 467 FEQAPPEFQG------KEAIRIRNVTKEYKGKPDKIeaLKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSV 540
Cdd:COG4618 312 LAAVPAEPERmplprpKGRLSVENLTVVPPGSKRPI--LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSV 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 541 TIynnklsEMADL-----ENLSKLTGVCPQsNVQ-FDFlTVRENLRLF-----------AKIKGI------LPQEVDKEI 597
Cdd:COG4618 390 RL------DGADLsqwdrEELGRHIGYLPQ-DVElFDG-TIAENIARFgdadpekvvaaAKLAGVhemilrLPDGYDTRI 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 572882597 598 qrvllelemkniqDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLD 648
Cdd:COG4618 462 -------------GEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLD 499
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1308-1461 |
7.53e-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: 7.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1308 NVSFCVRKGEVLGLLGHNGAGKSTSIKVITG--DTKPTAGQVLLKGSGGGDALE-FLGYCPQENALWPNLTVRQHLEVYA 1384
Cdd:cd03232 25 NISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLDKNFQrSTGYVEQQDVHSPNLTVREALRFSA 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 572882597 1385 AVKGLrkgdaevaitrlvdalklqdqlkspvkTLSEgiKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIR 1461
Cdd:cd03232 105 LLRGL---------------------------SVEQ--RKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLK 152
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1311-1476 |
8.02e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 69.49 E-value: 8.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1311 FCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG--SGGGDALEFLGYCPQENALWPNLTVRQHLEVYAAVKG 1388
Cdd:PRK13543 32 FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGktATRGDRSRFMAYLGHLPGLKADLSTLENLHFLCGLHG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1389 LRK----GDAeVAITRLVDalkLQDQLkspVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATF 1464
Cdd:PRK13543 112 RRAkqmpGSA-LAIVGLAG---YEDTL---VRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHL 184
|
170
....*....|..
gi 572882597 1465 RnTERGALLTTH 1476
Cdd:PRK13543 185 R-GGGAALVTTH 195
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1296-1508 |
8.82e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 70.40 E-value: 8.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1296 CFSKRKN-KIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-----SGGGDALEFLGYCPQEna 1369
Cdd:PRK13632 14 SFSYPNSeNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGitiskENLKEIRKKIGIIFQN-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1370 lwPN-----LTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCfVLSILG-NPSVVLLDE 1443
Cdd:PRK13632 92 --PDnqfigATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVA-IASVLAlNPEIIIFDE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 572882597 1444 pSTGM-DPEGQQQMWQAIRATFRNTERGALLTTHYMAEAeAVCDRVAIMVSGRLRCIGSIQH-LKSK 1508
Cdd:PRK13632 169 -STSMlDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEiLNNK 233
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
509-648 |
9.12e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 73.38 E-value: 9.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 509 GQITAILGHSGAGKSTLLNILSGL--SVPTKGSVTIYNNKLSemadlENLSKLTGVCPQSNVQFDFLTVRENLRLFAKIK 586
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRiqGNNFTGTILANNRKPT-----KQILKRTGFVTQDDILYPHLTVRETLVFCSLLR 168
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 572882597 587 giLPQEVDKEI-----QRVLLELEMKNIQDVLAQN-----LSGGQKRKLTFGIAILGDPQIFLLDEPTAGLD 648
Cdd:PLN03211 169 --LPKSLTKQEkilvaESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1287-1496 |
1.03e-12 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 69.13 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1287 KEYAGKRKgcfskrknkiATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSG----GGDALEFL- 1361
Cdd:PRK10908 9 KAYLGGRQ----------ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDitrlKNREVPFLr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1362 ---GYCPQENALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSV 1438
Cdd:PRK10908 79 rqiGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 572882597 1439 VLLDEPSTGMDPEgqqqMWQAIRATFRNTER---GALLTTHYMAEAEAVCDRVAIMVSGRL 1496
Cdd:PRK10908 159 LLADEPTGNLDDA----LSEGILRLFEEFNRvgvTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
480-699 |
1.05e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 70.04 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGS---VTIYNNKLSEMA----D 552
Cdd:PRK09984 5 IRVEKLAKTFNQH----QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAgshIELLGRTVQREGrlarD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 553 LENLSKLTGVCPQsnvQFDF---LTVRENLRLFAKikGILP----------QEVDKEIQRVLLELEMKNIQDVLAQNLSG 619
Cdd:PRK09984 81 IRKSRANTGYIFQ---QFNLvnrLSVLENVLIGAL--GSTPfwrtcfswftREQKQRALQALTRVGMVHFAHQRVSTLSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 620 GQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFST-QFMDEADILADRKVFLSQGKLKCAG 697
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDiNQNDGITVVVTlHQVDYALRYCERIVALRQGHVFYDG 235
|
..
gi 572882597 698 SS 699
Cdd:PRK09984 236 SS 237
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
505-684 |
1.15e-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: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 505 DIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMadlenlskltgvcPQSnVQFDF-LTVRENLRLFA 583
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYK-------------PQY-IKADYeGTVRDLLSSIT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 584 KIKGILPQ-EVDkeiqrVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRhqvwnLLKER 662
Cdd:cd03237 87 KDFYTHPYfKTE-----IAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQR-----LMASK 156
|
170 180
....*....|....*....|....*....
gi 572882597 663 KTDRVILF--STQFMDEADI-----LADR 684
Cdd:cd03237 157 VIRRFAENneKTAFVVEHDIimidyLADR 185
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1275-1495 |
1.25e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 69.57 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1275 DEKPVIIASCLRKEYaGKRKGCfskrknkiatRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGG 1354
Cdd:PRK11701 2 MDQPLLSVRGLTKLY-GPRKGC----------RDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1355 GDA-LEFLGYcPQENAL----WPnlTVRQHlevyaAVKGLRKG---DAEVAiTRL-----------------------VD 1403
Cdd:PRK11701 71 QLRdLYALSE-AERRRLlrteWG--FVHQH-----PRDGLRMQvsaGGNIG-ERLmavgarhygdiratagdwlerveID 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1404 ALKLQDQlksPvKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEA 1483
Cdd:PRK11701 142 AARIDDL---P-TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARL 217
|
250
....*....|..
gi 572882597 1484 VCDRVAIMVSGR 1495
Cdd:PRK11701 218 LAHRLLVMKQGR 229
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1307-1501 |
1.31e-12 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 69.06 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1307 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG---SGGG--DALEFLGYCPQEnalwPNL---TVRQ 1378
Cdd:cd03244 21 KNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiSKIGlhDLRSRISIIPQD----PVLfsgTIRS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1379 HL---------EVYAAVKglrkgdaEVAITRLVDAL--KLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTG 1447
Cdd:cd03244 97 NLdpfgeysdeELWQALE-------RVGLKEFVESLpgGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATAS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 572882597 1448 MDPEGQQQMWQAIRATFRNTergALLT-THYMaeaEAV--CDRVAIMVSGRLRCIGS 1501
Cdd:cd03244 170 VDPETDALIQKTIREAFKDC---TVLTiAHRL---DTIidSDRILVLDKGRVVEFDS 220
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
480-671 |
1.46e-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: 1.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKPDKIeaLKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLsVPTKGSVTIYNNKLSEMAdLENLSKL 559
Cdd:cd03289 3 MTVKDLTAKYTEGGNAV--LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWNSVP-LQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 TGVCPQSNVQFDFlTVRENLRLFAKIKgilpqevDKEIQRVLLELEMKNIQD--------VLAQN---LSGGQKRKLTFG 628
Cdd:cd03289 79 FGVIPQKVFIFSG-TFRKNLDPYGKWS-------DEEIWKVAEEVGLKSVIEqfpgqldfVLVDGgcvLSHGHKQLMCLA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 572882597 629 IAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFS 671
Cdd:cd03289 151 RSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILS 193
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1309-1504 |
1.55e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 71.87 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1309 VSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-----SGGGDALEF-LGYCPQ---ENALWPNLTVRQH 1379
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpidiRSPRDAIRAgIMLCPEdrkAEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1380 LEVYAAVKGLRKG----------DAEVAITRLvdALKLQDQlKSPVKTLSEGIKRKlcfvlSILG-----NPSVVLLDEP 1444
Cdd:PRK11288 352 INISARRHHLRAGclinnrweaeNADRFIRSL--NIKTPSR-EQLIMNLSGGNQQK-----AILGrwlseDMKVILLDEP 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 572882597 1445 STGMDPEGQQQMWQAIratFRNTERG--ALLTTHYMAEAEAVCDRVAIMVSGRLRciGSIQH 1504
Cdd:PRK11288 424 TRGIDVGAKHEIYNVI---YELAAQGvaVLFVSSDLPEVLGVADRIVVMREGRIA--GELAR 480
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
499-697 |
1.93e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 71.03 E-value: 1.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 499 LKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLsEMADLENLSKLTGVCPQ-SNVQFDFlTVRE 577
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDV-EALSARAASRRVASVPQdTSLSFEF-DVRQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 578 NLRL--------FAKIKGILPQEVDKEIQRVllelEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDp 649
Cdd:PRK09536 97 VVEMgrtphrsrFDTWTETDRAAVERAMERT----GVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD- 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 572882597 650 fSRHQVWNLLKERK---TDRVILFSTQFMDEADILADRKVFLSQGKLKCAG 697
Cdd:PRK09536 172 -INHQVRTLELVRRlvdDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
482-702 |
1.97e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 70.52 E-value: 1.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 482 IRNVTKEYkGKPDKIEalkDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIynnklsemaDLENLSKLT- 560
Cdd:PRK11432 9 LKNITKRF-GSNTVID---NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFI---------DGEDVTHRSi 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 561 ---GVCP--QSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDP 635
Cdd:PRK11432 76 qqrDICMvfQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 572882597 636 QIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVI--LFSTQFMDEADILADRKVFLSQGKLKCAGS---------SLFL 702
Cdd:PRK11432 156 KVLLFDEPLSNLDANLRRSMREKIRELQQQFNItsLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSpqelyrqpaSRFM 233
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1305-1505 |
2.21e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 69.27 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1305 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsgGGDALEflgycpqENALWpnlTVRQHLE--- 1381
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITV----GGMVLS-------EETVW---DVRRQVGmvf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1382 -------VYAAVK-----GL--RKGDAEVAITRLVDALKL---QDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEP 1444
Cdd:PRK13635 88 qnpdnqfVGATVQddvafGLenIGVPREEMVERVDQALRQvgmEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 572882597 1445 STGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAeAVCDRVAIMVSGRLRCIGSIQHL 1505
Cdd:PRK13635 168 TSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEEGTPEEI 227
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1307-1496 |
2.30e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 68.30 E-value: 2.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1307 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG------SGGGDAL---EFLGYCPQENALWPNLTVR 1377
Cdd:PRK11629 26 HNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpmsklSSAAKAElrnQKLGFIYQFHHLLPDFTAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1378 QHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMW 1457
Cdd:PRK11629 106 ENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIF 185
|
170 180 190
....*....|....*....|....*....|....*....
gi 572882597 1458 QAIRATFRNTERGALLTTHYMAEAEAVcDRVAIMVSGRL 1496
Cdd:PRK11629 186 QLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRL 223
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1307-1495 |
2.94e-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: 2.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1307 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGqvlLKGS---GGGDALEF-------LGYCPQENALWPNLTV 1376
Cdd:cd03233 24 KDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVS---VEGDihyNGIPYKEFaekypgeIIYVSEEDVHFPTLTV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1377 RQHLEVYAAVKGlrkgdaevaitrlvdalklqDQLkspVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQM 1456
Cdd:cd03233 101 RETLDFALRCKG--------------------NEF---VRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 572882597 1457 WQAIRaTFRNTERGALLTTHYMA--EAEAVCDRVAIMVSGR 1495
Cdd:cd03233 158 LKCIR-TMADVLKTTTFVSLYQAsdEIYDLFDKVLVLYEGR 197
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1308-1505 |
3.13e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 70.13 E-value: 3.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1308 NVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGD-ALEFLGYCP--QENALWPNLTVRQHleVYA 1384
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHrSIQQRDICMvfQSYALFPHMSLGEN--VGY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1385 AVKGLRKGDAEVAiTRLVDALKLQDQL---KSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIR 1461
Cdd:PRK11432 102 GLKMLGVPKEERK-QRVKEALELVDLAgfeDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIR 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 572882597 1462 ATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL 1505
Cdd:PRK11432 181 ELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
478-669 |
3.17e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 71.38 E-value: 3.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 478 EAIRIRNVtkeykgkPDKIEalKDLV-------FDIY------EGQITAILGHSGAGKSTLLNILSGLSVPTKGSvtiYN 544
Cdd:PRK13409 64 DAISIVNL-------PEELE--EEPVhrygvngFKLYglpipkEGKVTGILGPNGIGKTTAVKILSGELIPNLGD---YE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 545 NKLSemADlENLSKLTGvcpqSNVQFDFLTVRENlrlfaKIKGIL-PQEVDKeIQRV-------LLE------------- 603
Cdd:PRK13409 132 EEPS--WD-EVLKRFRG----TELQNYFKKLYNG-----EIKVVHkPQYVDL-IPKVfkgkvreLLKkvdergkldevve 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 572882597 604 -LEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVIL 669
Cdd:PRK13409 199 rLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVL 265
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1309-1449 |
3.96e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 68.04 E-value: 3.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1309 VSFCVRKGEVLGLLGHNGAGKSTSIKVITGdTKPTAGQVLLkgsgGGDALEFL---------GYCPQENALWPNLTVRQH 1379
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQF----AGQPLEAWsaaelarhrAYLSQQQTPPFAMPVFQY 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 572882597 1380 LEVYAAVkGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSIL-----GNPS--VVLLDEPSTGMD 1449
Cdd:PRK03695 90 LTLHQPD-KTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLqvwpdINPAgqLLLLDEPMNSLD 165
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
452-693 |
4.14e-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: 4.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 452 ALEDEMDADPSfHDSFEQAPPEFQGKEAIRIRNVTKEYKG-KPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILS 530
Cdd:COG4615 301 ELELALAAAEP-AAADAAAPPAPADFQTLELRGVTYRYPGeDGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLT 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 531 GLSVPTKGSVTIyNNKLSEMADLENLSKLTgvcpqSNVQFDFltvrenlRLFAKIKGILPQEVDKEIQRVLLELEMKN-- 608
Cdd:COG4615 380 GLYRPESGEILL-DGQPVTADNREAYRQLF-----SAVFSDF-------HLFDRLLGLDGEADPARARELLERLELDHkv 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 609 -IQD--VLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDP-FSR---HQVWNLLKER-KTdrVILFS--TQFMDea 678
Cdd:COG4615 447 sVEDgrFSTTDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPeFRRvfyTELLPELKARgKT--VIAIShdDRYFD-- 522
|
250
....*....|....*
gi 572882597 679 diLADRKVFLSQGKL 693
Cdd:COG4615 523 --LADRVLKMDYGKL 535
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
480-642 |
4.48e-12 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 70.69 E-value: 4.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKPDKIEALKDLV----------------FDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVtiy 543
Cdd:PRK13545 5 VKFEHVTKKYKMYNKPFDKLKDLFfrskdgeyhyalnnisFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 544 nnklsemaDLENLSKLTGVCPQSNVQfdfLTVRENLRLFAKIKGILPQEVDKEIQRVlleLEMKNIQDVLAQ---NLSGG 620
Cdd:PRK13545 82 --------DIKGSAALIAISSGLNGQ---LTGIENIELKGLMMGLTKEKIKEIIPEI---IEFADIGKFIYQpvkTYSSG 147
|
170 180
....*....|....*....|..
gi 572882597 621 QKRKLTFGIAILGDPQIFLLDE 642
Cdd:PRK13545 148 MKSRLGFAISVHINPDILVIDE 169
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
478-661 |
4.61e-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: 4.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 478 EAIRIRNVtkeykgkPDKIEalKDLV-------FDIY------EGQITAILGHSGAGKSTLLNILSGLSVPTKGsvtIYN 544
Cdd:COG1245 64 DAISIVNL-------PEELE--EDPVhrygengFRLYglpvpkKGKVTGILGPNGIGKSTALKILSGELKPNLG---DYD 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 545 NKLSEmaDlENLSKLTGvcpqSNVQFDFLTVRENlrlfaKIKGIL-PQEVDKeIQRV-------LLE------------- 603
Cdd:COG1245 132 EEPSW--D-EVLKRFRG----TELQDYFKKLANG-----EIKVAHkPQYVDL-IPKVfkgtvreLLEkvdergkldelae 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 572882597 604 -LEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE 661
Cdd:COG1245 199 kLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRE 257
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
469-693 |
4.68e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 70.77 E-value: 4.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 469 QAPPEFQgkeAIRIRNVTKEYkgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLS 548
Cdd:PRK10522 315 QAFPDWQ---TLELRNVTFAY---QDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 549 eMADLENLSKLtgvcpqsnvqfdFLTVRENLRLFAKIKGILPQEVDKEIQRVLLE-LEMKN---IQD--VLAQNLSGGQK 622
Cdd:PRK10522 389 -AEQPEDYRKL------------FSAVFTDFHLFDQLLGPEGKPANPALVEKWLErLKMAHkleLEDgrISNLKLSKGQK 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 572882597 623 RKLTFGIAILGDPQIFLLDEPTAGLDP-FSR---HQVWNLLKER-KTdrviLFSTQFMDEADILADRKVFLSQGKL 693
Cdd:PRK10522 456 KRLALLLALAEERDILLLDEWAADQDPhFRRefyQVLLPLLQEMgKT----IFAISHDDHYFIHADRLLEMRNGQL 527
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1307-1476 |
4.68e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 66.90 E-value: 4.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1307 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDAL----EFLGYCPQENALWPNLTVRQHlev 1382
Cdd:PRK13540 18 QQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLctyqKQLCFVGHRSGINPYLTLREN--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1383 yaAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRA 1462
Cdd:PRK13540 95 --CLYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQE 172
|
170
....*....|....
gi 572882597 1463 tFRNTERGALLTTH 1476
Cdd:PRK13540 173 -HRAKGGAVLLTSH 185
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1313-1492 |
5.11e-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: 5.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1313 VRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSgggdalefLGYCPQEnalwpnLTVRQHLEVYAAVKGLRKG 1392
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK--------ISYKPQY------ISPDYDGTVEEFLRSANTD 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1393 DAEVAI--TRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERG 1470
Cdd:COG1245 429 DFGSSYykTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKT 508
|
170 180
....*....|....*....|..
gi 572882597 1471 ALLTTHYMAEAEAVCDRvaIMV 1492
Cdd:COG1245 509 AMVVDHDIYLIDYISDR--LMV 528
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1303-1495 |
5.34e-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: 5.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1303 KIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGsgggdalEFLGYCPQEN-ALW---------- 1371
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDG-------KDVTKLPEYKrAKYigrvfqdpmm 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1372 ---PNLTVRQHLEVyAAVKGLRKG------DAEVAITRlvDALK-----LQDQLKSPVKTLSEGIKRKLCFVLSILGNPS 1437
Cdd:COG1101 92 gtaPSMTIEENLAL-AYRRGKRRGlrrgltKKRRELFR--ELLAtlglgLENRLDTKVGLLSGGQRQALSLLMATLTKPK 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 572882597 1438 VVLLDEPSTGMDPEGQQQMwqaIRATFRNTERG---ALLTTHYMAEAEAVCDRVAIMVSGR 1495
Cdd:COG1101 169 LLLLDEHTAALDPKTAALV---LELTEKIVEENnltTLMVTHNMEQALDYGNRLIMMHEGR 226
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
481-648 |
5.43e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 68.03 E-value: 5.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 481 RIRNVTKEYKGkpdkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVtIYNNKLSEMADLENLSklt 560
Cdd:PRK11701 8 SVRGLTKLYGP----RKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV-HYRMRDGQLRDLYALS--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 561 gvcpQSNVQFDFLT----VRENL----------------RLFA---KIKGILPQEVDKEIQRVllELEMKNIQDvLAQNL 617
Cdd:PRK11701 80 ----EAERRRLLRTewgfVHQHPrdglrmqvsaggnigeRLMAvgaRHYGDIRATAGDWLERV--EIDAARIDD-LPTTF 152
|
170 180 190
....*....|....*....|....*....|.
gi 572882597 618 SGGQKRKLTFGIAILGDPQIFLLDEPTAGLD 648
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLD 183
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
478-694 |
5.79e-12 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 67.92 E-value: 5.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 478 EAIRIRNVTKEY----------------KGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVT 541
Cdd:PRK13546 3 VSVNIKNVTKEYriyrtnkermkdalipKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 542 iYNNKLSEMADLENLS-KLTGVcpqSNVQFDFLTVRENLRlfaKIKGILPQEVDkeiqrvLLELEMKNIQDVlaQNLSGG 620
Cdd:PRK13546 83 -RNGEVSVIAISAGLSgQLTGI---ENIEFKMLCMGFKRK---EIKAMTPKIIE------FSELGEFIYQPV--KKYSSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 572882597 621 QKRKLTFGIAILGDPQIFLLDEP-TAGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEADILADRKVFLSQGKLK 694
Cdd:PRK13546 148 MRAKLGFSINITVNPDILVIDEAlSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLK 222
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
501-649 |
6.43e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 67.87 E-value: 6.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 501 DLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMA--DLENLSKLTGVCPQSNVQFDFLTVREN 578
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsRLYTVRKRMSMLFQSGALFTDMNVFDN 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 572882597 579 LRLFAKIKGILPQEVDKEIqrVLLELE---MKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDP 649
Cdd:PRK11831 105 VAYPLREHTQLPAPLLHST--VMMKLEavgLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDP 176
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
477-669 |
6.44e-12 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 70.43 E-value: 6.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 477 KEAIRIRNVTKEYKGKpdKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMAdLENL 556
Cdd:PRK11176 339 KGDIEFRNVTFTYPGK--EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYT-LASL 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 557 SKLTGVCPQsNVQFDFLTVRENLrLFAKiKGILPQEVDKEIQRVLLELE----MKNIQD-VLAQN---LSGGQKRKLTFG 628
Cdd:PRK11176 416 RNQVALVSQ-NVHLFNDTIANNI-AYAR-TEQYSREQIEEAARMAYAMDfinkMDNGLDtVIGENgvlLSGGQRQRIAIA 492
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 572882597 629 IAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVIL 669
Cdd:PRK11176 493 RALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSL 533
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
482-671 |
6.46e-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: 6.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 482 IRNVTKEYKGKPDKIeaLKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLsVPTKGSVTIYNNKLSEMAdLENLSKLTG 561
Cdd:TIGR01271 1220 VQGLTAKYTEAGRAV--LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSVT-LQTWRKAFG 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 562 VCPQSNVQFDFlTVRENLRLFAkikgilpQEVDKEIQRVLLELEMKNIQD--------VLAQN---LSGGQKRKLTFGIA 630
Cdd:TIGR01271 1296 VIPQKVFIFSG-TFRKNLDPYE-------QWSDEEIWKVAEEVGLKSVIEqfpdkldfVLVDGgyvLSNGHKQLMCLARS 1367
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 572882597 631 ILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFS 671
Cdd:TIGR01271 1368 ILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILS 1408
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1318-1501 |
7.86e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 67.72 E-value: 7.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1318 VLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGsgggDALEFlgycpQENALwpnLTVRQHLEV----------YAAVK 1387
Cdd:PRK13638 29 VTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQG----KPLDY-----SKRGL---LALRQQVATvfqdpeqqifYTDID 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1388 G-----LRK-GDAEVAITRLVD-ALKLQDQL---KSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMW 1457
Cdd:PRK13638 97 SdiafsLRNlGVPEAEITRRVDeALTLVDAQhfrHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 572882597 1458 QAIRATFRNTERgALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1501
Cdd:PRK13638 177 AIIRRIVAQGNH-VIISSHDIDLIYEISDAVYVLRQGQILTHGA 219
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
480-699 |
8.19e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 67.51 E-value: 8.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKP-----DKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLsEMADLE 554
Cdd:PRK15112 5 LEVRNLSKTFRYRTgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 555 NLSKL---------TGVCPQSNVQ--FDFltvreNLRLFAKIKgilPQEVDKEIQRVLLELEMKNIQ-DVLAQNLSGGQK 622
Cdd:PRK15112 84 YRSQRirmifqdpsTSLNPRQRISqiLDF-----PLRLNTDLE---PEQREKQIIETLRQVGLLPDHaSYYPHMLAPGQK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 572882597 623 RKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVI--LFSTQFMDEADILADRKVFLSQGKLKCAGSS 699
Cdd:PRK15112 156 QRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHLGMMKHISDQVLVMHQGEVVERGST 234
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1300-1494 |
8.22e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.60 E-value: 8.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1300 RKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDALE--FLGYCPQ-ENALWPNLTV 1376
Cdd:PRK15056 17 RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQknLVAYVPQsEEVDWSFPVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1377 RQHLEV---YAAVKGLRKGDA------EVAITRlVDALKLQDQlksPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTG 1447
Cdd:PRK15056 97 VEDVVMmgrYGHMGWLRRAKKrdrqivTAALAR-VDMVEFRHR---QIGELSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 572882597 1448 MDPEGQQQMWQAIRaTFRNTERGALLTTHYMAEAEAVCDrVAIMVSG 1494
Cdd:PRK15056 173 VDVKTEARIISLLR-ELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKG 217
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1307-1476 |
8.73e-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: 8.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1307 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsggGDALEFlGYCPQenalwpnltvrqhlevyaav 1386
Cdd:cd03221 17 KDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-----GSTVKI-GYFEQ-------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1387 kglrkgdaevaitrlvdalklqdqlkspvktLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQqqmwQAIRATFRN 1466
Cdd:cd03221 71 -------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESI----EALEEALKE 115
|
170
....*....|
gi 572882597 1467 TERGALLTTH 1476
Cdd:cd03221 116 YPGTVILVSH 125
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1307-1496 |
9.53e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 69.65 E-value: 9.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1307 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG------------SGG---------GDALeFLGYCP 1365
Cdd:PRK10762 269 NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGhevvtrspqdglANGivyisedrkRDGL-VLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1366 QENAlwpNLTVRQHLEvYAAVKgLRKGDAEVAITRLVDALKL----QDQlksPVKTLSEGIKRKLCFVLSILGNPSVVLL 1441
Cdd:PRK10762 348 KENM---SLTALRYFS-RAGGS-LKHADEQQAVSDFIRLFNIktpsMEQ---AIGLLSGGNQQKVAIARGLMTRPKVLIL 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 572882597 1442 DEPSTGMDPEGQQQMWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1496
Cdd:PRK10762 420 DEPTRGVDVGAKKEIYQLIN-QFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1313-1492 |
1.20e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 69.45 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1313 VRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVL--LKGSgggdaleflgYCPQENALWPNLTVRQHLEvyAAVKGLr 1390
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDpeLKIS----------YKPQYIKPDYDGTVEDLLR--SITDDL- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1391 kgDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERG 1470
Cdd:PRK13409 429 --GSSYYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREAT 506
|
170 180
....*....|....*....|..
gi 572882597 1471 ALLTTHYMAEAEAVCDRvaIMV 1492
Cdd:PRK13409 507 ALVVDHDIYMIDYISDR--LMV 526
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1300-1496 |
1.30e-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: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1300 RKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGS--GGGDALEF----LGYCPQE---NAL 1370
Cdd:COG3845 268 DRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEdiTGLSPRERrrlgVAYIPEDrlgRGL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1371 WPNLTVRQHL-----EVYAAVKG--LRKGDAEVAITRLVDALKLQ-DQLKSPVKTLSEGIKRKlcFVLS--ILGNPSVVL 1440
Cdd:COG3845 348 VPDMSVAENLilgryRRPPFSRGgfLDRKAIRAFAEELIEEFDVRtPGPDTPARSLSGGNQQK--VILAreLSRDPKLLI 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 572882597 1441 LDEPSTGMDPEGQQQMWQAIRATfRNteRGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1496
Cdd:COG3845 426 AAQPTRGLDVGAIEFIHQRLLEL-RD--AGAavLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
480-648 |
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 572882597 480 IRIRNVTKEYKGKpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVtiynnklsemadlENLSKL 559
Cdd:PRK09544 5 VSLENVSVSFGQR----RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-------------KRNGKL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 -TGVCPQsNVQFDF---LTVRENLRLFAKIKG--ILPQevdkeIQRV----LLELEMkniqdvlaQNLSGGQKRKLTFGI 629
Cdd:PRK09544 68 rIGYVPQ-KLYLDTtlpLTVNRFLRLRPGTKKedILPA-----LKRVqaghLIDAPM--------QKLSGGETQRVLLAR 133
|
170
....*....|....*....
gi 572882597 630 AILGDPQIFLLDEPTAGLD 648
Cdd:PRK09544 134 ALLNRPQLLVLDEPTQGVD 152
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
467-648 |
1.63e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 68.77 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 467 FEQAPPEFqgKEAIRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVtiynnK 546
Cdd:PRK15064 309 FEQDKKLH--RNALEVENLTKGFDNGP----LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-----K 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 547 LSEMADLenlskltGVCPQSNVQfDF---LTVRENLRLFAKikgilPQEVDKEIQRVLLELEMKNiQDVL--AQNLSGGQ 621
Cdd:PRK15064 378 WSENANI-------GYYAQDHAY-DFendLTLFDWMSQWRQ-----EGDDEQAVRGTLGRLLFSQ-DDIKksVKVLSGGE 443
|
170 180
....*....|....*....|....*..
gi 572882597 622 KRKLTFGIAILGDPQIFLLDEPTAGLD 648
Cdd:PRK15064 444 KGRMLFGKLMMQKPNVLVMDEPTNHMD 470
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1305-1505 |
2.01e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 68.73 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1305 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQV-----------------------LLKGSGGGD-ALEF 1360
Cdd:PRK10261 31 AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqvielseqsaaQMRHVRGADmAMIF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1361 lgycpQE--NALWPNLTV-RQHLEVYAAVKGLRKGDAEVAITRLVDALKL---QDQLKSPVKTLSEGIKRKLCFVLSILG 1434
Cdd:PRK10261 111 -----QEpmTSLNPVFTVgEQIAESIRLHQGASREEAMVEAKRMLDQVRIpeaQTILSRYPHQLSGGMRQRVMIAMALSC 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 572882597 1435 NPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL 1505
Cdd:PRK10261 186 RPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
472-694 |
2.15e-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: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 472 PEFQGKEAIRIRNVTKEYKGKPdKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGlSVPTK--GSVTIYNNKLSE 549
Cdd:TIGR02633 250 PHEIGDVILEARNLTCWDVINP-HRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFG-AYPGKfeGNVFINGKPVDI 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 550 MADLENLS----------KLTGVCPQsnvqfdfLTVRENLRL-----FAKIKGILPQEVDKEIQRVLLELEMKNIQDVLA 614
Cdd:TIGR02633 328 RNPAQAIRagiamvpedrKRHGIVPI-------LGVGKNITLsvlksFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLP 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 615 -QNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQfMDEADILADRKVFLSQG 691
Cdd:TIGR02633 401 iGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlaQEGVAIIVVSSE-LAEVLGLSDRVLVIGEG 479
|
...
gi 572882597 692 KLK 694
Cdd:TIGR02633 480 KLK 482
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
476-693 |
2.41e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 68.27 E-value: 2.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 476 GKEAIRIRNVTKEYKGKpdkieaLKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLEN 555
Cdd:PRK09700 262 HETVFEVRNVTSRDRKK------VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 556 LSKLTGVCPQS---NVQFDFLTVRENLRLFAKIK--------GILPQEVDKEI---QRVLLELEMKNIQdvlaQN---LS 618
Cdd:PRK09700 336 VKKGMAYITESrrdNGFFPNFSIAQNMAISRSLKdggykgamGLFHEVDEQRTaenQRELLALKCHSVN----QNiteLS 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 572882597 619 GGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTD-RVILFSTQFMDEADILADRKVFLSQGKL 693
Cdd:PRK09700 412 GGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
509-648 |
2.92e-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: 2.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 509 GQITAILGHSGAGKSTLLNILSGLSvPTKGSVTIYNNKLSEMaDLENLSKLTGVCPQSNVQFDFLTVRENLRLFAKikgi 588
Cdd:COG4138 22 GELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDW-SAAELARHRAYLSQQQSPPFAMPVFQYLALHQP---- 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 572882597 589 lPQEVDKEIQRVLLEL-EMKNIQDVLAQN---LSGG--QKRKLTfgiAIL--------GDPQIFLLDEPTAGLD 648
Cdd:COG4138 96 -AGASSEAVEQLLAQLaEALGLEDKLSRPltqLSGGewQRVRLA---AVLlqvwptinPEGQLLLLDEPMNSLD 165
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
471-648 |
3.25e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 68.61 E-value: 3.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 471 PPEFQGKEAIRIRNVTKEYKgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEM 550
Cdd:PLN03130 1229 PPGWPSSGSIKFEDVVLRYR--PELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKF 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 551 AdLENLSKLTGVCPQSNVQFDFlTVRENLRLFAKIKgilpqEVDkeiqrvLLE-LEMKNIQDVL--------------AQ 615
Cdd:PLN03130 1307 G-LMDLRKVLGIIPQAPVLFSG-TVRFNLDPFNEHN-----DAD------LWEsLERAHLKDVIrrnslgldaevseaGE 1373
|
170 180 190
....*....|....*....|....*....|...
gi 572882597 616 NLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLD 648
Cdd:PLN03130 1374 NFSVGQRQLLSLARALLRRSKILVLDEATAAVD 1406
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1313-1496 |
3.49e-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: 3.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1313 VRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLL--------KGSGGGDAL-----EFLGYCPQENALWPNLTVRQH 1379
Cdd:PRK11264 26 VKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidtaRSLSQQKGLirqlrQHVGFVFQNFNLFPHRTVLEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1380 -LEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQ 1458
Cdd:PRK11264 106 iIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLN 185
|
170 180 190
....*....|....*....|....*....|....*...
gi 572882597 1459 AIRAtFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1496
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 ... |
1296-1510 |
3.94e-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: 3.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1296 CFSKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsGGGD----ALEFL----GYCPQE 1367
Cdd:cd03253 7 TFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILI---DGQDirevTLDSLrraiGVVPQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1368 NALWpNLTVRQHL----------EVYAAVKglrKGDAEVAITRLVDA---------LKlqdqlkspvktLSEGIKRKLCF 1428
Cdd:cd03253 84 TVLF-NDTIGYNIrygrpdatdeEVIEAAK---AAQIHDKIMRFPDGydtivgergLK-----------LSGGEKQRVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1429 VLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNteRGALLTTHYMAEAeAVCDRVAIMVSGRLRCIGSIQHLKSK 1508
Cdd:cd03253 149 ARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKG--RTTIVIAHRLSTI-VNADKIIVLKDGRIVERGTHEELLAK 225
|
..
gi 572882597 1509 FG 1510
Cdd:cd03253 226 GG 227
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
480-686 |
4.03e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 65.48 E-value: 4.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYK-----GKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNnklsemADLE 554
Cdd:PRK10419 4 LNVSGLSHHYAhgglsGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRG------EPLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 555 NLSK-----------------LTGVCPQSNVQFdflTVRENLRlfaKIKGILPQEVDKEIQRVLLELEMK-NIQDVLAQN 616
Cdd:PRK10419 78 KLNRaqrkafrrdiqmvfqdsISAVNPRKTVRE---IIREPLR---HLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 617 LSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQ-------------FMDEADIL 681
Cdd:PRK10419 152 LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKlqQQFGTACLFITHdlrlverfcqrvmVMDNGQIV 231
|
....*
gi 572882597 682 ADRKV 686
Cdd:PRK10419 232 ETQPV 236
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
499-683 |
4.59e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 65.23 E-value: 4.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 499 LKDLVFDIYEGQITAILGHSGAGKSTLLNILSG--------LSVPTKGSVTIYNNKLSEMaDLENLSKLTGVCPQ-SNVQ 569
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltgggapRGARVTGDVTLNGEPLAAI-DAPRLARLRAVLPQaAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 570 FDFlTVRENLRL----FAKIKGILPQEvDKEIQRVLLEL---EMKNIQDVlaQNLSGGQKRKLTFGIAI---------LG 633
Cdd:PRK13547 96 FAF-SAREIVLLgrypHARRAGALTHR-DGEIAWQALALagaTALVGRDV--TTLSGGELARVQFARVLaqlwpphdaAQ 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 634 DPQIFLLDEPTAGLDPFSRHQV----------WNL----------LKERKTDRVILFStqfmdEADILAD 683
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLldtvrrlardWNLgvlaivhdpnLAARHADRIAMLA-----DGAIVAH 236
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1275-1351 |
5.25e-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: 5.25e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 572882597 1275 DEKPVIIASCLRKEYAgKRKGCFSKRKNKI-ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG 1351
Cdd:COG4608 3 MAEPLLEVRDLKKHFP-VRGGLFGRTVGVVkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDG 79
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1307-1451 |
5.42e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 67.22 E-value: 5.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1307 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVllKGSGGGDalefLGYCPQENALW--PNLTVRQHLEVYA 1384
Cdd:PRK15064 336 KNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV--KWSENAN----IGYYAQDHAYDfeNDLTLFDWMSQWR 409
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 572882597 1385 avkglRKGDAEVAIT----RLvdaLKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1451
Cdd:PRK15064 410 -----QEGDDEQAVRgtlgRL---LFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDME 472
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1307-1496 |
6.81e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 64.34 E-value: 6.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1307 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKP----TAGQVLLKG------SGGGDALEFLGYCPQeNALWPNLTV 1376
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGkpvapcALRGRKIATIMQNPR-SAFNPLHTM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1377 RQHLEVYAAVKGLRKGDAevAITRLVDALKLQDQ---LKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQ 1453
Cdd:PRK10418 99 HTHARETCLALGKPADDA--TLTAALEAVGLENAarvLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQ 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 572882597 1454 QQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1496
Cdd:PRK10418 177 ARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1316-1505 |
6.97e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 64.81 E-value: 6.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1316 GEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGS--GGGDALEF---LGYCPQENALWPNLTVRQHLEV-----YAA 1385
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQplESWSSKAFarkVAYLPQQLPAAEGMTVRELVAIgrypwHGA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1386 VKGLRKGD---AEVAITrLVDALKLQDQLkspVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRA 1462
Cdd:PRK10575 117 LGRFGAADrekVEEAIS-LVGLKPLAHRL---VDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHR 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 572882597 1463 TFRntERGALLTT--HYMAEAEAVCDRVAIMVSGRLRCIGSIQHL 1505
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 ... |
1301-1509 |
7.00e-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: 7.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1301 KNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITG--DTKPTAGQVLLKGS-----GGGDALEFLGY-CP------- 1365
Cdd:TIGR03269 11 DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYHVAlcekcGYVERPSKVGEpCPvcggtle 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1366 -QENALW-PNLTVRQHLEVYAAVKGLRK----GD-----------------AEVAITR---LVDALKLQDQLKSPVKTLS 1419
Cdd:TIGR03269 91 pEEVDFWnLSDKLRRRIRKRIAIMLQRTfalyGDdtvldnvlealeeigyeGKEAVGRavdLIEMVQLSHRITHIARDLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1420 EGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCI 1499
Cdd:TIGR03269 171 GGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIKEE 250
|
250
....*....|
gi 572882597 1500 GSIQHLKSKF 1509
Cdd:TIGR03269 251 GTPDEVVAVF 260
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1282-1511 |
7.02e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 64.71 E-value: 7.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1282 ASCLRKEYAGKrkGCFSKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGS-----GGGD 1356
Cdd:PRK10419 6 VSGLSHHYAHG--GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEplaklNRAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1357 ALEF-----LGYCPQENALWPNLTVRQHL-EVYAAVKGLRKGDAEVAITRLVDALKLQDQL--KSPvKTLSEGIKRKLCF 1428
Cdd:PRK10419 84 RKAFrrdiqMVFQDSISAVNPRKTVREIIrEPLRHLLSLDKAERLARASEMLRAVDLDDSVldKRP-PQLSGGQLQRVCL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1429 VLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL---RCIGSIQHL 1505
Cdd:PRK10419 163 ARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIvetQPVGDKLTF 242
|
....*.
gi 572882597 1506 KSKFGK 1511
Cdd:PRK10419 243 SSPAGR 248
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
502-649 |
7.41e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 63.71 E-value: 7.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 502 LVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIyNNKLSEMAD----LENLSKLTGVCPQsnvqfdfLTVRE 577
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQI-DGKTATRGDrsrfMAYLGHLPGLKAD-------LSTLE 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 572882597 578 NLRLFAKIKGILPQEVDKEiqrVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDP 649
Cdd:PRK13543 102 NLHFLCGLHGRRAKQMPGS---ALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
480-698 |
7.89e-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: 63.31 E-value: 7.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLS--VPTKGSVTIYNNKLSEMADLENLS 557
Cdd:cd03217 1 LEIKDLHVSVGGK----EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 558 KLTGVCPQSNVQFDFLTVRENLRlfakikgilpqEVDKeiqrvllelemkniqdvlaqNLSGGQKRKLTFGIAILGDPQI 637
Cdd:cd03217 77 LGIFLAFQYPPEIPGVKNADFLR-----------YVNE--------------------GFSGGEKKRNEILQLLLLEPDL 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 572882597 638 FLLDEPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEAD-ILADRKVFLSQGKLKCAGS 698
Cdd:cd03217 126 AILDEPDSGLDIDALRLVAEVINKlREEGKSVLIITHYQRLLDyIKPDRVHVLYDGRIVKSGD 188
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
500-661 |
8.24e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 64.62 E-value: 8.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 500 KDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLEnLSKLTGVCPQSNVQFDFLTVREnl 579
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKE-VARRIGLLAQNATTPGDITVQE-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 580 rLFAkiKGILPQEV------DKEIQRVLLELEMKNIQDVLAQN---LSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPF 650
Cdd:PRK10253 101 -LVA--RGRYPHQPlftrwrKEDEEAVTKAMQATGITHLADQSvdtLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS 177
|
170
....*....|.
gi 572882597 651 SRHQVWNLLKE 661
Cdd:PRK10253 178 HQIDLLELLSE 188
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1307-1548 |
1.03e-10 |
|
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: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1307 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITgDTKPTAGQVLLKG-SGGGDALE----FLGYCPQENALWPNlTVRQHLE 1381
Cdd:cd03289 21 ENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGvSWNSVPLQkwrkAFGVIPQKVFIFSG-TFRKNLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1382 VYAAVKG--LRKGDAEVAITRLVDAL--KLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPegqqQMW 1457
Cdd:cd03289 99 PYGKWSDeeIWKVAEEVGLKSVIEQFpgQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP----ITY 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1458 QAIRATFRNTERGA--LLTTHYMaEAEAVCDRVAIMVSGRLRCIGSIQHLKSKfgkdyllemkvKNLAQVEPLHAEILRL 1535
Cdd:cd03289 175 QVIRKTLKQAFADCtvILSEHRI-EAMLECQRFLVIEENKVRQYDSIQKLLNE-----------KSHFKQAISPSDRLKL 242
|
250
....*....|...
gi 572882597 1536 FPQAARQERYSSL 1548
Cdd:cd03289 243 FPRRNSSKSKRKP 255
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
462-693 |
1.05e-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: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 462 SFHDSFEQAPPEfQGKEAIRIRNVTKEykgkpdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVT 541
Cdd:COG1129 240 ELEDLFPKRAAA-PGEVVLEVEGLSVG--------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIR 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 542 IyNNKlsemaDLENLS----------------KLTGVCPQsnvqfdfLTVREN-----LRLFAKIKGILPQEVDKEIQRV 600
Cdd:COG1129 311 L-DGK-----PVRIRSprdairagiayvpedrKGEGLVLD-------LSIRENitlasLDRLSRGGLLDRRRERALAEEY 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 601 LLELEMK--NIqDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERkTDR---VILFSTQfM 675
Cdd:COG1129 378 IKRLRIKtpSP-EQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIREL-AAEgkaVIVISSE-L 454
|
250
....*....|....*...
gi 572882597 676 DEADILADRKVFLSQGKL 693
Cdd:COG1129 455 PELLGLSDRILVMREGRI 472
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
480-655 |
1.23e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.59 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKPDkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSV------------------- 540
Cdd:PTZ00265 383 IQFKNVRFHYDTRKD-VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIiindshnlkdinlkwwrsk 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 541 -------------TIYNN---KLSEMADLENLSKLTGvcPQSNVQFDFLTVRENLRlfAKIKGILPQEVDKEIQRVLLEL 604
Cdd:PTZ00265 462 igvvsqdpllfsnSIKNNikySLYSLKDLEALSNYYN--EDGNDSQENKNKRNSCR--AKCAGDLNDMSNTTDSNELIEM 537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 605 --EMKNIQD---------VL-------------------AQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQ 654
Cdd:PTZ00265 538 rkNYQTIKDsevvdvskkVLihdfvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYL 617
|
.
gi 572882597 655 V 655
Cdd:PTZ00265 618 V 618
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
1304-1449 |
1.33e-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: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1304 IATR--NVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTkPTAGQVLLkgsgGGDALE---------FLGYCPQENALWP 1372
Cdd:COG4138 8 VAGRlgPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILL----NGRPLSdwsaaelarHRAYLSQQQSPPF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1373 NLTVRQHLEVYAAvKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSIL-----GNPS--VVLLDEPS 1445
Cdd:COG4138 83 AMPVFQYLALHQP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptINPEgqLLLLDEPM 161
|
....
gi 572882597 1446 TGMD 1449
Cdd:COG4138 162 NSLD 165
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
465-698 |
1.54e-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: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 465 DSFEQAPPEFQGKEAIRIRNVTKEY-KGKPdkiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILsglsvptkgsvtiy 543
Cdd:TIGR00957 622 DSIERRTIKPGEGNSITVHNATFTWaRDLP---PTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL-------------- 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 544 nnkLSEMADLENLSKLTG----VCPQSNVQFDflTVRENLrLFAKikGILPQEVDKEIQR--VLLELEMKNIQDVL---- 613
Cdd:TIGR00957 685 ---LAEMDKVEGHVHMKGsvayVPQQAWIQND--SLRENI-LFGK--ALNEKYYQQVLEAcaLLPDLEILPSGDRTeige 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 614 -AQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWN-------LLKErKTDRVILFSTQFMDEADILadrk 685
Cdd:TIGR00957 757 kGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEhvigpegVLKN-KTRILVTHGISYLPQVDVI---- 831
|
250
....*....|...
gi 572882597 686 VFLSQGKLKCAGS 698
Cdd:TIGR00957 832 IVMSGGKISEMGS 844
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
492-661 |
1.59e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 64.34 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 492 KPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLSKltgvcpQSNVQFD 571
Cdd:PRK15079 30 PPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAV------RSDIQMI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 572 F----------LTV----RENLRLF-AKIKGilpQEVDKEIQRVLLELEM-KNIQDVLAQNLSGGQKRKLtfGIA---IL 632
Cdd:PRK15079 104 FqdplaslnprMTIgeiiAEPLRTYhPKLSR---QEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRI--GIAralIL 178
|
170 180
....*....|....*....|....*....
gi 572882597 633 gDPQIFLLDEPTAGLDPFSRHQVWNLLKE 661
Cdd:PRK15079 179 -EPKLIICDEPVSALDVSIQAQVVNLLQQ 206
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1310-1507 |
1.92e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 62.68 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1310 SFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDA--------LEFlgycpQENALWPNLTVRQH-- 1379
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTppsrrpvsMLF-----QENNLFSHLTVAQNig 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1380 ------LEVYAAVKGLRKGDAE-VAITRLVDALKLQdqlkspvktLSEGIKRKL----CFVLSilgNPsVVLLDEPSTGM 1448
Cdd:PRK10771 94 lglnpgLKLNAAQREKLHAIARqMGIEDLLARLPGQ---------LSGGQRQRValarCLVRE---QP-ILLLDEPFSAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 572882597 1449 DPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKS 1507
Cdd:PRK10771 161 DPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1318-1507 |
1.97e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 63.58 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1318 VLGLLGHNGAGKSTSIKVITGDTKPTAG-----QVLLKGSG---GGDALEF---LGYCPQENALWPnLTVRQHleVYAAV 1386
Cdd:PRK14271 49 VTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSifnYRDVLEFrrrVGMLFQRPNPFP-MSIMDN--VLAGV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1387 KGLR-------KGDAEVAITR--LVDALKlqDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMW 1457
Cdd:PRK14271 126 RAHKlvprkefRGVAQARLTEvgLWDAVK--DRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIE 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 572882597 1458 QAIRATFRNTErgALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKS 1507
Cdd:PRK14271 204 EFIRSLADRLT--VIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
469-745 |
2.08e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.15 E-value: 2.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 469 QAPPEFQGKEAIRIRNVTKEYKGKPDKiEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSG-LSVPTKGSVTIYNNkl 547
Cdd:PLN03232 604 QNPPLQPGAPAISIKNGYFSWDSKTSK-PTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRGS-- 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 548 semadlenlsklTGVCPQSNVQFDfLTVRENLRLFAKI------KGI----LPQEVDKEIQRVLLELEMKNIqdvlaqNL 617
Cdd:PLN03232 681 ------------VAYVPQVSWIFN-ATVRENILFGSDFeserywRAIdvtaLQHDLDLLPGRDLTEIGERGV------NI 741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 618 SGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWN-LLKER---KTDRVILFSTQFMDeadiLADRKVFLSQGKL 693
Cdd:PLN03232 742 SGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDsCMKDElkgKTRVLVTNQLHFLP----LMDRIILVSEGMI 817
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 572882597 694 KCAG-------SSLFLKKKWGIGYHLSLQLNEICVEENITSL---VKQHIPDAKLSAKSEGK 745
Cdd:PLN03232 818 KEEGtfaelskSGSLFKKLMENAGKMDATQEVNTNDENILKLgptVTIDVSERNLGSTKQGK 879
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
482-648 |
2.27e-10 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 62.78 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 482 IRNVTKEYKGKPdkIeaLKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSV--PTKGSVTIYNNKLSEMaDLENLSKL 559
Cdd:COG0396 3 IKNLHVSVEGKE--I--LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILEL-SPDERARA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 tGV--CPQSNVQFDFLTVRENLRLFAKIKG---ILPQEVDKEIQRVLLELEMKniQDVLAQNL----SGGQKRKL-TFGI 629
Cdd:COG0396 78 -GIflAFQYPVEIPGVSVSNFLRTALNARRgeeLSAREFLKLLKEKMKELGLD--EDFLDRYVnegfSGGEKKRNeILQM 154
|
170
....*....|....*....
gi 572882597 630 AILgDPQIFLLDEPTAGLD 648
Cdd:COG0396 155 LLL-EPKLAILDETDSGLD 172
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1305-1542 |
2.78e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 62.83 E-value: 2.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1305 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGggdaleflgyCPQENALWpnltVRQHL---- 1380
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGRE----------VNAENEKW----VRSKVglvf 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1381 -----EVYAAV-----------KGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEP 1444
Cdd:PRK13647 86 qdpddQVFSSTvwddvafgpvnMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1445 STGMDPEGQQQMwQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGsiqhlkskfGKDYLLEMKVKNLAQ 1524
Cdd:PRK13647 166 MAYLDPRGQETL-MEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG---------DKSLLTDEDIVEQAG 235
|
250
....*....|....*....
gi 572882597 1525 VE-PLHAEILRLFPQAARQ 1542
Cdd:PRK13647 236 LRlPLVAQIFEDLPELGQS 254
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1279-1451 |
3.07e-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: 3.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1279 VIIASCLRKEYAGKrkgcfskrknkIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsggGDAL 1358
Cdd:TIGR03719 322 VIEAENLTKAFGDK-----------LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-----GETV 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1359 EfLGYCPQE-NALWPNLTVRQhlEVYAAVKGLRKGDAEVAITRLVDA--LKLQDQLKsPVKTLSEGIKRKLCFVLSILGN 1435
Cdd:TIGR03719 386 K-LAYVDQSrDALDPNKTVWE--EISGGLDIIKLGKREIPSRAYVGRfnFKGSDQQK-KVGQLSGGERNRVHLAKTLKSG 461
|
170
....*....|....*.
gi 572882597 1436 PSVVLLDEPSTGMDPE 1451
Cdd:TIGR03719 462 GNVLLLDEPTNDLDVE 477
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1305-1496 |
3.62e-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: 3.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1305 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGD------ALEFLGYCPQENALWPNLTVRQ 1378
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwqtakiMREAVAIVPEGRRVFSRMTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1379 HLevyaAVKGL--RKGDAEVAITRLVDAL-KLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQ 1455
Cdd:PRK11614 100 NL----AMGGFfaERDQFQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQ 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 572882597 1456 MWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1496
Cdd:PRK11614 176 IFDTIE-QLREQGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
499-693 |
4.25e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 64.25 E-value: 4.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 499 LKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLSklTGVCPQS-NVQFDFL---- 573
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLA--NGIVYISeDRKRDGLvlgm 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 574 TVREN-----LRLFAKIKGILPQevDKEIQRVLLELEMKNI----QDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPT 644
Cdd:PRK10762 346 SVKENmsltaLRYFSRAGGSLKH--ADEQQAVSDFIRLFNIktpsMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPT 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 572882597 645 AGLDPFSRHQVWNLLKERKTD--RVILFSTQfMDEADILADRKVFLSQGKL 693
Cdd:PRK10762 424 RGVDVGAKKEIYQLINQFKAEglSIILVSSE-MPEVLGMSDRILVMHEGRI 473
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1285-1481 |
4.45e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 62.02 E-value: 4.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1285 LRKEYAGKRkgcfskrknkiATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLL-----KGSGGGDALE 1359
Cdd:PRK11248 7 LYADYGGKP-----------ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLdgkpvEGPGAERGVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1360 FlgycpQENALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVV 1439
Cdd:PRK11248 76 F-----QNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 572882597 1440 LLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEA 1481
Cdd:PRK11248 151 LLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEA 192
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1308-1501 |
5.77e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 62.44 E-value: 5.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1308 NVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsggGDAL--------------EFLGYCPQ--ENALW 1371
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-----GDIVvsstskqkeikpvrKKVGVVFQfpESQLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1372 PNlTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQL--KSPVKtLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMD 1449
Cdd:PRK13643 99 EE-TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFweKSPFE-LSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 572882597 1450 PEGQQQMWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1501
Cdd:PRK13643 177 PKARIEMMQLFE-SIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGT 227
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1307-1496 |
7.47e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 61.47 E-value: 7.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1307 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITG--DTKPTA---GQVLLKGSG--GGDALEF---LGYCPQENALWPNLTV 1376
Cdd:PRK14247 20 DGVNLEIPDNTITALMGPSGSGKSTLLRVFNRliELYPEArvsGEVYLDGQDifKMDVIELrrrVQMVFQIPNPIPNLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1377 RQHLEVYAAVKGLRKGDAEVAiTRLVDALK-------LQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMD 1449
Cdd:PRK14247 100 FENVALGLKLNRLVKSKKELQ-ERVRWALEkaqlwdeVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLD 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 572882597 1450 PEGQQQmwqaIRATF--RNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1496
Cdd:PRK14247 179 PENTAK----IESLFleLKKDMTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1303-1508 |
7.94e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 61.96 E-value: 7.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1303 KIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQV-----LLKGSGGGDALEFL----GYCPQ--ENALW 1371
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVtigerVITAGKKNKKLKPLrkkvGIVFQfpEHQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1372 PNlTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQL--KSPVKtLSEGIKRKLCF--VLSIlgNPSVVLLDEPSTG 1447
Cdd:PRK13634 100 EE-TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELlaRSPFE-LSGGQMRRVAIagVLAM--EPEVLVLDEPTAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 572882597 1448 MDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSK 1508
Cdd:PRK13634 176 LDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFAD 236
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
509-655 |
1.07e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 60.96 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 509 GQITAILGHSGAGKSTLLNILSGLSVPTKGSVtIYNNKLSEMADLENLSKLTGVCPQSNVQFDFLTVRENLRLfakikGI 588
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEI-LLDAQPLESWSSKAFARKVAYLPQQLPAAEGMTVRELVAI-----GR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 589 LP-------------QEVDKEIQRVLLelemKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDpfSRHQV 655
Cdd:PRK10575 111 YPwhgalgrfgaadrEKVEEAISLVGL----KPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD--IAHQV 184
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1297-1496 |
1.12e-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: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1297 FSKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG---------------SGGGDALEFL 1361
Cdd:cd03248 21 YPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGkpisqyehkylhskvSLVGQEPVLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1362 GYCPQENALWpNLTVRQHLEVYAAVKglrKGDAEVAITRLvdALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLL 1441
Cdd:cd03248 101 ARSLQDNIAY-GLQSCSFECVKEAAQ---KAHAHSFISEL--ASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLIL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 572882597 1442 DEPSTGMDPEGQQQMWQAIRATfrNTERGALLTTHYMAEAEAVcDRVAIMVSGRL 1496
Cdd:cd03248 175 DEATSALDAESEQQVQQALYDW--PERRTVLVIAHRLSTVERA-DQILVLDGGRI 226
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
475-693 |
1.14e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 62.76 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 475 QGKEAIRIRNVTKEykgkpdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLE 554
Cdd:PRK15439 264 AGAPVLTVEDLTGE---------GFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 555 NLSK----------LTGVCPQSNVQFDFLTVRENLRLFAkikgILPQEVDKEIQRVLLELEMK-NIQDVLAQNLSGGQKR 623
Cdd:PRK15439 335 RLARglvylpedrqSSGLYLDAPLAWNVCALTHNRRGFW----IKPARENAVLERYRRALNIKfNHAEQAARTLSGGNQQ 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 572882597 624 KLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRV-ILFSTQFMDEADILADRKVFLSQGKL 693
Cdd:PRK15439 411 KVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVaVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1305-1521 |
1.37e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 61.18 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1305 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLL---KGSGGGDALEFLGYCPQENAL---WPNL---- 1374
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgdyAIPANLKKIKEVKRLRKEIGLvfqFPEYqlfq 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1375 -TVRQHLEVYAAVKGLRKGDAEVAITRLVDALKL-QDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEG 1452
Cdd:PRK13645 106 eTIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKG 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 572882597 1453 QQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSI------QHLKSKFGKD----YLLEMKVKN 1521
Cdd:PRK13645 186 EEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPfeifsnQELLTKIEIDppklYQLMYKLKN 264
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1307-1515 |
1.46e-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: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1307 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSgggDALEF--------LGYCPQENALWpNLTVRQ 1378
Cdd:cd03251 19 RDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGH---DVRDYtlaslrrqIGLVSQDVFLF-NDTVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1379 HLeVYAAvkgLRKGDAEV-AITRLVDAL----KLQDQLKSPVK----TLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMD 1449
Cdd:cd03251 95 NI-AYGR---PGATREEVeEAARAANAHefimELPEGYDTVIGergvKLSGGQRQRIAIARALLKDPPILILDEATSALD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 572882597 1450 PEGQQQMWQAIRATFRNteRGALLTTHYMAEAEAVcDRVAIMVSGRLRCIGSIQHLKSKFGKDYLL 1515
Cdd:cd03251 171 TESERLVQAALERLMKN--RTTFVIAHRLSTIENA-DRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
473-698 |
1.47e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 62.57 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 473 EFQGKEAIRIRNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKS-TLLNIL-----SGLSVPTKGSVTIYNNK 546
Cdd:PRK10261 6 ELDARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMrlleqAGGLVQCDKMLLRRRSR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 547 ----LSEM----------ADL-----ENLSKLTGVCPQSNvqfdflTVRENLRLFakiKGILPQEVDKEIQRVLLELEMK 607
Cdd:PRK10261 86 qvieLSEQsaaqmrhvrgADMamifqEPMTSLNPVFTVGE------QIAESIRLH---QGASREEAMVEAKRMLDQVRIP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 608 NIQDVLAQ---NLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLK--ERKTDRVILFSTQFMDEADILA 682
Cdd:PRK10261 157 EAQTILSRyphQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKvlQKEMSMGVIFITHDMGVVAEIA 236
|
250
....*....|....*.
gi 572882597 683 DRKVFLSQGKLKCAGS 698
Cdd:PRK10261 237 DRVLVMYQGEAVETGS 252
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1307-1476 |
1.65e-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: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1307 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITG--DTKPTAGQVLLkgsgggdaleflgycpQENALWPNLTVRQHLevya 1384
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDV----------------PDNQFGREASLIDAI---- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1385 avkgLRKGDAEVAITRLVDAlKLQDQ--LKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRA 1462
Cdd:COG2401 107 ----GRKGDFKDAVELLNAV-GLSDAvlWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQK 181
|
170
....*....|....
gi 572882597 1463 TFRNTERGALLTTH 1476
Cdd:COG2401 182 LARRAGITLVVATH 195
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
498-693 |
1.66e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.44 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 498 ALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLS----------KLTGVcpQSN 567
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINhgfalvteerRSTGI--YAY 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 568 VQFDFLTVRENLRLFAKIKGILPQE-VDKEIQRVLLELEMKN-IQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTA 645
Cdd:PRK10982 341 LDIGFNSLISNIRNYKNKVGLLDNSrMKSDTQWVIDSMRVKTpGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTR 420
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 572882597 646 GLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKL 693
Cdd:PRK10982 421 GIDVGAKFEIYQLIAElAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1307-1541 |
1.79e-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: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1307 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITgDTKPTAGQVLLKG-SGGGDALE----FLGYCPQENALWPNlTVRQHLE 1381
Cdd:TIGR01271 1236 QDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDGvSWNSVTLQtwrkAFGVIPQKVFIFSG-TFRKNLD 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1382 VYA--AVKGLRKGDAEVAITRLVDAL--KLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMW 1457
Cdd:TIGR01271 1314 PYEqwSDEEIWKVAEEVGLKSVIEQFpdKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIR 1393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1458 QAIRATFRNTErgALLTTHYMaEAEAVCDRVAIMVSGRLRCIGSIQ-------HLKSKFGkdyllemkvknlaqveplHA 1530
Cdd:TIGR01271 1394 KTLKQSFSNCT--VILSEHRV-EALLECQQFLVIEGSSVKQYDSIQkllnetsLFKQAMS------------------AA 1452
|
250
....*....|.
gi 572882597 1531 EILRLFPQAAR 1541
Cdd:TIGR01271 1453 DRLKLFPLHRR 1463
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1305-1505 |
1.98e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 60.41 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1305 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIK----VITGDTKPTAGQVLL------KGSGGGD---ALEFLGYCPQENALW 1371
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGSHIELLgrtvqrEGRLARDirkSRANTGYIFQQFNLV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1372 PNLTVRQHLEVYAA------------VKGLRKGDAEVAITRlVDALKLQDQlksPVKTLSEGIKRKLCFVLSILGNPSVV 1439
Cdd:PRK09984 99 NRLSVLENVLIGALgstpfwrtcfswFTREQKQRALQALTR-VGMVHFAHQ---RVSTLSGGQQQRVAIARALMQQAKVI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 572882597 1440 LLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL 1505
Cdd:PRK09984 175 LADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1307-1496 |
2.15e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 59.98 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1307 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGS-------GGGDALEF-----------LGYCPQEN 1368
Cdd:PRK10619 22 KGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQtinlvrdKDGQLKVAdknqlrllrtrLTMVFQHF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1369 ALWPNLTVRQH-LEVYAAVKGLRKGDAEVAITRLVDALKLQD--QLKSPVKtLSEGIKRKLCFVLSILGNPSVVLLDEPS 1445
Cdd:PRK10619 102 NLWSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIDEraQGKYPVH-LSGGQQQRVSIARALAMEPEVLLFDEPT 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 572882597 1446 TGMDPEgqqQMWQAIRATFRNTERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1496
Cdd:PRK10619 181 SALDPE---LVGEVLRIMQQLAEEGKtmVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1302-1534 |
2.38e-09 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 60.03 E-value: 2.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1302 NKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG---SGGGD-----ALEFLgycPQENALWPN 1373
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpiSMLSSrqlarRLALL---PQHHLTPEG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1374 LTVRQHLEV----YAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGiKRKLCFVLSILG-NPSVVLLDEPSTGM 1448
Cdd:PRK11231 91 ITVRELVAYgrspWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGG-QRQRAFLAMVLAqDTPVVLLDEPTTYL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1449 DPEGQQQMWQAIRAtfRNTERGALLTT-HYMAEAEAVCDRVAIMVSGRLRCIGSIQHLkskfgkdylleMKVKNLAQVEP 1527
Cdd:PRK11231 170 DINHQVELMRLMRE--LNTQGKTVVTVlHDLNQASRYCDHLVVLANGHVMAQGTPEEV-----------MTPGLLRTVFD 236
|
....*..
gi 572882597 1528 LHAEILR 1534
Cdd:PRK11231 237 VEAEIHP 243
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1308-1532 |
2.52e-09 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 60.87 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1308 NVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGS--GGGDALE-FLGYCPQENALWPNLTVRQHLEVYA 1384
Cdd:PRK10851 20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvSRLHARDrKVGFVFQHYALFRHMTVFDNIAFGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1385 AVKGLRKGDAEVAI----TRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAI 1460
Cdd:PRK10851 100 TVLPRRERPNAAAIkakvTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 572882597 1461 RATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFGKDYLLEMkvknLAQVEPLHAEI 1532
Cdd:PRK10851 180 RQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEF----MGEVNRLQGTI 247
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1305-1505 |
3.68e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 60.12 E-value: 3.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1305 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGdtkptagqvLLKGSG--GGDAL----EFLGYCPQE----------- 1367
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMG---------LLAANGriGGSATfngrEILNLPEKElnklraeqism 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1368 ------NALWPNLTV-RQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKS----PvKTLSEGIKRKLCFVLSILGNP 1436
Cdd:PRK09473 102 ifqdpmTSLNPYMRVgEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRmkmyP-HEFSGGMRQRVMIAMALLCRP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 572882597 1437 SVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL 1505
Cdd:PRK09473 181 KLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1305-1510 |
3.72e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 61.38 E-value: 3.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1305 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsGGGDALEFlgycpQENALWPNLT-VRQHLEVY 1383
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILL---NGQPIADY-----SEAALRQAISvVSQRVHLF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1384 AAV--KGLRKGDAEVAITRLVDALK---LQDQLKSPV----------KTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGM 1448
Cdd:PRK11160 427 SATlrDNLLLAAPNASDEALIEVLQqvgLEKLLEDDKglnawlgeggRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGL 506
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 572882597 1449 DPEGQQQMWQAIRATFRNteRGALLTTHYMAEAEAVcDRVAIMVSGRLRCIGSIQHLKSKFG 1510
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 ... |
1285-1451 |
4.11e-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: 4.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1285 LRKEYAGKRKgcfskrknkiATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgSGGGDalefLGYC 1364
Cdd:TIGR03719 10 VSKVVPPKKE----------ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP--QPGIK----VGYL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1365 PQENALWPNLTVRQHLEvyAAVKGLRKgdaevAITRL-------------VDAL-----KLQDQLKS------------- 1413
Cdd:TIGR03719 74 PQEPQLDPTKTVRENVE--EGVAEIKD-----ALDRFneisakyaepdadFDKLaaeqaELQEIIDAadawdldsqleia 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 572882597 1414 -----------PVKTLSEGIKRK--LCFVLsiLGNPSVVLLDEPSTGMDPE 1451
Cdd:TIGR03719 147 mdalrcppwdaDVTKLSGGERRRvaLCRLL--LSKPDMLLLDEPTNHLDAE 195
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1302-1501 |
5.12e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 58.91 E-value: 5.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1302 NKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITG-----DTK-PTAGQVLLKGSG--GGDALEF---LGYCPQENAL 1370
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRlieiyDSKiKVDGKVLYFGKDifQIDAIKLrkeVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1371 WPNLTVRQHLEVYAAVKGLR-----KGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPS 1445
Cdd:PRK14246 102 FPHLSIYDNIAYPLKSHGIKekreiKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 572882597 1446 TGMDPEGQQQMWQAIraTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1501
Cdd:PRK14246 182 SMIDIVNSQAIEKLI--TELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGS 235
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
480-691 |
5.47e-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: 5.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKPD-------------------KIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSG--LSVPTKG 538
Cdd:COG2401 8 FVLMRVTKVYSSVLDlservaivleafgvelrvvERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 539 SVTIYNNKL-SEMADLENLSKLTgvcpqsnvqfDFLTVRENLR---------LFAKIKgilpqevdkeiqrvllelemkn 608
Cdd:COG2401 88 CVDVPDNQFgREASLIDAIGRKG----------DFKDAVELLNavglsdavlWLRRFK---------------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 609 iqdvlaqNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDP-FSRHQVWNLLKE-RKTDRVILFSTQFMD-EADILADRK 685
Cdd:COG2401 136 -------ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRqTAKRVARNLQKLaRRAGITLVVATHHYDvIDDLQPDLL 208
|
....*.
gi 572882597 686 VFLSQG 691
Cdd:COG2401 209 IFVGYG 214
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
479-648 |
5.50e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.53 E-value: 5.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 479 AIRIRNVTKEYKgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMAdLENLSK 558
Cdd:PLN03232 1234 SIKFEDVHLRYR--PGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFG-LTDLRR 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 559 LTGVCPQSNVQFDFlTVRENLRLFAkikgilpQEVDKEIQRVlleLEMKNIQDVL--------------AQNLSGGQKRK 624
Cdd:PLN03232 1311 VLSIIPQSPVLFSG-TVRFNIDPFS-------EHNDADLWEA---LERAHIKDVIdrnpfgldaevsegGENFSVGQRQL 1379
|
170 180
....*....|....*....|....
gi 572882597 625 LTFGIAILGDPQIFLLDEPTAGLD 648
Cdd:PLN03232 1380 LSLARALLRRSKILVLDEATASVD 1403
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1300-1460 |
5.56e-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: 5.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1300 RKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGD-ALEFL----GYCPQENALWPNl 1374
Cdd:cd03249 13 RPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlNLRWLrsqiGLVSQEPVLFDG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1375 TVRQHLEvYaavkGLRKGDAEVAITRLVDA------LKLQDQLKSPV----KTLSEGIKRKLCFVLSILGNPSVVLLDEP 1444
Cdd:cd03249 92 TIAENIR-Y----GKPDATDEEVEEAAKKAnihdfiMSLPDGYDTLVgergSQLSGGQKQRIAIARALLRNPKILLLDEA 166
|
170
....*....|....*.
gi 572882597 1445 STGMDPEGQQQMWQAI 1460
Cdd:cd03249 167 TSALDAESEKLVQEAL 182
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
504-648 |
6.03e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 60.73 E-value: 6.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 504 FDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVtIYNNKLSeMADLENlskltgvCPQSNVQ---FDFLT-----V 575
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRI-IYEQDLI-VARLQQ-------DPPRNVEgtvYDFVAegieeQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 576 RENLRLFAKIKGILPQEVD----KEIQRVLLELEMKN-------IQDVLAQ----------NLSGGQKRKLTFGIAILGD 634
Cdd:PRK11147 95 AEYLKRYHDISHLVETDPSeknlNELAKLQEQLDHHNlwqlenrINEVLAQlgldpdaalsSLSGGWLRKAALGRALVSN 174
|
170
....*....|....
gi 572882597 635 PQIFLLDEPTAGLD 648
Cdd:PRK11147 175 PDVLLLDEPTNHLD 188
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1309-1501 |
6.10e-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: 6.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1309 VSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsgGGDALEF----------------------LGYCPQ 1366
Cdd:COG4598 27 VSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRV----GGEEIRLkpdrdgelvpadrrqlqrirtrLGMVFQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1367 ENALWPNLTVRQHL-EVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEG------IKRKLCFvlsilgNPSVV 1439
Cdd:COG4598 103 SFNLWSHMTVLENViEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGqqqraaIARALAM------EPEVM 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 572882597 1440 LLDEPSTGMDPEGQQQMWQAIRATfrnTERGA--LLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1501
Cdd:COG4598 177 LFDEPTSALDPELVGEVLKVMRDL---AEEGRtmLVVTHEMGFARDVSSHVVFLHQGRIEEQGP 237
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1307-1495 |
6.30e-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: 6.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1307 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGG----DALEF---------LGYCPQenalwpN 1373
Cdd:COG4778 28 DGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWvdlaQASPReilalrrrtIGYVSQ------F 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1374 LTV--RQH-LEVYAAVkGLRKG-DAEVAITR---LVDALKLQDQLKS-PVKTLSEGIKRKLCFVLSILGNPSVVLLDEPS 1445
Cdd:COG4778 102 LRVipRVSaLDVVAEP-LLERGvDREEARARareLLARLNLPERLWDlPPATFSGGEQQRVNIARGFIADPPLLLLDEPT 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 572882597 1446 TGMDPEGQQ---QMWQAIRAtfrnteRG-ALLT-THYMAEAEAVCDRVAIMVSGR 1495
Cdd:COG4778 181 ASLDAANRAvvvELIEEAKA------RGtAIIGiFHDEEVREAVADRVVDVTPFS 229
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1300-1496 |
6.91e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 58.68 E-value: 6.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1300 RKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGD-TKPTA-------GQVLLKGS--GGGDALEFL---GYCPQ 1366
Cdd:PRK13547 11 RRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDlTGGGAprgarvtGDVTLNGEplAAIDAPRLArlrAVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1367 ENALWPNLTVRQ--------HLEVYAAVKGLRKGDAEVAITRL-VDALKLQDqlkspVKTLSEGIKRKLCF--VLSIL-- 1433
Cdd:PRK13547 91 AAQPAFAFSAREivllgrypHARRAGALTHRDGEIAWQALALAgATALVGRD-----VTTLSGGELARVQFarVLAQLwp 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 572882597 1434 -----GNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1496
Cdd:PRK13547 166 phdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAI 233
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
479-648 |
7.09e-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: 7.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 479 AIRIRNVTKEYKGkpDKIeALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEM--ADLENl 556
Cdd:PRK10790 340 RIDIDNVSFAYRD--DNL-VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLshSVLRQ- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 557 skltGVcpqSNVQFDFLTVRENlrLFAKI---KGILPQEVDKEIQRVLLELEMKNIQDVL-------AQNLSGGQKRKLT 626
Cdd:PRK10790 416 ----GV---AMVQQDPVVLADT--FLANVtlgRDISEEQVWQALETVQLAELARSLPDGLytplgeqGNNLSVGQKQLLA 486
|
170 180
....*....|....*....|..
gi 572882597 627 FGIAILGDPQIFLLDEPTAGLD 648
Cdd:PRK10790 487 LARVLVQTPQILILDEATANID 508
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1297-1496 |
7.46e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 58.25 E-value: 7.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1297 FSKRKnkiATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVIT--GDTKP---TAGQVLLKG----SGGGDALEF---LGYC 1364
Cdd:PRK14239 15 YNKKK---ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPevtITGSIVYNGhniySPRTDTVDLrkeIGMV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1365 PQENALWPnltvrqhLEVYA-AVKGLR-KG--DAEVAITRLVDALK-------LQDQLKSPVKTLSEGIKRKLCFVLSIL 1433
Cdd:PRK14239 92 FQQPNPFP-------MSIYEnVVYGLRlKGikDKQVLDEAVEKSLKgasiwdeVKDRLHDSALGLSGGQQQRVCIARVLA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 572882597 1434 GNPSVVLLDEPSTGMDPEGQQQmwqaIRATFRNTERG--ALLTTHYMAEAEAVCDRVAIMVSGRL 1496
Cdd:PRK14239 165 TSPKIILLDEPTSALDPISAGK----IEETLLGLKDDytMLLVTRSMQQASRISDRTGFFLDGDL 225
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
504-693 |
9.27e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 59.92 E-value: 9.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 504 FDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLSKLTGVCPQSNVQ---FDFLTVRENL- 579
Cdd:PRK11288 274 FSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMLCPEDRKAegiIPVHSVADNIn 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 580 ----RLFAKIKGIL--PQE---VDKEIQRVllelemkNIQ----DVLAQNLSGGQKRKltfgiAILG-----DPQIFLLD 641
Cdd:PRK11288 354 isarRHHLRAGCLInnRWEaenADRFIRSL-------NIKtpsrEQLIMNLSGGNQQK-----AILGrwlseDMKVILLD 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 572882597 642 EPTAGLDPFSRHQVWNLLKE-RKTDRVILFSTQFMDEADILADRKVFLSQGKL 693
Cdd:PRK11288 422 EPTRGIDVGAKHEIYNVIYElAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1308-1496 |
9.39e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 57.80 E-value: 9.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1308 NVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSG--GGDALEFL-----GYCPQENALWPNLTVrqhL 1380
Cdd:PRK09493 19 NIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKvnDPKVDERLirqeaGMVFQQFYLFPHLTA---L 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1381 EVYA----AVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQM 1456
Cdd:PRK09493 96 ENVMfgplRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEV 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 572882597 1457 WQAIRATfrnTERG--ALLTTHYMAEAEAVCDRVAIMVSGRL 1496
Cdd:PRK09493 176 LKVMQDL---AEEGmtMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1303-1522 |
1.02e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 58.27 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1303 KIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGdtkptagqVLLKGSGGGDALEFLGYCPQENALWpnlTVRQHLE- 1381
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLING--------LLLPDDNPNSKITVDGITLTAKTVW---DIREKVGi 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1382 ---------VYAAV----------KGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCfVLSILG-NPSVVLL 1441
Cdd:PRK13640 89 vfqnpdnqfVGATVgddvafglenRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVA-IAGILAvEPKIIIL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1442 DEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEA-----VCDRVAIMVSGRLRCIGSIQHLKSKFGKDYLLE 1516
Cdd:PRK13640 168 DESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMadqvlVLDDGKLLAQGSPVEIFSKVEMLKEIGLDIPFV 247
|
....*.
gi 572882597 1517 MKVKNL 1522
Cdd:PRK13640 248 YKLKNK 253
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
511-693 |
1.08e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 58.18 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 511 ITAILGHSGAGKSTLLNILSGLSVPTKG-----SVTIYNNKLSEMADLENLSKLTGVCPQSNVQFDfLTVRENLRLFAKI 585
Cdd:PRK14271 49 VTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVLEFRRRVGMLFQRPNPFP-MSIMDNVLAGVRA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 586 KGILP-QEVDKEIQRVLLELEMKN-IQDVLAQN---LSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLK 660
Cdd:PRK14271 128 HKLVPrKEFRGVAQARLTEVGLWDaVKDRLSDSpfrLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIR 207
|
170 180 190
....*....|....*....|....*....|...
gi 572882597 661 ERKTDRVILFSTQFMDEADILADRKVFLSQGKL 693
Cdd:PRK14271 208 SLADRLTVIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1308-1495 |
1.10e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 59.72 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1308 NVSFCVRKGEVLGLLGHNGAGKS-TSIKVI-----------TGDTKpTAGQVLLKGS--------GGGDALEFlgycpQE 1367
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSvTALSILrllpsppvvypSGDIR-FHGESLLHASeqtlrgvrGNKIAMIF-----QE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1368 N--ALWPNLTVRQHL-EVYAAVKGLRKGDAEVAITRLVDALKLQD---QLKSPVKTLSEGIKRKLCFVLSILGNPSVVLL 1441
Cdd:PRK15134 101 PmvSLNPLHTLEKQLyEVLSLHRGMRREAARGEILNCLDRVGIRQaakRLTDYPHQLSGGERQRVMIAMALLTRPELLIA 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 572882597 1442 DEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1495
Cdd:PRK15134 181 DEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1316-1496 |
1.24e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 57.77 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1316 GEVLGLLGHNGAGKSTSIKVITGDTKPTAGQvLLKGSGG-GDALEFLGYCPQENALWPNLTVRQHLEVyaavkGLrKGDA 1394
Cdd:PRK11247 38 GQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-LLAGTAPlAEAREDTRLMFQDARLLPWKKVIDNVGL-----GL-KGQW 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1395 EVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLT 1474
Cdd:PRK11247 111 RDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLV 190
|
170 180
....*....|....*....|..
gi 572882597 1475 THYMAEAEAVCDRVAIMVSGRL 1496
Cdd:PRK11247 191 THDVSEAVAMADRVLLIEEGKI 212
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1307-1476 |
1.27e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 60.24 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1307 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGdtKPTAGQVL--LKGSGGGDALEFL----GYCPQENALWPNLTVRQHL 1380
Cdd:PLN03140 897 REVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEgdIRISGFPKKQETFarisGYCEQNDIHSPQVTVRESL 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1381 eVYAAVKGLRKGDAEVAITRLVDA---LKLQDQLKSP------VKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1451
Cdd:PLN03140 975 -IYSAFLRLPKEVSKEEKMMFVDEvmeLVELDNLKDAivglpgVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDAR 1053
|
170 180
....*....|....*....|....*
gi 572882597 1452 GQQQMWQAIRATFrNTERGALLTTH 1476
Cdd:PLN03140 1054 AAAIVMRTVRNTV-DTGRTVVCTIH 1077
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1320-1451 |
1.28e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 59.36 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1320 GLLGHNGAGKSTSIKVITGDTKPTAGQ-VLLKGSGggdalefLGYCPQENALWPNLTVRQHLEvyAAVkglrkGDAEVAI 1398
Cdd:PRK11819 37 GVLGLNGAGKSTLLRIMAGVDKEFEGEaRPAPGIK-------VGYLPQEPQLDPEKTVRENVE--EGV-----AEVKAAL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1399 TRL-------------VDAL-----KLQDQLKS------------------------PVKTLSEGIKRK--LCFVLsiLG 1434
Cdd:PRK11819 103 DRFneiyaayaepdadFDALaaeqgELQEIIDAadawdldsqleiamdalrcppwdaKVTKLSGGERRRvaLCRLL--LE 180
|
170
....*....|....*..
gi 572882597 1435 NPSVVLLDEPSTGMDPE 1451
Cdd:PRK11819 181 KPDMLLLDEPTNHLDAE 197
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1309-1497 |
1.38e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 57.10 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1309 VSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSG-------GGDAL--EFLGYCPQENALWPNLTVRQH 1379
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPlhqmdeeARAKLraKHVGFVFQSFMLIPTLNALEN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1380 LEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQA 1459
Cdd:PRK10584 109 VELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADL 188
|
170 180 190
....*....|....*....|....*....|....*...
gi 572882597 1460 IRATFRNTERGALLTTHYMAEAeAVCDRVAIMVSGRLR 1497
Cdd:PRK10584 189 LFSLNREHGTTLILVTHDLQLA-ARCDRRLRLVNGQLQ 225
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1307-1496 |
1.48e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 59.29 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1307 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGS-----GGGDALEF-LGYCPQEnalwpnltvRQ-- 1378
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKeinalSTAQRLARgLVYLPED---------RQss 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1379 --HLE------VYAAVKGLR----KGDAEVAI-TRLVDALKLQ-DQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEP 1444
Cdd:PRK15439 351 glYLDaplawnVCALTHNRRgfwiKPARENAVlERYRRALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 572882597 1445 STGMDPEGQQQMWQAIRA-TFRNTerGALLTTHYMAEAEAVCDRVAIMVSGRL 1496
Cdd:PRK15439 431 TRGVDVSARNDIYQLIRSiAAQNV--AVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1316-1460 |
1.51e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 59.41 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1316 GEVLGLLGHNGAGKSTSIKVITGDTKPTAGQV-LLKGSGGG----DALEFLGycPQENALwpnltvrQHLEVYAavkglr 1390
Cdd:PRK10636 338 GSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGyfaqHQLEFLR--ADESPL-------QHLARLA------ 402
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 572882597 1391 KGDAEVAITRLVDALKLQ-DQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAI 1460
Cdd:PRK10636 403 PQELEQKLRDYLGGFGFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEAL 473
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1308-1494 |
1.74e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 57.45 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1308 NVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLlkgsgggdaleFLGYCPQENalwpNLT-VRQHLEV---- 1382
Cdd:PRK13648 27 DVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIF-----------YNNQAITDD----NFEkLRKHIGIvfqn 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1383 -----------YAAVKGLRK-----GDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPST 1446
Cdd:PRK13648 92 pdnqfvgsivkYDVAFGLENhavpyDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATS 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 572882597 1447 GMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAeAVCDRVAIMVSG 1494
Cdd:PRK13648 172 MLDPDARQNLLDLVRKVKSEHNITIISITHDLSEA-MEADHVIVMNKG 218
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1305-1519 |
1.86e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.86 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1305 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG-----SGGGDALEF-LGYCPQENALWPNLTVRQ 1378
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGkevtfNGPKSSQEAgIGIIHQELNLIPQLTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1379 HL----EVYAAVKGL--RKGDAEVaiTRLVDALKLQDQLKSPVKTLSEG------IKRKLCFvlsilgNPSVVLLDEPST 1446
Cdd:PRK10762 99 NIflgrEFVNRFGRIdwKKMYAEA--DKLLARLNLRFSSDKLVGELSIGeqqmveIAKVLSF------ESKVIIMDEPTD 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 572882597 1447 GMDPEGQQQMWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLrcIGsiQHLKSKFGKDYLLEMKV 1519
Cdd:PRK10762 171 ALTDTETESLFRVIR-ELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQF--IA--EREVADLTEDSLIEMMV 238
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1309-1496 |
1.92e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 57.41 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1309 VSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGS-----GGGDALEFLGYCPQE-NALWPNLTVRQHLEV 1382
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGElltaeNVWNLRRKIGMVFQNpDNQFVGATVEDDVAF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1383 YAAVKGLRKgdaEVAITRLVDAL----KLQDQLKSPVKtLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQ 1458
Cdd:PRK13642 106 GMENQGIPR---EEMIKRVDEALlavnMLDFKTREPAR-LSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMR 181
|
170 180 190
....*....|....*....|....*....|....*...
gi 572882597 1459 AIRATFRNTERGALLTTHYMAEAeAVCDRVAIMVSGRL 1496
Cdd:PRK13642 182 VIHEIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEI 218
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
502-648 |
2.00e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 56.86 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 502 LVFDIYEGQITAILGHSGAGKSTLLNILSGLSvPTKGSVTIYNNKLSEMaDLENLSKLTG-VCPQSNVQFDfLTVRENLR 580
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAW-SAAELARHRAyLSQQQTPPFA-MPVFQYLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 581 LFakikgiLPQEVDK-EIQRVLLEL-EMKNIQDVLA---QNLSGGQKRKLTFGIAIL-----GDP--QIFLLDEPTAGLD 648
Cdd:PRK03695 92 LH------QPDKTRTeAVASALNEVaEALGLDDKLGrsvNQLSGGEWQRVRLAAVVLqvwpdINPagQLLLLDEPMNSLD 165
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1307-1500 |
2.08e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 57.16 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1307 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITG--DTKPTA---GQVLLKG----SGGGDALEF---LGYCPQENALWPNL 1374
Cdd:PRK14267 21 KGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRllELNEEArveGEVRLFGrniySPDVDPIEVrreVGMVFQYPNPFPHL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1375 TVRQHLEVYAAVKGLRKGDAEVAiTRLVDALK-------LQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTG 1447
Cdd:PRK14267 101 TIYDNVAIGVKLNGLVKSKKELD-ERVEWALKkaalwdeVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTAN 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 572882597 1448 MDPEGQQQMWQAIRATfrNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1500
Cdd:PRK14267 180 IDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVG 230
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
467-648 |
2.17e-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: 59.03 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 467 FEQAPP--EFQGKEAIRIRNVTKEYKGKPDKIEAlkdlvFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIyN 544
Cdd:COG1245 327 FEVHAPrrEKEEETLVEYPDLTKSYGGFSLEVEG-----GEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDE-D 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 545 NKLSemadlenlSKltgvcPQSnVQFDF-LTVRENLRlfAKIKGILPqevDKEIQRVLLE-LEMKNIQDVLAQNLSGGQK 622
Cdd:COG1245 401 LKIS--------YK-----PQY-ISPDYdGTVEEFLR--SANTDDFG---SSYYKTEIIKpLGLEKLLDKNVKDLSGGEL 461
|
170 180
....*....|....*....|....*.
gi 572882597 623 RKLTFGIAILGDPQIFLLDEPTAGLD 648
Cdd:COG1245 462 QRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1306-1500 |
2.31e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 58.12 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1306 TRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGD---ALEFLGYCPQENALWPNLTVRQHLEV 1382
Cdd:PRK11000 19 SKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDvppAERGVGMVFQSYALYPHLSVAENMSF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1383 YAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRA 1462
Cdd:PRK11000 99 GLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISR 178
|
170 180 190
....*....|....*....|....*....|....*...
gi 572882597 1463 TFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1500
Cdd:PRK11000 179 LHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1298-1496 |
2.84e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 57.55 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1298 SKRKNKI-ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDALEFLGYCPQENA------- 1369
Cdd:PRK13631 33 EKQENELvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELITNPYSkkiknfk 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1370 ----------LWPNL-----TVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQL--KSPVKtLSEGIKRKLCF--VL 1430
Cdd:PRK13631 113 elrrrvsmvfQFPEYqlfkdTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSYleRSPFG-LSGGQKRRVAIagIL 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 572882597 1431 SIlgNPSVVLLDEPSTGMDPEGQQQMWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1496
Cdd:PRK13631 192 AI--QPEILIFDEPTAGLDPKGEHEMMQLIL-DAKANNKTVFVITHTMEHVLEVADEVIVMDKGKI 254
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1305-1496 |
3.03e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 57.10 E-value: 3.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1305 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsgggDALEF---------------LGYCPQ--E 1367
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTV------DDITIthktkdkyirpvrkrIGMVFQfpE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1368 NALWPNLTVRqhlEVYAAVKGLRKGDAEVAitrlVDALKLQDQL--------KSPVKtLSEGIKRKLCFVlSILG-NPSV 1438
Cdd:PRK13646 96 SQLFEDTVER---EIIFGPKNFKMNLDEVK----NYAHRLLMDLgfsrdvmsQSPFQ-MSGGQMRKIAIV-SILAmNPDI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 572882597 1439 VLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1496
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) ... |
508-683 |
3.21e-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: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 508 EGQITAILGHSGAGKSTLLNILSGLSVPtkgsvtiynnklsemadleNLSKLtgvcpQSNVQFDflTVRENLR------L 581
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKP-------------------NLGKF-----DDPPDWD--EILDEFRgselqnY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 582 FAKIKG------ILPQEVDkEIQRV-------LLE--------------LEMKNIQDVLAQNLSGGQKRKLTFGIAILGD 634
Cdd:cd03236 79 FTKLLEgdvkviVKPQYVD-LIPKAvkgkvgeLLKkkdergkldelvdqLELRHVLDRNIDQLSGGELQRVAIAAALARD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 572882597 635 PQIFLLDEPTAGLDPFSRHQVWNLLKER-KTDRVILFSTQFMDEADILAD 683
Cdd:cd03236 158 ADFYFFDEPSSYLDIKQRLNAARLIRELaEDDNYVLVVEHDLAVLDYLSD 207
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
494-648 |
4.37e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 56.19 E-value: 4.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 494 DKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSG---LSVpTKGSVTIYNNKLSEMaDLENLSKL----------- 559
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpaYKI-LEGDILFKGESILDL-EPEERAHLgiflafqypie 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 -TGVcpqSNVqfDFLTVRENLRL-FAKIKGILPQEVDKEIQRVLLELEMKniQDVLAQNL----SGGQKRKLTFGIAILG 633
Cdd:CHL00131 96 iPGV---SNA--DFLRLAYNSKRkFQGLPELDPLEFLEIINEKLKLVGMD--PSFLSRNVnegfSGGEKKRNEILQMALL 168
|
170
....*....|....*
gi 572882597 634 DPQIFLLDEPTAGLD 648
Cdd:CHL00131 169 DSELAILDETDSGLD 183
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
462-662 |
4.50e-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: 4.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 462 SFHDSFEQAPPEFQGKEAIR--------IRNVTKEykgKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLS 533
Cdd:COG4178 337 GFEEALEAADALPEAASRIEtsedgalaLEDLTLR---TPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLW 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 534 VPTKGSVTIynNKLSEMADLenlskltgvcPQSNvqfdFL---TVRENLrlfakikgILPQEV----DKEIQRVL----L 602
Cdd:COG4178 414 PYGSGRIAR--PAGARVLFL----------PQRP----YLplgTLREAL--------LYPATAeafsDAELREALeavgL 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 572882597 603 E--LEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKER 662
Cdd:COG4178 470 GhlAERLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREE 531
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
476-694 |
4.58e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 57.63 E-value: 4.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 476 GKEAIRIRNVTKEYKGKPdKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGlSVPTK--GSVTIYNNKLSEMADL 553
Cdd:PRK13549 256 GEVILEVRNLTAWDPVNP-HIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFG-AYPGRweGEIFIDGKPVKIRNPQ 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 554 ENLS----------KLTGVCPQSNVQFDFLTVreNLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLA-QNLSGGQK 622
Cdd:PRK13549 334 QAIAqgiamvpedrKRDGIVPVMGVGKNITLA--ALDRFTGGSRIDDAAELKTILESIQRLKVKTASPELAiARLSGGNQ 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 572882597 623 RKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQfMDEADILADRKVFLSQGKLK 694
Cdd:PRK13549 412 QKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQlvQQGVAIIVISSE-LPEVLGLSDRVLVMHEGKLK 484
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
482-648 |
4.69e-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: 4.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 482 IRNVTKEYkgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGsvtiynnklsEMADLENLSklTG 561
Cdd:TIGR03719 7 MNRVSKVV---PPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG----------EARPQPGIK--VG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 562 VCPQSNVQFDFLTVRENLRL-FAKIKGIL-------------PQEVDK------EIQRVL-----------LELEMKNIQ 610
Cdd:TIGR03719 72 YLPQEPQLDPTKTVRENVEEgVAEIKDALdrfneisakyaepDADFDKlaaeqaELQEIIdaadawdldsqLEIAMDALR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 572882597 611 ----DVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLD 648
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) ... |
1313-1461 |
5.26e-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: 5.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1313 VRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDALEFLGYCPQ-------ENALWPNLTVRQHLEVYAA 1385
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDEILDEFRGSELQnyftkllEGDVKVIVKPQYVDLIPKA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1386 VKG-----LRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAI 1460
Cdd:cd03236 103 VKGkvgelLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLI 182
|
.
gi 572882597 1461 R 1461
Cdd:cd03236 183 R 183
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
471-542 |
5.43e-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: 5.43e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 572882597 471 PPEFQGKEAIRIRNVTKEYKGKPdkieALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTI 542
Cdd:TIGR03719 314 PGPRLGDKVIEAENLTKAFGDKL----LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI 381
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
492-693 |
5.60e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 57.93 E-value: 5.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 492 KPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGL---SVPTKGSVTIYNNKLSEMADlenlSKLTGVCPQSNV 568
Cdd:PLN03140 174 KKTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKldpSLKVSGEITYNGYRLNEFVP----RKTSAYISQNDV 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 569 QFDFLTVRENLRLFAKIKG-------------------ILPQ-EVDKEIQRVLLELEMKN-------------------I 609
Cdd:PLN03140 250 HVGVMTVKETLDFSARCQGvgtrydllselarrekdagIFPEaEVDLFMKATAMEGVKSSlitdytlkilgldickdtiV 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 610 QDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFS-TQFMDEADILADRKV 686
Cdd:PLN03140 330 GDEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQivHLTEATVLMSlLQPAPETFDLFDDII 409
|
....*..
gi 572882597 687 FLSQGKL 693
Cdd:PLN03140 410 LLSEGQI 416
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
468-648 |
6.18e-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: 6.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 468 EQAPPE-FQGKEAIRIRNVTKEYKgkPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNK 546
Cdd:TIGR00957 1272 ETAPPSgWPPRGRVEFRNYCLRYR--EDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLN 1349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 547 LSEMAdLENL-SKLTgVCPQSNVQFDFlTVRENLRLFAkikgilpQEVDKEiqrVLLELEMKNIQDVLA----------- 614
Cdd:TIGR00957 1350 IAKIG-LHDLrFKIT-IIPQDPVLFSG-SLRMNLDPFS-------QYSDEE---VWWALELAHLKTFVSalpdkldheca 1416
|
170 180 190
....*....|....*....|....*....|....*..
gi 572882597 615 ---QNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLD 648
Cdd:TIGR00957 1417 eggENLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1453
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1293-1500 |
6.76e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.17 E-value: 6.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1293 RKGCFSKRKNKI-ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG------SGGG-----DALEF 1360
Cdd:PRK10261 326 RSGLLNRVTREVhAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqridtlSPGKlqalrRDIQF 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1361 LGYCPQEnALWPNLTVRQHLEVYAAVKGLRKGDAEVA-ITRLVD--ALKLQDQLKSPvKTLSEGIKRKLCFVLSILGNPS 1437
Cdd:PRK10261 406 IFQDPYA-SLDPRQTVGDSIMEPLRVHGLLPGKAAAArVAWLLErvGLLPEHAWRYP-HEFSGGQRQRICIARALALNPK 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 572882597 1438 VVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1500
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 ... |
1313-1490 |
7.78e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 54.12 E-value: 7.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1313 VRKGEVLGLLGHNGAGKSTSIKVITGDTKPTagqvllkgsgggdaleflgycpQENALWPNLTVrqhleVYaavkglrkg 1392
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPN----------------------GDNDEWDGITP-----VY--------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1393 daevaitrlvdalklqdqlKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGAL 1472
Cdd:cd03222 66 -------------------KPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTAL 126
|
170
....*....|....*...
gi 572882597 1473 LTTHYMAEAEAVCDRVAI 1490
Cdd:cd03222 127 VVEHDLAVLDYLSDRIHV 144
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1308-1497 |
8.24e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 56.76 E-value: 8.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1308 NVSFCVRKGEVLGLLGHNGAGKSTSIKVITG------------DTKPTAGQVLLKGSGGGDALeflgyCPQE---NALWP 1372
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGaypgkfegnvfiNGKPVDIRNPAQAIRAGIAM-----VPEDrkrHGIVP 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1373 NLTVRQH--LEVYAAVKGLRKGDAEV---AITRLVDALKLQDQLKS-PVKTLSEGIKRKLCFVLSILGNPSVVLLDEPST 1446
Cdd:TIGR02633 353 ILGVGKNitLSVLKSFCFKMRIDAAAelqIIGSAIQRLKVKTASPFlPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 572882597 1447 GMDPEGQQQMWQAIRATFRnteRGA--LLTTHYMAEAEAVCDRVAIMVSGRLR 1497
Cdd:TIGR02633 433 GVDVGAKYEIYKLINQLAQ---EGVaiIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
401-673 |
8.38e-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: 55.86 E-value: 8.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 401 TNFMLAFDTCLYLALAIYFEKILPNEYGHRRPPLFFL-------KSSFWSQTQKTDHVALEDEMDADPSFHDSFEQAPPE 473
Cdd:pfam13304 13 SNLLEALRFLADFDALVIGLTDERSRNGGIGGIPSLLngidpkePIEFEISEFLEDGVRYRYGLDLEREDVEEKLSSKPT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 474 FQGKEAIRIRNVTKEYKGKPDKIEALKDLVFDIYEGQITAIL---GHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEM 550
Cdd:pfam13304 93 LLEKRLLLREDSEEREPKFPPEAEELRLGLDVEERIELSLSElsdLISGLLLLSIISPLSFLLLLDEGLLLEDWAVLDLA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 551 ADLENLSKLTGVCPQSNVQFDFLTVRENLRLFAKIKGILpqEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIA 630
Cdd:pfam13304 173 ADLALFPDLKELLQRLVRGLKLADLNLSDLGEGIEKSLL--VDDRLRERGLILLENGGGGELPAFELSDGTKRLLALLAA 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 572882597 631 ILGDPQ---IFLLDEPTAGLDPFSRHQVWNLLKERKTDRV-ILFSTQ 673
Cdd:pfam13304 251 LLSALPkggLLLIDEPESGLHPKLLRRLLELLKELSRNGAqLILTTH 297
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1307-1511 |
8.53e-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: 8.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1307 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDT----KPTAGQVLLKGSGGGDALEF----LGYCPQENALWPNLTVRQ 1378
Cdd:TIGR00956 78 KPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTdgfhIGVEGVITYDGITPEEIKKHyrgdVVYNAETDVHFPHLTVGE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1379 HLEVYAAVKGlrKGDAEVAITRLVDALKLQDQLKSP---------------VKTLSEGIKRKLCFVLSILGNPSVVLLDE 1443
Cdd:TIGR00956 158 TLDFAARCKT--PQNRPDGVSREEYAKHIADVYMATyglshtrntkvgndfVRGVSGGERKRVSIAEASLGGAKIQCWDN 235
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1444 PSTGMDPEGQQQMWQAIRATFRNTERGALLTThYMAEAEA--VCDRVAIMVSGRLRCIGSIQHLKSKFGK 1511
Cdd:TIGR00956 236 ATRGLDSATALEFIRALKTSANILDTTPLVAI-YQCSQDAyeLFDKVIVLYEGYQIYFGPADKAKQYFEK 304
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1307-1495 |
8.77e-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: 8.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1307 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSgggdalefLGYCPQENalW-PNLTVRQHL----- 1380
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--------IAYVSQEP--WiQNGTIRENIlfgkp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1381 ---EVYAAVkglrkgdaevaitrlVDALKLQDQLKSPVK-----------TLSEGIKRKLCFVLSILGNPSVVLLDEPST 1446
Cdd:cd03250 92 fdeERYEKV---------------IKACALEPDLEILPDgdlteigekgiNLSGGQKQRISLARAVYSDADIYLLDDPLS 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 572882597 1447 GMDPE-GQQQMWQAIRATFRNtERGALLTTHYMAEAEAvCDRVAIMVSGR 1495
Cdd:cd03250 157 AVDAHvGRHIFENCILGLLLN-NKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1307-1514 |
8.79e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 55.03 E-value: 8.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1307 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITG--DTKPTAGQVLLKGSgggDALEFLgycPQEnalwpnltvRQHLEVYA 1384
Cdd:CHL00131 24 KGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGE---SILDLE---PEE---------RAHLGIFL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1385 A------VKGLRKGDaevaITRLVDALKLQDQLKSPVKTLS--EGIKRKLCFV------LS------------------- 1431
Cdd:CHL00131 89 AfqypieIPGVSNAD----FLRLAYNSKRKFQGLPELDPLEflEIINEKLKLVgmdpsfLSrnvnegfsggekkrneilq 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1432 -ILGNPSVVLLDEPSTGMDPEGQQQMWQAIRaTFRNTERGALLTTHYMAEAEAVC-DRVAIMVSGRLRCIGSIQ--HLKS 1507
Cdd:CHL00131 165 mALLDSELAILDETDSGLDIDALKIIAEGIN-KLMTSENSIILITHYQRLLDYIKpDYVHVMQNGKIIKTGDAElaKELE 243
|
....*..
gi 572882597 1508 KFGKDYL 1514
Cdd:CHL00131 244 KKGYDWL 250
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1307-1484 |
8.90e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 57.04 E-value: 8.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1307 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSG----GGDAL-----EFLGYCPQENALWPNLTVR 1377
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDvatlDADALaqlrrEHFGFIFQRYHLLSHLTAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1378 QHLEVYAAVKGL----RKGDAEVAITRlvdaLKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPE-G 1452
Cdd:PRK10535 105 QNVEVPAVYAGLerkqRLLRAQELLQR----LGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHsG 180
|
170 180 190
....*....|....*....|....*....|....*
gi 572882597 1453 QQQMwqAIRATFRNTERGALLTTH---YMAEAEAV 1484
Cdd:PRK10535 181 EEVM--AILHQLRDRGHTVIIVTHdpqVAAQAERV 213
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1316-1449 |
9.81e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 56.81 E-value: 9.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1316 GEVLGLLGHNGAGKSTSIKVITGDTKPT--AGQVLLKGSG-GGDALEFLGYCPQENALWPNLTVRQHLeVYAAVKGLRKG 1392
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKpTKQILKRTGFVTQDDILYPHLTVRETL-VFCSLLRLPKS 172
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 572882597 1393 DAEVAITRLVDAL-------KLQDQL--KSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMD 1449
Cdd:PLN03211 173 LTKQEKILVAESViselgltKCENTIigNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
458-661 |
1.21e-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: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 458 DADPSFhdsfEQAPPEFQGKEAIRIRNVTKEYKGK-------PDKIEALKDLVFDIYEGQITAILGHSGAGKSTL-LNIL 529
Cdd:COG4172 258 AAEPRG----DPRPVPPDAPPLLEARDLKVWFPIKrglfrrtVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 530 sGLsVPTKGSVTIYNNKLSEMADLENLSKltgvcpQSNVQFDF----------LTVR----ENLRLFAkiKGILPQEVDK 595
Cdd:COG4172 334 -RL-IPSEGEIRFDGQDLDGLSRRALRPL------RRRMQVVFqdpfgslsprMTVGqiiaEGLRVHG--PGLSAAERRA 403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 572882597 596 EIQRVLLELEMkniqDVLAQN-----LSGGQKRKLtfGIA---ILgDPQIFLLDEPTAGLDPFSRHQVWNLLKE 661
Cdd:COG4172 404 RVAEALEEVGL----DPAARHrypheFSGGQRQRI--AIAralIL-EPKLLVLDEPTSALDVSVQAQILDLLRD 470
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
509-692 |
1.87e-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: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 509 GQITAILGHSGAGKSTLLNILSGLSVPTKGSVT--IYNNKLSEmADLENLSKLTGV-CPQSNVQFDFLTVRENLRLFAKI 585
Cdd:TIGR00956 87 GELTVVLGRPGSGCSTLLKTIASNTDGFHIGVEgvITYDGITP-EEIKKHYRGDVVyNAETDVHFPHLTVGETLDFAARC 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 586 KGilPQE----VDKEIQRV-LLELEMK----------NIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPF 650
Cdd:TIGR00956 166 KT--PQNrpdgVSREEYAKhIADVYMAtyglshtrntKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSA 243
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 572882597 651 SRHQVWNLLkerKTDRVILFSTQFM------DEADILADRKVFLSQGK 692
Cdd:TIGR00956 244 TALEFIRAL---KTSANILDTTPLVaiyqcsQDAYELFDKVIVLYEGY 288
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1297-1497 |
2.14e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 54.27 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1297 FSKRKNKIaTRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITgDTKPTAGQVLLKGSgggdaLEFLGYCPQENALWPNLTV 1376
Cdd:PRK14258 15 FYYDTQKI-LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLN-RMNELESEVRVEGR-----VEFFNQNIYERRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1377 RQ-----------HLEVYAAVK-GLR------KGDAEVAITRLVDALKLQDQLKSPVKT----LSEGIKRKLCFVLSILG 1434
Cdd:PRK14258 88 RQvsmvhpkpnlfPMSVYDNVAyGVKivgwrpKLEIDDIVESALKDADLWDEIKHKIHKsaldLSGGQQQRLCIARALAV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 572882597 1435 NPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLR 1497
Cdd:PRK14258 168 KPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENR 230
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1308-1476 |
2.42e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 53.56 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1308 NVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSgggDALEF--------LGYCPQENALWPNlTVRQH 1379
Cdd:PRK10247 25 NISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGE---DISTLkpeiyrqqVSYCAQTPTLFGD-TVYDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1380 LEVYAAVKGlrKGDAEVAITRLVDALKLQDQ-LKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQ 1458
Cdd:PRK10247 101 LIFPWQIRN--QQPDPAIFLDDLERFALPDTiLTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNE 178
|
170
....*....|....*...
gi 572882597 1459 AIRATFRNTERGALLTTH 1476
Cdd:PRK10247 179 IIHRYVREQNIAVLWVTH 196
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
499-656 |
2.59e-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: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 499 LKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGsvtiynnKLSEMADLENLSKLTGVCPQsnvqfdflTVREN 578
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEG-------KIKHSGRISFSSQFSWIMPG--------TIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 579 LrlfakIKGILPQEVDKE--IQRVLLELEMKNIQD----VLAQ---NLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDP 649
Cdd:cd03291 118 I-----IFGVSYDEYRYKsvVKACQLEEDITKFPEkdntVLGEggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
....*..
gi 572882597 650 FSRHQVW 656
Cdd:cd03291 193 FTEKEIF 199
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
483-659 |
2.68e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 54.59 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 483 RNVTKEY---KG---KPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEmADLENL 556
Cdd:PRK11308 9 IDLKKHYpvkRGlfkPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLK-ADPEAQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 557 SKLtgvcpQSNVQFDFLTVRENLRLFAKIKGILpqEVDKEIQRVLLELEMK-NIQDVLAQ-------------NLSGGQK 622
Cdd:PRK11308 88 KLL-----RQKIQIVFQNPYGSLNPRKKVGQIL--EEPLLINTSLSAAERReKALAMMAKvglrpehydryphMFSGGQR 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 572882597 623 RKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLL 659
Cdd:PRK11308 161 QRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLM 197
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
477-669 |
2.76e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.81 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 477 KEAIRIRNVTKEYKGKPDkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNIL--------------------------- 529
Cdd:PTZ00265 1163 KGKIEIMDVNFRYISRPN-VPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtndmtneqd 1241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 530 --------------SGLSVPTKGS----VTIYNNKLSEMAD--------LENLSKLTGVCPQSNVQFDfLTVRENLRlFA 583
Cdd:PTZ00265 1242 yqgdeeqnvgmknvNEFSLTKEGGsgedSTVFKNSGKILLDgvdicdynLKDLRNLFSIVSQEPMLFN-MSIYENIK-FG 1319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 584 KIKGILpQEVDK-----EIQRVLLELEMKNIQDV--LAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVW 656
Cdd:PTZ00265 1320 KEDATR-EDVKRackfaAIDEFIESLPNKYDTNVgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIE 1398
|
250
....*....|....*
gi 572882597 657 NLLKE--RKTDRVIL 669
Cdd:PTZ00265 1399 KTIVDikDKADKTII 1413
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1301-1499 |
3.87e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.74 E-value: 3.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1301 KNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGS--GGGDALEFL----------------- 1361
Cdd:PRK10982 259 LRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKkiNNHNANEAInhgfalvteerrstgiy 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1362 GYCPQE-NALWPNltVRQHLEVYAAVKGLR-KGDAEVAItrlvDALKLQD-QLKSPVKTLSEGIKRKLCFVLSILGNPSV 1438
Cdd:PRK10982 339 AYLDIGfNSLISN--IRNYKNKVGLLDNSRmKSDTQWVI----DSMRVKTpGHRTQIGSLSGGNQQKVIIGRWLLTQPEI 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 572882597 1439 VLLDEPSTGMDPEGQQQMWQAIrATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCI 1499
Cdd:PRK10982 413 LMLDEPTRGIDVGAKFEIYQLI-AELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGI 472
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1308-1451 |
4.61e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.35 E-value: 4.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1308 NVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsggGDALEfLGYCPQE-NALWPNLTvrqhleVYAAV 1386
Cdd:PRK11819 342 DLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-----GETVK-LAYVDQSrDALDPNKT------VWEEI 409
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 572882597 1387 KG----LRKGDAEVAITRLVDA--LKLQDQLKsPVKTLSEGiKRK---LCFVLSILGNpsVVLLDEPSTGMDPE 1451
Cdd:PRK11819 410 SGgldiIKVGNREIPSRAYVGRfnFKGGDQQK-KVGVLSGG-ERNrlhLAKTLKQGGN--VLLLDEPTNDLDVE 479
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
481-531 |
4.76e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 54.41 E-value: 4.76e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 572882597 481 RIRNVTKEYKGkpdkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSG 531
Cdd:NF040905 3 EMRGITKTFPG----VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
495-670 |
4.77e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.48 E-value: 4.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 495 KIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADlenlSKLTGVcpQSNVQFDF-- 572
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSP----GKLQAL--RRDIQFIFqd 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 573 --------LTVRENLRLFAKIKGILPQEVDKEiqRVLLELEMKNIQDVLA----QNLSGGQKRKLTFGIAILGDPQIFLL 640
Cdd:PRK10261 410 pyasldprQTVGDSIMEPLRVHGLLPGKAAAA--RVAWLLERVGLLPEHAwrypHEFSGGQRQRICIARALALNPKVIIA 487
|
170 180 190
....*....|....*....|....*....|
gi 572882597 641 DEPTAGLDPFSRHQVWNLLKERKTDRVILF 670
Cdd:PRK10261 488 DEAVSALDVSIRGQIINLLLDLQRDFGIAY 517
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
499-673 |
4.80e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 52.26 E-value: 4.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 499 LKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSV-----TIYNNKLSEMADLENLSKLTGVCPqsnvqfdFL 573
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEIlferqSIKKDLCTYQKQLCFVGHRSGINP-------YL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 574 TVRENLrLFakikGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRH 653
Cdd:PRK13540 90 TLRENC-LY----DIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLL 164
|
170 180
....*....|....*....|..
gi 572882597 654 QVWNLLKE--RKTDRVILFSTQ 673
Cdd:PRK13540 165 TIITKIQEhrAKGGAVLLTSHQ 186
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1300-1510 |
5.39e-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: 5.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1300 RKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSgggDALEF--------LGYCPQENALW 1371
Cdd:TIGR00958 491 RPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGV---PLVQYdhhylhrqVALVGQEPVLF 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1372 pNLTVRQHLevyaaVKGLRKG-DAEV-AITRLVDALKLQDQLKSPVKT--------LSEGIKRKLCFVLSILGNPSVVLL 1441
Cdd:TIGR00958 568 -SGSVRENI-----AYGLTDTpDEEImAAAKAANAHDFIMEFPNGYDTevgekgsqLSGGQKQRIAIARALVRKPRVLIL 641
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 572882597 1442 DEPSTGMDPEGQQQMWQAIRAtfrnTERGALLTTHYMAEAEAvCDRVAIMVSGRLRCIGSIQHLKSKFG 1510
Cdd:TIGR00958 642 DEATSALDAECEQLLQESRSR----ASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQG 705
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1314-1449 |
6.86e-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: 6.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1314 RKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQ---------VL--LKGSGGGDALEFLgycpQENalwpNLTVR---QH 1379
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDydeepswdeVLkrFRGTELQDYFKKL----ANG----EIKVAhkpQY 168
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 572882597 1380 LEVYA-AVKG-----LRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMD 1449
Cdd:COG1245 169 VDLIPkVFKGtvrelLEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
499-664 |
8.09e-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: 8.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 499 LKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIynnklsemadlenlskltgvCPQSNVQFdfltvren 578
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM--------------------PEGEDLLF-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 579 lrlfakikgiLPQevdkeiqRVLLELemKNIQDVLA----QNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQ 654
Cdd:cd03223 69 ----------LPQ-------RPYLPL--GTLREQLIypwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDR 129
|
170
....*....|
gi 572882597 655 VWNLLKERKT 664
Cdd:cd03223 130 LYQLLKELGI 139
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1305-1495 |
8.18e-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: 8.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1305 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGdTKPTA---GQVL-----LKGSGGGDALEF-LGYCPQENALWPNLT 1375
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHGtwdGEIYwsgspLKASNIRDTERAgIVIIHQELTLVPELS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1376 VRQHL----EVyaAVKGLRKGDAevAITRLVDALKLQDQLKS-----PVKTLSEGIKRKLCFVLSILGNPSVVLLDEPST 1446
Cdd:TIGR02633 95 VAENIflgnEI--TLPGGRMAYN--AMYLRAKNLLRELQLDAdnvtrPVGDYGGGQQQLVEIAKALNKQARLLILDEPSS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 572882597 1447 GMDPEGQQQMWQAIRaTFRNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1495
Cdd:TIGR02633 171 SLTEKETEILLDIIR-DLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
504-692 |
8.24e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.48 E-value: 8.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 504 FDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSvtiYNNKLSEMADL--ENLSKLTGVCPQSNvQFDFLTVRENL-- 579
Cdd:PRK10938 24 LTLNAGDSWAFVGANGSGKSALARALAGELPLLSGE---RQSQFSHITRLsfEQLQKLVSDEWQRN-NTDMLSPGEDDtg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 580 RLFAKIkgIlpQEVDKEIQRVLLELEMKNIQDVLAQN---LSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVW 656
Cdd:PRK10938 100 RTTAEI--I--QDEVKDPARCEQLAQQFGITALLDRRfkyLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 572882597 657 NLLKERKTDRVIL------FST--QFMDEADILADRKVFLsQGK 692
Cdd:PRK10938 176 ELLASLHQSGITLvlvlnrFDEipDFVQFAGVLADCTLAE-TGE 218
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1293-1351 |
9.66e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 52.10 E-value: 9.66e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 572882597 1293 RKGCFsKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG 1351
Cdd:PRK15112 17 RTGWF-RRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDD 74
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1302-1489 |
9.72e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 52.09 E-value: 9.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1302 NKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVI--TGDTKPTA---GQVLLKGS----GGGDALEF---LGYCPQENA 1369
Cdd:PRK14243 22 SFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPGFrveGKVTFHGKnlyaPDVDPVEVrrrIGMVFQKPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1370 LWPNlTVRQHLEVYAAVKGLrKGDAEVAITRLVDALKLQDQLKSPVKT----LSEGIKRKLCFVLSILGNPSVVLLDEPS 1445
Cdd:PRK14243 102 PFPK-SIYDNIAYGARINGY-KGDMDELVERSLRQAALWDEVKDKLKQsglsLSGGQQQRLCIARAIAVQPEVILMDEPC 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 572882597 1446 TGMDPEGQQQMWQAIRATFRntERGALLTTHYMAEAEAVCDRVA 1489
Cdd:PRK14243 180 SALDPISTLRIEELMHELKE--QYTIIIVTHNMQQAARVSDMTA 221
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
499-659 |
1.02e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 51.03 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 499 LKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSemadleNLSK--LTGVCPQSNVQFDfLTVR 576
Cdd:PRK13541 16 LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNIN------NIAKpyCTYIGHNLGLKLE-MTVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 577 ENLRLFAKIkgilpQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVW 656
Cdd:PRK13541 89 ENLKFWSEI-----YNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLN 163
|
...
gi 572882597 657 NLL 659
Cdd:PRK13541 164 NLI 166
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1313-1449 |
1.18e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.27 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1313 VRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQ---------VL--LKGSGGGDALEFL-------GYCPQENALWPNl 1374
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDyeeepswdeVLkrFRGTELQNYFKKLyngeikvVHKPQYVDLIPK- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1375 tvrqhlevyaAVKG-----LRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMD 1449
Cdd:PRK13409 175 ----------VFKGkvrelLKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1302-1453 |
1.20e-06 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 51.91 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1302 NKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGS-----GGGDALEFLGYCPQeNALWP-NLT 1375
Cdd:PRK10253 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEhiqhyASKEVARRIGLLAQ-NATTPgDIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1376 VRQ--------HLEVYAAvkgLRKGDAEvAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTG 1447
Cdd:PRK10253 98 VQElvargrypHQPLFTR---WRKEDEE-AVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
....*.
gi 572882597 1448 MDPEGQ 1453
Cdd:PRK10253 174 LDISHQ 179
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
471-698 |
1.24e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.59 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 471 PPEFQGKEAIRIRNVTKEYKGKPDKiEALKDLVFDIYEGQITAILGHSGAGKSTLLN-ILSGLSVPTKGSVTIYNNklse 549
Cdd:PLN03130 606 PPLEPGLPAISIKNGYFSWDSKAER-PTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGT---- 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 550 madlenlsklTGVCPQSNVQFDfLTVRENLrLFAkikgiLPQEVDK--------EIQRVLLELEMKNIQDVLAQ--NLSG 619
Cdd:PLN03130 681 ----------VAYVPQVSWIFN-ATVRDNI-LFG-----SPFDPERyeraidvtALQHDLDLLPGGDLTEIGERgvNISG 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 620 GQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWN-LLKE--RKTDRViLFSTQ--FMDEadilADRKVFLSQGKLK 694
Cdd:PLN03130 744 GQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDkCIKDelRGKTRV-LVTNQlhFLSQ----VDRIILVHEGMIK 818
|
....
gi 572882597 695 CAGS 698
Cdd:PLN03130 819 EEGT 822
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1303-1451 |
1.80e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 52.65 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1303 KIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsggGDALEfLGYCPQENA-LWPNLTVrqhle 1381
Cdd:PRK11147 332 KQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-----GTKLE-VAYFDQHRAeLDPEKTV----- 400
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 572882597 1382 vyaaVKGLRKGDAEVAIT-RLVDALK-LQDQL------KSPVKTLSEGIKRKLcFVLSILGNPSVVL-LDEPSTGMDPE 1451
Cdd:PRK11147 401 ----MDNLAEGKQEVMVNgRPRHVLGyLQDFLfhpkraMTPVKALSGGERNRL-LLARLFLKPSNLLiLDEPTNDLDVE 474
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1285-1501 |
1.95e-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: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1285 LRKEYAGKRKgcfskrknkiATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGD-------- 1356
Cdd:PRK11650 9 VRKSYDGKTQ----------VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNElepadrdi 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1357 ALEFLGYcpqenALWPNLTVRQHLEvYA-AVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGN 1435
Cdd:PRK11650 79 AMVFQNY-----ALYPHMSVRENMA-YGlKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVRE 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 572882597 1436 PSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1501
Cdd:PRK11650 153 PAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGT 218
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1323-1451 |
2.47e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 49.87 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1323 GHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGD-ALEFLGYCPQENALWPNLTVRQHLEVYAAVKglrkgDAEVAITRL 1401
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNiAKPYCTYIGHNLGLKLEMTVFENLKFWSEIY-----NSAETLYAA 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 572882597 1402 VDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1451
Cdd:PRK13541 108 IHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKE 157
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
1309-1443 |
3.38e-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: 3.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1309 VSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLkgsgGGDALEflgycpQENALWpnltVRQHlevYAAV-- 1386
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILL----DGQPVT------ADNREA----YRQL---FSAVfs 413
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 572882597 1387 --------KGLRKGDAEVAITRLVDALKLQDQLK------SPVKtLSEGIKRKLCFVLSILGNPSVVLLDE 1443
Cdd:COG4615 414 dfhlfdrlLGLDGEADPARARELLERLELDHKVSvedgrfSTTD-LSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
493-531 |
3.57e-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: 3.57e-06
10 20 30
....*....|....*....|....*....|....*....
gi 572882597 493 PDKIEALKDLVfdiyEGQITAILGHSGAGKSTLLNILSG 531
Cdd:cd01854 73 GEGLDELRELL----KGKTSVLVGQSGVGKSTLLNALLP 107
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1305-1338 |
3.76e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.47 E-value: 3.76e-06
10 20 30
....*....|....*....|....*....|....
gi 572882597 1305 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITG 1338
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG 53
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1308-1496 |
4.43e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 50.13 E-value: 4.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1308 NVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG------SGGGDALEF---LGYCPQ--ENALWPNlTV 1376
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtlitstSKNKDIKQIrkkVGLVFQfpESQLFEE-TV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1377 RQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQL--KSPVKtLSEGIKRKLCfVLSILG-NPSVVLLDEPSTGMDPEGQ 1453
Cdd:PRK13649 104 LKDVAFGPQNFGVSQEEAEALAREKLALVGISESLfeKNPFE-LSGGQMRRVA-IAGILAmEPKILVLDEPTAGLDPKGR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 572882597 1454 QQMWQairaTFRNTERGAL---LTTHYMAEAEAVCDRVAIMVSGRL 1496
Cdd:PRK13649 182 KELMT----LFKKLHQSGMtivLVTHLMDDVANYADFVYVLEKGKL 223
|
|
| RsgA |
COG1162 |
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis]; |
496-531 |
4.61e-06 |
|
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440776 [Multi-domain] Cd Length: 300 Bit Score: 50.50 E-value: 4.61e-06
10 20 30
....*....|....*....|....*....|....*.
gi 572882597 496 IEALKDLVfdiyEGQITAILGHSGAGKSTLLNILSG 531
Cdd:COG1162 157 LDELRELL----KGKTSVLVGQSGVGKSTLINALLP 188
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
480-647 |
5.68e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 50.77 E-value: 5.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGkpdkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGS-------VTIYNNKLSEMAD 552
Cdd:PRK10762 5 LQLKGIDKAFPG----VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSilylgkeVTFNGPKSSQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 553 LENLSKLTGVCPQsnvqfdfLTVRENL---RLFAKIKG-ILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFG 628
Cdd:PRK10762 81 IGIIHQELNLIPQ-------LTIAENIflgREFVNRFGrIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIA 153
|
170
....*....|....*....
gi 572882597 629 IAILGDPQIFLLDEPTAGL 647
Cdd:PRK10762 154 KVLSFESKVIIMDEPTDAL 172
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1275-1351 |
9.31e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 49.58 E-value: 9.31e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 572882597 1275 DEKPVIIASCLRKEYAGKRkGCFSKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG 1351
Cdd:PRK11308 1 SQQPLLQAIDLKKHYPVKR-GLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQG 76
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1308-1476 |
1.11e-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: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1308 NVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKP---TAGQVLLKGSGGGDALE-FLGYCPQENALWPNLTVRQHLEVY 1383
Cdd:TIGR00956 781 NVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLDSSFQrSIGYVQQQDLHLPTSTVRESLRFS 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1384 AAvkgLRKgDAEVAIT---RLVDA----LKLQDQLKSPVKTLSEGI----KRKLCFVLSILGNP-SVVLLDEPSTGMDPE 1451
Cdd:TIGR00956 861 AY---LRQ-PKSVSKSekmEYVEEviklLEMESYADAVVGVPGEGLnveqRKRLTIGVELVAKPkLLLFLDEPTSGLDSQ 936
|
170 180
....*....|....*....|....*
gi 572882597 1452 GQQQMWQAIRATfRNTERGALLTTH 1476
Cdd:TIGR00956 937 TAWSICKLMRKL-ADHGQAILCTIH 960
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
471-542 |
1.83e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 49.35 E-value: 1.83e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 572882597 471 PPEFQGKEAIRIRNVTKEYKgkpDKIeALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTI 542
Cdd:PRK11819 316 PGPRLGDKVIEAENLSKSFG---DRL-LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1293-1510 |
2.15e-05 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 49.56 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1293 RKGCFSKRKNKIATRN-VSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSgggdalefLGYCPQEnALW 1371
Cdd:TIGR00957 640 HNATFTWARDLPPTLNgITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--------VAYVPQQ-AWI 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1372 PNLTVRQHLEVYAAVKGLRKGDAEVAITRLVD--ALKLQDQLKSPVK--TLSEGIKRKLCFVLSILGNPSVVLLDEPSTG 1447
Cdd:TIGR00957 711 QNDSLRENILFGKALNEKYYQQVLEACALLPDleILPSGDRTEIGEKgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSA 790
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 572882597 1448 MDPEGQQQMWQAI---RATFRNTERgaLLTTHYMAEAEAVcDRVAIMVSGRLRCIGSIQHLKSKFG 1510
Cdd:TIGR00957 791 VDAHVGKHIFEHVigpEGVLKNKTR--ILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQRDG 853
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
480-672 |
2.55e-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: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 480 IRIRNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKS-TLLNIL----SGLSVPTkGSVTiYNNK----LSEm 550
Cdd:COG4172 7 LSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILrllpDPAAHPS-GSIL-FDGQdllgLSE- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 551 ADL-------------ENLSKLTGVcpqsnvqfdfLTV----RENLRLFAKIKGilpqevdKEI-QRVLLELEMKNIQDV 612
Cdd:COG4172 84 RELrrirgnriamifqEPMTSLNPL----------HTIgkqiAEVLRLHRGLSG-------AAArARALELLERVGIPDP 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 572882597 613 ---LAQ---NLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFST 672
Cdd:COG4172 147 errLDAyphQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDlqRELGMALLLIT 214
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1307-1449 |
2.75e-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: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1307 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVllKGSGGgdalefLGYCPQENALWPNlTVRQHLevyaaV 1386
Cdd:TIGR01271 443 KNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI--KHSGR------ISFSPQTSWIMPG-TIKDNI-----I 508
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 572882597 1387 KGLRKGdaEVAITRLVDALKLQDQL-KSPVK----------TLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMD 1449
Cdd:TIGR01271 509 FGLSYD--EYRYTSVIKACQLEEDIaLFPEKdktvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
493-531 |
2.83e-05 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 46.38 E-value: 2.83e-05
10 20 30
....*....|....*....|....*....|....*....
gi 572882597 493 PDKIEALKDLVfdiyEGQITAILGHSGAGKSTLLNILSG 531
Cdd:pfam03193 94 GEGIEALKELL----KGKTTVLAGQSGVGKSTLLNALLP 128
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
499-648 |
2.95e-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: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 499 LKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTiYNNKLSemadlenlskltgVCPqsnvQFDFL---TV 575
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK-HSGRIS-------------FSP----QTSWImpgTI 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 576 RENLRLFAKIKGILPQEVDKEIQrvlLELEMKNIQD----VLAQ---NLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLD 648
Cdd:TIGR01271 504 KDNIIFGLSYDEYRYTSVIKACQ---LEEDIALFPEkdktVLGEggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1307-1459 |
5.00e-05 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 47.16 E-value: 5.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1307 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVllKGSGGgdalefLGYCPQENALWPNlTVRQHLEVYAAV 1386
Cdd:cd03291 54 KNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI--KHSGR------ISFSSQFSWIMPG-TIKENIIFGVSY 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 572882597 1387 KGLRKGDAEVAITRLVDALKLQDQLKSPVK----TLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQA 1459
Cdd:cd03291 125 DEYRYKSVVKACQLEEDITKFPEKDNTVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFES 201
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1305-1338 |
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 572882597 1305 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITG 1338
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1275-1331 |
5.81e-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: 5.81e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 572882597 1275 DEKPVIIASCLRKEYAGKRkGCFSKRKNKI-ATRNVSFCVRKGEVLGLLGHNGAGKST 1331
Cdd:COG4172 271 DAPPLLEARDLKVWFPIKR-GLFRRTVGHVkAVDGVSLTLRRGETLGLVGESGSGKST 327
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
483-647 |
5.94e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 47.62 E-value: 5.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 483 RNVTKEYKGkpdkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLsVPT---KGSVTIYNNKL--SEMADLENL- 556
Cdd:PRK13549 9 KNITKTFGG----VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEELqaSNIRDTERAg 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 557 -----SKLTGVcPQsnvqfdfLTVRENLRLFAKI--KGILP-QEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFG 628
Cdd:PRK13549 84 iaiihQELALV-KE-------LSVLENIFLGNEItpGGIMDyDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIA 155
|
170
....*....|....*....
gi 572882597 629 IAILGDPQIFLLDEPTAGL 647
Cdd:PRK13549 156 KALNKQARLLILDEPTASL 174
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
501-692 |
6.04e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.78 E-value: 6.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 501 DLVFDIYEGQITAILGHSGAGKS-TLLNILSGLSVP----TKGSVTIYNNKLSEmADLENLSKLTG-------------V 562
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLH-ASEQTLRGVRGnkiamifqepmvsL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 563 CPQSNVQ---FDFLTVRENLRLFAKIKGILpqevdKEIQRVLLELEMKNIQDVLAQnLSGGQKRKLTFGIAILGDPQIFL 639
Cdd:PRK15134 106 NPLHTLEkqlYEVLSLHRGMRREAARGEIL-----NCLDRVGIRQAAKRLTDYPHQ-LSGGERQRVMIAMALLTRPELLI 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 572882597 640 LDEPTAGLDPFSRHQVWNLLKE--RKTDRVILFSTQFMDEADILADRKVFLSQGK 692
Cdd:PRK15134 180 ADEPTTALDVSVQAQILQLLRElqQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1296-1450 |
6.18e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 47.66 E-value: 6.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1296 CFSKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSgggdaleflgycPQENALWPNLt 1375
Cdd:PRK10522 329 TFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK------------PVTAEQPEDY- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1376 vRQHlevYAAV-------KGLRKGDAEVAITRLVDA----LKLQDQLK------SPVKtLSEGIKRKLCFVLSILGNPSV 1438
Cdd:PRK10522 396 -RKL---FSAVftdfhlfDQLLGPEGKPANPALVEKwlerLKMAHKLEledgriSNLK-LSKGQKKRLALLLALAEERDI 470
|
170
....*....|..
gi 572882597 1439 VLLDEPSTGMDP 1450
Cdd:PRK10522 471 LLLDEWAADQDP 482
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
482-692 |
9.04e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.03 E-value: 9.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 482 IRNVTKEYKGkpdkIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLSKLTG 561
Cdd:PRK10982 1 MSNISKSFPG----VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGIS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 562 VCPQSNVQFDFLTVRENLRLFA-KIKGILpqeVD-----KEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDP 635
Cdd:PRK10982 77 MVHQELNLVLQRSVMDNMWLGRyPTKGMF---VDqdkmyRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 572882597 636 QIFLLDEPTAGLdpfSRHQVWNL------LKERKTDrvILFSTQFMDEADILADRKVFLSQGK 692
Cdd:PRK10982 154 KIVIMDEPTSSL---TEKEVNHLftiirkLKERGCG--IVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1288-1511 |
1.01e-04 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 46.88 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1288 EYAGKRKGCFskrknkiatrNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGD-ALEFL----G 1362
Cdd:PRK13657 343 SYDNSRQGVE----------DVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTvTRASLrrniA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1363 YCPQENALWpNLTVRQHLEVyaavkGlrKGDAEVAitRLVDALKLQDQL----KSPVK----------TLSEGIKRKLCF 1428
Cdd:PRK13657 413 VVFQDAGLF-NRSIEDNIRV-----G--RPDATDE--EMRAAAERAQAHdfieRKPDGydtvvgergrQLSGGERQRLAI 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1429 VLSILGNPSVVLLDEPSTGMDPEGQQQMWQAI------RATFRNTERgalLTThyMAEAeavcDRVAIMVSGRLRCIGSI 1502
Cdd:PRK13657 483 ARALLKDPPILILDEATSALDVETEAKVKAALdelmkgRTTFIIAHR---LST--VRNA----DRILVFDNGRVVESGSF 553
|
....*....
gi 572882597 1503 QHLKSKFGK 1511
Cdd:PRK13657 554 DELVARGGR 562
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
496-536 |
1.02e-04 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 46.35 E-value: 1.02e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 572882597 496 IEALKDLVfdiyEGQITAILGHSGAGKSTLLN-ILSGLSVPT 536
Cdd:PRK00098 155 LDELKPLL----AGKVTVLAGQSGVGKSTLLNaLAPDLELKT 192
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
500-667 |
1.21e-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: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 500 KDLVFDIYEGqITAILGHSGAGKSTllnILSGLSVPTKGSVTIYNNKLSEMADL----ENLS--KLTgvcpQSNVQFDFL 573
Cdd:cd03240 14 ERSEIEFFSP-LTLIVGQNGAGKTT---IIEALKYALTGELPPNSKGGAHDPKLiregEVRAqvKLA----FENANGKKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 574 TVRENLRLFAKIKgILPQEvdkEIqRVLLELEMKNiqdvlaqnLSGGQKRKLTFGIAI-----LGDP-QIFLLDEPTAGL 647
Cdd:cd03240 86 TITRSLAILENVI-FCHQG---ES-NWPLLDMRGR--------CSGGEKVLASLIIRLalaetFGSNcGILALDEPTTNL 152
|
170 180
....*....|....*....|.
gi 572882597 648 DPFSR-HQVWNLLKERKTDRV 667
Cdd:cd03240 153 DEENIeESLAEIIEERKSQKN 173
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
498-660 |
1.41e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 46.62 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 498 ALKDLVFDIYEGQITAILGHSGAGKSTllnilSGLS----VPTKGSVTIYNNKLSEMADLENL--------------SKL 559
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKST-----TGLAllrlINSQGEIWFDGQPLHNLNRRQLLpvrhriqvvfqdpnSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 560 TgvcPQSNVQfdfLTVRENLRLFAKIKGILPQEvdkeiQRVLLELEMKNIQDVLAQ----NLSGGQKRKLTFGIAILGDP 635
Cdd:PRK15134 376 N---PRLNVL---QIIEEGLRVHQPTLSAAQRE-----QQVIAVMEEVGLDPETRHrypaEFSGGQRQRIAIARALILKP 444
|
170 180
....*....|....*....|....*
gi 572882597 636 QIFLLDEPTAGLDPFSRHQVWNLLK 660
Cdd:PRK15134 445 SLIILDEPTSSLDKTVQAQILALLK 469
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1307-1461 |
1.59e-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: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1307 RNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG----SGGGDAL-EFLGYCPQENALWPNLTVRQhLe 1381
Cdd:COG4604 18 DDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGldvaTTPSRELaKRLAILRQENHINSRLTVRE-L- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1382 V----YAAVKG-LRKGDaEVAITRLVDALKLQDQLKSPVKTLSEGiKRKLCFVLSILG-NPSVVLLDEPSTGMDPEGQQQ 1455
Cdd:COG4604 96 VafgrFPYSKGrLTAED-REIIDEAIAYLDLEDLADRYLDELSGG-QRQRAFIAMVLAqDTDYVLLDEPLNNLDMKHSVQ 173
|
....*.
gi 572882597 1456 MWQAIR 1461
Cdd:COG4604 174 MMKLLR 179
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
509-691 |
1.91e-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: 43.52 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 509 GQITAILGHSGAGKSTLLNILSGLSVPTKGSVtiynnklsEMADLENlskltgvcpqsnvqfdfltvrenlrlfakikgi 588
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV--------IYIDGED--------------------------------- 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 589 lpqevdkeIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLL-------KE 661
Cdd:smart00382 41 --------ILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrllllLK 112
|
170 180 190
....*....|....*....|....*....|....*
gi 572882597 662 RKTDRVILFSTQFMDEAD-----ILADRKVFLSQG 691
Cdd:smart00382 113 SEKNLTVILTTNDEKDLGpallrRRFDRRIVLLLI 147
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
1303-1501 |
2.18e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 46.31 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1303 KIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSgggdalefLGYCPQEnALWPNLTVRQHLEV 1382
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERS--------IAYVPQQ-AWIMNATVRGNILF 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1383 YaavkglrkgDAEVAiTRLVDALKLQD------QLKSPVKT--------LSEGIKRKLCFVLSILGNPSVVLLDEPSTGM 1448
Cdd:PTZ00243 744 F---------DEEDA-ARLADAVRVSQleadlaQLGGGLETeigekgvnLSGGQKARVSLARAVYANRDVYLLDDPLSAL 813
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 572882597 1449 DPE-GQQQMWQAIRATFRNTERgaLLTTHYMaEAEAVCDRVAIMVSGRLRCIGS 1501
Cdd:PTZ00243 814 DAHvGERVVEECFLGALAGKTR--VLATHQV-HVVPRADYVVALGDGRVEFSGS 864
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1308-1349 |
2.34e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.65 E-value: 2.34e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 572882597 1308 NVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLL 1349
Cdd:PRK15064 19 NISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSL 60
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1309-1508 |
2.36e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.12 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1309 VSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGS-----GGGDALEFLGYCPQENALWPNlTVRQHLEVY 1383
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCdvakfGLTDLRRVLSIIPQSPVLFSG-TVRFNIDPF 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1384 AA------VKGLRKGDAEVAITRlvDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMW 1457
Cdd:PLN03232 1334 SEhndadlWEALERAHIKDVIDR--NPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQ 1411
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 572882597 1458 QAIRATFRNTergALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSK 1508
Cdd:PLN03232 1412 RTIREEFKSC---TMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSR 1459
|
|
| GAAP_like |
cd10429 |
Golgi antiapoptotic protein; GAAP (or transmembrane BAX inhibitor motif containing 4) is a ... |
266-373 |
3.06e-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: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 266 WLSWGLLYAGFIFIMALFLALVIRSTQFIILSGFmvvfSLFLLYGLSLVALAFLMSILVKKSFLTGLVVFLLTV--FWGC 343
Cdd:cd10429 67 WLFLISLIGSLILLIALYWKRHSHPVNLILLSLF----TLCEAYTVGLVVSFYDGKIVLQALILTLGVFVGLTAytFQTK 142
|
90 100 110
....*....|....*....|....*....|
gi 572882597 344 LGFTSLYRHLPASLeWILSLLSPFAFMLGM 373
Cdd:cd10429 143 RDFSSFGALLFILL-WALILLALIFQFFPY 171
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1318-1444 |
3.13e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 44.87 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 1318 VLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDALE--FL-------GYCPQENALWPNLTVRQHLEvYaavkG 1388
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKgiCLppekrriGYVFQDARLFPHYKVRGNLR-Y----G 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 572882597 1389 LRKGDAEvAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEP 1444
Cdd:PRK11144 101 MAKSMVA-QFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEP 155
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1293-1332 |
3.34e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 45.08 E-value: 3.34e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 572882597 1293 RKGCFsKRK--NKIATRNVSFCVRKGEVLGLLGHNGAGKSTS 1332
Cdd:PRK15134 288 RKGIL-KRTvdHNVVVKNISFTLRPGETLGLVGESGSGKSTT 328
|
|
| NosY |
COG1277 |
ABC-type transport system involved in multi-copper enzyme maturation, permease component ... |
213-340 |
3.67e-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: 43.65 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 213 SFIGQSGVITDLYLFSCIISFSSFIYY------ASVNVTRERKR--MKALMTMmGLRDSAF--------WLSWGLLYAgF 276
Cdd:COG1277 36 GGAASGFLGLGLALLASLFSLLSLLLPllapalGMDAISGERESgtLELLLTL-PISRWEIvlgkflgaLLVLLLALL-I 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 572882597 277 IFIMALFLALVIRSTQFIILSGFMVVFSLFLLYGLSLVALAFLMSILVKK---SFLTGLVVFLLTVF 340
Cdd:COG1277 114 TFLLALLLGLLLFGSPPPDLGAILGFYLGLLLLGLAFLAIGLFISALTRNqivAAILAIALWLLLVI 180
|
|
| 7TMR-DISM_7TM |
pfam07695 |
7TM diverse intracellular signalling; This entry represents the transmembrane region of the ... |
267-421 |
2.00e-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: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 267 LSWGLLYaGFIFIMA---LFLALVIRSTQFIILSGFMVVFSLFLLYGLSLVALAFLMSILVKKSFLTGLVVFLLTVFWGC 343
Cdd:pfam07695 3 LLLGLFY-GILLALAlynLFLFFSLRDRSYLYYVLYLLSFLLYQLSLNGLGFQYLWPNAPPWLNNKLLYLSLLLLLPFFA 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 572882597 344 LGFTSLYRHLPASLEWILSLLSPFAFMLGMAQLLhldydlnsnAFPHPSDGSNLIVATNFMLAFDTCLYLALAIYFEK 421
Cdd:pfam07695 82 LLFARSFLELKKYLPRLLRLLLGLALLLALLLLL---------LPLFPYTLSLPLAQLLALLFILFLLLLGIIAWRKG 150
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1297-1351 |
3.50e-03 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 41.62 E-value: 3.50e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 572882597 1297 FSKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG 1351
Cdd:PRK15079 28 WQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLG 82
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1305-1351 |
3.85e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 41.64 E-value: 3.85e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 572882597 1305 ATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKG 1351
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQG 59
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
499-649 |
5.19e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 41.69 E-value: 5.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882597 499 LKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLsVPTKGSVTIYNNKLSEMADLENLSKLTGVCPQSNVQFDFlTVREN 578
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRM-VEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDG-TVRQN 1403
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 572882597 579 LRLFAKIKgilPQEVDKEIQRVLLE----LEMKNIQD-VL--AQNLSGGQKRKLTFGIAILGDPQIF-LLDEPTAGLDP 649
Cdd:PTZ00243 1404 VDPFLEAS---SAEVWAALELVGLRervaSESEGIDSrVLegGSNYSVGQRQLMCMARALLKKGSGFiLMDEATANIDP 1479
|
|
| ABC_MutS2 |
cd03280 |
ATP-binding cassette domain of MutS2; MutS2 homologs in bacteria and eukaryotes. The MutS ... |
1417-1477 |
8.44e-03 |
|
ATP-binding cassette domain of MutS2; MutS2 homologs in bacteria and eukaryotes. The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family also possess a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213247 [Multi-domain] Cd Length: 200 Bit Score: 39.54 E-value: 8.44e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 572882597 1417 TLSEGIKRkLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHY 1477
Cdd:cd03280 91 TFSSHMKN-IARILQHADPDSLVLLDELGSGTDPVEGAALAIAILEELLERGALVIATTHY 150
|
|
| |
