|
Name |
Accession |
Description |
Interval |
E-value |
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
5-248 |
5.57e-156 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 433.20 E-value: 5.57e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 5 MQLQDVAESTRLGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGMTSGKGSIQFAGQPLEAWSATKLALHRAYLSQQQTP 84
Cdd:PRK03695 1 MQLNDVAVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 85 PFAMPVWHYLTLHQHDKTRTE----LLNDVAGALALDDKLGRSTNQLSGGEWQRVRLAAVVLQITPQANPAGQLLLLDEP 160
Cdd:PRK03695 81 PFAMPVFQYLTLHQPDKTRTEavasALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWPDINPAGQLLLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 161 MNSLDVAQQSALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPPNLAQAYGMNFRRLDIE 240
Cdd:PRK03695 161 MNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVFGVNFRRLDVE 240
|
....*...
gi 1432492527 241 GHRMLIST 248
Cdd:PRK03695 241 GHPMLIST 248
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
5-248 |
1.24e-151 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 421.94 E-value: 1.24e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 5 MQLQDVAESTRLGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGMTSGKGSIQFAGQPLEAWSATKLALHRAYLSQQQTP 84
Cdd:COG4138 1 LQLNDVAVAGRLGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQGEILLNGRPLSDWSAAELARHRAYLSQQQSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 85 PFAMPVWHYLTLHQHDKTRTE----LLNDVAGALALDDKLGRSTNQLSGGEWQRVRLAAVVLQITPQANPAGQLLLLDEP 160
Cdd:COG4138 81 PFAMPVFQYLALHQPAGASSEaveqLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQVWPTINPEGQLLLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 161 MNSLDVAQQSALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPPNLAQAYGMNFRRLDIE 240
Cdd:COG4138 161 MNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVFGVKFRRLEVE 240
|
....*...
gi 1432492527 241 GHRMLIST 248
Cdd:COG4138 241 GHRWLIPT 248
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
16-246 |
6.24e-61 |
|
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: 192.18 E-value: 6.24e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 16 LGPLSGEVRAGEILHLVGPNGAGKSTLLARMAG-MTSGKGSIQFAGQPLEAWSATKLALHRAYLSQQQTPPFAMPVW--- 91
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGlLKPSSGEVLLDGRDLASLSRRELARRIAYVPQEPPAPFGLTVRelv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 92 ------HYLTLHQHDKTRTELLNDVAGALALDDKLGRSTNQLSGGEWQRVRLAAVVLQITPqanpagqLLLLDEPMNSLD 165
Cdd:COG1120 97 algrypHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPP-------LLLLDEPTSHLD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 166 VAQQSALDKILSALCQ-QGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPPNLAQAYGMNFRRLDIE--GH 242
Cdd:COG1120 170 LAHQLEVLELLRRLAReRGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVYGVEARVIEDPvtGR 249
|
....
gi 1432492527 243 RMLI 246
Cdd:COG1120 250 PLVL 253
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
22-232 |
1.26e-58 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 186.47 E-value: 1.26e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLLARMAG-MTSGKGSIQFAGQPLEAWSATKLALHRAYLSQQQTPPFAMPVWHY--LTLHQ 98
Cdd:COG4559 23 TLRPGELTAIIGPNGAGKSTLLKLLTGeLTPSSGEVRLNGRPLAAWSPWELARRRAVLPQHSSLAFPFTVEEVvaLGRAP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 99 HDKTRTELLNDVAGALA---LDDKLGRSTNQLSGGEWQRVRLAAVVLQITPQANPAGQLLLLDEPMNSLDVAQQSALDKI 175
Cdd:COG4559 103 HGSSAAQDRQIVREALAlvgLAHLAGRSYQTLSGGEQQRVQLARVLAQLWEPVDGGPRWLFLDEPTSALDLAHQHAVLRL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1432492527 176 LSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPPNLAQAYGM 232
Cdd:COG4559 183 ARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLERVYGA 239
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
14-215 |
5.91e-58 |
|
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: 181.86 E-value: 5.91e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 14 TRLGPLSGEVRAGEILHLVGPNGAGKSTLLARMAG-MTSGKGSIQFAGQPLEAWSATKLALHRAYLSQqqtppfAMpvwh 92
Cdd:cd03214 13 TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGlLKPSSGEILLDGKDLASLSPKELARKIAYVPQ------AL---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 93 yltlhqhdktrtELLNdvagalaLDDKLGRSTNQLSGGEWQRVRLAAVVLQITPqanpagqLLLLDEPMNSLDVAQQSAL 172
Cdd:cd03214 83 ------------ELLG-------LAHLADRPFNELSGGERQRVLLARALAQEPP-------ILLLDEPTSHLDIAHQIEL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1432492527 173 DKILSALCQQ-GLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASG 215
Cdd:cd03214 137 LELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
22-231 |
9.32e-52 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 168.80 E-value: 9.32e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLLARMAG-MTSGKGSIQFAGQPLEAWSATKLALHRAYLSQQQTPPFAMPV----WHYLTL 96
Cdd:PRK13548 24 TLRPGEVVAILGPNGAGKSTLLRALSGeLSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLSFPFTVeevvAMGRAP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 97 HQHDKTRTELLndVAGALALDDKL---GRSTNQLSGGEWQRVRLAAVVLQITPQAnPAGQLLLLDEPMNSLDVAQQSALD 173
Cdd:PRK13548 104 HGLSRAEDDAL--VAAALAQVDLAhlaGRDYPQLSGGEQQRVQLARVLAQLWEPD-GPPRWLLLDEPTSALDLAHQHHVL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1432492527 174 KILSALC-QQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPPNLAQAYG 231
Cdd:PRK13548 181 RLARQLAhERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPETLRRVYG 239
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
19-238 |
1.17e-45 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 152.55 E-value: 1.17e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKSTLLARMAGM-TSGKGSIQFAGQPLeawsatKLALHR-AYLSQQQTPPFAMPV------ 90
Cdd:COG1121 25 VSLTIPPGEFVAIVGPNGAGKSTLLKAILGLlPPTSGTVRLFGKPP------RRARRRiGYVPQRAEVDWDFPItvrdvv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 91 ----WHYL----TLHQHDKTRtellndVAGALA---LDDKLGRSTNQLSGGEWQRVRLAAVVLQitpqaNPagQLLLLDE 159
Cdd:COG1121 99 lmgrYGRRglfrRPSRADREA------VDEALErvgLEDLADRPIGELSGGQQQRVLLARALAQ-----DP--DLLLLDE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1432492527 160 PMNSLDVAQQSALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGkMLASGRREEVLTPPNLAQAYGMNFRRLD 238
Cdd:COG1121 166 PFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVLTPENLSRAYGGPVALLA 243
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
12-244 |
9.40e-37 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 129.82 E-value: 9.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 12 ESTRLGPLSGEVRAGEILHLVGPNGAGKSTLLARMAG-MTSGKGSIQFAGQPLEAWSATKLALHRAYLsqQQTPPFAMpv 90
Cdd:COG4604 13 GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRlLPPDSGEVLVDGLDVATTPSRELAKRLAIL--RQENHINS-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 91 whYLTLHQ--------HDKTR-TEllND---VAGALA---LDDKLGRSTNQLSGGEWQRVRLAAVVLQITPqanpagqLL 155
Cdd:COG4604 89 --RLTVRElvafgrfpYSKGRlTA--EDreiIDEAIAyldLEDLADRYLDELSGGQRQRAFIAMVLAQDTD-------YV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 156 LLDEPMNSLDVAQQSALDKILSALC-QQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPPNLAQAYGMNF 234
Cdd:COG4604 158 LLDEPLNNLDMKHSVQMMKLLRRLAdELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEVLSDIYDTDI 237
|
250
....*....|
gi 1432492527 235 RRLDIEGHRM 244
Cdd:COG4604 238 EVEEIDGKRI 247
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
19-210 |
1.02e-35 |
|
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: 1.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKSTLLARMAGM-TSGKGSIQFAGQPLEAWSATKLALHRAYLSQ---QQtppFAMP----- 89
Cdd:cd03225 20 ISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLlGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQnpdDQ---FFGPtveee 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 90 -VWHYLTLHQHDKTRTELLNDVAGALALDDKLGRSTNQLSGGEWQRVRLAAVVLqitpqANPagQLLLLDEPMNSLDVAQ 168
Cdd:cd03225 97 vAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLA-----MDP--DILLLDEPTAGLDPAG 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1432492527 169 QSALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGK 210
Cdd:cd03225 170 RRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
19-221 |
1.25e-34 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 124.02 E-value: 1.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKSTLLARMAGM---TSGkgSIQFAGQPLEAWSATklALHR-AYLSQQQTPPFAMPVWHYL 94
Cdd:COG1131 19 VSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLlrpTSG--EVRVLGEDVARDPAE--VRRRiGYVPQEPALYPDLTVRENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 95 TLHQH-----DKTRTELLNDVAGALALDDKLGRSTNQLSGGEWQRVRLAAVVLqitpqANPagQLLLLDEPMNSLDVAQQ 169
Cdd:COG1131 95 RFFARlyglpRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALL-----HDP--ELLILDEPTSGLDPEAR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1432492527 170 SALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVL 221
Cdd:COG1131 168 RELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELK 219
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
19-215 |
2.35e-34 |
|
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: 122.64 E-value: 2.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKSTLLARMAG-MTSGKGSIQFAGQPLEawsatkLALHR-AYLSQQQTPPFAMPV------ 90
Cdd:cd03235 18 VSFEVKPGEFLAIVGPNGAGKSTLLKAILGlLKPTSGSIRVFGKPLE------KERKRiGYVPQRRSIDRDFPIsvrdvv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 91 ----WHYLTLHQH----DKTR-TELLNDVaGALALDDklgRSTNQLSGGEWQRVRLAAVVLQitpqaNPagQLLLLDEPM 161
Cdd:cd03235 92 lmglYGHKGLFRRlskaDKAKvDEALERV-GLSELAD---RQIGELSGGQQQRVLLARALVQ-----DP--DLLLLDEPF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1432492527 162 NSLDVAQQSALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKgGKMLASG 215
Cdd:cd03235 161 AGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLN-RTVVASG 213
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
10-211 |
2.50e-34 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 122.23 E-value: 2.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 10 VAESTRLGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGMTSG-KGSIQFAGQPLEAWSATKLalhR---AYLSQQqTPP 85
Cdd:COG4619 10 VGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPtSGEIYLDGKPLSAMPPPEW---RrqvAYVPQE-PAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 86 FAMPVWHYLTL---HQHDKTRTELLNDVAGALALDDK-LGRSTNQLSGGEWQRVRLAAvVLQITPqanpagQLLLLDEPM 161
Cdd:COG4619 86 WGGTVRDNLPFpfqLRERKFDRERALELLERLGLPPDiLDKPVERLSGGERQRLALIR-ALLLQP------DVLLLDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1432492527 162 NSLDVAQQSALDKILSALCQQ-GLAIVMSSHDLNHTLRHAHRAWLLKGGKM 211
Cdd:COG4619 159 SALDPENTRRVEELLREYLAEeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
11-231 |
4.25e-33 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 123.80 E-value: 4.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 11 AESTRLGPLSGEVRAGEILHLVGPNGAGKSTLLARMAG-MTSGKGSIQFAGQPLEAWSATKLALHRAYLSQQQTPPFAMP 89
Cdd:PRK09536 14 GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGtLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLSFEFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 90 VWHYLTLHQH------------DKTRTELLNDVAGALALDDklgRSTNQLSGGEWQRVRLAAVVLQITPqanpagqLLLL 157
Cdd:PRK09536 94 VRQVVEMGRTphrsrfdtwtetDRAAVERAMERTGVAQFAD---RPVTSLSGGERQRVLLARALAQATP-------VLLL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1432492527 158 DEPMNSLDVAQQSALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPPNLAQAYG 231
Cdd:PRK09536 164 DEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFD 237
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
16-222 |
1.94e-32 |
|
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: 118.20 E-value: 1.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 16 LGPLSGEVRAGEILHLVGPNGAGKSTLLARMAG-MTSGKGSIQFAGQPLEAWSATKLALHRAYLSQQqtpP----FAMPV 90
Cdd:COG1122 17 LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGlLKPTSGEVLVDGKDITKKNLRELRRKVGLVFQN---PddqlFAPTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 91 WHYLT--LHQHDKTRTELLNDVAGALA---LDDKLGRSTNQLSGGEWQRVRLAAVVlqitpqA-NPagQLLLLDEPMNSL 164
Cdd:COG1122 94 EEDVAfgPENLGLPREEIRERVEEALElvgLEHLADRPPHELSGGQKQRVAIAGVL------AmEP--EVLVLDEPTAGL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1432492527 165 DVAQQSALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLT 222
Cdd:COG1122 166 DPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFS 223
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-247 |
5.33e-32 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 117.81 E-value: 5.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 1 MSIVMQLQDVA--ESTRLGPLSGEVRAGEILHLVGPNGAGKSTLL---ARMagMTSGKGSIQFAGQPLEAWSATKLALHR 75
Cdd:PRK11231 1 MTLRTENLTVGygTKRILNDLSLSLPTGKITALIGPNGCGKSTLLkcfARL--LTPQSGTVFLGDKPISMLSSRQLARRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 76 AYLSQQQTPPFAMPVWH--------YLT----LHQHDKTRTELLNDVAGALALDDKLgrsTNQLSGGEWQRVRLAAVVLQ 143
Cdd:PRK11231 79 ALLPQHHLTPEGITVRElvaygrspWLSlwgrLSAEDNARVNQAMEQTRINHLADRR---LTDLSGGQRQRAFLAMVLAQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 144 ITPqanpagqLLLLDEPMNSLDVAQQSALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTP 223
Cdd:PRK11231 156 DTP-------VVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTP 228
|
250 260
....*....|....*....|....
gi 1432492527 224 PNLAQAYGmnfrrLDIEGHRMLIS 247
Cdd:PRK11231 229 GLLRTVFD-----VEAEIHPEPVS 247
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
9-243 |
2.25e-31 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 116.46 E-value: 2.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 9 DVAESTR--LGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGMTSG---------KGSIQFAGQPLEAWSATKLALHRAY 77
Cdd:PRK13547 8 HVARRHRaiLRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGggaprgarvTGDVTLNGEPLAAIDAPRLARLRAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 78 LSQQQTPPFAMPVWHYLTL------------HQHDKTRTELLNDVAGALALDdklGRSTNQLSGGEWQRVRLAAVVLQIT 145
Cdd:PRK13547 88 LPQAAQPAFAFSAREIVLLgrypharragalTHRDGEIAWQALALAGATALV---GRDVTTLSGGELARVQFARVLAQLW 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 146 P--QANPAGQLLLLDEPMNSLDVAQQSALDKILSALCQQ----GLAIVmssHDLNHTLRHAHRAWLLKGGKMLASGRREE 219
Cdd:PRK13547 165 PphDAAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwnlgVLAIV---HDPNLAARHADRIAMLADGAIVAHGAPAD 241
|
250 260
....*....|....*....|....
gi 1432492527 220 VLTPPNLAQAYGMNFRRLDIEGHR 243
Cdd:PRK13547 242 VLTPAHIARCYGFAVRLVDAGDGV 265
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
12-210 |
1.82e-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: 110.80 E-value: 1.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 12 ESTRLGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGMT-SGKGSIQFAGQPLEAWSATKLALHRAYLSQqqtppfampv 90
Cdd:cd00267 11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLkPTSGEILIDGKDIAKLPLEELRRRIGYVPQ---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 91 whyltlhqhdktrtellndvagalalddklgrstnqLSGGEWQRVRLAAVVLQitpqaNPagQLLLLDEPMNSLDVAQQS 170
Cdd:cd00267 81 ------------------------------------LSGGQRQRVALARALLL-----NP--DLLLLDEPTSGLDPASRE 117
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1432492527 171 ALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGK 210
Cdd:cd00267 118 RLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
16-232 |
8.61e-30 |
|
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: 111.71 E-value: 8.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 16 LGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGM---TSGkGSIQFAGQPLEAWSATKLALHRAYLS---QQQTPP---- 85
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDlppTYG-NDVRLFGERRGGEDVWELRKRIGLVSpalQLRFPRdetv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 86 --------FAMP-VWHYLTLHQHDKTRtELLNdvagALALDDKLGRSTNQLSGGEWQRVRLA-AVVlqitpqANPagQLL 155
Cdd:COG1119 98 ldvvlsgfFDSIgLYREPTDEQRERAR-ELLE----LLGLAHLADRPFGTLSQGEQRRVLIArALV------KDP--ELL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1432492527 156 LLDEPMNSLDVAQQSALDKILSALCQQG-LAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPPNLAQAYGM 232
Cdd:COG1119 165 ILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLTSENLSEAFGL 242
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
16-221 |
2.68e-29 |
|
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: 110.33 E-value: 2.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 16 LGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGM-TSGKGSIQFAGQPL-EAWSATKLALhrAYLSQQQTPPFAMPVWHY 93
Cdd:COG4555 17 LKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLlKPDSGSILIDGEDVrKEPREARRQI--GVLPDERGLYDRLTVREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 94 L----TLHQ-HDKTRTELLNDVAGALALDDKLGRSTNQLSGGEWQRVRLAAVVLQitpqaNPagQLLLLDEPMNSLDVAQ 168
Cdd:COG4555 95 IryfaELYGlFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVH-----DP--KVLLLDEPTNGLDVMA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1432492527 169 QSALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVL 221
Cdd:COG4555 168 RRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELR 220
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
19-211 |
1.02e-28 |
|
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: 106.71 E-value: 1.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKSTLLARMAGMTS-GKGSIQFAGQPLeaWSATKLALHR-AYLSQQqtppfaMPVWHYLTL 96
Cdd:cd03230 19 ISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKpDSGEIKVLGKDI--KKEPEEVKRRiGYLPEE------PSLYENLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 97 HQHdktrtellndvagalaLDdklgrstnqLSGGEWQRVRLAAVVLqitpqANPagQLLLLDEPMNSLDVAQQSALDKIL 176
Cdd:cd03230 91 REN----------------LK---------LSGGMKQRLALAQALL-----HDP--ELLILDEPTSGLDPESRREFWELL 138
|
170 180 190
....*....|....*....|....*....|....*
gi 1432492527 177 SALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKM 211
Cdd:cd03230 139 RELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
25-233 |
1.77e-28 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 108.36 E-value: 1.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 25 AGEILHLVGPNGAGKSTLLARMAG-MTSGKGSIQFAGQPLEAWSATKLALHRAYLSQQQtpPFAMPV------------- 90
Cdd:TIGR03873 26 PGSLTGLLGPNGSGKSTLLRLLAGaLRPDAGTVDLAGVDLHGLSRRARARRVALVEQDS--DTAVPLtvrdvvalgriph 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 91 ---WHYLTLHQHDKTRTELLNDVAGALAlddklGRSTNQLSGGEWQRVRLAAVVLQitpqaNPagQLLLLDEPMNSLDVA 167
Cdd:TIGR03873 104 rslWAGDSPHDAAVVDRALARTELSHLA-----DRDMSTLSGGERQRVHVARALAQ-----EP--KLLLLDEPTNHLDVR 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1432492527 168 QQSALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPPNLAQAYGMN 233
Cdd:TIGR03873 172 AQLETLALVRELAATGVTVVAALHDLNLAASYCDHVVVLDGGRVVAAGPPREVLTPALIRAVYGVD 237
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
16-192 |
3.43e-28 |
|
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: 106.41 E-value: 3.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 16 LGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGMTS-GKGSIQFAGQPLEAWSATkLALHRAYLSQQQTPPFAMPVWHYL 94
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPpSAGEVLWNGEPIRDARED-YRRRLAYLGHADGLKPELTVRENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 95 TLHQ---HDKTRTELLNDVAGALALDDKLGRSTNQLSGGEWQRVRLAAVVLQITPqanpagqLLLLDEPMNSLDVAQQSA 171
Cdd:COG4133 97 RFWAalyGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAP-------LWLLDEPFTALDAAGVAL 169
|
170 180
....*....|....*....|.
gi 1432492527 172 LDKILSALCQQGLAIVMSSHD 192
Cdd:COG4133 170 LAELIAAHLARGGAVLLTTHQ 190
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
10-232 |
7.14e-28 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 107.18 E-value: 7.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 10 VAESTRLGPLSGEVRAGEILHLVGPNGAGKSTLLaRMAG--MTSGKGSIQFAGQPLEAWSATKLALHRAYLSQQQTPPFA 87
Cdd:PRK10575 21 VPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLL-KMLGrhQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 88 MPV----------WHYL--TLHQHDKTRTELLNDVAGALALDDKLgrsTNQLSGGEWQRVRLAAVVLQITpqanpagQLL 155
Cdd:PRK10575 100 MTVrelvaigrypWHGAlgRFGAADREKVEEAISLVGLKPLAHRL---VDSLSGGERQRAWIAMLVAQDS-------RCL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1432492527 156 LLDEPMNSLDVAQQSALDKILSALCQQ-GLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPPNLAQAYGM 232
Cdd:PRK10575 170 LLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIYGI 247
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
22-224 |
1.68e-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: 109.99 E-value: 1.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLLARMAGM---TSGkgSIQFAGQPLEAWSATKLALHR---AYLSQQqtpPFA-----MPV 90
Cdd:COG1123 287 TLRRGETLGLVGESGSGKSTLARLLLGLlrpTSG--SILFDGKDLTKLSRRSLRELRrrvQMVFQD---PYSslnprMTV 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 91 WHYLT--LHQH-DKTRTELLNDVAGALAL----DDKLGRSTNQLSGGEWQRVRLAAVVLqitpqANPagQLLLLDEPMNS 163
Cdd:COG1123 362 GDIIAepLRLHgLLSRAERRERVAELLERvglpPDLADRYPHELSGGQRQRVAIARALA-----LEP--KLLILDEPTSA 434
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1432492527 164 LDVAQQSALDKILSALCQQ-GLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPP 224
Cdd:COG1123 435 LDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANP 496
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
6-221 |
5.30e-27 |
|
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: 108.69 E-value: 5.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 6 QLQDV-----AESTRLGPLSGEVRAGEILHLVGPNGAGKSTLLARMAG-MTSGKGSIQFAGQPLEAWSATKLALHRAYLS 79
Cdd:COG4988 338 ELEDVsfsypGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGfLPPYSGSILINGVDLSDLDPASWRRQIAWVP 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 80 QQqtpP--FAMPVWHYLTLHQHDKTRTELLN--DVAGALA--------LDDKLGRSTNQLSGGEWQRVRLAAVVLQITPq 147
Cdd:COG4988 418 QN---PylFAGTIRENLRLGRPDASDEELEAalEAAGLDEfvaalpdgLDTPLGEGGRGLSGGQAQRLALARALLRDAP- 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1432492527 148 anpagqLLLLDEPMNSLDVAQQSALDKILSALCqQGLAIVMSSHDLnHTLRHAHRAWLLKGGKMLASGRREEVL 221
Cdd:COG4988 494 ------LLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRL-ALLAQADRILVLDDGRIVEQGTHEELL 559
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-229 |
1.36e-26 |
|
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: 107.30 E-value: 1.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 1 MSIVMQLQDVAESTRLGP------LSGEVRAGEILHLVGPNGAGKSTLLARMAGMTSGK----GSIQFAGQPLEAWSATK 70
Cdd:COG1123 1 MTPLLEVRDLSVRYPGGDvpavdgVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgrisGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 71 LALHRAYLSQQ-QTPPFAMPVWHYL--TLHQHDKTRTELLNDVAGALA---LDDKLGRSTNQLSGGEWQRVRLAAVVLqi 144
Cdd:COG1123 81 RGRRIGMVFQDpMTQLNPVTVGDQIaeALENLGLSRAEARARVLELLEavgLERRLDRYPHQLSGGQRQRVAIAMALA-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 145 tpqANPagQLLLLDEPMNSLDVAQQSALDKILSALCQQ-GLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTP 223
Cdd:COG1123 159 ---LDP--DLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAA 233
|
....*.
gi 1432492527 224 PNLAQA 229
Cdd:COG1123 234 PQALAA 239
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-216 |
5.07e-25 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 98.58 E-value: 5.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 1 MSIVMQLQDVAESTRLGP-----LSG---EVRAGEILHLVGPNGAGKSTLLARMAGM---TSGkgSIQFAGQPLEAWSAT 69
Cdd:COG1136 1 MSPLLELRNLTKSYGTGEgevtaLRGvslSIEAGEFVAIVGPSGSGKSTLLNILGGLdrpTSG--EVLIDGQDISSLSER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 70 KLALHRA----YLSQQqtppF------------AMPvwhyLTL-HQHDKTRTELLNDVAGALALDDKLGRSTNQLSGGEW 132
Cdd:COG1136 79 ELARLRRrhigFVFQF----FnllpeltalenvALP----LLLaGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 133 QRVRLA-AVVlqitpqANPAgqLLLLDEPMNSLDvaQQSALD--KILSALCQQ-GLAIVMSSHDLnHTLRHAHRAWLLKG 208
Cdd:COG1136 151 QRVAIArALV------NRPK--LILADEPTGNLD--SKTGEEvlELLRELNRElGTTIVMVTHDP-ELAARADRVIRLRD 219
|
....*...
gi 1432492527 209 GKMLASGR 216
Cdd:COG1136 220 GRIVSDER 227
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
19-220 |
2.57e-24 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 96.87 E-value: 2.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKSTLL---ARMAGMTSGK---GSIQFAGQPLEAWSATKLALHRAY-LSQQQTPPFAMPVW 91
Cdd:cd03260 19 ISLDIPKGEITALIGPSGCGKSTLLrllNRLNDLIPGApdeGEVLLDGKDIYDLDVDVLELRRRVgMVFQKPNPFPGSIY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 92 ----HYLTLHQhDKTRTELLNDVAGAL---ALDDKLGRSTN--QLSGGEWQRVRLA-AVVLQitpqanPAgqLLLLDEPM 161
Cdd:cd03260 99 dnvaYGLRLHG-IKLKEELDERVEEALrkaALWDEVKDRLHalGLSGGQQQRLCLArALANE------PE--VLLLDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1432492527 162 NSLDVAQQSALDKILSALCQQgLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEV 220
Cdd:cd03260 170 SALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
16-162 |
2.65e-24 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 94.64 E-value: 2.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 16 LGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGMTSG-KGSIQFAGQPLEAWSATKLALHRAYLSQQQTPPFAMPVW--- 91
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPtEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRenl 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1432492527 92 ------HYLTLHQHDKTRTELLNDVAGALALDDKLGRSTNQLSGGEWQRVRLAAVVLQitpqaNPagQLLLLDEPMN 162
Cdd:pfam00005 81 rlglllKGLSKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLT-----KP--KLLLLDEPTA 150
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
22-224 |
1.12e-23 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 95.20 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLLARMAGMTS-GKGSIQFAGQPLEAWSATKLA---LHRAYlsqQQTPPFA-MPVW----- 91
Cdd:cd03219 22 SVRPGEIHGLIGPNGAGKTTLFNLISGFLRpTSGSVLFDGEDITGLPPHEIArlgIGRTF---QIPRLFPeLTVLenvmv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 92 -------HYLTLHQHDKTRTELLNDVAGALA---LDDKLGRSTNQLSGGEWQRVRLAAVVLQitpqaNPagQLLLLDEPM 161
Cdd:cd03219 99 aaqartgSGLLLARARREEREARERAEELLErvgLADLADRPAGELSYGQQRRLEIARALAT-----DP--KLLLLDEPA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1432492527 162 NSLDVAQQSALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPP 224
Cdd:cd03219 172 AGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNP 234
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
22-230 |
1.66e-23 |
|
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: 94.53 E-value: 1.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLLARMAGMTS-GKGSIQFAGQPLeawsaTKLALHR------AYLSQQQTppfampVWHYL 94
Cdd:cd03218 22 SVKQGEIVGLLGPNGAGKTTTFYMIVGLVKpDSGKILLDGQDI-----TKLPMHKrarlgiGYLPQEAS------IFRKL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 95 TLHQH-----------DKTRTELLNDVAGALALD---DKLGRStnqLSGGEWQRVRLA-AVVLqitpqaNPagQLLLLDE 159
Cdd:cd03218 91 TVEENilavleirglsKKEREEKLEELLEEFHIThlrKSKASS---LSGGERRRVEIArALAT------NP--KFLLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1432492527 160 PMNSLDVAQQSALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPPNLAQAY 230
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKVY 230
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
19-232 |
2.03e-23 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 95.44 E-value: 2.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKSTLLARMAG-MTSGKGSIQFAGQPLEAWSATKLALHRAYLSQQQTPPFAMPVWHYLTL- 96
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRlMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQELVARg 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 97 ---HQHDKTR-----TELLNDVAGALALDDKLGRSTNQLSGGEWQRVRLAAVVLQITpqanpagQLLLLDEPMNSLDVAQ 168
Cdd:PRK10253 106 rypHQPLFTRwrkedEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQET-------AIMLLDEPTTWLDISH 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1432492527 169 QSALDKILSALC-QQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPPNLAQAYGM 232
Cdd:PRK10253 179 QIDLLELLSELNrEKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGL 243
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-241 |
2.61e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 95.56 E-value: 2.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKSTLLaRMA-GMTSG-KGSIQFAGQPLeawsaTKLALHR-AYLsqqqtP------PfAMP 89
Cdd:COG4152 20 VSFTVPKGEIFGLLGPNGAGKTTTI-RIIlGILAPdSGEVLWDGEPL-----DPEDRRRiGYL-----PeerglyP-KMK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 90 VWH---YL-TLHQHDKTR-----TELLNdvagALALDDKLGRSTNQLSGGEWQRVRLAAVVLqitpqANPagQLLLLDEP 160
Cdd:COG4152 88 VGEqlvYLaRLKGLSKAEakrraDEWLE----RLGLGDRANKKVEELSKGNQQKVQLIAALL-----HDP--ELLILDEP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 161 MNSLD-VAQQSALDKILsALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLtppnlaQAYGMNFRRLDI 239
Cdd:COG4152 157 FSGLDpVNVELLKDVIR-ELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIR------RQFGRNTLRLEA 229
|
..
gi 1432492527 240 EG 241
Cdd:COG4152 230 DG 231
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
19-205 |
3.20e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 93.07 E-value: 3.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKSTLLARMAGMTsgkgsiqfagQPLEAWSATKLALHRAYLSQQQTPPFAMPV-------- 90
Cdd:NF040873 11 VDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVL----------RPTSGTVRRAGGARVAYVPQRSEVPDSLPLtvrdlvam 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 91 --W-HYLTLHQHDKTRTELLNDVAGALALDDKLGRSTNQLSGGEWQRVRLAAVVLQitpqanpAGQLLLLDEPMNSLDVA 167
Cdd:NF040873 81 grWaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQ-------EADLLLLDEPTTGLDAE 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 1432492527 168 QQSALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWL 205
Cdd:NF040873 154 SRERIIALLAEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
22-232 |
5.37e-23 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 93.28 E-value: 5.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLLARMAG-MTSGKGSIQFAGQPLEAwsatklalhraylsqqqTPPFAMPV---------- 90
Cdd:COG3840 21 TIAAGERVAILGPSGAGKSTLLNLIAGfLPPDSGRILWNGQDLTA-----------------LPPAERPVsmlfqennlf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 91 WHyLTLHQ------HDKTR-----TELLNDVAGALALDDKLGRSTNQLSGGEWQRVRLAAVVLQITPqanpagqLLLLDE 159
Cdd:COG3840 84 PH-LTVAQniglglRPGLKltaeqRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRP-------ILLLDE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1432492527 160 PMNSLDVAQQSALDKILSALCQ-QGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVL---TPPNLAQAYGM 232
Cdd:COG3840 156 PFSALDPALRQEMLDLVDELCReRGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLdgePPPALAAYLGI 232
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
11-215 |
6.53e-23 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 92.73 E-value: 6.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 11 AESTRLGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGMT-SGKGSIQFAGQPLEAWSATKLA-------LHRAYLSQQQ 82
Cdd:cd03269 11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIIlPDSGEVLFDGKPLDIAARNRIGylpeergLYPKMKVIDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 83 TPPFAMpvWHYLTLHQHDKTRTELLNdvagALALDDKLGRSTNQLSGGEWQRVRLAAVVLQitpqaNPagQLLLLDEPMN 162
Cdd:cd03269 91 LVYLAQ--LKGLKKEEARRRIDEWLE----RLELSEYANKRVEELSKGNQQKVQFIAAVIH-----DP--ELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1432492527 163 SLDVAQQSALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASG 215
Cdd:cd03269 158 GLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
22-219 |
1.24e-22 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 92.04 E-value: 1.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLLARMAGM---TSGKgsIQFAGQPLEAWSATKLALHRAY----------LSQqqtppfaM 88
Cdd:COG2884 24 EIEKGEFVFLTGPSGAGKSTLLKLLYGEerpTSGQ--VLVNGQDLSRLKRREIPYLRRRigvvfqdfrlLPD-------R 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 89 PVWH--YLTLHQHDKTRTELLNDVAGALA---LDDKLGRSTNQLSGGEWQRVRLA-AVVlqitpqANPagQLLLLDEPMN 162
Cdd:COG2884 95 TVYEnvALPLRVTGKSRKEIRRRVREVLDlvgLSDKAKALPHELSGGEQQRVAIArALV------NRP--ELLLADEPTG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1432492527 163 SLDvaQQSALD--KILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREE 219
Cdd:COG2884 167 NLD--PETSWEimELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARGV 223
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
22-232 |
2.52e-22 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 91.45 E-value: 2.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLLARMAGMTS-GKGSIQFAGQPleawsATKLALHRAYLSQQQTPPFAMPVWHYLTLHQHD 100
Cdd:TIGR03771 2 SADKGELLGLLGPNGAGKTTLLRAILGLIPpAKGTVKVAGAS-----PGKGWRHIGYVPQRHEFAWDFPISVAHTVMSGR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 101 KTRTELLND--VAGALALDDKL---------GRSTNQLSGGEWQRVrLAAVVLQITPQanpagqLLLLDEPMNSLDVAQQ 169
Cdd:TIGR03771 77 TGHIGWLRRpcVADFAAVRDALrrvgltelaDRPVGELSGGQRQRV-LVARALATRPS------VLLLDEPFTGLDMPTQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1432492527 170 SALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKgGKMLASGRREEVLTPPNLAQAYGM 232
Cdd:TIGR03771 150 ELLTELFIELAGAGTAILMTTHDLAQAMATCDRVVLLN-GRVIADGTPQQLQDPAPWMTTFGV 211
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
22-221 |
2.88e-22 |
|
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: 95.29 E-value: 2.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLLARMAGM-TSGKGSIQFAGQPLEAWSATKLALHRAYLSQQQTpPFAMPVWHYLTLHQHD 100
Cdd:COG2274 497 TIKPGERVAIVGRSGSGKSTLLKLLLGLyEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVF-LFSGTIRENITLGDPD 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 101 KTRTELLN--DVAGALA--------LDDKLGRSTNQLSGGEWQRVRLAAVVLQitpqaNPagQLLLLDEPMNSLDVAQQS 170
Cdd:COG2274 576 ATDEEIIEaaRLAGLHDfiealpmgYDTVVGEGGSNLSGGQRQRLAIARALLR-----NP--RILILDEATSALDAETEA 648
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1432492527 171 ALDKILSALCqQGLAIVMSSHDLnHTLRHAHRAWLLKGGKMLASGRREEVL 221
Cdd:COG2274 649 IILENLRRLL-KGRTVIIIAHRL-STIRLADRIIVLDKGRIVEDGTHEELL 697
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
22-214 |
3.01e-22 |
|
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: 89.41 E-value: 3.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLLARMAGMTS-GKGSIQFAGQPLEAWSATKlalhraylsqqqtppfampvwhyltlhqhd 100
Cdd:cd03216 22 SVRRGEVHALLGENGAGKSTLMKILSGLYKpDSGEILVDGKEVSFASPRD------------------------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 101 ktrtellndvagALALddklGRST-NQLSGGEWQRVRLAAVVLQitpqanpAGQLLLLDEPMNSLDVAQQSALDKILSAL 179
Cdd:cd03216 72 ------------ARRA----GIAMvYQLSVGERQMVEIARALAR-------NARLLILDEPTAALTPAEVERLFKVIRRL 128
|
170 180 190
....*....|....*....|....*....|....*
gi 1432492527 180 CQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLAS 214
Cdd:cd03216 129 RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
22-210 |
3.41e-22 |
|
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: 91.01 E-value: 3.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLLARMAGM-TSGKGSIQFAGQPLEAWSATKLALHRA----YLSQQ-------------QT 83
Cdd:cd03255 26 SIEKGEFVAIVGPSGSGKSTLLNILGGLdRPTSGEVRVDGTDISKLSEKELAAFRRrhigFVFQSfnllpdltalenvEL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 84 PPFAMPVwhyltLHQHDKTR-TELLndvaGALALDDKLGRSTNQLSGGEWQRVRLA-AVVlqitpqANPagQLLLLDEPM 161
Cdd:cd03255 106 PLLLAGV-----PKKERRERaEELL----ERVGLGDRLNHYPSELSGGQQQRVAIArALA------NDP--KIILADEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1432492527 162 NSLDVAQQSALDKILSALCQQ-GLAIVMSSHDLNhTLRHAHRAWLLKGGK 210
Cdd:cd03255 169 GNLDSETGKEVMELLRELNKEaGTTIVVVTHDPE-LAEYADRIIELRDGK 217
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
22-215 |
4.80e-22 |
|
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: 90.64 E-value: 4.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLLARMAGM---TSGKgsIQFAGQPLEAWSATKLALHR---AYLSQQqtpPFA-----MPV 90
Cdd:cd03257 27 SIKKGETLGLVGESGSGKSTLARAILGLlkpTSGS--IIFDGKDLLKLSRRLRKIRRkeiQMVFQD---PMSslnprMTI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 91 WHYLT---LHQHDKTRTELLNDVAGALA----LDDK-LGRSTNQLSGGEWQRVRLA-AVVLqitpqaNPagQLLLLDEPM 161
Cdd:cd03257 102 GEQIAeplRIHGKLSKKEARKEAVLLLLvgvgLPEEvLNRYPHELSGGQRQRVAIArALAL------NP--KLLIADEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1432492527 162 NSLDVAQQSALDKILSALCQQ-GLAIVMSSHDLnHTLRH-AHRAWLLKGGKMLASG 215
Cdd:cd03257 174 SALDVSVQAQILDLLKKLQEElGLTLLFITHDL-GVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
16-210 |
9.45e-22 |
|
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: 88.59 E-value: 9.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 16 LGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGMTSG-KGSIQFAGQPLEAWSATKLALHRAYLSQQqTPPFAMPVWHyl 94
Cdd:cd03228 18 LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPtSGEILIDGVDLRDLDLESLRKNIAYVPQD-PFLFSGTIRE-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 95 tlhqhdktrtellndvagalalddklgrstNQLSGGEWQRVRLAAVVLQitpqaNPagQLLLLDEPMNSLDVAQQSALDK 174
Cdd:cd03228 95 ------------------------------NILSGGQRQRIAIARALLR-----DP--PILILDEATSALDPETEALILE 137
|
170 180 190
....*....|....*....|....*....|....*.
gi 1432492527 175 ILSALCqQGLAIVMSSHDLnHTLRHAHRAWLLKGGK 210
Cdd:cd03228 138 ALRALA-KGKTVIVIAHRL-STIRDADRIIVLDDGR 171
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
15-206 |
1.02e-21 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 93.51 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 15 RLGPLSGEVRAGEILHLVGPNGAGKSTLLARMAG-MTSGKGSIQFAGQPLEAWSATKLALHRAYLSQQqtpPFAMP--VW 91
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGfVDPTEGSIAVNGVPLADADADSWRDQIAWVPQH---PFLFAgtIA 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 92 HYLTLHQHDKTRTEL--------LNDVAGAL--ALDDKLGRSTNQLSGGEWQRVRLAAVVLQITPqanpagqLLLLDEPM 161
Cdd:TIGR02857 414 ENIRLARPDASDAEIrealeragLDEFVAALpqGLDTPIGEGGAGLSGGQAQRLALARAFLRDAP-------LLLLDEPT 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1432492527 162 NSLDVAQQSALDKILSALCqQGLAIVMSSHDLnHTLRHAHRAWLL 206
Cdd:TIGR02857 487 AHLDAETEAEVLEALRALA-QGRTVLLVTHRL-ALAALADRIVVL 529
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
19-224 |
3.15e-21 |
|
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: 88.90 E-value: 3.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKSTLLA---RMAGMTSGKgsIQFAGQPLEAWSATKLALHRAYLSQQQTPPFAMPVWHYLT 95
Cdd:cd03295 20 LNLEIAKGEFLVLIGPSGSGKTTTMKminRLIEPTSGE--IFIDGEDIREQDPVELRRKIGYVIQQIGLFPHMTVEENIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 96 L---------HQHDKTRTELLNDVagalALDDK--LGRSTNQLSGGEWQRVRLAAVVlqitpQANPagQLLLLDEPMNSL 164
Cdd:cd03295 98 LvpkllkwpkEKIRERADELLALV----GLDPAefADRYPHELSGGQQQRVGVARAL-----AADP--PLLLMDEPFGAL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1432492527 165 DVAQQSALDKILSALCQQ-GLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPP 224
Cdd:cd03295 167 DPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSP 227
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
22-235 |
3.24e-21 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 88.55 E-value: 3.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLLARMAGMTS-GKGSIQFAGQPLeawsaTKLALH-RA-----YLSQQQTppfampVWHYL 94
Cdd:COG1137 25 EVNQGEIVGLLGPNGAGKTTTFYMIVGLVKpDSGRIFLDGEDI-----THLPMHkRArlgigYLPQEAS------IFRKL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 95 T--------LHQHDKTRTE-------LLND-----VAGALALddklgrstnQLSGGEWQRVRLA-AVVlqitpqANPagQ 153
Cdd:COG1137 94 TvednilavLELRKLSKKEreerleeLLEEfgithLRKSKAY---------SLSGGERRRVEIArALA------TNP--K 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 154 LLLLDEPMNSLD---VAQqsaLDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPPNLAQAY 230
Cdd:COG1137 157 FILLDEPFAGVDpiaVAD---IQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPLVRKVY 233
|
....*.
gi 1432492527 231 -GMNFR 235
Cdd:COG1137 234 lGEDFR 239
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
22-221 |
3.72e-21 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 88.26 E-value: 3.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLLARMAGMT-SGKGSIQFAGQPLEAWSATKLAlhRAYLSQQqtpPFAMPVWHYLT----- 95
Cdd:cd03224 22 TVPEGEIVALLGRNGAGKTTLLKTIMGLLpPRSGSIRFDGRDITGLPPHERA--RAGIGYV---PEGRRIFPELTveenl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 96 ----LHQHDKTRTELLNDVAGAL-ALDDKLGRSTNQLSGGEWQRVRLAAVVLqitpqANPagQLLLLDEPMNSL--DVAQ 168
Cdd:cd03224 97 llgaYARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALM-----SRP--KLLLLDEPSEGLapKIVE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1432492527 169 QsaLDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVL 221
Cdd:cd03224 170 E--IFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
22-222 |
5.41e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 88.10 E-value: 5.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLLARMAG-MTSGKGSIQFAGQPleawsatklalHRAylsqqqTPPFAMPV---------W 91
Cdd:PRK10771 21 TVERGERVAILGPSGAGKSTLLNLIAGfLTPASGSLTLNGQD-----------HTT------TPPSRRPVsmlfqennlF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 92 HYLTLHQH-----------DKTRTELLNDVAGALALDDKLGRSTNQLSGGEWQRVRLAAVVLQITPqanpagqLLLLDEP 160
Cdd:PRK10771 84 SHLTVAQNiglglnpglklNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQP-------ILLLDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1432492527 161 MNSLDVAQQSALDKILSALC-QQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLT 222
Cdd:PRK10771 157 FSALDPALRQEMLTLVSQVCqERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
16-215 |
2.06e-20 |
|
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: 86.03 E-value: 2.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 16 LGPLSGEVRAGEILHLVGPNGAGKSTLLARMAG-MTSGKGSIQFAGQPLeawsaTKLALHR---AYLSQQqtppFAMpvW 91
Cdd:cd03259 16 LDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGlERPDSGEILIDGRDV-----TGVPPERrniGMVFQD----YAL--F 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 92 HYLTLHQH-----------DKTRTELLNDVAGALALDDKLGRSTNQLSGGEWQRVRLA-AVVLQitPqanpagQLLLLDE 159
Cdd:cd03259 85 PHLTVAENiafglklrgvpKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALArALARE--P------SLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1432492527 160 PMNSLDVAQQSALDKILSALC-QQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASG 215
Cdd:cd03259 157 PLSALDAKLREELREELKELQrELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
22-230 |
3.21e-20 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 86.08 E-value: 3.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLLARMAGMTSG-KGSIQFAGQPLEAWSATKLALHR---AYLSQQ---------------- 81
Cdd:cd03256 23 SINPGEFVALIGPSGAGKSTLLRCLNGLVEPtSGSVLIDGTDINKLKGKALRQLRrqiGMIFQQfnlierlsvlenvlsg 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 82 ---QTPPF-AMPVWhyltLHQHDKTRT-ELLNDVAgalaLDDKLGRSTNQLSGGEWQRVRLAAVVLQitpqaNPagQLLL 156
Cdd:cd03256 103 rlgRRSTWrSLFGL----FPKEEKQRAlAALERVG----LLDKAYQRADQLSGGQQQRVAIARALMQ-----QP--KLIL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1432492527 157 LDEPMNSLDVAQQSALDKILSALCQQ-GLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEvLTPPNLAQAY 230
Cdd:cd03256 168 ADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAE-LTDEVLDEIY 241
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
22-224 |
3.28e-20 |
|
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: 86.40 E-value: 3.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLLARMAGMTSG-KGSIQFAGQPLEAwsATKLALHRA--YLSQQqtpPFA-----MPVWHY 93
Cdd:COG1124 27 EVAPGESFGLVGESGSGKSTLLRALAGLERPwSGEVTFDGRPVTR--RRRKAFRRRvqMVFQD---PYAslhprHTVDRI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 94 LT--LHQHDKTRT-----ELLNDVAgalaLDDK-LGRSTNQLSGGEWQRVRLA-AVVLQitPqanpagQLLLLDEPMNSL 164
Cdd:COG1124 102 LAepLRIHGLPDReeriaELLEQVG----LPPSfLDRYPHQLSGGQRQRVAIArALILE--P------ELLLLDEPTSAL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1432492527 165 DVAQQSaldKILSALC----QQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPP 224
Cdd:COG1124 170 DVSVQA---EILNLLKdlreERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGP 230
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
19-215 |
5.15e-20 |
|
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: 85.25 E-value: 5.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKSTLLARMAGMTS-GKGSIQFAGQPLeawsATKLALHRAYLS---QQQTppfampVWHYL 94
Cdd:cd03263 21 LSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRpTSGTAYINGYSI----RTDRKAARQSLGycpQFDA------LFDEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 95 TLHQH-----------DKTRTELLNDVAGALALDDKLGRSTNQLSGGEWQRVRLAAVVLqitpqANPagQLLLLDEPMNS 163
Cdd:cd03263 91 TVREHlrfyarlkglpKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALI-----GGP--SVLLLDEPTSG 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1432492527 164 LDVAQQSALDKILSALcQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASG 215
Cdd:cd03263 164 LDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
31-234 |
1.00e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 85.56 E-value: 1.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 31 LVGPNGAGKSTLLARMAGM-TSGKGSIQFAGQPL----EAWSATKLALhraylsQQQTPP---FAMPVWHYLTLHQHDK- 101
Cdd:PRK13647 36 LLGPNGAGKSTLLLHLNGIyLPQRGRVKVMGREVnaenEKWVRSKVGL------VFQDPDdqvFSSTVWDDVAFGPVNMg 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 102 -TRTELLNDVAGALA---LDDKLGRSTNQLSGGEWQRVRLAAVvLQITPQanpagqLLLLDEPMNSLDVAQQSALDKILS 177
Cdd:PRK13647 110 lDKDEVERRVEEALKavrMWDFRDKPPYHLSYGQKKRVAIAGV-LAMDPD------VIVLDEPMAYLDPRGQETLMEILD 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1432492527 178 ALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRReEVLTPPNLAQAYGMNF 234
Cdd:PRK13647 183 RLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK-SLLTDEDIVEQAGLRL 238
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
19-225 |
1.68e-19 |
|
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: 84.09 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKSTLLARMAG-MTSGKGSIQFAGQPLEAWSATKLALHR---AYLSQQQTPpF-------- 86
Cdd:cd03261 19 VDLDVRRGEILAIIGPSGSGKSTLLRLIVGlLRPDSGEVLIDGEDISGLSEAELYRLRrrmGMLFQSGAL-Fdsltvfen 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 87 -AMPvwhyltLHQH----DKTRTELLNDVAGALALDDKLGRSTNQLSGGEWQRVRLA-AVVLqitpqaNPagQLLLLDEP 160
Cdd:cd03261 98 vAFP------LREHtrlsEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALArALAL------DP--ELLLYDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1432492527 161 MNSLD-VAQQSALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPPN 225
Cdd:cd03261 164 TAGLDpIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASDD 229
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
16-215 |
1.80e-19 |
|
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: 83.40 E-value: 1.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 16 LGPLSGEVRAGeILHLVGPNGAGKSTLLARMAGMTS-GKGSIQFAGQPLEAwSATKLALHRAYLSQQQTPPFAMPVWHYL 94
Cdd:cd03264 16 LDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPpSSGTIRIDGQDVLK-QPQKLRRRIGYLPQEFGVYPNFTVREFL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 95 ----TLHQ-HDKTRTELLNDVAGALALDDKLGRSTNQLSGGEWQRVRLAAVVLqitpqANPagQLLLLDEPMNSLDVAQQ 169
Cdd:cd03264 94 dyiaWLKGiPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALV-----GDP--SILIVDEPTAGLDPEER 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1432492527 170 SALDKILSALcQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASG 215
Cdd:cd03264 167 IRFRNLLSEL-GEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
22-230 |
3.02e-19 |
|
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: 86.28 E-value: 3.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLLARMAGMTSGKGSIQFAGQPLEAWSATKLalhRAYLSQQQT---PPFA-----MPVWHY 93
Cdd:COG4172 308 TLRRGETLGLVGESGSGKSTLGLALLRLIPSEGEIRFDGQDLDGLSRRAL---RPLRRRMQVvfqDPFGslsprMTVGQI 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 94 ----LTLHQHDKTRTELLNDVAGALA---LD-DKLGRSTNQLSGGEWQRVRLA-AVVLQitPqanpagQLLLLDEPMNSL 164
Cdd:COG4172 385 iaegLRVHGPGLSAAERRARVAEALEevgLDpAARHRYPHEFSGGQRQRIAIArALILE--P------KLLVLDEPTSAL 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1432492527 165 DVAQQSALDKILSALCQQ-GLAIVMSSHDLnHTLRH-AHRAWLLKGGKMLASGRREEVLTPPnlAQAY 230
Cdd:COG4172 457 DVSVQAQILDLLRDLQREhGLAYLFISHDL-AVVRAlAHRVMVMKDGKVVEQGPTEQVFDAP--QHPY 521
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-210 |
4.25e-19 |
|
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: 81.46 E-value: 4.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 5 MQLQDVA----ESTRLGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGMTS-GKGSIQFAGQPLEAWSATKLALHR--AY 77
Cdd:cd03229 1 LELKNVSkrygQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEpDSGSILIDGEDLTDLEDELPPLRRriGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 78 LSQQQTPPFAMPVWHYLTLhqhdktrtellndvagalalddklgrstnQLSGGEWQRVRLA-AVVLqitpqaNPagQLLL 156
Cdd:cd03229 81 VFQDFALFPHLTVLENIAL-----------------------------GLSGGQQQRVALArALAM------DP--DVLL 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1432492527 157 LDEPMNSLDVAQQSALDKILSALCQQ-GLAIVMSSHDLNHTLRHAHRAWLLKGGK 210
Cdd:cd03229 124 LDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
19-235 |
4.50e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 83.02 E-value: 4.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKSTLLARMAGMTS-GKGSIQFAGQPLeawsaTKLALH-RA-----YLSQQQTPPFAMPVW 91
Cdd:PRK10895 22 VSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPrDAGNIIIDDEDI-----SLLPLHaRArrgigYLPQEASIFRRLSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 92 ----------HYLTLHQHDKTRTELLNDVAGAlALDDKLGRStnqLSGGEWQRVRLAAVVlqitpQANPagQLLLLDEPM 161
Cdd:PRK10895 97 dnlmavlqirDDLSAEQREDRANELMEEFHIE-HLRDSMGQS---LSGGERRRVEIARAL-----AANP--KFILLDEPF 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1432492527 162 NSLDVAQQSALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPPNLAQAY-GMNFR 235
Cdd:PRK10895 166 AGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYlGEDFR 240
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
22-230 |
4.66e-19 |
|
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: 82.72 E-value: 4.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLLARMAGMTSGK-GSIQFAGQPLEAWSATKLAlhRAYLSQqqtppfaMP----VWHYLTL 96
Cdd:COG0410 25 EVEEGEIVALLGRNGAGKTTLLKAISGLLPPRsGSIRFDGEDITGLPPHRIA--RLGIGY-------VPegrrIFPSLTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 97 H-------QHDKTRTELLNDVAGALA----LDDKLGRSTNQLSGGEWQRVRLA-AVVlqitpqANPagQLLLLDEPmnSL 164
Cdd:COG0410 96 EenlllgaYARRDRAEVRADLERVYElfprLKERRRQRAGTLSGGEQQMLAIGrALM------SRP--KLLLLDEP--SL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1432492527 165 DVAQQSALD--KILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPPNLAQAY 230
Cdd:COG0410 166 GLAPLIVEEifEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEVREAY 233
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
22-230 |
7.23e-19 |
|
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: 82.78 E-value: 7.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLLARMAGM---TSgkGSIQFAGQPLEAWSATKLA---LHRAYlsqQQTPPFA-MPVWHYL 94
Cdd:COG0411 26 EVERGEIVGLIGPNGAGKTTLFNLITGFyrpTS--GRILFDGRDITGLPPHRIArlgIARTF---QNPRLFPeLTVLENV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 95 TLHQHDKTRTELLN--------------------DVAGALALDDKLGRSTNQLSGGEWQRVRLA-AVVLQitPqanpagQ 153
Cdd:COG0411 101 LVAAHARLGRGLLAallrlprarreereareraeELLERVGLADRADEPAGNLSYGQQRRLEIArALATE--P------K 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1432492527 154 LLLLDEPMNSLDVAQQSALDKILSALCQ-QGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPPNLAQAY 230
Cdd:COG0411 173 LLLLDEPAAGLNPEETEELAELIRRLRDeRGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVRADPRVIEAY 250
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
23-210 |
7.27e-19 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 81.53 E-value: 7.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 23 VRAGEILHLVGPNGAGKSTLLARMAGMT-SGKGSIQFAGQPLEAWSATKLAlhrAYLSQQ-QTPPFAMPVWHYLTLhqHD 100
Cdd:cd03226 23 LYAGEIIALTGKNGAGKTTLAKILAGLIkESSGSILLNGKPIKAKERRKSI---GYVMQDvDYQLFTDSVREELLL--GL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 101 KTRTELLNDVAGAL------ALDDKLGRStnqLSGGEWQRVRLAAVVLQITPqanpagqLLLLDEPMNSLDVAQQSALDK 174
Cdd:cd03226 98 KELDAGNEQAETVLkdldlyALKERHPLS---LSGGQKQRLAIAAALLSGKD-------LLIFDEPTSGLDYKNMERVGE 167
|
170 180 190
....*....|....*....|....*....|....*.
gi 1432492527 175 ILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGK 210
Cdd:cd03226 168 LIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGA 203
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
16-211 |
7.43e-19 |
|
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: 82.07 E-value: 7.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 16 LGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGM-TSGKGSIQFAGQPLEAWSATKLALHRAY-------------LSQQ 81
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEeLPTSGTIRVNGQDVSDLRGRAIPYLRRKigvvfqdfrllpdRNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 82 QTPPFAMPVwhyltlhqHDKTRTELLNDVAGALA---LDDKLGRSTNQLSGGEWQRVRLA-AVVlqitpqANPAgqLLLL 157
Cdd:cd03292 97 ENVAFALEV--------TGVPPREIRKRVPAALElvgLSHKHRALPAELSGGEQQRVAIArAIV------NSPT--ILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1432492527 158 DEPMNSLDVAQQSALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKM 211
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
22-225 |
2.44e-18 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 82.84 E-value: 2.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLLaRM-AGM---TSGkgSIQFAGQPLeawsaTKLALHR---AYLSQQqtppFA-MPvwHy 93
Cdd:COG3842 27 SIEPGEFVALLGPSGCGKTTLL-RMiAGFetpDSG--RILLDGRDV-----TGLPPEKrnvGMVFQD----YAlFP--H- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 94 LT--------LHQHDKTRTELLNDVAGALA---LDDKLGRSTNQLSGGEWQRVRLA-AVVLQitPqanpagQLLLLDEPM 161
Cdd:COG3842 92 LTvaenvafgLRMRGVPKAEIRARVAELLElvgLEGLADRYPHQLSGGQQQRVALArALAPE--P------RVLLLDEPL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1432492527 162 NSLDvAQ-----QSALDKILSALcqqGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPPN 225
Cdd:COG3842 164 SALD-AKlreemREELRRLQREL---GITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPA 228
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
22-227 |
2.59e-18 |
|
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: 82.84 E-value: 2.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLLARMAGMTSG-KGSIQFAGQPLEAwSATKLAL--HR---AYLSQQQTppfampvwhylt 95
Cdd:COG4148 21 TLPGRGVTALFGPSGSGKTTLLRAIAGLERPdSGRIRLGGEVLQD-SARGIFLppHRrriGYVFQEAR------------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 96 LHQH---------------DKTRTELLNDVAGALALDDKLGRSTNQLSGGEWQRVRLAAVVLqitpqANPagQLLLLDEP 160
Cdd:COG4148 88 LFPHlsvrgnllygrkrapRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALL-----SSP--RLLLMDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1432492527 161 MNSLDVAQQSALDKILSALCQQ-GLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPPNLA 227
Cdd:COG4148 161 LAALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLL 228
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
23-215 |
6.99e-18 |
|
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: 6.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 23 VRAGEILHLVGPNGAGKSTLLARMAGM-TSGKGSIQFAGQPLEAwsatklalhraylsqqqTPPFAMPV---------WH 92
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFeTPQSGRVLINGVDVTA-----------------APPADRPVsmlfqennlFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 93 YLTLHQHD--------KTRTELLNDVAGALA---LDDKLGRSTNQLSGGEWQRVRLAAVVLQITPqanpagqLLLLDEPM 161
Cdd:cd03298 84 HLTVEQNVglglspglKLTAEDRQAIEVALArvgLAGLEKRLPGELSGGERQRVALARVLVRDKP-------VLLLDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1432492527 162 NSLDVAQQSALDKILSALC-QQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASG 215
Cdd:cd03298 157 AALDPALRAEMLDLVLDLHaETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
19-225 |
9.70e-18 |
|
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: 79.25 E-value: 9.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKSTLLARMAG-MTSGKGSIQFAGQPLEAWSATKLALHRA---YLSQQQtppfA----MPV 90
Cdd:COG1127 24 VSLDVPRGEILAIIGGSGSGKSVLLKLIIGlLRPDSGEILVDGQDITGLSEKELYELRRrigMLFQGG----AlfdsLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 91 WH--YLTLHQH-DKTRTELLNDVAGALA---LDDKLGRSTNQLSGGEWQRVRLA-AVVLqitpqaNPagQLLLLDEPMNS 163
Cdd:COG1127 100 FEnvAFPLREHtDLSEAEIRELVLEKLElvgLPGAADKMPSELSGGMRKRVALArALAL------DP--EILLYDEPTAG 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1432492527 164 LDVAQQSALDKILSALCQQ-GLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPPN 225
Cdd:COG1127 172 LDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASDD 234
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
22-226 |
1.20e-17 |
|
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: 80.93 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLLARMAGMTS-GKGSIQFAGQPL-EAWSATKLALHR---AYLSQQQTppfampvwhyltL 96
Cdd:TIGR02142 19 TLPGQGVTAIFGRSGSGKTTLIRLIAGLTRpDEGEIVLNGRTLfDSRKGIFLPPEKrriGYVFQEAR------------L 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 97 HQHDKTRTELL---------------NDVAGALALDDKLGRSTNQLSGGEWQRVRLAAVVLqitpqANPagQLLLLDEPM 161
Cdd:TIGR02142 87 FPHLSVRGNLRygmkrarpserrisfERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALL-----SSP--RLLLMDEPL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1432492527 162 NSLDVAQQSALDKILSALCQQ-GLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPPNL 226
Cdd:TIGR02142 160 AALDDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDL 225
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
14-241 |
1.38e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 79.54 E-value: 1.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 14 TRLGPLSGEVRAGEILHLVGPNGAGKSTLL-ARMAGMTSGKGSIQFAGQPleawsaTKLALHR---AYLSQQQTPPFAMP 89
Cdd:PRK15056 21 TALRDASFTVPGGSIAALVGVNGSGKSTLFkALMGFVRLASGKISILGQP------TRQALQKnlvAYVPQSEEVDWSFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 90 VW-----------HYLTLHQHDKTRTELLNDVAGALALDDKLGRSTNQLSGGEWQRVRLAAVVLQitpqanpAGQLLLLD 158
Cdd:PRK15056 95 VLvedvvmmgrygHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQ-------QGQVILLD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 159 EPMNSLDVAQQSALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKgGKMLASGRREEVLTPPNLAQAYGMNFRRLD 238
Cdd:PRK15056 168 EPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVK-GTVLASGPTETTFTAENLELAFSGVLRHVA 246
|
...
gi 1432492527 239 IEG 241
Cdd:PRK15056 247 LNG 249
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
19-193 |
1.45e-17 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 78.59 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKSTLLARMAGMTS-GKGSIQFAGQPleaWSATKLalhRAYLSQQQTPPfampVWHYLTLH 97
Cdd:TIGR03740 19 ISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRpTSGEIIFDGHP---WTRKDL---HKIGSLIESPP----LYENLTAR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 98 QHDKTRTELL-------NDVAGALALDDKLGRSTNQLSGGEWQRVRLAAVVLQitpqaNPagQLLLLDEPMNSLDVAQQS 170
Cdd:TIGR03740 89 ENLKVHTTLLglpdsriDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLN-----HP--KLLILDEPTNGLDPIGIQ 161
|
170 180
....*....|....*....|...
gi 1432492527 171 ALDKILSALCQQGLAIVMSSHDL 193
Cdd:TIGR03740 162 ELRELIRSFPEQGITVILSSHIL 184
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
16-193 |
1.81e-17 |
|
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: 78.28 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 16 LGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGMTS-GKGSIQFAGQPLEAWSAtklalHRAYLSQQqtpPFAMPvWhyL 94
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERpTSGEVLVDGEPVTGPGP-----DRGYVFQQ---DALLP-W--L 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 95 TLHQ--------HDKTRTELLNDVAGALA---LDDKLGRSTNQLSGGEWQRVRLA-AVVLqitpqaNPagQLLLLDEPMN 162
Cdd:cd03293 89 TVLDnvalglelQGVPKAEARERAEELLElvgLSGFENAYPHQLSGGMRQRVALArALAV------DP--DVLLLDEPFS 160
|
170 180 190
....*....|....*....|....*....|..
gi 1432492527 163 SLDVAQQSAL-DKILSALCQQGLAIVMSSHDL 193
Cdd:cd03293 161 ALDALTREQLqEELLDIWRETGKTVLLVTHDI 192
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
26-215 |
2.23e-17 |
|
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: 77.72 E-value: 2.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 26 GEILHLVGPNGAGKSTLLARMAGMTS-GKGSIQFAGQPLEAwSATKLAL-----HRAYLSQQQTPPFAMPVWH---YLTL 96
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKpDGGTIVLNGTVLFD-SRKKINLppqqrKIGLVFQQYALFPHLNVREnlaFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 97 HQHDKTRTELLNDVAGALALDDKLGRSTNQLSGGEWQRVRLAAVVLqitpqANPAgqLLLLDEPMNSLDVAQQSALDKIL 176
Cdd:cd03297 102 RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALA-----AQPE--LLLLDEPFSALDRALRLQLLPEL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1432492527 177 SALCQQ-GLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASG 215
Cdd:cd03297 175 KQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
22-236 |
4.71e-17 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 78.07 E-value: 4.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLLARMAGM---TSGKgsIQFAGQPLEAWSATKL-ALHRAYLS---QQqtppFA-MPvwHY 93
Cdd:cd03294 46 DVREGEIFVIMGLSGSGKSTLLRCINRLiepTSGK--VLIDGQDIAAMSRKELrELRRKKISmvfQS----FAlLP--HR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 94 LTL----------HQHDKTRTELLNDVAGALALDDKLGRSTNQLSGGEWQRVRLA-AVVlqitpqANPagQLLLLDEPMN 162
Cdd:cd03294 118 TVLenvafglevqGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLArALA------VDP--DILLMDEAFS 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1432492527 163 SLD-VAQQSALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPPnlAQAYGMNFRR 236
Cdd:cd03294 190 ALDpLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNP--ANDYVREFFR 262
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
19-192 |
9.51e-17 |
|
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: 75.54 E-value: 9.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKSTLLARMAG-MTSGKGSIQFAGQPLeAWSATKLALHR---AYLSQ---QQTppFAMPVW 91
Cdd:TIGR01166 11 LNFAAERGEVLALLGANGAGKSTLLLHLNGlLRPQSGAVLIDGEPL-DYSRKGLLERRqrvGLVFQdpdDQL--FAADVD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 92 H-----YLTLHQHDKTRTELLNDVAGALALDDKLGRSTNQLSGGEWQRVRLA-AVVLQitpqanpaGQLLLLDEPMNSLD 165
Cdd:TIGR01166 88 QdvafgPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAgAVAMR--------PDVLLLDEPTAGLD 159
|
170 180
....*....|....*....|....*..
gi 1432492527 166 VAQQSALDKILSALCQQGLAIVMSSHD 192
Cdd:TIGR01166 160 PAGREQMLAILRRLRAEGMTVVISTHD 186
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
19-215 |
1.04e-16 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 76.16 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKSTLLARMAGMTSGK----GSIQFAGQPLEAWSATKlalHRAYLSQQQ------------ 82
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttsGQILFNGQPRKPDQFQK---CVAYVRQDDillpgltvretl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 83 --TPPFAMPVwhyltlHQHDKTRTELLNDVA-GALALDDKLGRSTNQLSGGEWQRVRLAAVVLQitpqaNPAgqLLLLDE 159
Cdd:cd03234 103 tyTAILRLPR------KSSDAIRKKRVEDVLlRDLALTRIGGNLVKGISGGERRRVSIAVQLLW-----DPK--VLILDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 160 PMNSLDVAQQSALDKILSALCQQGLAIVMSSH----DLnhtLRHAHRAWLLKGGKMLASG 215
Cdd:cd03234 170 PTSGLDSFTALNLVSTLSQLARRNRIVILTIHqprsDL---FRLFDRILLLSSGEIVYSG 226
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
26-225 |
1.54e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 77.95 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 26 GEILHLVGPNGAGKSTLLARMAGM-TSGKGSIQFAGQPLeawsatklalhraylsqQQTPPFAMPV---------WHYLT 95
Cdd:PRK11607 45 GEIFALLGASGCGKSTLLRMLAGFeQPTAGQIMLDGVDL-----------------SHVPPYQRPInmmfqsyalFPHMT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 96 LHQH-------DK-TRTELLNDVAGALAL---DDKLGRSTNQLSGGEWQRVRLAAvVLQITPqanpagQLLLLDEPMNSL 164
Cdd:PRK11607 108 VEQNiafglkqDKlPKAEIASRVNEMLGLvhmQEFAKRKPHQLSGGQRQRVALAR-SLAKRP------KLLLLDEPMGAL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1432492527 165 DVAQQSALD-KILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPPN 225
Cdd:PRK11607 181 DKKLRDRMQlEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPT 242
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
19-210 |
2.63e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 77.80 E-value: 2.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKSTLLARMAG-MTSGKGSIQfagqpleaWSATklaLHRAYLSQQQT--PPfAMPVWHYLT 95
Cdd:COG0488 334 LSLRIDRGDRIGLIGPNGAGKSTLLKLLAGeLEPDSGTVK--------LGET---VKIGYFDQHQEelDP-DKTVLDELR 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 96 LHQHDKTRTELLNdVAGALALD-DKLGRSTNQLSGGEWQRVRLAAVVLQitpQANpagqLLLLDEPMNSLDVAqqsALDK 174
Cdd:COG0488 402 DGAPGGTEQEVRG-YLGRFLFSgDDAFKPVGVLSGGEKARLALAKLLLS---PPN----VLLLDEPTNHLDIE---TLEA 470
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1432492527 175 ILSALCQ-QGlAIVMSSHDlnhtlRH-----AHRAWLLKGGK 210
Cdd:COG0488 471 LEEALDDfPG-TVLLVSHD-----RYfldrvATRILEFEDGG 506
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
19-215 |
2.68e-16 |
|
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: 75.45 E-value: 2.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKSTLLARMAG-MTSGKGSIQFAGqpLEAWSATKLALHR--AYLSQQQTPPFAMPVWHYLT 95
Cdd:cd03267 40 ISFTIEKGEIVGFIGPNGAGKTTTLKILSGlLQPTSGEVRVAG--LVPWKRRKKFLRRigVVFGQKTQLWWDLPVIDSFY 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 96 LHQH----DKTR-TELLNDVAGALALDDKLGRSTNQLSGGEWQRVRLAAVVLQitpqaNPagQLLLLDEPMNSLDVAQQS 170
Cdd:cd03267 118 LLAAiydlPPARfKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLH-----EP--EILFLDEPTIGLDVVAQE 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1432492527 171 ALDKILSALCQQ-GLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASG 215
Cdd:cd03267 191 NIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
19-215 |
2.83e-16 |
|
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: 75.10 E-value: 2.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKSTLLARMAGMTS-GKGSIQFAG-----QPLEAWSatKLALHRAylsqqqtppfAMPVWH 92
Cdd:cd03266 24 VSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEpDAGFATVDGfdvvkEPAEARR--RLGFVSD----------STGLYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 93 YLTLHQ--------HDKTRTEL---LNDVAGALALDDKLGRSTNQLSGGEWQRVRLAAVVLQitpqanpAGQLLLLDEPM 161
Cdd:cd03266 92 RLTAREnleyfaglYGLKGDELtarLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVH-------DPPVLLLDEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1432492527 162 NSLDVAQQSALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASG 215
Cdd:cd03266 165 TGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
21-176 |
2.85e-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: 75.52 E-value: 2.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 21 GEVRAGEILHLVGPNGAGKSTLLARMAGMTSGKGsiqfaGQPLeaWSATKLalhrAYLSQQQTPPFAMPVWHYLtlhqHD 100
Cdd:cd03237 20 GSISESEVIGILGPNGIGKTTFIKMLAGVLKPDE-----GDIE--IELDTV----SYKPQYIKADYEGTVRDLL----SS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 101 KTR-----TELLNDVAGALALDDKLGRSTNQLSGGEWQRVRLAAVVLQitpqanPAgQLLLLDEPMNSLDVAQQSALDKI 175
Cdd:cd03237 85 ITKdfythPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSK------DA-DIYLLDEPSAYLDVEQRLMASKV 157
|
.
gi 1432492527 176 L 176
Cdd:cd03237 158 I 158
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
23-211 |
3.19e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 75.88 E-value: 3.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 23 VRAGEILHLVGPNGAGKSTLLARMAGMTS-GKGSIQFAGQPLEAWS-ATKLALHRAYLSQQQTPPFAM------------ 88
Cdd:PRK10419 35 LKSGETVALLGRSGCGKSTLARLLVGLESpSQGNVSWRGEPLAKLNrAQRKAFRRDIQMVFQDSISAVnprktvreiire 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 89 PVWHYLTLHQHDKTR--TELLNDVAGALALDDKLgrsTNQLSGGEWQRVRLAAvVLQITPqanpagQLLLLDEPMNSLDV 166
Cdd:PRK10419 115 PLRHLLSLDKAERLAraSEMLRAVDLDDSVLDKR---PPQLSGGQLQRVCLAR-ALAVEP------KLLILDEAVSNLDL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1432492527 167 AQQSALDKILSALCQQ-GLAIVMSSHDLNHTLRHAHRAWLLKGGKM 211
Cdd:PRK10419 185 VLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
16-225 |
3.76e-16 |
|
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: 74.97 E-value: 3.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 16 LGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGM-TSGKGSIQFAGQPLeawsatklalhraylsqQQTPPFAMPV---- 90
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFeTPTSGEILLDGKDI-----------------TNLPPHKRPVntvf 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 91 WHY---------------LTLHQHDKTrtELLNDVAGALA---LDDKLGRSTNQLSGGEWQRVRLA-AVVLQitPqanpa 151
Cdd:cd03300 79 QNYalfphltvfeniafgLRLKKLPKA--EIKERVAEALDlvqLEGYANRKPSQLSGGQQQRVAIArALVNE--P----- 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1432492527 152 gQLLLLDEPMNSLDVAQQSALDKILSALCQQ-GLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPPN 225
Cdd:cd03300 150 -KVLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
19-215 |
4.17e-16 |
|
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: 74.18 E-value: 4.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKSTLLARMAGM---TSGKgsIQFAGQpleAWSATKLALHR--AYLSqqqTPPFAMpvwhY 93
Cdd:cd03268 19 ISLHVKKGEIYGFLGPNGAGKTTTMKIILGLikpDSGE--ITFDGK---SYQKNIEALRRigALIE---APGFYP----N 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 94 LTLHQHDKT-------RTELLNDVAGALALDDKLGRSTNQLSGGEWQRVRLAAVVLqitpqANPagQLLLLDEPMNSLDV 166
Cdd:cd03268 87 LTARENLRLlarllgiRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALL-----GNP--DLLILDEPTNGLDP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1432492527 167 AQQSALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASG 215
Cdd:cd03268 160 DGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
19-221 |
4.52e-16 |
|
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: 77.10 E-value: 4.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKSTLLARMAGM-TSGKGSIQFAGQPLEAWSATKLALHRAYLSQQqtppfampvwhyltlh 97
Cdd:COG4618 351 VSFSLEPGEVLGVIGPSGSGKSTLARLLVGVwPPTAGSVRLDGADLSQWDREELGRHIGYLPQD---------------- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 98 qhdktrTELLN----------------DV------AGA----LAL----DDKLGRSTNQLSGGEWQRVRLA-AVVlqitp 146
Cdd:COG4618 415 ------VELFDgtiaeniarfgdadpeKVvaaaklAGVhemiLRLpdgyDTRIGEGGARLSGGQRQRIGLArALY----- 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1432492527 147 qANPAgqLLLLDEPMNSLDVAQQSALDKILSALCQQGLAIVMSSHDLNhTLRHAHRAWLLKGGKMLASGRREEVL 221
Cdd:COG4618 484 -GDPR--LVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDEVL 554
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
16-226 |
6.46e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 76.42 E-value: 6.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 16 LGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGMTSGKGSIQFAGQPLEAWSATKLALHRAYLSQQqtpP--FAMPVWHY 93
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQGSLKINGIELRELDPESWRKHLSWVGQN---PqlPHGTLRDN 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 94 LTLHQHDKTRTELLNDVAGA----------LALDDKLGRSTNQLSGGEWQRVRLAAVVLQitpqanpAGQLLLLDEPMNS 163
Cdd:PRK11174 443 VLLGNPDASDEQLQQALENAwvseflpllpQGLDTPIGDQAAGLSVGQAQRLALARALLQ-------PCQLLLLDEPTAS 515
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1432492527 164 LDVaqQSAlDKILSALCQ--QGLAIVMSSHDLNHtLRHAHRAWLLKGGKMLASGRREEVLTPPNL 226
Cdd:PRK11174 516 LDA--HSE-QLVMQALNAasRRQTTLMVTHQLED-LAQWDQIWVMQDGQIVQQGDYAELSQAGGL 576
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
22-221 |
6.53e-16 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 76.36 E-value: 6.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKST---LLARMAGMTSgkGSIQFAGQPLEAWSATKLalhRAYLS--QQQTPPFAMPVWHYLTL 96
Cdd:COG1132 362 TIPPGETVALVGPSGSGKSTlvnLLLRFYDPTS--GRILIDGVDIRDLTLESL---RRQIGvvPQDTFLFSGTIRENIRY 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 97 HQHDKTRTELLN--DVAGA----LALDDKL----GRSTNQLSGGEWQRVRLAAVVLqitpqANPagQLLLLDEPMNSLDV 166
Cdd:COG1132 437 GRPDATDEEVEEaaKAAQAhefiEALPDGYdtvvGERGVNLSGGQRQRIAIARALL-----KDP--PILILDEATSALDT 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1432492527 167 ----AQQSALDKILsalcqQGLAIVMSSHDLnHTLRHAHRAWLLKGGKMLASGRREEVL 221
Cdd:COG1132 510 eteaLIQEALERLM-----KGRTTIVIAHRL-STIRNADRILVLDDGRIVEQGTHEELL 562
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
16-191 |
8.30e-16 |
|
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: 73.16 E-value: 8.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 16 LGPLSGEVRAGEILHLVGPNGAGKSTLLARMAG-MTSGKGSIQFAGQPLeAWSATKLALHRAYLSQQQTPPFAMPVWHYL 94
Cdd:TIGR01189 16 FEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGlLRPDSGEVRWNGTPL-AEQRDEPHENILYLGHLPGLKPELSALENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 95 TLHQHDKTRTELlnDVAGALA---LDDKLGRSTNQLSGGEWQRVRLAAVVLQITPqanpagqLLLLDEPMNSLDVAQQSA 171
Cdd:TIGR01189 95 HFWAAIHGGAQR--TIEDALAavgLTGFEDLPAAQLSAGQQRRLALARLWLSRRP-------LWILDEPTTALDKAGVAL 165
|
170 180
....*....|....*....|
gi 1432492527 172 LDKILSALCQQGLAIVMSSH 191
Cdd:TIGR01189 166 LAGLLRAHLARGGIVLLTTH 185
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
16-194 |
8.46e-16 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 73.67 E-value: 8.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 16 LGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGMT----SGKGSIQFAGQPLeawsaTKLALHR---AYLSQQ------- 81
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLspafSASGEVLLNGRRL-----TALPAEQrriGILFQDdllfphl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 82 ---QTPPFAMPvwhyltlhqHDKTRTELLNDVAGALA---LDDKLGRSTNQLSGGEWQRVRLAAVVLqitpqANPagQLL 155
Cdd:COG4136 92 svgENLAFALP---------PTIGRAQRRARVEQALEeagLAGFADRDPATLSGGQRARVALLRALL-----AEP--RAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1432492527 156 LLDEPMNSLDVA-QQSALDKILSALCQQGLAIVMSSHDLN 194
Cdd:COG4136 156 LLDEPFSKLDAAlRAQFREFVFEQIRQRGIPALLVTHDEE 195
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
22-225 |
9.33e-16 |
|
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: 73.91 E-value: 9.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLLARMAG-MTSGKGSIQFAGQPLEAWSATKLALhrAYLSQQQTPPFAMPVW----HYLTL 96
Cdd:cd03299 21 EVERGDYFVILGPTGSGKSVLLETIAGfIKPDSGKILLNGKDITNLPPEKRDI--SYVPQNYALFPHMTVYkniaYGLKK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 97 HQHDK-TRTELLNDVAGALALDDKLGRSTNQLSGGEWQRVRLA-AVVLqitpqaNPagQLLLLDEPMNSLDVAQQSALDK 174
Cdd:cd03299 99 RKVDKkEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIArALVV------NP--KILLLDEPFSALDVRTKEKLRE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1432492527 175 ILSALCQQ-GLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPPN 225
Cdd:cd03299 171 ELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPK 222
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
11-211 |
1.08e-15 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 72.25 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 11 AESTRLGPLSGEVRAGEILHLVGPNGAGKSTLLARMAG-MTSGKGSIQFAGQPLEAWSATKLALHRAYLSQqqtppfamp 89
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGlLRPTSGRVRLDGADISQWDPNELGDHVGYLPQ--------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 90 vwhyltlhqhdktRTELLndvAGALAlddklgrsTNQLSGGEWQRVRLAAVVLQitpqaNPAgqLLLLDEPMNSLDVAQQ 169
Cdd:cd03246 84 -------------DDELF---SGSIA--------ENILSGGQRQRLGLARALYG-----NPR--ILVLDEPNSHLDVEGE 132
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1432492527 170 SALDKILSALCQQGLAIVMSSHDLNhTLRHAHRAWLLKGGKM 211
Cdd:cd03246 133 RALNQAIAALKAAGATRIVIAHRPE-TLASADRILVLEDGRV 173
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
23-226 |
1.68e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 73.96 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 23 VRAGEILHLVGPNGAGKSTLLARMAG-MTSGKGSIQFAGQPLEAWSATKLALHRAYLSQQQTPP---FAM---------P 89
Cdd:PRK13639 25 AEKGEMVALLGPNGAGKSTLFLHFNGiLKPTSGEVLIKGEPIKYDKKSLLEVRKTVGIVFQNPDdqlFAPtveedvafgP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 90 VWHYLTLHQHDKTRTELLNDVaGALALDDKlgrSTNQLSGGEWQRVRLAAVvLQITPQanpagqLLLLDEPMNSLDVAQQ 169
Cdd:PRK13639 105 LNLGLSKEEVEKRVKEALKAV-GMEGFENK---PPHHLSGGQKKRVAIAGI-LAMKPE------IIVLDEPTSGLDPMGA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1432492527 170 SALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPPNL 226
Cdd:PRK13639 174 SQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIET 230
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
22-224 |
1.81e-15 |
|
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: 73.00 E-value: 1.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLLARMAGM-TSGKGSIQFAGQPLEAWSATKLALHR---AYLSQQ----------QTPPFA 87
Cdd:cd03258 27 SVPKGEIFGIIGRSGAGKSTLIRCINGLeRPTSGSVLVDGTDLTLLSGKELRKARrriGMIFQHfnllssrtvfENVALP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 88 MPVWHYLTLHQHDKTRtELLNDVagalALDDKLGRSTNQLSGGEWQRVRLA-AVVlqitpqANPAgqLLLLDEPMNSLDV 166
Cdd:cd03258 107 LEIAGVPKAEIEERVL-ELLELV----GLEDKADAYPAQLSGGQKQRVGIArALA------NNPK--VLLCDEATSALDP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1432492527 167 AQ-QSALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPP 224
Cdd:cd03258 174 ETtQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
19-221 |
2.45e-15 |
|
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: 72.65 E-value: 2.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKST---LLARMAGMTSGkgSIQFAGQPLEAWSATKLALHRAYLSQQqTPPFAMPVWHYLT 95
Cdd:cd03253 20 VSFTIPAGKKVAIVGPSGSGKSTilrLLFRFYDVSSG--SILIDGQDIREVTLDSLRRAIGVVPQD-TVLFNDTIGYNIR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 96 LHQHDKTRTELLnDVAGALALDDKLGRSTNQ-----------LSGGEWQRVRLAAVVLQitpqaNPagQLLLLDEPMNSL 164
Cdd:cd03253 97 YGRPDATDEEVI-EAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAILK-----NP--PILLLDEATSAL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1432492527 165 DVAQQSALDKILSALCqQGLAIVMSSHDLnHTLRHAHRAWLLKGGKMLASGRREEVL 221
Cdd:cd03253 169 DTHTEREIQAALRDVS-KGRTTIVIAHRL-STIVNADKIIVLKDGRIVERGTHEELL 223
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
31-232 |
2.55e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 73.50 E-value: 2.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 31 LVGPNGAGKSTLLARMAGM-TSGKGSIQFAGQPLEAWSATKLALHRAYLSQQQTPPfaMPVWHY-------LTLHQHDKT 102
Cdd:PRK13638 32 LVGANGCGKSTLFMNLSGLlRPQKGAVLWQGKPLDYSKRGLLALRQQVATVFQDPE--QQIFYTdidsdiaFSLRNLGVP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 103 RTELLNDVAGALALDDKLG---RSTNQLSGGEWQRVRLA-AVVLQitpqanpaGQLLLLDEPMNSLDVAQQSALDKILSA 178
Cdd:PRK13638 110 EAEITRRVDEALTLVDAQHfrhQPIQCLSHGQKKRVAIAgALVLQ--------ARYLLLDEPTAGLDPAGRTQMIAIIRR 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1432492527 179 LCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPPNLAQAYGM 232
Cdd:PRK13638 182 IVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEAMEQAGL 235
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
10-230 |
2.60e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 74.74 E-value: 2.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 10 VAESTRLGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGMTSGKGSIQFAGQPLEAWSATKLALHR-------------- 75
Cdd:PRK15134 296 VDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGEIWFDGQPLHNLNRRQLLPVRhriqvvfqdpnssl 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 76 -AYLSQQQTPPFAMPVWH-YLTLHQHDKTRTELLNDVAgalaLD-DKLGRSTNQLSGGEWQRVRLA-AVVLQitpqanpa 151
Cdd:PRK15134 376 nPRLNVLQIIEEGLRVHQpTLSAAQREQQVIAVMEEVG----LDpETRHRYPAEFSGGQRQRIAIArALILK-------- 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 152 GQLLLLDEPMNSLDVAQQSALDKILSALCQQ-GLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPPnlAQAY 230
Cdd:PRK15134 444 PSLIILDEPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAP--QQEY 521
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
16-193 |
2.97e-15 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 72.81 E-value: 2.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 16 LGPLSGEVRAGEILHLVGPNGAGKSTLLaRM-AG-MTSGKGSIQFAGQPLeawsaTKLALHRAYLSQQqtppFA-MPvWh 92
Cdd:COG1116 27 LDDVSLTVAAGEFVALVGPSGCGKSTLL-RLiAGlEKPTSGEVLVDGKPV-----TGPGPDRGVVFQE----PAlLP-W- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 93 yLT--------LHQHDKTRTELLNDVAGALA---LDDKLGRSTNQLSGGEWQRVRLA-AVVLQitPqanpagQLLLLDEP 160
Cdd:COG1116 95 -LTvldnvalgLELRGVPKAERRERARELLElvgLAGFEDAYPHQLSGGMRQRVAIArALAND--P------EVLLMDEP 165
|
170 180 190
....*....|....*....|....*....|....
gi 1432492527 161 MNSLDVAQQSALDKILSALCQQ-GLAIVMSSHDL 193
Cdd:COG1116 166 FGALDALTRERLQDELLRLWQEtGKTVLFVTHDV 199
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
28-224 |
4.74e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 72.39 E-value: 4.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 28 ILHLVGPNGAGKSTLLA---RMAGMTSGK----GSIQFAGQPLEAWSATKLALHRAYLSQQQTPPFAMPVWHYLT--LHQ 98
Cdd:PRK14246 38 IFGIMGPSGSGKSTLLKvlnRLIEIYDSKikvdGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFPHLSIYDNIAypLKS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 99 H--------DKTRTELLNDVAGALALDDKLGRSTNQLSGGEWQRVRLAAVvLQITPQanpagqLLLLDEPMNSLDVAQQS 170
Cdd:PRK14246 118 HgikekreiKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARA-LALKPK------VLLMDEPTSMIDIVNSQ 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1432492527 171 ALDKILSALcQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPP 224
Cdd:PRK14246 191 AIEKLITEL-KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSP 243
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
22-220 |
5.07e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 73.90 E-value: 5.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLLARMAGM-TSGKGSIQFAGQPLEaWSATKLALHR------------AYLS--------- 79
Cdd:COG1129 26 ELRPGEVHALLGENGAGKSTLMKILSGVyQPDSGEILLDGEPVR-FRSPRDAQAAgiaiihqelnlvPNLSvaeniflgr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 80 QQQTPPF----AMpvwhyltlhqHDKTRtELLNDVAGALALDDKLGRstnqLSGGEWQRVRLA-AVVLQitpqanpaGQL 154
Cdd:COG1129 105 EPRRGGLidwrAM----------RRRAR-ELLARLGLDIDPDTPVGD----LSVAQQQLVEIArALSRD--------ARV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1432492527 155 LLLDEPMNSLDVAQQSALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEV 220
Cdd:COG1129 162 LILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-211 |
8.55e-15 |
|
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: 70.15 E-value: 8.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 3 IVMQLQDVAESTRLGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGMTSG-KGSIQFAGQPLEAWSATK-LALHRAYLSQ 80
Cdd:cd03215 3 PVLEVRGLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPaSGEITLDGKPVTRRSPRDaIRAGIAYVPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 81 --QQTPPFA-MPVWHYLTLHQHdktrtellndvagalalddklgrstnqLSGGEWQRVRLAAVVLqitpqANPagQLLLL 157
Cdd:cd03215 83 drKREGLVLdLSVAENIALSSL---------------------------LSGGNQQKVVLARWLA-----RDP--RVLIL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1432492527 158 DEPMNSLDVAQQSALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKM 211
Cdd:cd03215 129 DEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
22-221 |
1.51e-14 |
|
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: 70.72 E-value: 1.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKST---LLARMAGMTSGkgSIQFAGQPLEAWSATKLALHRAYLSQQqTPPFAMPVWHYLTLHQ 98
Cdd:cd03251 24 DIPAGETVALVGPSGSGKSTlvnLIPRFYDVDSG--RILIDGHDVRDYTLASLRRQIGLVSQD-VFLFNDTVAENIAYGR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 99 HDKTRTELLNDVAGALA----------LDDKLGRSTNQLSGGEWQRVRLAAVVLqitpqANPagQLLLLDEPMNSLDVAQ 168
Cdd:cd03251 101 PGATREEVEEAARAANAhefimelpegYDTVIGERGVKLSGGQRQRIAIARALL-----KDP--PILILDEATSALDTES 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1432492527 169 QSALDKILSALCQQGLAIVMsSHDLNhTLRHAHRAWLLKGGKMLASGRREEVL 221
Cdd:cd03251 174 ERLVQAALERLMKNRTTFVI-AHRLS-TIENADRIVVLEDGKIVERGTHEELL 224
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
20-176 |
1.52e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 72.53 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 20 SGEVRAGEILHLVGPNGAGKSTlLARMagmtsgkgsiqFAG--QPLEAWSATKLALhrAYLSQQQTPPFAMPVWHYLTlH 97
Cdd:PRK13409 359 GGEIYEGEVIGIVGPNGIGKTT-FAKL-----------LAGvlKPDEGEVDPELKI--SYKPQYIKPDYDGTVEDLLR-S 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 98 QHDKTRTELLN-DVAGALALDDKLGRSTNQLSGGEWQRVRLAAVVLQitpQANpagqLLLLDEPMNSLDVAQQSALDKIL 176
Cdd:PRK13409 424 ITDDLGSSYYKsEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSR---DAD----LYLLDEPSAHLDVEQRLAVAKAI 496
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
19-215 |
1.90e-14 |
|
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: 69.26 E-value: 1.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKSTLLARMAG-MTSGKGSIQFAGQPLEAWSATkLALHRAYLSQQqtppfampvwhyltLH 97
Cdd:cd03247 21 LSLELKQGEKIALLGRSGSGKSTLLQLLTGdLKPQQGEITLDGVPVSDLEKA-LSSLISVLNQR--------------PY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 98 QHDKTrtellndvagalaLDDKLGRstnQLSGGEWQRVRLAAVVLQITPqanpagqLLLLDEPMNSLD-VAQQSALDKIL 176
Cdd:cd03247 86 LFDTT-------------LRNNLGR---RFSGGERQRLALARILLQDAP-------IVLLDEPTVGLDpITERQLLSLIF 142
|
170 180 190
....*....|....*....|....*....|....*....
gi 1432492527 177 SALcqQGLAIVMSSHDLNhTLRHAHRAWLLKGGKMLASG 215
Cdd:cd03247 143 EVL--KDKTLIWITHHLT-GIEHMDKILFLENGKIIMQG 178
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
20-191 |
3.58e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 71.62 E-value: 3.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 20 SGEVRAGEILHLVGPNGAGKSTLLA-----RMAGMTsGKGSIQFAGQPLEAWSATKLAlhrAYLSQQQTPPFAMPVWHYL 94
Cdd:TIGR00955 45 SGVAKPGELLAVMGSSGAGKTTLMNalafrSPKGVK-GSGSVLLNGMPIDAKEMRAIS---AYVQQDDLFIPTLTVREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 95 TLHQH--------DKTRTELLNDVAGALAL----DDKLGRSTNQ--LSGGEWQRVRLAAVVLqitpqANPagQLLLLDEP 160
Cdd:TIGR00955 121 MFQAHlrmprrvtKKEKRERVDEVLQALGLrkcaNTRIGVPGRVkgLSGGERKRLAFASELL-----TDP--PLLFCDEP 193
|
170 180 190
....*....|....*....|....*....|.
gi 1432492527 161 MNSLDVAQQSALDKILSALCQQGLAIVMSSH 191
Cdd:TIGR00955 194 TSGLDSFMAYSVVQVLKGLAQKGKTIICTIH 224
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
22-215 |
5.10e-14 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 68.71 E-value: 5.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLLARMAGMTS-GKGSIQFAGQPleawsatklalhraylsqqqTPPFAM-----P------ 89
Cdd:cd03220 44 EVPRGERIGLIGRNGAGKSTLLRLLAGIYPpDSGTVTVRGRV--------------------SSLLGLgggfnPeltgre 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 90 -VWHYLTLHQHDKTR-TELLNDVAGALALDDKLGRSTNQLSGGewQRVRLA-AVVLQITPqanpagQLLLLDEPMNSLDV 166
Cdd:cd03220 104 nIYLNGRLLGLSRKEiDEKIDEIIEFSELGDFIDLPVKTYSSG--MKARLAfAIATALEP------DILLIDEVLAVGDA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1432492527 167 A-QQSALDKILSaLCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASG 215
Cdd:cd03220 176 AfQEKCQRRLRE-LLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
22-243 |
6.17e-14 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 70.10 E-value: 6.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLLaRM-AG---MTSGKgsIQFAGQPLeawsaTKLALHR---AYLSQQqtppFA----MPV 90
Cdd:COG3839 25 DIEDGEFLVLLGPSGCGKSTLL-RMiAGledPTSGE--ILIGGRDV-----TDLPPKDrniAMVFQS----YAlyphMTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 91 W----HYLTLHQHDK-TRTELLNDVAGALALDDKLGRSTNQLSGGEWQRVRLA-AVVlqitpqANPagQLLLLDEPMNSL 164
Cdd:COG3839 93 YeniaFPLKLRKVPKaEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGrALV------REP--KVFLLDEPLSNL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 165 DVAQQSALDKILSALCQQ-GLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVL-TPPNLAQAY-----GMNFRRL 237
Cdd:COG3839 165 DAKLRVEMRAEIKRLHRRlGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYdRPANLFVAGfigspPMNLLPG 244
|
....*.
gi 1432492527 238 DIEGHR 243
Cdd:COG3839 245 TVEGGG 250
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
23-193 |
8.76e-14 |
|
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: 68.93 E-value: 8.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 23 VRAGEILHLVGPNGAGKSTLLARMAG-MTSGKGsiQFAGQP-----LEAWSATKLALHRAYLSQQQTPPFAMPVWHYLTL 96
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGkLKPNLG--KFDDPPdwdeiLDEFRGSELQNYFTKLLEGDVKVIVKPQYVDLIP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 97 HQHDKTRTELLN---------DVAGALALDDKLGRSTNQLSGGEWQRVRLAAVVLQitpqanpAGQLLLLDEPMNSLDVA 167
Cdd:cd03236 101 KAVKGKVGELLKkkdergkldELVDQLELRHVLDRNIDQLSGGELQRVAIAAALAR-------DADFYFFDEPSSYLDIK 173
|
170 180
....*....|....*....|....*.
gi 1432492527 168 QQSALDKILSALCQQGLAIVMSSHDL 193
Cdd:cd03236 174 QRLNAARLIRELAEDDNYVLVVEHDL 199
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
20-176 |
1.02e-13 |
|
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: 70.20 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 20 SGEVRAGEILHLVGPNGAGKSTlLARM-AG-MTSGKGSIQfagqpleawsaTKLALhrAYLSQQQTPPFAMPVWHYLTLH 97
Cdd:COG1245 360 GGEIREGEVLGIVGPNGIGKTT-FAKIlAGvLKPDEGEVD-----------EDLKI--SYKPQYISPDYDGTVEEFLRSA 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 98 QHDKTRTELLN-DVAGALALDDKLGRSTNQLSGGEWQRVRLAAVVLQitpQANpagqLLLLDEPMNSLDVAQQSALDKIL 176
Cdd:COG1245 426 NTDDFGSSYYKtEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSR---DAD----LYLLDEPSAHLDVEQRLAVAKAI 498
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-194 |
1.72e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 68.58 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKSTLLARMAGM---TSgkGSIQFAGqpLEAWsatklALHRAYLSQ------QQTPPFA-M 88
Cdd:COG4586 41 ISFTIEPGEIVGFIGPNGAGKSTTIKMLTGIlvpTS--GEVRVLG--YVPF-----KRRKEFARRigvvfgQRSQLWWdL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 89 PVWHYLTLHQH-----DKTRTELLNDVAGALALDDKLGRSTNQLSGGewQRVR--LAAVVLQitpqaNPagQLLLLDEPM 161
Cdd:COG4586 112 PAIDSFRLLKAiyripDAEYKKRLDELVELLDLGELLDTPVRQLSLG--QRMRceLAAALLH-----RP--KILFLDEPT 182
|
170 180 190
....*....|....*....|....*....|....
gi 1432492527 162 NSLDVAQQSALDKILSALCQQ-GLAIVMSSHDLN 194
Cdd:COG4586 183 IGLDVVSKEAIREFLKEYNRErGTTILLTSHDMD 216
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
22-229 |
1.87e-13 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 68.63 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLLARMAGM-TSGKGSIQFAGQPLEAWSATKlalHR--AYLSQqqtppfampvwHY----- 93
Cdd:COG1118 24 EIASGELVALLGPSGSGKTTLLRIIAGLeTPDSGRIVLNGRDLFTNLPPR---ERrvGFVFQ-----------HYalfph 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 94 ----------LTLHQHDKTR-----TELLNDV-AGALAlddklGRSTNQLSGGEWQRVRLA---AVvlqitpqaNPagQL 154
Cdd:COG1118 90 mtvaeniafgLRVRPPSKAEirarvEELLELVqLEGLA-----DRYPSQLSGGQRQRVALAralAV--------EP--EV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1432492527 155 LLLDEPMNSLDVAQQSALDKILSALCQQ-GLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLT-PPNLAQA 229
Cdd:COG1118 155 LLLDEPFGALDAKVRKELRRWLRRLHDElGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDrPATPFVA 231
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
19-231 |
2.05e-13 |
|
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: 67.36 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKSTLLARMAGMTSG-KGSIQFAGQPLEAWSATK---------LALHRaYLSQQQTPPFAM 88
Cdd:cd03296 21 VSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPdSGTILFGGEDATDVPVQErnvgfvfqhYALFR-HMTVFDNVAFGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 89 PVWHYLTLHQHDKTR---TELLNDVAgalaLDDKLGRSTNQLSGGEWQRVRLAAvVLQITPqanpagQLLLLDEPMNSLD 165
Cdd:cd03296 100 RVKPRSERPPEAEIRakvHELLKLVQ----LDWLADRYPAQLSGGQRQRVALAR-ALAVEP------KVLLLDEPFGALD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1432492527 166 VAQQSALDKILSALCQQ-GLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPPNLAQAYG 231
Cdd:cd03296 169 AKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYS 235
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-211 |
3.67e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 66.66 E-value: 3.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 2 SIVMQLQDV----AESTRLGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGMTS-GKGSIQFAGQPLEAWSATKLALHRA 76
Cdd:PRK10247 5 SPLLQLQNVgylaGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISpTSGTLLFEGEDISTLKPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 77 YLSqqQTPP-FAMPVWHYLTL-----HQHDKtRTELLNDVAGALALDDKLGRSTNQLSGGEWQRVRLAAvVLQITPqanp 150
Cdd:PRK10247 85 YCA--QTPTlFGDTVYDNLIFpwqirNQQPD-PAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIR-NLQFMP---- 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1432492527 151 agQLLLLDEPMNSLDVAQQSALDKILSALC-QQGLAIVMSSHDLNHtLRHAHRAWLLK--GGKM 211
Cdd:PRK10247 157 --KVLLLDEITSALDESNKHNVNEIIHRYVrEQNIAVLWVTHDKDE-INHADKVITLQphAGEM 217
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
22-221 |
3.69e-13 |
|
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: 66.01 E-value: 3.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLLARMAGMTS---GKGSIQFAGQPLEAWSATKLALHRAYLSQQQtpPFAMPvwhyltlhq 98
Cdd:cd03217 22 TIKKGEVHALMGPNGSGKSTLAKTIMGHPKyevTEGEILFKGEDITDLPPEERARLGIFLAFQY--PPEIP--------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 99 hdktrtellndvagALALDDKLgRSTNQ-LSGGEWQRVRLAAVVLQitpqaNPagQLLLLDEPMNSLDVAQQSALDKILS 177
Cdd:cd03217 91 --------------GVKNADFL-RYVNEgFSGGEKKRNEILQLLLL-----EP--DLAILDEPDSGLDIDALRLVAEVIN 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1432492527 178 ALCQQGLAIVMSSHD---LNHTlrHAHRAWLLKGGKMLASGRREEVL 221
Cdd:cd03217 149 KLREEGKSVLIITHYqrlLDYI--KPDRVHVLYDGRIVKSGDKELAL 193
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
16-210 |
3.80e-13 |
|
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: 64.78 E-value: 3.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 16 LGPLSGEVRAGEILHLVGPNGAGKSTLLARMAG-MTSGKGSIQFAgqpleawSATKLAlhraYLSQqqtppfampvwhyl 94
Cdd:cd03221 16 LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGeLEPDEGIVTWG-------STVKIG----YFEQ-------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 95 tlhqhdktrtellndvagalalddklgrstnqLSGGEWQRVRLAAVVLQitpQANpagqLLLLDEPMNSLDVAQQSALDK 174
Cdd:cd03221 71 --------------------------------LSGGEKMRLALAKLLLE---NPN----LLLLDEPTNHLDLESIEALEE 111
|
170 180 190
....*....|....*....|....*....|....*....
gi 1432492527 175 ILSALcqQGlAIVMSSHD---LNHTlrhAHRAWLLKGGK 210
Cdd:cd03221 112 ALKEY--PG-TVILVSHDryfLDQV---ATKIIELEDGK 144
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-193 |
4.03e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 67.06 E-value: 4.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 1 MSIVMQLQDVA----ESTRLGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGMTS-GKGSIQFAGQPLEAWSATKLALhr 75
Cdd:PRK09544 1 MTSLVSLENVSvsfgQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVApDEGVIKRNGKLRIGYVPQKLYL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 76 aylsqqqTPPFAMPVWHYLTLHQHDKTRTEL--LNDVAGALALDDKLgrstNQLSGGEWQRVRLAAVVLQitpqanpAGQ 153
Cdd:PRK09544 79 -------DTTLPLTVNRFLRLRPGTKKEDILpaLKRVQAGHLIDAPM----QKLSGGETQRVLLARALLN-------RPQ 140
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1432492527 154 LLLLDEPMNSLDVAQQSALDKILSALCQQ-GLAIVMSSHDL 193
Cdd:PRK09544 141 LLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDL 181
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
4-226 |
5.61e-13 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 67.83 E-value: 5.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 4 VMQLQDVAES--TR-----LGPLSGEVRAGEILHLVGPNGAGKST---LLARMAGMTSgkGSIQFAGQPLEAWSATklAL 73
Cdd:TIGR00958 478 LIEFQDVSFSypNRpdvpvLKGLTFTLHPGEVVALVGPSGSGKSTvaaLLQNLYQPTG--GQVLLDGVPLVQYDHH--YL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 74 HRAYLSQQQTPP-FAMPVWHYLTLHQHDKTRTELLNDVAGALA----------LDDKLGRSTNQLSGGEWQRVRLAAVVL 142
Cdd:TIGR00958 554 HRQVALVGQEPVlFSGSVRENIAYGLTDTPDEEIMAAAKAANAhdfimefpngYDTEVGEKGSQLSGGQKQRIAIARALV 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 143 QitpqaNPAgqLLLLDEPMNSLDVAQQSALDKilsALCQQGLAIVMSSHDLnHTLRHAHRAWLLKGGKMLASGRREEVLT 222
Cdd:TIGR00958 634 R-----KPR--VLILDEATSALDAECEQLLQE---SRSRASRTVLLIAHRL-STVERADQILVLKKGSVVEMGTHKQLME 702
|
....
gi 1432492527 223 PPNL 226
Cdd:TIGR00958 703 DQGC 706
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-228 |
5.66e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 66.66 E-value: 5.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 11 AESTRLGPLSGEVRAGEILHLVGPNGAGKSTLLA---RMAGMTSG---KGSIQFAGQPLEAWSATKLALHRAYLSQQQTP 84
Cdd:PRK14271 32 AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRtlnRMNDKVSGyrySGDVLLGGRSIFNYRDVLEFRRRVGMLFQRPN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 85 PFAMPVW---------HYLTLHQHDKTRTEL-LNDVAGALALDDKLGRSTNQLSGGEWQRVRLAAvvlqiTPQANPagQL 154
Cdd:PRK14271 112 PFPMSIMdnvlagvraHKLVPRKEFRGVAQArLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLAR-----TLAVNP--EV 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1432492527 155 LLLDEPMNSLDVAQQSALDKILSALCQQgLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPPNLAQ 228
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAE 257
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-241 |
5.67e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 67.16 E-value: 5.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 2 SIVMQLQDVAESTRLGP----LSGEVRAGEILHLVGPNGAGKSTLLARMAGMTS-GKGSIQFAGQPLEAwsATKLALHR- 75
Cdd:PRK13536 39 TVAIDLAGVSKSYGDKAvvngLSFTVASGECFGLLGPNGAGKSTIARMILGMTSpDAGKITVLGVPVPA--RARLARARi 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 76 AYLSQQQTPPFAMPVWHYLTLH-QHDKTRTELLNDVAGAL----ALDDKLGRSTNQLSGGEWQRVRLAAVVLQitpqaNP 150
Cdd:PRK13536 117 GVVPQFDNLDLEFTVRENLLVFgRYFGMSTREIEAVIPSLlefaRLESKADARVSDLSGGMKRRLTLARALIN-----DP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 151 agQLLLLDEPMNSLDVAQQSALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVL--------- 221
Cdd:PRK13536 192 --QLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIdehigcqvi 269
|
250 260
....*....|....*....|....*
gi 1432492527 222 -----TPPNLAQAYGMNFRRLDIEG 241
Cdd:PRK13536 270 eiyggDPHELSSLVKPYARRIEVSG 294
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
22-221 |
5.86e-13 |
|
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: 67.91 E-value: 5.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLLARMAGM---TSGKGSIQFAGQ--------PLEAWSATKLA--LHRAYlsqqqtppfam 88
Cdd:TIGR03269 306 EVKEGEIFGIVGTSGAGKTTLSKIIAGVlepTSGEVNVRVGDEwvdmtkpgPDGRGRAKRYIgiLHQEY----------- 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 89 pvwhylTLHQHdKTRTELLNDVAGaLALDDKLGRS-----------------------TNQLSGGEWQRVRLAAVVLQit 145
Cdd:TIGR03269 375 ------DLYPH-RTVLDNLTEAIG-LELPDELARMkavitlkmvgfdeekaeeildkyPDELSEGERHRVALAQVLIK-- 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1432492527 146 pqaNPagQLLLLDEPMNSLD-VAQQSALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVL 221
Cdd:TIGR03269 445 ---EP--RIVILDEPTGTMDpITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-210 |
6.30e-13 |
|
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: 65.74 E-value: 6.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 5 MQLQDVAES----TRLGPLSGEVRAGEILHLVGPNGAGKSTLLARMAG---MTSGKgsIQFAGQPLEAWSATKLALHRAY 77
Cdd:cd03301 1 VELENVTKRfgnvTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGleePTSGR--IYIGGRDVTDLPPKDRDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 78 LSQQQTPpfAMPVW----HYLTLHQHDK-TRTELLNDVAGALALDDKLGRSTNQLSGGEWQRVRLA-AVVlqitpqANPa 151
Cdd:cd03301 79 QNYALYP--HMTVYdniaFGLKLRKVPKdEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGrAIV------REP- 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1432492527 152 gQLLLLDEPMNSLD----VAQQSALDKILSALcqqGLAIVMSSHDLNHTLRHAHRAWLLKGGK 210
Cdd:cd03301 150 -KVFLMDEPLSNLDaklrVQMRAELKRLQQRL---GTTTIYVTHDQVEAMTMADRIAVMNDGQ 208
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
19-194 |
7.20e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 65.99 E-value: 7.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKSTLLARMAGM-TSGKGSIQFAGQPLEAWSATKLALHR------AYLSQQQTPPF----- 86
Cdd:PRK11629 28 VSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLdTPTSGDVIFNGQPMSKLSSAAKAELRnqklgfIYQFHHLLPDFtalen 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 87 -AMPVwhyLTLHQHDKTRTELLNDVAGALALDDKLGRSTNQLSGGEWQRVRLAAVVLQitpqaNPAgqLLLLDEPMNSLD 165
Cdd:PRK11629 108 vAMPL---LIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVN-----NPR--LVLADEPTGNLD 177
|
170 180 190
....*....|....*....|....*....|
gi 1432492527 166 VAQQSALDKILSAL-CQQGLAIVMSSHDLN 194
Cdd:PRK11629 178 ARNADSIFQLLGELnRLQGTAFLVVTHDLQ 207
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
22-219 |
8.62e-13 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 65.53 E-value: 8.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLLARMAGM---TSgkGSIQFAGQPLEAWSATKLALHRAYL------SQQQTPPF------ 86
Cdd:COG4181 34 EVEAGESVAIVGASGSGKSTLLGLLAGLdrpTS--GTVRLAGQDLFALDEDARARLRARHvgfvfqSFQLLPTLtalenv 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 87 AMPvwhyLTLHQHDKTR---TELLNDVagalALDDKLGRSTNQLSGGEWQRVRLA-AVVLQitpqanPAgqLLLLDEPMN 162
Cdd:COG4181 112 MLP----LELAGRRDARaraRALLERV----GLGHRLDHYPAQLSGGEQQRVALArAFATE------PA--ILFADEPTG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1432492527 163 SLDVAQQSALDKILSALCQ-QGLAIVMSSHDLNHTLRhAHRAWLLKGGKMLASGRREE 219
Cdd:COG4181 176 NLDAATGEQIIDLLFELNReRGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTAATA 232
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
19-191 |
9.53e-13 |
|
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: 64.88 E-value: 9.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKSTLLARMAGMTSG---KGSIQFAGQPLeawSATKLALHRAYLSQQQtppFAMPvwhYLT 95
Cdd:cd03213 28 VSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgvSGEVLINGRPL---DKRSFRKIIGYVPQDD---ILHP---TLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 96 LHQhdktrtellndvagALALDDKLgRStnqLSGGEWQRVRLAAVVLqitpqANPagQLLLLDEPMNSLDVAQQSALDKI 175
Cdd:cd03213 99 VRE--------------TLMFAAKL-RG---LSGGERKRVSIALELV-----SNP--SLLFLDEPTSGLDSSSALQVMSL 153
|
170
....*....|....*.
gi 1432492527 176 LSALCQQGLAIVMSSH 191
Cdd:cd03213 154 LRRLADTGRTIICSIH 169
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
22-210 |
1.07e-12 |
|
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: 64.86 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLLARMAGMTS-GKGSIQFAGQPLEAwSATKLALHRAYLSQ--QQTPPFA-MPVWHYLTL- 96
Cdd:cd03262 22 TVKKGEVVVIIGPSGSGKSTLLRCINLLEEpDSGTIIIDGLKLTD-DKKNINELRQKVGMvfQQFNLFPhLTVLENITLa 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 97 ---------HQHDKTRTELLNDVagalALDDKLGRSTNQLSGGEWQRVRLA-AVVLqitpqaNPagQLLLLDEPmnsldv 166
Cdd:cd03262 101 pikvkgmskAEAEERALELLEKV----GLADKADAYPAQLSGGQQQRVAIArALAM------NP--KVMLFDEP------ 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1432492527 167 aqQSALD--------KILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGK 210
Cdd:cd03262 163 --TSALDpelvgevlDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
4-211 |
1.30e-12 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 65.18 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 4 VMQLQDVAESTRLGP-------LSGEVRAGEILHLVGPNGAGKST---LLARMAGMTsgKGSIQFAGQPLEAWSATKLAL 73
Cdd:cd03248 11 IVKFQNVTFAYPTRPdtlvlqdVSFTLHPGEVTALVGPSGSGKSTvvaLLENFYQPQ--GGQVLLDGKPISQYEHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 74 HRAYLSQQ----------------QTPPFAMPVWHYLTLHQHDKTrTELlndvagALALDDKLGRSTNQLSGGEWQRVRL 137
Cdd:cd03248 89 KVSLVGQEpvlfarslqdniayglQSCSFECVKEAAQKAHAHSFI-SEL------ASGYDTEVGEKGSQLSGGQKQRVAI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1432492527 138 AAVVLQitpqaNPagQLLLLDEPMNSLDVAQQSALDKILSAlCQQGLAIVMSSHDLNhTLRHAHRAWLLKGGKM 211
Cdd:cd03248 162 ARALIR-----NP--QVLILDEATSALDAESEQQVQQALYD-WPERRTVLVIAHRLS-TVERADQILVLDGGRI 226
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
22-209 |
1.61e-12 |
|
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: 64.79 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLLARMAGMTS-GKGSIQFAGQPLEAWSATKLALHRAY-----LSQQQTPPFAMPVwhylT 95
Cdd:TIGR01184 7 TIQQGEFISLIGHSGCGKSTLLNLISGLAQpTSGGVILEGKQITEPGPDRMVVFQNYsllpwLTVRENIALAVDR----V 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 96 LHQHDKT-RTELLNDVAGALALDDKLGRSTNQLSGGEWQRVRLAAvVLQITPqanpagQLLLLDEPMNSLDVAQQSALDK 174
Cdd:TIGR01184 83 LPDLSKSeRRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIAR-ALSIRP------KVLLLDEPFGALDALTRGNLQE 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 1432492527 175 ILSALCQQ-GLAIVMSSHDLNHTLRHAHRAWLLKGG 209
Cdd:TIGR01184 156 ELMQIWEEhRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
19-191 |
1.79e-12 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 64.44 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKSTLLARMAG-MTSGKGSIQFAGQPLeAWSATKLALHRAYLSQQQTPPFAMPVWHYLTLH 97
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGlSPPLAGRVLLNGGPL-DFQRDSIARGLLYLGHAPGIKTTLSVLENLRFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 98 QHDKTRTELLN--DVAGALALDDklgRSTNQLSGGEWQRVRLAAVVLQITPqanpagqLLLLDEPMNSLDVAQQSALDKI 175
Cdd:cd03231 98 HADHSDEQVEEalARVGLNGFED---RPVAQLSAGQQRRVALARLLLSGRP-------LWILDEPTTALDKAGVARFAEA 167
|
170
....*....|....*.
gi 1432492527 176 LSALCQQGLAIVMSSH 191
Cdd:cd03231 168 MAGHCARGGMVVLTTH 183
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
22-194 |
1.89e-12 |
|
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: 66.39 E-value: 1.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLLARMAGM---TSGKGSIQFAGQPLEAWSAT------------KLAL-------HRAYLS 79
Cdd:TIGR02633 23 EVRPGECVGLCGENGAGKSTLMKILSGVyphGTWDGEIYWSGSPLKASNIRdteragiviihqELTLvpelsvaENIFLG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 80 QQQTPPFAMPVWHYLTLHQHdktrtELLNDVAGAlalDDKLGRSTNQLSGGEWQRVRLAAVVlqitpqaNPAGQLLLLDE 159
Cdd:TIGR02633 103 NEITLPGGRMAYNAMYLRAK-----NLLRELQLD---ADNVTRPVGDYGGGQQQLVEIAKAL-------NKQARLLILDE 167
|
170 180 190
....*....|....*....|....*....|....*
gi 1432492527 160 PMNSLDVAQQSALDKILSALCQQGLAIVMSSHDLN 194
Cdd:TIGR02633 168 PSSSLTEKETEILLDIIRDLKAHGVACVYISHKLN 202
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
19-219 |
2.47e-12 |
|
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: 64.31 E-value: 2.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKST---LLARMAGMTSGKGSIqfAGQPLEAwSATKLALHRAYLSQQQTPPFAMPVWHYLT 95
Cdd:cd03265 19 VSFRVRRGEIFGLLGPNGAGKTTtikMLTTLLKPTSGRATV--AGHDVVR-EPREVRRRIGIVFQDLSVDDELTGWENLY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 96 LHQH-----DKTRTELLNDVAGALALDDKLGRSTNQLSGGEWQRVRLAAVVLQiTPqanpagQLLLLDEPMNSLDVAQQS 170
Cdd:cd03265 96 IHARlygvpGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVH-RP------EVLFLDEPTIGLDPQTRA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1432492527 171 ALDKILSALCQ-QGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREE 219
Cdd:cd03265 169 HVWEYIEKLKEeFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
22-221 |
2.93e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 64.33 E-value: 2.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLLARMAGM---TSG----KGSIQFagqPLEawsaTKLALH-------------RAY-LSQ 80
Cdd:COG1134 48 EVERGESVGIIGRNGAGKSTLLKLIAGIlepTSGrvevNGRVSA---LLE----LGAGFHpeltgreniylngRLLgLSR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 81 QQTPP-------FA-------MPVWHYltlhqhdktrtellndvagalalddklgrStnqlSGgewQRVRLA-AVVLQIT 145
Cdd:COG1134 121 KEIDEkfdeiveFAelgdfidQPVKTY-----------------------------S----SG---MRARLAfAVATAVD 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1432492527 146 PqanpagQLLLLDEPMNSLDVA-QQSALDKIlSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVL 221
Cdd:COG1134 165 P------DILLVDEVLAVGDAAfQKKCLARI-RELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVI 234
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
22-224 |
3.54e-12 |
|
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: 64.69 E-value: 3.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTL------LARMAGMTSGkgSIQFAGQPLEAWSATKLALHR----AYLSQQqtpPFA---- 87
Cdd:COG0444 27 DVRRGETLGLVGESGSGKSTLarailgLLPPPGITSG--EILFDGEDLLKLSEKELRKIRgreiQMIFQD---PMTslnp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 88 -MPVWHYL--TLHQHDK-TRTELLNDVAGALAL------DDKLGRSTNQLSGGEWQRVRLA-AVVLqitpqaNPagQLLL 156
Cdd:COG0444 102 vMTVGDQIaePLRIHGGlSKAEARERAIELLERvglpdpERRLDRYPHELSGGMRQRVMIArALAL------EP--KLLI 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1432492527 157 LDEPMNSLDV-AQQSALDkILSALCQQ-GLAIVMSSHDLNhTLRH-AHRAWLLKGGKMLASGRREEVLTPP 224
Cdd:COG0444 174 ADEPTTALDVtIQAQILN-LLKDLQRElGLAILFITHDLG-VVAEiADRVAVMYAGRIVEEGPVEELFENP 242
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
22-202 |
5.73e-12 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 64.37 E-value: 5.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTL---LARMAGMTSGkgSIQFAGQPLEAWSATKLALHRAYLsQ---QQtpPFA-----MPV 90
Cdd:COG4608 40 DIRRGETLGLVGESGCGKSTLgrlLLRLEEPTSG--EILFDGQDITGLSGRELRPLRRRM-QmvfQD--PYAslnprMTV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 91 WHY----LTLHqHDKTRTELLNDVAGALAL----DDKLGRSTNQLSGGEWQRVRLA-AVVLqitpqaNPagQLLLLDEPM 161
Cdd:COG4608 115 GDIiaepLRIH-GLASKAERRERVAELLELvglrPEHADRYPHEFSGGQRQRIGIArALAL------NP--KLIVCDEPV 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1432492527 162 NSLDVAQQSaldKILSALC--QQ--GLAIVMSSHDLNhTLRH-AHR 202
Cdd:COG4608 186 SALDVSIQA---QVLNLLEdlQDelGLTYLFISHDLS-VVRHiSDR 227
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-226 |
8.42e-12 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 64.20 E-value: 8.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 4 VMQLQDVAES----TRLGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGM-TSGKGSIQFAGQPLEAWSATK-------- 70
Cdd:PRK09452 14 LVELRGISKSfdgkEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFeTPDSGRIMLDGQDITHVPAENrhvntvfq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 71 -LAL--HR------AY-LSQQQTPpfampvwhyltlHQHDKTRtellndVAGALA---LDDKLGRSTNQLSGGEWQRVRL 137
Cdd:PRK09452 94 sYALfpHMtvfenvAFgLRMQKTP------------AAEITPR------VMEALRmvqLEEFAQRKPHQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 138 A-AVVlqitpqANPagQLLLLDEPMNSLDVAQQSALDKILSALCQQ-GLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASG 215
Cdd:PRK09452 156 ArAVV------NKP--KVLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDG 227
|
250
....*....|..
gi 1432492527 216 RREEVL-TPPNL 226
Cdd:PRK09452 228 TPREIYeEPKNL 239
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
22-221 |
1.07e-11 |
|
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: 62.63 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKST---LLARMAGMTsgKGSIQFAGQPLEAWSATKLALHRAYLsQQQTPPFAMPVWHYLTLhQ 98
Cdd:cd03254 25 SIKPGETVAIVGPTGAGKTTlinLLMRFYDPQ--KGQILIDGIDIRDISRKSLRSMIGVV-LQDTFLFSGTIMENIRL-G 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 99 HDKTRTELLNDVAGALALDD-----------KLGRSTNQLSGGEWQRVRLAAVVLqitpqANPAgqLLLLDEPMNSLDV- 166
Cdd:cd03254 101 RPNATDEEVIEAAKEAGAHDfimklpngydtVLGENGGNLSQGERQLLAIARAML-----RDPK--ILILDEATSNIDTe 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1432492527 167 ---AQQSALDKILsalcqQGLAIVMSSHDLNhTLRHAHRAWLLKGGKMLASGRREEVL 221
Cdd:cd03254 174 tekLIQEALEKLM-----KGRTSIIIAHRLS-TIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-193 |
1.30e-11 |
|
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: 62.07 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 1 MSIVMQLQDVAES--------TRLGPLSG---EVRAGEILHLVGPNGAGKSTLLaRMA----GMTSGKGSIQFAGQPLEA 65
Cdd:COG4778 1 MTTLLEVENLSKTftlhlqggKRLPVLDGvsfSVAAGECVALTGPSGAGKSTLL-KCIygnyLPDSGSILVRHDGGWVDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 66 WSATK---LALHR---AYLSQqqtppF--AMPvwhyltlhqhdktRTELLNDVAGALaLDDKLGRST---------NQL- 127
Cdd:COG4778 80 AQASPreiLALRRrtiGYVSQ-----FlrVIP-------------RVSALDVVAEPL-LERGVDREEarararellARLn 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 128 -------------SGGEWQRVRLAAVVlqITPQAnpagqLLLLDEPMNSLDVA-QQSALDKILSALcQQGLAIVMSSHDL 193
Cdd:COG4778 141 lperlwdlppatfSGGEQQRVNIARGF--IADPP-----LLLLDEPTASLDAAnRAVVVELIEEAK-ARGTAIIGIFHDE 212
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
23-246 |
1.83e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 62.56 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 23 VRAGEILHLVGPNGAGKSTLLARMAG-MTSGKGSIQFAGQPLEAWSATKLALHRAYLSQQQTPP---FAMPVWHYLTL-- 96
Cdd:PRK13636 29 IKKGEVTAILGGNGAGKSTLFQNLNGiLKPSSGRILFDGKPIDYSRKGLMKLRESVGMVFQDPDnqlFSASVYQDVSFga 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 97 ------HQHDKTRTELLNDVAGALALDDKlgrSTNQLSGGEWQRVRLAAVvLQITPQanpagqLLLLDEPMNSLDVAQQS 170
Cdd:PRK13636 109 vnlklpEDEVRKRVDNALKRTGIEHLKDK---PTHCLSFGQKKRVAIAGV-LVMEPK------VLVLDEPTAGLDPMGVS 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1432492527 171 ALDKILSALCQQ-GLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPPNLAQAYGMNFRRLdieGHRMLI 246
Cdd:PRK13636 179 EIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEMLRKVNLRLPRI---GHLMEI 252
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
19-222 |
1.93e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 63.31 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKSTLLARMA-GMTSGKGSIQFAGQPLEAWSATKLalhRAYLS--QQQTPPFAMPVWHYLT 95
Cdd:PRK11160 359 LSLQIKAGEKVALLGRTGCGKSTLLQLLTrAWDPQQGEILLNGQPIADYSEAAL---RQAISvvSQRVHLFSATLRDNLL 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 96 LHQHDKTRTEL---LNDVA-GALALDDK-----LGRSTNQLSGGEWQRVRLAAVVLQITPqanpagqLLLLDEPMNSLDV 166
Cdd:PRK11160 436 LAAPNASDEALievLQQVGlEKLLEDDKglnawLGEGGRQLSGGEQRRLGIARALLHDAP-------LLLLDEPTEGLDA 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1432492527 167 AQQSaldKILSALCQ--QGLAIVMSSHDLnHTLRHAHRAWLLKGGKMLASGRREEVLT 222
Cdd:PRK11160 509 ETER---QILELLAEhaQNKTVLMITHRL-TGLEQFDRICVMDNGQIIEQGTHQELLA 562
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
22-230 |
2.01e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 61.93 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLLARMAGM---TSgkGSIQFAGQPLEAWSATKLALHRAYLSQQQTPPF-AMPVWHYLTLH 97
Cdd:PRK11300 27 EVREQEIVSLIGPNGAGKTTVFNCLTGFykpTG--GTILLRGQHIEGLPGHQIARMGVVRTFQHVRLFrEMTVIENLLVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 98 QHDKTRTELLndvAGAL-----------ALD------DKLG------RSTNQLSGGEWQRVRLAAVVlqITpqaNPagQL 154
Cdd:PRK11300 105 QHQQLKTGLF---SGLLktpafrraeseALDraatwlERVGllehanRQAGNLAYGQQRRLEIARCM--VT---QP--EI 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1432492527 155 LLLDEPMNSLDVAQQSALDKILSALCQQ-GLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPPNLAQAY 230
Cdd:PRK11300 175 LMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNPDVIKAY 251
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-192 |
2.17e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 63.20 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 1 MSIVMQLQDVAESTRLGPLSGEV--------RAGEILHLVGPNGAGKSTLLARMAGM-TSGKGSIQFAGQPLEAWSATKL 71
Cdd:PRK10535 1 MTALLELKDIRRSYPSGEEQVEVlkgisldiYAGEMVAIVGASGSGKSTLMNILGCLdKPTSGTYRVAGQDVATLDADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 72 A-LHRAYLSqqqtppFAMPVWH---YLTLHQH-----------DKTRTELLNDVAGALALDDKLGRSTNQLSGGEWQRVR 136
Cdd:PRK10535 81 AqLRREHFG------FIFQRYHllsHLTAAQNvevpavyagleRKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVS 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1432492527 137 LAAVVLQitpqanpAGQLLLLDEPMNSLDVAQQSALDKILSALCQQGLAIVMSSHD 192
Cdd:PRK10535 155 IARALMN-------GGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD 203
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
16-221 |
2.20e-11 |
|
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: 61.79 E-value: 2.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 16 LGPLSGEVRAGEILHLVGPNGAGKST---LLARMAGMTSGkgSIQFAGQPLEAWSATKLALHRAYLSQQqtpP--FAMPV 90
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTvvsLLERFYDPTSG--EILLDGVDIRDLNLRWLRSQIGLVSQE---PvlFDGTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 91 WHYLTLHQHDKTRTELLNDVAGALA----------LDDKLGRSTNQLSGGEWQRVRLAAVVLQitpqaNPAgqLLLLDEP 160
Cdd:cd03249 94 AENIRYGKPDATDEEVEEAAKKANIhdfimslpdgYDTLVGERGSQLSGGQKQRIAIARALLR-----NPK--ILLLDEA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1432492527 161 MNSLDVAQ----QSALDKILsalcqQGLAIVMSSHDLnHTLRHAHRAWLLKGGKMLASGRREEVL 221
Cdd:cd03249 167 TSALDAESeklvQEALDRAM-----KGRTTIVIAHRL-STIRNADLIAVLQNGQVVEQGTHDELM 225
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
16-193 |
2.34e-11 |
|
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: 63.15 E-value: 2.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 16 LGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGMTSG-KGSIQFAGQPLEAWSATKLAlHRAYLSQQQTPPFAMPVWHYL 94
Cdd:TIGR02868 351 LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPlQGEVTLDGVPVSSLDQDEVR-RRVSVCAQDAHLFDTTVRENL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 95 TLHQHDKTRTEL--------LNDVAGAL--ALDDKLGRSTNQLSGGEWQRVRLAAVVLQITPqanpagqLLLLDEPMNSL 164
Cdd:TIGR02868 430 RLARPDATDEELwaalervgLADWLRALpdGLDTVLGEGGARLSGGERQRLALARALLADAP-------ILLLDEPTEHL 502
|
170 180 190
....*....|....*....|....*....|
gi 1432492527 165 DVAQQSA-LDKILSALcqQGLAIVMSSHDL 193
Cdd:TIGR02868 503 DAETADElLEDLLAAL--SGRTVVLITHHL 530
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
23-194 |
2.59e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.02 E-value: 2.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 23 VRAGEILHLVGPNGAGKSTLLARMAGM---TSGKGSIQFAGQPLEAWSA------------TKLAL-------HRAYLSQ 80
Cdd:PRK13549 28 VRAGEIVSLCGENGAGKSTLMKVLSGVyphGTYEGEIIFEGEELQASNIrdteragiaiihQELALvkelsvlENIFLGN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 81 QQTPPFAMpvwHYLTLHQHDKtrtELLNDVAGALALDDKLGrstnQLSGGEWQRVRLAAVVlqitpqaNPAGQLLLLDEP 160
Cdd:PRK13549 108 EITPGGIM---DYDAMYLRAQ---KLLAQLKLDINPATPVG----NLGLGQQQLVEIAKAL-------NKQARLLILDEP 170
|
170 180 190
....*....|....*....|....*....|....
gi 1432492527 161 MNSLDVAQQSALDKILSALCQQGLAIVMSSHDLN 194
Cdd:PRK13549 171 TASLTESETAVLLDIIRDLKAHGIACIYISHKLN 204
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-224 |
3.09e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 62.80 E-value: 3.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKS-TLLARMAGMTSG-----KGSIQFAGQPLEAWSATKLalhRAYLSQQQTPPFAMP--- 89
Cdd:PRK15134 28 VSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvypSGDIRFHGESLLHASEQTL---RGVRGNKIAMIFQEPmvs 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 90 ----------VWHYLTLHQ---HDKTRTELLN--DVAGALALDDKLGRSTNQLSGGEWQRVRLAAVVLqitpqANPagQL 154
Cdd:PRK15134 105 lnplhtlekqLYEVLSLHRgmrREAARGEILNclDRVGIRQAAKRLTDYPHQLSGGERQRVMIAMALL-----TRP--EL 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1432492527 155 LLLDEPMNSLDVAQQSALDKILSALCQQ-GLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPP 224
Cdd:PRK15134 178 LIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAP 248
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
12-191 |
3.17e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 62.59 E-value: 3.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 12 ESTRLGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGMTSGKGsiqFAGQPL-EAWSATKLALHRA-----------YLS 79
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNN---FTGTILaNNRKPTKQILKRTgfvtqddilypHLT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 80 QQQTPPFAMPVWHYLTLHQHDKTRteLLNDVAGALAL----DDKLGRS-TNQLSGGEWQRVRLAAVVLqitpqANPAgqL 154
Cdd:PLN03211 157 VRETLVFCSLLRLPKSLTKQEKIL--VAESVISELGLtkceNTIIGNSfIRGISGGERKRVSIAHEML-----INPS--L 227
|
170 180 190
....*....|....*....|....*....|....*..
gi 1432492527 155 LLLDEPMNSLDVAQQSALDKILSALCQQGLAIVMSSH 191
Cdd:PLN03211 228 LILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMH 264
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
19-231 |
3.31e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 62.76 E-value: 3.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKSTLLARMAGMTSGK-GSIQFAGQPLEAWS-ATKLALHRAYLSQ--QQTPPF--AMPVWH 92
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARgGRIMLNGKEINALStAQRLARGLVYLPEdrQSSGLYldAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 93 YLTLHQHDKTrteLLNDVAGALALDDKLGRSTN-----------QLSGGEWQRVRLAAVVlqitpQANPagQLLLLDEPM 161
Cdd:PRK15439 362 VCALTHNRRG---FWIKPARENAVLERYRRALNikfnhaeqaarTLSGGNQQKVLIAKCL-----EASP--QLLIVDEPT 431
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 162 NSLDVAQQSALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPPNLAQAYG 231
Cdd:PRK15439 432 RGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAINVDTIMRLAFG 501
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
23-211 |
3.34e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 61.04 E-value: 3.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 23 VRAGEILHLVGPNGAGKSTLLARMAGMTS-GKGSIQFAGQPLEAWSATKLAlhraYLSQQQTPPFAMpvwHYLTLHQ--H 99
Cdd:PRK10908 25 MRPGEMAFLTGHSGAGKSTLLKLICGIERpSAGKIWFSGHDITRLKNREVP----FLRRQIGMIFQD---HHLLMDRtvY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 100 DKTRTELLndVAGALALD---------DKLG---RSTN---QLSGGEWQRVRLAAVVLQitpqaNPAgqLLLLDEPMNSL 164
Cdd:PRK10908 98 DNVAIPLI--IAGASGDDirrrvsaalDKVGlldKAKNfpiQLSGGEQQRVGIARAVVN-----KPA--VLLADEPTGNL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1432492527 165 DVAQQSALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKM 211
Cdd:PRK10908 169 DDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
16-230 |
3.43e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 61.43 E-value: 3.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 16 LGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGMT-SGKGSIQFAGQPLEAWSATKLALHRAYLSQQQTPPFA-MPVWHY 93
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPrATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRRVFSrMTVEEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 94 LTLHQHDKTRTELLNDVAGALALDDKLGRSTNQ----LSGGEWQRVRLAAVVLqitpqANPagQLLLLDEPmnSLDVAQ- 168
Cdd:PRK11614 101 LAMGGFFAERDQFQERIKWVYELFPRLHERRIQragtMSGGEQQMLAIGRALM-----SQP--RLLLLDEP--SLGLAPi 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1432492527 169 --QSALDKIlSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPPNLAQAY 230
Cdd:PRK11614 172 iiQQIFDTI-EQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAY 234
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-224 |
3.61e-11 |
|
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: 62.39 E-value: 3.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKS-------TLLARMAGMTSGkgSIQFAGQPLEAWSATKLalhRAYLSQQ-----QTPpf 86
Cdd:COG4172 29 VSFDIAAGETLALVGESGSGKSvtalsilRLLPDPAAHPSG--SILFDGQDLLGLSEREL---RRIRGNRiamifQEP-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 87 aM----PVW-------HYLTLHQ-----HDKTRT-ELLNDVaGALALDDKLGRSTNQLSGGEWQRVRLAAVVlqitpqAN 149
Cdd:COG4172 102 -MtslnPLHtigkqiaEVLRLHRglsgaAARARAlELLERV-GIPDPERRLDAYPHQLSGGQRQRVMIAMAL------AN 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1432492527 150 -PagQLLLLDEPMNSLDVAQQSALDKILSALCQQ-GLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPP 224
Cdd:COG4172 174 eP--DLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAAP 248
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
22-228 |
3.80e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 62.35 E-value: 3.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLLARMAGM---TSgkGSIQFAGQPLEAWS---ATKLALhraylsqqqtppfAMpvwhylt 95
Cdd:COG3845 27 TVRPGEIHALLGENGAGKSTLMKILYGLyqpDS--GEILIDGKPVRIRSprdAIALGI-------------GM------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 96 LHQH---------------------------DKTRTELLnDVAGALALDDKLGRSTNQLSGGEWQRVRLAAVVLQitpQA 148
Cdd:COG3845 85 VHQHfmlvpnltvaenivlgleptkggrldrKAARARIR-ELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYR---GA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 149 npagQLLLLDEPMNSLDVAQQSALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVlTPPNLAQ 228
Cdd:COG3845 161 ----RILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAET-SEEELAE 235
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
23-215 |
5.59e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 60.80 E-value: 5.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 23 VRAGEILHLVGPNGAGKSTLLARMAGMTSGKGS----IQFAGQPLE-----AWSATKLALHRAYLSQQ------------ 81
Cdd:PRK09984 27 IHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSagshIELLGRTVQregrlARDIRKSRANTGYIFQQfnlvnrlsvlen 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 82 ------QTPPFAMPVWHYLTLHQHDKTRTELLNDVAGALAlddklGRSTNQLSGGEWQRVRLAAVVLQitpqanpAGQLL 155
Cdd:PRK09984 107 vligalGSTPFWRTCFSWFTREQKQRALQALTRVGMVHFA-----HQRVSTLSGGQQQRVAIARALMQ-------QAKVI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1432492527 156 LLDEPMNSLDVAQQSALDKILSALCQQ-GLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASG 215
Cdd:PRK09984 175 LADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
19-200 |
6.47e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 59.82 E-value: 6.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKSTLLARMAGMTS-GKGSIQFAGQPLeawSATKLALHR--AYLSQQQ------TPpfamp 89
Cdd:PRK13538 20 LSFTLNAGELVQIEGPNGAGKTSLLRILAGLARpDAGEVLWQGEPI---RRQRDEYHQdlLYLGHQPgiktelTA----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 90 vWHYLT--LHQHDKTRTELLNDVAGALALDDKLGRSTNQLSGGEWQRVRLAAVVLQITPqanpagqLLLLDEPMNSLDVA 167
Cdd:PRK13538 92 -LENLRfyQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAP-------LWILDEPFTAIDKQ 163
|
170 180 190
....*....|....*....|....*....|...
gi 1432492527 168 QQSALDKILSALCQQGLAIVMSSHdlnHTLRHA 200
Cdd:PRK13538 164 GVARLEALLAQHAEQGGMVILTTH---QDLPVA 193
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
16-191 |
7.23e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 59.86 E-value: 7.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 16 LGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGMT-SGKGSIQFAGQPLEAWSATKLALHRAYLSQQQTPPFAMPVWHYL 94
Cdd:PRK13543 27 FGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLhVESGQIQIDGKTATRGDRSRFMAYLGHLPGLKADLSTLENLHFL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 95 T-LHQHDKTRTEllndvAGALAL------DDKLGRstnQLSGGEWQRVRLAAVVLQITPqanpagqLLLLDEPMNSLDVA 167
Cdd:PRK13543 107 CgLHGRRAKQMP-----GSALAIvglagyEDTLVR---QLSAGQKKRLALARLWLSPAP-------LWLLDEPYANLDLE 171
|
170 180
....*....|....*....|....
gi 1432492527 168 QQSALDKILSALCQQGLAIVMSSH 191
Cdd:PRK13543 172 GITLVNRMISAHLRGGGAALVTTH 195
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
22-224 |
7.25e-11 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 60.39 E-value: 7.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLL---ARMAGMTSGkgSIQFAGQPLEAwSATKLALHRAYLS---QQqtppFA----MPVW 91
Cdd:COG1126 23 DVEKGEVVVIIGPSGSGKSTLLrciNLLEEPDSG--TITVDGEDLTD-SKKDINKLRRKVGmvfQQ----FNlfphLTVL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 92 HYLTLHQ---HDKTRTE-------LLNDVaGalaLDDKLGRSTNQLSGGEWQRVRLA-AVVLqitpqaNPagQLLLLDEP 160
Cdd:COG1126 96 ENVTLAPikvKKMSKAEaeerameLLERV-G---LADKADAYPAQLSGGQQQRVAIArALAM------EP--KVMLFDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1432492527 161 mnsldvaqQSALD--------KILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPP 224
Cdd:COG1126 164 --------TSALDpelvgevlDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENP 227
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
15-220 |
8.52e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 61.04 E-value: 8.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 15 RLGPLSGEVR----AGEILHLVGPNGAGKSTLLARMAGMTS-GKGSIQFAGQPL-EAWSATKLALHR---AYLSQQqtpp 85
Cdd:PRK11144 9 QLGDLCLTVNltlpAQGITAIFGRSGAGKTSLINAISGLTRpQKGRIVLNGRVLfDAEKGICLPPEKrriGYVFQD---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 86 fAMPVWHYLT----LHQHDKTRTELLNDVAGALALDDKLGRSTNQLSGGEWQRVRLAAVVLQitpqanpAGQLLLLDEPM 161
Cdd:PRK11144 85 -ARLFPHYKVrgnlRYGMAKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLT-------APELLLMDEPL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 162 NSLDVAQQSALDKILSALCQQ-GLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEV 220
Cdd:PRK11144 157 ASLDLPRKRELLPYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
22-218 |
8.99e-11 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 60.08 E-value: 8.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLLARMAG-----MTSgkGSIQFAGQPLEAWSATKlalhRA----YLSQQQTPPFA-MPVW 91
Cdd:COG0396 22 TIKPGEVHAIMGPNGSGKSTLAKVLMGhpkyeVTS--GSILLDGEDILELSPDE----RAragiFLAFQYPVEIPgVSVS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 92 HYLTL---HQHDKTRT-----ELLNDVAGALALDDK-LGRSTNQ-LSGGEWQRVRLAAVVLQitpqaNPAgqLLLLDEPM 161
Cdd:COG0396 96 NFLRTalnARRGEELSareflKLLKEKMKELGLDEDfLDRYVNEgFSGGEKKRNEILQMLLL-----EPK--LAILDETD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1432492527 162 NSLDVAqqsALdKILS----ALCQQGLAIVMSSHD---LNHTlrHAHRAWLLKGGKMLASGRRE 218
Cdd:COG0396 169 SGLDID---AL-RIVAegvnKLRSPDRGILIITHYqriLDYI--KPDFVHVLVDGRIVKSGGKE 226
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
31-226 |
1.00e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 60.20 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 31 LVGPNGAGKSTLLARMAG-MTSGKGSIQFAGQPLeawsaTKLALH--RAYL--------SQQQTPPFAMPV-WHYLTLHQ 98
Cdd:PRK13652 35 VIGPNGAGKSTLFRHFNGiLKPTSGSVLIRGEPI-----TKENIRevRKFVglvfqnpdDQIFSPTVEQDIaFGPINLGL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 99 HDKTRTELLNDVAGALALDDKLGRSTNQLSGGEWQRVRLAAVvLQITPQanpagqLLLLDEPMNSLDVAQQSALDKILSA 178
Cdd:PRK13652 110 DEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGV-IAMEPQ------VLVLDEPTAGLDPQGVKELIDFLND 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1432492527 179 LCQQ-GLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPPNL 226
Cdd:PRK13652 183 LPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDL 231
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
31-192 |
1.15e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 60.85 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 31 LVGPNGAGKSTLLARMAG-MTSGKGSIQFAGQpleawsatklaLHRAYLSQQQTPPFAMPVWHYltLHQHDKTRTELLN- 108
Cdd:COG0488 29 LVGRNGAGKSTLLKILAGeLEPDSGEVSIPKG-----------LRIGYLPQEPPLDDDLTVLDT--VLDGDAELRALEAe 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 109 -------------------------DVAGALALD-------DKLG-------RSTNQLSGGEWQRVRLAAVVLQitpqaN 149
Cdd:COG0488 96 leeleaklaepdedlerlaelqeefEALGGWEAEaraeeilSGLGfpeedldRPVSELSGGWRRRVALARALLS-----E 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1432492527 150 PagQLLLLDEPMNSLDVAQQSALDKILSALcqQGlAIVMSSHD 192
Cdd:COG0488 171 P--DLLLLDEPTNHLDLESIEWLEEFLKNY--PG-TVLVVSHD 208
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
20-193 |
1.19e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 60.71 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 20 SGEVRAGEILHLVGPNGAGKSTLLARMAGMTSGK--GSIQFAGQPLEAWS-ATKLALHRAYLSQQQ-----TPpfAMPVW 91
Cdd:PRK13549 282 SFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRweGEIFIDGKPVKIRNpQQAIAQGIAMVPEDRkrdgiVP--VMGVG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 92 HYLTLHQHDK-TRTELLNDVAGALALDDKLGR----------STNQLSGGEWQRVRLAAVVLqitpqANPagQLLLLDEP 160
Cdd:PRK13549 360 KNITLAALDRfTGGSRIDDAAELKTILESIQRlkvktaspelAIARLSGGNQQKAVLAKCLL-----LNP--KILILDEP 432
|
170 180 190
....*....|....*....|....*....|...
gi 1432492527 161 MNSLDVAQQSALDKILSALCQQGLAIVMSSHDL 193
Cdd:PRK13549 433 TRGIDVGAKYEIYKLINQLVQQGVAIIVISSEL 465
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
120-226 |
1.34e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 60.10 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 120 LGRSTNQLSGGEWQRVRLAAVvLQITPQanpagqLLLLDEPMNSLDVAQQSALDKILSALCQQGLAIVMSSHDLNHTLRH 199
Cdd:PRK13651 159 LQRSPFELSGGQKRRVALAGI-LAMEPD------FLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEW 231
|
90 100 110
....*....|....*....|....*....|....*...
gi 1432492527 200 AHRAWLLKGGKMLASGRREEVLT-----------PPNL 226
Cdd:PRK13651 232 TKRTIFFKDGKIIKDGDTYDILSdnkfliennmePPKL 269
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
15-214 |
1.48e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 60.61 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 15 RLGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGMTSGK--GSIQFAGQPLEAWSATKLALHRAYL----SQQQTPPFAM 88
Cdd:TIGR02633 275 RVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfeGNVFINGKPVDIRNPAQAIRAGIAMvpedRKRHGIVPIL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 89 PVWHYLTLHQHDK-TRTELLNDVAGALALDDKLGR----------STNQLSGGEWQRVRLAAVVLqitpqANPagQLLLL 157
Cdd:TIGR02633 355 GVGKNITLSVLKSfCFKMRIDAAAELQIIGSAIQRlkvktaspflPIGRLSGGNQQKAVLAKMLL-----TNP--RVLIL 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1432492527 158 DEPMNSLDVAQQSALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLAS 214
Cdd:TIGR02633 428 DEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGD 484
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
19-191 |
1.97e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 58.73 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKSTLLARMAGMTS-GKGSIQFAGQPLEawsATKLALHRAYLSQQQTPPFAMPVWHYLTLH 97
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPpAAGTIKLDGGDID---DPDVAEACHYLGHRNAMKPALTVAENLEFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 98 QHDKTRTELlnDVAGALA---LDDKLGRSTNQLSGGeWQRvRLAAVVLQITPQAnpagqLLLLDEPMNSLDVAQQSALDK 174
Cdd:PRK13539 98 AAFLGGEEL--DIAAALEavgLAPLAHLPFGYLSAG-QKR-RVALARLLVSNRP-----IWILDEPTAALDAAAVALFAE 168
|
170
....*....|....*..
gi 1432492527 175 ILSALCQQGLAIVMSSH 191
Cdd:PRK13539 169 LIRAHLAQGGIVIAATH 185
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
27-224 |
2.40e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 59.02 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 27 EILHLVGPNGAGKSTLLA---RMAGM---TSGKGSIQFAGQPLEAWSATKLALHRAY-LSQQQTPPFAMPVW----HYLT 95
Cdd:PRK14239 32 EITALIGPSGSGKSTLLRsinRMNDLnpeVTITGSIVYNGHNIYSPRTDTVDLRKEIgMVFQQPNPFPMSIYenvvYGLR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 96 LH-QHDKTRTE--LLNDVAGALALD---DKLGRSTNQLSGGEWQRVRLAAvVLQITPqanpagQLLLLDEPMNSLDVAQQ 169
Cdd:PRK14239 112 LKgIKDKQVLDeaVEKSLKGASIWDevkDRLHDSALGLSGGQQQRVCIAR-VLATSP------KIILLDEPTSALDPISA 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1432492527 170 SALDKILSALCQQgLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPP 224
Cdd:PRK14239 185 GKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNP 238
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
16-224 |
2.62e-10 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 59.71 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 16 LGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGM---TSGKgsIQFAGQPLEAWSATK---------LALHRaYLSQQQT 83
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLehqTSGH--IRFHGTDVSRLHARDrkvgfvfqhYALFR-HMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 84 PPFAMPVwhyLTLHQH------DKTRTELLNDVAgalaLDDKLGRSTNQLSGGEWQRVRLAAvVLQITPqanpagQLLLL 157
Cdd:PRK10851 95 IAFGLTV---LPRRERpnaaaiKAKVTQLLEMVQ----LAHLADRYPAQLSGGQKQRVALAR-ALAVEP------QILLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1432492527 158 DEPMNSLDVAQQSALDKILSALCQQ-GLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPP 224
Cdd:PRK10851 161 DEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP 228
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
14-201 |
3.30e-10 |
|
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: 57.16 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 14 TRLGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGM-TSGKGSIQFAGQPleawsatklalHRAYLSQQqtpPFaMPVwh 92
Cdd:cd03223 15 VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLwPWGSGRIGMPEGE-----------DLLFLPQR---PY-LPL-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 93 yLTLhqhdktRTELlndvagALALDDKlgrstnqLSGGEWQRVRLAAVVLQitpqaNPagQLLLLDEPMNSLDVAQQsal 172
Cdd:cd03223 78 -GTL------REQL------IYPWDDV-------LSGGEQQRLAFARLLLH-----KP--KFVFLDEATSALDEESE--- 127
|
170 180
....*....|....*....|....*....
gi 1432492527 173 DKILSALCQQGLAIVMSSHdlNHTLRHAH 201
Cdd:cd03223 128 DRLYQLLKELGITVISVGH--RPSLWKFH 154
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
23-219 |
3.32e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 59.68 E-value: 3.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 23 VRAGEILHLVGPNGAGKSTLLARMAGM-TSGKGSIQFAGQPLEAWSATKLALHRAYLSQQQtpPFAMP-------VWHYL 94
Cdd:PRK15439 34 LHAGEVHALLGGNGAGKSTLMKIIAGIvPPDSGTLEIGGNPCARLTPAKAHQLGIYLVPQE--PLLFPnlsvkenILFGL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 95 TLHQHDKTR-TELLNDVAGALALDDKLGrstnQLSGGEWQRVRLAAVVLQitpqanpAGQLLLLDEPMNSLDVAQQSALD 173
Cdd:PRK15439 112 PKRQASMQKmKQLLAALGCQLDLDSSAG----SLEVADRQIVEILRGLMR-------DSRILILDEPTASLTPAETERLF 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1432492527 174 KILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREE 219
Cdd:PRK15439 181 SRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTAD 226
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
24-193 |
3.52e-10 |
|
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: 59.41 E-value: 3.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 24 RAGEILHLVGPNGAGKSTLLARMAG-------MTSGKGSIQfagQPLEAWSATKLALHRAYLSQQQTPPFAMPVWHYLTL 96
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGelkpnlgDYDEEPSWD---EVLKRFRGTELQDYFKKLANGEIKVAHKPQYVDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 97 HQHDKTRTELLN---------DVAGALALDDKLGRSTNQLSGGEWQRVRLAAVVLQitpqanpAGQLLLLDEPMNSLDVA 167
Cdd:COG1245 174 KVFKGTVRELLEkvdergkldELAEKLGLENILDRDISELSGGELQRVAIAAALLR-------DADFYFFDEPSSYLDIY 246
|
170 180
....*....|....*....|....*.
gi 1432492527 168 QQSALDKILSALCQQGLAIVMSSHDL 193
Cdd:COG1245 247 QRLNVARLIRELAEEGKYVLVVEHDL 272
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
23-225 |
3.69e-10 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 58.18 E-value: 3.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 23 VRAGEILHLVGPNGAGKSTLLA-------------RMAGMTSGKGSIQFAGQPLEAwsatKLALHRAYLSQQQTppfAMP 89
Cdd:PRK09493 24 IDQGEVVVIIGPSGSGKSTLLRcinkleeitsgdlIVDGLKVNDPKVDERLIRQEA----GMVFQQFYLFPHLT---ALE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 90 VWHYLTLHQHDKTRTE---LLNDVAGALALDDKLGRSTNQLSGGEWQRVRLAAvVLQITPqanpagQLLLLDEPMNSLDV 166
Cdd:PRK09493 97 NVMFGPLRVRGASKEEaekQARELLAKVGLAERAHHYPSELSGGQQQRVAIAR-ALAVKP------KLMLFDEPTSALDP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 167 AQQSALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLT-PPN 225
Cdd:PRK09493 170 ELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKnPPS 229
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
25-215 |
3.86e-10 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 58.10 E-value: 3.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 25 AGEILHLVGPNGAGKSTLLARMAGM-TSGKGSIQFAGQ----PLEAWSATKLALHR--AYLSQQQTppfampVWHYLTLH 97
Cdd:COG4161 27 SGETLVLLGPSGAGKSSLLRVLNLLeTPDSGQLNIAGHqfdfSQKPSEKAIRLLRQkvGMVFQQYN------LWPHLTVM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 98 QH---------DKTRTELLNDVAGALA---LDDKLGRSTNQLSGGEWQRVRLAAvVLQITPqanpagQLLLLDEPMNSLD 165
Cdd:COG4161 101 ENlieapckvlGLSKEQAREKAMKLLArlrLTDKADRFPLHLSGGQQQRVAIAR-ALMMEP------QVLLFDEPTAALD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1432492527 166 VAQQSALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASG 215
Cdd:COG4161 174 PEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG 223
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
22-224 |
3.97e-10 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 58.94 E-value: 3.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLLaRMAGM----TSGkgSIQFAGQPLEAWSATKLALHRAYLS---QQqtppF-------- 86
Cdd:COG1135 27 TIEKGEIFGIIGYSGAGKSTLI-RCINLlerpTSG--SVLVDGVDLTALSERELRAARRKIGmifQH----Fnllssrtv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 87 ----AMPvwhyLTLHQHDKTR-----TELLNDVaGalaLDDKLGRSTNQLSGGEWQRV---R-LAavvlqitpqANPagQ 153
Cdd:COG1135 100 aenvALP----LEIAGVPKAEirkrvAELLELV-G---LSDKADAYPSQLSGGQKQRVgiaRaLA---------NNP--K 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 154 LLLLDEPmnsldvaqQSALD-----KILsALCQQ-----GLAIVMSSHDLnHTLRH-AHRAWLLKGGKMLASGRREEVLT 222
Cdd:COG1135 161 VLLCDEA--------TSALDpettrSIL-DLLKDinrelGLTIVLITHEM-DVVRRiCDRVAVLENGRIVEQGPVLDVFA 230
|
..
gi 1432492527 223 PP 224
Cdd:COG1135 231 NP 232
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
11-220 |
5.03e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 58.49 E-value: 5.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 11 AESTRLGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGM-TSGKGSIQFAGQPLEawSATKLALHRAYLSQQQTP----- 84
Cdd:PRK13635 18 AATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLlLPEAGTITVGGMVLS--EETVWDVRRQVGMVFQNPdnqfv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 85 --------PFAmpvwhyltLHQHDKTRTELLNDVAGALAL---DDKLGRSTNQLSGGEWQRVRLAAVVLQitpqanpAGQ 153
Cdd:PRK13635 96 gatvqddvAFG--------LENIGVPREEMVERVDQALRQvgmEDFLNREPHRLSGGQKQRVAIAGVLAL-------QPD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1432492527 154 LLLLDEPMNSLD-VAQQSALDKILSALCQQGLAIVMSSHDLNHTLRhAHRAWLLKGGKMLASGRREEV 220
Cdd:PRK13635 161 IIILDEATSMLDpRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEI 227
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
23-215 |
5.14e-10 |
|
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: 57.60 E-value: 5.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 23 VRAGEILHLVGPNGAGKSTLLARMAGM-TSGKGSIQFAGQPLEAWSATKLALHRAYLSQQQTpPFAMPVWHYLTLHQHDK 101
Cdd:cd03245 27 IRAGEKVAIIGRVGSGKSTLLKLLAGLyKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQDVT-LFYGTLRDNITLGAPLA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 102 TRTELLN--DVAGALALDDKLGRSTN--------QLSGGEWQRVRLAAVVLqitpqANPAgqLLLLDEPMNSLDvaqQSA 171
Cdd:cd03245 106 DDERILRaaELAGVTDFVNKHPNGLDlqigergrGLSGGQRQAVALARALL-----NDPP--ILLLDEPTSAMD---MNS 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1432492527 172 LDKILSALcQQGLA---IVMSSHDLNhTLRHAHRAWLLKGGKMLASG 215
Cdd:cd03245 176 EERLKERL-RQLLGdktLIIITHRPS-LLDLVDRIIVMDSGRIVADG 220
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
19-224 |
5.90e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 57.79 E-value: 5.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKS-TLLARM----AGMTSGKGSIQFAGQPLEAwsATKLALHRAYLSQQQTPPF----AMP 89
Cdd:PRK10418 22 VSLTLQRGRVLALVGGSGSGKSlTCAAALgilpAGVRQTAGRVLLDGKPVAP--CALRGRKIATIMQNPRSAFnplhTMH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 90 VWHYLTLHQHDKTRTE-LLNDVAGALALDDK---LGRSTNQLSGGEWQRVRLAAVVLQITPqanpagqLLLLDEPMNSLD 165
Cdd:PRK10418 100 THARETCLALGKPADDaTLTAALEAVGLENAarvLKLYPFEMSGGMLQRMMIALALLCEAP-------FIIADEPTTDLD 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 166 -VAQQSALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPP 224
Cdd:PRK10418 173 vVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAP 232
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
19-222 |
5.91e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 58.28 E-value: 5.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKSTLLARMAGMTS-GKGSIQFAGQPLEawSATKLALHRAYLSQQ---QTPPFAMP----- 89
Cdd:PRK13537 26 LSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHpDAGSISLCGEPVP--SRARHARQRVGVVPQfdnLDPDFTVRenllv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 90 VWHYLTLHQHD-KTRTELLNDVAgalALDDKLGRSTNQLSGGEWQRVRLAAVVLQitpqaNPagQLLLLDEPMNSLDVAQ 168
Cdd:PRK13537 104 FGRYFGLSAAAaRALVPPLLEFA---KLENKADAKVGELSGGMKRRLTLARALVN-----DP--DVLVLDEPTTGLDPQA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1432492527 169 QSALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLT 222
Cdd:PRK13537 174 RHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
19-219 |
8.13e-10 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 58.43 E-value: 8.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKSTLLA---RMAGMTSGKGSIQfaGQPLEawSATKLALHRAYLSQQQTPP-FAMPVWHYL 94
Cdd:PRK13657 354 VSFEAKPGQTVAIVGPTGAGKSTLINllqRVFDPQSGRILID--GTDIR--TVTRASLRRNIAVVFQDAGlFNRSIEDNI 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 95 TLHQHDKTRTELLNDVAGALALD------DKL----GRSTNQLSGGEWQRVRLAAVVLQITPqanpagqLLLLDEPMNSL 164
Cdd:PRK13657 430 RVGRPDATDEEMRAAAERAQAHDfierkpDGYdtvvGERGRQLSGGERQRLAIARALLKDPP-------ILILDEATSAL 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1432492527 165 DVAQ----QSALDKILsalcqQGLAIVMSSHDLNhTLRHAHRAWLLKGGKMLASGRREE 219
Cdd:PRK13657 503 DVETeakvKAALDELM-----KGRTTFIIAHRLS-TVRNADRILVFDNGRVVESGSFDE 555
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
19-192 |
1.06e-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: 58.02 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKSTLLARMAGM-TSGKGSIQFAgqpleawSATKLAL---HRAYLSQQQTppfampVWHyl 94
Cdd:TIGR03719 341 LSFKLPPGGIVGVIGPNGAGKSTLFRMITGQeQPDSGTIEIG-------ETVKLAYvdqSRDALDPNKT------VWE-- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 95 tlhqhdktrtellnDVAGALALDDKLGRSTN--------------------QLSGGEWQRVRLAAVVLQitpqanpAGQL 154
Cdd:TIGR03719 406 --------------EISGGLDIIKLGKREIPsrayvgrfnfkgsdqqkkvgQLSGGERNRVHLAKTLKS-------GGNV 464
|
170 180 190
....*....|....*....|....*....|....*...
gi 1432492527 155 LLLDEPMNSLDVAQQSALDKILSALcqQGLAIVMsSHD 192
Cdd:TIGR03719 465 LLLDEPTNDLDVETLRALEEALLNF--AGCAVVI-SHD 499
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
19-224 |
1.06e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 57.83 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKS-TLLARMaGMTSGKG-----SIQFAGQPLEAWSATK----------LALHRAYLSQQQ 82
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvSSLAIM-GLIDYPGrvmaeKLEFNGQDLQRISEKErrnlvgaevaMIFQDPMTSLNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 83 TPPFAMPVWHYLTLHQHDKTRT------ELLNDVaGALALDDKLGRSTNQLSGGEWQRVRLAAVVlqitpQANPagQLLL 156
Cdd:PRK11022 105 CYTVGFQIMEAIKVHQGGNKKTrrqraiDLLNQV-GIPDPASRLDVYPHQLSGGMSQRVMIAMAI-----ACRP--KLLI 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1432492527 157 LDEPMNSLDVAQQSALDKILSALCQQ-GLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPP 224
Cdd:PRK11022 177 ADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAP 245
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-224 |
1.26e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 56.84 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLL------------ARMAgmtsgkGSIQFAGQPLEAWSATKLALHRAYLSQQQTPPFAMP 89
Cdd:PRK14247 25 EIPDNTITALMGPSGSGKSTLLrvfnrlielypeARVS------GEVYLDGQDIFKMDVIELRRRVQMVFQIPNPIPNLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 90 VWHY----LTLHQHDKTRTELLNDVAGAL-------ALDDKLGRSTNQLSGGEWQRVRLAAvVLQITPqanpagQLLLLD 158
Cdd:PRK14247 99 IFENvalgLKLNRLVKSKKELQERVRWALekaqlwdEVKDRLDAPAGKLSGGQQQRLCIAR-ALAFQP------EVLLAD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1432492527 159 EPMNSLDVAQQSALDKILSALcQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPP 224
Cdd:PRK14247 172 EPTANLDPENTAKIESLFLEL-KKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNP 236
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
22-210 |
1.30e-09 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 56.32 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLLARMAG-MTSGKGSIQFAGqpleawsatklalHRAYLSQQqtpPFAMP-------VWHy 93
Cdd:cd03250 27 EVPKGELVAIVGPVGSGKSSLLSALLGeLEKLSGSVSVPG-------------SIAYVSQE---PWIQNgtireniLFG- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 94 ltlHQHDKTRtelLNDVAGALALDDKL------------GRSTNqLSGGEWQRVRLAAVVLQITpqanpagQLLLLDEPM 161
Cdd:cd03250 90 ---KPFDEER---YEKVIKACALEPDLeilpdgdlteigEKGIN-LSGGQKQRISLARAVYSDA-------DIYLLDDPL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1432492527 162 NSLD--VAQQSALDKILSALcQQGLAIVMSSHDLnHTLRHAHRAWLLKGGK 210
Cdd:cd03250 156 SAVDahVGRHIFENCILGLL-LNNKTRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
25-230 |
1.77e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 56.63 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 25 AGEILHLVGPNGAGKSTLLARMAG-MTSGKGSIQFAGQPLEAWSAtklalHRAYLSQQQtppfAMPVWH------YLTLH 97
Cdd:PRK11248 26 SGELLVVLGPSGCGKTTLLNLIAGfVPYQHGSITLDGKPVEGPGA-----ERGVVFQNE----GLLPWRnvqdnvAFGLQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 98 QHDKTRTELLNDVAGALALDDKLG---RSTNQLSGGEWQRVRLAAVVlqitpQANPagQLLLLDEPMNSLDVAQQSALDK 174
Cdd:PRK11248 97 LAGVEKMQRLEIAHQMLKKVGLEGaekRYIWQLSGGQRQRVGIARAL-----AANP--QLLLLDEPFGALDAFTREQMQT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1432492527 175 ILSALCQ-QGLAIVMSSHDLNHTLRHAHRAWLLKGGkmlaSGRREEVLtPPNLAQAY 230
Cdd:PRK11248 170 LLLKLWQeTGKQVLLITHDIEEAVFMATELVLLSPG----PGRVVERL-PLNFARRF 221
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
31-198 |
1.98e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 57.49 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 31 LVGPNGAGKSTLLARMAG-MTSGKGSIQFA-GQPLEAWSATKLALHRAYLSqqqtppfamPVWHYLTLhqHDKTRTELLN 108
Cdd:PRK10636 343 LLGRNGAGKSTLIKLLAGeLAPVSGEIGLAkGIKLGYFAQHQLEFLRADES---------PLQHLARL--APQELEQKLR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 109 DVAGALALD-DKLGRSTNQLSGGEWQRVRLAAVVLQitpqaNPagQLLLLDEPMNSLDVAQQSALDKilsALCQQGLAIV 187
Cdd:PRK10636 412 DYLGGFGFQgDKVTEETRRFSGGEKARLVLALIVWQ-----RP--NLLLLDEPTNHLDLDMRQALTE---ALIDFEGALV 481
|
170
....*....|.
gi 1432492527 188 MSSHDlNHTLR 198
Cdd:PRK10636 482 VVSHD-RHLLR 491
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
16-224 |
2.54e-09 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 56.02 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 16 LGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGMTS-GKGSIQFAGQPLEAWSATklalhRAYLSQQQTppfAMP----- 89
Cdd:COG4525 23 LQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLApSSGEITLDGVPVTGPGAD-----RGVVFQKDA---LLPwlnvl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 90 --VWHYLTLHQHDK-TRTELLNDVAGALALDDKLGRSTNQLSGGEWQRVRLAAVVlqitpQANPagQLLLLDEPMNSLDV 166
Cdd:COG4525 95 dnVAFGLRLRGVPKaERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARAL-----AADP--RFLLMDEPFGALDA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1432492527 167 A---QQSALdkILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGkmlaSGRREEVLTPP 224
Cdd:COG4525 168 LtreQMQEL--LLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPG----PGRIVERLELD 222
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
23-226 |
2.64e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 56.15 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 23 VRAGEILHLVGPNGAGKSTLLARMAGMTS-GKGSIQFAGqpLEAWSATKLALHRAYL----SQQQTPPFAMPVWHYLTLH 97
Cdd:PRK13644 25 IKKGEYIGIIGKNGSGKSTLALHLNGLLRpQKGKVLVSG--IDTGDFSKLQGIRKLVgivfQNPETQFVGRTVEEDLAFG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 98 QHDKT--RTELLNDVAGALA---LDDKLGRSTNQLSGGEWQRVRLAAVvLQITPQAnpagqlLLLDEPMNSLDVAQQSAL 172
Cdd:PRK13644 103 PENLClpPIEIRKRVDRALAeigLEKYRHRSPKTLSGGQGQCVALAGI-LTMEPEC------LIFDEVTSMLDPDSGIAV 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1432492527 173 DKILSALCQQGLAIVMSSHDLNHtLRHAHRAWLLKGGKMLASGRREEVLTPPNL 226
Cdd:PRK13644 176 LERIKKLHEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSL 228
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
19-221 |
4.39e-09 |
|
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: 55.18 E-value: 4.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKSTLLARMAGM-TSGKGSIQFAGQPLEAWSATKLALHRAYLSQQQTPpFAMPVWHYLTLH 97
Cdd:cd03252 21 ISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFyVPENGRVLVDGHDLALADPAWLRRQVGVVLQENVL-FNRSIRDNIALA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 98 QH--DKTRTELLNDVAGA--------LALDDKLGRSTNQLSGGEWQRVRLAAVVLQitpqaNPagQLLLLDEPMNSLDVA 167
Cdd:cd03252 100 DPgmSMERVIEAAKLAGAhdfiselpEGYDTIVGEQGAGLSGGQRQRIAIARALIH-----NP--RILIFDEATSALDYE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1432492527 168 QQSALDKILSALCQQGLAIVMsSHDLNhTLRHAHRAWLLKGGKMLASGRREEVL 221
Cdd:cd03252 173 SEHAIMRNMHDICAGRTVIII-AHRLS-TVKNADRIIVMEKGRIVEQGSHDELL 224
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
22-224 |
5.25e-09 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 55.04 E-value: 5.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLLA---RMAGMTSG---KGSIQFAGQPLEAwSATKLALHRA---YLSQQQTPpFAMPVWH 92
Cdd:COG1117 33 DIPENKVTALIGPSGCGKSTLLRclnRMNDLIPGarvEGEILLDGEDIYD-PDVDVVELRRrvgMVFQKPNP-FPKSIYD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 93 ---Y-LTLHqHDKTRTELLNDVAGAL---AL----DDKLGRSTNQLSGGEWQRVRLA---AVvlqitpqaNPagQLLLLD 158
Cdd:COG1117 111 nvaYgLRLH-GIKSKSELDEIVEESLrkaALwdevKDRLKKSALGLSGGQQQRLCIAralAV--------EP--EVLLMD 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1432492527 159 EPMnsldvaqqSALD-----KI---LSALCQQgLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPP 224
Cdd:COG1117 180 EPT--------SALDpistaKIeelILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNP 244
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
25-215 |
5.60e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 55.02 E-value: 5.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 25 AGEILHLVGPNGAGKSTL---LARMAGMTSGKGSI-----QFAGQPLEAwsaTKLALHR--AYLSQQQTppfampVWHYL 94
Cdd:PRK11124 27 QGETLVLLGPSGAGKSSLlrvLNLLEMPRSGTLNIagnhfDFSKTPSDK---AIRELRRnvGMVFQQYN------LWPHL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 95 TLHQH-----------DKTRT-----ELLNdvagALALDDKLGRSTNQLSGGEWQRVRLAAvVLQITPqanpagQLLLLD 158
Cdd:PRK11124 98 TVQQNlieapcrvlglSKDQAlaraeKLLE----RLRLKPYADRFPLHLSGGQQQRVAIAR-ALMMEP------QVLLFD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1432492527 159 EPMNSLDVAQQSALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASG 215
Cdd:PRK11124 167 EPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
12-220 |
6.94e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 54.76 E-value: 6.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 12 ESTRLGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGMTSGK-GSIQFAGQPLEAWSATKLALHRAYLSQQQTPPFAMPV 90
Cdd:PRK13648 21 ASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKsGEIFYNNQAITDDNFEKLRKHIGIVFQNPDNQFVGSI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 91 WHY---LTLHQHDKTRTELLNDVAGALALDDKLGRST---NQLSGGEWQRVRLAAvVLQITPqanpagQLLLLDEPMNSL 164
Cdd:PRK13648 101 VKYdvaFGLENHAVPYDEMHRRVSEALKQVDMLERADyepNALSGGQKQRVAIAG-VLALNP------SVIILDEATSML 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1432492527 165 D-VAQQSALDKILSALCQQGLAIVMSSHDLNHTLrHAHRAWLLKGGKMLASGRREEV 220
Cdd:PRK13648 174 DpDARQNLLDLVRKVKSEHNITIISITHDLSEAM-EADHVIVMNKGTVYKEGTPTEI 229
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
22-222 |
8.02e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 55.13 E-value: 8.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAG--KSTLLARMAGMTSGKGSIQFAgqpleAWSATKLALHRAY-----LSQQQTPPFAMPVWHYL 94
Cdd:NF000106 35 DVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRPWRF*-----TWCANRRALRRTIg*hrpVR*GRRESFSGRENLYM 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 95 TLHQHDKTRTEL---LNDVAGALALDDKLGRSTNQLSGGEWQRVRLAAVVLqitpqANPAgqLLLLDEPMNSLDVAQQSA 171
Cdd:NF000106 110 IGR*LDLSRKDArarADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMI-----GRPA--VLYLDEPTTGLDPRTRNE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1432492527 172 LDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLT 222
Cdd:NF000106 183 VWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKT 233
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-237 |
8.06e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 54.66 E-value: 8.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKSTL---LARMAGMTSG---KGSIQFAGQPLEAWSATKLALHRAyLSQQQTPPFAMPVWH 92
Cdd:PRK14258 26 VSMEIYQSKVTAIIGPSGCGKSTFlkcLNRMNELESEvrvEGRVEFFNQNIYERRVNLNRLRRQ-VSMVHPKPNLFPMSV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 93 YLTLHQHDKT-----RTELLNDVAGALA-------LDDKLGRSTNQLSGGEWQRVRLAAvVLQITPqanpagQLLLLDEP 160
Cdd:PRK14258 105 YDNVAYGVKIvgwrpKLEIDDIVESALKdadlwdeIKHKIHKSALDLSGGQQQRLCIAR-ALAVKP------KVLLMDEP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 161 MNSLDVAQQSALDKILSAL-CQQGLAIVMSSHDLNHTLRHAHRAWLLKG-----GKMLASGRREEVLTPPNLAQAYGMNF 234
Cdd:PRK14258 178 CFGLDPIASMKVESLIQSLrLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSPHDSRTREYVL 257
|
...
gi 1432492527 235 RRL 237
Cdd:PRK14258 258 SRL 260
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
22-220 |
8.08e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.56 E-value: 8.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLLARMAGM-TSGKGSIQFAGQP---LEAWSATKLALHRAY--------LSQQQT------ 83
Cdd:PRK09700 27 TVYPGEIHALLGENGAGKSTLMKVLSGIhEPTKGTITINNINynkLDHKLAAQLGIGIIYqelsvideLTVLENlyigrh 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 84 ---PPFAMPVWHYLTLhqhdKTRTELLNDVAG-ALALDDKLGrstnQLSGGEWQRVRLAAVVLQitpqanpAGQLLLLDE 159
Cdd:PRK09700 107 ltkKVCGVNIIDWREM----RVRAAMMLLRVGlKVDLDEKVA----NLSISHKQMLEIAKTLML-------DAKVIIMDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1432492527 160 PMNSLDVAQQSALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEV 220
Cdd:PRK09700 172 PTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
19-222 |
9.01e-09 |
|
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: 54.36 E-value: 9.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKSTLlARM--AGMTSGKGSIQFAGqpLEAWSATKLALHR--------------------- 75
Cdd:TIGR04520 21 VSLSIEKGEFVAIIGHNGSGKSTL-AKLlnGLLLPTSGKVTVDG--LDTLDEENLWEIRkkvgmvfqnpdnqfvgatved 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 76 --AY-LSQQQTPPFAMpvwhyltlhqhdKTRTellNDVAGALALDDKLGRSTNQLSGGEWQRVRLAAvVLQITPqanpag 152
Cdd:TIGR04520 98 dvAFgLENLGVPREEM------------RKRV---DEALKLVGMEDFRDREPHLLSGGQKQRVAIAG-VLAMRP------ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1432492527 153 QLLLLDEPMNSLD-VAQQSALDKILSALCQQGLAIVMSSHDLNHTLrHAHRAWLLKGGKMLASGRREEVLT 222
Cdd:TIGR04520 156 DIIILDEATSMLDpKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKGKIVAEGTPREIFS 225
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
23-193 |
9.46e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.20 E-value: 9.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 23 VRAGEILHLVGPNGAGKSTLLARMAG-MTSGKGsiQFAGQP-----LEAWSATKLALHRAYLSQQQTPPFAMPvwHYLTL 96
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGeLIPNLG--DYEEEPswdevLKRFRGTELQNYFKKLYNGEIKVVHKP--QYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 97 --HQHDKTRTELL---------NDVAGALALDDKLGRSTNQLSGGEWQRVRLAAVVLQitpqanpAGQLLLLDEPMNSLD 165
Cdd:PRK13409 172 ipKVFKGKVRELLkkvdergklDEVVERLGLENILDRDISELSGGELQRVAIAAALLR-------DADFYFFDEPTSYLD 244
|
170 180
....*....|....*....|....*...
gi 1432492527 166 VAQQSALDKILSALcQQGLAIVMSSHDL 193
Cdd:PRK13409 245 IRQRLNVARLIREL-AEGKYVLVVEHDL 271
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
19-222 |
1.00e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 54.61 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKSTLLARMAGM---TSGKGSI--------------------------QFAGQPLE---AW 66
Cdd:PRK13632 28 VSFEINEGEYVAILGHNGSGKSTISKILTGLlkpQSGEIKIdgitiskenlkeirkkigiifqnpdnQFIGATVEddiAF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 67 SatklalhrayLSQQQTPPFAMPvwhyltlhqhdktrtELLNDVAGALALDDKLGRSTNQLSGGEWQRVRLAAvVLQITP 146
Cdd:PRK13632 108 G----------LENKKVPPKKMK---------------DIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIAS-VLALNP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1432492527 147 qanpagQLLLLDEPMNSLDVAQQSALDKILSALCQQGLAIVMS-SHDLNHTLRhAHRAWLLKGGKMLASGRREEVLT 222
Cdd:PRK13632 162 ------EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISiTHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILN 231
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
20-224 |
1.19e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 54.16 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 20 SGEVRAGEILHLVGPNGAGKSTLLARMAG-MTSGKGSIQFA---GQPLEAWS---ATKLALHR---AYLSQQQTPPFAMP 89
Cdd:PRK11701 26 SFDLYPGEVLGIVGESGSGKTTLLNALSArLAPDAGEVHYRmrdGQLRDLYAlseAERRRLLRtewGFVHQHPRDGLRMQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 90 VW---------------HYLTLHQhdkTRTELLNDVAGALALDDKLGRStnqLSGGEWQRvrlaavvLQITPQANPAGQL 154
Cdd:PRK11701 106 VSaggnigerlmavgarHYGDIRA---TAGDWLERVEIDAARIDDLPTT---FSGGMQQR-------LQIARNLVTHPRL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1432492527 155 LLLDEPMNSLDVAQQSALDKILSALC-QQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPP 224
Cdd:PRK11701 173 VFMDEPTGGLDVSVQARLLDLLRGLVrELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDDP 243
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
19-191 |
1.22e-08 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 53.80 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKSTLLARMAGMTSGK---GSIQFAGQ---------------------PLEAWSATKLALH 74
Cdd:TIGR01978 19 VNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSYEvtsGTILFKGQdllelepderaraglflafqyPEEIPGVSNLEFL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 75 R----AYLSQQQTPPFAMPVWHyltlhqhdktrtELLNDVAGALALD-DKLGRSTNQ-LSGGEWQRVRLaavvLQ---IT 145
Cdd:TIGR01978 99 RsalnARRSARGEEPLDLLDFE------------KLLKEKLALLDMDeEFLNRSVNEgFSGGEKKRNEI----LQmalLE 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1432492527 146 PqanpagQLLLLDEPMNSLDVAQQSALDKILSALCQQGLAIVMSSH 191
Cdd:TIGR01978 163 P------KLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITH 202
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
9-191 |
1.87e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.03 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 9 DVAESTRLGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGM-TSGKGSIQFAGQPLEAWSATklalhraYLSQQQTPPFA 87
Cdd:PRK13540 10 DYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLlNPEKGEILFERQSIKKDLCT-------YQKQLCFVGHR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 88 MPVWHYLTLHQ------HDKTRTELLNDVAGALALDDKLGRSTNQLSGGEWQRVRLAAVVLQitpqanpAGQLLLLDEPM 161
Cdd:PRK13540 83 SGINPYLTLREnclydiHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMS-------KAKLWLLDEPL 155
|
170 180 190
....*....|....*....|....*....|...
gi 1432492527 162 NSLDvaqQSALDKILSALCQ---QGLAIVMSSH 191
Cdd:PRK13540 156 VALD---ELSLLTIITKIQEhraKGGAVLLTSH 185
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
25-210 |
2.62e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 53.14 E-value: 2.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 25 AGEILHLVGPNGAGKSTLLARMAGMTSGKGSIQFAGQ-PL-EAWSATKLALHRAYLSQQQTppfampVWHYLTLHQHDKT 102
Cdd:PRK11247 37 AGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTaPLaEAREDTRLMFQDARLLPWKK------VIDNVGLGLKGQW 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 103 RTELLNDVAgALALDDKLGRSTNQLSGGEWQRVRLAAVVLQitpqaNPagQLLLLDEPMNSLDVAQQSALDKILSALCQQ 182
Cdd:PRK11247 111 RDAALQALA-AVGLADRANEWPAALSGGQKQRVALARALIH-----RP--GLLLLDEPLGALDALTRIEMQDLIESLWQQ 182
|
170 180
....*....|....*....|....*....
gi 1432492527 183 -GLAIVMSSHDLNHTLRHAHRAWLLKGGK 210
Cdd:PRK11247 183 hGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
101-215 |
3.79e-08 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 52.26 E-value: 3.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 101 KTRTELLNDVA-GALALDdklgRSTNQLSGGEWQRVRLAAvvlQItpQANPAGQLLLLDEPMNSLDVAQQSALDKILSAL 179
Cdd:cd03270 115 RERLGFLVDVGlGYLTLS----RSAPTLSGGEAQRIRLAT---QI--GSGLTGVLYVLDEPSIGLHPRDNDRLIETLKRL 185
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1432492527 180 CQQGLAIVMSSHDLNhTLRHAHraWLL--------KGGKMLASG 215
Cdd:cd03270 186 RDLGNTVLVVEHDED-TIRAAD--HVIdigpgagvHGGEIVAQG 226
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
14-224 |
5.10e-08 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 52.89 E-value: 5.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 14 TRLGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGM-TSGKGSIQF-AGQPLeawsatklalhrAYLSQQqtPpfampvw 91
Cdd:COG4178 377 PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLwPYGSGRIARpAGARV------------LFLPQR--P------- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 92 hYL---TLHQ-----------HDKTRTELLNDVA-GALA--LDDKLgRSTNQLSGGEWQRVRLAAVVLQitpqaNPagQL 154
Cdd:COG4178 436 -YLplgTLREallypataeafSDAELREALEAVGlGHLAerLDEEA-DWDQVLSLGEQQRLAFARLLLH-----KP--DW 506
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1432492527 155 LLLDEPMNSLDVAQQSALDKILSALCqQGLAIVMSSHDlnHTLRHAH-RAWLLKGGkmlASGRREEVLTPP 224
Cdd:COG4178 507 LFLDEATSALDEENEAALYQLLREEL-PGTTVISVGHR--STLAAFHdRVLELTGD---GSWQLLPAEAPA 571
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
119-215 |
5.14e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 51.17 E-value: 5.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 119 KLGRSTNQLSGGEWQRVRLAAVVlqitpQANPAGQLLLLDEPMNSLDVAQQSALDKILSALCQQGLAIVMSSHDLNhTLR 198
Cdd:cd03238 80 TLGQKLSTLSGGELQRVKLASEL-----FSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLD-VLS 153
|
90 100
....*....|....*....|....*
gi 1432492527 199 HAHraWLLK--------GGKMLASG 215
Cdd:cd03238 154 SAD--WIIDfgpgsgksGGKVVFSG 176
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
119-220 |
6.36e-08 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 53.09 E-value: 6.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 119 KLGRSTNQLSGGEWQRVRLAAVVlqitpQANPAGQ-LLLLDEPMNSL---DVAQqsaLDKILSALCQQGLAIVMSSHDLn 194
Cdd:TIGR00630 822 RLGQPATTLSGGEAQRIKLAKEL-----SKRSTGRtLYILDEPTTGLhfdDIKK---LLEVLQRLVDKGNTVVVIEHNL- 892
|
90 100 110
....*....|....*....|....*....|....
gi 1432492527 195 HTLRHAHraWLL--------KGGKMLASGRREEV 220
Cdd:TIGR00630 893 DVIKTAD--YIIdlgpeggdGGGTVVASGTPEEV 924
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
4-191 |
7.08e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.61 E-value: 7.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 4 VMQLQDVaestrlgplSGEVRAGEILHLVGPNGAGKSTLLARMAGM-TSGKGSIQFAGQPLeAWSATKLALHR--AYLSQ 80
Cdd:PRK11288 17 VKALDDI---------SFDCRAGQVHALMGENGAGKSTLLKILSGNyQPDAGSILIDGQEM-RFASTTAALAAgvAIIYQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 81 Q-QTPPfAMPVWHYLTL----HQHDKTRTELLNDVAGA----LALD----DKLGRstnqLSGGEWQRVRLAAVVLQitpq 147
Cdd:PRK11288 87 ElHLVP-EMTVAENLYLgqlpHKGGIVNRRLLNYEAREqlehLGVDidpdTPLKY----LSIGQRQMVEIAKALAR---- 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1432492527 148 anpAGQLLLLDEPMNSLDVAQQSALDKILSALCQQGLAIVMSSH 191
Cdd:PRK11288 158 ---NARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSH 198
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
103-233 |
7.92e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 51.72 E-value: 7.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 103 RTELLNDVAGALA---LDDKLGRSTNQLSGGEWQRVRLAAvVLQITPqanpagQLLLLDEPMNSLDVAQQSALDKILSAL 179
Cdd:PRK13640 117 RPEMIKIVRDVLAdvgMLDYIDSEPANLSGGQKQRVAIAG-ILAVEP------KIIILDESTSMLDPAGKEQILKLIRKL 189
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1432492527 180 CQQ-GLAIVMSSHDLNHTlRHAHRAWLLKGGKMLASGRREEVLTPPNLAQAYGMN 233
Cdd:PRK13640 190 KKKnNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVEMLKEIGLD 243
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
31-165 |
1.03e-07 |
|
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: 52.24 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 31 LVGPNGAGKSTLLARMAGMTSgkgsiQFAGqplEAWSAtkLALHRAYLSQQ-QTPP------------------------ 85
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVDK-----DFNG---EARPQ--PGIKVGYLPQEpQLDPtktvrenveegvaeikdaldrfne 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 86 ----FAMPVWHYLTLHQhDKTRTELLNDVAGALALDDKLGR------------STNQLSGGEWQRVRLAAVVLQitpqaN 149
Cdd:TIGR03719 106 isakYAEPDADFDKLAA-EQAELQEIIDAADAWDLDSQLEIamdalrcppwdaDVTKLSGGERRRVALCRLLLS-----K 179
|
170
....*....|....*.
gi 1432492527 150 PagQLLLLDEPMNSLD 165
Cdd:TIGR03719 180 P--DMLLLDEPTNHLD 193
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
19-249 |
1.22e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 51.65 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKS-TLLARMAGMTSG---KGSIQFAGQPLEAWSATKLALHRAylsQQ-----QTP----- 84
Cdd:PRK09473 35 LNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgriGGSATFNGREILNLPEKELNKLRA---EQismifQDPmtsln 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 85 PFaMPVWHYLT----LHQHDKTRTELLNDVA--GALALDDKLGRST---NQLSGGEWQRVRLAAVVLqitpqANPagQLL 155
Cdd:PRK09473 112 PY-MRVGEQLMevlmLHKGMSKAEAFEESVRmlDAVKMPEARKRMKmypHEFSGGMRQRVMIAMALL-----CRP--KLL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 156 LLDEPMNSLDVAQQSALDKILSALCQQ-GLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPPNLAQAYGM-- 232
Cdd:PRK09473 184 IADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPYSIGLln 263
|
250
....*....|....*..
gi 1432492527 233 NFRRLDIEGHRMLisTI 249
Cdd:PRK09473 264 AVPRLDAEGESLL--TI 278
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
12-179 |
1.40e-07 |
|
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: 50.34 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 12 ESTRLGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGMTSGK----GSIQFAG-QPLEAwsATKLALHRAYLSQQQtppf 86
Cdd:cd03233 19 KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsveGDIHYNGiPYKEF--AEKYPGEIIYVSEED---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 87 ampvwhyltLHQHDKTRTELLNdvagaLALDDKLGRSTNQLSGGEWQRVRLAAVVLqitpqANPAgqLLLLDEPMNSLDV 166
Cdd:cd03233 93 ---------VHFPTLTVRETLD-----FALRCKGNEFVRGISGGERKRVSIAEALV-----SRAS--VLCWDNSTRGLDS 151
|
170
....*....|...
gi 1432492527 167 AqqSALDkILSAL 179
Cdd:cd03233 152 S--TALE-ILKCI 161
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
120-227 |
1.83e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 51.75 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 120 LGRSTNQLSGGEWQRVRLAAVVLqiTPQANPAgqLLLLDEPMNSLDVAQQSALDKILSALCQQGLAIVMSSHDLnHTLRH 199
Cdd:PRK00635 803 LGRPLSSLSGGEIQRLKLAYELL--APSKKPT--LYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNM-HVVKV 877
|
90 100 110
....*....|....*....|....*....|....*..
gi 1432492527 200 AHRAWLL------KGGKMLASGRREEVL---TPPNLA 227
Cdd:PRK00635 878 ADYVLELgpeggnLGGYLLASCSPEELIhlhTPTAKA 914
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
23-208 |
1.96e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 50.16 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 23 VRAGEILHLVGPNGAGKSTLLARMAGMTSG-KGSIQFAGQPLEAWSATKLALHRAY-----------------LSQQQTP 84
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGsSGEVSLVGQPLHQMDEEARAKLRAKhvgfvfqsfmliptlnaLENVELP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 85 PfampvwhyLTLHQHDKTRTELLNDVAGALALDDKLGRSTNQLSGGEWQRVRLAAVVlqitpqaNPAGQLLLLDEPMNSL 164
Cdd:PRK10584 113 A--------LLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAF-------NGRPDVLFADEPTGNL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1432492527 165 DVAQQSALDKILSALCQ-QGLAIVMSSHDLNHTLRHAHRAWLLKG 208
Cdd:PRK10584 178 DRQTGDKIADLLFSLNReHGTTLILVTHDLQLAARCDRRLRLVNG 222
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
118-233 |
1.99e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 50.79 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 118 DKLGRSTNQLSGGEWQRVRLAAvVLQITPqanpagQLLLLDEPMNSLDVAQQSALDKILSALCQ-QGLAIVMSSHDLNHT 196
Cdd:PRK13634 137 ELLARSPFELSGGQMRRVAIAG-VLAMEP------EVLVLDEPTAGLDPKGRKEMMEMFYKLHKeKGLTTVLVTHSMEDA 209
|
90 100 110
....*....|....*....|....*....|....*..
gi 1432492527 197 LRHAHRAWLLKGGKMLASGRREEVLTPPNLAQAYGMN 233
Cdd:PRK13634 210 ARYADQIVVMHKGTVFLQGTPREIFADPDELEAIGLD 246
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
12-225 |
2.32e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 50.60 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 12 ESTRLGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGM-TSGKGSIQFAGQPLEAWSATKlALHRayLSQQQTPPFAMP- 89
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALlKPSSGTITIAGYHITPETGNK-NLKK--LRKKVSLVFQFPe 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 90 --VWHYLTLH-----------QHDKTRTELLNDVAGALALDDKLGRSTNQLSGGEWQRVRLAAVvLQITPQanpagqLLL 156
Cdd:PRK13641 96 aqLFENTVLKdvefgpknfgfSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGV-MAYEPE------ILC 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1432492527 157 LDEPMNSLDVAQQSALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPPN 225
Cdd:PRK13641 169 LDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-220 |
2.33e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 51.17 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 3 IVMQLQDVAESTRLGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGMTSGK-GSIQFAGQPLEAWSATKlALHR--AYLS 79
Cdd:COG1129 255 VVLEVEGLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADsGEIRLDGKPVRIRSPRD-AIRAgiAYVP 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 80 ---QQQ--TPPfaMPVWHYLTL-HQHDKTRTELLNDVA-GALALD--DKLG---RSTNQ----LSGGEWQRVRLAAVVLq 143
Cdd:COG1129 334 edrKGEglVLD--LSIRENITLaSLDRLSRGGLLDRRReRALAEEyiKRLRiktPSPEQpvgnLSGGNQQKVVLAKWLA- 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1432492527 144 itpqANPagQLLLLDEPMNSLDVAQQSALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEV 220
Cdd:COG1129 411 ----TDP--KVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGELDREEA 481
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
23-192 |
2.73e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.10 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 23 VRAGEILHLVGPNGAGKSTLLARMAG---MTSGKgsIQFAgqpleawsaTKLALHRAylsqQQTPPFAMP---------- 89
Cdd:PRK11147 26 IEDNERVCLVGRNGAGKSTLMKILNGevlLDDGR--IIYE---------QDLIVARL----QQDPPRNVEgtvydfvaeg 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 90 -------------VWHYLTLHQHDKTRTEL------------------LNDVAGALALD-DKlgrSTNQLSGGeWQR-VR 136
Cdd:PRK11147 91 ieeqaeylkryhdISHLVETDPSEKNLNELaklqeqldhhnlwqlenrINEVLAQLGLDpDA---ALSSLSGG-WLRkAA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1432492527 137 LA-AVVlqitpqANPagQLLLLDEPMNSLDVAQQSALDKILSALcqQGlAIVMSSHD 192
Cdd:PRK11147 167 LGrALV------SNP--DVLLLDEPTNHLDIETIEWLEGFLKTF--QG-SIIFISHD 212
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
25-193 |
2.77e-07 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 50.48 E-value: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 25 AGEILHLVGPNGAGKSTLLARMAGM-TSGKGSIQFAGQPLEAWSATKLALHRAYLSQQQTPPFA-----MPVWHY----L 94
Cdd:PRK15079 46 EGETLGVVGESGCGKSTFARAIIGLvKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQDPLAslnprMTIGEIiaepL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 95 TLHQHDKTRTELLNDVAGALA----LDDKLGRSTNQLSGGEWQRVRLA-AVVLQitpqanPagQLLLLDEPMNSLDVAQQ 169
Cdd:PRK15079 126 RTYHPKLSRQEVKDRVKAMMLkvglLPNLINRYPHEFSGGQCQRIGIArALILE------P--KLIICDEPVSALDVSIQ 197
|
170 180
....*....|....*....|....*
gi 1432492527 170 SALDKILSALCQQ-GLAIVMSSHDL 193
Cdd:PRK15079 198 AQVVNLLQQLQREmGLSLIFIAHDL 222
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
16-193 |
4.18e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 49.96 E-value: 4.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 16 LGPLSGEVRAGEILHLVGPNGAGKSTLlARMAGM--TSGKGSIQFAGQPLEAWSATKLALHRaylsQQQTPPFAMPvwhY 93
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTL-ARLLTMieTPTGGELYYQGQDLLKADPEAQKLLR----QKIQIVFQNP---Y 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 94 LTLHQHDKTRTEL-----LND-------VAGALALDDKLG-------RSTNQLSGGEWQRVRLA-AVVLqitpqaNPagQ 153
Cdd:PRK11308 103 GSLNPRKKVGQILeepllINTslsaaerREKALAMMAKVGlrpehydRYPHMFSGGQRQRIAIArALML------DP--D 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1432492527 154 LLLLDEPMNSLDVAQQSALDKILSALCQQ-GLAIVMSSHDL 193
Cdd:PRK11308 175 VVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDL 215
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
9-191 |
4.92e-07 |
|
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: 48.78 E-value: 4.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 9 DVAESTR--LGPLSGEVRAGEILHLVGPNGAGKSTLLARMAG-MTSG--KGSIQFAGQPLEAwsatklALHR--AYLSQQ 81
Cdd:cd03232 14 PVKGGKRqlLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrKTAGviTGEILINGRPLDK------NFQRstGYVEQQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 82 QTppfampvwhyltlhqHDKTRTellndVAGALALDDKL-GRSTNqlsggewQRVRLA-AVVLqitpQANPagQLLLLDE 159
Cdd:cd03232 88 DV---------------HSPNLT-----VREALRFSALLrGLSVE-------QRKRLTiGVEL----AAKP--SILFLDE 134
|
170 180 190
....*....|....*....|....*....|....
gi 1432492527 160 PMNSLDvaQQSALD--KILSALCQQGLAIVMSSH 191
Cdd:cd03232 135 PTSGLD--SQAAYNivRFLKKLADSGQAILCTIH 166
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
117-220 |
4.93e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 49.36 E-value: 4.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 117 DDKLGRSTNQLSGGEWQRVRLAAVvLQITPQanpagqLLLLDEPMNSLDVAQQSALDKILSALCQQGLAIVMSSHDLNHT 196
Cdd:PRK13649 136 ESLFEKNPFELSGGQMRRVAIAGI-LAMEPK------ILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDV 208
|
90 100
....*....|....*....|....
gi 1432492527 197 LRHAHRAWLLKGGKMLASGRREEV 220
Cdd:PRK13649 209 ANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
13-186 |
5.23e-07 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 49.72 E-value: 5.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 13 STRLGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGM---TSGKgsIQFAGQpleawSATKLALhraylsQQQTppFAMp 89
Cdd:PRK11432 19 NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLekpTEGQ--IFIDGE-----DVTHRSI------QQRD--ICM- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 90 VWHYLTLHQH--------------DKTRTELLNDVAGALALDDKLG---RSTNQLSGGEWQRVRLA-AVVLQitPqanpa 151
Cdd:PRK11432 83 VFQSYALFPHmslgenvgyglkmlGVPKEERKQRVKEALELVDLAGfedRYVDQISGGQQQRVALArALILK--P----- 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 1432492527 152 gQLLLLDEPMNSLDV-AQQSALDKILSalCQQGLAI 186
Cdd:PRK11432 156 -KVLLFDEPLSNLDAnLRRSMREKIRE--LQQQFNI 188
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
22-191 |
8.10e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 48.42 E-value: 8.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLLARMAG-MTSGKGSIQFAGQPLEAWSATKLALHrayLSQQQTPPFAMpvwhyltlhqhd 100
Cdd:COG2401 52 EIEPGEIVLIVGASGSGKSTLLRLLAGaLKGTPVAGCVDVPDNQFGREASLIDA---IGRKGDFKDAV------------ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 101 ktrtELLNDVagalalddKLG------RSTNQLSGGEWQRVRLAAVVLQitpqanpAGQLLLLDEPMNSLDVAQQSALDK 174
Cdd:COG2401 117 ----ELLNAV--------GLSdavlwlRRFKELSTGQKFRFRLALLLAE-------RPKLLVIDEFCSHLDRQTAKRVAR 177
|
170
....*....|....*...
gi 1432492527 175 ILSALCQQ-GLAIVMSSH 191
Cdd:COG2401 178 NLQKLARRaGITLVVATH 195
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
117-228 |
1.02e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 48.85 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 117 DDKLGRSTNQLSGGEWQRVRLAAVVLQitpqanpAGQLLLLDEPMNSLDVAQQSALDKILSALCQ-QGLAIVMSSHDLNH 195
Cdd:PRK13645 141 EDYVKRSPFELSGGQKRRVALAGIIAM-------DGNTLVLDEPTGGLDPKGEEDFINLFERLNKeYKKRIIMVTHNMDQ 213
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1432492527 196 TLRHAHRAWLLKGGKMLASGRREEVLT-----------PPNLAQ 228
Cdd:PRK13645 214 VLRIADEVIVMHEGKVISIGSPFEIFSnqelltkieidPPKLYQ 257
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
15-141 |
1.11e-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: 49.03 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 15 RLGPLSGEVRAGEILHLVGPNGAGKSTLLARMAG-MTSGKGSIQFAGQPLEawsatklALHRAYLSQQQTPPFAMpvwHY 93
Cdd:COG4615 347 TLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGlYRPESGEILLDGQPVT-------ADNREAYRQLFSAVFSD---FH 416
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1432492527 94 L---TLHQHDKTRTELLNDVAGALALDDKL----GR-STNQLSGGewQRVRLAAVV 141
Cdd:COG4615 417 LfdrLLGLDGEADPARARELLERLELDHKVsvedGRfSTTDLSQG--QRKRLALLV 470
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
31-221 |
1.27e-06 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 48.95 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 31 LVGPNGAGKSTLLARMAGMTS-GKGSIQFAGQPLEAWSATKLALHRAYLsqQQTPP------FA----------MPVWHY 93
Cdd:PRK10790 372 LVGHTGSGKSTLASLLMGYYPlTEGEIRLDGRPLSSLSHSVLRQGVAMV--QQDPVvladtfLAnvtlgrdiseEQVWQA 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 94 LTLHQhdktrtelLNDVAGAL--ALDDKLGRSTNQLSGGEWQRVRLAAVVLQiTPqanpagQLLLLDEPMNSLDVAQQSA 171
Cdd:PRK10790 450 LETVQ--------LAELARSLpdGLYTPLGEQGNNLSVGQKQLLALARVLVQ-TP------QILILDEATANIDSGTEQA 514
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1432492527 172 LDKILSALCQQGLAIVMsSHDLNhTLRHAHRAWLLKGGKMLASGRREEVL 221
Cdd:PRK10790 515 IQQALAAVREHTTLVVI-AHRLS-TIVEADTILVLHRGQAVEQGTHQQLL 562
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
2-221 |
1.34e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 48.17 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 2 SIVMQLQDVAESTRLGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGM-TSGKGSIQFAGQPLEAWSATKLALHRAYLSQ 80
Cdd:PRK13642 9 NLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLfEEFEGKVKIDGELLTAENVWNLRRKIGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 81 QQTPPFAMPVWH---YLTLHQHDKTRTELLNDVAGAL----ALDDKLgRSTNQLSGGEWQRVRLAAVVlQITPqanpagQ 153
Cdd:PRK13642 89 NPDNQFVGATVEddvAFGMENQGIPREEMIKRVDEALlavnMLDFKT-REPARLSGGQKQRVAVAGII-ALRP------E 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1432492527 154 LLLLDEPMNSLDVAQQSALDKILSALCQQGLAIVMS-SHDLNHTLRhAHRAWLLKGGKMLASGRREEVL 221
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSiTHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
22-167 |
1.36e-06 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 48.49 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLLARMAGM---TSGKgsIQFAGQPLEAWSATK---------LALHrAYLSQQQTPPFAmp 89
Cdd:PRK11000 25 DIHEGEFVVFVGPSGCGKSTLLRMIAGLediTSGD--LFIGEKRMNDVPPAErgvgmvfqsYALY-PHLSVAENMSFG-- 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1432492527 90 vwhyLTLHQHDKT-RTELLNDVAGALALDDKLGRSTNQLSGGEWQRVRLAAvvlqiTPQANPagQLLLLDEPMNSLDVA 167
Cdd:PRK11000 100 ----LKLAGAKKEeINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGR-----TLVAEP--SVFLLDEPLSNLDAA 167
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
22-228 |
1.47e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.47 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLLARMAG---MTSGKGSIQFAgqpleawsatklalHRAYLSQQQTPPFAMPVWH-----Y 93
Cdd:PRK10938 25 TLNAGDSWAFVGANGSGKSALARALAGelpLLSGERQSQFS--------------HITRLSFEQLQKLVSDEWQrnntdM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 94 LTLHQHDKTRT------------ELLNDVAGALALDDKLGRSTNQLSGGEWQRVRLAAVVLqitpqANPagQLLLLDEPM 161
Cdd:PRK10938 91 LSPGEDDTGRTtaeiiqdevkdpARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALM-----SEP--DLLILDEPF 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1432492527 162 NSLDVAQQSALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPPNLAQ 228
Cdd:PRK10938 164 DGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQALVAQ 230
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
120-230 |
1.60e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 48.86 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 120 LGRSTNQLSGGEWQRVRLAAvvlQITPQAnpAGQLLLLDEPmnSLDVAQQ--SALDKILSALCQQGLAIVMSSHDlNHTL 197
Cdd:TIGR00630 482 LSRAAGTLSGGEAQRIRLAT---QIGSGL--TGVLYVLDEP--SIGLHQRdnRRLINTLKRLRDLGNTLIVVEHD-EDTI 553
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1432492527 198 RHAHraWLLK--------GGKMLASGRREEVLTPPN-LAQAY 230
Cdd:TIGR00630 554 RAAD--YVIDigpgagehGGEVVASGTPEEILANPDsLTGQY 593
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
25-234 |
1.62e-06 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 48.48 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 25 AGEILHLVGPNGAGKST---LLARMAGMTSGkgSIQFAGQPLEAWSATKLALHRAYLSQQqTPPFAMPVWHYLTLHQHDK 101
Cdd:PRK11176 368 AGKTVALVGRSGSGKSTianLLTRFYDIDEG--EILLDGHDLRDYTLASLRNQVALVSQN-VHLFNDTIANNIAYARTEQ 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 102 -TRTELLNDVAGALALD--DKL--------GRSTNQLSGGEWQRVRLAAVVLQITPqanpagqLLLLDEPMNSLDV---- 166
Cdd:PRK11176 445 ySREQIEEAARMAYAMDfiNKMdngldtviGENGVLLSGGQRQRIAIARALLRDSP-------ILILDEATSALDTeser 517
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1432492527 167 AQQSALDKIlsalcQQGLAIVMSSHDLNhTLRHAHRAWLLKGGKMLASGRREEVLTPPNL-AQAYGMNF 234
Cdd:PRK11176 518 AIQAALDEL-----QKNRTSLVIAHRLS-TIEKADEILVVEDGEIVERGTHAELLAQNGVyAQLHKMQF 580
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
23-174 |
1.83e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 48.35 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 23 VRAGEILHLVGPNGAGKSTLLARMAG-MTSGKGSIQfagqpleaWSATKlalHRAYLSQQQTPPFA--MPVWHYLTLHQH 99
Cdd:PRK15064 342 LEAGERLAIIGENGVGKTTLLRTLVGeLEPDSGTVK--------WSENA---NIGYYAQDHAYDFEndLTLFDWMSQWRQ 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 100 DKTRTELLNDVAGALAL-DDKLGRSTNQLSGGEWQRVRLAAVVLQitpQANpagqLLLLDEPMNSLDV----AQQSALDK 174
Cdd:PRK15064 411 EGDDEQAVRGTLGRLLFsQDDIKKSVKVLSGGEKGRMLFGKLMMQ---KPN----VLVMDEPTNHMDMesieSLNMALEK 483
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
26-224 |
2.08e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 48.31 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 26 GEILHLVGPNGAGKSTL---LARMagMTSGKGSIQFAGQPLEAWSATKL-ALHR----------AYLSQQQTPPFAM--P 89
Cdd:PRK10261 350 GETLSLVGESGSGKSTTgraLLRL--VESQGGEIIFNGQRIDTLSPGKLqALRRdiqfifqdpyASLDPRQTVGDSImeP 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 90 VW-HYLTLHQHDKTRTELLNDVAGALAldDKLGRSTNQLSGGEWQRVRLA-AVVLqitpqaNPagQLLLLDEPMNSLDVA 167
Cdd:PRK10261 428 LRvHGLLPGKAAAARVAWLLERVGLLP--EHAWRYPHEFSGGQRQRICIArALAL------NP--KVIIADEAVSALDVS 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1432492527 168 QQSALDKILSALCQQ-GLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPP 224
Cdd:PRK10261 498 IRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
19-192 |
2.09e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.19 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKSTLLARMAGM-TSGKGSIQFaGQpleawsATKLAL---HRAYLSQQQTppfampVWH-- 92
Cdd:PRK11819 343 LSFSLPPGGIVGIIGPNGAGKSTLFKMITGQeQPDSGTIKI-GE------TVKLAYvdqSRDALDPNKT------VWEei 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 93 -----YLTLHQHDktrtelLNDVA--------GAlaldD---KLGrstnQLSGGEWQRVRLAAVVLQitpqanpAGQLLL 156
Cdd:PRK11819 410 sggldIIKVGNRE------IPSRAyvgrfnfkGG----DqqkKVG----VLSGGERNRLHLAKTLKQ-------GGNVLL 468
|
170 180 190
....*....|....*....|....*....|....*.
gi 1432492527 157 LDEPMNSLDVAQQSALDKILSALcqQGLAIVMsSHD 192
Cdd:PRK11819 469 LDEPTNDLDVETLRALEEALLEF--PGCAVVI-SHD 501
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
14-202 |
2.34e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 48.10 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 14 TRLGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGM-TSGKGSIQFAGQPLEAWSATKLALHR-AYLsqqqtP------- 84
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLrPPASGSIRLDGEDITGLSPRERRRLGvAYI-----Pedrlgrg 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 85 --PfAMPVWHYLTLHQHDK---TRTELLN-DVAGALALD-----DKLGRSTNQ----LSGGEWQRVRLAAVVLQitpqaN 149
Cdd:COG3845 347 lvP-DMSVAENLILGRYRRppfSRGGFLDrKAIRAFAEElieefDVRTPGPDTparsLSGGNQQKVILARELSR-----D 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1432492527 150 PagQLLLLDEPMNSLDVAQQSALDKILSALCQQGLAIVMSSHDLNHTLRHAHR 202
Cdd:COG3845 421 P--KLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDR 471
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
23-236 |
2.39e-06 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 47.72 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 23 VRAGEILHLVGPNGAGKST---LLARMAGMTsgKGSIQFAGQPLEAWSATKLALHRAYLSQQQTPPFA-MPvwHYLTLHQ 98
Cdd:PRK10070 51 IEEGEIFVIMGLSGSGKSTmvrLLNRLIEPT--RGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFAlMP--HMTVLDN 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 99 HD----------KTRTELLNDVAGALALDDKLGRSTNQLSGGEWQRVRLAAVvLQITPQanpagqLLLLDEPMNSLDVAQ 168
Cdd:PRK10070 127 TAfgmelaginaEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARA-LAINPD------ILLMDEAFSALDPLI 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1432492527 169 QSAL-DKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPPnlAQAYGMNFRR 236
Cdd:PRK10070 200 RTEMqDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNP--ANDYVRTFFR 266
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
22-198 |
2.59e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 47.47 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLLA---RMAGMTSG---KGSIQFAGQPLEAWSATKLALHRAYLSQQQTP-PFAMPVWHYL 94
Cdd:PRK14243 32 DIPKNQITAFIGPSGCGKSTILRcfnRLNDLIPGfrvEGKVTFHGKNLYAPDVDPVEVRRRIGMVFQKPnPFPKSIYDNI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 95 T----LHQHDKTRTELLNDVAGALAL----DDKLGRSTNQLSGGEWQRVRLAAvVLQITPqanpagQLLLLDEPMNSLDV 166
Cdd:PRK14243 112 AygarINGYKGDMDELVERSLRQAALwdevKDKLKQSGLSLSGGQQQRLCIAR-AIAVQP------EVILMDEPCSALDP 184
|
170 180 190
....*....|....*....|....*....|..
gi 1432492527 167 AQQSALDKILSALCQQgLAIVMSSHDLNHTLR 198
Cdd:PRK14243 185 ISTLRIEELMHELKEQ-YTIIIVTHNMQQAAR 215
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
26-224 |
2.66e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 47.49 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 26 GEILHLVGPNGAGKSTLLARMAGMTSGKGSI-----QFAGQPLEAWSAT---KLALHRAYLSQQQTPPF----------- 86
Cdd:PRK15093 33 GEIRGLVGESGSGKSLIAKAICGVTKDNWRVtadrmRFDDIDLLRLSPRerrKLVGHNVSMIFQEPQSCldpservgrql 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 87 --AMPVWHY-----LTLHQHDKTRTELLNDVaGALALDDKLGRSTNQLSGGEWQRVrLAAVVLQITPQanpagqLLLLDE 159
Cdd:PRK15093 113 mqNIPGWTYkgrwwQRFGWRKRRAIELLHRV-GIKDHKDAMRSFPYELTEGECQKV-MIAIALANQPR------LLIADE 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1432492527 160 PMNSLDVAQQSALDKILSALCQ-QGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPP 224
Cdd:PRK15093 185 PTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTP 250
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
21-193 |
2.94e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 46.41 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 21 GEVRAGEILHLVGPNGAGKSTLLARMAGmtsgkgSIQFAGQPLEaWSATKLALHRAYLSqqqtppfampvwhyltlhqhd 100
Cdd:cd03222 20 GVVKEGEVIGIVGPNGTGKTTAVKILAG------QLIPNGDNDE-WDGITPVYKPQYID--------------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 101 ktrtellndvagalalddklgrstnqLSGGEWQRVRLAAVVLQitpqanpAGQLLLLDEPMNSLDVAQQSALDKILSALC 180
Cdd:cd03222 72 --------------------------LSGGELQRVAIAAALLR-------NATFYLFDEPSAYLDIEQRLNAARAIRRLS 118
|
170
....*....|....
gi 1432492527 181 QQGLAIVM-SSHDL 193
Cdd:cd03222 119 EEGKKTALvVEHDL 132
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-226 |
3.06e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 47.00 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKSTLLARMAG-MTSGKGSIQFAGQPLEAWSATK--------------------------- 70
Cdd:COG1101 25 LNLTIEEGDFVTVIGSNGAGKSTLLNAIAGsLPPDSGSILIDGKDVTKLPEYKrakyigrvfqdpmmgtapsmtieenla 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 71 LALHRAylsqqQTPPFAMPVwhylTLHQHD--KTRTELLNdvagaLALDDKLGRSTNQLSGGEWQRVRLAAVVLQitpqa 148
Cdd:COG1101 105 LAYRRG-----KRRGLRRGL----TKKRRElfRELLATLG-----LGLENRLDTKVGLLSGGQRQALSLLMATLT----- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 149 NPagQLLLLDEPMNSLDvaQQSAlDKILSALCQ----QGLAIVMSSHDLNHTLRHAHRAWLLKGGKML--ASGRREEVLT 222
Cdd:COG1101 166 KP--KLLLLDEHTAALD--PKTA-ALVLELTEKiveeNNLTTLMVTHNMEQALDYGNRLIMMHEGRIIldVSGEEKKKLT 240
|
....
gi 1432492527 223 PPNL 226
Cdd:COG1101 241 VEDL 244
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
16-224 |
3.14e-06 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 46.89 E-value: 3.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 16 LGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGMTS-GKGSIQFAGQ----------PLEAWSATKLALHRAYLsqqqTP 84
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKpSEGSIVVNGQtinlvrdkdgQLKVADKNQLRLLRTRL----TM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 85 PFA-MPVWHYLTL---------------HQHDKTRTELLNDVAGalaLDDKL-GRSTNQLSGGEWQRVRLAAVvLQITPQ 147
Cdd:PRK10619 97 VFQhFNLWSHMTVlenvmeapiqvlglsKQEARERAVKYLAKVG---IDERAqGKYPVHLSGGQQQRVSIARA-LAMEPE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1432492527 148 anpagqLLLLDEPMNSLDVAQQSALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPP 224
Cdd:PRK10619 173 ------VLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNP 243
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
22-224 |
3.24e-06 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 47.05 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 22 EVRAGEILHLVGPNGAGKSTLLARMAGM---TSGK---GSIQF-AGQPLEAwsatKLALHRAyLSQQqtppfAMPVWHYL 94
Cdd:PRK11264 25 EVKPGEVVAIIGPSGSGKTTLLRCINLLeqpEAGTirvGDITIdTARSLSQ----QKGLIRQ-LRQH-----VGFVFQNF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 95 TLHQHdktRTELLNDVAG-----------ALALDDKL-------GRST---NQLSGGEWQRVRLAAvVLQITPqanpagQ 153
Cdd:PRK11264 95 NLFPH---RTVLENIIEGpvivkgepkeeATARARELlakvglaGKETsypRRLSGGQQQRVAIAR-ALAMRP------E 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1432492527 154 LLLLDEPMNSLDVAQQSALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPP 224
Cdd:PRK11264 165 VILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADP 235
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
16-224 |
3.38e-06 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 47.10 E-value: 3.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 16 LGPLSGEVRAGEILHLVGPNGAGKSTLLaRMAGM----TSGKgsIQFAGQPLEAWSATKLALHRA---------YLSQQQ 82
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLI-RCINLlerpTSGR--VLVDGQDLTALSEKELRKARRqigmifqhfNLLSSR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 83 TpPF---AMPvwhyLTL-----HQHDKTRTELLNDVagalALDDKLGRSTNQLSGGEWQRVRLAavvlqitpQA---NPa 151
Cdd:PRK11153 98 T-VFdnvALP----LELagtpkAEIKARVTELLELV----GLSDKADRYPAQLSGGQKQRVAIA--------RAlasNP- 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1432492527 152 gQLLLLDEPMNSLDVA-QQSALD---KILSALcqqGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPP 224
Cdd:PRK11153 160 -KVLLCDEATSALDPAtTRSILEllkDINREL---GLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHP 232
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
27-234 |
3.39e-06 |
|
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: 47.70 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 27 EILHLVGPNGAGKSTLLARMAG-MTSGKGSIQFAGQPLEawsaTKLALHRAYLSQqqtPPFAMPVWHYLTLHQH------ 99
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGlLPPTSGTVLVGGKDIE----TNLDAVRQSLGM---CPQHNILFHHLTVAEHilfyaq 1029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 100 ------DKTRTE---LLNDVagalALDDKLGRSTNQLSGGEWQRVRLAAVVLQitpqanpAGQLLLLDEPMNSLD-VAQQ 169
Cdd:TIGR01257 1030 lkgrswEEAQLEmeaMLEDT----GLHHKRNEEAQDLSGGMQRKLSVAIAFVG-------DAKVVVLDEPTSGVDpYSRR 1098
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1432492527 170 SALDKILSAlcQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGrreevlTPPNLAQAYGMNF 234
Cdd:TIGR01257 1099 SIWDLLLKY--RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG------TPLFLKNCFGTGF 1155
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
119-215 |
4.01e-06 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 46.84 E-value: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 119 KLGRSTNQLSGGEWQRVRLAAVVLQITPqanpaGQ-LLLLDEPMNSLDVAQQSALDKILSALCQQGLAIVMSSHDLnHTL 197
Cdd:cd03271 162 KLGQPATTLSGGEAQRIKLAKELSKRST-----GKtLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNL-DVI 235
|
90 100
....*....|....*....|....*.
gi 1432492527 198 RHAHraWLL--------KGGKMLASG 215
Cdd:cd03271 236 KCAD--WIIdlgpeggdGGGQVVASG 259
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
31-165 |
5.11e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.04 E-value: 5.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 31 LVGPNGAGKSTLLARMAGMTSgkgsiQFAGqplEAWSATKLALhrAYLSQQqtPP------------------------- 85
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDK-----EFEG---EARPAPGIKV--GYLPQE--PQldpektvrenveegvaevkaaldrf 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 86 ------FAMPVWHYltlhqhDKT---RTELLN--DVAGALALDDKLGRS------------TNQLSGGEWQRVRLAAVVL 142
Cdd:PRK11819 106 neiyaaYAEPDADF------DALaaeQGELQEiiDAADAWDLDSQLEIAmdalrcppwdakVTKLSGGERRRVALCRLLL 179
|
170 180
....*....|....*....|...
gi 1432492527 143 QitpqaNPagQLLLLDEPMNSLD 165
Cdd:PRK11819 180 E-----KP--DMLLLDEPTNHLD 195
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-224 |
7.03e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 46.77 E-value: 7.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKS-TLLARMAGMTSGKGSIQFAGQPLEAWSATKLALHRAYLSQQQ--------------- 82
Cdd:PRK10261 35 LSFSLQRGETLAIVGESGSGKSvTALALMRLLEQAGGLVQCDKMLLRRRSRQVIELSEQSAAQMRhvrgadmamifqepm 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 83 ---TPPFAM--PVWHYLTLHQhDKTRTELLNDVAGALAL------DDKLGRSTNQLSGGEWQRVRLAAVVlqitpQANPA 151
Cdd:PRK10261 115 tslNPVFTVgeQIAESIRLHQ-GASREEAMVEAKRMLDQvripeaQTILSRYPHQLSGGMRQRVMIAMAL-----SCRPA 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1432492527 152 gqLLLLDEPMNSLDVAQQSALDKILSALCQQ-GLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPP 224
Cdd:PRK10261 189 --VLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAP 260
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-192 |
7.54e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.48 E-value: 7.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 3 IVMQLQDV----AESTRLGPLSGEVRAGEILHLVGPNGAGKSTLLARMAG-MTSGKGSIQfagqpleawSATKLALhrAY 77
Cdd:PRK11147 318 IVFEMENVnyqiDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGqLQADSGRIH---------CGTKLEV--AY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 78 LSQqqtppfampvwhYLTLHQHDKTRTELLND------VAG----ALA-LDD-----KLGRS-TNQLSGGEWQRVRLAAV 140
Cdd:PRK11147 387 FDQ------------HRAELDPEKTVMDNLAEgkqevmVNGrprhVLGyLQDflfhpKRAMTpVKALSGGERNRLLLARL 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1432492527 141 VLQitpqanPAgQLLLLDEPMNSLDVAQQSALDKILSALcqQG-LAIVmsSHD 192
Cdd:PRK11147 455 FLK------PS-NLLILDEPTNDLDVETLELLEELLDSY--QGtVLLV--SHD 496
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
29-192 |
8.48e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.39 E-value: 8.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 29 LHLVGPNGAGKSTLLARMAGMTsgkgsiqfagQPLEAWSATKLALHRAYLSQQQ--------TPPFAMPVWHYLTLHQhd 100
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGEL----------QPSSGTVFRSAKVRMAVFSQHHvdgldlssNPLLYMMRCFPGVPEQ-- 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 101 KTRTELLN-DVAGALALddklgRSTNQLSGGEWQRVRLAAVVLQitpqaNPagQLLLLDEPMNSLDVAQQSALDKILsAL 179
Cdd:PLN03073 606 KLRAHLGSfGVTGNLAL-----QPMYTLSGGQKSRVAFAKITFK-----KP--HILLLDEPSNHLDLDAVEALIQGL-VL 672
|
170
....*....|...
gi 1432492527 180 CQQGlaIVMSSHD 192
Cdd:PLN03073 673 FQGG--VLMVSHD 683
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
28-224 |
1.05e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 45.60 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 28 ILHLVGPNGAGKSTLLA---RMAGMTSG---KGSIQFAGQPLEAWSATKLALHRAYLSQQQTP-PFA-MPVWHY----LT 95
Cdd:PRK14267 32 VFALMGPSGCGKSTLLRtfnRLLELNEEarvEGEVRLFGRNIYSPDVDPIEVRREVGMVFQYPnPFPhLTIYDNvaigVK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 96 LHQHDKTRTELLNDVAGALA-------LDDKLGRSTNQLSGGEWQRVRLAAvVLQITPqanpagQLLLLDEPMNSLDVAQ 168
Cdd:PRK14267 112 LNGLVKSKKELDERVEWALKkaalwdeVKDRLNDYPSNLSGGQRQRLVIAR-ALAMKP------KILLMDEPTANIDPVG 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1432492527 169 QSALDKILSALcQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPP 224
Cdd:PRK14267 185 TAKIEELLFEL-KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENP 239
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-193 |
1.24e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 45.76 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 1 MSIVMQLQDVAES-TRLGPLSG---EVRAGEILHLVGPNGAGKSTLLARMAGM-TSGKGSIQFAGQ------PLEAWSAT 69
Cdd:PRK10762 1 MQALLQLKGIDKAfPGVKALSGaalNVYPGRVMALVGENGAGKSTMMKVLTGIyTRDAGSILYLGKevtfngPKSSQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 70 KLALHRA-------------YLSQQQTPPFAMPVWhyltlhqhDKTRTEllndvagALALDDKLG------RSTNQLSGG 130
Cdd:PRK10762 81 IGIIHQElnlipqltiaeniFLGREFVNRFGRIDW--------KKMYAE-------ADKLLARLNlrfssdKLVGELSIG 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1432492527 131 EWQRVRLAAVVlqitpqaNPAGQLLLLDEPMNSLDVAQQSALDKILSALCQQGLAIVMSSHDL 193
Cdd:PRK10762 146 EQQMVEIAKVL-------SFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRL 201
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
16-211 |
1.37e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 45.73 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 16 LGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGM-TSGKGSIQFAGQPLeawSATKLALHRAYLSQQQTppfamPVW--H 92
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLyQPQSGEILLDGKPV---TAEQPEDYRKLFSAVFT-----DFHlfD 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 93 YLTLHQHDKTRTELLNDVAGALALDDKL----GRSTN-QLSGGewQRVRLaAVVLQITPQANpagqLLLLDEPMNSLD-V 166
Cdd:PRK10522 411 QLLGPEGKPANPALVEKWLERLKMAHKLeledGRISNlKLSKG--QKKRL-ALLLALAEERD----ILLLDEWAADQDpH 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1432492527 167 AQQSALDKILSALCQQGLAIVMSSHDlNHTLRHAHRAWLLKGGKM 211
Cdd:PRK10522 484 FRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
4-64 |
2.28e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.78 E-value: 2.28e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1432492527 4 VMQLQDVaestrlgplSGEVRAGEILHLVGPNGAGKSTLLARMAGM---TSGKGSIQFAGQPLE 64
Cdd:NF040905 14 VKALDDV---------NLSVREGEIHALCGENGAGKSTLMKVLSGVyphGSYEGEILFDGEVCR 68
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
120-227 |
2.95e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.82 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 120 LGRSTNQLSGGEWQRVRLAAVvLQITPQaNPAgqLLLLDEPMNSLDVAQQSALDKILSALCQQGLAIVMSSHDLnHTLRH 199
Cdd:PRK00635 1693 LGQNLSSLSLSEKIAIKIAKF-LYLPPK-HPT--LFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDP-ALLKQ 1767
|
90 100 110
....*....|....*....|....*....|....
gi 1432492527 200 AH------RAWLLKGGKMLASGRreevltPPNLA 227
Cdd:PRK00635 1768 ADyliemgPGSGKTGGKILFSGP------PKDIS 1795
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
26-224 |
3.06e-05 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 44.70 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 26 GEILHLVGPNGAGKSTLLA---RMAGMTSGKgsIQFAGQPLeawsaTKLALH--RAYLS-QQQTP-PFAMPVWHYLTLHQ 98
Cdd:PRK10789 341 GQMLGICGPTGSGKSTLLSliqRHFDVSEGD--IRFHDIPL-----TKLQLDswRSRLAvVSQTPfLFSDTVANNIALGR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 99 HDKTRTELLNDVAGALALDDKL----------GRSTNQLSGGEWQRVRLAAVVLQITpqanpagQLLLLDEPMNSLDVAQ 168
Cdd:PRK10789 414 PDATQQEIEHVARLASVHDDILrlpqgydtevGERGVMLSGGQKQRISIARALLLNA-------EILILDDALSAVDGRT 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1432492527 169 QSaldKILSALCQ--QGLAIVMSSHDLNhTLRHAHRAWLLKGGKMLASGRREEVLTPP 224
Cdd:PRK10789 487 EH---QILHNLRQwgEGRTVIISAHRLS-ALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
10-63 |
3.12e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 44.01 E-value: 3.12e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1432492527 10 VAESTRLGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGMTSGK---GSIQFAGQPL 63
Cdd:PRK09580 11 VEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvtgGTVEFKGKDL 67
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
18-165 |
3.52e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 44.06 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 18 PLSGEVRAGEILHLVGPNGAGKSTLLaRM-AGM---TSGKGSIqfAGQP---LEawsatklalhraylsqqqtpP----F 86
Cdd:PRK11650 22 GIDLDVADGEFIVLVGPSGCGKSTLL-RMvAGLeriTSGEIWI--GGRVvneLE--------------------PadrdI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 87 AMpVWHYLTLHQH----------------DK-TRTELLNDVAGALALDDKLGRSTNQLSGGEWQRVRLA-AVVLQitpqa 148
Cdd:PRK11650 79 AM-VFQNYALYPHmsvrenmayglkirgmPKaEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGrAIVRE----- 152
|
170
....*....|....*..
gi 1432492527 149 nPAgqLLLLDEPMNSLD 165
Cdd:PRK11650 153 -PA--VFLFDEPLSNLD 166
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
19-175 |
4.44e-05 |
|
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: 44.04 E-value: 4.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKST---LLARMAGMTSgkGSIQFAGQPLEAwsATKLALHRAY-LSQQQTPPFAMPVWHYL 94
Cdd:COG5265 377 VSFEVPAGKTVAIVGPSGAGKSTlarLLFRFYDVTS--GRILIDGQDIRD--VTQASLRAAIgIVPQDTVLFNDTIAYNI 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 95 TLHQHDKTRTElLNDVAGALALDD---KL--GRSTN------QLSGGEWQRVRLAAVVLqitpqANPAgqLLLLDEPMNS 163
Cdd:COG5265 453 AYGRPDASEEE-VEAAARAAQIHDfieSLpdGYDTRvgerglKLSGGEKQRVAIARTLL-----KNPP--ILIFDEATSA 524
|
170
....*....|....*.
gi 1432492527 164 LDV----AQQSALDKI 175
Cdd:COG5265 525 LDSrterAIQAALREV 540
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
23-214 |
1.10e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.79 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 23 VRAGEILHLVGPNGAGKSTLLARMAGMTS-GKGSIQFAGQPLEaWSATKLALHRAY--------LSQQQTPPFAMPVWHY 93
Cdd:PRK10982 21 VRPHSIHALMGENGAGKSTLLKCLFGIYQkDSGSILFQGKEID-FKSSKEALENGIsmvhqelnLVLQRSVMDNMWLGRY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 94 LT---LHQHDKtrteLLNDVAgalALDDKLGRSTN------QLSGGEWQRVRLAAVVlqitpqaNPAGQLLLLDEPMNSL 164
Cdd:PRK10982 100 PTkgmFVDQDK----MYRDTK---AIFDELDIDIDprakvaTLSVSQMQMIEIAKAF-------SYNAKIVIMDEPTSSL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1432492527 165 DVAQQSALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLAS 214
Cdd:PRK10982 166 TEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIAT 215
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
119-220 |
1.27e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 42.75 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 119 KLGRSTNQLSGGEWQRVRLAAVVlqitpQANPAGQ-LLLLDEPMNSL---DVAQqsaLDKILSALCQQGLAIVMSSHDLN 194
Cdd:PRK00349 823 KLGQPATTLSGGEAQRVKLAKEL-----SKRSTGKtLYILDEPTTGLhfeDIRK---LLEVLHRLVDKGNTVVVIEHNLD 894
|
90 100 110
....*....|....*....|....*....|....
gi 1432492527 195 hTLRHAHraWLL--------KGGKMLASGRREEV 220
Cdd:PRK00349 895 -VIKTAD--WIIdlgpeggdGGGEIVATGTPEEV 925
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
20-192 |
1.41e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.85 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 20 SGEVRAGEILHLVGPNGAGKSTLLARMAG-MTSGKGSIQFAGQPLEAWsatklalhraylSQQQTPPFAMPVWHYLT--- 95
Cdd:PRK10636 21 TATINPGQKVGLVGKNGCGKSTLLALLKNeISADGGSYTFPGNWQLAW------------VNQETPALPQPALEYVIdgd 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 96 ----------LHQHDKTRTELLNDVAGAL-------------ALDDKLGRSTNQL-------SGGEWQRVRLAAVVLqit 145
Cdd:PRK10636 89 reyrqleaqlHDANERNDGHAIATIHGKLdaidawtirsraaSLLHGLGFSNEQLerpvsdfSGGWRMRLNLAQALI--- 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1432492527 146 pqanPAGQLLLLDEPMNSLDVAQQSALDKILSALcqQGLAIVMsSHD 192
Cdd:PRK10636 166 ----CRSDLLLLDEPTNHLDLDAVIWLEKWLKSY--QGTLILI-SHD 205
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
26-200 |
1.85e-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: 40.82 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 26 GEILHLVGPNGAGKSTLLARMAGMTSGKGSIQFagqpleawsatklalhraYLSqqqtppfampvwhyltlhqhdktrTE 105
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVI------------------YID------------------------GE 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 106 LLNDVAGALALDDKLGRSTNQLSGGEWQRVRLAAVvlqitpqANPAGQLLLLDEPMNSLDVAQQSALDKILSALC----- 180
Cdd:smart00382 40 DILEEVLDQLLLIIVGGKKASGSGELRLRLALALA-------RKLKPDVLILDEITSLLDAEQEALLLLLEELRLllllk 112
|
170 180
....*....|....*....|.
gi 1432492527 181 -QQGLAIVMSSHDLNHTLRHA 200
Cdd:smart00382 113 sEKNLTVILTTNDEKDLGPAL 133
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
31-192 |
2.06e-04 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 41.10 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 31 LVGPNGAGKSTLLARMA----GMTSGKGSI-----QFAGQPLEAWSATKLAL-HRAYLsqqqtppfampVWHYLTLHQHD 100
Cdd:cd03279 33 ICGPTGAGKSTILDAITyalyGKTPRYGRQenlrsVFAPGEDTAEVSFTFQLgGKKYR-----------VERSRGLDYDQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 101 KTRTELL--NDvagalaLDDKLGRSTNQLSGGEWQRVRLAaVVLQITPQANPAG----QLLLLDEPMNSLDvaqQSALDK 174
Cdd:cd03279 102 FTRIVLLpqGE------FDRFLARPVSTLSGGETFLASLS-LALALSEVLQNRGgarlEALFIDEGFGTLD---PEALEA 171
|
170 180
....*....|....*....|.
gi 1432492527 175 ILSALCQQ---GLAIVMSSHD 192
Cdd:cd03279 172 VATALELIrteNRMVGVISHV 192
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
101-160 |
2.24e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.94 E-value: 2.24e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1432492527 101 KTRTELLNDVA-GALALDdklgRSTNQLSGGEWQRVRLAAvvlQI----TpqanpaGQLLLLDEP 160
Cdd:COG0178 463 RSRLGFLVDVGlDYLTLD----RSAGTLSGGEAQRIRLAT---QIgsglV------GVLYVLDEP 514
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-215 |
2.52e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 42.07 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKSTLLARMAGmtsgkgsiQFAGQPLEAWSATKLalhrAYLSQQQTPPFAMPVWHYLTLHQ 98
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLS--------QFEISEGRVWAERSI----AYVPQQAWIMNATVRGNILFFDE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 99 HDKTR-------TELLNDVAG-ALALDDKLGRSTNQLSGGEWQRVRLAAVVLqitpqANPagQLLLLDEPMNSLD--VAQ 168
Cdd:PTZ00243 747 EDAARladavrvSQLEADLAQlGGGLETEIGEKGVNLSGGQKARVSLARAVY-----ANR--DVYLLDDPLSALDahVGE 819
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1432492527 169 QSALDKILSALcqQGLAIVMSSHDLnHTLRHAHRAWLLKGGKMLASG 215
Cdd:PTZ00243 820 RVVEECFLGAL--AGKTRVLATHQV-HVVPRADYVVALGDGRVEFSG 863
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-193 |
3.06e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 41.69 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKSTLLARMAGMTSGK-GSIQFAGQPLEAWS---ATKLALhrAYLSQQQT-----PPFA-- 87
Cdd:PRK09700 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAgGEIRLNGKDISPRSpldAVKKGM--AYITESRRdngffPNFSia 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 88 --MPVWHYLTLHQ--------HDKTRTELLNDVAGALALD-DKLGRSTNQLSGGEWQRVRLAAVVLqitpqANPagQLLL 156
Cdd:PRK09700 360 qnMAISRSLKDGGykgamglfHEVDEQRTAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLC-----CCP--EVII 432
|
170 180 190
....*....|....*....|....*....|....*..
gi 1432492527 157 LDEPMNSLDVAQQSALDKILSALCQQGLAIVMSSHDL 193
Cdd:PRK09700 433 FDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSEL 469
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
101-160 |
3.16e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.60 E-value: 3.16e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1432492527 101 KTRTELLNDVA-GALALDdklgRSTNQLSGGEWQRVRLAAvvlQITpqANPAGQLLLLDEP 160
Cdd:PRK00349 467 RERLKFLVDVGlDYLTLS----RSAGTLSGGEAQRIRLAT---QIG--SGLTGVLYVLDEP 518
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
19-176 |
3.16e-04 |
|
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: 40.55 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKSTLLA---RMAGMTSgkGSIQFAGQPLeawsaTKLALHRayLSQQ-----QTP------ 84
Cdd:cd03244 23 ISFSIKPGEKVGIVGRTGSGKSSLLLalfRLVELSS--GSILIDGVDI-----SKIGLHD--LRSRisiipQDPvlfsgt 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 85 ------PFampvwhyltlHQH-DKTRTELLNDV-------AGALALDDKLGRSTNQLSGGEWQRVRLAAVVLQITPqanp 150
Cdd:cd03244 94 irsnldPF----------GEYsDEELWQALERVglkefveSLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSK---- 159
|
170 180
....*....|....*....|....*.
gi 1432492527 151 agqLLLLDEPMNSLDVAQQSALDKIL 176
Cdd:cd03244 160 ---ILVLDEATASVDPETDALIQKTI 182
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
26-209 |
4.57e-04 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 40.39 E-value: 4.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 26 GEILHLVGPNGAGKSTLLARMAG-MTSGKGSIQFAGQ-PLEAWSATKLALHR---AYLSQQqtpPFAM--PVWHYLTLHQ 98
Cdd:cd03290 27 GQLTMIVGQVGCGKSSLLLAILGeMQTLEGKVHWSNKnESEPSFEATRSRNRysvAYAAQK---PWLLnaTVEENITFGS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 99 -HDKTRTELLNDvAGALALD---------DKLGRSTNQLSGGEWQRVRLAAVVLQITpqanpagQLLLLDEPMNSLDVAQ 168
Cdd:cd03290 104 pFNKQRYKAVTD-ACSLQPDidllpfgdqTEIGERGINLSGGQRQRICVARALYQNT-------NIVFLDDPFSALDIHL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1432492527 169 QSAL--DKILSALCQQGLAIVMSSHDLNHtLRHAHRAWLLKGG 209
Cdd:cd03290 176 SDHLmqEGILKFLQDDKRTLVLVTHKLQY-LPHADWIIAMKDG 217
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
119-220 |
4.71e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.17 E-value: 4.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 119 KLGRSTNQLSGGEWQRVRLAAvVLQitpQANPAGQLLLLDEPMNSL---DVAQqsaLDKILSALCQQG---LAI-----V 187
Cdd:COG0178 819 KLGQPATTLSGGEAQRVKLAS-ELS---KRSTGKTLYILDEPTTGLhfhDIRK---LLEVLHRLVDKGntvVVIehnldV 891
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1432492527 188 MSSHDlnhtlrhahraWLL--------KGGKMLASGRREEV 220
Cdd:COG0178 892 IKTAD-----------WIIdlgpeggdGGGEIVAEGTPEEV 921
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-142 |
5.21e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 41.25 E-value: 5.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 16 LGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGMTSG-----KGSIQFAGQPLE----------AWSAtKLALHRAYLSQ 80
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGfhigvEGVITYDGITPEeikkhyrgdvVYNA-ETDVHFPHLTV 155
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1432492527 81 QQTPPFAM----PVWHYLTLHQhdKTRTELLNDVAGA-LALDDKlgRSTN-------QLSGGEWQRVRLAAVVL 142
Cdd:TIGR00956 156 GETLDFAArcktPQNRPDGVSR--EEYAKHIADVYMAtYGLSHT--RNTKvgndfvrGVSGGERKRVSIAEASL 225
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
19-48 |
6.09e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.77 E-value: 6.09e-04
10 20 30
....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKSTLLARMAG 48
Cdd:PRK10938 279 LSWQVNPGEHWQIVGPNGAGKSTLLSLITG 308
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
126-193 |
8.54e-04 |
|
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: 40.07 E-value: 8.54e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1432492527 126 QLSGGEWQRVRLAAVVLQitpqANPAGQLLLLDEPMNSLDVAQQSALDKILSALCQQGLAIVMSSHDL 193
Cdd:pfam13304 236 ELSDGTKRLLALLAALLS----ALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSP 299
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
18-224 |
8.70e-04 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 39.77 E-value: 8.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 18 PLSGEVRAGEILHLVGPNGAGKSTLLARMAGMTS-GKGSIQFAGQPLE----AWSATKLAL----------HRAYLSQQQ 82
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEpTSGELLIDDHPLHfgdySYRSQRIRMifqdpstslnPRQRISQIL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 83 TPPFAMPVwhYLTLHQHDKTRTELLNDVAgalALDDKLGRSTNQLSGGEWQRVRLA-AVVLQitpqanpaGQLLLLDEPM 161
Cdd:PRK15112 111 DFPLRLNT--DLEPEQREKQIIETLRQVG---LLPDHASYYPHMLAPGQKQRLGLArALILR--------PKVIIADEAL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1432492527 162 NSLDVAQQSALDKILSALCQ-QGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPP 224
Cdd:PRK15112 178 ASLDMSMRSQLINLMLELQEkQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASP 241
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
100-206 |
9.48e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.40 E-value: 9.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 100 DKTRTELLNDVAGAL--ALDDKLGRSTNQLSGGEWQRVRLAAVVLQitpqaNPagQLLLLDEPMNSLDVAQQSALDKILS 177
Cdd:PTZ00265 551 DVSKKVLIHDFVSALpdKYETLVGSNASKLSGGQKQRISIARAIIR-----NP--KILILDEATSSLDNKSEYLVQKTIN 623
|
90 100 110
....*....|....*....|....*....|
gi 1432492527 178 AL-CQQGLAIVMSSHDLNhTLRHAHRAWLL 206
Cdd:PTZ00265 624 NLkGNENRITIIIAHRLS-TIRYANTIFVL 652
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
18-219 |
1.10e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 39.89 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 18 PLSGEVRAGEILHLVGPNGAGKSTLLARMAGMTSGK-GSIQFAGQPLEAwSATKLALHRAYL------------------ 78
Cdd:PRK11288 271 PISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTaGQVYLDGKPIDI-RSPRDAIRAGIMlcpedrkaegiipvhsva 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 79 ------SQQQTPPFAMPVwhyltlhqHDKTRTELLNDVAGALALDDklgRSTNQ----LSGGEWQRVRLA---AVVLQIt 145
Cdd:PRK11288 350 dninisARRHHLRAGCLI--------NNRWEAENADRFIRSLNIKT---PSREQlimnLSGGNQQKAILGrwlSEDMKV- 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1432492527 146 pqanpagqlLLLDEPMNSLDVAQQSALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREE 219
Cdd:PRK11288 418 ---------ILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGELAREQ 482
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
23-61 |
1.11e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 39.24 E-value: 1.11e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1432492527 23 VRAGEILHLVGPNGAGKSTLLARMAGMTSGK---GSIQFAGQ 61
Cdd:CHL00131 30 INKGEIHAIMGPNGSGKSTLSKVIAGHPAYKileGDILFKGE 71
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
16-73 |
1.24e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 39.87 E-value: 1.24e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1432492527 16 LGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGMT-SGKGSIQFAGqpleawSATKLAL 73
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTmPNKGTVDIKG------SAALIAI 92
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
19-220 |
1.94e-03 |
|
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: 39.02 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 19 LSGEVRAGEILHLVGPNGAGKSTLLARMAGM-----TSGK-----------GSIQ---FAGQP------------LEAWS 67
Cdd:TIGR03269 19 ISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqyepTSGRiiyhvalcekcGYVErpsKVGEPcpvcggtlepeeVDFWN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 68 ATKlALHRAYLSQ-----QQTppFAmpvwhyltLHQHDKTRTELLNDV--AGALAlDDKLGRSTN--------------- 125
Cdd:TIGR03269 99 LSD-KLRRRIRKRiaimlQRT--FA--------LYGDDTVLDNVLEALeeIGYEG-KEAVGRAVDliemvqlshrithia 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 126 -QLSGGEWQRVRLAAvvlQITpqANPAgqLLLLDEPMNSLDvAQQSAL--DKILSALCQQGLAIVMSSHDLNHTLRHAHR 202
Cdd:TIGR03269 167 rDLSGGEKQRVVLAR---QLA--KEPF--LFLADEPTGTLD-PQTAKLvhNALEEAVKASGISMVLTSHWPEVIEDLSDK 238
|
250
....*....|....*...
gi 1432492527 203 AWLLKGGKMLASGRREEV 220
Cdd:TIGR03269 239 AIWLENGEIKEEGTPDEV 256
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-165 |
2.14e-03 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 39.12 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 16 LGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGMTSGKGSIQFAGQpleAWSATKLALHRAYLSQQQTPPFAMPVWHYLT 95
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQIDGV---SWNSVTLQTWRKAFGVIPQKVFIFSGTFRKN 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 96 LHQHDKTRTELLNDVAGALALD-------DKLGRSTNQ----LSGGEWQRVRLAAVVLQitpqanpAGQLLLLDEPMNSL 164
Cdd:TIGR01271 1312 LDPYEQWSDEEIWKVAEEVGLKsvieqfpDKLDFVLVDggyvLSNGHKQLMCLARSILS-------KAKILLLDEPSAHL 1384
|
.
gi 1432492527 165 D 165
Cdd:TIGR01271 1385 D 1385
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
5-111 |
9.81e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 37.13 E-value: 9.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432492527 5 MQLQDVAESTRLGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGMTSG----KGSIQFAGQPLEAWSATKLAlhrAYLSQ 80
Cdd:PLN03140 170 INLAKKTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPslkvSGEITYNGYRLNEFVPRKTS---AYISQ 246
|
90 100 110
....*....|....*....|....*....|....
gi 1432492527 81 QQTPPFAMPVWHYLTLH---QHDKTRTELLNDVA 111
Cdd:PLN03140 247 NDVHVGVMTVKETLDFSarcQGVGTRYDLLSELA 280
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1-62 |
9.81e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 37.13 E-value: 9.81e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1432492527 1 MSIVMQLQDVAEsTRLGPL---SGEVRAGEILHLVGPNGAGKSTLLARMAGMTSG---KGSIQFAGQP 62
Cdd:PLN03140 879 MPAEMKEQGVTE-DRLQLLrevTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGgyiEGDIRISGFP 945
|
|
| |
