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Conserved domains on  [gi|1997829365|ref|WP_206288543|]
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esterase FrsA [Escherichia coli]

Protein Classification

esterase FrsA( domain architecture ID 10792382)

esterase FrsA is an alpha/beta hydrolase family protein that displays esterase activity toward pNP-butyrate and may function as a fermentation/respiration switch protein

CATH:  3.40.50.1820
EC:  3.1.1.-
Gene Symbol:  frsA
Gene Ontology:  GO:0016787|GO:0005975
SCOP:  3000102

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
frsA PRK05077
esterase FrsA;
1-414 0e+00

esterase FrsA;


:

Pssm-ID: 235337  Cd Length: 414  Bit Score: 869.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997829365   1 MTQANLSETLFKPRFKHPETSTLVRRFNHGAQPPVQSALDGKTIPHWYRMINRLMWIWRGIDPREILDVQARIVMSDAER 80
Cdd:PRK05077    1 MTQANLSETLFKPRFKHPETSTLVRRFNHGSQPPIQSALDGKTVPHWYRMINRLMWIWRGIDPIEIEEVLARIAMSDAER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997829365  81 TDDDLYDTVIGYRGGNWIYEWATQAMVWQQKACAEDDPQLSGRHWLHAATLYNIAAYPHLKGDDLAEQAQALSNRAYEEA 160
Cdd:PRK05077   81 TDDELLDTVIGYRGGNWIYEWAKQAMEWQQKACAEEDPEEAGRHWLHAANLYSIAAYPHLKGDELAEQAQVLANRAYEEA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997829365 161 AQRLPGTMRQMEFTVPGGAPITGFLHMPKGDGPFPTVLMCGGLDAMQTDYYSLYERYFAPRGIAMLTIDMPSVGFSSKWK 240
Cdd:PRK05077  161 AKRLPGELKELEFPIPGGGPITGFLHLPKGDGPFPTVLVCGGLDSLQTDYYRLFRDYLAPRGIAMLTIDMPSVGFSSKWK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997829365 241 LTQDSSLLHQHVLKALPNVPWVDHTRVAAFGFRCGANVAVRLAYLESPRLKAVACLGPVVHTLLSDFKCQQQVPEMYLDV 320
Cdd:PRK05077  241 LTQDSSLLHQAVLNALPNVPWVDHTRVAAFGFRFGANVAVRLAYLEPPRLKAVACLGPVVHTLLTDPKRQQQVPEMYLDV 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997829365 321 LASRLGMHDASDEALRVELNRYSLKVQGLLGRRCPTPMLSGYWKNDPFSPEEDSRLITSSSADGKLLEIPFNPVYRNFDK 400
Cdd:PRK05077  321 LASRLGMHDASDEALRVELNRYSLKVQGLLGRRCPTPMLSGYWKNDPFSPEEDSRLIASSSADGKLLEIPFKPVYRNFDK 400
                         410
                  ....*....|....
gi 1997829365 401 GLQEITDWIEKRLC 414
Cdd:PRK05077  401 ALQEISDWLEDRLC 414
 
Name Accession Description Interval E-value
frsA PRK05077
esterase FrsA;
1-414 0e+00

esterase FrsA;


Pssm-ID: 235337  Cd Length: 414  Bit Score: 869.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997829365   1 MTQANLSETLFKPRFKHPETSTLVRRFNHGAQPPVQSALDGKTIPHWYRMINRLMWIWRGIDPREILDVQARIVMSDAER 80
Cdd:PRK05077    1 MTQANLSETLFKPRFKHPETSTLVRRFNHGSQPPIQSALDGKTVPHWYRMINRLMWIWRGIDPIEIEEVLARIAMSDAER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997829365  81 TDDDLYDTVIGYRGGNWIYEWATQAMVWQQKACAEDDPQLSGRHWLHAATLYNIAAYPHLKGDDLAEQAQALSNRAYEEA 160
Cdd:PRK05077   81 TDDELLDTVIGYRGGNWIYEWAKQAMEWQQKACAEEDPEEAGRHWLHAANLYSIAAYPHLKGDELAEQAQVLANRAYEEA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997829365 161 AQRLPGTMRQMEFTVPGGAPITGFLHMPKGDGPFPTVLMCGGLDAMQTDYYSLYERYFAPRGIAMLTIDMPSVGFSSKWK 240
Cdd:PRK05077  161 AKRLPGELKELEFPIPGGGPITGFLHLPKGDGPFPTVLVCGGLDSLQTDYYRLFRDYLAPRGIAMLTIDMPSVGFSSKWK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997829365 241 LTQDSSLLHQHVLKALPNVPWVDHTRVAAFGFRCGANVAVRLAYLESPRLKAVACLGPVVHTLLSDFKCQQQVPEMYLDV 320
Cdd:PRK05077  241 LTQDSSLLHQAVLNALPNVPWVDHTRVAAFGFRFGANVAVRLAYLEPPRLKAVACLGPVVHTLLTDPKRQQQVPEMYLDV 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997829365 321 LASRLGMHDASDEALRVELNRYSLKVQGLLGRRCPTPMLSGYWKNDPFSPEEDSRLITSSSADGKLLEIPFNPVYRNFDK 400
Cdd:PRK05077  321 LASRLGMHDASDEALRVELNRYSLKVQGLLGRRCPTPMLSGYWKNDPFSPEEDSRLIASSSADGKLLEIPFKPVYRNFDK 400
                         410
                  ....*....|....
gi 1997829365 401 GLQEITDWIEKRLC 414
Cdd:PRK05077  401 ALQEISDWLEDRLC 414
FrsA-like pfam06500
Esterase FrsA-like; The FrsA-like family includes FrsA, an esterase found to have the alpha ...
1-414 0e+00

Esterase FrsA-like; The FrsA-like family includes FrsA, an esterase found to have the alpha/beta-hydrolase fold. t also includes the hydrolytic polyketide shortening protein Ayg1 from fungi, 2,6-dihydropseudooxynicotine hydrolase from Paenarthrobacter nicotinovorans and Fus2 from Gibberella species. The enzyme 2,6-dihydroxy-pseudo-oxynicotine hydrolase is involved in the nicotine-degradation pathway of Arthrobacter nicotinovorans. Fus2 is part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Fus2 catalyzes closure of the 2-pyrrolidone ring of the intermediate 20-hydroxy-prefusarin to form another intermediate, 20-hydroxy-fusarin, which is then oxidized by Fus8.


Pssm-ID: 428978 [Multi-domain]  Cd Length: 414  Bit Score: 793.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997829365   1 MTQANLSETLFKPRFKHPETSTLVRRFNHGAQPPVQSALDGKTIPHWYRMINRLMWIWRGIDPREILDVQARIVMSDAER 80
Cdd:pfam06500   1 MTQANLSETLFKPHFKHPETSTLVRRMPHSAQPPILSALDGQTIPHWYRMINRLMWIWRGIDPREIEEVLSRIASSKAER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997829365  81 TDDDLYDTVIGYRGGNWIYEWATQAMVWQQKACAEDDPQLSGRHWLHAATLYNIAAYPHLKGDDLAEQAQALSNRAYEEA 160
Cdd:pfam06500  81 THDDLLDTVMGYRSGNWIYEWATQGMVWQQKACEEDDPQLAGDHWLHAALLYSIAGYPHLKGDNLAEQAQVLSNRAYEEA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997829365 161 AQRLPGTMRQMEFTVPGGAPITGFLHMPKGDGPFPTVLMCGGLDAMQTDYYSLYERYFAPRGIAMLTIDMPSVGFSSKWK 240
Cdd:pfam06500 161 AKRLPYTMKQLEFPYQGGAKITGFLHMPKGDGPFPTVLMCGGLDSLQTDYWRLFRDYFAPKGIAMLTIDMPSVGASSHWK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997829365 241 LTQDSSLLHQHVLKALPNVPWVDHTRVAAFGFRCGANVAVRLAYLESPRLKAVACLGPVVHTLLSDFKCQQQVPEMYLDV 320
Cdd:pfam06500 241 LTQDSSCLHQAVLNALADVPWVDHTRVGLFGFRFGANVAVRLAYLESPRVKAVACLGPPVHDLLTSPKKLQKVPKMYLDV 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997829365 321 LASRLGMHDASDEALRVELNRYSLKVQGLLGRRCPTPMLSGYWKNDPFSPEEDSRLITSSSADGKLLEIPFNPVYRNFDK 400
Cdd:pfam06500 321 LASRLGMHDVDDESLRGEMNRYSLKVQGLLGRRCKTPMLAGYWENDPFSPYEDNQLIASSSADGKLLKIPSKPIYRNFEQ 400
                         410
                  ....*....|....
gi 1997829365 401 GLQEITDWIEKRLC 414
Cdd:pfam06500 401 SLDLAIDWLEDELC 414
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
172-413 1.02e-18

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 84.68  E-value: 1.02e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997829365 172 EFTVPGGAPITGFLHMPKGDGPFPTVLMCGGLDAMQTDYYSLYERYFAPRGIAMLTIDMPSVGFSSK---WKLTQDSSLL 248
Cdd:COG1506     1 TFKSADGTTLPGWLYLPADGKKYPVVVYVHGGPGSRDDSFLPLAQALASRGYAVLAPDYRGYGESAGdwgGDEVDDVLAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997829365 249 HQHVLKAlpnvPWVDHTRVAAFGFRCGANVAVRLAYLESPRLKAVACLGPvVHTLLSDFKCQQQVPEMYLDVLASRLGMH 328
Cdd:COG1506    81 IDYLAAR----PYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAG-VSDLRSYYGTTREYTERLMGGPWEDPEAY 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997829365 329 DASDEALRVElnryslkvqgllgrRCPTPMLSGYWKNDPFSPEEDSRLI----TSSSADGKLLEIPF---NPVYRNFDKG 401
Cdd:COG1506   156 AARSPLAYAD--------------KLKTPLLLIHGEADDRVPPEQAERLyealKKAGKPVELLVYPGeghGFSGAGAPDY 221
                         250
                  ....*....|..
gi 1997829365 402 LQEITDWIEKRL 413
Cdd:COG1506   222 LERILDFLDRHL 233
 
Name Accession Description Interval E-value
frsA PRK05077
esterase FrsA;
1-414 0e+00

esterase FrsA;


Pssm-ID: 235337  Cd Length: 414  Bit Score: 869.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997829365   1 MTQANLSETLFKPRFKHPETSTLVRRFNHGAQPPVQSALDGKTIPHWYRMINRLMWIWRGIDPREILDVQARIVMSDAER 80
Cdd:PRK05077    1 MTQANLSETLFKPRFKHPETSTLVRRFNHGSQPPIQSALDGKTVPHWYRMINRLMWIWRGIDPIEIEEVLARIAMSDAER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997829365  81 TDDDLYDTVIGYRGGNWIYEWATQAMVWQQKACAEDDPQLSGRHWLHAATLYNIAAYPHLKGDDLAEQAQALSNRAYEEA 160
Cdd:PRK05077   81 TDDELLDTVIGYRGGNWIYEWAKQAMEWQQKACAEEDPEEAGRHWLHAANLYSIAAYPHLKGDELAEQAQVLANRAYEEA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997829365 161 AQRLPGTMRQMEFTVPGGAPITGFLHMPKGDGPFPTVLMCGGLDAMQTDYYSLYERYFAPRGIAMLTIDMPSVGFSSKWK 240
Cdd:PRK05077  161 AKRLPGELKELEFPIPGGGPITGFLHLPKGDGPFPTVLVCGGLDSLQTDYYRLFRDYLAPRGIAMLTIDMPSVGFSSKWK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997829365 241 LTQDSSLLHQHVLKALPNVPWVDHTRVAAFGFRCGANVAVRLAYLESPRLKAVACLGPVVHTLLSDFKCQQQVPEMYLDV 320
Cdd:PRK05077  241 LTQDSSLLHQAVLNALPNVPWVDHTRVAAFGFRFGANVAVRLAYLEPPRLKAVACLGPVVHTLLTDPKRQQQVPEMYLDV 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997829365 321 LASRLGMHDASDEALRVELNRYSLKVQGLLGRRCPTPMLSGYWKNDPFSPEEDSRLITSSSADGKLLEIPFNPVYRNFDK 400
Cdd:PRK05077  321 LASRLGMHDASDEALRVELNRYSLKVQGLLGRRCPTPMLSGYWKNDPFSPEEDSRLIASSSADGKLLEIPFKPVYRNFDK 400
                         410
                  ....*....|....
gi 1997829365 401 GLQEITDWIEKRLC 414
Cdd:PRK05077  401 ALQEISDWLEDRLC 414
FrsA-like pfam06500
Esterase FrsA-like; The FrsA-like family includes FrsA, an esterase found to have the alpha ...
1-414 0e+00

Esterase FrsA-like; The FrsA-like family includes FrsA, an esterase found to have the alpha/beta-hydrolase fold. t also includes the hydrolytic polyketide shortening protein Ayg1 from fungi, 2,6-dihydropseudooxynicotine hydrolase from Paenarthrobacter nicotinovorans and Fus2 from Gibberella species. The enzyme 2,6-dihydroxy-pseudo-oxynicotine hydrolase is involved in the nicotine-degradation pathway of Arthrobacter nicotinovorans. Fus2 is part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Fus2 catalyzes closure of the 2-pyrrolidone ring of the intermediate 20-hydroxy-prefusarin to form another intermediate, 20-hydroxy-fusarin, which is then oxidized by Fus8.


Pssm-ID: 428978 [Multi-domain]  Cd Length: 414  Bit Score: 793.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997829365   1 MTQANLSETLFKPRFKHPETSTLVRRFNHGAQPPVQSALDGKTIPHWYRMINRLMWIWRGIDPREILDVQARIVMSDAER 80
Cdd:pfam06500   1 MTQANLSETLFKPHFKHPETSTLVRRMPHSAQPPILSALDGQTIPHWYRMINRLMWIWRGIDPREIEEVLSRIASSKAER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997829365  81 TDDDLYDTVIGYRGGNWIYEWATQAMVWQQKACAEDDPQLSGRHWLHAATLYNIAAYPHLKGDDLAEQAQALSNRAYEEA 160
Cdd:pfam06500  81 THDDLLDTVMGYRSGNWIYEWATQGMVWQQKACEEDDPQLAGDHWLHAALLYSIAGYPHLKGDNLAEQAQVLSNRAYEEA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997829365 161 AQRLPGTMRQMEFTVPGGAPITGFLHMPKGDGPFPTVLMCGGLDAMQTDYYSLYERYFAPRGIAMLTIDMPSVGFSSKWK 240
Cdd:pfam06500 161 AKRLPYTMKQLEFPYQGGAKITGFLHMPKGDGPFPTVLMCGGLDSLQTDYWRLFRDYFAPKGIAMLTIDMPSVGASSHWK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997829365 241 LTQDSSLLHQHVLKALPNVPWVDHTRVAAFGFRCGANVAVRLAYLESPRLKAVACLGPVVHTLLSDFKCQQQVPEMYLDV 320
Cdd:pfam06500 241 LTQDSSCLHQAVLNALADVPWVDHTRVGLFGFRFGANVAVRLAYLESPRVKAVACLGPPVHDLLTSPKKLQKVPKMYLDV 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997829365 321 LASRLGMHDASDEALRVELNRYSLKVQGLLGRRCPTPMLSGYWKNDPFSPEEDSRLITSSSADGKLLEIPFNPVYRNFDK 400
Cdd:pfam06500 321 LASRLGMHDVDDESLRGEMNRYSLKVQGLLGRRCKTPMLAGYWENDPFSPYEDNQLIASSSADGKLLKIPSKPIYRNFEQ 400
                         410
                  ....*....|....
gi 1997829365 401 GLQEITDWIEKRLC 414
Cdd:pfam06500 401 SLDLAIDWLEDELC 414
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
172-413 1.02e-18

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 84.68  E-value: 1.02e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997829365 172 EFTVPGGAPITGFLHMPKGDGPFPTVLMCGGLDAMQTDYYSLYERYFAPRGIAMLTIDMPSVGFSSK---WKLTQDSSLL 248
Cdd:COG1506     1 TFKSADGTTLPGWLYLPADGKKYPVVVYVHGGPGSRDDSFLPLAQALASRGYAVLAPDYRGYGESAGdwgGDEVDDVLAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997829365 249 HQHVLKAlpnvPWVDHTRVAAFGFRCGANVAVRLAYLESPRLKAVACLGPvVHTLLSDFKCQQQVPEMYLDVLASRLGMH 328
Cdd:COG1506    81 IDYLAAR----PYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAG-VSDLRSYYGTTREYTERLMGGPWEDPEAY 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997829365 329 DASDEALRVElnryslkvqgllgrRCPTPMLSGYWKNDPFSPEEDSRLI----TSSSADGKLLEIPF---NPVYRNFDKG 401
Cdd:COG1506   156 AARSPLAYAD--------------KLKTPLLLIHGEADDRVPPEQAERLyealKKAGKPVELLVYPGeghGFSGAGAPDY 221
                         250
                  ....*....|..
gi 1997829365 402 LQEITDWIEKRL 413
Cdd:COG1506   222 LERILDFLDRHL 233
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
167-299 8.46e-13

Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 67.30  E-value: 8.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997829365 167 TMRQMEFTVPGGAPITGFLHMPKGDGPFPTVLM---CGGLdamqTDYYSLYERYFAPRGIAMLTIDM---------PSVG 234
Cdd:COG0412     2 TTETVTIPTPDGVTLPGYLARPAGGGPRPGVVVlheIFGL----NPHIRDVARRLAAAGYVVLAPDLygrggpgddPDEA 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1997829365 235 FSSKWKLTQDsSLLH--QHVLKALPNVPWVDHTRVAAFGFRCGANVAVRLAyLESPRLKAVACLGPV 299
Cdd:COG0412    78 RALMGALDPE-LLAAdlRAALDWLKAQPEVDAGRVGVVGFCFGGGLALLAA-ARGPDLAAAVSFYGG 142
Axe1 COG3458
Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, ...
154-308 1.13e-05

Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442681 [Multi-domain]  Cd Length: 318  Bit Score: 47.11  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997829365 154 NRAYEEAAQR-LPGTMRQMEFTVP------------GGAPITGFLHMPKGDGPFPTVLMCGGldamqtdY----YSLYER 216
Cdd:COG3458    29 DATLAEARAVpLDPELTPVETGLPgvevydvtftgfGGARIYGWLLRPKGEGPLPAVVEFHG-------YgggrGLPHED 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997829365 217 Y-FAPRGIAMLTIDMPsvGFSSKWKLTQDSSL-----LHQHVLK----------------------ALPNVPWVDHTRVA 268
Cdd:COG3458   102 LdWAAAGYAVLVMDTR--GQGSSWGDTPDPGGysggaLPGYMTRgiddpdtyyyrrvyldavravdALRSLPEVDGKRIG 179
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1997829365 269 AFGFRCGANVAVRLAYLEsPRLKAVACLGPvvhtLLSDFK 308
Cdd:COG3458   180 VTGGSQGGGLALAAAALD-PRVKAAAADVP----FLCDFR 214
AXE1 pfam05448
Acetyl xylan esterase (AXE1); This family consists of several bacterial acetyl xylan esterase ...
145-308 3.27e-04

Acetyl xylan esterase (AXE1); This family consists of several bacterial acetyl xylan esterase proteins. Acetyl xylan esterases are enzymes that hydrolyse the ester linkages of the acetyl groups in position 2 and/or 3 of the xylose moieties of natural acetylated xylan from hardwood. These enzymes are one of the accessory enzymes which are part of the xylanolytic system, together with xylanases, beta-xylosidases, alpha-arabinofuranosidases and methylglucuronidases; these are all required for the complete hydrolysis of xylan.


Pssm-ID: 398876 [Multi-domain]  Cd Length: 316  Bit Score: 42.39  E-value: 3.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997829365 145 LAEQAQALSNRAYEEAAQRLPGT-MRQMEFTVPGGAPITGFLHMPKG-DGPFPTVL------MCGGLDAMQTDYYSLYER 216
Cdd:pfam05448  31 LAELRKVDPDLELEPVDFHLPTVeCYDLTFEGFGGARIYAWYVVPKEsEEKHPAVVhfhgynGRRGDWHDMLHWAAHGYA 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997829365 217 YFA--PRGIAMLTIDMPSVGFSSKWK------LTQDSSLLHQHV-------LKALPNVPWVDHTRVAAFGFRCGANVAVR 281
Cdd:pfam05448 111 VFVmdVRGQGGLSEDDPRGPKGNTYKghitrgLLDRETYYYRRVfldavraVEIVMSFPEVDEERIVVTGGSQGGALALA 190
                         170       180
                  ....*....|....*....|....*..
gi 1997829365 282 LAYLeSPRLKAVACLGPvvhtLLSDFK 308
Cdd:pfam05448 191 AAAL-SPRIKAVVADYP----FLSDFR 212
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
167-298 7.08e-04

Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 40.76  E-value: 7.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997829365 167 TMRQMEFTVPGGAPITGFLHMPKgDGPFPTVLMCGGLdamqTDYYSLYE---RYFAPRGIAMLTIDMPSVGFSSKWK--- 240
Cdd:COG2267     2 TRRLVTLPTRDGLRLRGRRWRPA-GSPRGTVVLVHGL----GEHSGRYAelaEALAAAGYAVLAFDLRGHGRSDGPRghv 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1997829365 241 -----LTQDSSLLHQHvLKALPNVPWVdhtrVAAFGFrcGANVAVRLAYLESPRLKAVACLGP 298
Cdd:COG2267    77 dsfddYVDDLRAALDA-LRARPGLPVV----LLGHSM--GGLIALLYAARYPDRVAGLVLLAP 132
mdoG PRK13274
glucan biosynthesis protein G; Provisional
143-173 7.69e-03

glucan biosynthesis protein G; Provisional


Pssm-ID: 237328  Cd Length: 516  Bit Score: 38.33  E-value: 7.69e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1997829365 143 DDLAEQAQALSNRAYEEAAQRLPGTMRQMEF 173
Cdd:PRK13274   33 DDVAKLARALAAKPYEAPKSNLPAALADLDY 63
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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