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Conserved domains on  [gi|1002281963|ref|XP_015645274|]
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carboxylesterase 15 [Oryza sativa Japonica Group]

Protein Classification

alpha/beta hydrolase( domain architecture ID 11171394)

alpha/beta hydrolase catalyzes the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

CATH:  3.40.50.1820
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  37582413|12369917|19508187

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 79-300 2.51e-67

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


:

Pssm-ID: 400284 [Multi-domain]  Cd Length: 208  Bit Score: 209.76  E-value: 2.51e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281963  79 VAYFHGGGFCIGSGRWPnfHAWCLRLAAELPAVVLSFDYRLAPEHRLPAAQEDGATAMAWVRDSAARdpwlaDAADFSRV 158
Cdd:pfam07859   1 LVYFHGGGFVLGSADTH--DRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAE-----LGADPSRI 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281963 159 FVAGDSAGGNITHHMAVRFGKAGLgpqVRLRGHVLLMPAMAGETR--TRAELECRPGAFLTAEMSDRYARLILPgGATRD 236
Cdd:pfam07859  74 AVAGDSAGGNLAAAVALRARDEGL---PKPAGQVLIYPGTDLRTEspSYLAREFADGPLLTRAAMDWFWRLYLP-GADRD 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002281963 237 YPVLNP-AGPEAPGLeavamAPSLVVAAEHDILRDRNEHYARRMReEWGKEVAFVEFAGEQHGFF 300
Cdd:pfam07859 150 DPLASPlFASDLSGL-----PPALVVVAEFDPLRDEGEAYAERLR-AAGVPVELIEYPGMPHGFH 208
 
Name Accession Description Interval E-value
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 79-300 2.51e-67

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 400284 [Multi-domain]  Cd Length: 208  Bit Score: 209.76  E-value: 2.51e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281963  79 VAYFHGGGFCIGSGRWPnfHAWCLRLAAELPAVVLSFDYRLAPEHRLPAAQEDGATAMAWVRDSAARdpwlaDAADFSRV 158
Cdd:pfam07859   1 LVYFHGGGFVLGSADTH--DRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAE-----LGADPSRI 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281963 159 FVAGDSAGGNITHHMAVRFGKAGLgpqVRLRGHVLLMPAMAGETR--TRAELECRPGAFLTAEMSDRYARLILPgGATRD 236
Cdd:pfam07859  74 AVAGDSAGGNLAAAVALRARDEGL---PKPAGQVLIYPGTDLRTEspSYLAREFADGPLLTRAAMDWFWRLYLP-GADRD 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002281963 237 YPVLNP-AGPEAPGLeavamAPSLVVAAEHDILRDRNEHYARRMReEWGKEVAFVEFAGEQHGFF 300
Cdd:pfam07859 150 DPLASPlFASDLSGL-----PPALVVVAEFDPLRDEGEAYAERLR-AAGVPVELIEYPGMPHGFH 208
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
61-324 2.91e-35

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 126.91  E-value: 2.91e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281963  61 RLYRPrhlgAANDARVPVVAYFHGGGFCIGSgrWPNFHAWCLRLAAELPAVVLSFDYRLAPEHRLPAAQEDGATAMAWVR 140
Cdd:COG0657     2 DVYRP----AGAKGPLPVVVYFHGGGWVSGS--KDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281963 141 DSAARdpWLADAadfSRVFVAGDSAGGNITHHMAVRFGKAGLgpqVRLRGHVLLmpamagetrtraelecrpgafltaem 220
Cdd:COG0657    76 ANAAE--LGIDP---DRIAVAGDSAGGHLAAALALRARDRGG---PRPAAQVLI-------------------------- 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281963 221 sdryarlilpggatrdYPVLNPAgpEAPGLEAVA-MAPSLVVAAEHDILRDRNEHYARRMREEwGKEVAFVEFAGEQHGF 299
Cdd:COG0657   122 ----------------YPVLDLT--ASPLRADLAgLPPTLIVTGEADPLVDESEALAAALRAA-GVPVELHVYPGGGHGF 182

                         250       260
                  ....*....|....*....|....*
gi 1002281963 300 FeVDPWSERADELVRLIRSFVVEHM 324
Cdd:COG0657   183 G-LLAGLPEARAALAEIAAFLRRAL 206
PRK10162 PRK10162
acetyl esterase;
61-299 7.17e-12

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 65.12  E-value: 7.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281963  61 RLYRPRHLGAAndarvpVVAYFHGGGFCIGSgrwPNFHAWCLR-LAAELPAVVLSFDYRLAPEHRLPAAQEDGATAMAWV 139
Cdd:PRK10162   72 RLYYPQPDSQA------TLFYLHGGGFILGN---LDTHDRIMRlLASYSGCTVIGIDYTLSPEARFPQAIEEIVAVCCYF 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281963 140 RDSAARdpwlaDAADFSRVFVAGDSAGGNIT--HHMAVR---------------FGKAGL--GPQVRLRGHVLlmpamag 200
Cdd:PRK10162  143 HQHAED-----YGINMSRIGFAGDSAGAMLAlaSALWLRdkqidcgkvagvllwYGLYGLrdSVSRRLLGGVW------- 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281963 201 ETRTRAELECRPGAFLT--AEMSDRYARLILpGGATRDYPvlnpagpeapgleavamaPSLVVAAEHDILRDRNEHYARR 278
Cdd:PRK10162  211 DGLTQQDLQMYEEAYLSndADRESPYYCLFN-NDLTRDVP------------------PCFIAGAEFDPLLDDSRLLYQT 271

                         250       260
                  ....*....|....*....|.
gi 1002281963 279 MrEEWGKEVAFVEFAGEQHGF 299
Cdd:PRK10162  272 L-AAHQQPCEFKLYPGTLHAF 291
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 46-172 3.32e-08

Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on carboxylic esters (EC: 3.1.1.-). The catalytic apparatus involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine.These catalytic residues are responsible for the nucleophilic attack on the carbonyl carbon atom of the ester bond. In contrast with other alpha/beta hydrolase fold family members, p-nitrobenzyl esterase and acetylcholine esterase have a Glu instead of Asp at the active site carboxylate.


Pssm-ID: 238191 [Multi-domain]  Cd Length: 493  Bit Score: 54.65  E-value: 3.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281963  46 EWKDVTYDAEHDLNARLYRPRhlGAANDARVPVVAYFHGGGFCIGSGRWPNFHawclRLAAELPAVVL-SFDYRLAP--- 121
Cdd:cd00312    67 LWNAKLPGSEDCLYLNVYTPK--NTKPGNSLPVMVWIHGGGFMFGSGSLYPGD----GLAREGDNVIVvSINYRLGVlgf 140

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281963 122 ----EHRLP--AAQEDGATAMAWVRDSAAR---DPwladaadfSRVFVAGDSAGGNITHH 172
Cdd:cd00312   141 lstgDIELPgnYGLKDQRLALKWVQDNIAAfggDP--------DSVTIFGESAGGASVSL 192
 
Name Accession Description Interval E-value
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 79-300 2.51e-67

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 400284 [Multi-domain]  Cd Length: 208  Bit Score: 209.76  E-value: 2.51e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281963  79 VAYFHGGGFCIGSGRWPnfHAWCLRLAAELPAVVLSFDYRLAPEHRLPAAQEDGATAMAWVRDSAARdpwlaDAADFSRV 158
Cdd:pfam07859   1 LVYFHGGGFVLGSADTH--DRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAE-----LGADPSRI 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281963 159 FVAGDSAGGNITHHMAVRFGKAGLgpqVRLRGHVLLMPAMAGETR--TRAELECRPGAFLTAEMSDRYARLILPgGATRD 236
Cdd:pfam07859  74 AVAGDSAGGNLAAAVALRARDEGL---PKPAGQVLIYPGTDLRTEspSYLAREFADGPLLTRAAMDWFWRLYLP-GADRD 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002281963 237 YPVLNP-AGPEAPGLeavamAPSLVVAAEHDILRDRNEHYARRMReEWGKEVAFVEFAGEQHGFF 300
Cdd:pfam07859 150 DPLASPlFASDLSGL-----PPALVVVAEFDPLRDEGEAYAERLR-AAGVPVELIEYPGMPHGFH 208
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
61-324 2.91e-35

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 126.91  E-value: 2.91e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281963  61 RLYRPrhlgAANDARVPVVAYFHGGGFCIGSgrWPNFHAWCLRLAAELPAVVLSFDYRLAPEHRLPAAQEDGATAMAWVR 140
Cdd:COG0657     2 DVYRP----AGAKGPLPVVVYFHGGGWVSGS--KDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281963 141 DSAARdpWLADAadfSRVFVAGDSAGGNITHHMAVRFGKAGLgpqVRLRGHVLLmpamagetrtraelecrpgafltaem 220
Cdd:COG0657    76 ANAAE--LGIDP---DRIAVAGDSAGGHLAAALALRARDRGG---PRPAAQVLI-------------------------- 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281963 221 sdryarlilpggatrdYPVLNPAgpEAPGLEAVA-MAPSLVVAAEHDILRDRNEHYARRMREEwGKEVAFVEFAGEQHGF 299
Cdd:COG0657   122 ----------------YPVLDLT--ASPLRADLAgLPPTLIVTGEADPLVDESEALAAALRAA-GVPVELHVYPGGGHGF 182

                         250       260
                  ....*....|....*....|....*
gi 1002281963 300 FeVDPWSERADELVRLIRSFVVEHM 324
Cdd:COG0657   183 G-LLAGLPEARAALAEIAAFLRRAL 206
PRK10162 PRK10162
acetyl esterase;
61-299 7.17e-12

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 65.12  E-value: 7.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281963  61 RLYRPRHLGAAndarvpVVAYFHGGGFCIGSgrwPNFHAWCLR-LAAELPAVVLSFDYRLAPEHRLPAAQEDGATAMAWV 139
Cdd:PRK10162   72 RLYYPQPDSQA------TLFYLHGGGFILGN---LDTHDRIMRlLASYSGCTVIGIDYTLSPEARFPQAIEEIVAVCCYF 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281963 140 RDSAARdpwlaDAADFSRVFVAGDSAGGNIT--HHMAVR---------------FGKAGL--GPQVRLRGHVLlmpamag 200
Cdd:PRK10162  143 HQHAED-----YGINMSRIGFAGDSAGAMLAlaSALWLRdkqidcgkvagvllwYGLYGLrdSVSRRLLGGVW------- 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281963 201 ETRTRAELECRPGAFLT--AEMSDRYARLILpGGATRDYPvlnpagpeapgleavamaPSLVVAAEHDILRDRNEHYARR 278
Cdd:PRK10162  211 DGLTQQDLQMYEEAYLSndADRESPYYCLFN-NDLTRDVP------------------PCFIAGAEFDPLLDDSRLLYQT 271

                         250       260
                  ....*....|....*....|.
gi 1002281963 279 MrEEWGKEVAFVEFAGEQHGF 299
Cdd:PRK10162  272 L-AAHQQPCEFKLYPGTLHAF 291
COesterase pfam00135
Carboxylesterase family;
63-174 9.24e-09

Carboxylesterase family;


Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 56.55  E-value: 9.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281963  63 YRPRHLgAANDARVPVVAYFHGGGFCIGSGRW--PNFhawclrLAAELPAVVLSFDYRLAP--------EHrLP--AAQE 130
Cdd:pfam00135  91 YTPKEL-KENKNKLPVMVWIHGGGFMFGSGSLydGSY------LAAEGDVIVVTINYRLGPlgflstgdDE-APgnYGLL 162

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1002281963 131 DGATAMAWVRDSAAR---DPwladaadfSRVFVAGDSAGGNITH-HMA 174
Cdd:pfam00135 163 DQVLALRWVQENIASfggDP--------NRVTLFGESAGAASVSlLLL 202
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 46-172 3.32e-08

Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on carboxylic esters (EC: 3.1.1.-). The catalytic apparatus involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine.These catalytic residues are responsible for the nucleophilic attack on the carbonyl carbon atom of the ester bond. In contrast with other alpha/beta hydrolase fold family members, p-nitrobenzyl esterase and acetylcholine esterase have a Glu instead of Asp at the active site carboxylate.


Pssm-ID: 238191 [Multi-domain]  Cd Length: 493  Bit Score: 54.65  E-value: 3.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281963  46 EWKDVTYDAEHDLNARLYRPRhlGAANDARVPVVAYFHGGGFCIGSGRWPNFHawclRLAAELPAVVL-SFDYRLAP--- 121
Cdd:cd00312    67 LWNAKLPGSEDCLYLNVYTPK--NTKPGNSLPVMVWIHGGGFMFGSGSLYPGD----GLAREGDNVIVvSINYRLGVlgf 140

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281963 122 ----EHRLP--AAQEDGATAMAWVRDSAAR---DPwladaadfSRVFVAGDSAGGNITHH 172
Cdd:cd00312   141 lstgDIELPgnYGLKDQRLALKWVQDNIAAfggDP--------DSVTIFGESAGGASVSL 192
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
56-324 4.42e-08

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 53.10  E-value: 4.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281963  56 HDLNARLYRPrhlgaANDARVPVVAYFHGGgfciGSGRWPNFHAWCLRLAAelpA--VVLSFDYRLAPEHRLPAAQEDGA 133
Cdd:COG1506     8 TTLPGWLYLP-----ADGKKYPVVVYVHGG----PGSRDDSFLPLAQALAS---RgyAVLAPDYRGYGESAGDWGGDEVD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281963 134 TAMAWVrDSAARDPWladaADFSRVFVAGDSAGGNITHHMAVRFGKaglgpqvRLRGHVLLMPAmagetrtraeleCRPG 213
Cdd:COG1506    76 DVLAAI-DYLAARPY----VDPDRIGIYGHSYGGYMALLAAARHPD-------RFKAAVALAGV------------SDLR 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281963 214 AFLTAEMSDRYARLILPGGATRDYPVLNPAgPEAPGLEavamAPSLVVAAEHD--ILRDRNEHYARRMREEwGKEVAFVE 291
Cdd:COG1506   132 SYYGTTREYTERLMGGPWEDPEAYAARSPL-AYADKLK----TPLLLIHGEADdrVPPEQAERLYEALKKA-GKPVELLV 205

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1002281963 292 FAGEQHGFFevdpwSERADELVRLIRSFVVEHM 324
Cdd:COG1506   206 YPGEGHGFS-----GAGAPDYLERILDFLDRHL 233
PnbA COG2272
Carboxylesterase type B [Lipid transport and metabolism];
70-174 1.45e-07

Carboxylesterase type B [Lipid transport and metabolism];


Pssm-ID: 441873  Cd Length: 500  Bit Score: 52.58  E-value: 1.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281963  70 AANDARVPVVAYFHGGGFCIGSGRWPNFHAWclRLAAELpAVVLSFDYRL------------APEHRLPA--AQEDGATA 135
Cdd:COG2272    99 LAAGAKLPVMVWIHGGGFVSGSGSEPLYDGA--ALARRG-VVVVTINYRLgalgflalpalsGESYGASGnyGLLDQIAA 175

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1002281963 136 MAWVRDSAAR---DPwladaadfSRVFVAGDSAGG-NITHHMA 174
Cdd:COG2272   176 LRWVRDNIAAfggDP--------DNVTIFGESAGAaSVAALLA 210
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
 62-174 5.76e-07

BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, previously known as bifunctional carbohydrate esterase (CE)), which is active on complex natural xylans and was identified as the basis of a monophyletic clade gathering all homologs identified in PULs (polysaccharide utilization loci) predicted to act on xylan. It adopts an alpha-beta-hydrolase fold with the catalytic triad Ser-Asp-His. This new family of proteins is a new candidate for biomass processing due to its capacity to remove ferulic acid and acetic acid from natural corn and birchwood xylan substrates.


Pssm-ID: 466583 [Multi-domain]  Cd Length: 215  Bit Score: 49.49  E-value: 5.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281963  62 LYRPrhlgAANDARVPVVAYFHGGGFCIGS-----GRWPNFHAwclRLAAELPAVVlSFDYRLAPEHRLPAAQEDGATAM 136
Cdd:pfam20434   3 IYLP----KNAKGPYPVVIWIHGGGWNSGDkeadmGFMTNTVK---ALLKAGYAVA-SINYRLSTDAKFPAQIQDVKAAI 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1002281963 137 AWVRDSAAR---DPwladaadfSRVFVAGDSAGGnithHMA 174
Cdd:pfam20434  75 RFLRANAAKygiDT--------NKIALMGFSAGG----HLA 103
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 77-323 4.14e-04

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 41.14  E-value: 4.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281963  77 PVVAYFHGGGfciGSGRwpNFHAWCLRLAAELPavVLSFDYRlapEHRLPAAQEDGATAMAWVRDSAArdpwLADAADFS 156
Cdd:COG0596    24 PPVVLLHGLP---GSSY--EWRPLIPALAAGYR--VIAPDLR---GHGRSDKPAGGYTLDDLADDLAA----LLDALGLE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281963 157 RVFVAGDSAGGNITHHMAVRFgkaglgPQvRLRGHVLLMPAMAGETRTRAELECRPGAFLTAemsdryarliLPGGATRD 236
Cdd:COG0596    90 RVVLVGHSMGGMVALELAARH------PE-RVAGLVLVDEVLAALAEPLRRPGLAPEALAAL----------LRALARTD 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281963 237 YpvlnpagpeAPGLEAVAMaPSLVVAAEHDILRDRneHYARRMREEWgKEVAFVEFAGEQHGFFEvdpwsERADELVRLI 316
Cdd:COG0596   153 L---------RERLARITV-PTLVIWGEKDPIVPP--ALARRLAELL-PNAELVVLPGAGHFPPL-----EQPEAFAAAL 214


                  ....*..
gi 1002281963 317 RSFVVEH 323
Cdd:COG0596   215 RDFLARL 221
Say1_Mug180 pfam10340
Steryl acetyl hydrolase; This entry includes budding yeast steryl acetyl hydrolase 1 (Say1) ...
 77-168 6.60e-04

Steryl acetyl hydrolase; This entry includes budding yeast steryl acetyl hydrolase 1 (Say1) and fission yeast Mug180. Say1 is a a membrane-anchored deacetylase required for the deacetylation of acetylated sterols. It is involved in the resistance to eugenol and pregnenolone toxicity. Mug180 has a role in meiosis.


Pssm-ID: 313549  Cd Length: 374  Bit Score: 40.97  E-value: 6.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281963  77 PVVAYFHGGGFCIGSGRWPNFHAWCLRLAAELPAVVLSfDYRLApehrlpAAQEDGATAMAWVRDSAARDPWLADAADFS 156
Cdd:pfam10340 123 PILLYYHGGGFALKLIPVTLVFLNNLGKYFPDMAILVS-DYTVT------ANCPQSYTYPLQVLQCLAVYDYLTLTKGCK 195

                          90
                  ....*....|..
gi 1002281963 157 RVFVAGDSAGGN 168
Cdd:pfam10340 196 NVTLMGDSAGGN 207
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 48-176 8.45e-03

Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 37.20  E-value: 8.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281963  48 KDVTYDAE--HDLNARLYRPrhlgAANDARVPVVAYFHGGGFCIgsgrwpnfhAWCLRLAAELPA---VVLSFDYR---- 118
Cdd:COG1073    11 EDVTFKSRdgIKLAGDLYLP----AGASKKYPAVVVAHGNGGVK---------EQRALYAQRLAElgfNVLAFDYRgyge 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002281963 119 ---LAPEHRLPAAQeDGATAMAWVRDSAARDPwladaadfSRVFVAGDSAGGNITHHMAVR 176
Cdd:COG1073    78 segEPREEGSPERR-DARAAVDYLRTLPGVDP--------ERIGLLGISLGGGYALNAAAT 129
 
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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