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Conserved domains on  [gi|1955874342|ref|XP_038895106|]
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probable carboxylesterase 18 [Benincasa hispida]

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.
 93-310 1.46e-71

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: 220.93  E-value: 1.46e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955874342  93 LIYFHGGGFVFFSSDFlpFDILCRQLARNLQAIVVSVNYRLSPEHRYPSQYEDEFDALKFIDEldsSAFPEKSDFGRCFI 172
Cdd:pfam07859   1 LVYFHGGGFVLGSADT--HDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAE---QAAELGADPSRIAV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955874342 173 SGDSAGGNIAHHVVVRSGDYdfKKVKIRGLIAIQPffGGEERTESE----IRFAKSPTLNLERADWYWKAFLPdGSNRKH 248
Cdd:pfam07859  76 AGDSAGGNLAAAVALRARDE--GLPKPAGQVLIYP--GTDLRTESPsylaREFADGPLLTRAAMDWFWRLYLP-GADRDD 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1955874342 249 PAAH-VFGADgvnisAVKFPATLVIVGGCDQLQDWDRKYYEWLKNAGKEVELVEYPKAIHAFY 310
Cdd:pfam07859 151 PLASpLFASD-----LSGLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHGFH 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.
 93-310 1.46e-71

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: 220.93  E-value: 1.46e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955874342  93 LIYFHGGGFVFFSSDFlpFDILCRQLARNLQAIVVSVNYRLSPEHRYPSQYEDEFDALKFIDEldsSAFPEKSDFGRCFI 172
Cdd:pfam07859   1 LVYFHGGGFVLGSADT--HDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAE---QAAELGADPSRIAV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955874342 173 SGDSAGGNIAHHVVVRSGDYdfKKVKIRGLIAIQPffGGEERTESE----IRFAKSPTLNLERADWYWKAFLPdGSNRKH 248
Cdd:pfam07859  76 AGDSAGGNLAAAVALRARDE--GLPKPAGQVLIYP--GTDLRTESPsylaREFADGPLLTRAAMDWFWRLYLP-GADRDD 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1955874342 249 PAAH-VFGADgvnisAVKFPATLVIVGGCDQLQDWDRKYYEWLKNAGKEVELVEYPKAIHAFY 310
Cdd:pfam07859 151 PLASpLFASD-----LSGLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHGFH 208
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
77-334 2.96e-42

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 145.79  E-value: 2.96e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955874342  77 RLFVPSPTSDdlPMPILIYFHGGGFVFFSSDFlpFDILCRQLARNLQAIVVSVNYRLSPEHRYPSQYEDEFDALKFIDEl 156
Cdd:COG0657     2 DVYRPAGAKG--PLPVVVYFHGGGWVSGSKDT--HDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRA- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955874342 157 dsSAFPEKSDFGRCFISGDSAGGNIAHHVVVRSGDYDfkKVKIRGLIAIQPFFggeerteseirfakSPTLNLERADwyw 236
Cdd:COG0657    77 --NAAELGIDPDRIAVAGDSAGGHLAAALALRARDRG--GPRPAAQVLIYPVL--------------DLTASPLRAD--- 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955874342 237 kafLPDgsnrkhpaahvfgadgvnisavkFPATLVIVGGCDQLQDWDRKYYEWLKNAGKEVELVEYPKAIHAFYTIPELP 316
Cdd:COG0657   136 ---LAG-----------------------LPPTLIVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHGFGLLAGLP 189

                         250
                  ....*....|....*...
gi 1955874342 317 EASLLIKDVKNFIQKTVS 334
Cdd:COG0657   190 EARAALAEIAAFLRRALA 207
PRK10162 PRK10162
acetyl esterase;
61-309 1.09e-23

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 99.02  E-value: 1.09e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955874342  61 VFTRD-TVIDPSRNLWFRLFVPSPTSDdlpmPILIYFHGGGFVFFSSDflPFDILCRQLARNLQAIVVSVNYRLSPEHRY 139
Cdd:PRK10162   55 MATRAyMVPTPYGQVETRLYYPQPDSQ----ATLFYLHGGGFILGNLD--THDRIMRLLASYSGCTVIGIDYTLSPEARF 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955874342 140 PSQYEDEFDALKFIDEL--DSSAFPEKSDFGrcfisGDSAGGNIAHHVVVRSGDYDFKKVKIRGLIAIQPFFGgeERTES 217
Cdd:PRK10162  129 PQAIEEIVAVCCYFHQHaeDYGINMSRIGFA-----GDSAGAMLALASALWLRDKQIDCGKVAGVLLWYGLYG--LRDSV 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955874342 218 EIRFAKSPTLNLERADW--YWKAFLPDGSNRKHPAAHVFGAD---GVnisavkfPATLVIVGGCDQLQDWDRKYYEWLKN 292
Cdd:PRK10162  202 SRRLLGGVWDGLTQQDLqmYEEAYLSNDADRESPYYCLFNNDltrDV-------PPCFIAGAEFDPLLDDSRLLYQTLAA 274

                         250
                  ....*....|....*..
gi 1955874342 293 AGKEVELVEYPKAIHAF 309
Cdd:PRK10162  275 HQQPCEFKLYPGTLHAF 291
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 78-135 1.88e-06

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: 49.25  E-value: 1.88e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1955874342  78 LFVPSPTSDDLPMPILIYFHGGGFVFFSSDFLPFDilcrQLARNLQA-IVVSVNYRLSP 135
Cdd:cd00312    83 VYTPKNTKPGNSLPVMVWIHGGGFMFGSGSLYPGD----GLAREGDNvIVVSINYRLGV 137
 
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.
 93-310 1.46e-71

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: 220.93  E-value: 1.46e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955874342  93 LIYFHGGGFVFFSSDFlpFDILCRQLARNLQAIVVSVNYRLSPEHRYPSQYEDEFDALKFIDEldsSAFPEKSDFGRCFI 172
Cdd:pfam07859   1 LVYFHGGGFVLGSADT--HDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAE---QAAELGADPSRIAV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955874342 173 SGDSAGGNIAHHVVVRSGDYdfKKVKIRGLIAIQPffGGEERTESE----IRFAKSPTLNLERADWYWKAFLPdGSNRKH 248
Cdd:pfam07859  76 AGDSAGGNLAAAVALRARDE--GLPKPAGQVLIYP--GTDLRTESPsylaREFADGPLLTRAAMDWFWRLYLP-GADRDD 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1955874342 249 PAAH-VFGADgvnisAVKFPATLVIVGGCDQLQDWDRKYYEWLKNAGKEVELVEYPKAIHAFY 310
Cdd:pfam07859 151 PLASpLFASD-----LSGLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHGFH 208
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
77-334 2.96e-42

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 145.79  E-value: 2.96e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955874342  77 RLFVPSPTSDdlPMPILIYFHGGGFVFFSSDFlpFDILCRQLARNLQAIVVSVNYRLSPEHRYPSQYEDEFDALKFIDEl 156
Cdd:COG0657     2 DVYRPAGAKG--PLPVVVYFHGGGWVSGSKDT--HDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRA- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955874342 157 dsSAFPEKSDFGRCFISGDSAGGNIAHHVVVRSGDYDfkKVKIRGLIAIQPFFggeerteseirfakSPTLNLERADwyw 236
Cdd:COG0657    77 --NAAELGIDPDRIAVAGDSAGGHLAAALALRARDRG--GPRPAAQVLIYPVL--------------DLTASPLRAD--- 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955874342 237 kafLPDgsnrkhpaahvfgadgvnisavkFPATLVIVGGCDQLQDWDRKYYEWLKNAGKEVELVEYPKAIHAFYTIPELP 316
Cdd:COG0657   136 ---LAG-----------------------LPPTLIVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHGFGLLAGLP 189

                         250
                  ....*....|....*...
gi 1955874342 317 EASLLIKDVKNFIQKTVS 334
Cdd:COG0657   190 EARAALAEIAAFLRRALA 207
PRK10162 PRK10162
acetyl esterase;
61-309 1.09e-23

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 99.02  E-value: 1.09e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955874342  61 VFTRD-TVIDPSRNLWFRLFVPSPTSDdlpmPILIYFHGGGFVFFSSDflPFDILCRQLARNLQAIVVSVNYRLSPEHRY 139
Cdd:PRK10162   55 MATRAyMVPTPYGQVETRLYYPQPDSQ----ATLFYLHGGGFILGNLD--THDRIMRLLASYSGCTVIGIDYTLSPEARF 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955874342 140 PSQYEDEFDALKFIDEL--DSSAFPEKSDFGrcfisGDSAGGNIAHHVVVRSGDYDFKKVKIRGLIAIQPFFGgeERTES 217
Cdd:PRK10162  129 PQAIEEIVAVCCYFHQHaeDYGINMSRIGFA-----GDSAGAMLALASALWLRDKQIDCGKVAGVLLWYGLYG--LRDSV 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955874342 218 EIRFAKSPTLNLERADW--YWKAFLPDGSNRKHPAAHVFGAD---GVnisavkfPATLVIVGGCDQLQDWDRKYYEWLKN 292
Cdd:PRK10162  202 SRRLLGGVWDGLTQQDLqmYEEAYLSNDADRESPYYCLFNNDltrDV-------PPCFIAGAEFDPLLDDSRLLYQTLAA 274

                         250
                  ....*....|....*..
gi 1955874342 293 AGKEVELVEYPKAIHAF 309
Cdd:PRK10162  275 HQQPCEFKLYPGTLHAF 291
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
74-333 3.42e-12

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 65.04  E-value: 3.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955874342  74 LWFRLFVPSptsDDLPMPILIYFHGGGfvffSSDFLPFDILCRQLARNlQAIVVSVNYRLSPEHRYPSQYEDEFDALKFI 153
Cdd:COG1506    10 LPGWLYLPA---DGKKYPVVVYVHGGP----GSRDDSFLPLAQALASR-GYAVLAPDYRGYGESAGDWGGDEVDDVLAAI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955874342 154 DELDSSAFpekSDFGRCFISGDSAGGNIAHHVVVRSGDYdfkkvkIRGLIAIQPFFGGEERTESEIRFAKsptlnlERAD 233
Cdd:COG1506    82 DYLAARPY---VDPDRIGIYGHSYGGYMALLAAARHPDR------FKAAVALAGVSDLRSYYGTTREYTE------RLMG 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955874342 234 WYWKAflPDGSNRKHPAAHvfgADGVNIsavkfpATLVIVGGCDQLQDWD--RKYYEWLKNAGKEVELVEYPKAIHAFYt 311
Cdd:COG1506   147 GPWED--PEAYAARSPLAY---ADKLKT------PLLLIHGEADDRVPPEqaERLYEALKKAGKPVELLVYPGEGHGFS- 214

                         250       260
                  ....*....|....*....|..
gi 1955874342 312 ipeLPEASLLIKDVKNFIQKTV 333
Cdd:COG1506   215 ---GAGAPDYLERILDFLDRHL 233
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
 83-182 1.31e-08

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: 54.49  E-value: 1.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955874342  83 PTSDDLPMPILIYFHGGGFVFFSS-DFLPFDILCRQLARNLQAIVVSVNYRLSPEHRYPSQYEDEFDALKFIDE------ 155
Cdd:pfam20434   6 PKNAKGPYPVVIWIHGGGWNSGDKeADMGFMTNTVKALLKAGYAVASINYRLSTDAKFPAQIQDVKAAIRFLRAnaakyg 85

                          90       100
                  ....*....|....*....|....*..
gi 1955874342 156 LDSSafpeksdfgRCFISGDSAGGNIA 182
Cdd:pfam20434  86 IDTN---------KIALMGFSAGGHLA 103
PnbA COG2272
Carboxylesterase type B [Lipid transport and metabolism];
73-133 5.76e-08

Carboxylesterase type B [Lipid transport and metabolism];


Pssm-ID: 441873  Cd Length: 500  Bit Score: 54.12  E-value: 5.76e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1955874342  73 NLWfrlfVPSPTSDDlPMPILIYFHGGGFVFFSSDFLPFDilCRQLARNlQAIVVSVNYRL 133
Cdd:COG2272    93 NVW----TPALAAGA-KLPVMVWIHGGGFVSGSGSEPLYD--GAALARR-GVVVVTINYRL 145
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 78-135 1.88e-06

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: 49.25  E-value: 1.88e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1955874342  78 LFVPSPTSDDLPMPILIYFHGGGFVFFSSDFLPFDilcrQLARNLQA-IVVSVNYRLSP 135
Cdd:cd00312    83 VYTPKNTKPGNSLPVMVWIHGGGFMFGSGSLYPGD----GLAREGDNvIVVSINYRLGV 137
COesterase pfam00135
Carboxylesterase family;
79-135 5.64e-06

Carboxylesterase family;


Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 47.69  E-value: 5.64e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1955874342  79 FVPSPTSD-DLPMPILIYFHGGGFVFFS-SDFLPfdilcRQLARNLQAIVVSVNYRLSP 135
Cdd:pfam00135  91 YTPKELKEnKNKLPVMVWIHGGGFMFGSgSLYDG-----SYLAAEGDVIVVTINYRLGP 144
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
77-331 1.74e-05

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 45.38  E-value: 1.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955874342  77 RLFVPSPTSDDLPMPILIYFHGGGfvffsSDFLPFDILCRQLARNlQAIVVSVNYR---LSPEHR-YPSQYEDEFDALK- 151
Cdd:COG2267    15 RLRGRRWRPAGSPRGTVVLVHGLG-----EHSGRYAELAEALAAA-GYAVLAFDLRghgRSDGPRgHVDSFDDYVDDLRa 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955874342 152 FIDELdssafpEKSDFGRCFISGDSAGGNIAHHVVVRSGDydfkkvKIRGLIAIQPffggeerteseiRFAKSPtLNLER 231
Cdd:COG2267    89 ALDAL------RARPGLPVVLLGHSMGGLIALLYAARYPD------RVAGLVLLAP------------AYRADP-LLGPS 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955874342 232 ADWYWKAFLPDgsnrkhpaahvfgadgvNISAVKFPaTLVIVGGCDQLQDWD--RKYYEWLknaGKEVELVEYPKAIHAF 309
Cdd:COG2267   144 ARWLRALRLAE-----------------ALARIDVP-VLVLHGGADRVVPPEaaRRLAARL---SPDVELVLLPGARHEL 202

                         250       260
                  ....*....|....*....|..
gi 1955874342 310 YTIPELPEAsllIKDVKNFIQK 331
Cdd:COG2267   203 LNEPAREEV---LAAILAWLER 221
Fes COG2382
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];
56-303 3.13e-03

Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];


Pssm-ID: 441948 [Multi-domain]  Cd Length: 314  Bit Score: 39.07  E-value: 3.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955874342  56 AAHDGVFTRDTVIDPSRNLWFRLFV---PSPTSDDLPMPILIYFHGGGFVFFS-SDFLPFDILCRQLARNLQA---IVVS 128
Cdd:COG2382    75 DVPHGTVETVTYPSKALGRTRRVWVylpPGYDNPGKKYPVLYLLDGGGGDEQDwFDQGRLPTILDNLIAAGKIppmIVVM 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955874342 129 VNY----RLSPEHRYPSQYEDEF--DALKFIDeldsSAFPEKSDFGRCFISGDSAGGNIAHHVVVRSGDYdFKKVkirgl 202
Cdd:COG2382   155 PDGgdggDRGTEGPGNDAFERFLaeELIPFVE----KNYRVSADPEHRAIAGLSMGGLAALYAALRHPDL-FGYV----- 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955874342 203 IAIQPFFGGEERTESEIRfaksptlnleradwyWKAFLPDGSNRKHpaahvfgadgvnisaVKFpatLVIVGGCDQLQDW 282
Cdd:COG2382   225 GSFSGSFWWPPGDADRGG---------------WAELLAAGAPKKP---------------LRF---YLDVGTEDDLLEA 271

                         250       260
                  ....*....|....*....|.
gi 1955874342 283 DRKYYEWLKNAGKEVELVEYP 303
Cdd:COG2382   272 NRALAAALKAKGYDVEYREFP 292
Say1_Mug180 pfam10340
Steryl acetyl hydrolase; This entry includes budding yeast steryl acetyl hydrolase 1 (Say1) ...
 83-223 4.55e-03

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: 38.66  E-value: 4.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955874342  83 PTSDdlpmPILIYFHGGGFVFfssDFLPFDILCRQLARNL---QAIVVS---VNYRLSPEHRYPSQYEDEFDALKFIDEL 156
Cdd:pfam10340 119 PKVD----PILLYYHGGGFAL---KLIPVTLVFLNNLGKYfpdMAILVSdytVTANCPQSYTYPLQVLQCLAVYDYLTLT 191

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1955874342 157 DSsafpeksdFGRCFISGDSAGGNIAHHVVVRSGDYDfKKVKIRGLIAIQPFFGGEERTESEIRFAK 223
Cdd:pfam10340 192 KG--------CKNVTLMGDSAGGNLVLNILLYLHKCN-KVVLPKKAIAISPWLNLTDRNEKEKEYMK 249
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
269-309 5.31e-03

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 37.64  E-value: 5.31e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1955874342 269 TLVIVGGCDQL--QDWDRKYYEWLKNAGKEVELVEYPKAIHAF 309
Cdd:COG0412   159 VLLLYGEKDPLvpPEQVAALEAALAAAGVDVELHVYPGAGHGF 201
 
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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