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Conserved domains on  [gi|778717692|ref|XP_004143400|]
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probable carboxylesterase 15 [Cucumis sativus]

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.
 78-295 5.66e-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: 219.00  E-value: 5.66e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778717692   78 LFFFHGGGFCVGSRSWPnsHNCCVRLALGLGALVIAPDYRLAPEHRLPAAVEDGAKAIEWVSKAGKldewiEESGDLQRV 157
Cdd:pfam07859   1 LVYFHGGGFVLGSADTH--DRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAA-----ELGADPSRI 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778717692  158 FVMGDSSGGNIAHHLAVRIGTENEkFGVRGFVLMAPffGGVGRTKSEEGPAEQ-----FFDLEALDRFWRLSLPiGEDRD 232
Cdd:pfam07859  74 AVAGDSAGGNLAAAVALRARDEGL-PKPAGQVLIYP--GTDLRTESPSYLAREfadgpLLTRAAMDWFWRLYLP-GADRD 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 778717692  233 HPLANPFGASSMSleevNLEPILVIVGGDEMLKDRAETYAKTLSQLGKRIEYVEFDGKQHGFF 295
Cdd:pfam07859 150 DPLASPLFASDLS----GLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHGFH 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.
 78-295 5.66e-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: 219.00  E-value: 5.66e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778717692   78 LFFFHGGGFCVGSRSWPnsHNCCVRLALGLGALVIAPDYRLAPEHRLPAAVEDGAKAIEWVSKAGKldewiEESGDLQRV 157
Cdd:pfam07859   1 LVYFHGGGFVLGSADTH--DRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAA-----ELGADPSRI 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778717692  158 FVMGDSSGGNIAHHLAVRIGTENEkFGVRGFVLMAPffGGVGRTKSEEGPAEQ-----FFDLEALDRFWRLSLPiGEDRD 232
Cdd:pfam07859  74 AVAGDSAGGNLAAAVALRARDEGL-PKPAGQVLIYP--GTDLRTESPSYLAREfadgpLLTRAAMDWFWRLYLP-GADRD 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 778717692  233 HPLANPFGASSMSleevNLEPILVIVGGDEMLKDRAETYAKTLSQLGKRIEYVEFDGKQHGFF 295
Cdd:pfam07859 150 DPLASPLFASDLS----GLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHGFH 208
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
57-315 1.12e-40

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 141.16  E-value: 1.12e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778717692  57 RLYKPAPSTTsspttnkKLPILFFFHGGGFCVGSRSwpNSHNCCVRLALGLGALVIAPDYRLAPEHRLPAAVEDGAKAIE 136
Cdd:COG0657    2 DVYRPAGAKG-------PLPVVVYFHGGGWVSGSKD--THDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALR 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778717692 137 WVSKAGKldewiEESGDLQRVFVMGDSSGGNIAHHLAVRIGTENEKfGVRGFVLMAPffggvgrtkseegpaeqFFDLEA 216
Cdd:COG0657   73 WLRANAA-----ELGIDPDRIAVAGDSAGGHLAAALALRARDRGGP-RPAAQVLIYP-----------------VLDLTA 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778717692 217 ldrfwrlslpigedrdHPLANPFGassmsleevNLEPILVIVGGDEMLKDRAETYAKTLSQLGKRIEYVEFDGKQHGFFT 296
Cdd:COG0657  130 ----------------SPLRADLA---------GLPPTLIVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHGFGL 184

                        250
                 ....*....|....*....
gi 778717692 297 NSQDTQlAHQVIAIIKKFM 315
Cdd:COG0657  185 LAGLPE-ARAALAEIAAFL 202
PRK10162 PRK10162
acetyl esterase;
57-294 1.21e-17

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 81.69  E-value: 1.21e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778717692  57 RLYKPAPSTTSspttnkklpILFFFHGGGFCVGSRswpNSHNCCVR-LALGLGALVIAPDYRLAPEHRLPAAVEDGAKAI 135
Cdd:PRK10162  72 RLYYPQPDSQA---------TLFYLHGGGFILGNL---DTHDRIMRlLASYSGCTVIGIDYTLSPEARFPQAIEEIVAVC 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778717692 136 EWVSKAGkldewiEESG-DLQRVFVMGDSSGGNI--AHHLAVRigtenEKFGVRGFVL-MAPFFGGVGRTKSEE----GP 207
Cdd:PRK10162 140 CYFHQHA------EDYGiNMSRIGFAGDSAGAMLalASALWLR-----DKQIDCGKVAgVLLWYGLYGLRDSVSrrllGG 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778717692 208 AEQFFDLEALDRFWRLSLPIGEDRDHPLANPFGAssmSLEEvNLEPILVIVGGDEMLKDRAETYAKTLSQLGKRIEYVEF 287
Cdd:PRK10162 209 VWDGLTQQDLQMYEEAYLSNDADRESPYYCLFNN---DLTR-DVPPCFIAGAEFDPLLDDSRLLYQTLAAHQQPCEFKLY 284


                 ....*..
gi 778717692 288 DGKQHGF 294
Cdd:PRK10162 285 PGTLHAF 291
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 54-172 1.03e-07

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: 53.10  E-value: 1.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778717692  54 LHLRLYKPAPsttssPTTNKKLPILFFFHGGGFCVGSRSWPNSHNccvRLALGLGALVIAPDYRLAP-------EHRLP- 125
Cdd:cd00312   79 LYLNVYTPKN-----TKPGNSLPVMVWIHGGGFMFGSGSLYPGDG---LAREGDNVIVVSINYRLGVlgflstgDIELPg 150

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 778717692 126 -AAVEDGAKAIEWVSKA----GkldewieesGDLQRVFVMGDSSGGNIAHHL 172
Cdd:cd00312  151 nYGLKDQRLALKWVQDNiaafG---------GDPDSVTIFGESAGGASVSLL 193
 
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.
 78-295 5.66e-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: 219.00  E-value: 5.66e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778717692   78 LFFFHGGGFCVGSRSWPnsHNCCVRLALGLGALVIAPDYRLAPEHRLPAAVEDGAKAIEWVSKAGKldewiEESGDLQRV 157
Cdd:pfam07859   1 LVYFHGGGFVLGSADTH--DRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAA-----ELGADPSRI 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778717692  158 FVMGDSSGGNIAHHLAVRIGTENEkFGVRGFVLMAPffGGVGRTKSEEGPAEQ-----FFDLEALDRFWRLSLPiGEDRD 232
Cdd:pfam07859  74 AVAGDSAGGNLAAAVALRARDEGL-PKPAGQVLIYP--GTDLRTESPSYLAREfadgpLLTRAAMDWFWRLYLP-GADRD 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 778717692  233 HPLANPFGASSMSleevNLEPILVIVGGDEMLKDRAETYAKTLSQLGKRIEYVEFDGKQHGFF 295
Cdd:pfam07859 150 DPLASPLFASDLS----GLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHGFH 208
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
57-315 1.12e-40

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 141.16  E-value: 1.12e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778717692  57 RLYKPAPSTTsspttnkKLPILFFFHGGGFCVGSRSwpNSHNCCVRLALGLGALVIAPDYRLAPEHRLPAAVEDGAKAIE 136
Cdd:COG0657    2 DVYRPAGAKG-------PLPVVVYFHGGGWVSGSKD--THDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALR 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778717692 137 WVSKAGKldewiEESGDLQRVFVMGDSSGGNIAHHLAVRIGTENEKfGVRGFVLMAPffggvgrtkseegpaeqFFDLEA 216
Cdd:COG0657   73 WLRANAA-----ELGIDPDRIAVAGDSAGGHLAAALALRARDRGGP-RPAAQVLIYP-----------------VLDLTA 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778717692 217 ldrfwrlslpigedrdHPLANPFGassmsleevNLEPILVIVGGDEMLKDRAETYAKTLSQLGKRIEYVEFDGKQHGFFT 296
Cdd:COG0657  130 ----------------SPLRADLA---------GLPPTLIVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHGFGL 184

                        250
                 ....*....|....*....
gi 778717692 297 NSQDTQlAHQVIAIIKKFM 315
Cdd:COG0657  185 LAGLPE-ARAALAEIAAFL 202
PRK10162 PRK10162
acetyl esterase;
57-294 1.21e-17

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 81.69  E-value: 1.21e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778717692  57 RLYKPAPSTTSspttnkklpILFFFHGGGFCVGSRswpNSHNCCVR-LALGLGALVIAPDYRLAPEHRLPAAVEDGAKAI 135
Cdd:PRK10162  72 RLYYPQPDSQA---------TLFYLHGGGFILGNL---DTHDRIMRlLASYSGCTVIGIDYTLSPEARFPQAIEEIVAVC 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778717692 136 EWVSKAGkldewiEESG-DLQRVFVMGDSSGGNI--AHHLAVRigtenEKFGVRGFVL-MAPFFGGVGRTKSEE----GP 207
Cdd:PRK10162 140 CYFHQHA------EDYGiNMSRIGFAGDSAGAMLalASALWLR-----DKQIDCGKVAgVLLWYGLYGLRDSVSrrllGG 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778717692 208 AEQFFDLEALDRFWRLSLPIGEDRDHPLANPFGAssmSLEEvNLEPILVIVGGDEMLKDRAETYAKTLSQLGKRIEYVEF 287
Cdd:PRK10162 209 VWDGLTQQDLQMYEEAYLSNDADRESPYYCLFNN---DLTR-DVPPCFIAGAEFDPLLDDSRLLYQTLAAHQQPCEFKLY 284


                 ....*..
gi 778717692 288 DGKQHGF 294
Cdd:PRK10162 285 PGTLHAF 291
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
54-315 3.27e-14

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 70.82  E-value: 3.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778717692  54 LHLRLYKPAPsttsspttNKKLPILFFFHGGGfcvGSRSWPNSHNccVRLALGLGALVIAPDYRLAPEHR---LPAAVED 130
Cdd:COG1506   10 LPGWLYLPAD--------GKKYPVVVYVHGGP---GSRDDSFLPL--AQALASRGYAVLAPDYRGYGESAgdwGGDEVDD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778717692 131 GAKAIEWVSKAGKLDEwieesgdlQRVFVMGDSSGGniahHLAVRIGTENEKFgVRGFVLMAPF--FGGVGRTKSEEGPA 208
Cdd:COG1506   77 VLAAIDYLAARPYVDP--------DRIGIYGHSYGG----YMALLAAARHPDR-FKAAVALAGVsdLRSYYGTTREYTER 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778717692 209 EQFFDLEALDRFWRLSlpigedrdhPLANpfgassmsLEEVNlEPILVIVGGDemlkDR------AETYAKTLSQLGKRI 282
Cdd:COG1506  144 LMGGPWEDPEAYAARS---------PLAY--------ADKLK-TPLLLIHGEA----DDrvppeqAERLYEALKKAGKPV 201

                        250       260       270
                 ....*....|....*....|....*....|...
gi 778717692 283 EYVEFDGKQHGfFTNSQDTQLAHQVIAIIKKFM 315
Cdd:COG1506  202 ELLVYPGEGHG-FSGAGAPDYLERILDFLDRHL 233
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
 56-180 4.15e-12

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: 64.51  E-value: 4.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778717692   56 LRLYKPapsttssPTTNKKLPILFFFHGGGFCVGSRSWPNSHNCCVRLAL-GLGALVIAPDYRLAPEHRLPAAVEDGAKA 134
Cdd:pfam20434   1 LDIYLP-------KNAKGPYPVVIWIHGGGWNSGDKEADMGFMTNTVKALlKAGYAVASINYRLSTDAKFPAQIQDVKAA 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 778717692  135 IEWV-SKAGKLdewieeSGDLQRVFVMGDSSGGniahHLAVRIGTEN 180
Cdd:pfam20434  74 IRFLrANAAKY------GIDTNKIALMGFSAGG----HLALLAGLSN 110
Say1_Mug180 pfam10340
Steryl acetyl hydrolase; This entry includes budding yeast steryl acetyl hydrolase 1 (Say1) ...
 66-280 6.55e-08

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: 53.30  E-value: 6.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778717692   66 TSSPTTNkklPILFFFHGGGFCVGSRSWPNSHNCCVRLALGLGALVIaPDYRLApehrlpAAVEDGAKAIEWVSKAGKLD 145
Cdd:pfam10340 116 TFDPKVD---PILLYYHGGGFALKLIPVTLVFLNNLGKYFPDMAILV-SDYTVT------ANCPQSYTYPLQVLQCLAVY 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778717692  146 EWIEESGDLQRVFVMGDSSGGNIAHHLAVRIGTENEKFGVRGFVLMAP-----FFGGVGRTKSEEGPAEQFFDLEALDRF 220
Cdd:pfam10340 186 DYLTLTKGCKNVTLMGDSAGGNLVLNILLYLHKCNKVVLPKKAIAISPwlnltDRNEKEKEYMKANDKLDGLCYKGLNMF 265

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 778717692  221 WRLSLPIGEDRDHPLANPFGASSMSLEEVNLEPI------LVIVGGDEMLKDRAETYAKTLSQLGK 280
Cdd:pfam10340 266 GKLYVPNVEPEESLFTDPFVNIEMNFDIETWSKIlekcklLITYGDDEILSDQIKSFIDKISELKA 331
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 54-172 1.03e-07

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: 53.10  E-value: 1.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778717692  54 LHLRLYKPAPsttssPTTNKKLPILFFFHGGGFCVGSRSWPNSHNccvRLALGLGALVIAPDYRLAP-------EHRLP- 125
Cdd:cd00312   79 LYLNVYTPKN-----TKPGNSLPVMVWIHGGGFMFGSGSLYPGDG---LAREGDNVIVVSINYRLGVlgflstgDIELPg 150

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 778717692 126 -AAVEDGAKAIEWVSKA----GkldewieesGDLQRVFVMGDSSGGNIAHHL 172
Cdd:cd00312  151 nYGLKDQRLALKWVQDNiaafG---------GDPDSVTIFGESAGGASVSLL 193
Fes COG2382
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];
35-289 2.53e-06

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


Pssm-ID: 441948 [Multi-domain]  Cd Length: 314  Bit Score: 48.31  E-value: 2.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778717692  35 LTLDSSVLFRDVlyqpshalHLRLYKPApsttSSPTTNKKLPILFFFHGGGFcvGSRSWPNSHnccvRLALGLGAL---- 110
Cdd:COG2382   84 VTYPSKALGRTR--------RVWVYLPP----GYDNPGKKYPVLYLLDGGGG--DEQDWFDQG----RLPTILDNLiaag 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778717692 111 ------VIAPDYRlAPEHRLPAAvEDGAKAIEWVskagkLDE---WIEE----SGDLQRVFVMGDSSGGNIAHHLAVRig 177
Cdd:COG2382  146 kippmiVVMPDGG-DGGDRGTEG-PGNDAFERFL-----AEElipFVEKnyrvSADPEHRAIAGLSMGGLAALYAALR-- 216

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778717692 178 teN-EKFGvrGFVLMAPFFGGVGRTKSEEGPAEQFfdlealdrfwrlslpigedRDHPLANPFgassmsleevnlePILV 256
Cdd:COG2382  217 --HpDLFG--YVGSFSGSFWWPPGDADRGGWAELL-------------------AAGAPKKPL-------------RFYL 260

                        250       260       270
                 ....*....|....*....|....*....|...
gi 778717692 257 IVGGDEMLKDRAETYAKTLSQLGKRIEYVEFDG 289
Cdd:COG2382  261 DVGTEDDLLEANRALAAALKAKGYDVEYREFPG 293
COesterase pfam00135
Carboxylesterase family;
54-170 9.53e-06

Carboxylesterase family;


Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 46.92  E-value: 9.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778717692   54 LHLRLYKPAPSTTSspttNKKLPILFFFHGGGFCVGSRSW--PNShnccvrLALGLGALVIAPDYRLAP--------EHr 123
Cdd:pfam00135  86 LYLNVYTPKELKEN----KNKLPVMVWIHGGGFMFGSGSLydGSY------LAAEGDVIVVTINYRLGPlgflstgdDE- 154

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 778717692  124 LP--AAVEDGAKAIEWVSKA----GkldewieesGDLQRVFVMGDSSGGNIAH 170
Cdd:pfam00135 155 APgnYGLLDQVLALRWVQENiasfG---------GDPNRVTLFGESAGAASVS 198
PnbA COG2272
Carboxylesterase type B [Lipid transport and metabolism];
65-173 3.86e-05

Carboxylesterase type B [Lipid transport and metabolism];


Pssm-ID: 441873  Cd Length: 500  Bit Score: 44.88  E-value: 3.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778717692  65 TTSSPTTNKKLPILFFFHGGGFCVGSRSWPNSHncCVRLALGlGALVIAPDYRL------------APEHRLPA--AVED 130
Cdd:COG2272   95 WTPALAAGAKLPVMVWIHGGGFVSGSGSEPLYD--GAALARR-GVVVVTINYRLgalgflalpalsGESYGASGnyGLLD 171

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 778717692 131 GAKAIEWVSK--A--GkldewieesGDLQRVFVMGDSSGG-NIAHHLA 173
Cdd:COG2272  172 QIAALRWVRDniAafG---------GDPDNVTIFGESAGAaSVAALLA 210
YpfH COG0400
Predicted esterase [General function prediction only];
76-317 4.43e-05

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 43.74  E-value: 4.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778717692  76 PILFFFHGGGfcvGSrswPNSHnccVRLALGL---GALVIAPD------------YRLAPEHRLPAAvEDGAKAIEWVSK 140
Cdd:COG0400    6 PLVVLLHGYG---GD---EEDL---LPLAPELalpGAAVLAPRapvpegpggrawFDLSFLEGREDE-EGLAAAAEALAA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778717692 141 AgkLDEWIEESG-DLQRVFVMGDSSGGNIAHHLAVRigtenEKFGVRGFVLMAPFFggvgrtkseegpaeqffdlealdr 219
Cdd:COG0400   76 F--IDELEARYGiDPERIVLAGFSQGAAMALSLALR-----RPELLAGVVALSGYL------------------------ 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778717692 220 fwrLSLPIGEDRDHPLANPfgassmsleevnlePILVIVGG-DEML-KDRAETYAKTLSQLGKRIEYVEFDGkQHGfftn 297
Cdd:COG0400  125 ---PGEEALPAPEAALAGT--------------PVFLAHGTqDPVIpVERAREAAEALEAAGADVTYREYPG-GHE---- 182

                        250       260
                 ....*....|....*....|
gi 778717692 298 sqdtqLAHQVIAIIKKFMLH 317
Cdd:COG0400  183 -----ISPEELADARAWLAE 197
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
108-315 5.01e-05

Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 43.78  E-value: 5.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778717692 108 GALVIAPDYrlaPEHRLPAAVEDGAKAIEWVSKAGKLDEWIEESGDlqRVFVMGDSSGGNIAHHLAVRIGtenekfGVRG 187
Cdd:COG1647   42 GYTVYAPRL---PGHGTSPEDLLKTTWEDWLEDVEEAYEILKAGYD--KVIVIGLSMGGLLALLLAARYP------DVAG 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778717692 188 FVLMAPFFggvgRTKSEEGPAEQFfdLEALDRFWRLslpIGEDRDHPLANPFGASSMSLEEV------------NLE--- 252
Cdd:COG1647  111 LVLLSPAL----KIDDPSAPLLPL--LKYLARSLRG---IGSDIEDPEVAEYAYDRTPLRALaelqrlirevrrDLPkit 181

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 778717692 253 -PILVIVGG-DEMLKDR-AETYAKTLSqlGKRIEYVEFDGKQHgFFTNSQDtqlAHQVIAIIKKFM 315
Cdd:COG1647  182 aPTLIIQSRkDEVVPPEsARYIYERLG--SPDKELVWLEDSGH-VITLDKD---REEVAEEILDFL 241
Chlorophyllase2 pfam12740
Chlorophyllase enzyme; This family consists of several chlorophyllase and chlorophyllase-2 (EC: ...
 61-183 1.21e-04

Chlorophyllase enzyme; This family consists of several chlorophyllase and chlorophyllase-2 (EC:3.1.1.14) enzymes. Chlorophyllase (Chlase) is the first enzyme involved in chlorophyll (Chl) degradation and catalyzes the hydrolysis of an ester bond to yield chlorophyllide and phytol. The family includes both plant and Amphioxus members.


Pssm-ID: 432755  Cd Length: 254  Bit Score: 42.69  E-value: 1.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778717692   61 PAPSTTSSPTTNKKLPILFFFHggGFCVGSRSWPN------SHnccvrlalglGALVIAPD-YRLAPehRLPAAVEDGAK 133
Cdd:pfam12740   3 PKPLLVFTPTEAGTYPVLLFLH--GYLLYNSFYSQllqhiaSH----------GFIVVAPQlYLVAG--PDGDEIKSAAK 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 778717692  134 AIEWVSKagKLDEWIEES--GDLQRVFVMGDSSGGNIAHHLAVRIGTENEKF 183
Cdd:pfam12740  69 VANWLSN--GLQHVLPEGvePDLSKLALSGHSRGGKTAFALALGHAKTSLKF 118
COG4099 COG4099
Predicted peptidase [General function prediction only];
54-175 1.46e-04

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 42.26  E-value: 1.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778717692  54 LHLRLYKPApsttsSPTTNKKLPILFFFHGGG---------FCVGSRSWPNSHNccvrlALGLGALVIAPDYRLAPEHRL 124
Cdd:COG4099   33 LPYRLYLPK-----GYDPGKKYPLVLFLHGAGergtdnekqLTHGAPKFINPEN-----QAKFPAIVLAPQCPEDDYWSD 102

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 778717692 125 PAAVEDGAKAIEWVSKAGKLDEwieesgdlQRVFVMGDSSGGNIAHHLAVR 175
Cdd:COG4099  103 TKALDAVLALLDDLIAEYRIDP--------DRIYLTGLSMGGYGTWDLAAR 145
Chlorophyllase pfam07224
Chlorophyllase; This family consists of several plant specific Chlorophyllase proteins (EC:3.1. ...
 61-179 2.16e-04

Chlorophyllase; This family consists of several plant specific Chlorophyllase proteins (EC:3.1.1.14). Chlorophyllase (Chlase) is the first enzyme involved in chlorophyll (Chl) degradation and catalyzes the hydrolysis of ester bond to yield chlorophyllide and phytol.


Pssm-ID: 254111  Cd Length: 307  Bit Score: 42.52  E-value: 2.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778717692   61 PAPSTTSSPTTNKKLPILFFFHGggFCVGSRSWPN------SHnccvrlalglGALVIAPD-YRLAPEHRLPAAVEDGAK 133
Cdd:pfam07224  32 PKPLIIITPKEAGTYPVVLFLHG--TMLSNEFYSLffnhiaSH----------GFIVVAPQlYRLFPPPSQQDEIDSAAE 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 778717692  134 AIEWVSKAgkLDEWIEES--GDLQRVFVMGDSSGGNIAHHLAVRIGTE 179
Cdd:pfam07224 100 VANWLPLG--LQVVLPTGveANLSKLALSGHSRGGKTAFALALGYSLD 145
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 76-295 2.90e-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: 41.53  E-value: 2.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778717692  76 PILFFFHGGGFcvGSRSWPNshnccVRLALGLGALVIAPDYR-------LAPEHRLPAAVEDgakaiewvskagkLDEWI 148
Cdd:COG0596   24 PPVVLLHGLPG--SSYEWRP-----LIPALAAGYRVIAPDLRghgrsdkPAGGYTLDDLADD-------------LAALL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778717692 149 EESGdLQRVFVMGDSSGGNIAHHLAVRIGTEnekfgVRGFVLMAPFFGGVGRTKSEEGpaeqfFDLEALDRFWRLSlpig 228
Cdd:COG0596   84 DALG-LERVVLVGHSMGGMVALELAARHPER-----VAGLVLVDEVLAALAEPLRRPG-----LAPEALAALLRAL---- 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 778717692 229 edRDHPLANPFGASSMsleevnlePILVIVGGDEMLKDRAetYAKTLSQLGKRIEYVEFDGKQHGFF 295
Cdd:COG0596  149 --ARTDLRERLARITV--------PTLVIWGEKDPIVPPA--LARRLAELLPNAELVVLPGAGHFPP 203
PLN00021 PLN00021
chlorophyllase
 61-178 1.18e-03

chlorophyllase


Pssm-ID: 177659  Cd Length: 313  Bit Score: 40.03  E-value: 1.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778717692  61 PAPSTTSSPTTNKKLPILFFFHggGFCVGSRSWPN------SHnccvrlalglGALVIAPD-YRLAPEHRLPaAVEDGAK 133
Cdd:PLN00021  38 PKPLLVATPSEAGTYPVLLFLH--GYLLYNSFYSQllqhiaSH----------GFIVVAPQlYTLAGPDGTD-EIKDAAA 104

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 778717692 134 AIEWVSK--AGKLDEWIEesGDLQRVFVMGDSSGGNIAHHLAVRIGT 178
Cdd:PLN00021 105 VINWLSSglAAVLPEGVR--PDLSKLALAGHSRGGKTAFALALGKAA 149
 
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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