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Conserved domains on  [gi|71988362|ref|NP_492210|]
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Alpha/beta hydrolase domain-containing protein aho-3 [Caenorhabditis elegans]

Protein Classification

alpha/beta hydrolase( domain architecture ID 11437497)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
109-303 2.60e-40

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


:

Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 141.98  E-value: 2.60e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988362 109 PNSHFTLLFSHGNAVDLGQMTSF---LYGLGFhlncNVFSYDYSGYGCSTGKPSEKNLYA--DITAAFELLKSEFGVPKE 183
Cdd:COG1073  34 SKKYPAVVVAHGNGGVKEQRALYaqrLAELGF----NVLAFDYRGYGESEGEPREEGSPErrDARAAVDYLRTLPGVDPE 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988362 184 KIILYGQSIGTVPSVDLASRE-DLAALVLHSPLMSGMRVA-----------FPG-------TTTTWCCDAFPSIEKVPRV 244
Cdd:COG1073 110 RIGLLGISLGGGYALNAAATDpRVKAVILDSPFTSLEDLAaqrakeargayLPGvpylpnvRLASLLNDEFDPLAKIEKI 189
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71988362 245 KCPTLVIHGTDDEVIDFSHGVSIYERCPTSVEPLWVPGAGHND--VELHAAYLERLRSFID 303
Cdd:COG1073 190 SRPLLFIHGEKDEAVPFYMSEDLYEAAAEPKELLIVPGAGHVDlyDRPEEEYFDKLAEFFK 250
 
Name Accession Description Interval E-value
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
109-303 2.60e-40

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 141.98  E-value: 2.60e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988362 109 PNSHFTLLFSHGNAVDLGQMTSF---LYGLGFhlncNVFSYDYSGYGCSTGKPSEKNLYA--DITAAFELLKSEFGVPKE 183
Cdd:COG1073  34 SKKYPAVVVAHGNGGVKEQRALYaqrLAELGF----NVLAFDYRGYGESEGEPREEGSPErrDARAAVDYLRTLPGVDPE 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988362 184 KIILYGQSIGTVPSVDLASRE-DLAALVLHSPLMSGMRVA-----------FPG-------TTTTWCCDAFPSIEKVPRV 244
Cdd:COG1073 110 RIGLLGISLGGGYALNAAATDpRVKAVILDSPFTSLEDLAaqrakeargayLPGvpylpnvRLASLLNDEFDPLAKIEKI 189
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71988362 245 KCPTLVIHGTDDEVIDFSHGVSIYERCPTSVEPLWVPGAGHND--VELHAAYLERLRSFID 303
Cdd:COG1073 190 SRPLLFIHGEKDEAVPFYMSEDLYEAAAEPKELLIVPGAGHVDlyDRPEEEYFDKLAEFFK 250
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
132-291 3.41e-08

Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.


Pssm-ID: 463473 [Multi-domain]  Cd Length: 238  Bit Score: 53.37  E-value: 3.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988362   132 LYGLGFHlncnVFSYDYSGYGCSTGK----PSEKNLYADITAAFELLKSEFgvPKEKIILYGQSIGTVPSVDLASR--ED 205
Cdd:pfam12146  27 LAAQGFA----VYAYDHRGHGRSDGKrghvPSFDDYVDDLDTFVDKIREEH--PGLPLFLLGHSMGGLIAALYALRypDK 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988362   206 LAALVLHSPLMSG---------------MRVAFP-------------------------------GTTTTW---CCDAFP 236
Cdd:pfam12146 101 VDGLILSAPALKIkpylappilkllaklLGKLFPrlrvpnnllpdslsrdpevvaayaadplvhgGISARTlyeLLDAGE 180
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 71988362   237 SIEK-VPRVKCPTLVIHGTDDEVIDFSHGVSIYERCP-TSVEPLWVPGAGHndvELH 291
Cdd:pfam12146 181 RLLRrAAAITVPLLLLHGGADRVVDPAGSREFYERAGsTDKTLKLYPGLYH---ELL 234
PHA02857 PHA02857
monoglyceride lipase; Provisional
139-286 1.83e-03

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 39.48  E-value: 1.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988362  139 LNCNVFSYDYSGYGCSTGKP---SEKNLYA-DITAAFELLKSEF-GVPkekIILYGQSIGTVPSVdLASRED---LAALV 210
Cdd:PHA02857  51 LGILVFSHDHIGHGRSNGEKmmiDDFGVYVrDVVQHVVTIKSTYpGVP---VFLLGHSMGATISI-LAAYKNpnlFTAMI 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988362  211 LHSPLMSGMRVAFPGTTTTWCCDAF-PSI-----------------------------------------------EKVP 242
Cdd:PHA02857 127 LMSPLVNAEAVPRLNLLAAKLMGIFyPNKivgklcpesvsrdmdevykyqydplvnhekikagfasqvlkatnkvrKIIP 206
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 71988362  243 RVKCPTLVIHGTDDEVIDFSHGVSIYERCPTSVEPLWVPGAGHN 286
Cdd:PHA02857 207 KIKTPILILQGTNNEISDVSGAYYFMQHANCNREIKIYEGAKHH 250
 
Name Accession Description Interval E-value
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
109-303 2.60e-40

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 141.98  E-value: 2.60e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988362 109 PNSHFTLLFSHGNAVDLGQMTSF---LYGLGFhlncNVFSYDYSGYGCSTGKPSEKNLYA--DITAAFELLKSEFGVPKE 183
Cdd:COG1073  34 SKKYPAVVVAHGNGGVKEQRALYaqrLAELGF----NVLAFDYRGYGESEGEPREEGSPErrDARAAVDYLRTLPGVDPE 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988362 184 KIILYGQSIGTVPSVDLASRE-DLAALVLHSPLMSGMRVA-----------FPG-------TTTTWCCDAFPSIEKVPRV 244
Cdd:COG1073 110 RIGLLGISLGGGYALNAAATDpRVKAVILDSPFTSLEDLAaqrakeargayLPGvpylpnvRLASLLNDEFDPLAKIEKI 189
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71988362 245 KCPTLVIHGTDDEVIDFSHGVSIYERCPTSVEPLWVPGAGHND--VELHAAYLERLRSFID 303
Cdd:COG1073 190 SRPLLFIHGEKDEAVPFYMSEDLYEAAAEPKELLIVPGAGHVDlyDRPEEEYFDKLAEFFK 250
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
100-303 1.23e-28

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 110.09  E-value: 1.23e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988362 100 VACTMIRPLPNSHFTLLFSHGNAVDLGQMTSF---LYGLGFHlncnVFSYDYSGYGCSTGK----PSEKNLYADITAAFE 172
Cdd:COG2267  16 LRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELaeaLAAAGYA----VLAFDLRGHGRSDGPrghvDSFDDYVDDLRAALD 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988362 173 LLKSEfgvPKEKIILYGQSIGTVPSVDLASR--EDLAALVLHSPLMsgMRVAFPGTTTTWCCDAFPsIEKVPRVKCPTLV 250
Cdd:COG2267  92 ALRAR---PGLPVVLLGHSMGGLIALLYAARypDRVAGLVLLAPAY--RADPLLGPSARWLRALRL-AEALARIDVPVLV 165
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 71988362 251 IHGTDDEVIDFSHGVSIYERCPTSVEPLWVPGAGHNDV--ELHAAYLERLRSFID 303
Cdd:COG2267 166 LHGGADRVVPPEAARRLAARLSPDVELVLLPGARHELLnePAREEVLAAILAWLE 220
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
100-303 4.45e-23

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 95.47  E-value: 4.45e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988362 100 VACTMIRPLPNSHF-TLLFSHGN----AVDLGQMTSFLYGLGFhlncNVFSYDYSGYGCSTGKPSEKNlYADITAAFELL 174
Cdd:COG1506  10 LPGWLYLPADGKKYpVVVYVHGGpgsrDDSFLPLAQALASRGY----AVLAPDYRGYGESAGDWGGDE-VDDVLAAIDYL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988362 175 KSEFGVPKEKIILYGQSIGTVPSVDLASRED--LAALVLHSPL--MSGMRVAFPGTTTTWC---------CDAFPSIEKV 241
Cdd:COG1506  85 AARPYVDPDRIGIYGHSYGGYMALLAAARHPdrFKAAVALAGVsdLRSYYGTTREYTERLMggpwedpeaYAARSPLAYA 164
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71988362 242 PRVKCPTLVIHGTDDEVIDFSHGVSIYERCPTS---VEPLWVPGAGHNDV-ELHAAYLERLRSFID 303
Cdd:COG1506 165 DKLKTPLLLIHGEADDRVPPEQAERLYEALKKAgkpVELLVYPGEGHGFSgAGAPDYLERILDFLD 230
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
114-303 4.03e-18

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: 81.59  E-value: 4.03e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988362 114 TLLFSHGNAVDLGQMTSFLYGL--GFHlncnVFSYDYSGYGCSTgKPSEKNLYADITAAFELLKSEFGVpkEKIILYGQS 191
Cdd:COG0596  25 PVVLLHGLPGSSYEWRPLIPALaaGYR----VIAPDLRGHGRSD-KPAGGYTLDDLADDLAALLDALGL--ERVVLVGHS 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988362 192 IGTVPSVDLASR--EDLAALVLHSPLMSGMR--VAFPGTTTTWCCDAFPSI------EKVPRVKCPTLVIHGTDDEVIDF 261
Cdd:COG0596  98 MGGMVALELAARhpERVAGLVLVDEVLAALAepLRRPGLAPEALAALLRALartdlrERLARITVPTLVIWGEKDPIVPP 177
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 71988362 262 SHGVSIYERCPTSvEPLWVPGAGHN-DVELHAAYLERLRSFID 303
Cdd:COG0596 178 ALARRLAELLPNA-ELVVLPGAGHFpPLEQPEAFAAALRDFLA 219
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
108-303 8.30e-14

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 69.97  E-value: 8.30e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988362 108 LPNSHFTLLFSHG---NAVDLGQMTSFLYGLGFhlncNVFSYDYSGYGCSTG---KPSEKNLYADITAAFELLKSEFgvp 181
Cdd:COG1647  11 LEGGRKGVLLLHGftgSPAEMRPLAEALAKAGY----TVYAPRLPGHGTSPEdllKTTWEDWLEDVEEAYEILKAGY--- 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988362 182 kEKIILYGQSIGTVPSVDLASR-EDLAALVLHSP--LMSGMRVAF--------------------PGTTTTWCcDAFPS- 237
Cdd:COG1647  84 -DKVIVIGLSMGGLLALLLAARyPDVAGLVLLSPalKIDDPSAPLlpllkylarslrgigsdiedPEVAEYAY-DRTPLr 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988362 238 --------IEKV----PRVKCPTLVIHGTDDEVIDFSHGVSIYERCPTS-VEPLWVPGAGH---NDVELHAAYlERLRSF 301
Cdd:COG1647 162 alaelqrlIREVrrdlPKITAPTLIIQSRKDEVVPPESARYIYERLGSPdKELVWLEDSGHvitLDKDREEVA-EEILDF 240

                ..
gi 71988362 302 ID 303
Cdd:COG1647 241 LE 242
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
165-285 9.61e-09

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 54.97  E-value: 9.61e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988362 165 ADITAAFELLKSEFGVPKEKIILYGQSIGTVPSVDLASRE-DLAALVlhsplmsgmrvAFPGTtttwcCDAFPSIEKVPR 243
Cdd:COG0412  91 ADLRAALDWLKAQPEVDAGRVGVVGFCFGGGLALLAAARGpDLAAAV-----------SFYGG-----LPADDLLDLAAR 154
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 71988362 244 VKCPTLVIHGTDDEVIDFSHGVSIYERCPTS---VEPLWVPGAGH 285
Cdd:COG0412 155 IKAPVLLLYGEKDPLVPPEQVAALEAALAAAgvdVELHVYPGAGH 199
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
132-291 3.41e-08

Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.


Pssm-ID: 463473 [Multi-domain]  Cd Length: 238  Bit Score: 53.37  E-value: 3.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988362   132 LYGLGFHlncnVFSYDYSGYGCSTGK----PSEKNLYADITAAFELLKSEFgvPKEKIILYGQSIGTVPSVDLASR--ED 205
Cdd:pfam12146  27 LAAQGFA----VYAYDHRGHGRSDGKrghvPSFDDYVDDLDTFVDKIREEH--PGLPLFLLGHSMGGLIAALYALRypDK 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988362   206 LAALVLHSPLMSG---------------MRVAFP-------------------------------GTTTTW---CCDAFP 236
Cdd:pfam12146 101 VDGLILSAPALKIkpylappilkllaklLGKLFPrlrvpnnllpdslsrdpevvaayaadplvhgGISARTlyeLLDAGE 180
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 71988362   237 SIEK-VPRVKCPTLVIHGTDDEVIDFSHGVSIYERCP-TSVEPLWVPGAGHndvELH 291
Cdd:pfam12146 181 RLLRrAAAITVPLLLLHGGADRVVDPAGSREFYERAGsTDKTLKLYPGLYH---ELL 234
YpfH COG0400
Predicted esterase [General function prediction only];
165-302 1.42e-06

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 47.98  E-value: 1.42e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988362 165 ADITAAFELLKSEFGVPKEKIILYGQSIGTVPSVDLASR--EDLAALVLHSPlmsgmrvAFPGttttwccDAFPSIEKVP 242
Cdd:COG0400  71 EALAAFIDELEARYGIDPERIVLAGFSQGAAMALSLALRrpELLAGVVALSG-------YLPG-------EEALPAPEAA 136
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71988362 243 RVKCPTLVIHGTDDEVIDFSHGVSIYERCPT---SVEPLWVPGaGHndvELHAAYLERLRSFI 302
Cdd:COG0400 137 LAGTPVFLAHGTQDPVIPVERAREAAEALEAagaDVTYREYPG-GH---EISPEELADARAWL 195
COG2945 COG2945
Alpha/beta superfamily hydrolase [General function prediction only];
165-303 2.24e-06

Alpha/beta superfamily hydrolase [General function prediction only];


Pssm-ID: 442188 [Multi-domain]  Cd Length: 201  Bit Score: 47.46  E-value: 2.24e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988362 165 ADITAAFELLKSEFGVPkekIILYGQSIGTVPSVDLASR-EDLAALVLHSPLMSGMRVAFpgttttwccdafpsiekVPR 243
Cdd:COG2945  81 DDAAAALDWLRAQNPLP---LWLAGFSFGAYVALQLAMRlPEVEGLILVAPPVNRYDFSF-----------------LAP 140
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988362 244 VKCPTLVIHGTDDEVIDFSHGVSIYERCPTSVEPLWVPGAGHNDVElhaaYLERLRSFID 303
Cdd:COG2945 141 CPAPTLVIHGEQDEVVPPAEVLDWARPLSPPLPVVVVPGADHFFHG----KLDELKELVA 196
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
115-297 9.27e-06

Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 45.93  E-value: 9.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988362   115 LLFSHGNAVDLGQMTSFLYGlgfhlNCNVFSYDYSGYGCSTGKPSEknlYADITAAFELLKSEFGVPkeKIILYGQSIGT 194
Cdd:pfam12697   1 VVLVHGAGLSAAPLAALLAA-----GVAVLAPDLPGHGSSSPPPLD---LADLADLAALLDELGAAR--PVVLVGHSLGG 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988362   195 VPSVDLASREDLAAlVLHSPLMSG------------------------------------------MRVAFPGTTTTWCC 232
Cdd:pfam12697  71 AVALAAAAAALVVG-VLVAPLAAPpgllaallallarlgaalaapawlaaeslargflddlpadaeWAAALARLAALLAA 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71988362   233 DAFPSIEKVPRVKCPTLVIHGTDDEVIDFSHGVSIYERCPTSVEplwVPGAGHNDVELHAAYLER 297
Cdd:pfam12697 150 LALLPLAAWRDLPVPVLVLAEEDRLVPELAQRLLAALAGARLVV---LPGAGHLPLDDPEEVAEA 211
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
114-219 3.85e-04

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


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 41.34  E-value: 3.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988362   114 TLLFSHGNAVDLGQMTSFLYGL---GFHlncnVFSYDYSGYGCSTgKPSEKNLYADITAA--FELLKSEFGVpkEKIILY 188
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALardGFR----VIALDLRGFGKSS-RPKAQDDYRTDDLAedLEYILEALGL--EKVNLV 74
                          90       100       110
                  ....*....|....*....|....*....|...
gi 71988362   189 GQSIGTVPSVDLASRED--LAALVLHSPLMSGM 219
Cdd:pfam00561  75 GHSMGGLIALAYAAKYPdrVKALVLLGALDPPH 107
FSH1 pfam03959
Serine hydrolase (FSH1); This is a family of serine hydrolases.
242-285 5.20e-04

Serine hydrolase (FSH1); This is a family of serine hydrolases.


Pssm-ID: 461110  Cd Length: 208  Bit Score: 40.73  E-value: 5.20e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 71988362   242 PRVKCPTLVIHGTDDEVIDFSHGVSIYERCPTSVEPLWVPGaGH 285
Cdd:pfam03959 155 DPIQTPSLHVIGELDTVVPEERSEKLAEACKNSPTVLEHPG-GH 197
Abhydrolase_2 pfam02230
Phospholipase/Carboxylesterase; This family consists of both phospholipases and ...
109-285 7.16e-04

Phospholipase/Carboxylesterase; This family consists of both phospholipases and carboxylesterases with broad substrate specificity, and is structurally related to alpha/beta hydrolases pfam00561.


Pssm-ID: 396693 [Multi-domain]  Cd Length: 217  Bit Score: 40.44  E-value: 7.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988362   109 PNSHFTLLFSHGNAVDLGqmtsFLYGLGfhlncnVFSYdYSGYGCSTGKPSEKNLYADITAAF-ELLKSEF--GVPKEKI 185
Cdd:pfam02230  39 PLPNIKFIFPHGPEIPVT----LNGGMR------MPAW-FDLVGLSPNAKEDEAGIKNSAETIeELIDAEQkkGIPSSRI 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988362   186 ILYGQSIGtvpsvdlasredlAALVLHS----PLMSGMRVAFPGttttwccdAFPSIEKVPR------VKCPTLVIHGTD 255
Cdd:pfam02230 108 IIGGFSQG-------------AMLALYSaltlPLPLGGIVAFSG--------FLPLPTKFPShpnlvtKKTPIFLIHGEE 166
                         170       180       190
                  ....*....|....*....|....*....|...
gi 71988362   256 DEVIDFSHGVSIYER---CPTSVEPLWVPGAGH 285
Cdd:pfam02230 167 DPVVPLALGKLAKEYlktSLNKVELKIYEGLAH 199
PHA02857 PHA02857
monoglyceride lipase; Provisional
139-286 1.83e-03

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 39.48  E-value: 1.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988362  139 LNCNVFSYDYSGYGCSTGKP---SEKNLYA-DITAAFELLKSEF-GVPkekIILYGQSIGTVPSVdLASRED---LAALV 210
Cdd:PHA02857  51 LGILVFSHDHIGHGRSNGEKmmiDDFGVYVrDVVQHVVTIKSTYpGVP---VFLLGHSMGATISI-LAAYKNpnlFTAMI 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988362  211 LHSPLMSGMRVAFPGTTTTWCCDAF-PSI-----------------------------------------------EKVP 242
Cdd:PHA02857 127 LMSPLVNAEAVPRLNLLAAKLMGIFyPNKivgklcpesvsrdmdevykyqydplvnhekikagfasqvlkatnkvrKIIP 206
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 71988362  243 RVKCPTLVIHGTDDEVIDFSHGVSIYERCPTSVEPLWVPGAGHN 286
Cdd:PHA02857 207 KIKTPILILQGTNNEISDVSGAYYFMQHANCNREIKIYEGAKHH 250
DLH pfam01738
Dienelactone hydrolase family;
165-308 6.24e-03

Dienelactone hydrolase family;


Pssm-ID: 396343 [Multi-domain]  Cd Length: 213  Bit Score: 37.33  E-value: 6.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988362   165 ADITAAFELLKSEFGVPKEKIILYGQSIGTVPSVDLASREDLAALVlhsplmsgmrVAFPGTTttwccdAFPSIEKVPRV 244
Cdd:pfam01738  78 DDLEAAVNYLKSQPEVSPKKVGVVGYCMGGALAVLLAAKGPLVDAA----------VGFYGVG------PEPPLIEAPDI 141
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71988362   245 KCPTLVIHGTDDEVIDFSHGVSIYERCPTSVEPL---WVPGAGHndvelhaAYLERLRSFIDMEASA 308
Cdd:pfam01738 142 KAPILFHFGEEDHFVPADSRELIEEALKAANVDHqihSYPGAGH-------AFANDSRPSYNAAAAE 201
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
166-285 7.28e-03

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 37.16  E-value: 7.28e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988362 166 DITAAFELLKS---EFGVPKEKIILYGQS--------IGTVPSVDLASRedLAALVLHSPlMSGMRVAfPgttttwccdA 234
Cdd:COG0657  66 DAYAALRWLRAnaaELGIDPDRIAVAGDSagghlaaaLALRARDRGGPR--PAAQVLIYP-VLDLTAS-P---------L 132
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 71988362 235 FPSIEKVPrvkcPTLVIHGTDDEVIDfsHGVSIYERCP---TSVEPLWVPGAGH 285
Cdd:COG0657 133 RADLAGLP----PTLIVTGEADPLVD--ESEALAAALRaagVPVELHVYPGGGH 180
 
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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