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Conserved domains on  [gi|1034670288|ref|XP_016870278|]
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alpha/beta hydrolase domain-containing protein 17B isoform X2 [Homo sapiens]

Protein Classification

alpha/beta hydrolase( domain architecture ID 11437497)

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

Gene Ontology:  GO:0016787
PubMed:  12369917|19508187

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]; ...
58-285 2.15e-43

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


:

Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 148.52  E-value: 2.15e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670288  58 YSSREKDAIECFMTRTSKGNRIACM-FVRCSPNAKY-TLLFSHGNAVDLGQMSSF---YIGLGSrincNIFSYDYSGYGA 132
Cdd:COG1073     2 FPPSDKVNKEDVTFKSRDGIKLAGDlYLPAGASKKYpAVVVAHGNGGVKEQRALYaqrLAELGF----NVLAFDYRGYGE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670288 133 SSGKPTEKNLYA--DIEAAWLALRTRYGIRPENVIIYGQSIGTVPSVDLAARYES-AAVILHSPLTSGMRVA-------- 201
Cdd:COG1073    78 SEGEPREEGSPErrDARAAVDYLRTLPGVDPERIGLLGISLGGGYALNAAATDPRvKAVILDSPFTSLEDLAaqrakear 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670288 202 ---FPDTKKTYCF-------DAFPNIDKISKITSPVLIIHGTEDEVIDFSHGLALFERCQRPVEPLWVEGAGHND--VEL 269
Cdd:COG1073   158 gayLPGVPYLPNVrlasllnDEFDPLAKIEKISRPLLFIHGEKDEAVPFYMSEDLYEAAAEPKELLIVPGAGHVDlyDRP 237
                         250
                  ....*....|....*.
gi 1034670288 270 YGQYLERLKQFVSQEL 285
Cdd:COG1073   238 EEEYFDKLAEFFKKNL 253
 
Name Accession Description Interval E-value
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
58-285 2.15e-43

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 148.52  E-value: 2.15e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670288  58 YSSREKDAIECFMTRTSKGNRIACM-FVRCSPNAKY-TLLFSHGNAVDLGQMSSF---YIGLGSrincNIFSYDYSGYGA 132
Cdd:COG1073     2 FPPSDKVNKEDVTFKSRDGIKLAGDlYLPAGASKKYpAVVVAHGNGGVKEQRALYaqrLAELGF----NVLAFDYRGYGE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670288 133 SSGKPTEKNLYA--DIEAAWLALRTRYGIRPENVIIYGQSIGTVPSVDLAARYES-AAVILHSPLTSGMRVA-------- 201
Cdd:COG1073    78 SEGEPREEGSPErrDARAAVDYLRTLPGVDPERIGLLGISLGGGYALNAAATDPRvKAVILDSPFTSLEDLAaqrakear 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670288 202 ---FPDTKKTYCF-------DAFPNIDKISKITSPVLIIHGTEDEVIDFSHGLALFERCQRPVEPLWVEGAGHND--VEL 269
Cdd:COG1073   158 gayLPGVPYLPNVrlasllnDEFDPLAKIEKISRPLLFIHGEKDEAVPFYMSEDLYEAAAEPKELLIVPGAGHVDlyDRP 237
                         250
                  ....*....|....*.
gi 1034670288 270 YGQYLERLKQFVSQEL 285
Cdd:COG1073   238 EEEYFDKLAEFFKKNL 253
PHA02857 PHA02857
monoglyceride lipase; Provisional
66-265 2.39e-09

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 56.82  E-value: 2.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670288  66 IECFMTrtSKGNRIACMFVRCSPNAKYTLLFSHGNavdlGQMSSFYIGLG---SRINCNIFSYDYSGYGASSGKP---TE 139
Cdd:PHA02857    2 ANCMFN--LDNDYIYCKYWKPITYPKALVFISHGA----GEHSGRYEELAeniSSLGILVFSHDHIGHGRSNGEKmmiDD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670288 140 KNLYA-DIEAAWLALRTRYGIRPenVIIYGQSIGTVPSVDLAARYES--AAVILHSPLTSGMRVAFPDTKKTYCFDAFP- 215
Cdd:PHA02857   76 FGVYVrDVVQHVVTIKSTYPGVP--VFLLGHSMGATISILAAYKNPNlfTAMILMSPLVNAEAVPRLNLLAAKLMGIFYp 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670288 216 --------------NID---------------------------------KISKITSPVLIIHGTEDEVIDFSHGLALFE 248
Cdd:PHA02857  154 nkivgklcpesvsrDMDevykyqydplvnhekikagfasqvlkatnkvrkIIPKIKTPILILQGTNNEISDVSGAYYFMQ 233
                         250
                  ....*....|....*..
gi 1034670288 249 RCQRPVEPLWVEGAGHN 265
Cdd:PHA02857  234 HANCNREIKIYEGAKHH 250
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
88-264 2.56e-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: 2.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670288  88 PNAKYTLLFSHGnavdLGQMSSFYIGLGSRIN-CNI--FSYDYSGYGASSGK----PTEKNLYADIEAAWLALRTRYGIR 160
Cdd:pfam12146   1 GEPRAVVVLVHG----LGEHSGRYAHLADALAaQGFavYAYDHRGHGRSDGKrghvPSFDDYVDDLDTFVDKIREEHPGL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670288 161 PenVIIYGQSIGTVPSVDLAARYES--AAVILHSP--------LTSGMRVA-------FPD------TKKTYC------- 210
Cdd:pfam12146  77 P--LFLLGHSMGGLIAALYALRYPDkvDGLILSAPalkikpylAPPILKLLakllgklFPRlrvpnnLLPDSLsrdpevv 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034670288 211 --FDAFPNI-DKIS-------------------KITSPVLIIHGTEDEVIDFSHGLALFERCQRP-VEPLWVEGAGH 264
Cdd:pfam12146 155 aaYAADPLVhGGISartlyelldagerllrraaAITVPLLLLHGGADRVVDPAGSREFYERAGSTdKTLKLYPGLYH 231
 
Name Accession Description Interval E-value
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
58-285 2.15e-43

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 148.52  E-value: 2.15e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670288  58 YSSREKDAIECFMTRTSKGNRIACM-FVRCSPNAKY-TLLFSHGNAVDLGQMSSF---YIGLGSrincNIFSYDYSGYGA 132
Cdd:COG1073     2 FPPSDKVNKEDVTFKSRDGIKLAGDlYLPAGASKKYpAVVVAHGNGGVKEQRALYaqrLAELGF----NVLAFDYRGYGE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670288 133 SSGKPTEKNLYA--DIEAAWLALRTRYGIRPENVIIYGQSIGTVPSVDLAARYES-AAVILHSPLTSGMRVA-------- 201
Cdd:COG1073    78 SEGEPREEGSPErrDARAAVDYLRTLPGVDPERIGLLGISLGGGYALNAAATDPRvKAVILDSPFTSLEDLAaqrakear 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670288 202 ---FPDTKKTYCF-------DAFPNIDKISKITSPVLIIHGTEDEVIDFSHGLALFERCQRPVEPLWVEGAGHND--VEL 269
Cdd:COG1073   158 gayLPGVPYLPNVrlasllnDEFDPLAKIEKISRPLLFIHGEKDEAVPFYMSEDLYEAAAEPKELLIVPGAGHVDlyDRP 237
                         250
                  ....*....|....*.
gi 1034670288 270 YGQYLERLKQFVSQEL 285
Cdd:COG1073   238 EEEYFDKLAEFFKKNL 253
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
72-285 4.74e-27

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 105.10  E-value: 4.74e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670288  72 RTSKGNRIACMFVRCSPNAKY-TLLFSHGNAvdlGQMSSFYIGLGSRIN---CNIFSYDYSGYGASSGKPTEKNlYADIE 147
Cdd:COG1506     3 KSADGTTLPGWLYLPADGKKYpVVVYVHGGP---GSRDDSFLPLAQALAsrgYAVLAPDYRGYGESAGDWGGDE-VDDVL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670288 148 AAWLALRTRYGIRPENVIIYGQSIGTVPSVDLAARYES--AAVILHSPLTS-----------GMRVAFPDTKKTYCFDAF 214
Cdd:COG1506    79 AAIDYLAARPYVDPDRIGIYGHSYGGYMALLAAARHPDrfKAAVALAGVSDlrsyygttreyTERLMGGPWEDPEAYAAR 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034670288 215 PNIDKISKITSPVLIIHGTEDEVIDFSHGLALFERCQR---PVEPLWVEGAGHNDV-ELYGQYLERLKQFVSQEL 285
Cdd:COG1506   159 SPLAYADKLKTPLLLIHGEADDRVPPEQAERLYEALKKagkPVELLVYPGEGHGFSgAGAPDYLERILDFLDRHL 233
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
72-283 2.37e-23

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 95.07  E-value: 2.37e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670288  72 RTSKGNRIACMFVRCSPNAKYTLLFSHGNAVDLGQMSSFYIGLGSRiNCNIFSYDYSGYGASSGK----PTEKNLYADIE 147
Cdd:COG2267     9 PTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAA-GYAVLAFDLRGHGRSDGPrghvDSFDDYVDDLR 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670288 148 AAWLALRTRYGIRpenVIIYGQSIGTVPSVDLAARYES--AAVILHSPLtsgmRVAFPDTKKTYCF-DAFPNIDKISKIT 224
Cdd:COG2267    88 AALDALRARPGLP---VVLLGHSMGGLIALLYAARYPDrvAGLVLLAPA----YRADPLLGPSARWlRALRLAEALARID 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034670288 225 SPVLIIHGTEDEVIDFSHGLALFERCQRPVEPLWVEGAGHNDV--ELYGQYLERLKQFVSQ 283
Cdd:COG2267   161 VPVLVLHGGADRVVPPEAARRLAARLSPDVELVLLPGARHELLnePAREEVLAAILAWLER 221
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
82-283 2.17e-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: 2.17e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670288  82 MFVRCSPNAKYTLLFSHGNAVDLGQMSSFYIGLGSRinCNIFSYDYSGYGASSgKPTEKNLYADIEAAWLALRTRYGIRP 161
Cdd:COG0596    14 LHYREAGPDGPPVVLLHGLPGSSYEWRPLIPALAAG--YRVIAPDLRGHGRSD-KPAGGYTLDDLADDLAALLDALGLER 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670288 162 enVIIYGQSIGTVPSVDLAARYES--AAVILHSPLTSGMRVAFPDTKKTY-----CFDAFPNID---KISKITSPVLIIH 231
Cdd:COG0596    91 --VVLVGHSMGGMVALELAARHPErvAGLVLVDEVLAALAEPLRRPGLAPealaaLLRALARTDlreRLARITVPTLVIW 168
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034670288 232 GTEDEVIDFSHGLALFERCQRpVEPLWVEGAGHN-DVELYGQYLERLKQFVSQ 283
Cdd:COG0596   169 GEKDPIVPPALARRLAELLPN-AELVVLPGAGHFpPLEQPEAFAAALRDFLAR 220
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
88-283 4.34e-14

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 70.36  E-value: 4.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670288  88 PNAKYTLLFSHGNAVDLGQMSSfyigLGSRIN---CNIFSYDYSGYGASSG---KPTEKNLYADIEAAWLALRTRYgirp 161
Cdd:COG1647    12 EGGRKGVLLLHGFTGSPAEMRP----LAEALAkagYTVYAPRLPGHGTSPEdllKTTWEDWLEDVEEAYEILKAGY---- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670288 162 ENVIIYGQSIGTVPSVDLAARYES-AAVILHSP-----------------LTSGMRVAFPDTKKT----YCFDAFPNI-- 217
Cdd:COG1647    84 DKVIVIGLSMGGLLALLLAARYPDvAGLVLLSPalkiddpsapllpllkyLARSLRGIGSDIEDPevaeYAYDRTPLRal 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670288 218 -----------DKISKITSPVLIIHGTEDEVIDFSHGLALFERC-QRPVEPLWVEGAGH---NDVELyGQYLERLKQFVS 282
Cdd:COG1647   164 aelqrlirevrRDLPKITAPTLIIQSRKDEVVPPESARYIYERLgSPDKELVWLEDSGHvitLDKDR-EEVAEEILDFLE 242

                  .
gi 1034670288 283 Q 283
Cdd:COG1647   243 R 243
YpfH COG0400
Predicted esterase [General function prediction only];
88-285 2.91e-10

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 58.38  E-value: 2.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670288  88 PNAKYTLLFSHGNAVDLGQMSSFYiglgsRINCNIFSYDYSGYGASSgkpteknlyADIEAAWLALRTRYGIRPENVIIY 167
Cdd:COG0400    29 ALPGAAVLAPRAPVPEGPGGRAWF-----DLSFLEGREDEEGLAAAA---------EALAAFIDELEARYGIDPERIVLA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670288 168 GQSIGTVPSVDLAARYES--AAVILHSPltsgmRVAFPDTKKTYCFDAfpnidkiSKItsPVLIIHGTEDEVIDFSHGLA 245
Cdd:COG0400    95 GFSQGAAMALSLALRRPEllAGVVALSG-----YLPGEEALPAPEAAL-------AGT--PVFLAHGTQDPVIPVERARE 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1034670288 246 LFERCQR---PVEPLWVEGaGHndvELYGQYLERLKQFVSQEL 285
Cdd:COG0400   161 AAEALEAagaDVTYREYPG-GH---EISPEELADARAWLAERL 199
PHA02857 PHA02857
monoglyceride lipase; Provisional
66-265 2.39e-09

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 56.82  E-value: 2.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670288  66 IECFMTrtSKGNRIACMFVRCSPNAKYTLLFSHGNavdlGQMSSFYIGLG---SRINCNIFSYDYSGYGASSGKP---TE 139
Cdd:PHA02857    2 ANCMFN--LDNDYIYCKYWKPITYPKALVFISHGA----GEHSGRYEELAeniSSLGILVFSHDHIGHGRSNGEKmmiDD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670288 140 KNLYA-DIEAAWLALRTRYGIRPenVIIYGQSIGTVPSVDLAARYES--AAVILHSPLTSGMRVAFPDTKKTYCFDAFP- 215
Cdd:PHA02857   76 FGVYVrDVVQHVVTIKSTYPGVP--VFLLGHSMGATISILAAYKNPNlfTAMILMSPLVNAEAVPRLNLLAAKLMGIFYp 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670288 216 --------------NID---------------------------------KISKITSPVLIIHGTEDEVIDFSHGLALFE 248
Cdd:PHA02857  154 nkivgklcpesvsrDMDevykyqydplvnhekikagfasqvlkatnkvrkIIPKIKTPILILQGTNNEISDVSGAYYFMQ 233
                         250
                  ....*....|....*..
gi 1034670288 249 RCQRPVEPLWVEGAGHN 265
Cdd:PHA02857  234 HANCNREIKIYEGAKHH 250
COG2945 COG2945
Alpha/beta superfamily hydrolase [General function prediction only];
129-285 5.10e-09

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


Pssm-ID: 442188 [Multi-domain]  Cd Length: 201  Bit Score: 54.78  E-value: 5.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670288 129 GYGASSGK----PTEKnlyADIEAA--WLalRTRYgirPENVIIYGQSIGTvpsvDLAARY-----ESAAVILHSPLTSg 197
Cdd:COG2945    65 GVGRSEGEfdegRGEL---DDAAAAldWL--RAQN---PLPLWLAGFSFGA----YVALQLamrlpEVEGLILVAPPVN- 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670288 198 mRVAFPDtkktycfdafpnidkISKITSPVLIIHGTEDEVIDFSHGLALFERCQRPVEPLWVEGAGHndveLYGQYLERL 277
Cdd:COG2945   132 -RYDFSF---------------LAPCPAPTLVIHGEQDEVVPPAEVLDWARPLSPPLPVVVVPGADH----FFHGKLDEL 191

                  ....*...
gi 1034670288 278 KQFVSQEL 285
Cdd:COG2945   192 KELVARYL 199
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
88-264 2.56e-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: 2.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670288  88 PNAKYTLLFSHGnavdLGQMSSFYIGLGSRIN-CNI--FSYDYSGYGASSGK----PTEKNLYADIEAAWLALRTRYGIR 160
Cdd:pfam12146   1 GEPRAVVVLVHG----LGEHSGRYAHLADALAaQGFavYAYDHRGHGRSDGKrghvPSFDDYVDDLDTFVDKIREEHPGL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670288 161 PenVIIYGQSIGTVPSVDLAARYES--AAVILHSP--------LTSGMRVA-------FPD------TKKTYC------- 210
Cdd:pfam12146  77 P--LFLLGHSMGGLIAALYALRYPDkvDGLILSAPalkikpylAPPILKLLakllgklFPRlrvpnnLLPDSLsrdpevv 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034670288 211 --FDAFPNI-DKIS-------------------KITSPVLIIHGTEDEVIDFSHGLALFERCQRP-VEPLWVEGAGH 264
Cdd:pfam12146 155 aaYAADPLVhGGISartlyelldagerllrraaAITVPLLLLHGGADRVVDPAGSREFYERAGSTdKTLKLYPGLYH 231
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
140-264 5.95e-08

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 52.23  E-value: 5.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670288 140 KNLYADIEAAWLALRTRYGIRPENVIIYGQS--------------------IGTVPSVDLAaRYESAAvilHSPLTSG-M 198
Cdd:pfam00326  42 QNEFDDFIAAAEYLIEQGYTDPDRLAIWGGSyggyltgaalnqrpdlfkaaVAHVPVVDWL-AYMSDT---SLPFTERyM 117
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034670288 199 RVAFPDTKKTYcFDAFPNID--KISKITSPVLIIHGTEDEVIDFSHGLALFERCQR---PVEPLWVEGAGH 264
Cdd:pfam00326 118 EWGNPWDNEEG-YDYLSPYSpaDNVKVYPPLLLIHGLLDDRVPPWQSLKLVAALQRkgvPFLLLIFPDEGH 187
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
144-264 5.92e-07

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 49.19  E-value: 5.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670288 144 ADIEAAWLALRTRYGIRPENVIIYGQSIGTVPSVDLAARYE--SAAVILHSPLtsgmrvafpdtkktycfDAFPNIDKIS 221
Cdd:COG0412    91 ADLRAALDWLKAQPEVDAGRVGVVGFCFGGGLALLAAARGPdlAAAVSFYGGL-----------------PADDLLDLAA 153
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1034670288 222 KITSPVLIIHGTEDEVIDFSHGLALFERCQR---PVEPLWVEGAGH 264
Cdd:COG0412   154 RIKAPVLLLYGEKDPLVPPEQVAALEAALAAagvDVELHVYPGAGH 199
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
145-264 8.47e-07

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 48.72  E-value: 8.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670288 145 DIEAAWLALRTR---YGIRPENVIIYGQSIG--TVPSVDLAARYES----AAVILHSPLTSgMRVAfPDTkktYCFDAFP 215
Cdd:COG0657    66 DAYAALRWLRANaaeLGIDPDRIAVAGDSAGghLAAALALRARDRGgprpAAQVLIYPVLD-LTAS-PLR---ADLAGLP 140
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034670288 216 nidkiskitsPVLIIHGTEDEVIDfsHGLALFERCQR---PVEPLWVEGAGH 264
Cdd:COG0657   141 ----------PTLIVTGEADPLVD--ESEALAAALRAagvPVELHVYPGGGH 180
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
92-198 7.22e-05

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: 43.26  E-value: 7.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670288  92 YTLLFSHGnavdLGQMSSFYIGLG---SRINCNIFSYDYSGYGASSGKPTEKNLYADIEAAWL-ALRTRYGIrpENVIIY 167
Cdd:pfam00561   1 PPVLLLHG----LPGSSDLWRKLApalARDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLeYILEALGL--EKVNLV 74
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1034670288 168 GQSIGTVPSVDLAARYES--AAVILHSPLTSGM 198
Cdd:pfam00561  75 GHSMGGLIALAYAAKYPDrvKALVLLGALDPPH 107
UPF0227 pfam05728
Uncharacterized protein family (UPF0227); Despite being classed as uncharacterized proteins, ...
159-280 2.87e-04

Uncharacterized protein family (UPF0227); Despite being classed as uncharacterized proteins, the members of this family are almost certainly enzymes that are distantly related to the pfam00561.


Pssm-ID: 283403 [Multi-domain]  Cd Length: 187  Bit Score: 40.86  E-value: 2.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670288 159 IRPENVIIYGQSIGTVPSVDLAARYESAAVIL------HSPLTSGM-RVAFPDTKKTYCFDAFPNID----KISKITSPV 227
Cdd:pfam05728  56 LGDDNPLLVGSSLGGYYATWLGFRCGLRQVLFnpavrpYENLAGKLgEQANPYTGQTYVLEEYHDIElkclEVFRLKNPD 135
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034670288 228 --LIIHGTEDEVIDFSHGLALFERCQRPVEplwvEGAGH--NDVElygQYLERLKQF 280
Cdd:pfam05728 136 rcLVLLQKGDEVLDYRRAAAHYRPYYEIVW----DGGDHkfKDFS---RHLQQIKAF 185
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
94-190 6.37e-04

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 40.15  E-value: 6.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670288  94 LLFSHGNAVDLGQMSSFyigLGSRINCniFSYDYSGYGASSGKPTEKNLYADIEAAWLALrtrygIRPENVIIYGQSIGT 173
Cdd:pfam12697   1 VVLVHGAGLSAAPLAAL---LAAGVAV--LAPDLPGHGSSSPPPLDLADLADLAALLDEL-----GAARPVVLVGHSLGG 70
                          90
                  ....*....|....*..
gi 1034670288 174 VPSVDLAARYESAAVIL 190
Cdd:pfam12697  71 AVALAAAAAALVVGVLV 87
Abhydrolase_2 pfam02230
Phospholipase/Carboxylesterase; This family consists of both phospholipases and ...
88-282 6.45e-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: 40.05  E-value: 6.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670288  88 PNAKYtlLFSHGNA--VDL---GQMSSFYiglgsrincNIFSYDYSGYGASSGKPTEKNLYADIEAAWLAlrtrYGIRPE 162
Cdd:pfam02230  41 PNIKF--IFPHGPEipVTLnggMRMPAWF---------DLVGLSPNAKEDEAGIKNSAETIEELIDAEQK----KGIPSS 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670288 163 NVIIYGQSIGtvpsvdlaaryesAAVILHSPLTSGMR----VAF-----PDTKktycfdaFPNIDKISKITSPVLIIHGT 233
Cdd:pfam02230 106 RIIIGGFSQG-------------AMLALYSALTLPLPlggiVAFsgflpLPTK-------FPSHPNLVTKKTPIFLIHGE 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034670288 234 EDEVIDFSHGLALFER---CQRPVEPLWVEGAGHndvELYGQYLERLKQFVS 282
Cdd:pfam02230 166 EDPVVPLALGKLAKEYlktSLNKVELKIYEGLAH---SICGREMQDIKKFLS 214
PRK11460 PRK11460
putative hydrolase; Provisional
94-283 4.12e-03

putative hydrolase; Provisional


Pssm-ID: 183144 [Multi-domain]  Cd Length: 232  Bit Score: 37.71  E-value: 4.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670288  94 LLFsHG---NAVDLGQMSSFY---------IGLGSrincnifsYDYSGYGA-----SSGKPTEKNLYADIEAAWLAL--- 153
Cdd:PRK11460   20 LLF-HGvgdNPVAMGEIGSWFapafpdalvVSVGG--------PEPSGNGAgrqwfSVQGITEDNRQARVAAIMPTFiet 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670288 154 ----RTRYGIRPENVIIYGQSIGTVPSVdlaaryesAAVILHSPLtSGMRVAFpdtkkTYCFDAFPniDKISKITSpVLI 229
Cdd:PRK11460   91 vrywQQQSGVGASATALIGFSQGAIMAL--------EAVKAEPGL-AGRVIAF-----SGRYASLP--ETAPTATT-IHL 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034670288 230 IHGTEDEVIDFSHGLALFERCQR---PVEPLWVEGAGHN-DVELYGQYLERLKQFVSQ 283
Cdd:PRK11460  154 IHGGEDPVIDVAHAVAAQEALISlggDVTLDIVEDLGHAiDPRLMQFALDRLRYTVPK 211
 
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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