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Conserved domains on  [gi|1063723173|ref|NP_001328384|]
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alpha/beta-Hydrolases superfamily protein [Arabidopsis thaliana]

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
PubMed:  19508187|12369917|37582413

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]; ...
 43-288 3.66e-36

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


:

Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 132.35  E-value: 3.66e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723173  43 KCKRQDLELTNSRGHTLRCSHYVPSSsrEDTPLPCVIYCHGNSGCRADANEAVMVLLPSNITVFTLDFSGSGLSEGDYVS 122
Cdd:COG1073     7 KVNKEDVTFKSRDGIKLAGDLYLPAG--ASKKYPAVVVAHGNGGVKEQRALYAQRLAELGFNVLAFDYRGYGESEGEPRE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723173 123 LGWHEKDDLKTVVSYLRNSNQV--SRIGLWGRSMGAVTSLLYGAEDPSIAGMVLDSAFSNLFDLM-MELVDVYKIRLPkf 199
Cdd:COG1073    85 EGSPERRDARAAVDYLRTLPGVdpERIGLLGISLGGGYALNAAATDPRVKAVILDSPFTSLEDLAaQRAKEARGAYLP-- 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723173 200 tvkvAVQYMRRIIqkkakfnIMDLNCVKVSPKTFI-----PALFGHASGDKFIQPHHSDLILKCYAGDKNIIKFDG-DHN 273
Cdd:COG1073   163 ----GVPYLPNVR-------LASLLNDEFDPLAKIekisrPLLFIHGEKDEAVPFYMSEDLYEAAAEPKELLIVPGaGHV 231

                         250
                  ....*....|....*...
gi 1063723173 274 SS---RPQSYYDSVLVFF 288
Cdd:COG1073   232 DLydrPEEEYFDKLAEFF 249
 
Name Accession Description Interval E-value
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 43-288 3.66e-36

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 132.35  E-value: 3.66e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723173  43 KCKRQDLELTNSRGHTLRCSHYVPSSsrEDTPLPCVIYCHGNSGCRADANEAVMVLLPSNITVFTLDFSGSGLSEGDYVS 122
Cdd:COG1073     7 KVNKEDVTFKSRDGIKLAGDLYLPAG--ASKKYPAVVVAHGNGGVKEQRALYAQRLAELGFNVLAFDYRGYGESEGEPRE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723173 123 LGWHEKDDLKTVVSYLRNSNQV--SRIGLWGRSMGAVTSLLYGAEDPSIAGMVLDSAFSNLFDLM-MELVDVYKIRLPkf 199
Cdd:COG1073    85 EGSPERRDARAAVDYLRTLPGVdpERIGLLGISLGGGYALNAAATDPRVKAVILDSPFTSLEDLAaQRAKEARGAYLP-- 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723173 200 tvkvAVQYMRRIIqkkakfnIMDLNCVKVSPKTFI-----PALFGHASGDKFIQPHHSDLILKCYAGDKNIIKFDG-DHN 273
Cdd:COG1073   163 ----GVPYLPNVR-------LASLLNDEFDPLAKIekisrPLLFIHGEKDEAVPFYMSEDLYEAAAEPKELLIVPGaGHV 231

                         250
                  ....*....|....*...
gi 1063723173 274 SS---RPQSYYDSVLVFF 288
Cdd:COG1073   232 DLydrPEEEYFDKLAEFF 249
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 102-174 9.43e-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: 52.60  E-value: 9.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723173 102 NITVFTLDFSGSGLSEG---------DYVslgwhekDDLKTVVSYLRNSNQVSRIGLWGRSMGAVTSLLYGAEDP-SIAG 171
Cdd:pfam12146  31 GFAVYAYDHRGHGRSDGkrghvpsfdDYV-------DDLDTFVDKIREEHPGLPLFLLGHSMGGLIAALYALRYPdKVDG 103


                  ...
gi 1063723173 172 MVL 174
Cdd:pfam12146 104 LIL 106
PHA02857 PHA02857
monoglyceride lipase; Provisional
 53-264 1.62e-03

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 39.87  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723173  53 NSRGHTLRCSHYVPSSsredTPLPCVIYCHGNSGCRADANEAVMVLLPSNITVFTLDFSGSGLSEGDYVSL---GWHEKD 129
Cdd:PHA02857    7 NLDNDYIYCKYWKPIT----YPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIddfGVYVRD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723173 130 DLKTVVSYLRNSNQVSrIGLWGRSMGAVTSLLYGAEDPSI-AGMVLDSAFSNLFDLmmELVDVYKIRL------PKFTVK 202
Cdd:PHA02857   83 VVQHVVTIKSTYPGVP-VFLLGHSMGATISILAAYKNPNLfTAMILMSPLVNAEAV--PRLNLLAAKLmgifypNKIVGK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723173 203 VAVQYMRRIIQKKAKFNIMDLNC-------------------VKVSPKTFIPALFGHASGDK---------FIQPHHSDL 254
Cdd:PHA02857  160 LCPESVSRDMDEVYKYQYDPLVNhekikagfasqvlkatnkvRKIIPKIKTPILILQGTNNEisdvsgayyFMQHANCNR 239

                         250
                  ....*....|
gi 1063723173 255 ILKCYAGDKN 264
Cdd:PHA02857  240 EIKIYEGAKH 249
 
Name Accession Description Interval E-value
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 43-288 3.66e-36

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 132.35  E-value: 3.66e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723173  43 KCKRQDLELTNSRGHTLRCSHYVPSSsrEDTPLPCVIYCHGNSGCRADANEAVMVLLPSNITVFTLDFSGSGLSEGDYVS 122
Cdd:COG1073     7 KVNKEDVTFKSRDGIKLAGDLYLPAG--ASKKYPAVVVAHGNGGVKEQRALYAQRLAELGFNVLAFDYRGYGESEGEPRE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723173 123 LGWHEKDDLKTVVSYLRNSNQV--SRIGLWGRSMGAVTSLLYGAEDPSIAGMVLDSAFSNLFDLM-MELVDVYKIRLPkf 199
Cdd:COG1073    85 EGSPERRDARAAVDYLRTLPGVdpERIGLLGISLGGGYALNAAATDPRVKAVILDSPFTSLEDLAaQRAKEARGAYLP-- 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723173 200 tvkvAVQYMRRIIqkkakfnIMDLNCVKVSPKTFI-----PALFGHASGDKFIQPHHSDLILKCYAGDKNIIKFDG-DHN 273
Cdd:COG1073   163 ----GVPYLPNVR-------LASLLNDEFDPLAKIekisrPLLFIHGEKDEAVPFYMSEDLYEAAAEPKELLIVPGaGHV 231

                         250
                  ....*....|....*...
gi 1063723173 274 SS---RPQSYYDSVLVFF 288
Cdd:COG1073   232 DLydrPEEEYFDKLAEFF 249
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
50-288 6.10e-23

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 96.24  E-value: 6.10e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723173  50 ELTNSRGHTLRCSHYVPsssREDTPLPCVIYCHGNSGCRADANEAVMVLLPSN-ITVFTLDFSGSGLSEGDYvslGWHEK 128
Cdd:COG1506     1 TFKSADGTTLPGWLYLP---ADGKKYPVVVYVHGGPGSRDDSFLPLAQALASRgYAVLAPDYRGYGESAGDW---GGDEV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723173 129 DDLKTVVSYLRNSNQV--SRIGLWGRSMGAVTSLLYGAEDPS-IAGMVLDSAFSNLFDlMMELVDVYKIRLPKFTVKVAV 205
Cdd:COG1506    75 DDVLAAIDYLAARPYVdpDRIGIYGHSYGGYMALLAAARHPDrFKAAVALAGVSDLRS-YYGTTREYTERLMGGPWEDPE 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723173 206 QYMRRiiqkkakfnimdlncvkvSPKTFI-----PALFGHASGDKFIQPHHSDLI---LKCYAGDKNIIKFDG-DHNSSR 276
Cdd:COG1506   154 AYAAR------------------SPLAYAdklktPLLLIHGEADDRVPPEQAERLyeaLKKAGKPVELLVYPGeGHGFSG 215

                         250
                  ....*....|....
gi 1063723173 277 PQS--YYDSVLVFF 288
Cdd:COG1506   216 AGApdYLERILDFL 229
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
45-272 4.22e-15

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 73.88  E-value: 4.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723173  45 KRQDLELTNSRGHTLRCSHYVPsssrEDTPLPCVIYCHGNSGCRADANEAVMVLLPSNITVFTLDFSGSGLSEG------ 118
Cdd:COG2267     2 TRRLVTLPTRDGLRLRGRRWRP----AGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGprghvd 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723173 119 ---DYVslgwhekDDLKTVVSYLRnSNQVSRIGLWGRSMGAVTSLLYGAEDPS-IAGMVLDSAFSNLFDLMMelvdvyki 194
Cdd:COG2267    78 sfdDYV-------DDLRAALDALR-ARPGLPVVLLGHSMGGLIALLYAARYPDrVAGLVLLAPAYRADPLLG-------- 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723173 195 rlpkftvkVAVQYMR--RIIQKKAKFNimdlncvkvspktfIPALFGHASGDKFIQPHHSDLILKCYAGDKNIIKFDG-D 271
Cdd:COG2267   142 --------PSARWLRalRLAEALARID--------------VPVLVLHGGADRVVPPEAARRLAARLSPDVELVLLPGaR 199


                  .
gi 1063723173 272 H 272
Cdd:COG2267   200 H 200
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
76-272 6.45e-12

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 64.96  E-value: 6.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723173  76 PCVIYCHGNSGCRADANEAVMVLLPSNITVFTLDFSGSGLSEGDYVSLGWHE-KDDLKTVVSYLRNS-NQVSRIGLwgrS 153
Cdd:COG1647    16 KGVLLLHGFTGSPAEMRPLAEALAKAGYTVYAPRLPGHGTSPEDLLKTTWEDwLEDVEEAYEILKAGyDKVIVIGL---S 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723173 154 MGAVTSLLYGAEDPSIAGMVLDSAFSNLFDLMMELV--------------------DVYKIRLPKFTVKvAVQYMRRIIq 213
Cdd:COG1647    93 MGGLLALLLAARYPDVAGLVLLSPALKIDDPSAPLLpllkylarslrgigsdiedpEVAEYAYDRTPLR-ALAELQRLI- 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063723173 214 KKAKFNIMDLNCvkvspktfiPALFGHASGDKFIQPHHSDLILKCYAG-DKNIIKF-DGDH 272
Cdd:COG1647   171 REVRRDLPKITA---------PTLIIQSRKDEVVPPESARYIYERLGSpDKELVWLeDSGH 222
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 102-174 9.43e-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: 52.60  E-value: 9.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723173 102 NITVFTLDFSGSGLSEG---------DYVslgwhekDDLKTVVSYLRNSNQVSRIGLWGRSMGAVTSLLYGAEDP-SIAG 171
Cdd:pfam12146  31 GFAVYAYDHRGHGRSDGkrghvpsfdDYV-------DDLDTFVDKIREEHPGLPLFLLGHSMGGLIAALYALRYPdKVDG 103


                  ...
gi 1063723173 172 MVL 174
Cdd:pfam12146 104 LIL 106
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 78-199 2.13e-07

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: 51.35  E-value: 2.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723173  78 VIYCHGNSGCRaDANEAVMVLLPSNI-TVFTLDFSGSGLSEGdyvSLGWHE--KDDLKTVVSYLRNSNQVSRIGLWGRSM 154
Cdd:pfam00561   3 VLLLHGLPGSS-DLWRKLAPALARDGfRVIALDLRGFGKSSR---PKAQDDyrTDDLAEDLEYILEALGLEKVNLVGHSM 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1063723173 155 GAVTSLLYGAEDPS-IAGMVLDSAFSNLFDLmMELVDVYKIRLPKF 199
Cdd:pfam00561  79 GGLIALAYAAKYPDrVKALVLLGALDPPHEL-DEADRFILALFPGF 123
Axe1 COG3458
Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, ...
 21-191 4.83e-06

Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442681 [Multi-domain]  Cd Length: 318  Bit Score: 47.88  E-value: 4.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723173  21 PPRAEYDPdqylweKEFSLGGTKCkrQDLELTNSRGHTLRCSHYVPsssREDTPLPCVIYCHGNSGCRADANEavMVLLP 100
Cdd:COG3458    39 PLDPELTP------VETGLPGVEV--YDVTFTGFGGARIYGWLLRP---KGEGPLPAVVEFHGYGGGRGLPHE--DLDWA 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723173 101 SN-ITVFTLDFSGSGLSEGD--------------YVSLGWHEKDD-------LKTV--VSYLRNSNQV--SRIGLWGRSM 154
Cdd:COG3458   106 AAgYAVLVMDTRGQGSSWGDtpdpggysggalpgYMTRGIDDPDTyyyrrvyLDAVraVDALRSLPEVdgKRIGVTGGSQ 185

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1063723173 155 GAVTSLLYGAEDPSIAGMVLDS-AFSNlFDLMMELVDV 191
Cdd:COG3458   186 GGGLALAAAALDPRVKAAAADVpFLCD-FRRALELGRA 222
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
45-171 1.74e-05

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 45.73  E-value: 1.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723173  45 KRQDLELTNSRGHTLRCSHYVPSSsreDTPLPCVIYCHGNSGcRADANEAVMVLLPS-NITVFTLD-FSGSGLSEGDYVS 122
Cdd:COG0412     2 TTETVTIPTPDGVTLPGYLARPAG---GGPRPGVVVLHEIFG-LNPHIRDVARRLAAaGYVVLAPDlYGRGGPGDDPDEA 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1063723173 123 LGWHEK-------DDLKTVVSYLRNSNQV--SRIGLWGRSMGAVTSLLYGAEDPSIAG 171
Cdd:COG0412    78 RALMGAldpellaADLRAALDWLKAQPEVdaGRVGVVGFCFGGGLALLAAARGPDLAA 135
Peptidase_S15 pfam02129
X-Pro dipeptidyl-peptidase (S15 family);
112-183 1.03e-04

X-Pro dipeptidyl-peptidase (S15 family);


Pssm-ID: 396621 [Multi-domain]  Cd Length: 264  Bit Score: 43.48  E-value: 1.03e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063723173 112 GSGLSEGDYVSLGWHEKDDLKTVVSYLRN---SNqvSRIGLWGRSMGAVTSLLYGAE-DPSIAGMVLDSAFSNLFD 183
Cdd:pfam02129  61 GTGGSEGVFTVGGPQEAADGKDVIDWLAGqpwCN--GKVGMTGISYLGTTQLAAAATgPPGLKAIAPESGISDLYD 134
AXE1 pfam05448
Acetyl xylan esterase (AXE1); This family consists of several bacterial acetyl xylan esterase ...
 24-190 4.13e-04

Acetyl xylan esterase (AXE1); This family consists of several bacterial acetyl xylan esterase proteins. Acetyl xylan esterases are enzymes that hydrolyse the ester linkages of the acetyl groups in position 2 and/or 3 of the xylose moieties of natural acetylated xylan from hardwood. These enzymes are one of the accessory enzymes which are part of the xylanolytic system, together with xylanases, beta-xylosidases, alpha-arabinofuranosidases and methylglucuronidases; these are all required for the complete hydrolysis of xylan.


Pssm-ID: 398876 [Multi-domain]  Cd Length: 316  Bit Score: 42.00  E-value: 4.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723173  24 AEYDPDQYLWEKEFSLGGTKCkrQDLELTNSRGHTLRCSHYVPSSSREdtPLPCVIYCHGNSGCRADANEavMVLLPSN- 102
Cdd:pfam05448  35 RKVDPDLELEPVDFHLPTVEC--YDLTFEGFGGARIYAWYVVPKESEE--KHPAVVHFHGYNGRRGDWHD--MLHWAAHg 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723173 103 ITVFTLDFSG-SGLSEGDYV------SLGWH-----EKD---------DLKTVVSYLRNSNQV--SRIGLWGRSMGAVTS 159
Cdd:pfam05448 109 YAVFVMDVRGqGGLSEDDPRgpkgntYKGHItrgllDREtyyyrrvflDAVRAVEIVMSFPEVdeERIVVTGGSQGGALA 188

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1063723173 160 LLYGAEDPSIAGMVLDSAFSNLFDLMMELVD 190
Cdd:pfam05448 189 LAAAALSPRIKAVVADYPFLSDFRRAWEMDL 219
PHA02857 PHA02857
monoglyceride lipase; Provisional
 53-264 1.62e-03

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 39.87  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723173  53 NSRGHTLRCSHYVPSSsredTPLPCVIYCHGNSGCRADANEAVMVLLPSNITVFTLDFSGSGLSEGDYVSL---GWHEKD 129
Cdd:PHA02857    7 NLDNDYIYCKYWKPIT----YPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIddfGVYVRD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723173 130 DLKTVVSYLRNSNQVSrIGLWGRSMGAVTSLLYGAEDPSI-AGMVLDSAFSNLFDLmmELVDVYKIRL------PKFTVK 202
Cdd:PHA02857   83 VVQHVVTIKSTYPGVP-VFLLGHSMGATISILAAYKNPNLfTAMILMSPLVNAEAV--PRLNLLAAKLmgifypNKIVGK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723173 203 VAVQYMRRIIQKKAKFNIMDLNC-------------------VKVSPKTFIPALFGHASGDK---------FIQPHHSDL 254
Cdd:PHA02857  160 LCPESVSRDMDEVYKYQYDPLVNhekikagfasqvlkatnkvRKIIPKIKTPILILQGTNNEisdvsgayyFMQHANCNR 239

                         250
                  ....*....|
gi 1063723173 255 ILKCYAGDKN 264
Cdd:PHA02857  240 EIKIYEGAKH 249
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
64-182 6.03e-03

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 37.55  E-value: 6.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723173  64 YVPSssREDTPLPCVIYCHG---NSGCRADANEAVMVLL-PSNITVFTLDFSgsgLS-EGDY-VSLgwhekDDLKTVVSY 137
Cdd:COG0657     4 YRPA--GAKGPLPVVVYFHGggwVSGSKDTHDPLARRLAaRAGAAVVSVDYR---LApEHPFpAAL-----EDAYAALRW 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063723173 138 LRNSNQ-----VSRIGLWGRSMG----AVTSLLYGAED-PSIAGMVL-----DSAFSNLF 182
Cdd:COG0657    74 LRANAAelgidPDRIAVAGDSAGghlaAALALRARDRGgPRPAAQVLiypvlDLTASPLR 133
 
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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