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Conserved domains on  [gi|148674914|gb|EDL06861|]
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RIKEN cDNA 2210412D01 [Mus musculus]

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]; ...
 99-317 1.50e-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: 1.50e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148674914  99 EVFFsRTARDNRL-GCMFVRCAPSSRY-TLLFSHGNAVDLGQMcSFYIGLGSRINCNIFSYDYSGYGVSSGKPSEKNLYA 176
Cdd:COG1073   12 DVTF-KSRDGIKLaGDLYLPAGASKKYpAVVVAHGNGGVKEQR-ALYAQRLAELGFNVLAFDYRGYGESEGEPREEGSPE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148674914 177 --DIDAAWQALRTRYGVSPENIILYGQSIGTVPTVDLASRYE-CAAVILHSPLMSGLRVA-----------FPDTRKTYC 242
Cdd:COG1073   90 rrDARAAVDYLRTLPGVDPERIGLLGISLGGGYALNAAATDPrVKAVILDSPFTSLEDLAaqrakeargayLPGVPYLPN 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148674914 243 F-------DAFPSIDKISKVTSPVLVIHGTEDEVIDFSHGLAMYERCPRAVEPLWVEGAGHNDI--ELYAQYLERLKQFI 313
Cdd:COG1073  170 VrlasllnDEFDPLAKIEKISRPLLFIHGEKDEAVPFYMSEDLYEAAAEPKELLIVPGAGHVDLydRPEEEYFDKLAEFF 249


                 ....
gi 148674914 314 SHEL 317
Cdd:COG1073  250 KKNL 253
 
Name Accession Description Interval E-value
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 99-317 1.50e-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: 1.50e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148674914  99 EVFFsRTARDNRL-GCMFVRCAPSSRY-TLLFSHGNAVDLGQMcSFYIGLGSRINCNIFSYDYSGYGVSSGKPSEKNLYA 176
Cdd:COG1073   12 DVTF-KSRDGIKLaGDLYLPAGASKKYpAVVVAHGNGGVKEQR-ALYAQRLAELGFNVLAFDYRGYGESEGEPREEGSPE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148674914 177 --DIDAAWQALRTRYGVSPENIILYGQSIGTVPTVDLASRYE-CAAVILHSPLMSGLRVA-----------FPDTRKTYC 242
Cdd:COG1073   90 rrDARAAVDYLRTLPGVDPERIGLLGISLGGGYALNAAATDPrVKAVILDSPFTSLEDLAaqrakeargayLPGVPYLPN 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148674914 243 F-------DAFPSIDKISKVTSPVLVIHGTEDEVIDFSHGLAMYERCPRAVEPLWVEGAGHNDI--ELYAQYLERLKQFI 313
Cdd:COG1073  170 VrlasllnDEFDPLAKIEKISRPLLFIHGEKDEAVPFYMSEDLYEAAAEPKELLIVPGAGHVDLydRPEEEYFDKLAEFF 249


                 ....
gi 148674914 314 SHEL 317
Cdd:COG1073  250 KKNL 253
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 120-296 9.50e-09

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: 54.91  E-value: 9.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148674914  120 PSSRYTLLFSHGnavdLGQMCSFYIGLGSRIN-CNI--FSYDYSGYGVSSGK----PSEKNLYADIDAAWQALRTRYGVS 192
Cdd:pfam12146   1 GEPRAVVVLVHG----LGEHSGRYAHLADALAaQGFavYAYDHRGHGRSDGKrghvPSFDDYVDDLDTFVDKIREEHPGL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148674914  193 PenIILYGQSIGTVPTVDLASRYEC--AAVILHSP----------------------LMSGLRVAF----------PDTR 238
Cdd:pfam12146  77 P--LFLLGHSMGGLIAALYALRYPDkvDGLILSAPalkikpylappilkllakllgkLFPRLRVPNnllpdslsrdPEVV 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148674914  239 KTYcfDAFPSI-DKIS-------------------KVTSPVLVIHGTEDEVIDFSHGLAMYERCPRA-VEPLWVEGAGH 296
Cdd:pfam12146 155 AAY--AADPLVhGGISartlyelldagerllrraaAITVPLLLLHGGADRVVDPAGSREFYERAGSTdKTLKLYPGLYH 231
PHA02857 PHA02857
monoglyceride lipase; Provisional
 113-297 2.84e-04

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 41.80  E-value: 2.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148674914 113 CMFVRCAPSSRYTLLFSHGNavdlGQMCSFYIGLG---SRINCNIFSYDYSGYGVSSGKP---SEKNLYA-DIDAAWQAL 185
Cdd:PHA02857  15 CKYWKPITYPKALVFISHGA----GEHSGRYEELAeniSSLGILVFSHDHIGHGRSNGEKmmiDDFGVYVrDVVQHVVTI 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148674914 186 RTRYGVSPenIILYGQSIGTVPTVDLASRYE--CAAVILHSPLMSGLRVAFPDTRKTYCFDAF-PSI------------- 249
Cdd:PHA02857  91 KSTYPGVP--VFLLGHSMGATISILAAYKNPnlFTAMILMSPLVNAEAVPRLNLLAAKLMGIFyPNKivgklcpesvsrd 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148674914 250 ----------------------------------DKISKVTSPVLVIHGTEDEVIDFSHGLAMYERCPRAVEPLWVEGAG 295
Cdd:PHA02857 169 mdevykyqydplvnhekikagfasqvlkatnkvrKIIPKIKTPILILQGTNNEISDVSGAYYFMQHANCNREIKIYEGAK 248


                 ..
gi 148674914 296 HN 297
Cdd:PHA02857 249 HH 250
 
Name Accession Description Interval E-value
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 99-317 1.50e-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: 1.50e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148674914  99 EVFFsRTARDNRL-GCMFVRCAPSSRY-TLLFSHGNAVDLGQMcSFYIGLGSRINCNIFSYDYSGYGVSSGKPSEKNLYA 176
Cdd:COG1073   12 DVTF-KSRDGIKLaGDLYLPAGASKKYpAVVVAHGNGGVKEQR-ALYAQRLAELGFNVLAFDYRGYGESEGEPREEGSPE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148674914 177 --DIDAAWQALRTRYGVSPENIILYGQSIGTVPTVDLASRYE-CAAVILHSPLMSGLRVA-----------FPDTRKTYC 242
Cdd:COG1073   90 rrDARAAVDYLRTLPGVDPERIGLLGISLGGGYALNAAATDPrVKAVILDSPFTSLEDLAaqrakeargayLPGVPYLPN 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148674914 243 F-------DAFPSIDKISKVTSPVLVIHGTEDEVIDFSHGLAMYERCPRAVEPLWVEGAGHNDI--ELYAQYLERLKQFI 313
Cdd:COG1073  170 VrlasllnDEFDPLAKIEKISRPLLFIHGEKDEAVPFYMSEDLYEAAAEPKELLIVPGAGHVDLydRPEEEYFDKLAEFF 249


                 ....
gi 148674914 314 SHEL 317
Cdd:COG1073  250 KKNL 253
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
152-318 7.68e-23

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 94.70  E-value: 7.68e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148674914 152 CNIFSYDYSGYGVSSGKPSEKNlYADIDAAWQALRTRYGVSPENIILYGQSIGTVPTVDLASRYE--CAAVILHSPL--- 226
Cdd:COG1506   52 YAVLAPDYRGYGESAGDWGGDE-VDDVLAAIDYLAARPYVDPDRIGIYGHSYGGYMALLAAARHPdrFKAAVALAGVsdl 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148674914 227 --MSGLRVAFPDTRKT------YCFDAFPSIDKISKVTSPVLVIHGTEDEVIDFSHGLAMYERCPRA---VEPLWVEGAG 295
Cdd:COG1506  131 rsYYGTTREYTERLMGgpwedpEAYAARSPLAYADKLKTPLLLIHGEADDRVPPEQAERLYEALKKAgkpVELLVYPGEG 210

                        170       180
                 ....*....|....*....|....
gi 148674914 296 HNDIELYA-QYLERLKQFISHELP 318
Cdd:COG1506  211 HGFSGAGApDYLERILDFLDRHLK 234
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
105-313 1.06e-22

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 93.91  E-value: 1.06e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148674914 105 TARDN-RLGCMFVRCAPSSRYTLLFSHGNAVDLGQmcsfYIGLGSRIN---CNIFSYDYSGYGVSSGK----PSEKNLYA 176
Cdd:COG2267    9 PTRDGlRLRGRRWRPAGSPRGTVVLVHGLGEHSGR----YAELAEALAaagYAVLAFDLRGHGRSDGPrghvDSFDDYVD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148674914 177 DIDAAWQALRTRYGvspENIILYGQSIGTVPTVDLASRY--ECAAVILHSPLMsglrVAFPDTRKTYCF-DAFPSIDKIS 253
Cdd:COG2267   85 DLRAALDALRARPG---LPVVLLGHSMGGLIALLYAARYpdRVAGLVLLAPAY----RADPLLGPSARWlRALRLAEALA 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148674914 254 KVTSPVLVIHGTEDEVIDFSHGLAMYERCPRAVEPLWVEGAGHNDI--ELYAQYLERLKQFI 313
Cdd:COG2267  158 RIDVPVLVLHGGADRVVPPEAARRLAARLSPDVELVLLPGARHELLnePAREEVLAAILAWL 219
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 114-314 1.58e-17

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: 79.66  E-value: 1.58e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148674914 114 MFVRCAPSSRYTLLFSHGNAVDLGQMCSFYIGLGSRinCNIFSYDYSGYGvSSGKPSEKNLYADIDAAWQALRTRYGVsp 193
Cdd:COG0596   14 LHYREAGPDGPPVVLLHGLPGSSYEWRPLIPALAAG--YRVIAPDLRGHG-RSDKPAGGYTLDDLADDLAALLDALGL-- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148674914 194 ENIILYGQSIGTVPTVDLASRY--ECAAVILHSPLMSGLRVAFPDTRKTY-----CFDAFPSID---KISKVTSPVLVIH 263
Cdd:COG0596   89 ERVVLVGHSMGGMVALELAARHpeRVAGLVLVDEVLAALAEPLRRPGLAPealaaLLRALARTDlreRLARITVPTLVIW 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 148674914 264 GTEDEVIDFSHGLAMYERCPRAvEPLWVEGAGHN-DIELYAQYLERLKQFIS 314
Cdd:COG0596  169 GEKDPIVPPALARRLAELLPNA-ELVVLPGAGHFpPLEQPEAFAAALRDFLA 219
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
120-313 2.65e-13

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 68.43  E-value: 2.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148674914 120 PSSRYTLLFSHGNAVDLGQMcsfyIGLGSRIN---CNIFSYDYSGYGVSSG---KPSEKNLYADIDAAWQALRTRYgvsp 193
Cdd:COG1647   12 EGGRKGVLLLHGFTGSPAEM----RPLAEALAkagYTVYAPRLPGHGTSPEdllKTTWEDWLEDVEEAYEILKAGY---- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148674914 194 ENIILYGQSIGTVPTVDLASRY-ECAAVILHSP----------LMSGLRVAFPDTRK-----------TYCFDAFPSI-- 249
Cdd:COG1647   84 DKVIVIGLSMGGLLALLLAARYpDVAGLVLLSPalkiddpsapLLPLLKYLARSLRGigsdiedpevaEYAYDRTPLRal 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148674914 250 -----------DKISKVTSPVLVIHGTEDEVIDFSHGLAMYERCP-RAVEPLWVEGAGH-----NDIELYAQyleRLKQF 312
Cdd:COG1647  164 aelqrlirevrRDLPKITAPTLIIQSRKDEVVPPESARYIYERLGsPDKELVWLEDSGHvitldKDREEVAE---EILDF 240


                 .
gi 148674914 313 I 313
Cdd:COG1647  241 L 241
YpfH COG0400
Predicted esterase [General function prediction only];
176-318 1.25e-10

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 59.92  E-value: 1.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148674914 176 ADIDAAWQALRTRYGVSPENIILYGQSIGTVPTVDLASRYE--CAAVILHSP-LMSGLRVAFPDTRKTycfdafpsidki 252
Cdd:COG0400   71 EALAAFIDELEARYGIDPERIVLAGFSQGAAMALSLALRRPelLAGVVALSGyLPGEEALPAPEAALA------------ 138

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148674914 253 skvTSPVLVIHGTEDEVIDFSHGLAMYERCPRA---VEPLWVEGaGHndiELYAQYLERLKQFISHELP 318
Cdd:COG0400  139 ---GTPVFLAHGTQDPVIPVERAREAAEALEAAgadVTYREYPG-GH---EISPEELADARAWLAERLA 200
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 120-296 9.50e-09

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: 54.91  E-value: 9.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148674914  120 PSSRYTLLFSHGnavdLGQMCSFYIGLGSRIN-CNI--FSYDYSGYGVSSGK----PSEKNLYADIDAAWQALRTRYGVS 192
Cdd:pfam12146   1 GEPRAVVVLVHG----LGEHSGRYAHLADALAaQGFavYAYDHRGHGRSDGKrghvPSFDDYVDDLDTFVDKIREEHPGL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148674914  193 PenIILYGQSIGTVPTVDLASRYEC--AAVILHSP----------------------LMSGLRVAF----------PDTR 238
Cdd:pfam12146  77 P--LFLLGHSMGGLIAALYALRYPDkvDGLILSAPalkikpylappilkllakllgkLFPRLRVPNnllpdslsrdPEVV 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148674914  239 KTYcfDAFPSI-DKIS-------------------KVTSPVLVIHGTEDEVIDFSHGLAMYERCPRA-VEPLWVEGAGH 296
Cdd:pfam12146 155 AAY--AADPLVhGGISartlyelldagerllrraaAITVPLLLLHGGADRVVDPAGSREFYERAGSTdKTLKLYPGLYH 231
COG2945 COG2945
Alpha/beta superfamily hydrolase [General function prediction only];
176-318 6.22e-08

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


Pssm-ID: 442188 [Multi-domain]  Cd Length: 201  Bit Score: 52.09  E-value: 6.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148674914 176 ADIDAAWQALRTRYgvsPENIILYGQSIGTVPTVDLASR-YECAAVILHSPLMSglRVAFPDtrktycfdafpsidkISK 254
Cdd:COG2945   81 DDAAAALDWLRAQN---PLPLWLAGFSFGAYVALQLAMRlPEVEGLILVAPPVN--RYDFSF---------------LAP 140

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148674914 255 VTSPVLVIHGTEDEVIDFSHGLAMYERCPRAVEPLWVEGAGHndieLYAQYLERLKQFISHELP 318
Cdd:COG2945  141 CPAPTLVIHGEQDEVVPPAEVLDWARPLSPPLPVVVVPGADH----FFHGKLDELKELVARYLP 200
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
176-296 6.96e-07

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 49.19  E-value: 6.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148674914 176 ADIDAAWQALRTRYGVSPENIILYGQSIGTVPTVDLASRYE--CAAVILHSPLmsglrvafpdtrktycfDAFPSIDKIS 253
Cdd:COG0412   91 ADLRAALDWLKAQPEVDAGRVGVVGFCFGGGLALLAAARGPdlAAAVSFYGGL-----------------PADDLLDLAA 153

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 148674914 254 KVTSPVLVIHGTEDEVIDFSHGLAMYERCPRA---VEPLWVEGAGH 296
Cdd:COG0412  154 RIKAPVLLLYGEKDPLVPPEQVAALEAALAAAgvdVELHVYPGAGH 199
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
172-311 2.32e-05

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 44.53  E-value: 2.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148674914  172 KNLYADIDAAWQALRTRYGVSPENIILYGQSIG--TVPTV--DLASRYECAavILHSP------LMSGLRVAF------- 234
Cdd:pfam00326  42 QNEFDDFIAAAEYLIEQGYTDPDRLAIWGGSYGgyLTGAAlnQRPDLFKAA--VAHVPvvdwlaYMSDTSLPFterymew 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148674914  235 --PDTRKTYcFDAFPSID--KISKVTSPVLVIHGTEDEVIDFSHGLAMYERCPRAVEP---LWVEGAGH------NDIEL 301
Cdd:pfam00326 120 gnPWDNEEG-YDYLSPYSpaDNVKVYPPLLLIHGLLDDRVPPWQSLKLVAALQRKGVPfllLIFPDEGHgigkprNKVEE 198

                         170
                  ....*....|
gi 148674914  302 YAQYLERLKQ 311
Cdd:pfam00326 199 YARELAFLLE 208
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
177-296 1.82e-04

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 41.78  E-value: 1.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148674914 177 DIDAAWQALRTR---YGVSPENIILYGQS--------IGTVPTVDLASRYecAAVILHSPlMSGLRVAfPDTrktYCFDA 245
Cdd:COG0657   66 DAYAALRWLRANaaeLGIDPDRIAVAGDSagghlaaaLALRARDRGGPRP--AAQVLIYP-VLDLTAS-PLR---ADLAG 138

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 148674914 246 FPsidkiskvtsPVLVIHGTEDEVIDfsHGLAMYERCPRA---VEPLWVEGAGH 296
Cdd:COG0657  139 LP----------PTLIVTGEADPLVD--ESEALAAALRAAgvpVELHVYPGGGH 180
PHA02857 PHA02857
monoglyceride lipase; Provisional
 113-297 2.84e-04

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 41.80  E-value: 2.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148674914 113 CMFVRCAPSSRYTLLFSHGNavdlGQMCSFYIGLG---SRINCNIFSYDYSGYGVSSGKP---SEKNLYA-DIDAAWQAL 185
Cdd:PHA02857  15 CKYWKPITYPKALVFISHGA----GEHSGRYEELAeniSSLGILVFSHDHIGHGRSNGEKmmiDDFGVYVrDVVQHVVTI 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148674914 186 RTRYGVSPenIILYGQSIGTVPTVDLASRYE--CAAVILHSPLMSGLRVAFPDTRKTYCFDAF-PSI------------- 249
Cdd:PHA02857  91 KSTYPGVP--VFLLGHSMGATISILAAYKNPnlFTAMILMSPLVNAEAVPRLNLLAAKLMGIFyPNKivgklcpesvsrd 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148674914 250 ----------------------------------DKISKVTSPVLVIHGTEDEVIDFSHGLAMYERCPRAVEPLWVEGAG 295
Cdd:PHA02857 169 mdevykyqydplvnhekikagfasqvlkatnkvrKIIPKIKTPILILQGTNNEISDVSGAYYFMQHANCNREIKIYEGAK 248


                 ..
gi 148674914 296 HN 297
Cdd:PHA02857 249 HH 250
Abhydrolase_2 pfam02230
Phospholipase/Carboxylesterase; This family consists of both phospholipases and ...
 159-314 1.30e-03

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: 39.28  E-value: 1.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148674914  159 YSGYGVSSGKPSEKNLYADIDAAWQAL---RTRYGVSPENIILYGQSIGtvptvdlasryecAAVILHSPLMS------- 228
Cdd:pfam02230  67 FDLVGLSPNAKEDEAGIKNSAETIEELidaEQKKGIPSSRIIIGGFSQG-------------AMLALYSALTLplplggi 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148674914  229 -GLRVAFPDTRKtycfdaFPSIDKISKVTSPVLVIHGTEDEVIDFSHGLAMYER---CPRAVEPLWVEGAGHndiELYAQ 304
Cdd:pfam02230 134 vAFSGFLPLPTK------FPSHPNLVTKKTPIFLIHGEEDPVVPLALGKLAKEYlktSLNKVELKIYEGLAH---SICGR 204

                         170
                  ....*....|
gi 148674914  305 YLERLKQFIS 314
Cdd:pfam02230 205 EMQDIKKFLS 214
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 154-228 2.45e-03

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: 38.64  E-value: 2.45e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148674914  154 IFSYDYSGYGVSSgKPSEKNLYADIDAAW--QALRTRYGVspENIILYGQSIGTVPTVDLASRYE--CAAVILHSPLMS 228
Cdd:pfam00561  30 VIALDLRGFGKSS-RPKAQDDYRTDDLAEdlEYILEALGL--EKVNLVGHSMGGLIALAYAAKYPdrVKALVLLGALDP 105
UPF0227 pfam05728
Uncharacterized protein family (UPF0227); Despite being classed as uncharacterized proteins, ...
 192-312 4.77e-03

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: 37.39  E-value: 4.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148674914  192 SPENIILYGQSIGTVPTVDLASRYECAAVILHSPL-----MSGL--RVAFPDTRKTYCFDAFPSID----KISKVTSPV- 259
Cdd:pfam05728  57 GDDNPLLVGSSLGGYYATWLGFRCGLRQVLFNPAVrpyenLAGKlgEQANPYTGQTYVLEEYHDIElkclEVFRLKNPDr 136

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 148674914  260 -LVIHGTEDEVIDFSHGLAMYERCPRAVEplwvEGAGHNdIELYAQYLERLKQF 312
Cdd:pfam05728 137 cLVLLQKGDEVLDYRRAAAHYRPYYEIVW----DGGDHK-FKDFSRHLQQIKAF 185
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 126-235 6.99e-03

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 37.07  E-value: 6.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148674914  126 LLFSHGNAVDLGQMcsfyIGLGSRiNCNIFSYDYSGYGVSSGKPSEKNLYADIDAAWQALRTRygvspENIILYGQSIGT 205
Cdd:pfam12697   1 VVLVHGAGLSAAPL----AALLAA-GVAVLAPDLPGHGSSSPPPLDLADLADLAALLDELGAA-----RPVVLVGHSLGG 70

                          90       100       110
                  ....*....|....*....|....*....|
gi 148674914  206 VPTVDLASRYECAAVILhSPLMSGLRVAFP 235
Cdd:pfam12697  71 AVALAAAAAALVVGVLV-APLAAPPGLLAA 99
 
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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