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Conserved domains on  [gi|9625029|ref|NP_062092|]
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serine hydrolase RBBP9 [Rattus norvegicus]

Protein Classification

RBBP9/YdeN family alpha/beta hydrolase( domain architecture ID 10007544)

RBBP9/YdeN family alpha/beta hydrolase has serine hydrolase activity, similar to human serine hydrolase RBBP9 (retinoblastoma-binding protein 9)

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
YdeN COG3545
Predicted esterase of the alpha/beta hydrolase fold [General function prediction only];
8-170 2.55e-23

Predicted esterase of the alpha/beta hydrolase fold [General function prediction only];


:

Pssm-ID: 442766 [Multi-domain]  Cd Length: 170  Bit Score: 90.68  E-value: 2.55e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9625029    8 VIVPGNGGGDvATHgWYGWVRkglEQIPGFQCLAknMPDPITARESIWLPFMETELH-CDEKTIIIGHSSGAIAAMRYAE 86
Cdd:COG3545   1 LIVPGLGGSG-PDH-WQSWWE---RELPTVRRVE--QPDWDRPDLDDWLAALDAAVAaADGPVVLVAHSLGCLAVAHWAA 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9625029   87 THQ--VYALILVSAYTSDLGDEN-ERASGYFSRPWQWEKIKAncphiIQFGSTDDPFLPWKEQQEVADRLDAKLYKFTDR 163
Cdd:COG3545  74 RLPrkVAGALLVAPPDPERPGFLpELDAGFAPIPRAPLPFPS-----IVVASRNDPYVSFERAERLARAWGAELIDLGAA 148

                ....*..
gi 9625029  164 GHFqNTE 170
Cdd:COG3545 149 GHI-NAE 154
 
Name Accession Description Interval E-value
YdeN COG3545
Predicted esterase of the alpha/beta hydrolase fold [General function prediction only];
8-170 2.55e-23

Predicted esterase of the alpha/beta hydrolase fold [General function prediction only];


Pssm-ID: 442766 [Multi-domain]  Cd Length: 170  Bit Score: 90.68  E-value: 2.55e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9625029    8 VIVPGNGGGDvATHgWYGWVRkglEQIPGFQCLAknMPDPITARESIWLPFMETELH-CDEKTIIIGHSSGAIAAMRYAE 86
Cdd:COG3545   1 LIVPGLGGSG-PDH-WQSWWE---RELPTVRRVE--QPDWDRPDLDDWLAALDAAVAaADGPVVLVAHSLGCLAVAHWAA 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9625029   87 THQ--VYALILVSAYTSDLGDEN-ERASGYFSRPWQWEKIKAncphiIQFGSTDDPFLPWKEQQEVADRLDAKLYKFTDR 163
Cdd:COG3545  74 RLPrkVAGALLVAPPDPERPGFLpELDAGFAPIPRAPLPFPS-----IVVASRNDPYVSFERAERLARAWGAELIDLGAA 148

                ....*..
gi 9625029  164 GHFqNTE 170
Cdd:COG3545 149 GHI-NAE 154
Ser_hydrolase pfam06821
Serine hydrolase; Members of this family have serine hydrolase activity. They contain a ...
8-166 1.26e-06

Serine hydrolase; Members of this family have serine hydrolase activity. They contain a conserved serine hydrolase motif, GXSXG/A, where the serine is a putative nucleophile. This family has an alpha-beta hydrolase fold. Eukaryotic members of this family have a conserved LXCXE motif, which binds to retinoblastomas. This motif is absent from prokaryotic members of this family.


Pssm-ID: 399658 [Multi-domain]  Cd Length: 171  Bit Score: 46.17  E-value: 1.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9625029      8 VIVPGNGGGDvATHgWYGWVRKGLEQipgfqCLAKNMPDPITARESIWLPFMETELH-CDEKTIIIGHSSGAIAAMRYAE 86
Cdd:pfam06821   2 LIVPGWGGSG-PGH-WQSHWERRLPA-----ARRVEQDDWLQPVLDDWVAALSRAVAaLPGPVILVAHSLGCLAVAHWAA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9625029     87 ---THQVYALILVSAYTSDLGDENERASGYFSR-PWQWEKIKAncphiIQFGSTDDPFLPWKEQQEVADRLDAKLYKFTD 162
Cdd:pfam06821  75 lqlRAKVAGALLVAPADVEERPPRPAALANFAPiPRDPLPFPS-----LVVASRNDPYCPFERAASLAQAWGAELVDLGH 149

                  ....
gi 9625029    163 RGHF 166
Cdd:pfam06821 150 AGHI 153
 
Name Accession Description Interval E-value
YdeN COG3545
Predicted esterase of the alpha/beta hydrolase fold [General function prediction only];
8-170 2.55e-23

Predicted esterase of the alpha/beta hydrolase fold [General function prediction only];


Pssm-ID: 442766 [Multi-domain]  Cd Length: 170  Bit Score: 90.68  E-value: 2.55e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9625029    8 VIVPGNGGGDvATHgWYGWVRkglEQIPGFQCLAknMPDPITARESIWLPFMETELH-CDEKTIIIGHSSGAIAAMRYAE 86
Cdd:COG3545   1 LIVPGLGGSG-PDH-WQSWWE---RELPTVRRVE--QPDWDRPDLDDWLAALDAAVAaADGPVVLVAHSLGCLAVAHWAA 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9625029   87 THQ--VYALILVSAYTSDLGDEN-ERASGYFSRPWQWEKIKAncphiIQFGSTDDPFLPWKEQQEVADRLDAKLYKFTDR 163
Cdd:COG3545  74 RLPrkVAGALLVAPPDPERPGFLpELDAGFAPIPRAPLPFPS-----IVVASRNDPYVSFERAERLARAWGAELIDLGAA 148

                ....*..
gi 9625029  164 GHFqNTE 170
Cdd:COG3545 149 GHI-NAE 154
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
66-176 2.20e-08

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 51.93  E-value: 2.20e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9625029   66 DEKTIIIGHSSGAIAAMRYAETHQ--VYALILVS-AYTSDlgDENERASGYFSRPWQWEKIKA-NCP-HIIQfgSTDDPF 140
Cdd:COG2267  98 GLPVVLLGHSMGGLIALLYAARYPdrVAGLVLLApAYRAD--PLLGPSARWLRALRLAEALARiDVPvLVLH--GGADRV 173
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 9625029  141 LPWKEQQEVADRL--DAKLYKFTDRGHFQnteFHELIR 176
Cdd:COG2267 174 VPPEAARRLAARLspDVELVLLPGARHEL---LNEPAR 208
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
67-176 5.89e-08

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: 50.77  E-value: 5.89e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9625029   67 EKTIIIGHSSGAIAAMRYAETH--QVYALILVSAYTSDLGDENERASGY----------FSRPWQWEKIKA-NCP-HIIQ 132
Cdd:COG0596  89 ERVVLVGHSMGGMVALELAARHpeRVAGLVLVDEVLAALAEPLRRPGLApealaallraLARTDLRERLARiTVPtLVIW 168
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 9625029  133 fgSTDDPFLPWKEQQEVADRL-DAKLYKFTDRGHF----QNTEFHELIR 176
Cdd:COG0596 169 --GEKDPIVPPALARRLAELLpNAELVVLPGAGHFppleQPEAFAAALR 215
Ser_hydrolase pfam06821
Serine hydrolase; Members of this family have serine hydrolase activity. They contain a ...
8-166 1.26e-06

Serine hydrolase; Members of this family have serine hydrolase activity. They contain a conserved serine hydrolase motif, GXSXG/A, where the serine is a putative nucleophile. This family has an alpha-beta hydrolase fold. Eukaryotic members of this family have a conserved LXCXE motif, which binds to retinoblastomas. This motif is absent from prokaryotic members of this family.


Pssm-ID: 399658 [Multi-domain]  Cd Length: 171  Bit Score: 46.17  E-value: 1.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9625029      8 VIVPGNGGGDvATHgWYGWVRKGLEQipgfqCLAKNMPDPITARESIWLPFMETELH-CDEKTIIIGHSSGAIAAMRYAE 86
Cdd:pfam06821   2 LIVPGWGGSG-PGH-WQSHWERRLPA-----ARRVEQDDWLQPVLDDWVAALSRAVAaLPGPVILVAHSLGCLAVAHWAA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9625029     87 ---THQVYALILVSAYTSDLGDENERASGYFSR-PWQWEKIKAncphiIQFGSTDDPFLPWKEQQEVADRLDAKLYKFTD 162
Cdd:pfam06821  75 lqlRAKVAGALLVAPADVEERPPRPAALANFAPiPRDPLPFPS-----LVVASRNDPYCPFERAASLAQAWGAELVDLGH 149

                  ....
gi 9625029    163 RGHF 166
Cdd:pfam06821 150 AGHI 153
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
8-127 1.27e-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: 44.03  E-value: 1.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9625029      8 VIVPGNGGGdvaTHGWYGWVRkGLEQiPGFQCLAKNMPDPITARESIWLPFMETELHCD-----------EKTIIIGHSS 76
Cdd:pfam00561   4 LLLHGLPGS---SDLWRKLAP-ALAR-DGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEdleyilealglEKVNLVGHSM 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 9625029     77 GAIAAMRYAETHQ--VYALILVSA--YTSDLGDENERASGYFsrPWQWEKIKANC 127
Cdd:pfam00561  79 GGLIALAYAAKYPdrVKALVLLGAldPPHELDEADRFILALF--PGFFDGFVADF 131
 
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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