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Conserved domains on  [gi|24119166|ref|NP_006597|]
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serine hydrolase RBBP9 [Homo sapiens]

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 1.64e-25

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


:

Pssm-ID: 442766 [Multi-domain]  Cd Length: 170  Bit Score: 96.46  E-value: 1.64e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24119166   8 VIVPGNGGGDvTTHgWYGWVKKELEkipgfQCLAKNMPDPITARESIWLPFMETELH-CDEKTIIIGHSSGAIAAMRYAE 86
Cdd:COG3545   1 LIVPGLGGSG-PDH-WQSWWERELP-----TVRRVEQPDWDRPDLDDWLAALDAAVAaADGPVVLVAHSLGCLAVAHWAA 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24119166  87 TH--RVYAIVLVSAYTSDLGDEN-ERASGYFTRPWQwekiKANCPYIVqFGSTDDPFLPWKEQQEVADRLETKLHKFTDC 163
Cdd:COG3545  74 RLprKVAGALLVAPPDPERPGFLpELDAGFAPIPRA----PLPFPSIV-VASRNDPYVSFERAERLARAWGAELIDLGAA 148

                ....*..
gi 24119166 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 1.64e-25

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


Pssm-ID: 442766 [Multi-domain]  Cd Length: 170  Bit Score: 96.46  E-value: 1.64e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24119166   8 VIVPGNGGGDvTTHgWYGWVKKELEkipgfQCLAKNMPDPITARESIWLPFMETELH-CDEKTIIIGHSSGAIAAMRYAE 86
Cdd:COG3545   1 LIVPGLGGSG-PDH-WQSWWERELP-----TVRRVEQPDWDRPDLDDWLAALDAAVAaADGPVVLVAHSLGCLAVAHWAA 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24119166  87 TH--RVYAIVLVSAYTSDLGDEN-ERASGYFTRPWQwekiKANCPYIVqFGSTDDPFLPWKEQQEVADRLETKLHKFTDC 163
Cdd:COG3545  74 RLprKVAGALLVAPPDPERPGFLpELDAGFAPIPRA----PLPFPSIV-VASRNDPYVSFERAERLARAWGAELIDLGAA 148

                ....*..
gi 24119166 164 GHFqNTE 170
Cdd:COG3545 149 GHI-NAE 154
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
8-127 5.04e-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: 48.27  E-value: 5.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24119166     8 VIVPGNGGGdvtTHGWYGWVKkELEKiPGFQCLAKNMPDPITARESIWLPFMETELHCD-----------EKTIIIGHSS 76
Cdd:pfam00561   4 LLLHGLPGS---SDLWRKLAP-ALAR-DGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEdleyilealglEKVNLVGHSM 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 24119166    77 GAIAAMRYAETH--RVYAIVLVSA--YTSDLGDENERASGYFtrPWQWEKIKANC 127
Cdd:pfam00561  79 GGLIALAYAAKYpdRVKALVLLGAldPPHELDEADRFILALF--PGFFDGFVADF 131
 
Name Accession Description Interval E-value
YdeN COG3545
Predicted esterase of the alpha/beta hydrolase fold [General function prediction only];
8-170 1.64e-25

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


Pssm-ID: 442766 [Multi-domain]  Cd Length: 170  Bit Score: 96.46  E-value: 1.64e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24119166   8 VIVPGNGGGDvTTHgWYGWVKKELEkipgfQCLAKNMPDPITARESIWLPFMETELH-CDEKTIIIGHSSGAIAAMRYAE 86
Cdd:COG3545   1 LIVPGLGGSG-PDH-WQSWWERELP-----TVRRVEQPDWDRPDLDDWLAALDAAVAaADGPVVLVAHSLGCLAVAHWAA 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24119166  87 TH--RVYAIVLVSAYTSDLGDEN-ERASGYFTRPWQwekiKANCPYIVqFGSTDDPFLPWKEQQEVADRLETKLHKFTDC 163
Cdd:COG3545  74 RLprKVAGALLVAPPDPERPGFLpELDAGFAPIPRA----PLPFPSIV-VASRNDPYVSFERAERLARAWGAELIDLGAA 148

                ....*..
gi 24119166 164 GHFqNTE 170
Cdd:COG3545 149 GHI-NAE 154
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
67-166 6.17e-09

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: 53.47  E-value: 6.17e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24119166  67 EKTIIIGHSSGAIAAMRYAETH--RVYAIVLVSAYTSDLGDENERASGY----------FTRPWQWEKIKA-NCPYIVQF 133
Cdd:COG0596  89 ERVVLVGHSMGGMVALELAARHpeRVAGLVLVDEVLAALAEPLRRPGLApealaallraLARTDLRERLARiTVPTLVIW 168
                        90       100       110
                ....*....|....*....|....*....|....
gi 24119166 134 GsTDDPFLPWKEQQEVADRLE-TKLHKFTDCGHF 166
Cdd:COG0596 169 G-EKDPIVPPALARRLAELLPnAELVVLPGAGHF 201
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
66-170 7.01e-09

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 53.08  E-value: 7.01e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24119166  66 DEKTIIIGHSSGAIAAMRYAETH--RVYAIVLVS-AYTSDlgDENERASGYFTRPWQWEKIKA-NCP-YIVQfgSTDDPF 140
Cdd:COG2267  98 GLPVVLLGHSMGGLIALLYAARYpdRVAGLVLLApAYRAD--PLLGPSARWLRALRLAEALARiDVPvLVLH--GGADRV 173
                        90       100       110
                ....*....|....*....|....*....|..
gi 24119166 141 LPWKEQQEVADRL--ETKLHKFTDCGHFQNTE 170
Cdd:COG2267 174 VPPEAARRLAARLspDVELVLLPGARHELLNE 205
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
8-127 5.04e-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: 48.27  E-value: 5.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24119166     8 VIVPGNGGGdvtTHGWYGWVKkELEKiPGFQCLAKNMPDPITARESIWLPFMETELHCD-----------EKTIIIGHSS 76
Cdd:pfam00561   4 LLLHGLPGS---SDLWRKLAP-ALAR-DGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEdleyilealglEKVNLVGHSM 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 24119166    77 GAIAAMRYAETH--RVYAIVLVSA--YTSDLGDENERASGYFtrPWQWEKIKANC 127
Cdd:pfam00561  79 GGLIALAYAAKYpdRVKALVLLGAldPPHELDEADRFILALF--PGFFDGFVADF 131
Ser_hydrolase pfam06821
Serine hydrolase; Members of this family have serine hydrolase activity. They contain a ...
8-150 1.21e-05

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: 43.47  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24119166     8 VIVPGNGGGDvTTHgWYGWVKKELEkipgfQCLAKNMPDPITARESIWLPFMETELH-CDEKTIIIGHSSGAIAAMRYAE 86
Cdd:pfam06821   2 LIVPGWGGSG-PGH-WQSHWERRLP-----AARRVEQDDWLQPVLDDWVAALSRAVAaLPGPVILVAHSLGCLAVAHWAA 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24119166    87 ---THRVYAIVLVSAYTSDLGDENERASGYFTR-PWQWEKIKAncpyiVQFGSTDDPFLPWKEQQEVA 150
Cdd:pfam06821  75 lqlRAKVAGALLVAPADVEERPPRPAALANFAPiPRDPLPFPS-----LVVASRNDPYCPFERAASLA 137
 
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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