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Conserved domains on  [gi|62078837|ref|NP_001014074|]
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protein ABHD16B [Rattus norvegicus]

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

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]; ...
165-329 6.11e-15

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


:

Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 74.57  E-value: 6.11e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078837 165 PGSHGRGLCLVICCEGNAGFYEMGCLSAPL--EAGYSVLGWNHPGFGGSTGAP-----FPQHDANAMdvvVKYALHRLHF 237
Cdd:COG1073  30 PAGASKKYPAVVVAHGNGGVKEQRALYAQRlaELGFNVLAFDYRGYGESEGEPreegsPERRDARAA---VDYLRTLPGV 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078837 238 SPANVVVYGWSIGGFTATWATMTYPELGALVLDATFDDLVPLALKVMPQSWKGL-----------VVRTVREHF-NLNVA 305
Cdd:COG1073 107 DPERIGLLGISLGGGYALNAAATDPRVKAVILDSPFTSLEDLAAQRAKEARGAYlpgvpylpnvrLASLLNDEFdPLAKI 186
                       170       180
                ....*....|....*....|....
gi 62078837 306 EQLccyPGPVLLLRRTQDDVVSTS 329
Cdd:COG1073 187 EKI---SRPLLFIHGEKDEAVPFY 207
 
Name Accession Description Interval E-value
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
165-329 6.11e-15

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 74.57  E-value: 6.11e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078837 165 PGSHGRGLCLVICCEGNAGFYEMGCLSAPL--EAGYSVLGWNHPGFGGSTGAP-----FPQHDANAMdvvVKYALHRLHF 237
Cdd:COG1073  30 PAGASKKYPAVVVAHGNGGVKEQRALYAQRlaELGFNVLAFDYRGYGESEGEPreegsPERRDARAA---VDYLRTLPGV 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078837 238 SPANVVVYGWSIGGFTATWATMTYPELGALVLDATFDDLVPLALKVMPQSWKGL-----------VVRTVREHF-NLNVA 305
Cdd:COG1073 107 DPERIGLLGISLGGGYALNAAATDPRVKAVILDSPFTSLEDLAAQRAKEARGAYlpgvpylpnvrLASLLNDEFdPLAKI 186
                       170       180
                ....*....|....*....|....
gi 62078837 306 EQLccyPGPVLLLRRTQDDVVSTS 329
Cdd:COG1073 187 EKI---SRPLLFIHGEKDEAVPFY 207
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
174-292 4.17e-09

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: 57.13  E-value: 4.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078837   174 LVICCEGNAG----FYEMgcLSAPLEAGYSVLGWNHPGFGGSTGAPfPQHDANAMDVV--VKYAlhRLHFSPANVVVYGW 247
Cdd:pfam00561   2 PVLLLHGLPGssdlWRKL--APALARDGFRVIALDLRGFGKSSRPK-AQDDYRTDDLAedLEYI--LEALGLEKVNLVGH 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 62078837   248 SIGGFTATWATMTYPEL-GALVLDAT------FDDLVPLALKVMPQSWKGLV 292
Cdd:pfam00561  77 SMGGLIALAYAAKYPDRvKALVLLGAldppheLDEADRFILALFPGFFDGFV 128
 
Name Accession Description Interval E-value
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
165-329 6.11e-15

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 74.57  E-value: 6.11e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078837 165 PGSHGRGLCLVICCEGNAGFYEMGCLSAPL--EAGYSVLGWNHPGFGGSTGAP-----FPQHDANAMdvvVKYALHRLHF 237
Cdd:COG1073  30 PAGASKKYPAVVVAHGNGGVKEQRALYAQRlaELGFNVLAFDYRGYGESEGEPreegsPERRDARAA---VDYLRTLPGV 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078837 238 SPANVVVYGWSIGGFTATWATMTYPELGALVLDATFDDLVPLALKVMPQSWKGL-----------VVRTVREHF-NLNVA 305
Cdd:COG1073 107 DPERIGLLGISLGGGYALNAAATDPRVKAVILDSPFTSLEDLAAQRAKEARGAYlpgvpylpnvrLASLLNDEFdPLAKI 186
                       170       180
                ....*....|....*....|....
gi 62078837 306 EQLccyPGPVLLLRRTQDDVVSTS 329
Cdd:COG1073 187 EKI---SRPLLFIHGEKDEAVPFY 207
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
195-326 2.81e-10

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 60.42  E-value: 2.81e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078837 195 EAGYSVLGWNHPGFGGSTGAPFPQHDANAMDVVvKYALHRLHFSPANVVVYGWSIGGFTATWATMTYPEL-GALVLDATF 273
Cdd:COG1506  49 SRGYAVLAPDYRGYGESAGDWGGDEVDDVLAAI-DYLAARPYVDPDRIGIYGHSYGGYMALLAAARHPDRfKAAVALAGV 127
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 62078837 274 DDLVPLA--LKVMPQSWKGL---VVRTVREHFNLNVAEQLccyPGPVLLLRRTQDDVV 326
Cdd:COG1506 128 SDLRSYYgtTREYTERLMGGpweDPEAYAARSPLAYADKL---KTPLLLIHGEADDRV 182
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
194-330 1.11e-09

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 58.47  E-value: 1.11e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078837 194 LEAGYSVLGWNHPGFGGSTGAPFPQHD----ANAMDVVVKYALHRlhfSPANVVVYGWSIGGFTATWATMTYPE-LGALV 268
Cdd:COG2267  52 AAAGYAVLAFDLRGHGRSDGPRGHVDSfddyVDDLRAALDALRAR---PGLPVVLLGHSMGGLIALLYAARYPDrVAGLV 128
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62078837 269 LDATFDDLVPLAlkvmpqswkGLVVRTVREhfnLNVAEQLCCYPGPVLLLRRTQDDVVSTSG 330
Cdd:COG2267 129 LLAPAYRADPLL---------GPSARWLRA---LRLAEALARIDVPVLVLHGGADRVVPPEA 178
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
174-292 4.17e-09

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: 57.13  E-value: 4.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078837   174 LVICCEGNAG----FYEMgcLSAPLEAGYSVLGWNHPGFGGSTGAPfPQHDANAMDVV--VKYAlhRLHFSPANVVVYGW 247
Cdd:pfam00561   2 PVLLLHGLPGssdlWRKL--APALARDGFRVIALDLRGFGKSSRPK-AQDDYRTDDLAedLEYI--LEALGLEKVNLVGH 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 62078837   248 SIGGFTATWATMTYPEL-GALVLDAT------FDDLVPLALKVMPQSWKGLV 292
Cdd:pfam00561  77 SMGGLIALAYAAKYPDRvKALVLLGAldppheLDEADRFILALFPGFFDGFV 128
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
192-327 1.11e-07

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: 52.31  E-value: 1.11e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078837 192 APLEAGYSVLGWNHPGFGGSTgAPFPQHDANAMDVVVKYALHRLHFSPANVVvyGWSIGGFTATWATMTYPE-LGALVL- 269
Cdd:COG0596  44 PALAAGYRVIAPDLRGHGRSD-KPAGGYTLDDLADDLAALLDALGLERVVLV--GHSMGGMVALELAARHPErVAGLVLv 120
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 62078837 270 DATFDDLvpLALKVMPQSWKGLVVRTVREHFNLNVAEQLCCYPGPVLLLRRTQDDVVS 327
Cdd:COG0596 121 DEVLAAL--AEPLRRPGLAPEALAALLRALARTDLRERLARITVPTLVIWGEKDPIVP 176
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
195-303 2.46e-04

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: 42.59  E-value: 2.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078837   195 EAGYSVLGWNHPGFGGSTGAP--FPQHDANAMDVVVKYALHRLHFSPANVVVYGWSIGGFTATWATMTYPE-LGALVLDA 271
Cdd:pfam12146  29 AQGFAVYAYDHRGHGRSDGKRghVPSFDDYVDDLDTFVDKIREEHPGLPLFLLGHSMGGLIAALYALRYPDkVDGLILSA 108
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 62078837   272 TF----DDLVPLALKVMpQSWKGLVVRTVREHFNLN 303
Cdd:pfam12146 109 PAlkikPYLAPPILKLL-AKLLGKLFPRLRVPNNLL 143
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
227-278 8.31e-03

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 37.59  E-value: 8.31e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 62078837   227 VVKYALHRLHFSPANVVVYGWSIGGFTATWATMTYPEL------GALVLDATFDDLVP 278
Cdd:pfam00326  51 AAEYLIEQGYTDPDRLAIWGGSYGGYLTGAALNQRPDLfkaavaHVPVVDWLAYMSDT 108
 
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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