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Conserved domains on  [gi|162287331|ref|NP_001104648|]
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phosphatidylserine lipase ABHD16A [Danio rerio]

Protein Classification

alpha/beta hydrolase( domain architecture ID 11455169)

alpha/beta hydrolase family protein catalyzes the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

Gene Ontology:  GO:0016787
PubMed:  12369917|19508187

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
289-461 3.51e-12

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


:

Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 65.79  E-value: 3.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287331 289 GYSVLGWNHPGFGGSTG----VPFPQNEANAMDVVIQFAVHKLGfqlRDIIVYAWSIGGFTASWAVMSYPE-IRALVLDA 363
Cdd:COG2267   55 GYAVLAFDLRGHGRSDGprghVDSFDDYVDDLRAALDALRARPG---LPVVLLGHSMGGLIALLYAARYPDrVAGLVLLA 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287331 364 SFDDllplalkvmpdsWRPLVTHTVRQYMNLNNAEQLCKYQGPVLLIRRTRDEIITTTGPEDIMSNRGNDLLLrllqYRY 443
Cdd:COG2267  132 PAYR------------ADPLLGPSARWLRALRLAEALARIDVPVLVLHGGADRVVPPEAARRLAARLSPDVEL----VLL 195
                        170       180
                 ....*....|....*....|....*.
gi 162287331 444 PK----VMTD----DAVTAVRRWLAA 461
Cdd:COG2267  196 PGarheLLNEpareEVLAAILAWLER 221
 
Name Accession Description Interval E-value
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
289-461 3.51e-12

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 65.79  E-value: 3.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287331 289 GYSVLGWNHPGFGGSTG----VPFPQNEANAMDVVIQFAVHKLGfqlRDIIVYAWSIGGFTASWAVMSYPE-IRALVLDA 363
Cdd:COG2267   55 GYAVLAFDLRGHGRSDGprghVDSFDDYVDDLRAALDALRARPG---LPVVLLGHSMGGLIALLYAARYPDrVAGLVLLA 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287331 364 SFDDllplalkvmpdsWRPLVTHTVRQYMNLNNAEQLCKYQGPVLLIRRTRDEIITTTGPEDIMSNRGNDLLLrllqYRY 443
Cdd:COG2267  132 PAYR------------ADPLLGPSARWLRALRLAEALARIDVPVLVLHGGADRVVPPEAARRLAARLSPDVEL----VLL 195
                        170       180
                 ....*....|....*....|....*.
gi 162287331 444 PK----VMTD----DAVTAVRRWLAA 461
Cdd:COG2267  196 PGarheLLNEpareEVLAAILAWLER 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
265-381 4.40e-08

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: 54.05  E-value: 4.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287331  265 TLVICCEGNAG----FYEVgcMNTPLEGGYSVLGWNHPGFGGSTGvPFPQNEANAMDVV--IQFAVHKLGFQlrDIIVYA 338
Cdd:pfam00561   1 PPVLLLHGLPGssdlWRKL--APALARDGFRVIALDLRGFGKSSR-PKAQDDYRTDDLAedLEYILEALGLE--KVNLVG 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 162287331  339 WSIGGFTASWAVMSYPE-IRALVLDAS------FDDLLPLALKVMPDSWR 381
Cdd:pfam00561  76 HSMGGLIALAYAAKYPDrVKALVLLGAldppheLDEADRFILALFPGFFD 125
 
Name Accession Description Interval E-value
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
289-461 3.51e-12

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 65.79  E-value: 3.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287331 289 GYSVLGWNHPGFGGSTG----VPFPQNEANAMDVVIQFAVHKLGfqlRDIIVYAWSIGGFTASWAVMSYPE-IRALVLDA 363
Cdd:COG2267   55 GYAVLAFDLRGHGRSDGprghVDSFDDYVDDLRAALDALRARPG---LPVVLLGHSMGGLIALLYAARYPDrVAGLVLLA 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287331 364 SFDDllplalkvmpdsWRPLVTHTVRQYMNLNNAEQLCKYQGPVLLIRRTRDEIITTTGPEDIMSNRGNDLLLrllqYRY 443
Cdd:COG2267  132 PAYR------------ADPLLGPSARWLRALRLAEALARIDVPVLVLHGGADRVVPPEAARRLAARLSPDVEL----VLL 195
                        170       180
                 ....*....|....*....|....*.
gi 162287331 444 PK----VMTD----DAVTAVRRWLAA 461
Cdd:COG2267  196 PGarheLLNEpareEVLAAILAWLER 221
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
259-420 1.68e-11

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 64.55  E-value: 1.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287331 259 GGTAGKTLVICCEGNAGFYEVGCMNTPL--EGGYSVLGWNHPGFGGSTGVPFPQNEANAMDV--VIQFAVHKLGFQLRDI 334
Cdd:COG1073   32 GASKKYPAVVVAHGNGGVKEQRALYAQRlaELGFNVLAFDYRGYGESEGEPREEGSPERRDAraAVDYLRTLPGVDPERI 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287331 335 IVYAWSIGGFTASWAVMSYPEIRALVLDASFDDLLPLA---------LKVMPDSWRPLVthTVRQYMN--LNNAEQLCKY 403
Cdd:COG1073  112 GLLGISLGGGYALNAAATDPRVKAVILDSPFTSLEDLAaqrakeargAYLPGVPYLPNV--RLASLLNdeFDPLAKIEKI 189
                        170
                 ....*....|....*..
gi 162287331 404 QGPVLLIRRTRDEIITT 420
Cdd:COG1073  190 SRPLLFIHGEKDEAVPF 206
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
257-419 4.31e-11

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: 62.71  E-value: 4.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287331 257 RDGGTAGKTLVICcegnAGFYEVGCMNTP----LEGGYSVLGWNHPGFGGSTGVPFPQNEANAMDVVIQFAVHkLGfqLR 332
Cdd:COG0596   17 REAGPDGPPVVLL----HGLPGSSYEWRPlipaLAAGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAALLDA-LG--LE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287331 333 DIIVYAWSIGGFTASWAVMSYPE-IRALVLDASFDDLLpLALKVMPDSWRPLVTHTVRQYMNLNNAEQLCKYQGPVLLIR 411
Cdd:COG0596   90 RVVLVGHSMGGMVALELAARHPErVAGLVLVDEVLAAL-AEPLRRPGLAPEALAALLRALARTDLRERLARITVPTLVIW 168

                 ....*...
gi 162287331 412 RTRDEIIT 419
Cdd:COG0596  169 GEKDPIVP 176
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
289-418 3.75e-09

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 57.33  E-value: 3.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287331 289 GYSVLGWNHPGFGGSTGVPFPQNEANAMDvVIQFAVHKLGFQLRDIIVYAWSIGGFTASWAVMSYPE-IRALVLDASFDD 367
Cdd:COG1506   51 GYAVLAPDYRGYGESAGDWGGDEVDDVLA-AIDYLAARPYVDPDRIGIYGHSYGGYMALLAAARHPDrFKAAVALAGVSD 129
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 162287331 368 LLPLA--LKVMPDSWRPLVTHTVRQYMNLNNAEQLCKYQGPVLLIRRTRDEII 418
Cdd:COG1506  130 LRSYYgtTREYTERLMGGPWEDPEAYAARSPLAYADKLKTPLLLIHGEADDRV 182
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
265-381 4.40e-08

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: 54.05  E-value: 4.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287331  265 TLVICCEGNAG----FYEVgcMNTPLEGGYSVLGWNHPGFGGSTGvPFPQNEANAMDVV--IQFAVHKLGFQlrDIIVYA 338
Cdd:pfam00561   1 PPVLLLHGLPGssdlWRKL--APALARDGFRVIALDLRGFGKSSR-PKAQDDYRTDDLAedLEYILEALGLE--KVNLVG 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 162287331  339 WSIGGFTASWAVMSYPE-IRALVLDAS------FDDLLPLALKVMPDSWR 381
Cdd:pfam00561  76 HSMGGLIALAYAAKYPDrVKALVLLGAldppheLDEADRFILALFPGFFD 125
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
289-376 7.11e-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: 41.43  E-value: 7.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287331  289 GYSVLGWNHPGFGGSTGVP--FPQNEANAMDVVIQFAVHKLGFQLRDIIVYAWSIGGFTASWAVMSYPE-IRALVLDASF 365
Cdd:pfam12146  31 GFAVYAYDHRGHGRSDGKRghVPSFDDYVDDLDTFVDKIREEHPGLPLFLLGHSMGGLIAALYALRYPDkVDGLILSAPA 110
                          90
                  ....*....|....*
gi 162287331  366 ----DDLLPLALKVM 376
Cdd:pfam12146 111 lkikPYLAPPILKLL 125
 
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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