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Conserved domains on  [gi|237757346|ref|NP_001153620|]
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phospholipase DDHD1 isoform c [Homo sapiens]

Protein Classification

DDHD family phospholipase( domain architecture ID 10502158)

DDHD family phospholipase similar to Homo sapiens phospholipase DDHD1 that hydrolyzes phosphatidic acid, including 1,2-dioleoyl-sn-phosphatidic acid

EC:  3.1.1.-
Gene Ontology:  GO:0008970|GO:0046872

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DDHD pfam02862
DDHD domain; The DDHD domain is 180 residues long and contains four conserved residues that ...
611-885 1.18e-70

DDHD domain; The DDHD domain is 180 residues long and contains four conserved residues that may form a metal binding site. The domain is named after these four residues. This pattern of conservation of metal binding residues is often seen in phosphoesterase domains. This domain is found in retinal degeneration B proteins, as well as a family of probable phospholipases. It has been shown that this domain is found in a longer C terminal region that binds to PYK2 tyrosine kinase. These proteins have been called N-terminal domain-interacting receptor (Nir1, Nir2 and Nir3). This suggests that this region is involved in functionally important interactions in other members of this family.


:

Pssm-ID: 460725  Cd Length: 241  Bit Score: 233.48  E-value: 1.18e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757346  611 LKFKVENFFCMGSPLAVFLALRGIRPGNTGSQDHILPREICNRLLNIFHPTDPVAYRLEPLILKHYSNISPVQIHWYNTS 690
Cdd:pfam02862   1 LDFEVENFFLLGSPLGLFLALRGAQIAGRSRSDHIYGSPACKQLYNIFHPYDPVAYRLEPLIDPAYSNLKPVLIPYYKKR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757346  691 NPLPyehmkpsflnpakeptsvsenegistipspvtspvlsrRHYGESITNIGKASILGA----ASIGKGLGGMLFSRFG 766
Cdd:pfam02862  81 GLRH--------------------------------------LELGEGLTRIGAAVGQSVsglwSSLSSGASLNRSLGLS 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757346  767 RSSTTQSSETSKDSMEDEKKPVASPSATTVGTQTLPHSSSGFLDSAyfRLQESFFNLPQLLFPENVMQNKDNALVEL--D 844
Cdd:pfam02862 123 DESSASSADSEQSHERSSEASSASESSLQAQSSSAPSSTSSSNGIK--EIEETELDWSESERKADKLEREEAKVRALnpN 200
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 237757346  845 HRIDFELREGLVESRYWSAVTSHTAYWSSLDVALFLLTFMY 885
Cdd:pfam02862 201 GRIDYVLQEGALESQYLSALTSHLSYWESEDVALFLLRQLL 241
 
Name Accession Description Interval E-value
DDHD pfam02862
DDHD domain; The DDHD domain is 180 residues long and contains four conserved residues that ...
611-885 1.18e-70

DDHD domain; The DDHD domain is 180 residues long and contains four conserved residues that may form a metal binding site. The domain is named after these four residues. This pattern of conservation of metal binding residues is often seen in phosphoesterase domains. This domain is found in retinal degeneration B proteins, as well as a family of probable phospholipases. It has been shown that this domain is found in a longer C terminal region that binds to PYK2 tyrosine kinase. These proteins have been called N-terminal domain-interacting receptor (Nir1, Nir2 and Nir3). This suggests that this region is involved in functionally important interactions in other members of this family.


Pssm-ID: 460725  Cd Length: 241  Bit Score: 233.48  E-value: 1.18e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757346  611 LKFKVENFFCMGSPLAVFLALRGIRPGNTGSQDHILPREICNRLLNIFHPTDPVAYRLEPLILKHYSNISPVQIHWYNTS 690
Cdd:pfam02862   1 LDFEVENFFLLGSPLGLFLALRGAQIAGRSRSDHIYGSPACKQLYNIFHPYDPVAYRLEPLIDPAYSNLKPVLIPYYKKR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757346  691 NPLPyehmkpsflnpakeptsvsenegistipspvtspvlsrRHYGESITNIGKASILGA----ASIGKGLGGMLFSRFG 766
Cdd:pfam02862  81 GLRH--------------------------------------LELGEGLTRIGAAVGQSVsglwSSLSSGASLNRSLGLS 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757346  767 RSSTTQSSETSKDSMEDEKKPVASPSATTVGTQTLPHSSSGFLDSAyfRLQESFFNLPQLLFPENVMQNKDNALVEL--D 844
Cdd:pfam02862 123 DESSASSADSEQSHERSSEASSASESSLQAQSSSAPSSTSSSNGIK--EIEETELDWSESERKADKLEREEAKVRALnpN 200
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 237757346  845 HRIDFELREGLVESRYWSAVTSHTAYWSSLDVALFLLTFMY 885
Cdd:pfam02862 201 GRIDYVLQEGALESQYLSALTSHLSYWESEDVALFLLRQLL 241
 
Name Accession Description Interval E-value
DDHD pfam02862
DDHD domain; The DDHD domain is 180 residues long and contains four conserved residues that ...
611-885 1.18e-70

DDHD domain; The DDHD domain is 180 residues long and contains four conserved residues that may form a metal binding site. The domain is named after these four residues. This pattern of conservation of metal binding residues is often seen in phosphoesterase domains. This domain is found in retinal degeneration B proteins, as well as a family of probable phospholipases. It has been shown that this domain is found in a longer C terminal region that binds to PYK2 tyrosine kinase. These proteins have been called N-terminal domain-interacting receptor (Nir1, Nir2 and Nir3). This suggests that this region is involved in functionally important interactions in other members of this family.


Pssm-ID: 460725  Cd Length: 241  Bit Score: 233.48  E-value: 1.18e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757346  611 LKFKVENFFCMGSPLAVFLALRGIRPGNTGSQDHILPREICNRLLNIFHPTDPVAYRLEPLILKHYSNISPVQIHWYNTS 690
Cdd:pfam02862   1 LDFEVENFFLLGSPLGLFLALRGAQIAGRSRSDHIYGSPACKQLYNIFHPYDPVAYRLEPLIDPAYSNLKPVLIPYYKKR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757346  691 NPLPyehmkpsflnpakeptsvsenegistipspvtspvlsrRHYGESITNIGKASILGA----ASIGKGLGGMLFSRFG 766
Cdd:pfam02862  81 GLRH--------------------------------------LELGEGLTRIGAAVGQSVsglwSSLSSGASLNRSLGLS 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757346  767 RSSTTQSSETSKDSMEDEKKPVASPSATTVGTQTLPHSSSGFLDSAyfRLQESFFNLPQLLFPENVMQNKDNALVEL--D 844
Cdd:pfam02862 123 DESSASSADSEQSHERSSEASSASESSLQAQSSSAPSSTSSSNGIK--EIEETELDWSESERKADKLEREEAKVRALnpN 200
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 237757346  845 HRIDFELREGLVESRYWSAVTSHTAYWSSLDVALFLLTFMY 885
Cdd:pfam02862 201 GRIDYVLQEGALESQYLSALTSHLSYWESEDVALFLLRQLL 241
 
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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