NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|109083637|ref|XP_001083858|]
View 

phospholipase DDHD1 isoform X6 [Macaca mulatta]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
617-863 1.78e-69

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: 230.02  E-value: 1.78e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109083637  617 LKFKVENFFCMGSPLAVFLALRGIRPGNTGSQDHILPREICNRLLNIFHPTDPVAYRLEPLILKHYSNISPVQIHWYNTS 696
Cdd:pfam02862   1 LDFEVENFFLLGSPLGLFLALRGAQIAGRSRSDHIYGSPACKQLYNIFHPYDPVAYRLEPLIDPAYSNLKPVLIPYYKKR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109083637  697 NPLPyehmkpsflnpakeptsvsenegistipspvtspvlsrRHYGESITNIGKASILGA----ASIGKGLGGMLFSRFG 772
Cdd:pfam02862  81 GLRH--------------------------------------LELGEGLTRIGAAVGQSVsglwSSLSSGASLNRSLGLS 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109083637  773 RSSTTPSSETSKDSMEDEKKPVASPSATTVATQTLPHSSSG--------------------FLDSALELDH--------R 824
Cdd:pfam02862 123 DESSASSADSEQSHERSSEASSASESSLQAQSSSAPSSTSSsngikeieeteldwseserkADKLEREEAKvralnpngR 202
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 109083637  825 IDFELREGLVESRYWSAVTSHTAYWSSLDVALFLLTFMY 863
Cdd:pfam02862 203 IDYVLQEGALESQYLSALTSHLSYWESEDVALFLLRQLL 241
 
Name Accession Description Interval E-value
DDHD pfam02862
DDHD domain; The DDHD domain is 180 residues long and contains four conserved residues that ...
617-863 1.78e-69

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: 230.02  E-value: 1.78e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109083637  617 LKFKVENFFCMGSPLAVFLALRGIRPGNTGSQDHILPREICNRLLNIFHPTDPVAYRLEPLILKHYSNISPVQIHWYNTS 696
Cdd:pfam02862   1 LDFEVENFFLLGSPLGLFLALRGAQIAGRSRSDHIYGSPACKQLYNIFHPYDPVAYRLEPLIDPAYSNLKPVLIPYYKKR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109083637  697 NPLPyehmkpsflnpakeptsvsenegistipspvtspvlsrRHYGESITNIGKASILGA----ASIGKGLGGMLFSRFG 772
Cdd:pfam02862  81 GLRH--------------------------------------LELGEGLTRIGAAVGQSVsglwSSLSSGASLNRSLGLS 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109083637  773 RSSTTPSSETSKDSMEDEKKPVASPSATTVATQTLPHSSSG--------------------FLDSALELDH--------R 824
Cdd:pfam02862 123 DESSASSADSEQSHERSSEASSASESSLQAQSSSAPSSTSSsngikeieeteldwseserkADKLEREEAKvralnpngR 202
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 109083637  825 IDFELREGLVESRYWSAVTSHTAYWSSLDVALFLLTFMY 863
Cdd:pfam02862 203 IDYVLQEGALESQYLSALTSHLSYWESEDVALFLLRQLL 241
 
Name Accession Description Interval E-value
DDHD pfam02862
DDHD domain; The DDHD domain is 180 residues long and contains four conserved residues that ...
617-863 1.78e-69

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: 230.02  E-value: 1.78e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109083637  617 LKFKVENFFCMGSPLAVFLALRGIRPGNTGSQDHILPREICNRLLNIFHPTDPVAYRLEPLILKHYSNISPVQIHWYNTS 696
Cdd:pfam02862   1 LDFEVENFFLLGSPLGLFLALRGAQIAGRSRSDHIYGSPACKQLYNIFHPYDPVAYRLEPLIDPAYSNLKPVLIPYYKKR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109083637  697 NPLPyehmkpsflnpakeptsvsenegistipspvtspvlsrRHYGESITNIGKASILGA----ASIGKGLGGMLFSRFG 772
Cdd:pfam02862  81 GLRH--------------------------------------LELGEGLTRIGAAVGQSVsglwSSLSSGASLNRSLGLS 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109083637  773 RSSTTPSSETSKDSMEDEKKPVASPSATTVATQTLPHSSSG--------------------FLDSALELDH--------R 824
Cdd:pfam02862 123 DESSASSADSEQSHERSSEASSASESSLQAQSSSAPSSTSSsngikeieeteldwseserkADKLEREEAKvralnpngR 202
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 109083637  825 IDFELREGLVESRYWSAVTSHTAYWSSLDVALFLLTFMY 863
Cdd:pfam02862 203 IDYVLQEGALESQYLSALTSHLSYWESEDVALFLLRQLL 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH