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Conserved domains on  [gi|2462558087|ref|XP_054173437|]
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membrane-associated phosphatidylinositol transfer protein 3 isoform X2 [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

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 ...
390-593 2.33e-45

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: 162.99  E-value: 2.33e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558087 390 FDFDVSDFFLFGSPLGLVLAMR---RTVLPGLDGFQVRPACSQVYSFFHCADPSASRLEPLLEPKFHLVPPVSVPRYQRF 466
Cdd:pfam02862   1 LDFEVENFFLLGSPLGLFLALRgaqIAGRSRSDHIYGSPACKQLYNIFHPYDPVAYRLEPLIDPAYSNLKPVLIPYYKKR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558087 467 P---------------------------------------LGDGQSLLLADALHTHSPLFLEGSSRDSPPLLDAPASPPQ 507
Cdd:pfam02862  81 GlrhlelgegltrigaavgqsvsglwsslssgaslnrslgLSDESSASSADSEQSHERSSEASSASESSLQAQSSSAPSS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558087 508 ASRFQRPGRRMSEGSSHSESSESSDSMAPVGASRITAKWWGskRIDYALYcPDVLTA--FPTVALphlfHASYWESTDVV 585
Cdd:pfam02862 161 TSSSNGIKEIEETELDWSESERKADKLEREEAKVRALNPNG--RIDYVLQ-EGALESqyLSALTS----HLSYWESEDVA 233

                  ....*...
gi 2462558087 586 AFILRQVM 593
Cdd:pfam02862 234 LFLLRQLL 241
HAD_like super family cl21460
Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes ...
739-770 2.34e-04

Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes carbon and phosphorus hydrolases such as 2-haloalkonoate dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, among others. These proteins catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a conserve alpha/beta core domain, and many also possess a small cap domain, with varying folds and functions.


The actual alignment was detected with superfamily member smart00775:

Pssm-ID: 473868  Cd Length: 157  Bit Score: 42.26  E-value: 2.34e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462558087  739 VVFS-IDGSFAAS------VSIMGSDpKVRPGAVDVVRN 770
Cdd:smart00775   1 IVISdIDGTITKSdvlghvVPIIGKD-WTHPGVAKLYRD 38
 
Name Accession Description Interval E-value
DDHD pfam02862
DDHD domain; The DDHD domain is 180 residues long and contains four conserved residues that ...
390-593 2.33e-45

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: 162.99  E-value: 2.33e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558087 390 FDFDVSDFFLFGSPLGLVLAMR---RTVLPGLDGFQVRPACSQVYSFFHCADPSASRLEPLLEPKFHLVPPVSVPRYQRF 466
Cdd:pfam02862   1 LDFEVENFFLLGSPLGLFLALRgaqIAGRSRSDHIYGSPACKQLYNIFHPYDPVAYRLEPLIDPAYSNLKPVLIPYYKKR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558087 467 P---------------------------------------LGDGQSLLLADALHTHSPLFLEGSSRDSPPLLDAPASPPQ 507
Cdd:pfam02862  81 GlrhlelgegltrigaavgqsvsglwsslssgaslnrslgLSDESSASSADSEQSHERSSEASSASESSLQAQSSSAPSS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558087 508 ASRFQRPGRRMSEGSSHSESSESSDSMAPVGASRITAKWWGskRIDYALYcPDVLTA--FPTVALphlfHASYWESTDVV 585
Cdd:pfam02862 161 TSSSNGIKEIEETELDWSESERKADKLEREEAKVRALNPNG--RIDYVLQ-EGALESqyLSALTS----HLSYWESEDVA 233

                  ....*...
gi 2462558087 586 AFILRQVM 593
Cdd:pfam02862 234 LFLLRQLL 241
LNS2 smart00775
This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal ...
739-770 2.34e-04

This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal lipin domain and phosphatidylinositol transfer proteins; SMP2 is involved in plasmid maintenance and respiration. Lipin proteins are involved in adipose tissue development and insulin resistance.


Pssm-ID: 197870  Cd Length: 157  Bit Score: 42.26  E-value: 2.34e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462558087  739 VVFS-IDGSFAAS------VSIMGSDpKVRPGAVDVVRN 770
Cdd:smart00775   1 IVISdIDGTITKSdvlghvVPIIGKD-WTHPGVAKLYRD 38
 
Name Accession Description Interval E-value
DDHD pfam02862
DDHD domain; The DDHD domain is 180 residues long and contains four conserved residues that ...
390-593 2.33e-45

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: 162.99  E-value: 2.33e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558087 390 FDFDVSDFFLFGSPLGLVLAMR---RTVLPGLDGFQVRPACSQVYSFFHCADPSASRLEPLLEPKFHLVPPVSVPRYQRF 466
Cdd:pfam02862   1 LDFEVENFFLLGSPLGLFLALRgaqIAGRSRSDHIYGSPACKQLYNIFHPYDPVAYRLEPLIDPAYSNLKPVLIPYYKKR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558087 467 P---------------------------------------LGDGQSLLLADALHTHSPLFLEGSSRDSPPLLDAPASPPQ 507
Cdd:pfam02862  81 GlrhlelgegltrigaavgqsvsglwsslssgaslnrslgLSDESSASSADSEQSHERSSEASSASESSLQAQSSSAPSS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558087 508 ASRFQRPGRRMSEGSSHSESSESSDSMAPVGASRITAKWWGskRIDYALYcPDVLTA--FPTVALphlfHASYWESTDVV 585
Cdd:pfam02862 161 TSSSNGIKEIEETELDWSESERKADKLEREEAKVRALNPNG--RIDYVLQ-EGALESqyLSALTS----HLSYWESEDVA 233

                  ....*...
gi 2462558087 586 AFILRQVM 593
Cdd:pfam02862 234 LFLLRQLL 241
LNS2 smart00775
This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal ...
739-770 2.34e-04

This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal lipin domain and phosphatidylinositol transfer proteins; SMP2 is involved in plasmid maintenance and respiration. Lipin proteins are involved in adipose tissue development and insulin resistance.


Pssm-ID: 197870  Cd Length: 157  Bit Score: 42.26  E-value: 2.34e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462558087  739 VVFS-IDGSFAAS------VSIMGSDpKVRPGAVDVVRN 770
Cdd:smart00775   1 IVISdIDGTITKSdvlghvVPIIGKD-WTHPGVAKLYRD 38
 
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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