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Conserved domains on  [gi|190358515|ref|NP_112497|]
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membrane-associated phosphatidylinositol transfer protein 3 isoform 1 [Homo sapiens]

Protein Classification

DDHD family phospholipase( domain architecture ID 11139245)

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
LNS2 smart00775
This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal ...
 739-869 1.44e-46

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: 163.60  E-value: 1.44e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358515   739 VVFS-IDGSFAAS------VSIMGSDpKVRPGAVDVVRHWQDLGYMILYITGRPDMQKQRVVSWLSQ-----HNFPQGMI 806
Cdd:smart00775   1 IVISdIDGTITKSdvlghvVPIIGKD-WTHPGVAKLYRDIQNNGYKILYLTARPIGQADRTRSYLSQikqdgHNLPHGPV 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 190358515   807 FFSDG----------LVHDPLRQKAIFLRNLMQECF---IKISAAYGS-TKDISVYSVLGLPASQIFIVGRPTKKYQ 869
Cdd:smart00775  80 LLSPDrlfaalhrevISKKPEVFKIACLRDIKNLFPpqgNPFYAGFGNrITDVISYSAVGIPPSRIFTINPKGEVHQ 156
DDHD pfam02862
DDHD domain; The DDHD domain is 180 residues long and contains four conserved residues that ...
 390-593 4.13e-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: 4.13e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358515  390 FDFDVSDFFLFGSPLGLVLAMR---RTVLPGLDGFQVRPACSQVYSFFHCADPSASRLEPLLEPKFHLVPPVSVPRYQRF 466
Cdd:pfam02862   1 LDFEVENFFLLGSPLGLFLALRgaqIAGRSRSDHIYGSPACKQLYNIFHPYDPVAYRLEPLIDPAYSNLKPVLIPYYKKR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358515  467 P---------------------------------------LGDGQSLLLADALHTHSPLFLEGSSRDSPPLLDAPASPPQ 507
Cdd:pfam02862  81 GlrhlelgegltrigaavgqsvsglwsslssgaslnrslgLSDESSASSADSEQSHERSSEASSASESSLQAQSSSAPSS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358515  508 ASRFQRPGRRMSEGSSHSESSESSDSMAPVGASRITAKWWGskRIDYALYcPDVLTA--FPTVALphlfHASYWESTDVV 585
Cdd:pfam02862 161 TSSSNGIKEIEETELDWSESERKADKLEREEAKVRALNPNG--RIDYVLQ-EGALESqyLSALTS----HLSYWESEDVA 233


                  ....*...
gi 190358515  586 AFILRQVM 593
Cdd:pfam02862 234 LFLLRQLL 241
 
Name Accession Description Interval E-value
LNS2 smart00775
This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal ...
 739-869 1.44e-46

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: 163.60  E-value: 1.44e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358515   739 VVFS-IDGSFAAS------VSIMGSDpKVRPGAVDVVRHWQDLGYMILYITGRPDMQKQRVVSWLSQ-----HNFPQGMI 806
Cdd:smart00775   1 IVISdIDGTITKSdvlghvVPIIGKD-WTHPGVAKLYRDIQNNGYKILYLTARPIGQADRTRSYLSQikqdgHNLPHGPV 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 190358515   807 FFSDG----------LVHDPLRQKAIFLRNLMQECF---IKISAAYGS-TKDISVYSVLGLPASQIFIVGRPTKKYQ 869
Cdd:smart00775  80 LLSPDrlfaalhrevISKKPEVFKIACLRDIKNLFPpqgNPFYAGFGNrITDVISYSAVGIPPSRIFTINPKGEVHQ 156
DDHD pfam02862
DDHD domain; The DDHD domain is 180 residues long and contains four conserved residues that ...
 390-593 4.13e-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: 4.13e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358515  390 FDFDVSDFFLFGSPLGLVLAMR---RTVLPGLDGFQVRPACSQVYSFFHCADPSASRLEPLLEPKFHLVPPVSVPRYQRF 466
Cdd:pfam02862   1 LDFEVENFFLLGSPLGLFLALRgaqIAGRSRSDHIYGSPACKQLYNIFHPYDPVAYRLEPLIDPAYSNLKPVLIPYYKKR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358515  467 P---------------------------------------LGDGQSLLLADALHTHSPLFLEGSSRDSPPLLDAPASPPQ 507
Cdd:pfam02862  81 GlrhlelgegltrigaavgqsvsglwsslssgaslnrslgLSDESSASSADSEQSHERSSEASSASESSLQAQSSSAPSS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358515  508 ASRFQRPGRRMSEGSSHSESSESSDSMAPVGASRITAKWWGskRIDYALYcPDVLTA--FPTVALphlfHASYWESTDVV 585
Cdd:pfam02862 161 TSSSNGIKEIEETELDWSESERKADKLEREEAKVRALNPNG--RIDYVLQ-EGALESqyLSALTS----HLSYWESEDVA 233


                  ....*...
gi 190358515  586 AFILRQVM 593
Cdd:pfam02862 234 LFLLRQLL 241
YqfW COG5663
Uncharacterized conserved protein YqfW, HAD superfamily [General function prediction only];
747-833 7.08e-07

Uncharacterized conserved protein YqfW, HAD superfamily [General function prediction only];


Pssm-ID: 444382 [Multi-domain]  Cd Length: 187  Bit Score: 50.61  E-value: 7.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358515 747 FAASVSIMGSDPKVRPGAVDVVRHWQDlGYMILYITGRPDMQKQRVVSWLSQHNFPqgmiFFSDGLVHDplRQKAIFLRN 826
Cdd:COG5663   55 FEENEEEIYTEAPPVPGAKEVLNKLKD-QHELYYITARPKHLEEVTENWLEKHGIP----YDELILLGS--HDKVEAAKE 127


                 ....*..
gi 190358515 827 LMQECFI 833
Cdd:COG5663  128 LGIDLFI 134
HAD_PNKP-C cd07502
C-terminal phosphatase domain of T4 polynucleotide kinase/phosphatase (PNKP) and related ...
 739-836 4.53e-03

C-terminal phosphatase domain of T4 polynucleotide kinase/phosphatase (PNKP) and related phosphatases; This family includes the C-terminal domain of the bifunctional enzyme T4 polynucleotide kinase/phosphatase, PNKP. The PNKP phosphatase domain can catalyze the hydrolytic removal of the 3'-phosphoryl of DNA, RNA and deoxynucleoside 3'-monophosphates. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319805  Cd Length: 145  Bit Score: 38.66  E-value: 4.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358515 739 VVFSIDGSFA-----------------ASVSIMGSDPKVRPGaVDVVRHWQDLGYMILYITGRPDMQKQRVVSWLSQHNF 801
Cdd:cd07502    4 VIFDLDGTLAdtngrqpylerrprdwdAFFEAADHDPPNAPV-IELVKESALTGYEIVYLSGRPERYRRDTLRWLAKHGI 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 190358515 802 PqgmiffsDGLVH---------DPLRQKAIFLRNLMQECFIKIS 836
Cdd:cd07502   83 P-------DDALHmrgnadrrkDRRVKLEILRRLIRTRFEVRLL 119
pseT PHA02530
polynucleotide kinase; Provisional
 737-802 7.83e-03

polynucleotide kinase; Provisional


Pssm-ID: 222856 [Multi-domain]  Cd Length: 300  Bit Score: 39.62  E-value: 7.83e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 190358515 737 ECVVFSIDGSFAAsvsiMGS----------DPKVRPGAVDVVRHWQDLGYMILYITGRPDMQKQRVVSWLSQHNFP 802
Cdd:PHA02530 159 KAVIFDIDGTLAK----MGGrspydwtkvkEDKPNPMVVELVKMYKAAGYEIIVVSGRDGVCEEDTVEWLRQTDIW 230
 
Name Accession Description Interval E-value
LNS2 smart00775
This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal ...
 739-869 1.44e-46

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: 163.60  E-value: 1.44e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358515   739 VVFS-IDGSFAAS------VSIMGSDpKVRPGAVDVVRHWQDLGYMILYITGRPDMQKQRVVSWLSQ-----HNFPQGMI 806
Cdd:smart00775   1 IVISdIDGTITKSdvlghvVPIIGKD-WTHPGVAKLYRDIQNNGYKILYLTARPIGQADRTRSYLSQikqdgHNLPHGPV 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 190358515   807 FFSDG----------LVHDPLRQKAIFLRNLMQECF---IKISAAYGS-TKDISVYSVLGLPASQIFIVGRPTKKYQ 869
Cdd:smart00775  80 LLSPDrlfaalhrevISKKPEVFKIACLRDIKNLFPpqgNPFYAGFGNrITDVISYSAVGIPPSRIFTINPKGEVHQ 156
DDHD pfam02862
DDHD domain; The DDHD domain is 180 residues long and contains four conserved residues that ...
 390-593 4.13e-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: 4.13e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358515  390 FDFDVSDFFLFGSPLGLVLAMR---RTVLPGLDGFQVRPACSQVYSFFHCADPSASRLEPLLEPKFHLVPPVSVPRYQRF 466
Cdd:pfam02862   1 LDFEVENFFLLGSPLGLFLALRgaqIAGRSRSDHIYGSPACKQLYNIFHPYDPVAYRLEPLIDPAYSNLKPVLIPYYKKR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358515  467 P---------------------------------------LGDGQSLLLADALHTHSPLFLEGSSRDSPPLLDAPASPPQ 507
Cdd:pfam02862  81 GlrhlelgegltrigaavgqsvsglwsslssgaslnrslgLSDESSASSADSEQSHERSSEASSASESSLQAQSSSAPSS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358515  508 ASRFQRPGRRMSEGSSHSESSESSDSMAPVGASRITAKWWGskRIDYALYcPDVLTA--FPTVALphlfHASYWESTDVV 585
Cdd:pfam02862 161 TSSSNGIKEIEETELDWSESERKADKLEREEAKVRALNPNG--RIDYVLQ-EGALESqyLSALTS----HLSYWESEDVA 233


                  ....*...
gi 190358515  586 AFILRQVM 593
Cdd:pfam02862 234 LFLLRQLL 241
YqfW COG5663
Uncharacterized conserved protein YqfW, HAD superfamily [General function prediction only];
747-833 7.08e-07

Uncharacterized conserved protein YqfW, HAD superfamily [General function prediction only];


Pssm-ID: 444382 [Multi-domain]  Cd Length: 187  Bit Score: 50.61  E-value: 7.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358515 747 FAASVSIMGSDPKVRPGAVDVVRHWQDlGYMILYITGRPDMQKQRVVSWLSQHNFPqgmiFFSDGLVHDplRQKAIFLRN 826
Cdd:COG5663   55 FEENEEEIYTEAPPVPGAKEVLNKLKD-QHELYYITARPKHLEEVTENWLEKHGIP----YDELILLGS--HDKVEAAKE 127


                 ....*..
gi 190358515 827 LMQECFI 833
Cdd:COG5663  128 LGIDLFI 134
HAD_PNKP-C cd07502
C-terminal phosphatase domain of T4 polynucleotide kinase/phosphatase (PNKP) and related ...
 739-836 4.53e-03

C-terminal phosphatase domain of T4 polynucleotide kinase/phosphatase (PNKP) and related phosphatases; This family includes the C-terminal domain of the bifunctional enzyme T4 polynucleotide kinase/phosphatase, PNKP. The PNKP phosphatase domain can catalyze the hydrolytic removal of the 3'-phosphoryl of DNA, RNA and deoxynucleoside 3'-monophosphates. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319805  Cd Length: 145  Bit Score: 38.66  E-value: 4.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358515 739 VVFSIDGSFA-----------------ASVSIMGSDPKVRPGaVDVVRHWQDLGYMILYITGRPDMQKQRVVSWLSQHNF 801
Cdd:cd07502    4 VIFDLDGTLAdtngrqpylerrprdwdAFFEAADHDPPNAPV-IELVKESALTGYEIVYLSGRPERYRRDTLRWLAKHGI 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 190358515 802 PqgmiffsDGLVH---------DPLRQKAIFLRNLMQECFIKIS 836
Cdd:cd07502   83 P-------DDALHmrgnadrrkDRRVKLEILRRLIRTRFEVRLL 119
pseT PHA02530
polynucleotide kinase; Provisional
 737-802 7.83e-03

polynucleotide kinase; Provisional


Pssm-ID: 222856 [Multi-domain]  Cd Length: 300  Bit Score: 39.62  E-value: 7.83e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 190358515 737 ECVVFSIDGSFAAsvsiMGS----------DPKVRPGAVDVVRHWQDLGYMILYITGRPDMQKQRVVSWLSQHNFP 802
Cdd:PHA02530 159 KAVIFDIDGTLAK----MGGrspydwtkvkEDKPNPMVVELVKMYKAAGYEIIVVSGRDGVCEEDTVEWLRQTDIW 230
 
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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