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Conserved domains on  [gi|1958646935|ref|XP_038936916|]
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phosphatidylcholine:ceramide cholinephosphotransferase 1 isoform X1 [Rattus norvegicus]

Protein Classification

sphingomyelin synthase family protein; SAM domain-containing protein( domain architecture ID 10175736)

sphingomyelin synthase family protein belonging to the type 2 phosphatidic acid phosphatase (PAP2) superfamily, similar to phosphatidylinositol:ceramide inositolphosphotransferase that is capable of converting phosphatidylinositol (PI) and ceramide to inositol-phosphorylceramide (IPC) and diacylglycerol (DAG) and vice versa| SAM (sterile alpha motif) domain-containing protein may be involved in protein-protein interaction and in developmental regulation; similar to Drosophila melanogaster protein matrimony, a polo kinase inhibitor required to maintain G2 arrest in the meiotic cell cycle in females

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SAM_SGMS1 cd09514
SAM domain of sphingomyelin synthase; SAM (sterile alpha motif) domain of SGMS-1 ...
 7-78 7.29e-43

SAM domain of sphingomyelin synthase; SAM (sterile alpha motif) domain of SGMS-1 (sphingomyelin synthase) subfamily is a potential protein-protein interaction domain. Sphingomyelin synthase 1 is a transmembrane protein with a SAM domain at the N-terminus and a catalytic domain at the C-terminus. Sphingomyelin synthase 1 is a Golgi-associated enzyme, and depending on the concentration of diacylglycerol and ceramide, can catalyze synthesis phosphocholine or sphingomyelin, respectively. It plays a central role in sphingolipid and glycerophospholipid metabolism.


:

Pssm-ID: 188913  Cd Length: 72  Bit Score: 144.93  E-value: 7.29e-43
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958646935   7 MKEVVYWSPKKVADWLLENAMPEYCEPLGHFTGQDLINLTQEDFTKPPLCRVSSDNGQRLLDMIETLKMEHH 78
Cdd:cd09514     1 MKEVVQWSPKEVSDWLSEEGMQEYSEALRSFDGQALLNLTEEDFKKTPLSLVSSDSGRQLLEMIETLKIEHH 72
PAP2_C pfam14360
PAP2 superfamily C-terminal; This family is closely related to the C-terminal a region of PAP2.
 282-355 6.34e-34

PAP2 superfamily C-terminal; This family is closely related to the C-terminal a region of PAP2.


:

Pssm-ID: 464150  Cd Length: 74  Bit Score: 121.16  E-value: 6.34e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958646935 282 MCGDYLYSGHTVMLTLTYLFIKEYSPRRLWWYHWICWLLSVVGIFCILLAHDHYTVDVVVAYYITTRLFWWYHT 355
Cdd:pfam14360   1 GCGDLIFSGHTVFTTLFVLFIWEYSPRRLWILKVILWLLAAIGYFLIIASRKHYTVDVLLGYYITTLVFLLYHT 74
 
Name Accession Description Interval E-value
SAM_SGMS1 cd09514
SAM domain of sphingomyelin synthase; SAM (sterile alpha motif) domain of SGMS-1 ...
 7-78 7.29e-43

SAM domain of sphingomyelin synthase; SAM (sterile alpha motif) domain of SGMS-1 (sphingomyelin synthase) subfamily is a potential protein-protein interaction domain. Sphingomyelin synthase 1 is a transmembrane protein with a SAM domain at the N-terminus and a catalytic domain at the C-terminus. Sphingomyelin synthase 1 is a Golgi-associated enzyme, and depending on the concentration of diacylglycerol and ceramide, can catalyze synthesis phosphocholine or sphingomyelin, respectively. It plays a central role in sphingolipid and glycerophospholipid metabolism.


Pssm-ID: 188913  Cd Length: 72  Bit Score: 144.93  E-value: 7.29e-43
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958646935   7 MKEVVYWSPKKVADWLLENAMPEYCEPLGHFTGQDLINLTQEDFTKPPLCRVSSDNGQRLLDMIETLKMEHH 78
Cdd:cd09514     1 MKEVVQWSPKEVSDWLSEEGMQEYSEALRSFDGQALLNLTEEDFKKTPLSLVSSDSGRQLLEMIETLKIEHH 72
PAP2_C pfam14360
PAP2 superfamily C-terminal; This family is closely related to the C-terminal a region of PAP2.
 282-355 6.34e-34

PAP2 superfamily C-terminal; This family is closely related to the C-terminal a region of PAP2.


Pssm-ID: 464150  Cd Length: 74  Bit Score: 121.16  E-value: 6.34e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958646935 282 MCGDYLYSGHTVMLTLTYLFIKEYSPRRLWWYHWICWLLSVVGIFCILLAHDHYTVDVVVAYYITTRLFWWYHT 355
Cdd:pfam14360   1 GCGDLIFSGHTVFTTLFVLFIWEYSPRRLWILKVILWLLAAIGYFLIIASRKHYTVDVLLGYYITTLVFLLYHT 74
acidPPc smart00014
Acid phosphatase homologues;
289-345 5.04e-04

Acid phosphatase homologues;


Pssm-ID: 214471 [Multi-domain]  Cd Length: 116  Bit Score: 39.64  E-value: 5.04e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958646935  289 SGHTVMLTLTYLFIKEYSPRRLWWYHWICWLLSVVGIFCI--LLAHDHYTVDVVVAYYI 345
Cdd:smart00014  49 SGHTAFAFAFALFLLLYLPARAGRKLLIFLLLLLALVVGFsrVYLGAHWPSDVLAGSLL 107
PAP2_like cd01610
PAP2_like proteins, a super-family of histidine phosphatases and vanadium haloperoxidases, ...
 289-354 1.93e-03

PAP2_like proteins, a super-family of histidine phosphatases and vanadium haloperoxidases, includes type 2 phosphatidic acid phosphatase or lipid phosphate phosphatase (LPP), Glucose-6-phosphatase, Phosphatidylglycerophosphatase B and bacterial acid phosphatase, vanadium chloroperoxidases, vanadium bromoperoxidases, and several other mostly uncharacterized subfamilies. Several members of this superfamily have been predicted to be transmembrane proteins.


Pssm-ID: 238813 [Multi-domain]  Cd Length: 122  Bit Score: 38.21  E-value: 1.93e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958646935 289 SGHTVMLTLTYLFIKEYSPRRLW--WYHWICWLLSVVGIFCILLAHDHYTVDVVVAYYITTRLFWWYH 354
Cdd:cd01610    55 SGHAAFAFALALFLALLLPRRLLrlLLGLLLLLLALLVGLSRVYLGVHYPSDVLAGALLGILVALLVL 122
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 10-49 6.07e-03

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 35.35  E-value: 6.07e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1958646935   10 VVYWSPKKVADWLLENAMPEYCEPL--GHFTGQDLINLTQED 49
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFrkNGIDGALLLLLTSEE 42
 
Name Accession Description Interval E-value
SAM_SGMS1 cd09514
SAM domain of sphingomyelin synthase; SAM (sterile alpha motif) domain of SGMS-1 ...
 7-78 7.29e-43

SAM domain of sphingomyelin synthase; SAM (sterile alpha motif) domain of SGMS-1 (sphingomyelin synthase) subfamily is a potential protein-protein interaction domain. Sphingomyelin synthase 1 is a transmembrane protein with a SAM domain at the N-terminus and a catalytic domain at the C-terminus. Sphingomyelin synthase 1 is a Golgi-associated enzyme, and depending on the concentration of diacylglycerol and ceramide, can catalyze synthesis phosphocholine or sphingomyelin, respectively. It plays a central role in sphingolipid and glycerophospholipid metabolism.


Pssm-ID: 188913  Cd Length: 72  Bit Score: 144.93  E-value: 7.29e-43
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958646935   7 MKEVVYWSPKKVADWLLENAMPEYCEPLGHFTGQDLINLTQEDFTKPPLCRVSSDNGQRLLDMIETLKMEHH 78
Cdd:cd09514     1 MKEVVQWSPKEVSDWLSEEGMQEYSEALRSFDGQALLNLTEEDFKKTPLSLVSSDSGRQLLEMIETLKIEHH 72
PAP2_C pfam14360
PAP2 superfamily C-terminal; This family is closely related to the C-terminal a region of PAP2.
 282-355 6.34e-34

PAP2 superfamily C-terminal; This family is closely related to the C-terminal a region of PAP2.


Pssm-ID: 464150  Cd Length: 74  Bit Score: 121.16  E-value: 6.34e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958646935 282 MCGDYLYSGHTVMLTLTYLFIKEYSPRRLWWYHWICWLLSVVGIFCILLAHDHYTVDVVVAYYITTRLFWWYHT 355
Cdd:pfam14360   1 GCGDLIFSGHTVFTTLFVLFIWEYSPRRLWILKVILWLLAAIGYFLIIASRKHYTVDVLLGYYITTLVFLLYHT 74
acidPPc smart00014
Acid phosphatase homologues;
289-345 5.04e-04

Acid phosphatase homologues;


Pssm-ID: 214471 [Multi-domain]  Cd Length: 116  Bit Score: 39.64  E-value: 5.04e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958646935  289 SGHTVMLTLTYLFIKEYSPRRLWWYHWICWLLSVVGIFCI--LLAHDHYTVDVVVAYYI 345
Cdd:smart00014  49 SGHTAFAFAFALFLLLYLPARAGRKLLIFLLLLLALVVGFsrVYLGAHWPSDVLAGSLL 107
SAM_CP2-like cd09537
SAM domain of CP2-like transcription factors; SAM (sterile alpha motif) domain of CP2-like ...
 14-52 1.21e-03

SAM domain of CP2-like transcription factors; SAM (sterile alpha motif) domain of CP2-like transcription factor is a putative protein-protein interaction domain. Proteins of this group have an N-terminal DNA-binding CP2 domain, a central predicted SAM domain and some also have a C-terminal dimerization domain. CP2-like family of transcriptional factors includes three subgroups: LBP1, TFCP2, and LBP9. Members of this family are involved in transcriptional regulation from early development to terminal differentiation. They play a role in regulation of expression of P450scc (the cholesterol side-chain cleavage enzyme, cytochrome) in placenta, and alpha-globin in erythroid cells. They are required for proper maturation of the dust (epithelial component of tubular organs) of kidney and salivary gland. Human LBP1 is known to be induced by HIV type I infection in lymphocytes; it represses HIV transcription by preventing the binding of TFIID to the virus promoter. Additionally, it has been suggested that UBP1 (LBP1) regulator might be a member of a blood pressure controlling network. LBP1 protein isoforms are able to form dimers apparently via SAM domain since SAM deletion or mutation resulted in a loss of this ability.


Pssm-ID: 188936  Cd Length: 67  Bit Score: 37.34  E-value: 1.21e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1958646935  14 SPKKVADWLLENAMPEYCEPLGHFTGQDLINLTQEDFTK 52
Cdd:cd09537     1 SPQQTTQWLRKNRFGAYLRTFSNFSGADLLRLTRDDLIQ 39
PAP2 pfam01569
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ...
 289-356 1.30e-03

PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), Glucose-6-phosphatase EC:3.1.3.9, Phosphatidylglycerophosphatase B EC:3.1.3.27 and bacterial acid phosphatase EC:3.1.3.2. The family also includes a variety of haloperoxidases that function by oxidising halides in the presence of hydrogen peroxide to form the corresponding hypohalous acids.


Pssm-ID: 426329 [Multi-domain]  Cd Length: 124  Bit Score: 38.56  E-value: 1.30e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958646935 289 SGHTVMLTLTYLFIKEYSPRRLWWYHWICWLLSVVGIFCI----LLAHDHYTVDVVVAYYITTRLFWWYHTM 356
Cdd:pfam01569  50 SGHSATAFALALLLALLLRRLRKIVRVLLALLLLVLALLVglsrLYLGVHFPSDVLAGALIGILLALLVYRL 121
PAP2_like cd01610
PAP2_like proteins, a super-family of histidine phosphatases and vanadium haloperoxidases, ...
 289-354 1.93e-03

PAP2_like proteins, a super-family of histidine phosphatases and vanadium haloperoxidases, includes type 2 phosphatidic acid phosphatase or lipid phosphate phosphatase (LPP), Glucose-6-phosphatase, Phosphatidylglycerophosphatase B and bacterial acid phosphatase, vanadium chloroperoxidases, vanadium bromoperoxidases, and several other mostly uncharacterized subfamilies. Several members of this superfamily have been predicted to be transmembrane proteins.


Pssm-ID: 238813 [Multi-domain]  Cd Length: 122  Bit Score: 38.21  E-value: 1.93e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958646935 289 SGHTVMLTLTYLFIKEYSPRRLW--WYHWICWLLSVVGIFCILLAHDHYTVDVVVAYYITTRLFWWYH 354
Cdd:cd01610    55 SGHAAFAFALALFLALLLPRRLLrlLLGLLLLLLALLVGLSRVYLGVHYPSDVLAGALLGILVALLVL 122
SAM_TFCP2 cd09589
SAM domain of TFCP2 transcription factors; SAM (sterile alpha motif) domain of TFCP2 ...
 14-49 3.14e-03

SAM domain of TFCP2 transcription factors; SAM (sterile alpha motif) domain of TFCP2 transcription factors is a putative protein-protein interaction domain. Proteins of this group have an N-terminal DNA-binding CP2 domain, a central predicted SAM domain and a C-terminal dimerization domain. They are involved in transcriptional regulation from early development to terminal differentiation. In particular, they regulate expression of erythroid cell-specific alpha-globin, fibrinogen, and sex-determining gene SRY as well as lens alpha-crystallin. TFCP2 regulators can interact with NF-E4 proteins forming heteromeric stage selector protein complex (SSP). This complex is able to bind stage selector element (SSE) and regulate embryonic globin expression in fetal-erythroid cells.


Pssm-ID: 188988  Cd Length: 67  Bit Score: 36.11  E-value: 3.14e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1958646935  14 SPKKVADWLLENAMPEYCEPLGHFTGQDLINLTQED 49
Cdd:cd09589     1 TPQEAQQWLHRNRFSTFSRLFTNFSGADLLKLTRED 36
SAM_LBP9 cd09590
SAM domain of LBP9 transcriptional factors; SAM (sterile alpha motif) domain of LBP9 (also ...
 14-71 3.48e-03

SAM domain of LBP9 transcriptional factors; SAM (sterile alpha motif) domain of LBP9 (also known as TFCP2L1 or CRTR-1 (CP2-Related Transcriptional Repressor-1)) transcription factor is a putative protein-protein interaction domain. Proteins of this group have an N-terminal DNA-binding CP2 domain, a central predicted SAM domain and a C-terminal dimerization domain. They are involved in transcriptional regulation from early development to terminal differentiation. In particular, they are required for proper maturation of the dust (epithelial component of tubular organs) of kidney and salivary gland as well as for regulation of P450scc (the cholesterol side-chain cleavage enzyme, cytochrome) in human placenta.


Pssm-ID: 188989  Cd Length: 67  Bit Score: 36.03  E-value: 3.48e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958646935  14 SPKKVADWLLENAMPEYCEPLGHFTGQDLINLTQEDFTKppLCrvSSDNGQRLLDMIE 71
Cdd:cd09590     1 SIQDAQQWLHRNRFSQFCRLFSSFSGADLLKMSRDDFIQ--IC--GPADGIRLFNAIK 54
SAM_SGMS1-like cd09515
SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of ...
 13-55 4.26e-03

SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of SGMS-like (sphingomyelin synthase) subfamily is a potential protein-protein interaction domain. This group of proteins is related to sphingomyelin synthase 1, and contains an N-terminal SAM domain. The function of SGMS1-like proteins is unknown; they may play a role in sphingolipid metabolism.


Pssm-ID: 188914  Cd Length: 70  Bit Score: 35.69  E-value: 4.26e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1958646935  13 WSPKKVADWLLENAMPEYCEPLGH---FTGQDLINLTQEDFTKPPL 55
Cdd:cd09515     4 WTCEDVAKWLKKEGFSKYVDLLCNkhrIDGKVLLSLTEEDLRSPPL 49
SAM_LBP1 cd09588
SAM domain of LBP1 (UBP1) transcription factors; SAM (sterile alpha motif) domain of LBP1 ...
 21-72 4.91e-03

SAM domain of LBP1 (UBP1) transcription factors; SAM (sterile alpha motif) domain of LBP1 (also known as UBP1) transcription factor is a putative protein-protein interaction domain. Proteins of this group have an N-terminal DNA-binding CP2 domain, a central predicted SAM domain and some also have a C-terminal dimerization domain. They are involved in transcriptional regulation from early development to terminal differentiation. In particular, they regulate alpha-globin in erythroid cells and P450scc (the cholesterol side-chain cleavage enzyme, cytochrome) in human placenta. Human LBP1 is known to be induced by HIV type I infection in lymphocytes; it represses HIV transcription by preventing the binding of TFIID to the virus promoter. Additionally, it has been suggested that UBP1 (LPB1) regulator might be a member of a blood pressure controlling network. LBP1 protein isoforms are able to form dimers, apparently via SAM domain since SAM deletion or mutation resulted in a loss of this ability.


Pssm-ID: 188987  Cd Length: 67  Bit Score: 35.35  E-value: 4.91e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958646935  21 WLLENAMPEYCEPLGHFTGQDLINLTQEDFTKppLCrvSSDNGQRLLDMIET 72
Cdd:cd09588     8 WLLKNRFSSYTRLFSNFSGADLLKLTREDLVQ--IC--GAADGIRLYNALKS 55
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 18-72 5.12e-03

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 34.91  E-value: 5.12e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958646935  18 VADWLLENAMPEYCEPL--GHFTGQDLINLTQEDFTKppLCRVSSDNGQRLLDMIET 72
Cdd:cd09487     2 VAEWLESLGLEQYADLFrkNEIDGDALLLLTDEDLKE--LGITSPGHRKKILRAIQR 56
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 10-49 6.07e-03

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 35.35  E-value: 6.07e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1958646935   10 VVYWSPKKVADWLLENAMPEYCEPL--GHFTGQDLINLTQED 49
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFrkNGIDGALLLLLTSEE 42
 
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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