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Conserved domains on  [gi|2254538773|ref|NP_001395256|]
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divergent protein kinase domain 1C isoform 2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PIP49_C super family cl48131
Protein-kinase domain of FAM69; This is the C-terminal region of a family of FAM69 proteins ...
 184-285 1.03e-33

Protein-kinase domain of FAM69; This is the C-terminal region of a family of FAM69 proteins from Metazoa and Viridiplantae that are active protein-kinases. The family members have a short transmembrane helix close to the N-terminus, and thereafter are highly enriched with cysteines. FAM69 proteins are localized to the endoplasmic reticulum. Many members also have a short EF-hand, calcium-binding, domain just upstream of the kinase domain. The exact function of the more N-terminal family is uncertain.


The actual alignment was detected with superfamily member pfam12260:

Pssm-ID: 463512  Cd Length: 188  Bit Score: 123.17  E-value: 1.03e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254538773 184 AWSLLQQEEYVYFSLLPDlSRHILPVLGSCGHFYAVEYLAAGSPHHKALFPLD-DAGQAQAISHIALSFLDMVSHFDSDF 262
Cdd:pfam12260   1 LWALLQNNEPLLLQIFQD-REPFPKYLGSCGRLYVVEYVGAGPLLGISRRPLDwFSPPWPRRAKIALQLLELVEDLFNGD 79

                          90       100
                  ....*....|....*....|...
gi 2254538773 263 SHRLHLCDVKPENFAIKRDFTVI 285
Cdd:pfam12260  80 PGFLYMCDVSLENFGVTNDGRLK 102
PIP49_N super family cl20769
N-term cysteine-rich ER, FAM69; The FAM69 family of cysteine-rich type II transmembrane ...
 43-168 4.61e-10

N-term cysteine-rich ER, FAM69; The FAM69 family of cysteine-rich type II transmembrane proteins localize to the endoplasmic reticulum (ER) in cultured cells, probably via N-terminal di-arginine motifs. These proteins carry at least 14 luminal cysteines which are conserved in all FAM69s. There are currently few indications of the involvement of FAM69 members in human diseases. It would appear that FAM69 proteins are predicted to be have a protein kinase structure and function. Analysis of three-dimensional structure models and conservation of the classic catalytic motifs of protein kinases in four of human FAM69 proteins suggests they might have retained catalytic phosphotransferase activity. An EF-hand Ca2+-binding domain, inserted within the structure of the kinase domain, suggests they function as Ca2+-dependent kinases (unpublished).


The actual alignment was detected with superfamily member pfam14875:

Pssm-ID: 464353  Cd Length: 158  Bit Score: 57.76  E-value: 4.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254538773  43 HPSVLSERCTDEKSRRILaalCQDYRRGWLTGALCEDLCVGGELLYQRCLYYERGKKVLQAQWRGRTVVLKSKRE--AFS 120
Cdd:pfam14875  28 QYSSYTELCRGHDCENII---CDKYRKGIISGSACSSLCEKSTLYLGRCLSTKPNNQVYTGLWGDLEVVIKCGIEevPRS 104

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2254538773 121 SFPPLTLLEEEAGA---GAPGIPEAELLLMVAGEVKNTLGLELPNNSIAPL 168
Cdd:pfam14875 105 NYEPLSWPRSEYVLfdkPTRGTSVEEFKEMVKSFLKAKLGEQASLSKLVTL 155
 
Name Accession Description Interval E-value
PIP49_C pfam12260
Protein-kinase domain of FAM69; This is the C-terminal region of a family of FAM69 proteins ...
 184-285 1.03e-33

Protein-kinase domain of FAM69; This is the C-terminal region of a family of FAM69 proteins from Metazoa and Viridiplantae that are active protein-kinases. The family members have a short transmembrane helix close to the N-terminus, and thereafter are highly enriched with cysteines. FAM69 proteins are localized to the endoplasmic reticulum. Many members also have a short EF-hand, calcium-binding, domain just upstream of the kinase domain. The exact function of the more N-terminal family is uncertain.


Pssm-ID: 463512  Cd Length: 188  Bit Score: 123.17  E-value: 1.03e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254538773 184 AWSLLQQEEYVYFSLLPDlSRHILPVLGSCGHFYAVEYLAAGSPHHKALFPLD-DAGQAQAISHIALSFLDMVSHFDSDF 262
Cdd:pfam12260   1 LWALLQNNEPLLLQIFQD-REPFPKYLGSCGRLYVVEYVGAGPLLGISRRPLDwFSPPWPRRAKIALQLLELVEDLFNGD 79

                          90       100
                  ....*....|....*....|...
gi 2254538773 263 SHRLHLCDVKPENFAIKRDFTVI 285
Cdd:pfam12260  80 PGFLYMCDVSLENFGVTNDGRLK 102
PIP49_N pfam14875
N-term cysteine-rich ER, FAM69; The FAM69 family of cysteine-rich type II transmembrane ...
 43-168 4.61e-10

N-term cysteine-rich ER, FAM69; The FAM69 family of cysteine-rich type II transmembrane proteins localize to the endoplasmic reticulum (ER) in cultured cells, probably via N-terminal di-arginine motifs. These proteins carry at least 14 luminal cysteines which are conserved in all FAM69s. There are currently few indications of the involvement of FAM69 members in human diseases. It would appear that FAM69 proteins are predicted to be have a protein kinase structure and function. Analysis of three-dimensional structure models and conservation of the classic catalytic motifs of protein kinases in four of human FAM69 proteins suggests they might have retained catalytic phosphotransferase activity. An EF-hand Ca2+-binding domain, inserted within the structure of the kinase domain, suggests they function as Ca2+-dependent kinases (unpublished).


Pssm-ID: 464353  Cd Length: 158  Bit Score: 57.76  E-value: 4.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254538773  43 HPSVLSERCTDEKSRRILaalCQDYRRGWLTGALCEDLCVGGELLYQRCLYYERGKKVLQAQWRGRTVVLKSKRE--AFS 120
Cdd:pfam14875  28 QYSSYTELCRGHDCENII---CDKYRKGIISGSACSSLCEKSTLYLGRCLSTKPNNQVYTGLWGDLEVVIKCGIEevPRS 104

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2254538773 121 SFPPLTLLEEEAGA---GAPGIPEAELLLMVAGEVKNTLGLELPNNSIAPL 168
Cdd:pfam14875 105 NYEPLSWPRSEYVLfdkPTRGTSVEEFKEMVKSFLKAKLGEQASLSKLVTL 155
 
Name Accession Description Interval E-value
PIP49_C pfam12260
Protein-kinase domain of FAM69; This is the C-terminal region of a family of FAM69 proteins ...
 184-285 1.03e-33

Protein-kinase domain of FAM69; This is the C-terminal region of a family of FAM69 proteins from Metazoa and Viridiplantae that are active protein-kinases. The family members have a short transmembrane helix close to the N-terminus, and thereafter are highly enriched with cysteines. FAM69 proteins are localized to the endoplasmic reticulum. Many members also have a short EF-hand, calcium-binding, domain just upstream of the kinase domain. The exact function of the more N-terminal family is uncertain.


Pssm-ID: 463512  Cd Length: 188  Bit Score: 123.17  E-value: 1.03e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254538773 184 AWSLLQQEEYVYFSLLPDlSRHILPVLGSCGHFYAVEYLAAGSPHHKALFPLD-DAGQAQAISHIALSFLDMVSHFDSDF 262
Cdd:pfam12260   1 LWALLQNNEPLLLQIFQD-REPFPKYLGSCGRLYVVEYVGAGPLLGISRRPLDwFSPPWPRRAKIALQLLELVEDLFNGD 79

                          90       100
                  ....*....|....*....|...
gi 2254538773 263 SHRLHLCDVKPENFAIKRDFTVI 285
Cdd:pfam12260  80 PGFLYMCDVSLENFGVTNDGRLK 102
PIP49_N pfam14875
N-term cysteine-rich ER, FAM69; The FAM69 family of cysteine-rich type II transmembrane ...
 43-168 4.61e-10

N-term cysteine-rich ER, FAM69; The FAM69 family of cysteine-rich type II transmembrane proteins localize to the endoplasmic reticulum (ER) in cultured cells, probably via N-terminal di-arginine motifs. These proteins carry at least 14 luminal cysteines which are conserved in all FAM69s. There are currently few indications of the involvement of FAM69 members in human diseases. It would appear that FAM69 proteins are predicted to be have a protein kinase structure and function. Analysis of three-dimensional structure models and conservation of the classic catalytic motifs of protein kinases in four of human FAM69 proteins suggests they might have retained catalytic phosphotransferase activity. An EF-hand Ca2+-binding domain, inserted within the structure of the kinase domain, suggests they function as Ca2+-dependent kinases (unpublished).


Pssm-ID: 464353  Cd Length: 158  Bit Score: 57.76  E-value: 4.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254538773  43 HPSVLSERCTDEKSRRILaalCQDYRRGWLTGALCEDLCVGGELLYQRCLYYERGKKVLQAQWRGRTVVLKSKRE--AFS 120
Cdd:pfam14875  28 QYSSYTELCRGHDCENII---CDKYRKGIISGSACSSLCEKSTLYLGRCLSTKPNNQVYTGLWGDLEVVIKCGIEevPRS 104

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2254538773 121 SFPPLTLLEEEAGA---GAPGIPEAELLLMVAGEVKNTLGLELPNNSIAPL 168
Cdd:pfam14875 105 NYEPLSWPRSEYVLfdkPTRGTSVEEFKEMVKSFLKAKLGEQASLSKLVTL 155
 
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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