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Conserved domains on  [gi|1958762769|ref|XP_038961289|]
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divergent protein kinase domain 1B isoform X2 [Rattus norvegicus]

Protein Classification

divergent protein kinase domain 1( domain architecture ID 10632812)

divergent protein kinase domain 1, also called protein FAM69, is a cysteine-rich type II transmembrane protein that localizes to the endoplasmic reticulum, and may function as Ca2+-dependent kinase

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PIP49_N pfam14875
N-term cysteine-rich ER, FAM69; The FAM69 family of cysteine-rich type II transmembrane ...
23-163 4.78e-74

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domain, inserted within the structure of the kinase domain, suggests they function as Ca2+-dependent kinases (unpublished).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: 226.86  E-value: 4.78e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762769  23 RLPGLRVKYVLLVWLGIFVGSWMVYVHYSSYSELCRGHVCQVVICDQYQKGIISGSVCQDLCELQKVEWRTCLSSAPGQQ 102
Cdd:pfam14875   2 RFSYRRVKYLFLVWLAVFVGSWVVYVQYSSYTELCRGHDCENIICDKYRKGIISGSACSSLCEKSTLYLGRCLSTKPNNQ 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958762769 103 VYSGLWQDKEVTIKCGIEEALNSKAWPDAVPRRELVLFDKPTRGTSIKEFREMTLSFLKEK 163
Cdd:pfam14875  82 VYTGLWGDLEVVIKCGIEEVPRSNYEPLSWPRSEYVLFDKPTRGTSVEEFKEMVKSFLKAK 142
PIP49_C pfam12260
Protein-kinase domain of FAM69; This is the C-terminal region of a family of FAM69 proteins ...
155-347 1.05e-67

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: 211.76  E-value: 1.05e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762769 155 MTLSFLKEKEHASRLLGYCGDLYLTESIPHGSWHGAVllpalrpllpsvlHRALQqWFGPAWPWRAKIAIGLLEFVEELF 234
Cdd:pfam12260  11 LLLQIFQDREPFPKYLGSCGRLYVVEYVGAGPLLGIS-------------RRPLD-WFSPPWPRRAKIALQLLELVEDLF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762769 235 HGSYGTFYMCETTLANVGYTATYDFKMADLQQVAPEATVRRFLQGRHCEQSSDCIYgRDCRAPCDKLMRQCKGDLIQPNL 314
Cdd:pfam12260  77 NGDPGFLYMCDVSLENFGVTNDGRLKLVDLDNVFPEDKLRRKISEQKCEKDEDCDF-FDCLSFCDLEKDRCSSEVVNPNL 155
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1958762769 315 AKVCELLRDYLLPGAPADLYEELGKQLRTCTTL 347
Cdd:pfam12260 156 QKVCQKLLDYLLRGPPSPLPEELEKLLQECAAP 188
 
Name Accession Description Interval E-value
PIP49_N pfam14875
N-term cysteine-rich ER, FAM69; The FAM69 family of cysteine-rich type II transmembrane ...
23-163 4.78e-74

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: 226.86  E-value: 4.78e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762769  23 RLPGLRVKYVLLVWLGIFVGSWMVYVHYSSYSELCRGHVCQVVICDQYQKGIISGSVCQDLCELQKVEWRTCLSSAPGQQ 102
Cdd:pfam14875   2 RFSYRRVKYLFLVWLAVFVGSWVVYVQYSSYTELCRGHDCENIICDKYRKGIISGSACSSLCEKSTLYLGRCLSTKPNNQ 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958762769 103 VYSGLWQDKEVTIKCGIEEALNSKAWPDAVPRRELVLFDKPTRGTSIKEFREMTLSFLKEK 163
Cdd:pfam14875  82 VYTGLWGDLEVVIKCGIEEVPRSNYEPLSWPRSEYVLFDKPTRGTSVEEFKEMVKSFLKAK 142
PIP49_C pfam12260
Protein-kinase domain of FAM69; This is the C-terminal region of a family of FAM69 proteins ...
155-347 1.05e-67

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: 211.76  E-value: 1.05e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762769 155 MTLSFLKEKEHASRLLGYCGDLYLTESIPHGSWHGAVllpalrpllpsvlHRALQqWFGPAWPWRAKIAIGLLEFVEELF 234
Cdd:pfam12260  11 LLLQIFQDREPFPKYLGSCGRLYVVEYVGAGPLLGIS-------------RRPLD-WFSPPWPRRAKIALQLLELVEDLF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762769 235 HGSYGTFYMCETTLANVGYTATYDFKMADLQQVAPEATVRRFLQGRHCEQSSDCIYgRDCRAPCDKLMRQCKGDLIQPNL 314
Cdd:pfam12260  77 NGDPGFLYMCDVSLENFGVTNDGRLKLVDLDNVFPEDKLRRKISEQKCEKDEDCDF-FDCLSFCDLEKDRCSSEVVNPNL 155
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1958762769 315 AKVCELLRDYLLPGAPADLYEELGKQLRTCTTL 347
Cdd:pfam12260 156 QKVCQKLLDYLLRGPPSPLPEELEKLLQECAAP 188
 
Name Accession Description Interval E-value
PIP49_N pfam14875
N-term cysteine-rich ER, FAM69; The FAM69 family of cysteine-rich type II transmembrane ...
23-163 4.78e-74

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: 226.86  E-value: 4.78e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762769  23 RLPGLRVKYVLLVWLGIFVGSWMVYVHYSSYSELCRGHVCQVVICDQYQKGIISGSVCQDLCELQKVEWRTCLSSAPGQQ 102
Cdd:pfam14875   2 RFSYRRVKYLFLVWLAVFVGSWVVYVQYSSYTELCRGHDCENIICDKYRKGIISGSACSSLCEKSTLYLGRCLSTKPNNQ 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958762769 103 VYSGLWQDKEVTIKCGIEEALNSKAWPDAVPRRELVLFDKPTRGTSIKEFREMTLSFLKEK 163
Cdd:pfam14875  82 VYTGLWGDLEVVIKCGIEEVPRSNYEPLSWPRSEYVLFDKPTRGTSVEEFKEMVKSFLKAK 142
PIP49_C pfam12260
Protein-kinase domain of FAM69; This is the C-terminal region of a family of FAM69 proteins ...
155-347 1.05e-67

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: 211.76  E-value: 1.05e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762769 155 MTLSFLKEKEHASRLLGYCGDLYLTESIPHGSWHGAVllpalrpllpsvlHRALQqWFGPAWPWRAKIAIGLLEFVEELF 234
Cdd:pfam12260  11 LLLQIFQDREPFPKYLGSCGRLYVVEYVGAGPLLGIS-------------RRPLD-WFSPPWPRRAKIALQLLELVEDLF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762769 235 HGSYGTFYMCETTLANVGYTATYDFKMADLQQVAPEATVRRFLQGRHCEQSSDCIYgRDCRAPCDKLMRQCKGDLIQPNL 314
Cdd:pfam12260  77 NGDPGFLYMCDVSLENFGVTNDGRLKLVDLDNVFPEDKLRRKISEQKCEKDEDCDF-FDCLSFCDLEKDRCSSEVVNPNL 155
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1958762769 315 AKVCELLRDYLLPGAPADLYEELGKQLRTCTTL 347
Cdd:pfam12260 156 QKVCQKLLDYLLRGPPSPLPEELEKLLQECAAP 188
 
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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