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Conserved domains on  [gi|195546915|ref|NP_001037834|]
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divergent protein kinase domain 1C [Homo sapiens]

Protein Classification

DIPK family protein( domain architecture ID 10385645)

DIPK (divergent protein kinase) family protein similar to divergent protein kinase domain 1C

Graphical summary

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List of domain hits

 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 ...
 187-385 7.30e-74

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: 229.10  E-value: 7.30e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195546915  187 LWALLQQEEYVYFSLLQDLSpHVLPVLGSCGHFYAVEFLAAGSPHHRALFPLDRAPGAPgggqaKAISDIALSFLDMVNH 266
Cdd:pfam12260   1 LWALLQNNEPLLLQIFQDRE-PFPKYLGSCGRLYVVEYVGAGPLLGISRRPLDWFSPPW-----PRRAKIALQLLELVED 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195546915  267 FDSDFSHRLHLCDIKPENFAIRSDFTVVAIDVDMAFFEPKMREIL-EQNCTGDEDCNFFDCFSRCDLRVNKCGAQRVNNN 345
Cdd:pfam12260  75 LFNGDPGFLYMCDVSLENFGVTNDGRLKLVDLDNVFPEDKLRRKIsEQKCEKDEDCDFFDCLSFCDLEKDRCSSEVVNPN 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 195546915  346 LQVICDKIFRHWFSAPlkssavSFQLQLQLQEAVQECADP 385
Cdd:pfam12260 155 LQKVCQKLLDYLLRGP------PSPLPEELEKLLQECAAP 188
PIP49_N super family cl20769
N-term cysteine-rich ER, FAM69; The FAM69 family of cysteine-rich type II transmembrane ...
 51-168 4.49e-11

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: 60.84  E-value: 4.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195546915   51 SERCTDEKSRRILaalCQDYQGGTLAGDLCEDLCVAGELLFQRCLHYNRGKKVLQADWRGRPVVLKSK-EEAF-SSFPPL 128
Cdd:pfam14875  33 TELCRGHDCENII---CDKYRKGIISGSACSSLCEKSTLYLGRCLSTKPNNQVYTGLWGDLEVVIKCGiEEVPrSNYEPL 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 195546915  129 SLLEEEAGEggQDMP-----EAELLLMVAGEVKSALGLELSNSSL 168
Cdd:pfam14875 110 SWPRSEYVL--FDKPtrgtsVEEFKEMVKSFLKAKLGEQASLSKL 152
 
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 ...
 187-385 7.30e-74

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: 229.10  E-value: 7.30e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195546915  187 LWALLQQEEYVYFSLLQDLSpHVLPVLGSCGHFYAVEFLAAGSPHHRALFPLDRAPGAPgggqaKAISDIALSFLDMVNH 266
Cdd:pfam12260   1 LWALLQNNEPLLLQIFQDRE-PFPKYLGSCGRLYVVEYVGAGPLLGISRRPLDWFSPPW-----PRRAKIALQLLELVED 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195546915  267 FDSDFSHRLHLCDIKPENFAIRSDFTVVAIDVDMAFFEPKMREIL-EQNCTGDEDCNFFDCFSRCDLRVNKCGAQRVNNN 345
Cdd:pfam12260  75 LFNGDPGFLYMCDVSLENFGVTNDGRLKLVDLDNVFPEDKLRRKIsEQKCEKDEDCDFFDCLSFCDLEKDRCSSEVVNPN 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 195546915  346 LQVICDKIFRHWFSAPlkssavSFQLQLQLQEAVQECADP 385
Cdd:pfam12260 155 LQKVCQKLLDYLLRGP------PSPLPEELEKLLQECAAP 188
PIP49_N pfam14875
N-term cysteine-rich ER, FAM69; The FAM69 family of cysteine-rich type II transmembrane ...
 51-168 4.49e-11

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: 60.84  E-value: 4.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195546915   51 SERCTDEKSRRILaalCQDYQGGTLAGDLCEDLCVAGELLFQRCLHYNRGKKVLQADWRGRPVVLKSK-EEAF-SSFPPL 128
Cdd:pfam14875  33 TELCRGHDCENII---CDKYRKGIISGSACSSLCEKSTLYLGRCLSTKPNNQVYTGLWGDLEVVIKCGiEEVPrSNYEPL 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 195546915  129 SLLEEEAGEggQDMP-----EAELLLMVAGEVKSALGLELSNSSL 168
Cdd:pfam14875 110 SWPRSEYVL--FDKPtrgtsVEEFKEMVKSFLKAKLGEQASLSKL 152
 
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 ...
 187-385 7.30e-74

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: 229.10  E-value: 7.30e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195546915  187 LWALLQQEEYVYFSLLQDLSpHVLPVLGSCGHFYAVEFLAAGSPHHRALFPLDRAPGAPgggqaKAISDIALSFLDMVNH 266
Cdd:pfam12260   1 LWALLQNNEPLLLQIFQDRE-PFPKYLGSCGRLYVVEYVGAGPLLGISRRPLDWFSPPW-----PRRAKIALQLLELVED 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195546915  267 FDSDFSHRLHLCDIKPENFAIRSDFTVVAIDVDMAFFEPKMREIL-EQNCTGDEDCNFFDCFSRCDLRVNKCGAQRVNNN 345
Cdd:pfam12260  75 LFNGDPGFLYMCDVSLENFGVTNDGRLKLVDLDNVFPEDKLRRKIsEQKCEKDEDCDFFDCLSFCDLEKDRCSSEVVNPN 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 195546915  346 LQVICDKIFRHWFSAPlkssavSFQLQLQLQEAVQECADP 385
Cdd:pfam12260 155 LQKVCQKLLDYLLRGP------PSPLPEELEKLLQECAAP 188
PIP49_N pfam14875
N-term cysteine-rich ER, FAM69; The FAM69 family of cysteine-rich type II transmembrane ...
 51-168 4.49e-11

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: 60.84  E-value: 4.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195546915   51 SERCTDEKSRRILaalCQDYQGGTLAGDLCEDLCVAGELLFQRCLHYNRGKKVLQADWRGRPVVLKSK-EEAF-SSFPPL 128
Cdd:pfam14875  33 TELCRGHDCENII---CDKYRKGIISGSACSSLCEKSTLYLGRCLSTKPNNQVYTGLWGDLEVVIKCGiEEVPrSNYEPL 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 195546915  129 SLLEEEAGEggQDMP-----EAELLLMVAGEVKSALGLELSNSSL 168
Cdd:pfam14875 110 SWPRSEYVL--FDKPtrgtsVEEFKEMVKSFLKAKLGEQASLSKL 152
 
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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