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Conserved domains on  [gi|1034603433|ref|XP_016881040|]
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divergent protein kinase domain 1C isoform X2 [Homo sapiens]

Protein Classification

divergent protein kinase domain-containing protein( domain architecture ID 10573880)

divergent protein kinase (DIPK) domain-containing protein similar to vertebrate divergent protein kinase domain 2A and 2B proteins

CATH:  1.10.510.10
PubMed:  21334309|16244704
SCOP:  3000066

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 ...
 46-244 2.18e-75

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: 227.94  E-value: 2.18e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603433  46 LWALLQQEEYVYFSLLQDLSpHVLPVLGSCGHFYAVEFLAAGSPHHRALFPLDRAPGAPgggqaKAISDIALSFLDMVNH 125
Cdd:pfam12260   1 LWALLQNNEPLLLQIFQDRE-PFPKYLGSCGRLYVVEYVGAGPLLGISRRPLDWFSPPW-----PRRAKIALQLLELVED 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603433 126 FDSDFSHRLHLCDIKPENFAIRSDFTVVAIDVDMAFFEPKMREIL-EQNCTGDEDCNFFDCFSRCDLRVNKCGAQRVNNN 204
Cdd:pfam12260  75 LFNGDPGFLYMCDVSLENFGVTNDGRLKLVDLDNVFPEDKLRRKIsEQKCEKDEDCDFFDCLSFCDLEKDRCSSEVVNPN 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1034603433 205 LQVICDKIFRHWFSAPlkssavSFQLQLQLQEAVQECADP 244
Cdd:pfam12260 155 LQKVCQKLLDYLLRGP------PSPLPEELEKLLQECAAP 188
 
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 ...
 46-244 2.18e-75

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: 227.94  E-value: 2.18e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603433  46 LWALLQQEEYVYFSLLQDLSpHVLPVLGSCGHFYAVEFLAAGSPHHRALFPLDRAPGAPgggqaKAISDIALSFLDMVNH 125
Cdd:pfam12260   1 LWALLQNNEPLLLQIFQDRE-PFPKYLGSCGRLYVVEYVGAGPLLGISRRPLDWFSPPW-----PRRAKIALQLLELVED 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603433 126 FDSDFSHRLHLCDIKPENFAIRSDFTVVAIDVDMAFFEPKMREIL-EQNCTGDEDCNFFDCFSRCDLRVNKCGAQRVNNN 204
Cdd:pfam12260  75 LFNGDPGFLYMCDVSLENFGVTNDGRLKLVDLDNVFPEDKLRRKIsEQKCEKDEDCDFFDCLSFCDLEKDRCSSEVVNPN 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1034603433 205 LQVICDKIFRHWFSAPlkssavSFQLQLQLQEAVQECADP 244
Cdd:pfam12260 155 LQKVCQKLLDYLLRGP------PSPLPEELEKLLQECAAP 188
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
 107-155 8.09e-03

Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Pat1 (also called Ran1), Saccharomyces cerevisiae VHS1 and KSP1, and similar fungal STKs. Pat1 blocks Mei2, an RNA-binding protein which is indispensable in the initiation of meiosis. Pat1 is inactivated and Mei2 activated, which initiates meiosis, under nutrient-deprived conditions through a signaling cascade involving Ste11. Meiosis induced by Pat1 inactivation may show different characteristics than normal meiosis including aberrant positioning of centromeres. VHS1 was identified in a screen for suppressors of cell cycle arrest at the G1/S transition, while KSP1 may be involved in regulating PRP20, which is required for mRNA export and maintenance of nuclear structure. The Pat1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270895 [Multi-domain]  Cd Length: 267  Bit Score: 36.94  E-value: 8.09e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1034603433 107 GQAKAISDIALSFLDMVNHFDSdfsHRLHLCDIKPENFAIRSDFTVVAI 155
Cdd:cd13993   104 GKTELIKNVFLQLIDAVKHCHS---LGIYHRDIKPENILLSQDEGTVKL 149
 
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 ...
 46-244 2.18e-75

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: 227.94  E-value: 2.18e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603433  46 LWALLQQEEYVYFSLLQDLSpHVLPVLGSCGHFYAVEFLAAGSPHHRALFPLDRAPGAPgggqaKAISDIALSFLDMVNH 125
Cdd:pfam12260   1 LWALLQNNEPLLLQIFQDRE-PFPKYLGSCGRLYVVEYVGAGPLLGISRRPLDWFSPPW-----PRRAKIALQLLELVED 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603433 126 FDSDFSHRLHLCDIKPENFAIRSDFTVVAIDVDMAFFEPKMREIL-EQNCTGDEDCNFFDCFSRCDLRVNKCGAQRVNNN 204
Cdd:pfam12260  75 LFNGDPGFLYMCDVSLENFGVTNDGRLKLVDLDNVFPEDKLRRKIsEQKCEKDEDCDFFDCLSFCDLEKDRCSSEVVNPN 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1034603433 205 LQVICDKIFRHWFSAPlkssavSFQLQLQLQEAVQECADP 244
Cdd:pfam12260 155 LQKVCQKLLDYLLRGP------PSPLPEELEKLLQECAAP 188
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
 107-155 8.09e-03

Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Pat1 (also called Ran1), Saccharomyces cerevisiae VHS1 and KSP1, and similar fungal STKs. Pat1 blocks Mei2, an RNA-binding protein which is indispensable in the initiation of meiosis. Pat1 is inactivated and Mei2 activated, which initiates meiosis, under nutrient-deprived conditions through a signaling cascade involving Ste11. Meiosis induced by Pat1 inactivation may show different characteristics than normal meiosis including aberrant positioning of centromeres. VHS1 was identified in a screen for suppressors of cell cycle arrest at the G1/S transition, while KSP1 may be involved in regulating PRP20, which is required for mRNA export and maintenance of nuclear structure. The Pat1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270895 [Multi-domain]  Cd Length: 267  Bit Score: 36.94  E-value: 8.09e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1034603433 107 GQAKAISDIALSFLDMVNHFDSdfsHRLHLCDIKPENFAIRSDFTVVAI 155
Cdd:cd13993   104 GKTELIKNVFLQLIDAVKHCHS---LGIYHRDIKPENILLSQDEGTVKL 149
 
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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