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Conserved domains on  [gi|1863909941|ref|NP_004188|]
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inactive serine/threonine-protein kinase 19 isoform 1 [Homo sapiens]

Protein Classification

Stk19 family serine/threonine-protein kinase( domain architecture ID 10564673)

Stk19 family serine/threonine-protein kinase, similar to Homo sapiens serine/threonine-protein kinase 19 that acts as a key regulator of NRAS signaling by mediating phosphorylation of NRAS at 'Ser-89', thereby enhancing NRAS-binding to its downstream effectors

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Stk19 pfam10494
Serine-threonine protein kinase 19; This serine-threonine protein kinase number 19 is ...
52-251 1.78e-35

Serine-threonine protein kinase 19; This serine-threonine protein kinase number 19 is expressed from the MHC and predominantly in the nucleus. Protein kinases are involved in signal transduction pathways and play fundamental roles in the regulation of cell functions. This is a novel Ser/Thr protein kinase, that has Mn2+-dependent protein kinase activity that phosphorylates alpha -casein at Ser/Thr residues and histone at Ser residues. It can be covalently modified by the reactive ATP analogue 5'-p-fluorosulfonylbenzoyladenosine in the absence of ATP, and this modification is prevented in the presence of 1 mM ATP, indicating that the kinase domain of is capable of binding ATP.


:

Pssm-ID: 431315  Cd Length: 262  Bit Score: 127.03  E-value: 1.78e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909941  52 FEDALPPIVLRSQVYSLVPDRTVADRQLKELQEQGEIRIVQLGFDLDA-----HGIIFTEDYRtRVLKACDGRPYAgAVQ 126
Cdd:pfam10494  25 FRRSLPPLVTVAHLHALLHSPTFVERELEELIRAGKLRKFVIPGRGPDisglgECLVLTEDYE-KLIQESSGLEDE-LKQ 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909941 127 KFLASVLPACGDLSFQQDQmtqtfgFRDSEITHLVNAGVLTVR----------------DAGSWWLAVPGAGRFIKYFVK 190
Cdd:pfam10494 103 KFLELLKENPTASSISTSS------FTDEEISALVRAGFLTSSnlasltsasgshlneiETATYTLSLPNTGPFLKLLNA 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909941 191 GRQAVLSMVRKAKYRELLLSELLGR-----------------RAPVVVR-------LGLTYHVHDLIGAQLVDCISTTS- 245
Cdd:pfam10494 177 GRAHLLSLLKKSKYKEAPESLLRERwdgavegdskmsnakrgVLPGRTKkwkefygLDFRWVLADALGAGLVEVFETGSv 256

                  ....*.
gi 1863909941 246 GTLLRL 251
Cdd:pfam10494 257 GRGVRL 262
 
Name Accession Description Interval E-value
Stk19 pfam10494
Serine-threonine protein kinase 19; This serine-threonine protein kinase number 19 is ...
52-251 1.78e-35

Serine-threonine protein kinase 19; This serine-threonine protein kinase number 19 is expressed from the MHC and predominantly in the nucleus. Protein kinases are involved in signal transduction pathways and play fundamental roles in the regulation of cell functions. This is a novel Ser/Thr protein kinase, that has Mn2+-dependent protein kinase activity that phosphorylates alpha -casein at Ser/Thr residues and histone at Ser residues. It can be covalently modified by the reactive ATP analogue 5'-p-fluorosulfonylbenzoyladenosine in the absence of ATP, and this modification is prevented in the presence of 1 mM ATP, indicating that the kinase domain of is capable of binding ATP.


Pssm-ID: 431315  Cd Length: 262  Bit Score: 127.03  E-value: 1.78e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909941  52 FEDALPPIVLRSQVYSLVPDRTVADRQLKELQEQGEIRIVQLGFDLDA-----HGIIFTEDYRtRVLKACDGRPYAgAVQ 126
Cdd:pfam10494  25 FRRSLPPLVTVAHLHALLHSPTFVERELEELIRAGKLRKFVIPGRGPDisglgECLVLTEDYE-KLIQESSGLEDE-LKQ 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909941 127 KFLASVLPACGDLSFQQDQmtqtfgFRDSEITHLVNAGVLTVR----------------DAGSWWLAVPGAGRFIKYFVK 190
Cdd:pfam10494 103 KFLELLKENPTASSISTSS------FTDEEISALVRAGFLTSSnlasltsasgshlneiETATYTLSLPNTGPFLKLLNA 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909941 191 GRQAVLSMVRKAKYRELLLSELLGR-----------------RAPVVVR-------LGLTYHVHDLIGAQLVDCISTTS- 245
Cdd:pfam10494 177 GRAHLLSLLKKSKYKEAPESLLRERwdgavegdskmsnakrgVLPGRTKkwkefygLDFRWVLADALGAGLVEVFETGSv 256

                  ....*.
gi 1863909941 246 GTLLRL 251
Cdd:pfam10494 257 GRGVRL 262
 
Name Accession Description Interval E-value
Stk19 pfam10494
Serine-threonine protein kinase 19; This serine-threonine protein kinase number 19 is ...
52-251 1.78e-35

Serine-threonine protein kinase 19; This serine-threonine protein kinase number 19 is expressed from the MHC and predominantly in the nucleus. Protein kinases are involved in signal transduction pathways and play fundamental roles in the regulation of cell functions. This is a novel Ser/Thr protein kinase, that has Mn2+-dependent protein kinase activity that phosphorylates alpha -casein at Ser/Thr residues and histone at Ser residues. It can be covalently modified by the reactive ATP analogue 5'-p-fluorosulfonylbenzoyladenosine in the absence of ATP, and this modification is prevented in the presence of 1 mM ATP, indicating that the kinase domain of is capable of binding ATP.


Pssm-ID: 431315  Cd Length: 262  Bit Score: 127.03  E-value: 1.78e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909941  52 FEDALPPIVLRSQVYSLVPDRTVADRQLKELQEQGEIRIVQLGFDLDA-----HGIIFTEDYRtRVLKACDGRPYAgAVQ 126
Cdd:pfam10494  25 FRRSLPPLVTVAHLHALLHSPTFVERELEELIRAGKLRKFVIPGRGPDisglgECLVLTEDYE-KLIQESSGLEDE-LKQ 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909941 127 KFLASVLPACGDLSFQQDQmtqtfgFRDSEITHLVNAGVLTVR----------------DAGSWWLAVPGAGRFIKYFVK 190
Cdd:pfam10494 103 KFLELLKENPTASSISTSS------FTDEEISALVRAGFLTSSnlasltsasgshlneiETATYTLSLPNTGPFLKLLNA 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909941 191 GRQAVLSMVRKAKYRELLLSELLGR-----------------RAPVVVR-------LGLTYHVHDLIGAQLVDCISTTS- 245
Cdd:pfam10494 177 GRAHLLSLLKKSKYKEAPESLLRERwdgavegdskmsnakrgVLPGRTKkwkefygLDFRWVLADALGAGLVEVFETGSv 256

                  ....*.
gi 1863909941 246 GTLLRL 251
Cdd:pfam10494 257 GRGVRL 262
 
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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