NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1622934766|ref|XP_014991522|]
View 

serine/threonine-protein kinase 19 [Macaca mulatta]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
171-370 3.51e-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: 129.73  E-value: 3.51e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934766 171 FEDALPPIVLRSQVYSLVPDRTVADRQLKELQEQGEIRIVQLGFDLDA-----HGIIFTEDYRtRVLKACDGRPYAgAVQ 245
Cdd:pfam10494  25 FRRSLPPLVTVAHLHALLHSPTFVERELEELIRAGKLRKFVIPGRGPDisglgECLVLTEDYE-KLIQESSGLEDE-LKQ 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934766 246 KFLASVLPACGDLSFQqeqmtqTFGFRDSEITHLVNAGVLTVR----------------DAGSWWLAVPGAGRFIKYFVK 309
Cdd:pfam10494 103 KFLELLKENPTASSIS------TSSFTDEEISALVRAGFLTSSnlasltsasgshlneiETATYTLSLPNTGPFLKLLNA 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934766 310 GRQAVLGMVRKSKYRELLLSELLGRRAPAVVR------------------------LGLTYHVHDLIGAQLVDCISTTS- 364
Cdd:pfam10494 177 GRAHLLSLLKKSKYKEAPESLLRERWDGAVEGdskmsnakrgvlpgrtkkwkefygLDFRWVLADALGAGLVEVFETGSv 256

                  ....*.
gi 1622934766 365 GTLLRL 370
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 ...
171-370 3.51e-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: 129.73  E-value: 3.51e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934766 171 FEDALPPIVLRSQVYSLVPDRTVADRQLKELQEQGEIRIVQLGFDLDA-----HGIIFTEDYRtRVLKACDGRPYAgAVQ 245
Cdd:pfam10494  25 FRRSLPPLVTVAHLHALLHSPTFVERELEELIRAGKLRKFVIPGRGPDisglgECLVLTEDYE-KLIQESSGLEDE-LKQ 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934766 246 KFLASVLPACGDLSFQqeqmtqTFGFRDSEITHLVNAGVLTVR----------------DAGSWWLAVPGAGRFIKYFVK 309
Cdd:pfam10494 103 KFLELLKENPTASSIS------TSSFTDEEISALVRAGFLTSSnlasltsasgshlneiETATYTLSLPNTGPFLKLLNA 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934766 310 GRQAVLGMVRKSKYRELLLSELLGRRAPAVVR------------------------LGLTYHVHDLIGAQLVDCISTTS- 364
Cdd:pfam10494 177 GRAHLLSLLKKSKYKEAPESLLRERWDGAVEGdskmsnakrgvlpgrtkkwkefygLDFRWVLADALGAGLVEVFETGSv 256

                  ....*.
gi 1622934766 365 GTLLRL 370
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 ...
171-370 3.51e-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: 129.73  E-value: 3.51e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934766 171 FEDALPPIVLRSQVYSLVPDRTVADRQLKELQEQGEIRIVQLGFDLDA-----HGIIFTEDYRtRVLKACDGRPYAgAVQ 245
Cdd:pfam10494  25 FRRSLPPLVTVAHLHALLHSPTFVERELEELIRAGKLRKFVIPGRGPDisglgECLVLTEDYE-KLIQESSGLEDE-LKQ 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934766 246 KFLASVLPACGDLSFQqeqmtqTFGFRDSEITHLVNAGVLTVR----------------DAGSWWLAVPGAGRFIKYFVK 309
Cdd:pfam10494 103 KFLELLKENPTASSIS------TSSFTDEEISALVRAGFLTSSnlasltsasgshlneiETATYTLSLPNTGPFLKLLNA 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622934766 310 GRQAVLGMVRKSKYRELLLSELLGRRAPAVVR------------------------LGLTYHVHDLIGAQLVDCISTTS- 364
Cdd:pfam10494 177 GRAHLLSLLKKSKYKEAPESLLRERWDGAVEGdskmsnakrgvlpgrtkkwkefygLDFRWVLADALGAGLVEVFETGSv 256

                  ....*.
gi 1622934766 365 GTLLRL 370
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH