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Conserved domains on  [gi|1005574743|ref|WP_061667045|]
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MULTISPECIES: serine/threonine protein kinase [Bacillus]

Protein Classification

protein kinase family protein( domain architecture ID 229378)

protein kinase family protein may catalyze the transfer of the gamma-phosphoryl group from ATP to substrates such as serine/threonine and/or tyrosine residues on proteins, or may be a pseudokinase

CATH:  1.10.510.10
PubMed:  16244704
SCOP:  4003661

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
 78-243 4.13e-06

Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.


The actual alignment was detected with superfamily member cd14192:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 261  Bit Score: 47.26  E-value: 4.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005574743  78 LKNSVTIYEDLKHESLIRLIDHFPVQSGYVLIFDWFDGEclhshwrfpspEKYKNPNSPFYKFRHLSAI-------ERIH 150
Cdd:cd14192    48 VKNEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVDGG-----------ELFDRITDESYQLTELDAIlftrqicEGVH 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005574743 151 SLHSIFSFHTYVEKKNYVAIdfydgsilyNFNTNETKICDIDLYSKKPYINKMGRLWGSSRFMSPEEFELNaIIDERTNV 230
Cdd:cd14192   117 YLHQHYILHLDLKPENILCV---------NSTGNQIKIIDFGLARRYKPREKLKVNFGTPEFLAPEVVNYD-FVSFPTDM 186

                         170
                  ....*....|...
gi 1005574743 231 FNMGAMAFSLLGG 243
Cdd:cd14192   187 WSVGVITYMLLSG 199
 
Name Accession Description Interval E-value
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
 78-243 4.13e-06

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK3 (or MYLK3) phosphorylates myosin regulatory light chain 2 and controls the contraction of cardiac muscles. It is expressed specifically in both the atrium and ventricle of the heart and its expression is regulated by the cardiac protein Nkx2-5. MLCK3 plays an important role in cardiogenesis by regulating the assembly of cardiac sarcomeres, the repeating contractile unit of striated muscle. MLCK3 contains a single kinase domain near the C-terminus and a unique N-terminal half, and unlike MLCK1/2, it does not appear to be regulated by Ca2+/calmodulin. The MLCK3 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: 271094 [Multi-domain]  Cd Length: 261  Bit Score: 47.26  E-value: 4.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005574743  78 LKNSVTIYEDLKHESLIRLIDHFPVQSGYVLIFDWFDGEclhshwrfpspEKYKNPNSPFYKFRHLSAI-------ERIH 150
Cdd:cd14192    48 VKNEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVDGG-----------ELFDRITDESYQLTELDAIlftrqicEGVH 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005574743 151 SLHSIFSFHTYVEKKNYVAIdfydgsilyNFNTNETKICDIDLYSKKPYINKMGRLWGSSRFMSPEEFELNaIIDERTNV 230
Cdd:cd14192   117 YLHQHYILHLDLKPENILCV---------NSTGNQIKIIDFGLARRYKPREKLKVNFGTPEFLAPEVVNYD-FVSFPTDM 186

                         170
                  ....*....|...
gi 1005574743 231 FNMGAMAFSLLGG 243
Cdd:cd14192   187 WSVGVITYMLLSG 199
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
73-292 1.31e-05

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 46.16  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005574743  73 DAIKRLKNSVTIYEDLKHESLIRLIDHFPVQSGYVLIFDWFDG----ECLHSHWRFPSPEkyknpnspfykFRHL----- 143
Cdd:COG0515    49 EARERFRREARALARLNHPNIVRVYDVGEEDGRPYLVMEYVEGeslaDLLRRRGPLPPAE-----------ALRIlaqla 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005574743 144 SAIERIHSLHSIfsfHtyvekknyvaidfYD---GSILYNFNtNETKICD--IDLYSKKPYINKMGRLWGSSRFMSPEEF 218
Cdd:COG0515   118 EALAAAHAAGIV---H-------------RDikpANILLTPD-GRVKLIDfgIARALGGATLTQTGTVVGTPGYMAPEQA 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005574743 219 ElNAIIDERTNVFNMGAMAFSLLGGEK--------------------DRSFIKWEASKELYEVAHRAVSDNRTERYASVI 278
Cdd:COG0515   181 R-GEPVDPRSDVYSLGVTLYELLTGRPpfdgdspaellrahlrepppPPSELRPDLPPALDAIVLRALAKDPEERYQSAA 259

                         250
                  ....*....|....
gi 1005574743 279 EFYEAWLKAANAER 292
Cdd:COG0515   260 ELAAALRAVLRSLA 273
 
Name Accession Description Interval E-value
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
 78-243 4.13e-06

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK3 (or MYLK3) phosphorylates myosin regulatory light chain 2 and controls the contraction of cardiac muscles. It is expressed specifically in both the atrium and ventricle of the heart and its expression is regulated by the cardiac protein Nkx2-5. MLCK3 plays an important role in cardiogenesis by regulating the assembly of cardiac sarcomeres, the repeating contractile unit of striated muscle. MLCK3 contains a single kinase domain near the C-terminus and a unique N-terminal half, and unlike MLCK1/2, it does not appear to be regulated by Ca2+/calmodulin. The MLCK3 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: 271094 [Multi-domain]  Cd Length: 261  Bit Score: 47.26  E-value: 4.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005574743  78 LKNSVTIYEDLKHESLIRLIDHFPVQSGYVLIFDWFDGEclhshwrfpspEKYKNPNSPFYKFRHLSAI-------ERIH 150
Cdd:cd14192    48 VKNEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVDGG-----------ELFDRITDESYQLTELDAIlftrqicEGVH 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005574743 151 SLHSIFSFHTYVEKKNYVAIdfydgsilyNFNTNETKICDIDLYSKKPYINKMGRLWGSSRFMSPEEFELNaIIDERTNV 230
Cdd:cd14192   117 YLHQHYILHLDLKPENILCV---------NSTGNQIKIIDFGLARRYKPREKLKVNFGTPEFLAPEVVNYD-FVSFPTDM 186

                         170
                  ....*....|...
gi 1005574743 231 FNMGAMAFSLLGG 243
Cdd:cd14192   187 WSVGVITYMLLSG 199
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
73-292 1.31e-05

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 46.16  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005574743  73 DAIKRLKNSVTIYEDLKHESLIRLIDHFPVQSGYVLIFDWFDG----ECLHSHWRFPSPEkyknpnspfykFRHL----- 143
Cdd:COG0515    49 EARERFRREARALARLNHPNIVRVYDVGEEDGRPYLVMEYVEGeslaDLLRRRGPLPPAE-----------ALRIlaqla 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005574743 144 SAIERIHSLHSIfsfHtyvekknyvaidfYD---GSILYNFNtNETKICD--IDLYSKKPYINKMGRLWGSSRFMSPEEF 218
Cdd:COG0515   118 EALAAAHAAGIV---H-------------RDikpANILLTPD-GRVKLIDfgIARALGGATLTQTGTVVGTPGYMAPEQA 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005574743 219 ElNAIIDERTNVFNMGAMAFSLLGGEK--------------------DRSFIKWEASKELYEVAHRAVSDNRTERYASVI 278
Cdd:COG0515   181 R-GEPVDPRSDVYSLGVTLYELLTGRPpfdgdspaellrahlrepppPPSELRPDLPPALDAIVLRALAKDPEERYQSAA 259

                         250
                  ....*....|....
gi 1005574743 279 EFYEAWLKAANAER 292
Cdd:COG0515   260 ELAAALRAVLRSLA 273
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
 78-243 6.72e-04

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. MLCK4 (or MYLK4 or SgK085) contains a single kinase domain near the C-terminus. The MLCK4 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: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 40.28  E-value: 6.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005574743  78 LKNSVTIYEDLKHESLIRLIDHFPVQSGYVLIFDWFDGECLHshwrfpspEKYKNPNspfYKFRHLSAI-------ERIH 150
Cdd:cd14193    48 VKNEIEVMNQLNHANLIQLYDAFESRNDIVLVMEYVDGGELF--------DRIIDEN---YNLTELDTIlfikqicEGIQ 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005574743 151 SLHSIFSFHTYVEKKNYVAIdfydgsilyNFNTNETKICDIDLYSKKPYINKMGRLWGSSRFMSPEEFELNaIIDERTNV 230
Cdd:cd14193   117 YMHQMYILHLDLKPENILCV---------SREANQVKIIDFGLARRYKPREKLRVNFGTPEFLAPEVVNYE-FVSFPTDM 186

                         170
                  ....*....|...
gi 1005574743 231 FNMGAMAFSLLGG 243
Cdd:cd14193   187 WSLGVIAYMLLSG 199
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
 68-243 9.83e-04

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk 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: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 40.01  E-value: 9.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005574743  68 EGTAGDAIKRLKNSV-TIYEDLKHESLIRLIDHFPVQSGYVLIFDWFDGECLHSHwrfpspekyknpnspFYKFRHLSAI 146
Cdd:cd14174    36 EKNAGHSRSRVFREVeTLYQCQGNKNILELIEFFEDDTRFYLVFEKLRGGSILAH---------------IQKRKHFNER 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005574743 147 ERIHSLHSIFSFHTYVEKKNYVAIDFYDGSILYNF--NTNETKICDIDLYSKKPYIN--------KMGRLWGSSRFMSPE 216
Cdd:cd14174   101 EASRVVRDIASALDFLHTKGIAHRDLKPENILCESpdKVSPVKICDFDLGSGVKLNSactpittpELTTPCGSAEYMAPE 180

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1005574743 217 EFEL----NAIIDERTNVFNMGAMAFSLLGG 243
Cdd:cd14174   181 VVEVftdeATFYDKRCDLWSLGVILYIMLSG 211
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
 161-274 3.56e-03

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Protein Kinase regulated by RNA; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKR (or EIF2AK2) contains an N-terminal double-stranded RNA (dsRNA) binding domain and a C-terminal catalytic kinase domain. It is activated by dsRNA, which is produced as a replication intermediate in virally infected cells. It plays a key role in mediating innate immune responses to viral infection. PKR is also directly activated by PACT (protein activator of PKR) and heparin, and is inhibited by viral proteins and RNAs. PKR also regulates transcription and signal transduction in diseased cells, playing roles in tumorigenesis and neurodegenerative diseases. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PKR 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: 270949 [Multi-domain]  Cd Length: 267  Bit Score: 38.24  E-value: 3.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005574743 161 YVEKKNYVAIDFYDGSILYNfNTNETKICDIDLYSKKPYINKMGRLWGSSRFMSPEEFELNAiIDERTNVFNMGAMAFSL 240
Cdd:cd14047   132 YIHSKKLIHRDLKPSNIFLV-DTGKVKIGDFGLVTSLKNDGKRTKSKGTLSYMSPEQISSQD-YGKEVDIYALGLILFEL 209

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1005574743 241 LGGEKDRSfikwEASKELYEVAHRAVSDNRTERY 274
Cdd:cd14047   210 LHVCDSAF----EKSKFWTDLRNGILPDIFDKRY 239
 
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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