NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|445948666|ref|WP_000026521|]
View 

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 39-162 4.61e-04

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 cd05122:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 254  Bit Score: 40.26  E-value: 4.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445948666  39 KCLGTGNYAAVF--MHKEHKgwvvKVYARKG---EGIEKESEVYRRIG-----NHP-------SYsrlIYKGENFIVLKR 101
Cdd:cd05122    6 EKIGKGGFGVVYkaRHKKTG----QIVAIKKinlESKEKKESILNEIAilkkcKHPnivkyygSY---LKKDELWIVMEF 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 445948666 102 LKEITLYDAI-HKGIKIPKQ----VILDINEALEYAREQGLTPCDVHGKNVMM-ENGRgyvVDVSDF 162
Cdd:cd05122   79 CSGGSLKDLLkNTNKTLTEQqiayVCKEVLKGLEYLHSHGIIHRDIKAANILLtSDGE---VKLIDF 142
 
Name Accession Description Interval E-value
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
 39-162 4.61e-04

Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. This family is composed of STKs, and some dual-specificity PKs that phosphorylate both threonine and tyrosine residues of target proteins. Most members are kinases involved in mitogen-activated protein kinase (MAPK) signaling cascades, acting as MAPK kinases (MAPKKs), MAPKK kinases (MAPKKKs), or MAPKKK kinases (MAP4Ks). The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPKK, which itself is phosphorylated and activated by a MAPKKK. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAPKKK to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Other STE family members include p21-activated kinases (PAKs) and class III myosins, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain, which can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, as well as autophosphorylate the C-terminal motor domain. They play an important role in maintaining the structural integrity of photoreceptor cell microvilli. The STE family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 40.26  E-value: 4.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445948666  39 KCLGTGNYAAVF--MHKEHKgwvvKVYARKG---EGIEKESEVYRRIG-----NHP-------SYsrlIYKGENFIVLKR 101
Cdd:cd05122    6 EKIGKGGFGVVYkaRHKKTG----QIVAIKKinlESKEKKESILNEIAilkkcKHPnivkyygSY---LKKDELWIVMEF 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 445948666 102 LKEITLYDAI-HKGIKIPKQ----VILDINEALEYAREQGLTPCDVHGKNVMM-ENGRgyvVDVSDF 162
Cdd:cd05122   79 CSGGSLKDLLkNTNKTLTEQqiayVCKEVLKGLEYLHSHGIIHRDIKAANILLtSDGE---VKLIDF 142
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
 86-172 1.47e-03

putative serine/threonine kinase; Provisional


Pssm-ID: 165211 [Multi-domain]  Cd Length: 294  Bit Score: 38.78  E-value: 1.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445948666  86 YSRLIYKgenFIVLKRLKEIT---LYDAIHKGIKIPKQVILDINEALEYAREQGLTPCDVHGKNVMME-NGRGYVVD--- 158
Cdd:PHA02882  96 RCRMYYR---FILLEKLVENTkeiFKRIKCKNKKLIKNIMKDMLTTLEYIHEHGISHGDIKPENIMVDgNNRGYIIDygi 172

                         90       100
                 ....*....|....*....|.
gi 445948666 159 VSDFL-------KTKEDSKWR 172
Cdd:PHA02882 173 ASHFIihgkhieYSKEQKDLH 193
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
39-162 2.54e-03

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 38.46  E-value: 2.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445948666  39 KCLGTGNYAAVFM-HKEHKGW--VVKV----YARKGEGIE---KESEVYRRIgNHPS----YSRLIYKGENFIVLKRLKE 104
Cdd:COG0515   13 RLLGRGGMGVVYLaRDLRLGRpvALKVlrpeLAADPEARErfrREARALARL-NHPNivrvYDVGEEDGRPYLVMEYVEG 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 445948666 105 ITLYDAIHKGIKIP----KQVILDINEALEYAREQGLtpcdVHG--K--NVMMeNGRGYVVdVSDF 162
Cdd:COG0515   92 ESLADLLRRRGPLPpaeaLRILAQLAEALAAAHAAGI----VHRdiKpaNILL-TPDGRVK-LIDF 151
 
Name Accession Description Interval E-value
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
 39-162 4.61e-04

Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. This family is composed of STKs, and some dual-specificity PKs that phosphorylate both threonine and tyrosine residues of target proteins. Most members are kinases involved in mitogen-activated protein kinase (MAPK) signaling cascades, acting as MAPK kinases (MAPKKs), MAPKK kinases (MAPKKKs), or MAPKKK kinases (MAP4Ks). The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPKK, which itself is phosphorylated and activated by a MAPKKK. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAPKKK to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Other STE family members include p21-activated kinases (PAKs) and class III myosins, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain, which can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, as well as autophosphorylate the C-terminal motor domain. They play an important role in maintaining the structural integrity of photoreceptor cell microvilli. The STE family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 40.26  E-value: 4.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445948666  39 KCLGTGNYAAVF--MHKEHKgwvvKVYARKG---EGIEKESEVYRRIG-----NHP-------SYsrlIYKGENFIVLKR 101
Cdd:cd05122    6 EKIGKGGFGVVYkaRHKKTG----QIVAIKKinlESKEKKESILNEIAilkkcKHPnivkyygSY---LKKDELWIVMEF 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 445948666 102 LKEITLYDAI-HKGIKIPKQ----VILDINEALEYAREQGLTPCDVHGKNVMM-ENGRgyvVDVSDF 162
Cdd:cd05122   79 CSGGSLKDLLkNTNKTLTEQqiayVCKEVLKGLEYLHSHGIIHRDIKAANILLtSDGE---VKLIDF 142
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
 41-162 8.02e-04

Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and more than 500 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase.


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 39.18  E-value: 8.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445948666  41 LGTGNYAAVFM---HKEHKGWVVKVYARKGEG-----IEKESEVYRRIgNHPS----YSRLIYKGENFIVLKRLKEITLY 108
Cdd:cd00180    1 LGKGSFGKVYKardKETGKKVAVKVIPKEKLKklleeLLREIEILKKL-NHPNivklYDVFETENFLYLVMEYCEGGSLK 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 445948666 109 DAIHKGIKIP-----KQVILDINEALEYAREQGLTPCDVHGKNVMMeNGRGYVVdVSDF 162
Cdd:cd00180   80 DLLKENKGPLseeeaLSILRQLLSALEYLHSNGIIHRDLKPENILL-DSDGTVK-LADF 136
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
 86-172 1.47e-03

putative serine/threonine kinase; Provisional


Pssm-ID: 165211 [Multi-domain]  Cd Length: 294  Bit Score: 38.78  E-value: 1.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445948666  86 YSRLIYKgenFIVLKRLKEIT---LYDAIHKGIKIPKQVILDINEALEYAREQGLTPCDVHGKNVMME-NGRGYVVD--- 158
Cdd:PHA02882  96 RCRMYYR---FILLEKLVENTkeiFKRIKCKNKKLIKNIMKDMLTTLEYIHEHGISHGDIKPENIMVDgNNRGYIIDygi 172

                         90       100
                 ....*....|....*....|.
gi 445948666 159 VSDFL-------KTKEDSKWR 172
Cdd:PHA02882 173 ASHFIihgkhieYSKEQKDLH 193
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
39-162 2.54e-03

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 38.46  E-value: 2.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445948666  39 KCLGTGNYAAVFM-HKEHKGW--VVKV----YARKGEGIE---KESEVYRRIgNHPS----YSRLIYKGENFIVLKRLKE 104
Cdd:COG0515   13 RLLGRGGMGVVYLaRDLRLGRpvALKVlrpeLAADPEARErfrREARALARL-NHPNivrvYDVGEEDGRPYLVMEYVEG 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 445948666 105 ITLYDAIHKGIKIP----KQVILDINEALEYAREQGLtpcdVHG--K--NVMMeNGRGYVVdVSDF 162
Cdd:COG0515   92 ESLADLLRRRGPLPpaeaLRILAQLAEALAAAHAAGI----VHRdiKpaNILL-TPDGRVK-LIDF 151
 
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