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Conserved domains on  [gi|29896335|gb|AAP09615|]
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Serine/threonine protein kinase [Bacillus cereus ATCC 14579]

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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 ...
69-283 1.42e-07

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 cd14014:

Pssm-ID: 304357 [Multi-domain]  Cd Length: 260  Bit Score: 50.28  E-value: 1.42e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29896335  69 GTTGDAIERLKNSVTIYEDLKHKSLIRLIDHFPVQSGYVLIFDWFDGECLHS----HWRFPSPEKYKnpnspfyKFRH-L 143
Cdd:cd14014  38 AEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVMEYVEGGSLADllreRGPLPPREALR-------ILAQiA 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29896335 144 SAIERIHSLHSIfsfHSYVekK--NyvaidfydgsILYNFNtNETKICD--IDLYSKKPYINRMGRLWGSSRFMSPEEFE 219
Cdd:cd14014 111 DALAAAHRAGIV---HRDI--KpaN----------ILLTED-GRVKLTDfgIARALGDSGLTQTGSVLGTPAYMAPEQAR 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29896335 220 lNATIDERTNVFNMGAMAFSLLGGE---------KDRSFIKWEA-----------SKELYEVAYRAVNANRAERYASVIE 279
Cdd:cd14014 175 -GGPVDPRSDIYSLGVVLYELLTGRppfdgdspaAVLAKHLQEAppppsplnpdvPPALDAIILRALAKDPEERPQSAAE 253

                ....
gi 29896335 280 FYEA 283
Cdd:cd14014 254 LLAA 257
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
71-251 3.60e-10

Serine/threonine protein kinase [Signal transduction mechanisms];


:

Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 58.99  E-value: 3.60e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29896335  71 TGDAIERLKNSVTIYEDLKHKSLI-RLIDHFPVQSGYVLIFDWFDGECLHSHWR-FPSPEKYKNPNSPFYKFRHLSAIER 148
Cdd:COG0515  37 KSKEVERFLREIQILASLNHPPNIvKLYDFFQDEGSLYLVMEYVDGGSLEDLLKkIGRKGPLSESEALFILAQILSALEY 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29896335 149 IHSLHSIfsfHSYVEKKNyvaidfydgsILYNFNTNETKICDI-------DLYSKKPYINRMGRLWGSSRFMSPEEFEL- 220
Cdd:COG0515 117 LHSKGII---HRDIKPEN----------ILLDRDGRVVKLIDFglakllpDPGSTSSIPALPSTSVGTPGYMAPEVLLGl 183
                       170       180       190
                ....*....|....*....|....*....|..
gi 29896335 221 -NATIDERTNVFNMGAMAFSLLGGEKDRSFIK 251
Cdd:COG0515 184 sLAYASSSSDIWSLGITLYELLTGLPPFEGEK 215
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
69-283 1.42e-07

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB 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: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 50.28  E-value: 1.42e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29896335  69 GTTGDAIERLKNSVTIYEDLKHKSLIRLIDHFPVQSGYVLIFDWFDGECLHS----HWRFPSPEKYKnpnspfyKFRH-L 143
Cdd:cd14014  38 AEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVMEYVEGGSLADllreRGPLPPREALR-------ILAQiA 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29896335 144 SAIERIHSLHSIfsfHSYVekK--NyvaidfydgsILYNFNtNETKICD--IDLYSKKPYINRMGRLWGSSRFMSPEEFE 219
Cdd:cd14014 111 DALAAAHRAGIV---HRDI--KpaN----------ILLTED-GRVKLTDfgIARALGDSGLTQTGSVLGTPAYMAPEQAR 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29896335 220 lNATIDERTNVFNMGAMAFSLLGGE---------KDRSFIKWEA-----------SKELYEVAYRAVNANRAERYASVIE 279
Cdd:cd14014 175 -GGPVDPRSDIYSLGVVLYELLTGRppfdgdspaAVLAKHLQEAppppsplnpdvPPALDAIILRALAKDPEERPQSAAE 253

                ....
gi 29896335 280 FYEA 283
Cdd:cd14014 254 LLAA 257
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
71-251 3.60e-10

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 58.99  E-value: 3.60e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29896335  71 TGDAIERLKNSVTIYEDLKHKSLI-RLIDHFPVQSGYVLIFDWFDGECLHSHWR-FPSPEKYKNPNSPFYKFRHLSAIER 148
Cdd:COG0515  37 KSKEVERFLREIQILASLNHPPNIvKLYDFFQDEGSLYLVMEYVDGGSLEDLLKkIGRKGPLSESEALFILAQILSALEY 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29896335 149 IHSLHSIfsfHSYVEKKNyvaidfydgsILYNFNTNETKICDI-------DLYSKKPYINRMGRLWGSSRFMSPEEFEL- 220
Cdd:COG0515 117 LHSKGII---HRDIKPEN----------ILLDRDGRVVKLIDFglakllpDPGSTSSIPALPSTSVGTPGYMAPEVLLGl 183
                       170       180       190
                ....*....|....*....|....*....|..
gi 29896335 221 -NATIDERTNVFNMGAMAFSLLGGEKDRSFIK 251
Cdd:COG0515 184 sLAYASSSSDIWSLGITLYELLTGLPPFEGEK 215
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
69-283 1.42e-07

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB 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: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 50.28  E-value: 1.42e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29896335  69 GTTGDAIERLKNSVTIYEDLKHKSLIRLIDHFPVQSGYVLIFDWFDGECLHS----HWRFPSPEKYKnpnspfyKFRH-L 143
Cdd:cd14014  38 AEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVMEYVEGGSLADllreRGPLPPREALR-------ILAQiA 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29896335 144 SAIERIHSLHSIfsfHSYVekK--NyvaidfydgsILYNFNtNETKICD--IDLYSKKPYINRMGRLWGSSRFMSPEEFE 219
Cdd:cd14014 111 DALAAAHRAGIV---HRDI--KpaN----------ILLTED-GRVKLTDfgIARALGDSGLTQTGSVLGTPAYMAPEQAR 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29896335 220 lNATIDERTNVFNMGAMAFSLLGGE---------KDRSFIKWEA-----------SKELYEVAYRAVNANRAERYASVIE 279
Cdd:cd14014 175 -GGPVDPRSDIYSLGVVLYELLTGRppfdgdspaAVLAKHLQEAppppsplnpdvPPALDAIILRALAKDPEERPQSAAE 253

                ....
gi 29896335 280 FYEA 283
Cdd:cd14014 254 LLAA 257
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
76-243 3.31e-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: 46.11  E-value: 3.31e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29896335  76 ERLKNSVTIYEDLKHKSLIRLIDHFPVQSGYVLIFDWFDGEclhshwrfpspEKYKNPNSPFYKFRHLSAI-------ER 148
Cdd:cd14192  46 EEVKNEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVDGG-----------ELFDRITDESYQLTELDAIlftrqicEG 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29896335 149 IHSLHSIFSFHSYVEKKNYVAIdfydgsilyNFNTNETKICDIDLYSKKPYINRMGRLWGSSRFMSPEEFELNaTIDERT 228
Cdd:cd14192 115 VHYLHQHYILHLDLKPENILCV---------NSTGNQIKIIDFGLARRYKPREKLKVNFGTPEFLAPEVVNYD-FVSFPT 184
                       170
                ....*....|....*
gi 29896335 229 NVFNMGAMAFSLLGG 243
Cdd:cd14192 185 DMWSVGVITYMLLSG 199
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
84-243 1.11e-04

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 2; 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: 271075 [Multi-domain]  Cd Length: 288  Bit Score: 41.55  E-value: 1.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29896335  84 IYEDLKHKSLIRLIDHFPVQSGYVLIFDWFDGECLHSHwrfpspekyknpnspFYKFRHLSAIERIHSLHSIFSFHSYVE 163
Cdd:cd14173  53 LYQCQGHRNVLELIEFFEEEDKFYLVFEKMRGGSILSH---------------IHRRRHFNELEASVVVQDIASALDFLH 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29896335 164 KKNYVAIDFYDGSIL--YNFNTNETKICDIDLYSKKPYINRMGRL--------WGSSRFMSP---EEFELNATI-DERTN 229
Cdd:cd14173 118 NKGIAHRDLKPENILceHPNQVSPVKICDFDLGSGIKLNSDCSPIstpelltpCGSAEYMAPevvEAFNEEASIyDKRCD 197
                       170
                ....*....|....
gi 29896335 230 VFNMGAMAFSLLGG 243
Cdd:cd14173 198 LWSLGVILYIMLSG 211
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
68-243 2.31e-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: 40.78  E-value: 2.31e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29896335  68 EGTTGDAIERLKNSV-TIYEDLKHKSLIRLIDHFPVQSGYVLIFDWFDGECLHSHwrfpspekyknpnspFYKFRHLSAI 146
Cdd:cd14174  36 EKNAGHSRSRVFREVeTLYQCQGNKNILELIEFFEDDTRFYLVFEKLRGGSILAH---------------IQKRKHFNER 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29896335 147 ERIHSLHSIFSFHSYVEKKNYVAIDFYDGSILYNF--NTNETKICDIDLYSKKPYIN--------RMGRLWGSSRFMSPE 216
Cdd:cd14174 101 EASRVVRDIASALDFLHTKGIAHRDLKPENILCESpdKVSPVKICDFDLGSGVKLNSactpittpELTTPCGSAEYMAPE 180
                       170       180       190
                ....*....|....*....|....*....|.
gi 29896335 217 EFEL---NATI-DERTNVFNMGAMAFSLLGG 243
Cdd:cd14174 181 VVEVftdEATFyDKRCDLWSLGVILYIMLSG 211
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
76-243 4.51e-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: 39.51  E-value: 4.51e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29896335  76 ERLKNSVTIYEDLKHKSLIRLIDHFPVQSGYVLIFDWFDGECLHshwrfpspEKYKNPNspfYKFRHLSAI-------ER 148
Cdd:cd14193  46 EEVKNEIEVMNQLNHANLIQLYDAFESRNDIVLVMEYVDGGELF--------DRIIDEN---YNLTELDTIlfikqicEG 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29896335 149 IHSLHSIFSFHSYVEKKNYVAIdfydgsilyNFNTNETKICDIDLYSKKPYINRMGRLWGSSRFMSPEEFELNaTIDERT 228
Cdd:cd14193 115 IQYMHQMYILHLDLKPENILCV---------SREANQVKIIDFGLARRYKPREKLRVNFGTPEFLAPEVVNYE-FVSFPT 184
                       170
                ....*....|....*
gi 29896335 229 NVFNMGAMAFSLLGG 243
Cdd:cd14193 185 DMWSLGVIAYMLLSG 199
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
90-224 7.24e-04

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: 38.87  E-value: 7.24e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29896335  90 HKSLIRLIDHFPVQSGYVLIFDWFDG----ECLHSHWRFP-SPEKYKNpnspfyKFRHL-SAIERIHSlHSIFsfHSYVE 163
Cdd:cd13993  64 HPNIITLHDVFETEVAIYIVLEYCPNgdlfEAITENRIYVgKTELIKN------VFLQLiDAVKHCHS-LGIY--HRDIK 134
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29896335 164 KKNyvaidfydgsILYNFNTNETKICDIDLYSKKPYINRMGRlwGSSRFMSPEEFELNATI 224
Cdd:cd13993 135 PEN----------ILLSQDEGTVKLCDFGLATTEKISMDFGV--GSEFYMAPECFDEVGRS 183
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
88-256 1.26e-03

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated Kinase-1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAK1 is also known as mitogen-activated protein kinase kinase kinase 7 (MAPKKK7 or MAP3K7), TAK, or MEKK7. As a MAPKKK, it is an important mediator of cellular responses to extracellular signals. It regulates both the c-Jun N-terminal kinase and p38 MAPK cascades by activating the MAPK kinases, MKK4 and MKK3/6. In addition, TAK1 plays diverse roles in immunity and development, in different biological contexts, through many signaling pathways including TGFbeta/BMP, Wnt/Fz, and NF-kB. It is also implicated in the activation of the tumor suppressor kinase, LKB1. The TAK1 subfamily 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: 270960 [Multi-domain]  Cd Length: 253  Bit Score: 38.19  E-value: 1.26e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29896335  88 LKHKSLIRLIDHFPVQSGYVLIFDWFDGECLHS--HWRFPSPEkYKNPNSPFYKFRHLSAIERIHSLHSIFSFHSYVEKK 165
Cdd:cd14058  43 VDHPNIIKLYGACSNQKPVCLVMEYAEGGSLYNvlHGKEPKPI-YTAAHAMSWALQCAKGVAYLHSMKPKALIHRDLKPP 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29896335 166 NYvaidfydgsILYNFNTNeTKICDIDLYSKKPyiNRMGRLWGSSRFMSPEEFE-LNATidERTNVFNMGAM-------- 236
Cdd:cd14058 122 NL---------LLTNGGTV-LKICDFGTACDIS--THMTNNKGSAAWMAPEVFEgSKYS--EKCDVFSWGIIlwevitrr 187
                       170       180
                ....*....|....*....|.
gi 29896335 237 -AFSLLGGEkdRSFIKWEASK 256
Cdd:cd14058 188 kPFDHIGGP--AFRIMWAVHN 206
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
55-244 1.33e-03

Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chk1 is implicated in many major checkpoints of the cell cycle, providing a link between upstream sensors and the cell cycle engine. It plays an important role in DNA damage response and maintaining genomic stability. Chk1 acts as an effector of the sensor kinase, ATR (ATM and Rad3-related), a member of the PI3K family, which is activated upon DNA replication stress. Chk1 delays mitotic entry in response to replication blocks by inhibiting cyclin dependent kinase (Cdk) activity. In addition, Chk1 contributes to the function of centrosome and spindle-based checkpoints, inhibits firing of origins of DNA replication (Ori), and represses transcription of cell cycle proteins including cyclin B and Cdk1. The Chk1 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: 270971 [Multi-domain]  Cd Length: 261  Bit Score: 38.08  E-value: 1.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29896335  55 KFIKYAGAqtiayegtTGDAIERLKNSVTIYEDLKHKSLIRLIDHFPVQSGYVLIFDWFDGECLHSHWRF----PSPEky 130
Cdd:cd14069  32 KFVDMKRA--------PGDCPENIKKEVCIQKMLSHKNVVRFYGHRREGEFQYLFLEYASGGELFDKIEPdvgmPEDV-- 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29896335 131 knpnSPFYkFRHLsaIERIHSLHSIFSFHSYVEKKNyvaidfydgsILYNFNTNeTKICDIDLYSKKPYINR---MGRLW 207
Cdd:cd14069 102 ----AQFY-FQQL--MAGLKYLHSCGITHRDIKPEN----------LLLDENDN-LKISDFGLATVFRYKGKerlLNKMC 163
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 29896335 208 GSSRFMSPEEFELNATIDERTNVFNMGAMAFSLLGGE 244
Cdd:cd14069 164 GTLPYVAPELLAKKKYRAEPVDVWSCGIVLFAMLAGE 200
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
75-243 3.61e-03

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK4, also called SAK or STK18, is structurally different from other PLKs in that it contains only one polo box that can form two adjacent polo boxes and a functional PDB by homodimerization. It is required for late mitotic progression, cell survival, and embryonic development. It localizes to centrosomes and is required for centriole duplication and chromosomal stability. Overexpression of PLK4 may be associated with colon tumors. The PLK4 subfamily 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: 271088 [Multi-domain]  Cd Length: 256  Bit Score: 36.76  E-value: 3.61e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29896335  75 IERLKNSVTIYEDLKHKSLIRLIDHFPvQSGYV-LIFDWFDGECLHSHwrfpspekYKNPNSPFykfrhlSAIERIHSLH 153
Cdd:cd14186  45 VQRVRNEVEIHCQLKHPSILELYNYFE-DSNYVyLVLEMCHNGEMSRY--------LKNRKKPF------TEDEARHFMH 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29896335 154 SIFSFHSYVEKKNYVAIDFYDGSILYNFNTNeTKICDIDLYS--KKPYINRMgRLWGSSRFMSPEEFELNATIDErTNVF 231
Cdd:cd14186 110 QIVTGMLYLHSHGILHRDLTLSNLLLTRNMN-IKIADFGLATqlKMPHEKHF-TMCGTPNYISPEIATRSAHGLE-SDVW 186
                       170
                ....*....|..
gi 29896335 232 NMGAMAFSLLGG 243
Cdd:cd14186 187 SLGCMFYTLLVG 198
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
161-241 4.57e-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: 36.70  E-value: 4.57e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29896335 161 YVEKKNYVAIDFYDGSILYNfNTNETKICDIDLYSKKPYINRMGRLWGSSRFMSPEEFELNaTIDERTNVFNMGAMAFSL 240
Cdd:cd14047 132 YIHSKKLIHRDLKPSNIFLV-DTGKVKIGDFGLVTSLKNDGKRTKSKGTLSYMSPEQISSQ-DYGKEVDIYALGLILFEL 209

                .
gi 29896335 241 L 241
Cdd:cd14047 210 L 210
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
84-268 6.04e-03

Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin 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: 271009 [Multi-domain]  Cd Length: 257  Bit Score: 36.02  E-value: 6.04e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29896335  84 IYEDLKHKSLIRLIDHFPVQSGYVLIFDWFDGECLHSHWrfpspekyknpnspfykFRHLSAIERIHSLH--SIFSFHSY 161
Cdd:cd14107  51 ILARLSHRRLTCLLDQFETRKTLILILELCSSEELLDRL-----------------FLKGVVTEAEVKLYiqQVLEGIGY 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29896335 162 VEKKNYVAIDFYDGSILYNFNTNE-TKICDIDLYSKKPYINRMGRLWGSSRFMSPEEFELNAtIDERTNVFNMGAMAF-- 238
Cdd:cd14107 114 LHGMNILHLDIKPDNILMVSPTREdIKICDFGFAQEITPSEHQFSKYGSPEFVAPEIVHQEP-VSAATDIWALGVIAYls 192
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 29896335 239 ----SLLGGEKDRSFIKWEASKELY----EVAYRAVNA 268
Cdd:cd14107 193 ltchSPFAGENDRATLLNVAEGVVSwdtpEITHLSEDA 230
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
71-251 3.60e-10

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 58.99  E-value: 3.60e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29896335  71 TGDAIERLKNSVTIYEDLKHKSLI-RLIDHFPVQSGYVLIFDWFDGECLHSHWR-FPSPEKYKNPNSPFYKFRHLSAIER 148
Cdd:COG0515  37 KSKEVERFLREIQILASLNHPPNIvKLYDFFQDEGSLYLVMEYVDGGSLEDLLKkIGRKGPLSESEALFILAQILSALEY 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29896335 149 IHSLHSIfsfHSYVEKKNyvaidfydgsILYNFNTNETKICDI-------DLYSKKPYINRMGRLWGSSRFMSPEEFEL- 220
Cdd:COG0515 117 LHSKGII---HRDIKPEN----------ILLDRDGRVVKLIDFglakllpDPGSTSSIPALPSTSVGTPGYMAPEVLLGl 183
                       170       180       190
                ....*....|....*....|....*....|..
gi 29896335 221 -NATIDERTNVFNMGAMAFSLLGGEKDRSFIK 251
Cdd:COG0515 184 sLAYASSSSDIWSLGITLYELLTGLPPFEGEK 215
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.15
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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