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Conserved domains on  [gi|32481209|ref|NP_116584|]
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MAP kinase-activated protein kinase 2 isoform 2 [Homo sapiens]

Protein Classification

STKc_MAPKAPK2 domain-containing protein (domain architecture ID 10197684)

STKc_MAPKAPK2 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
61-363 0e+00

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 2 (MAPKAP2 or MK2) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK2 is a bonafide substrate for the MAPK p38. It is closely related to MK3 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. The MK2 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: 271072  Cd Length: 303  Bit Score: 624.75  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209  61 DDYKVTSQVLGLGINGKVLQIFNKRTQEKFALKMLQDCPKARREVELHWRASQCPHIVRIVDVYENLYAGRKCLLIVMEC 140
Cdd:cd14170   1 DDYKVTSQVLGLGINGKVLQIFNKRTQEKFALKMLQDCPKARREVELHWRASQCPHIVRIVDVYENLYAGRKCLLIVMEC 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209 141 LDGGELFSRIQDRGDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAILKLTDFGFAKETTSHNSL 220
Cdd:cd14170  81 LDGGELFSRIQDRGDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAILKLTDFGFAKETTSHNSL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209 221 TTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAISPGMKTRIRMGQYEFPNPEWSEVSEEVKM 300
Cdd:cd14170 161 TTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAISPGMKTRIRMGQYEFPNPEWSEVSEEVKM 240
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32481209 301 LIRNLLKTEPTQRMTITEFMNHPWIMQSTKVPQTPLHTSRVLKEDKERWEDVKEEMTSALATM 363
Cdd:cd14170 241 LIRNLLKTEPTQRMTITEFMNHPWIMQSTKVPQTPLHTSRVLKEDKERWEDVKEEMTSALATM 303
 
Name Accession Description Interval E-value
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
61-363 0e+00

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 2 (MAPKAP2 or MK2) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK2 is a bonafide substrate for the MAPK p38. It is closely related to MK3 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. The MK2 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: 271072  Cd Length: 303  Bit Score: 624.75  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209  61 DDYKVTSQVLGLGINGKVLQIFNKRTQEKFALKMLQDCPKARREVELHWRASQCPHIVRIVDVYENLYAGRKCLLIVMEC 140
Cdd:cd14170   1 DDYKVTSQVLGLGINGKVLQIFNKRTQEKFALKMLQDCPKARREVELHWRASQCPHIVRIVDVYENLYAGRKCLLIVMEC 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209 141 LDGGELFSRIQDRGDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAILKLTDFGFAKETTSHNSL 220
Cdd:cd14170  81 LDGGELFSRIQDRGDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAILKLTDFGFAKETTSHNSL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209 221 TTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAISPGMKTRIRMGQYEFPNPEWSEVSEEVKM 300
Cdd:cd14170 161 TTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAISPGMKTRIRMGQYEFPNPEWSEVSEEVKM 240
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32481209 301 LIRNLLKTEPTQRMTITEFMNHPWIMQSTKVPQTPLHTSRVLKEDKERWEDVKEEMTSALATM 363
Cdd:cd14170 241 LIRNLLKTEPTQRMTITEFMNHPWIMQSTKVPQTPLHTSRVLKEDKERWEDVKEEMTSALATM 303
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
68-325 1.64e-93

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567  Cd Length: 254  Bit Score: 284.81  E-value: 1.64e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209     68 QVLGLGINGKVLQIFNKRTQEKFALKML------QDCPKARREVELHWRAsQCPHIVRIVDVYENlyagRKCLLIVMECL 141
Cdd:smart00220   5 EKLGEGSFGKVYLARDKKTGKLVAIKVIkkkkikKDRERILREIKILKKL-KHPNIVRLYDVFED----EDKLYLVMEYC 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209    142 DGGELFSRIQDRGdqAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSkrpNAILKLTDFGFAKETTSHNSLT 221
Cdd:smart00220  80 EGGDLFDLLKKRG--RLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDE---DGHVKLADFGLARQLDPGEKLT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209    222 TPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAIspgMKTRIRMGQYEFPNPEWsEVSEEVKML 301
Cdd:smart00220 155 TFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLE---LFKKIGKPKPPFPPPEW-DISPEAKDL 230
                          250       260
                   ....*....|....*....|....
gi 32481209    302 IRNLLKTEPTQRMTITEFMNHPWI 325
Cdd:smart00220 231 IRKLLVKDPEKRLTAEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
65-325 3.60e-82

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 255.60  E-value: 3.60e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209    65 VTSQVLGLGINGKVLQIFNKRTQEKFALKML-------QDCPKARREVELHwRASQCPHIVRIVDVYE---NLYagrkcl 134
Cdd:pfam00069   2 EVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIkkekikkKKDKNILREIKIL-KKLNHPNIVRLYDAFEdkdNLY------ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209   135 lIVMECLDGGELFSRIQDRGdqAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKrpnAILKLTDFGFAKET 214
Cdd:pfam00069  75 -LVLEYVEGGSLFDLLSEKG--AFSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENILIDED---GNLKITDFGLARQL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209   215 TSHNSLTTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAIspgmKTRIRMGQYEFpnPEWSEV 294
Cdd:pfam00069 149 NSGSSLTSFVGTPWYMAPEVLRGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEI----YEKIIDQDFDS--PRPSSI 222
                         250       260       270
                  ....*....|....*....|....*....|.
gi 32481209   295 SEEVKMLIRNLLKTEPTQRMTITEFMNHPWI 325
Cdd:pfam00069 223 SEEAKDLLKKLLKKDPSKRLTATEALQHPWF 253
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
62-386 8.83e-42

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 153.36  E-value: 8.83e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209  62 DYKVTsQVLGLGINGKVLQIFNKRtqeKFALKML--------QDCPKARREVELHWRASQCPHIVRIVDVYENlyagRKC 133
Cdd:COG0515   1 SYRIL-RKLGEGSFGEVYLARDRK---LVALKVLakklesksKEVERFLREIQILASLNHPPNIVKLYDFFQD----EGS 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209 134 LLIVMECLDGGELFSRIQDRGDQA-FTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKrpNAILKLTDFGFAK 212
Cdd:COG0515  73 LYLVMEYVDGGSLEDLLKKIGRKGpLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRD--GRVVKLIDFGLAK 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209 213 ETTSHNS-------LTTPCYTPYYVAPEVLG---PEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAISPGMKTRIRMG 282
Cdd:COG0515 151 LLPDPGStssipalPSTSVGTPGYMAPEVLLglsLAYASSSSDIWSLGITLYELLTGLPPFEGEKNSSATSQTLKIILEL 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209 283 QYEFPNPEWS-----EVSEEVKMLIRNLLKTEPTQRMTITEFMNHPWIMQ--STKVPQTPLHTSRVLKEDKERWEDVKEE 355
Cdd:COG0515 231 PTPSLASPLSpsnpeLISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHlkLKESDLSDLLKPDDSAPLRLSLPPSLEA 310
                       330       340       350
                ....*....|....*....|....*....|.
gi 32481209 356 MTSALATMRVDYEQIKIKKIEDASNPLLLKR 386
Cdd:COG0515 311 LISSLNSLAISGSDLKLDDSNFSKELAPNGV 341
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
70-324 6.48e-37

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289  Cd Length: 329  Bit Score: 138.41  E-value: 6.48e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209   70 LGLGINGKVLQIFNKRTQEKFALKMLQdcpkaRREVelhWRASQCPHIVR------------IVDVYENLYAGRKcLLIV 137
Cdd:PTZ00263  26 LGTGSFGRVRIAKHKGTGEYYAIKCLK-----KREI---LKMKQVQHVAQeksilmelshpfIVNMMCSFQDENR-VYFL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209  138 MECLDGGELFSRIQDRGdqAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKrpnAILKLTDFGFAKETTSH 217
Cdd:PTZ00263  97 LEFVVGGELFTHLRKAG--RFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNK---GHVKVTDFGFAKKVPDR 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209  218 NslTTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNhglaiSPgMKT--RIRMGQYEFPNpeWseVS 295
Cdd:PTZ00263 172 T--FTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDD-----TP-FRIyeKILAGRLKFPN--W--FD 239
                        250       260       270
                 ....*....|....*....|....*....|....
gi 32481209  296 EEVKMLIRNLLKTEPTQRM-----TITEFMNHPW 324
Cdd:PTZ00263 240 GRARDLVKGLLQTDHTKRLgtlkgGVADVKNHPY 273
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
86-261 8.63e-12

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274846  Cd Length: 1266  Bit Score: 66.79  E-value: 8.63e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209     86 TQEKFALKMLQ-DCP-------KARREVELHWRASQcPHIVRIVDVYEnlyAGRKCLLIVMECLDGGELFSRIQDRGdqA 157
Cdd:TIGR03903    2 TGHEVAIKLLRtDAPeeehqraRFRRETALCARLYH-PNIVALLDSGE---APPGLLFAVFEYVPGRTLREVLAADG--A 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209    158 FTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSK--RPNAilKLTDFGF------------AKETTSHNSLTTP 223
Cdd:TIGR03903   76 LPAGETGRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTgvRPHA--KVLDFGIgtllpgvrdadvATLTRTTEVLGTP 153
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 32481209    224 CYTpyyvAPEVLGPEKYDKSCDMWSLGVIMYILLCGYP 261
Cdd:TIGR03903  154 TYC----APEQLRGEPVTPNSDLYAWGLIFLECLTGQR 187
 
Name Accession Description Interval E-value
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
61-363 0e+00

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 2 (MAPKAP2 or MK2) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK2 is a bonafide substrate for the MAPK p38. It is closely related to MK3 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. The MK2 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: 271072  Cd Length: 303  Bit Score: 624.75  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209  61 DDYKVTSQVLGLGINGKVLQIFNKRTQEKFALKMLQDCPKARREVELHWRASQCPHIVRIVDVYENLYAGRKCLLIVMEC 140
Cdd:cd14170   1 DDYKVTSQVLGLGINGKVLQIFNKRTQEKFALKMLQDCPKARREVELHWRASQCPHIVRIVDVYENLYAGRKCLLIVMEC 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209 141 LDGGELFSRIQDRGDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAILKLTDFGFAKETTSHNSL 220
Cdd:cd14170  81 LDGGELFSRIQDRGDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAILKLTDFGFAKETTSHNSL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209 221 TTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAISPGMKTRIRMGQYEFPNPEWSEVSEEVKM 300
Cdd:cd14170 161 TTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAISPGMKTRIRMGQYEFPNPEWSEVSEEVKM 240
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32481209 301 LIRNLLKTEPTQRMTITEFMNHPWIMQSTKVPQTPLHTSRVLKEDKERWEDVKEEMTSALATM 363
Cdd:cd14170 241 LIRNLLKTEPTQRMTITEFMNHPWIMQSTKVPQTPLHTSRVLKEDKERWEDVKEEMTSALATM 303
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
62-324 0e+00

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPK-activated protein kinases MK2, MK3, MK5 (also called PRAK for p38-regulated/activated protein kinase), and related proteins. These proteins contain a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. In addition, MK2 and MK3 contain an N-terminal proline-rich region that can bind to SH3 domains. MK2 and MK3 are bonafide substrates for the MAPK p38, while MK5 plays a functional role in the p38 MAPK pathway although their direct interaction has been difficult to detect. MK2 and MK3 are closely related and show, thus far, indistinguishable substrate specificity, while MK5 shows a distinct spectrum of substrates. MK2 and MK3 are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK 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: 270991  Cd Length: 263  Bit Score: 591.57  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209  62 DYKVTSQVLGLGINGKVLQIFNKRTQEKFALKMLQDCPKARREVELHWRASQCPHIVRIVDVYENLYAGRKCLLIVMECL 141
Cdd:cd14089   1 DYTISKQVLGLGINGKVLECFHKKTGEKFALKVLRDNPKARREVELHWRASGCPHIVRIIDVYENTYQGRKCLLVVMECM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209 142 DGGELFSRIQDRGDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAILKLTDFGFAKETTSHNSLT 221
Cdd:cd14089  81 EGGELFSRIQERADSAFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGPNAILKLTDFGFAKETTTKKSLQ 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209 222 TPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAISPGMKTRIRMGQYEFPNPEWSEVSEEVKML 301
Cdd:cd14089 161 TPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAISPGMKKRIRNGQYEFPNPEWSNVSEEAKDL 240
                       250       260
                ....*....|....*....|...
gi 32481209 302 IRNLLKTEPTQRMTITEFMNHPW 324
Cdd:cd14089 241 IRGLLKTDPSERLTIEEVMNHPW 263
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
59-325 0e+00

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 3 (MAPKAP3 or MK3) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK3 is a bonafide substrate for the MAPK p38. It is closely related to MK2 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK3 activity is only significant when MK2 is absent. The MK3 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: 271074  Cd Length: 267  Bit Score: 524.55  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209  59 IIDDYKVTSQVLGLGINGKVLQIFNKRTQEKFALKMLQDCPKARREVELHWRASQCPHIVRIVDVYENLYAGRKCLLIVM 138
Cdd:cd14172   1 VTDDYKLSKQVLGLGVNGKVLECFHRRTGQKCALKLLYDSPKARREVEHHWRASGGPHIVHILDVYENMHHGKRCLLIIM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209 139 ECLDGGELFSRIQDRGDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAILKLTDFGFAKETTSHN 218
Cdd:cd14172  81 ECMEGGELFSRIQERGDQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTSKEKDAVLKLTDFGFAKETTVQN 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209 219 SLTTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAISPGMKTRIRMGQYEFPNPEWSEVSEEV 298
Cdd:cd14172 161 ALQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFYSNTGQAISPGMKRRIRMGQYGFPNPEWAEVSEEA 240
                       250       260
                ....*....|....*....|....*..
gi 32481209 299 KMLIRNLLKTEPTQRMTITEFMNHPWI 325
Cdd:cd14172 241 KQLIRHLLKTDPTERMTITQFMNHPWI 267
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
62-324 6.74e-117

The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. CAMKIV is implicated in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors, as well as in T-cell development and signaling. The CAMK family also consists of other related kinases including the Phosphorylase kinase Gamma subunit (PhKG), the C-terminal kinase domains of Ribosomal S6 kinase (RSK) and Mitogen and stress-activated kinase (MSK), Doublecortin-like kinase (DCKL), and the MAPK-activated protein kinases MK2, MK3, and MK5, among others. The CAMK family 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: 270687  Cd Length: 258  Bit Score: 344.85  E-value: 6.74e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209  62 DYKVtSQVLGLGINGKVLQIFNKRTQEKFALKMLQDCP-------KARREVELHWRASqCPHIVRIVDVYENlyagRKCL 134
Cdd:cd05117   1 KYEL-GKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKlksedeeMLRREIEILKRLD-HPNIVKLYEVFED----DKNL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209 135 LIVMECLDGGELFSRIQDRGdqAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAILKLTDFGFAKET 214
Cdd:cd05117  75 YLVMELCTGGELFDRIVKKG--SFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPDSPIKIIDFGLAKIF 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209 215 TSHNSLTTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHglaiSPGMKTRIRMGQYEFPNPEWSEV 294
Cdd:cd05117 153 EEGEKLKTVCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGET----EQELFEKILKGKYSFDSPEWKNV 228
                       250       260       270
                ....*....|....*....|....*....|
gi 32481209 295 SEEVKMLIRNLLKTEPTQRMTITEFMNHPW 324
Cdd:cd05117 229 SEEAKDLIKRLLVVDPKKRLTAAEALNHPW 258
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
58-325 4.22e-108

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 5 (MAPKAP5 or MK5) is also called PRAK (p38-regulated/activated protein kinase). It contains a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK 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: 271073  Cd Length: 289  Bit Score: 323.64  E-value: 4.22e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209  58 AIIDDYKVT-SQVLGLGINGKVLQIFNKRTQEKFALKMLQDCPKARREVELHWRASQCPHIVRIVDVYEN--LYAG---- 130
Cdd:cd14171   1 SILEEYEVNwTQKLGTGISGPVRVCVKKSTGERFALKILLDRPKARTEVRLHMMCSGHPNIVQIYDVYANsvQFPGessp 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209 131 RKCLLIVMECLDGGELFSRIQDRgdQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAILKLTDFGF 210
Cdd:cd14171  81 RARLLIVMELMEGGELFDRISQH--RHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDNSEDAPIKLCDFGF 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209 211 AKEttSHNSLTTPCYTPYYVAPEVLGPEK-----------------YDKSCDMWSLGVIMYILLCGYPPFYSNH-GLAIS 272
Cdd:cd14171 159 AKV--DQGDLMTPQFTPYYVAPQVLEAQRrhrkersgiptsptpytYDKSCDMWSLGVIIYIMLCGYPPFYSEHpSRTIT 236
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 32481209 273 PGMKTRIRMGQYEFPNPEWSEVSEEVKMLIRNLLKTEPTQRMTITEFMNHPWI 325
Cdd:cd14171 237 KDMKRKIMTGSYEFPEEEWSQISEMAKDIVRKLLCVDPEERMTIEEVLHHPWL 289
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
68-325 1.64e-93

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567  Cd Length: 254  Bit Score: 284.81  E-value: 1.64e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209     68 QVLGLGINGKVLQIFNKRTQEKFALKML------QDCPKARREVELHWRAsQCPHIVRIVDVYENlyagRKCLLIVMECL 141
Cdd:smart00220   5 EKLGEGSFGKVYLARDKKTGKLVAIKVIkkkkikKDRERILREIKILKKL-KHPNIVRLYDVFED----EDKLYLVMEYC 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209    142 DGGELFSRIQDRGdqAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSkrpNAILKLTDFGFAKETTSHNSLT 221
Cdd:smart00220  80 EGGDLFDLLKKRG--RLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDE---DGHVKLADFGLARQLDPGEKLT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209    222 TPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAIspgMKTRIRMGQYEFPNPEWsEVSEEVKML 301
Cdd:smart00220 155 TFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLE---LFKKIGKPKPPFPPPEW-DISPEAKDL 230
                          250       260
                   ....*....|....*....|....
gi 32481209    302 IRNLLKTEPTQRMTITEFMNHPWI 325
Cdd:smart00220 231 IRKLLVKDPEKRLTAEEALQHPFF 254
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
83-346 1.12e-85

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK 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: 270994  Cd Length: 311  Bit Score: 266.47  E-value: 1.12e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209  83 NKRTQEKFALKMLQDCPKARREVELhWRASQC-PHIVRIVDVYEN---LYagrkcllIVMECLDGGELFSRIqdRGDQAF 158
Cdd:cd14092  27 HKKTGQEFAVKIVSRRLDTSREVQL-LRLCQGhPNIVKLHEVFQDelhTY-------LVMELLRGGELLERI--RKKKRF 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209 159 TEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAILKLTDFGFAKETTSHNSLTTPCYTPYYVAPEVL--- 235
Cdd:cd14092  97 TESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTDEDDDAEIKIVDFGFARLKPENQPLKTPCFTLPYAAPEVLkqa 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209 236 -GPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAISPGMKTRIRMGQYEFPNPEWSEVSEEVKMLIRNLLKTEPTQRM 314
Cdd:cd14092 177 lSTQGYDESCDLWSLGVILYTMLSGQVPFQSPSRNESAAEIMKRIKSGDFSFDGEEWKNVSSEAKSLIQGLLTVDPSKRL 256
                       250       260       270
                ....*....|....*....|....*....|..
gi 32481209 315 TITEFMNHPWIMQSTKVPQTPLHTSRVLKEDK 346
Cdd:cd14092 257 TMSELRNHPWLQGSSSPSSTPLMTPGVLSSSA 288
Pkinase pfam00069
Protein kinase domain;
65-325 3.60e-82

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 255.60  E-value: 3.60e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209    65 VTSQVLGLGINGKVLQIFNKRTQEKFALKML-------QDCPKARREVELHwRASQCPHIVRIVDVYE---NLYagrkcl 134
Cdd:pfam00069   2 EVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIkkekikkKKDKNILREIKIL-KKLNHPNIVRLYDAFEdkdNLY------ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209   135 lIVMECLDGGELFSRIQDRGdqAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKrpnAILKLTDFGFAKET 214
Cdd:pfam00069  75 -LVLEYVEGGSLFDLLSEKG--AFSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENILIDED---GNLKITDFGLARQL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209   215 TSHNSLTTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAIspgmKTRIRMGQYEFpnPEWSEV 294
Cdd:pfam00069 149 NSGSSLTSFVGTPWYMAPEVLRGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEI----YEKIIDQDFDS--PRPSSI 222
                         250       260       270
                  ....*....|....*....|....*....|.
gi 32481209   295 SEEVKMLIRNLLKTEPTQRMTITEFMNHPWI 325
Cdd:pfam00069 223 SEEAKDLLKKLLKKDPSKRLTATEALQHPWF 253
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
62-340 1.58e-78

C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), 90 kDa ribosomal protein S6 kinases (p90-RSKs), or p90S6Ks. The RSK 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: 270993  Cd Length: 291  Bit Score: 247.55  E-value: 1.58e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209  62 DYKVtSQVLGLGINGKVLQIFNKRTQEKFALKMLQ----DCpkaRREVELHWRASQCPHIVRIVDVYENlyaGRKCLLiV 137
Cdd:cd14091   1 EYEI-KEEIGKGSYSVCKRCIHKATGKEYAVKIIDkskrDP---SEEIEILLRYGQHPNIITLRDVYDD---GNSVYL-V 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209 138 MECLDGGELFSRIQDRGDqaFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNA-ILKLTDFGFAKETTS 216
Cdd:cd14091  73 TELLRGGELLDRILRQKF--FSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESGDPeSLRICDFGFAKQLRA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209 217 HNS-LTTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFysnhglAISPG-----MKTRIRMGQYEFPNPE 290
Cdd:cd14091 151 ENGlLMTPCYTANFVAPEVLKKQGYDAACDIWSLGVLLYTMLAGYTPF------ASGPNdtpevILARIGSGKIDLSGGN 224
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 32481209 291 WSEVSEEVKMLIRNLLKTEPTQRMTITEFMNHPWIMQSTKVPQTPLHTSR 340
Cdd:cd14091 225 WDHVSDSAKDLVRKMLHVDPSQRPTAAQVLQHPWIRNRDSLPQRQLTDPQ 274
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
59-324 1.49e-73

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270985  Cd Length: 259  Bit Score: 233.42  E-value: 1.49e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209  59 IIDDYKvTSQVLGLGINGKVLQIFNKRTQEKFALKMLQDCPKARREVELH-----WRASQCPHIVRIVDVYENlyagRKC 133
Cdd:cd14083   1 IRDKYE-FKEVLGTGAFSEVVLAEDKATGKLVAIKCIDKKALKGKEDSLEneiavLRKIKHPNIVQLLDIYES----KSH 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209 134 LLIVMECLDGGELFSRIQDRGdqAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAILKLTDFGFAKe 213
Cdd:cd14083  76 LYLVMELVTGGELFDRIVEKG--SYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYYSPDEDSKIMISDFGLSK- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209 214 TTSHNSLTTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHglaiSPGMKTRIRMGQYEFPNPEWSE 293
Cdd:cd14083 153 MEDSGVMSTACGTPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPFYDEN----DSKLFAQILKAEYEFDSPYWDD 228
                       250       260       270
                ....*....|....*....|....*....|.
gi 32481209 294 VSEEVKMLIRNLLKTEPTQRMTITEFMNHPW 324
Cdd:cd14083 229 ISDSAKDFIRHLMEKDPNKRYTCEQALEHPW 259
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
62-324 3.20e-72

Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AMPK-like subfamily is composed of AMPK, MARK, BRSK, NUAK, MELK, SNRK, TSSK, and SIK, among others. LKB1 serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. BRSKs play important roles in establishing neuronal polarity. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. The AMPK-like 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: 270905  Cd Length: 252  Bit Score: 229.71  E-value: 3.20e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209  62 DYKVtSQVLGLGINGKVLQIFNKRTQEKFALKML-------QDCPKARREVELHwRASQCPHIVRIVDVYENlyagRKCL 134
Cdd:cd14003   1 NYEL-GKTLGEGSFGKVKLARHKLTGEKVAIKIIdksklkeEIEEKIKREIEIM-KLLNHPNIIKLYEVIET----ENKI 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209 135 LIVMECLDGGELFSRIQDRGdqAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYtSKRPNaiLKLTDFGFAKET 214
Cdd:cd14003  75 YLVMEYASGGELFDYIVNNG--RLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILL-DKNGN--LKIIDFGLSNEF 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209 215 TSHNSLTTPCYTPYYVAPEVLGPEKYD-KSCDMWSLGVIMYILLCGYPPFY-SNHglaisPGMKTRIRMGQYEFPnpewS 292
Cdd:cd14003 150 RGGSLLKTFCGTPAYAAPEVLLGRKYDgPKADVWSLGVILYAMLTGYLPFDdDND-----SKLFRKILKGKYPIP----S 220
                       250       260       270
                ....*....|....*....|....*....|..
gi 32481209 293 EVSEEVKMLIRNLLKTEPTQRMTITEFMNHPW 324
Cdd:cd14003 221 HLSPDARDLIRRMLVVDPSKRITIEEILNHPW 252
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
61-325 2.14e-69

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase signal-integrating kinases; 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: 270992  Cd Length: 289  Bit Score: 223.83  E-value: 2.14e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209  61 DDYKVTSQVLGLGINGKVLQIFNKRTQEKFALKMLQDCP-----KARREVELHWRASQCPHIVRIVDVYENlyagRKCLL 135
Cdd:cd14090   1 DLYKLTGELLGEGAYASVQTCINLYTGKEYAVKIIEKHPghsrsRVFREVETLHQCQGHPNILQLIEYFED----DERFY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209 136 IVMECLDGGELFSRIQDRGdqAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAILKLTDFGFA---K 212
Cdd:cd14090  77 LVFEKMRGGPLLSHIEKRV--HFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKVSPVKICDFDLGsgiK 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209 213 ETTSHNS------LTTPCYTPYYVAPEVLG-----PEKYDKSCDMWSLGVIMYILLCGYPPFYSNHG-----------LA 270
Cdd:cd14090 155 LSSTSMTpvttpeLLTPVGSAEYMAPEVVDafvgeALSYDKRCDLWSLGVILYIMLCGYPPFYGRCGedcgwdrgeacQD 234
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 32481209 271 ISPGMKTRIRMGQYEFPNPEWSEVSEEVKMLIRNLLKTEPTQRMTITEFMNHPWI 325
Cdd:cd14090 235 CQELLFHSIQEGEYEFPEKEWSHISAEAKDLISHLLVRDASQRYTAEQVLQHPWV 289
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
68-329 1.34e-68

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I gamma; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271068  Cd Length: 285  Bit Score: 221.79  E-value: 1.34e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209  68 QVLGLGINGKVLQIFNKRTQEKFALKMLQDCPKAR-----REVELHWRASQcPHIVRIVDVYENlyagRKCLLIVMECLD 142
Cdd:cd14166   9 EVLGSGAFSEVYLVKQRSTGKLYALKCIKKSPLSRdssleNEIAVLKRIKH-ENIVTLEDIYES----TTHYYLVMQLVS 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209 143 GGELFSRIQDRGdqAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAILKLTDFGFAKeTTSHNSLTT 222
Cdd:cd14166  84 GGELFDRILERG--VYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYLTPDENSKIMITDFGLSK-MEQNGIMST 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209 223 PCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHglaiSPGMKTRIRMGQYEFPNPEWSEVSEEVKMLI 302
Cdd:cd14166 161 ACGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFYEET----ESRLFEKIKEGYYEFESPFWDDISESAKDFI 236
                       250       260
                ....*....|....*....|....*..
gi 32481209 303 RNLLKTEPTQRMTITEFMNHPWIMQST 329
Cdd:cd14166 237 RHLLEKNPSKRYTCEKALSHPWIIGNT 263
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
68-325 4.22e-66

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271069  Cd Length: 263  Bit Score: 214.51  E-value: 4.22e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209  68 QVLGLGINGKVLQIFNKRTQEKFALKMLQDCPKARREVELH-----WRASQCPHIVRIVDVYENlyagRKCLLIVMECLD 142
Cdd:cd14167   9 EVLGTGAFSEVVLAEEKRTQKLVAIKCIAKKALEGKETSIEneiavLHKIKHPNIVALDDIYES----GGHLYLIMQLVS 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209 143 GGELFSRIQDRGdqAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAILKLTDFGFAKETTSHNSLTT 222
Cdd:cd14167  85 GGELFDRIVEKG--FYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLYYSLDEDSKIMISDFGLSKIEGSGSVMST 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209 223 PCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHglaiSPGMKTRIRMGQYEFPNPEWSEVSEEVKMLI 302
Cdd:cd14167 163 ACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDEN----DAKLFEQILKAEYEFDSPYWDDISDSAKDFI 238
                       250       260
                ....*....|....*....|...
gi 32481209 303 RNLLKTEPTQRMTITEFMNHPWI 325
Cdd:cd14167 239 QHLMEKDPEKRFTCEQALQHPWI 261
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
68-324 6.38e-66

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called Doublecortin-like and CAM kinase-like); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL (or DCAMKL) proteins belong to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL proteins contain a C-terminal kinase domain with similarity to CAMKs. They are involved in the regulation of cAMP signaling. Vertebrates contain three DCKL proteins (DCKL1-3); DCKL1 and 2 also contain a serine, threonine, and proline rich domain (SP), while DCKL3 contains only a single DCX domain instead of tandem domains. The DCKL 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: 270997  Cd Length: 258  Bit Score: 213.73  E-value: 6.38e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209  68 QVLGLGINGKVLQIFNKRTQEKFALKMLqDCPKAR-------REVELHWRASQcPHIVRIVDVYEnlyaGRKCLLIVMEC 140
Cdd:cd14095   6 RVIGDGNFAVVKECRDKATDKEYALKII-DKAKCKgkehmieNEVAILRRVKH-PNIVQLIEEYD----TDTELYLVMEL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209 141 LDGGELFSRIQDRGDqaFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAI-LKLTDFGFAKETTshNS 219
Cdd:cd14095  80 VKGGDLFDAITSSTK--FTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHEDGSKsLKLADFGLATEVK--EP 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32481209 220 LTTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLaiSPGMKTRIRMGQYEFPNPEWSEVSEEVK 299
Cdd:cd14095 156 LFTVCGTPTYVAPEILAETGYGLKVDIWAAGVITYILLCGF