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Conserved domains on  [gi|17864380|ref|NP_524769|]
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MAP kinase activated protein-kinase-2, isoform B [Drosophila melanogaster]

Protein Classification

STKc_MAPKAPK domain-containing protein (domain architecture ID 10197449)

STKc_MAPKAPK domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
18-280 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: 568.84  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380  18 DYVTSNTVLGYGINGKVVQCTHRRTQQNYALKVLLDSERARREVDLHWRVSGCRYIVNIIDVYENTFKDRKCLLVVMECM 97
Cdd:cd14089   1 DYTISKQVLGLGINGKVLECFHKKTGEKFALKVLRDNPKARREVELHWRASGCPHIVRIIDVYENTYQGRKCLLVVMECM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380  98 EGGELFQRIQDKADGAFTEREAAQIMHEICAAVDYLHSRDIAHRDLKPENLLYTTTQPNATLKLTDFGFAKETFTSYTLQ 177
Cdd:cd14089  81 EGGELFSRIQERADSAFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGPNAILKLTDFGFAKETTTKKSLQ 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380 178 TPCYTPYYVAPEVLGPEKYDKSCDIWSLGVVMYIIMCGFPPFYSNHGLAISPGMKNRIRTGQYDFPDPEWTNVSQAAKDL 257
Cdd:cd14089 161 TPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAISPGMKKRIRNGQYEFPNPEWSNVSEEAKDL 240
                       250       260
                ....*....|....*....|...
gi 17864380 258 IKGMLNVDPSKRLRIQDVISNKW 280
Cdd:cd14089 241 IRGLLKTDPSERLTIEEVMNHPW 263
 
Name Accession Description Interval E-value
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
18-280 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: 568.84  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380  18 DYVTSNTVLGYGINGKVVQCTHRRTQQNYALKVLLDSERARREVDLHWRVSGCRYIVNIIDVYENTFKDRKCLLVVMECM 97
Cdd:cd14089   1 DYTISKQVLGLGINGKVLECFHKKTGEKFALKVLRDNPKARREVELHWRASGCPHIVRIIDVYENTYQGRKCLLVVMECM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380  98 EGGELFQRIQDKADGAFTEREAAQIMHEICAAVDYLHSRDIAHRDLKPENLLYTTTQPNATLKLTDFGFAKETFTSYTLQ 177
Cdd:cd14089  81 EGGELFSRIQERADSAFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGPNAILKLTDFGFAKETTTKKSLQ 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380 178 TPCYTPYYVAPEVLGPEKYDKSCDIWSLGVVMYIIMCGFPPFYSNHGLAISPGMKNRIRTGQYDFPDPEWTNVSQAAKDL 257
Cdd:cd14089 161 TPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAISPGMKKRIRNGQYEFPNPEWSNVSEEAKDL 240
                       250       260
                ....*....|....*....|...
gi 17864380 258 IKGMLNVDPSKRLRIQDVISNKW 280
Cdd:cd14089 241 IRGLLKTDPSERLTIEEVMNHPW 263
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
25-281 2.87e-93

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


Pssm-ID: 214567  Cd Length: 254  Bit Score: 282.50  E-value: 2.87e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380     25 VLGYGINGKVVQCTHRRTQQNYALKVL------LDSERARREVDLHWRVsGCRYIVNIIDVYEntfkDRKCLLVVMECME 98
Cdd:smart00220   6 KLGEGSFGKVYLARDKKTGKLVAIKVIkkkkikKDRERILREIKILKKL-KHPNIVRLYDVFE----DEDKLYLVMEYCE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380     99 GGELFQRIQDKadGAFTEREAAQIMHEICAAVDYLHSRDIAHRDLKPENLLYTTtqpNATLKLTDFGFAKETFTSYTLQT 178
Cdd:smart00220  81 GGDLFDLLKKR--GRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDE---DGHVKLADFGLARQLDPGEKLTT 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380    179 PCYTPYYVAPEVLGPEKYDKSCDIWSLGVVMYIIMCGFPPFYSNHGLAIspgMKNRIRTGQYDFPDPEWtNVSQAAKDLI 258
Cdd:smart00220 156 FVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLE---LFKKIGKPKPPFPPPEW-DISPEAKDLI 231
                          250       260
                   ....*....|....*....|...
gi 17864380    259 KGMLNVDPSKRLRIQDVISNKWI 281
Cdd:smart00220 232 RKLLVKDPEKRLTAEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
25-281 5.95e-85

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 261.38  E-value: 5.95e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380    25 VLGYGINGKVVQCTHRRTQQNYALKVL-------LDSERARREVDLHwRVSGCRYIVNIIDVYENtfKDRkcLLVVMECM 97
Cdd:pfam00069   6 KLGSGSFGTVYKAKHRDTGKIVAIKKIkkekikkKKDKNILREIKIL-KKLNHPNIVRLYDAFED--KDN--LYLVLEYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380    98 EGGELFQRIQDKadGAFTEREAAQIMHEICAAVDYLHSRDIAHRDLKPENLLYTttqPNATLKLTDFGFAKETFTSYTLQ 177
Cdd:pfam00069  81 EGGSLFDLLSEK--GAFSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENILID---EDGNLKITDFGLARQLNSGSSLT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380   178 TPCYTPYYVAPEVLGPEKYDKSCDIWSLGVVMYIIMCGFPPFYSNHGLAISPGMKNRirtgqyDFPDPEWTNVSQAAKDL 257
Cdd:pfam00069 156 SFVGTPWYMAPEVLRGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYEKIIDQ------DFDSPRPSSISEEAKDL 229
                         250       260
                  ....*....|....*....|....
gi 17864380   258 IKGMLNVDPSKRLRIQDVISNKWI 281
Cdd:pfam00069 230 LKKLLKKDPSKRLTATEALQHPWF 253
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
25-337 4.39e-48

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 169.54  E-value: 4.39e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380  25 VLGYGINGKVVQCTHRRTqqnYALKVLLDS--------ERARREVDLHWRVSGCRYIVNIIDVyentFKDRKCLLVVMEC 96
Cdd:COG0515   7 KLGEGSFGEVYLARDRKL---VALKVLAKKleskskevERFLREIQILASLNHPPNIVKLYDF----FQDEGSLYLVMEY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380  97 MEGGELFQRI-QDKADGAFTEREAAQIMHEICAAVDYLHSRDIAHRDLKPENLLYttTQPNATLKLTDFGFAKE------ 169
Cdd:COG0515  80 VDGGSLEDLLkKIGRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILL--DRDGRVVKLIDFGLAKLlpdpgs 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380 170 -TFTSYTLQTPCYTPYYVAPEVLG---PEKYDKSCDIWSLGVVMYIIMCGFPPFYSNHGLAISPGMKNRIRTGQYDFPDP 245
Cdd:COG0515 158 tSSIPALPSTSVGTPGYMAPEVLLglsLAYASSSSDIWSLGITLYELLTGLPPFEGEKNSSATSQTLKIILELPTPSLAS 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380 246 EWT-----NVSQAAKDLIKGMLNVDPSKRLRIQDVISNKWIAQYNAVPQTPLCtGRMLKEAEETWPEVQEEMTRSLATMR 320
Cdd:COG0515 238 PLSpsnpeLISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKESDLSD-LLKPDDSAPLRLSLPPSLEALISSLN 316
                       330
                ....*....|....*..
gi 17864380 321 VDYDQMQIKALDKSNNP 337
Cdd:COG0515 317 SLAISGSDLKLDDSNFS 333
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
26-285 6.42e-44

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289  Cd Length: 329  Bit Score: 156.52  E-value: 6.42e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380   26 LGYGINGKVVQCTHRRTQQNYALKVLLDSERAR-REVDLHWRVSGC------RYIVNIIdvyeNTFKDRKCLLVVMECME 98
Cdd:PTZ00263  26 LGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKmKQVQHVAQEKSIlmelshPFIVNMM----CSFQDENRVYFLLEFVV 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380   99 GGELFQRIQdKAdGAFTEREAAQIMHEICAAVDYLHSRDIAHRDLKPENLLYTTtqpNATLKLTDFGFAKE-TFTSYTLq 177
Cdd:PTZ00263 102 GGELFTHLR-KA-GRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDN---KGHVKVTDFGFAKKvPDRTFTL- 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380  178 tpCYTPYYVAPEVLGPEKYDKSCDIWSLGVVMYIIMCGFPPFYSNHGLAISpgmkNRIRTGQYDFpdPEWtnVSQAAKDL 257
Cdd:PTZ00263 176 --CGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIY----EKILAGRLKF--PNW--FDGRARDL 245
                        250       260       270
                 ....*....|....*....|....*....|...
gi 17864380  258 IKGMLNVDPSKRL-----RIQDVISNKWIAQYN 285
Cdd:PTZ00263 246 VKGLLQTDHTKRLgtlkgGVADVKNHPYFHGAN 278
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
42-208 7.70e-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: 7.70e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380     42 TQQNYALKVLLD--SERARREVDLHWRVSGCR-----YIVNIIDVYEnTFKDRkcLLVVMECMEGGELFQRIQdkADGAF 114
Cdd:TIGR03903    2 TGHEVAIKLLRTdaPEEEHQRARFRRETALCArlyhpNIVALLDSGE-APPGL--LFAVFEYVPGRTLREVLA--ADGAL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380    115 TEREAAQIMHEICAAVDYLHSRDIAHRDLKPENLLYTTT--QPNAtlKLTDFG-------FAKETFTSYTLQTPCY-TPY 184
Cdd:TIGR03903   77 PAGETGRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTgvRPHA--KVLDFGigtllpgVRDADVATLTRTTEVLgTPT 154
                          170       180
                   ....*....|....*....|....
gi 17864380    185 YVAPEVLGPEKYDKSCDIWSLGVV 208
Cdd:TIGR03903  155 YCAPEQLRGEPVTPNSDLYAWGLI 178
 
Name Accession Description Interval E-value
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
18-280 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: 568.84  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380  18 DYVTSNTVLGYGINGKVVQCTHRRTQQNYALKVLLDSERARREVDLHWRVSGCRYIVNIIDVYENTFKDRKCLLVVMECM 97
Cdd:cd14089   1 DYTISKQVLGLGINGKVLECFHKKTGEKFALKVLRDNPKARREVELHWRASGCPHIVRIIDVYENTYQGRKCLLVVMECM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380  98 EGGELFQRIQDKADGAFTEREAAQIMHEICAAVDYLHSRDIAHRDLKPENLLYTTTQPNATLKLTDFGFAKETFTSYTLQ 177
Cdd:cd14089  81 EGGELFSRIQERADSAFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGPNAILKLTDFGFAKETTTKKSLQ 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380 178 TPCYTPYYVAPEVLGPEKYDKSCDIWSLGVVMYIIMCGFPPFYSNHGLAISPGMKNRIRTGQYDFPDPEWTNVSQAAKDL 257
Cdd:cd14089 161 TPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAISPGMKKRIRNGQYEFPNPEWSNVSEEAKDL 240
                       250       260
                ....*....|....*....|...
gi 17864380 258 IKGMLNVDPSKRLRIQDVISNKW 280
Cdd:cd14089 241 IRGLLKTDPSERLTIEEVMNHPW 263
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
17-319 1.01e-161

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: 459.11  E-value: 1.01e-161
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380  17 DDYVTSNTVLGYGINGKVVQCTHRRTQQNYALKVLLDSERARREVDLHWRVSGCRYIVNIIDVYENTFKDRKCLLVVMEC 96
Cdd:cd14170   1 DDYKVTSQVLGLGINGKVLQIFNKRTQEKFALKMLQDCPKARREVELHWRASQCPHIVRIVDVYENLYAGRKCLLIVMEC 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380  97 MEGGELFQRIQDKADGAFTEREAAQIMHEICAAVDYLHSRDIAHRDLKPENLLYTTTQPNATLKLTDFGFAKETFTSYTL 176
Cdd:cd14170  81 LDGGELFSRIQDRGDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAILKLTDFGFAKETTSHNSL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380 177 QTPCYTPYYVAPEVLGPEKYDKSCDIWSLGVVMYIIMCGFPPFYSNHGLAISPGMKNRIRTGQYDFPDPEWTNVSQAAKD 256
Cdd:cd14170 161 TTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAISPGMKTRIRMGQYEFPNPEWSEVSEEVKM 240
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17864380 257 LIKGMLNVDPSKRLRIQDVISNKWIAQYNAVPQTPLCTGRMLKEAEETWPEVQEEMTRSLATM 319
Cdd:cd14170 241 LIRNLLKTEPTQRMTITEFMNHPWIMQSTKVPQTPLHTSRVLKEDKERWEDVKEEMTSALATM 303
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
15-281 1.73e-152

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: 434.42  E-value: 1.73e-152
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380  15 LTDDYVTSNTVLGYGINGKVVQCTHRRTQQNYALKVLLDSERARREVDLHWRVSGCRYIVNIIDVYENTFKDRKCLLVVM 94
Cdd:cd14172   1 VTDDYKLSKQVLGLGVNGKVLECFHRRTGQKCALKLLYDSPKARREVEHHWRASGGPHIVHILDVYENMHHGKRCLLIIM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380  95 ECMEGGELFQRIQDKADGAFTEREAAQIMHEICAAVDYLHSRDIAHRDLKPENLLYTTTQPNATLKLTDFGFAKETFTSY 174
Cdd:cd14172  81 ECMEGGELFSRIQERGDQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTSKEKDAVLKLTDFGFAKETTVQN 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380 175 TLQTPCYTPYYVAPEVLGPEKYDKSCDIWSLGVVMYIIMCGFPPFYSNHGLAISPGMKNRIRTGQYDFPDPEWTNVSQAA 254
Cdd:cd14172 161 ALQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFYSNTGQAISPGMKRRIRMGQYGFPNPEWAEVSEEA 240
                       250       260
                ....*....|....*....|....*..
gi 17864380 255 KDLIKGMLNVDPSKRLRIQDVISNKWI 281
Cdd:cd14172 241 KQLIRHLLKTDPTERMTITQFMNHPWI 267
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
18-280 2.90e-115

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: 339.07  E-value: 2.90e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380  18 DYVTSNtVLGYGINGKVVQCTHRRTQQNYALKVL-------LDSERARREVDLHWRVSgCRYIVNIIDVYEntfkDRKCL 90
Cdd:cd05117   1 KYELGK-VLGRGSFGVVRLAVHKKTGEEYAVKIIdkkklksEDEEMLRREIEILKRLD-HPNIVKLYEVFE----DDKNL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380  91 LVVMECMEGGELFQRIQDKadGAFTEREAAQIMHEICAAVDYLHSRDIAHRDLKPENLLYTTTQPNATLKLTDFGFAKET 170
Cdd:cd05117  75 YLVMELCTGGELFDRIVKK--GSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPDSPIKIIDFGLAKIF 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380 171 FTSYTLQTPCYTPYYVAPEVLGPEKYDKSCDIWSLGVVMYIIMCGFPPFYSNHglaiSPGMKNRIRTGQYDFPDPEWTNV 250
Cdd:cd05117 153 EEGEKLKTVCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGET----EQELFEKILKGKYSFDSPEWKNV 228
                       250       260       270
                ....*....|....*....|....*....|
gi 17864380 251 SQAAKDLIKGMLNVDPSKRLRIQDVISNKW 280
Cdd:cd05117 229 SEEAKDLIKRLLVVDPKKRLTAAEALNHPW 258
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
15-281 3.94e-106

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: 317.10  E-value: 3.94e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380  15 LTDDY-VTSNTVLGYGINGKVVQCTHRRTQQNYALKVLLDSERARREVDLHWRVSGCRYIVNIIDVYENTFK------DR 87
Cdd:cd14171   2 ILEEYeVNWTQKLGTGISGPVRVCVKKSTGERFALKILLDRPKARTEVRLHMMCSGHPNIVQIYDVYANSVQfpgessPR 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380  88 KCLLVVMECMEGGELFQRIQDKAdgAFTEREAAQIMHEICAAVDYLHSRDIAHRDLKPENLLYTTTQPNATLKLTDFGFA 167
Cdd:cd14171  82 ARLLIVMELMEGGELFDRISQHR--HFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDNSEDAPIKLCDFGFA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380 168 KEtfTSYTLQTPCYTPYYVAPEVLGPEK-----------------YDKSCDIWSLGVVMYIIMCGFPPFYSNH-GLAISP 229
Cdd:cd14171 160 KV--DQGDLMTPQFTPYYVAPQVLEAQRrhrkersgiptsptpytYDKSCDMWSLGVIIYIMLCGYPPFYSEHpSRTITK 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 17864380 230 GMKNRIRTGQYDFPDPEWTNVSQAAKDLIKGMLNVDPSKRLRIQDVISNKWI 281
Cdd:cd14171 238 DMKRKIMTGSYEFPEEEWSQISEMAKDIVRKLLCVDPEERMTIEEVLHHPWL 289
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
25-281 2.87e-93

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


Pssm-ID: 214567  Cd Length: 254  Bit Score: 282.50  E-value: 2.87e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380     25 VLGYGINGKVVQCTHRRTQQNYALKVL------LDSERARREVDLHWRVsGCRYIVNIIDVYEntfkDRKCLLVVMECME 98
Cdd:smart00220   6 KLGEGSFGKVYLARDKKTGKLVAIKVIkkkkikKDRERILREIKILKKL-KHPNIVRLYDVFE----DEDKLYLVMEYCE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380     99 GGELFQRIQDKadGAFTEREAAQIMHEICAAVDYLHSRDIAHRDLKPENLLYTTtqpNATLKLTDFGFAKETFTSYTLQT 178
Cdd:smart00220  81 GGDLFDLLKKR--GRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDE---DGHVKLADFGLARQLDPGEKLTT 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380    179 PCYTPYYVAPEVLGPEKYDKSCDIWSLGVVMYIIMCGFPPFYSNHGLAIspgMKNRIRTGQYDFPDPEWtNVSQAAKDLI 258
Cdd:smart00220 156 FVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLE---LFKKIGKPKPPFPPPEW-DISPEAKDLI 231
                          250       260
                   ....*....|....*....|...
gi 17864380    259 KGMLNVDPSKRLRIQDVISNKWI 281
Cdd:smart00220 232 RKLLVKDPEKRLTAEEALQHPFF 254
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
37-294 1.45e-91

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: 280.34  E-value: 1.45e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380  37 CTHRRTQQNYALKVLldSER--ARREVDLHWRVSGCRYIVNIIDVYEntfkDRKCLLVVMECMEGGELFQRIQDKAdgAF 114
Cdd:cd14092  25 CVHKKTGQEFAVKIV--SRRldTSREVQLLRLCQGHPNIVKLHEVFQ----DELHTYLVMELLRGGELLERIRKKK--RF 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380 115 TEREAAQIMHEICAAVDYLHSRDIAHRDLKPENLLYTTTQPNATLKLTDFGFAKETFTSYTLQTPCYTPYYVAPEVL--- 191
Cdd:cd14092  97 TESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTDEDDDAEIKIVDFGFARLKPENQPLKTPCFTLPYAAPEVLkqa 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380 192 -GPEKYDKSCDIWSLGVVMYIIMCGFPPFYSNHGLAISPGMKNRIRTGQYDFPDPEWTNVSQAAKDLIKGMLNVDPSKRL 270
Cdd:cd14092 177 lSTQGYDESCDLWSLGVILYTMLSGQVPFQSPSRNESAAEIMKRIKSGDFSFDGEEWKNVSSEAKSLIQGLLTVDPSKRL 256
                       250       260
                ....*....|....*....|....
gi 17864380 271 RIQDVISNKWIAQYNAVPQTPLCT 294
Cdd:cd14092 257 TMSELRNHPWLQGSSSPSSTPLMT 280
Pkinase pfam00069
Protein kinase domain;
25-281 5.95e-85

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 261.38  E-value: 5.95e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380    25 VLGYGINGKVVQCTHRRTQQNYALKVL-------LDSERARREVDLHwRVSGCRYIVNIIDVYENtfKDRkcLLVVMECM 97
Cdd:pfam00069   6 KLGSGSFGTVYKAKHRDTGKIVAIKKIkkekikkKKDKNILREIKIL-KKLNHPNIVRLYDAFED--KDN--LYLVLEYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380    98 EGGELFQRIQDKadGAFTEREAAQIMHEICAAVDYLHSRDIAHRDLKPENLLYTttqPNATLKLTDFGFAKETFTSYTLQ 177
Cdd:pfam00069  81 EGGSLFDLLSEK--GAFSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENILID---EDGNLKITDFGLARQLNSGSSLT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380   178 TPCYTPYYVAPEVLGPEKYDKSCDIWSLGVVMYIIMCGFPPFYSNHGLAISPGMKNRirtgqyDFPDPEWTNVSQAAKDL 257
Cdd:pfam00069 156 SFVGTPWYMAPEVLRGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYEKIIDQ------DFDSPRPSSISEEAKDL 229
                         250       260
                  ....*....|....*....|....
gi 17864380   258 IKGMLNVDPSKRLRIQDVISNKWI 281
Cdd:pfam00069 230 LKKLLKKDPSKRLTATEALQHPWF 253
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
18-292 1.74e-81

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: 253.71  E-value: 1.74e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380  18 DYVTSNTvLGYGINGKVVQCTHRRTQQNYALKVLLDSER-ARREVDLHWRVSGCRYIVNIIDVYENtfkDRKCLLVvMEC 96
Cdd:cd14091   1 EYEIKEE-IGKGSYSVCKRCIHKATGKEYAVKIIDKSKRdPSEEIEILLRYGQHPNIITLRDVYDD---GNSVYLV-TEL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380  97 MEGGELFQRIQDKadGAFTEREAAQIMHEICAAVDYLHSRDIAHRDLKPENLLYTTTQPNA-TLKLTDFGFAKE-TFTSY 174
Cdd:cd14091  76 LRGGELLDRILRQ--KFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESGDPeSLRICDFGFAKQlRAENG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380 175 TLQTPCYTPYYVAPEVLGPEKYDKSCDIWSLGVVMYIIMCGFPPFysnhglAISPG-----MKNRIRTGQYDFPDPEWTN 249
Cdd:cd14091 154 LLMTPCYTANFVAPEVLKKQGYDAACDIWSLGVLLYTMLAGYTPF------ASGPNdtpevILARIGSGKIDLSGGNWDH 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 17864380 250 VSQAAKDLIKGMLNVDPSKRLRIQDVISNKWIAQYNAVPQTPL 292
Cdd:cd14091 228 VSDSAKDLVRKMLHVDPSQRPTAAQVLQHPWIRNRDSLPQRQL 270
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
25-280 3.47e-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: 228.17  E-value: 3.47e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380  25 VLGYGINGKVVQCTHRRTQQNYALKVL-------LDSERARREVDLHWRVSGCrYIVNIIDVYENTFKdrkcLLVVMECM 97
Cdd:cd14003   7 TLGEGSFGKVKLARHKLTGEKVAIKIIdksklkeEIEEKIKREIEIMKLLNHP-NIIKLYEVIETENK----IYLVMEYA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380  98 EGGELFQRIqdKADGAFTEREAAQIMHEICAAVDYLHSRDIAHRDLKPENLLYtTTQPNatLKLTDFGFAKETFTSYTLQ 177
Cdd:cd14003  82 SGGELFDYI--VNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILL-DKNGN--LKIIDFGLSNEFRGGSLLK 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380 178 TPCYTPYYVAPEVLGPEKYD-KSCDIWSLGVVMYIIMCGFPPFY-SNHglaisPGMKNRIRTGQYDFPdpewTNVSQAAK 255
Cdd:cd14003 157 TFCGTPAYAAPEVLLGRKYDgPKADVWSLGVILYAMLTGYLPFDdDND-----SKLFRKILKGKYPIP----SHLSPDAR 227
                       250       260
                ....*....|....*....|....*
gi 17864380 256 DLIKGMLNVDPSKRLRIQDVISNKW 280
Cdd:cd14003 228 DLIRRMLVVDPSKRITIEEILNHPW 252
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
17-292 4.05e-69

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called Ribosomal protein S6 kinase alpha-1 or 90kDa ribosomal protein S6 kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK1 is also called S6K-alpha-1, RPS6KA1, p90RSK1 or MAPK-activated protein kinase 1a (MAPKAPK-1a). It is a component of the insulin transduction pathway, regulating the function of IRS1. It also interacts with PKA and promotes its inactivation. RSK1 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. 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. The RSK1 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: 271077  Cd Length: 291  Bit Score: 221.82  E-value: 4.05e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380  17 DDYVTSNTVlGYGINGKVVQCTHRRTQQNYALKVLLDSER-ARREVDLHWRVSGCRYIVNIIDVYentfKDRKCLLVVME 95
Cdd:cd14175   1 DGYVVKETI-GVGSYSVCKRCVHKATNMEYAVKVIDKSKRdPSEEIEILLRYGQHPNIITLKDVY----DDGKHVYLVTE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380  96 CMEGGELFQRIQDKAdgAFTEREAAQIMHEICAAVDYLHSRDIAHRDLKPENLLYTTTQPNA-TLKLTDFGFAKETFTSY 174
Cdd:cd14175  76 LMRGGELLDKILRQK--FFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILYVDESGNPeSLRICDFGFAKQLRAEN 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380 175 -TLQTPCYTPYYVAPEVLGPEKYDKSCDIWSLGVVMYIIMCGFPPFysNHGLAISP-GMKNRIRTGQYDFPDPEWTNVSQ 252
Cdd:cd14175 154 gLLMTPCYTANFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPF--ANGPSDTPeEILTRIGSGKFTLSGGNWNTVSD 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 17864380 253 AAKDLIKGMLNVDPSKRLRIQDVISNKWIAQYNAVPQTPL 292
Cdd:cd14175 232 AAKDLVSKMLHVDPHQRLTAKQVLQHPWITQKDKLPQSQL 271
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
25-280 8.57e-69

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: 219.89  E-value: 8.57e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380  25 VLGYGiNGKVV-QCTHRRTQQNYALKVLlDSERAR-------REVDLHWRVSGcryiVNIIDVYENTFKDRKcLLVVMEC 96
Cdd:cd14095   7 VIGDG-NFAVVkECRDKATDKEYALKII-DKAKCKgkehmieNEVAILRRVKH----PNIVQLIEEYDTDTE-LYLVMEL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380  97 MEGGELFQRIQDKadGAFTEREAAQIMHEICAAVDYLHSRDIAHRDLKPENLLYTTTQPNA-TLKLTDFGFAKETftSYT 175
Cdd:cd14095  80 VKGGDLFDAITSS--TKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHEDGSkSLKLADFGLATEV--KEP 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380 176 LQTPCYTPYYVAPEVLGPEKYDKSCDIWSLGVVMYIIMCGFPPFYSNHGLaiSPGMKNRIRTGQYDFPDPEWTNVSQAAK 255
Cdd:cd14095 156 LFTVCGTPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFRSPDRD--QEELFDLILAGEFEFLSPYWDNISDSAK 233
                       250       260
                ....*....|....*....|....*
gi 17864380 256 DLIKGMLNVDPSKRLRIQDVISNKW 280
Cdd:cd14095 234 DLISRMLVVDPEKRYSAGQVLDHPW 258
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
25-280 1.44e-67

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: 216.85  E-value: 1.44e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380  25 VLGYGINGKVVQCTHRRTQQNYALKVLLDSERARREVDLHWRVSGCRY-----IVNIIDVYEntfkDRKCLLVVMECMEG 99
Cdd:cd14083  10 VLGTGAFSEVVLAEDKATGKLVAIKCIDKKALKGKEDSLENEIAVLRKikhpnIVQLLDIYE----SKSHLYLVMELVTG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380 100 GELFQRIQDKadGAFTEREAAQIMHEICAAVDYLHSRDIAHRDLKPENLLYTTTQPNATLKLTDFGFAKeTFTSYTLQTP 179
Cdd:cd14083  86 GELFDRIVEK--GSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYYSPDEDSKIMISDFGLSK-MEDSGVMSTA 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380 180 CYTPYYVAPEVLGPEKYDKSCDIWSLGVVMYIIMCGFPPFYSNHglaiSPGMKNRIRTGQYDFPDPEWTNVSQAAKDLIK 259
Cdd:cd14083 163 CGTPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPFYDEN----DSKLFAQILKAEYEFDSPYWDDISDSAKDFIR 238
                       250       260
                ....*....|....*....|.
gi 17864380 260 GMLNVDPSKRLRIQDVISNKW 280
Cdd:cd14083 239 HLMEKDPNKRYTCEQALEHPW 259
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
17-281 3.28e-67

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: 216.90  E-value: 3.28e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380  17 DDYVTSNTVLGYGINGKVVQCTHRRTQQNYALKVLLDS---ERAR--REVDLHWRVSGCRYIVNIIDVYEntfkDRKCLL 91
Cdd:cd14090   1 DLYKLTGELLGEGAYASVQTCINLYTGKEYAVKIIEKHpghSRSRvfREVETLHQCQGHPNILQLIEYFE----DDERFY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380  92 VVMECMEGGELFQRIQDKadGAFTEREAAQIMHEICAAVDYLHSRDIAHRDLKPENLLYTTTQPNATLKLTDFGFAKETF 171
Cdd:cd14090  77 LVFEKMRGGPLLSHIEKR--VHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKVSPVKICDFDLGSGIK 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864380 172 TSYT---------LQTPCYTPYYVAPEVLG-----PEKYDKSCDIWSLGVVMYIIMCGFPPFYS--------NHGLAISP 229
Cdd:cd14090 155 LSSTsmtpvttpeLLTPVGSAEYMAPEVVDafvgeALSYDKRCDLWSLGVILYIMLCGYPPFYGrcgedcgwDRGEACQD 234
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17864380 230 GMKN---RIRTGQYDFPDPEWTNVSQAAKDLIKGMLNVDPSKRLRIQDVISNKWI 281
Cdd:cd14090 235 CQELlfhSIQEGEYEFPEKEWSHISAEAKDLISHLLVRDASQRYTAEQVLQHPWV 289
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
23-301 5.40e-67

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. 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, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which i