NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|4336426|gb|AAD17800|]
View 

Ca2+-dependent protein kinase [Mesembryanthemum crystallinum]

Protein Classification

calcium-dependent protein kinase (domain architecture ID 11563077)

calcium-dependent protein kinase plays an essential role in plant defense response, may be involved in signal transduction pathways that utilize calcium as a second messenger

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
86-343 1.04e-139

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 [Multi-domain]  Cd Length: 258  Bit Score: 403.40  E-value: 1.04e-139
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426   86 YTLGRELGRGQFGVTYLCTDKKTGQQYACKSISKKKLVTKaDKDDMRREIQIMQHMSgQPNIVEFKGAYEDKTSVNLVME 165
Cdd:cd05117   2 YELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSE-DEEMLRREIEILKRLD-HPNIVKLYEVFEDDKNLYLVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426  166 LCAGGELFDRIIAKGHYSEKAAATMLRQIVNVVHVCHFMGVMHRDLKPENFLLSSKDENSLLKATDFGLSVFIEEGKVYR 245
Cdd:cd05117  80 LCTGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPDSPIKIIDFGLAKIFEEGEKLK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426  246 DIVGSAYYVAPEVLRRR-YGKEIDVWSAGVMLYILLSGVPPFWAETEKGIFDAILQGHIDFESKPWPSISNGAKDLVRKM 324
Cdd:cd05117 160 TVCGTPYYVAPEVLKGKgYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYSFDSPEWKNVSEEAKDLIKRL 239
                       250
                ....*....|....*....
gi 4336426  325 LTQDPKKRITAAQVLEHPW 343
Cdd:cd05117 240 LVVDPKKRLTAAEALNHPW 258
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
382-522 1.52e-28

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


:

Pssm-ID: 227455 [Multi-domain]  Cd Length: 160  Bit Score: 110.86  E-value: 1.52e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426  382 NLPDEEIQGLKQMFANMDTDGSGSITYEELREGLARLGSKLTETEVKALMEAADqDGSGSIDYYEFITAtMHRY--RLER 459
Cdd:COG5126  13 QLTEEQIQELKEAFQLFDRDSDGLIDRNELGKILRSLGFNPSEAEINKLFEEID-AGNETVDFPEFLTV-MSVKlkRGDK 90
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4336426  460 DEHLYKAFQYFDKDNSGFITTDELETAMKEYGIA-DENCIAEILLEVDTDNDGRINYDEFSAMM 522
Cdd:COG5126  91 EEELREAFKLFDKDHDGYISIGELRRVLKSLGERlSDEEVEKLLKEYDEDGDGEIDYEEFKKLI 154
 
Name Accession Description Interval E-value
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
86-343 1.04e-139

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 [Multi-domain]  Cd Length: 258  Bit Score: 403.40  E-value: 1.04e-139
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426   86 YTLGRELGRGQFGVTYLCTDKKTGQQYACKSISKKKLVTKaDKDDMRREIQIMQHMSgQPNIVEFKGAYEDKTSVNLVME 165
Cdd:cd05117   2 YELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSE-DEEMLRREIEILKRLD-HPNIVKLYEVFEDDKNLYLVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426  166 LCAGGELFDRIIAKGHYSEKAAATMLRQIVNVVHVCHFMGVMHRDLKPENFLLSSKDENSLLKATDFGLSVFIEEGKVYR 245
Cdd:cd05117  80 LCTGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPDSPIKIIDFGLAKIFEEGEKLK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426  246 DIVGSAYYVAPEVLRRR-YGKEIDVWSAGVMLYILLSGVPPFWAETEKGIFDAILQGHIDFESKPWPSISNGAKDLVRKM 324
Cdd:cd05117 160 TVCGTPYYVAPEVLKGKgYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYSFDSPEWKNVSEEAKDLIKRL 239
                       250
                ....*....|....*....
gi 4336426  325 LTQDPKKRITAAQVLEHPW 343
Cdd:cd05117 240 LVVDPKKRLTAAEALNHPW 258
Pkinase pfam00069
Protein kinase domain;
86-344 8.56e-106

Protein kinase domain;


Pssm-ID: 333812 [Multi-domain]  Cd Length: 259  Bit Score: 316.87  E-value: 8.56e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426     86 YTLGRELGRGQFGVTYLCTDKKTGQQYACKSISKKKlVTKADKDDMRREIQIMQHMSGqPNIVEFKGAYEDKTSVNLVME 165
Cdd:pfam00069   1 YEVLEKLGEGSFGTVYKAKHKDTGKIVAIKKIKKEK-IKKKKEKNVLREIKILKKLSH-PNIVRLYDVFEDKDHLYLVLE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426    166 LCAGGELFDRIIAKGHYSEKAAATMLRQIVNVVHVCHFMGVMHRDLKPENFLLsskDENSLLKATDFGLSVFIEEGKVYR 245
Cdd:pfam00069  79 YVEGGSLFDLLSEKGVFSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENILI---DEDGNLKITDFGLAKQLSSGSKLT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426    246 DIVGSAYYVAPEVLRRR-YGKEIDVWSAGVMLYILLSGVPPFWAETEKGIF----DAILQGHIDFESKPWPSISNGAKDL 320
Cdd:pfam00069 156 TFVGTPWYMAPEVLGGNpYGPKVDVWSLGCILYELLTGKPPFPGINGDDIYelilDQLERIPEDFSSPFPSSLSEEAKDL 235
                         250       260
                  ....*....|....*....|....
gi 4336426    321 VRKMLTQDPKKRITAAQVLEHPWL 344
Cdd:pfam00069 236 LKKLLKKDPSKRLTATQALQHPWF 259
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
86-344 1.33e-105

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 316.39  E-value: 1.33e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426      86 YTLGRELGRGQFGVTYLCTDKKTGQQYACKSISKKKLvtKADKDDMRREIQIMQHMsGQPNIVEFKGAYEDKTSVNLVME 165
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKI--KKDRERILREIKILKKL-KHPNIVRLYDVFEDEDKLYLVME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426     166 LCAGGELFDRIIAKGHYSEKAAATMLRQIVNVVHVCHFMGVMHRDLKPENFLLsskDENSLLKATDFGLSVFIEEGKVYR 245
Cdd:smart00220  78 YCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILL---DEDGHVKLADFGLARQLDPGEKLT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426     246 DIVGSAYYVAPEVLRRR-YGKEIDVWSAGVMLYILLSGVPPFWA-ETEKGIFDAILQGHIDFESKPWPsISNGAKDLVRK 323
Cdd:smart00220 155 TFVGTPEYMAPEVLLGKgYGKAVDIWSLGVILYELLTGKPPFPGdDQLLELFKKIGKPKPPFPPPEWD-ISPEAKDLIRK 233
                          250       260
                   ....*....|....*....|.
gi 4336426     324 MLTQDPKKRITAAQVLEHPWL 344
Cdd:smart00220 234 LLVKDPEKRLTAEEALQHPFF 254
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
86-353 4.49e-56

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 192.65  E-value: 4.49e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426   86 YTLGRELGRGQFGVTYLCTDKKTgqqYACKSISKKKLVTKADKDDMRREIQIMQHMSGQPNIVEFKGAYEDKTSVNLVME 165
Cdd:COG0515   2 YRILRKLGEGSFGEVYLARDRKL---VALKVLAKKLESKSKEVERFLREIQILASLNHPPNIVKLYDFFQDEGSLYLVME 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426  166 LCAGGELFDRI---IAKGHYSEKAAATMLRQIVNVVHVCHFMGVMHRDLKPENFLLSSKDenSLLKATDFGLSVFIEEGK 242
Cdd:COG0515  79 YVDGGSLEDLLkkiGRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDG--RVVKLIDFGLAKLLPDPG 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426  243 V-------YRDIVGSAYYVAPEVLR----RRYGKEIDVWSAGVMLYILLSGVPPFWAETEKGIFDAILQgHIDFESKPW- 310
Cdd:COG0515 157 StssipalPSTSVGTPGYMAPEVLLglslAYASSSSDIWSLGITLYELLTGLPPFEGEKNSSATSQTLK-IILELPTPSl 235
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 4336426  311 ---------PSISNGAKDLVRKMLTQDPKKRITAAQVLEHPWLRDGEASDKP 353
Cdd:COG0515 236 asplspsnpELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKESD 287
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
88-345 4.38e-40

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 147.66  E-value: 4.38e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426    88 LGRELGRGQFGVTYLCTDKKTGQQYACKSISKKKLVTKADKDDMRREIQIMQHMSgQPNIVEFKGAYEDKTSVNLVMELC 167
Cdd:PTZ00263  22 MGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSILMELS-HPFIVNMMCSFQDENRVYFLLEFV 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426   168 AGGELFDRIIAKGHYSEKAAATMLRQIVNVVHVCHFMGVMHRDLKPENFLLSSKDEnslLKATDFGLSVFIEEgKVYrDI 247
Cdd:PTZ00263 101 VGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGH---VKVTDFGFAKKVPD-RTF-TL 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426   248 VGSAYYVAPEVLRRR-YGKEIDVWSAGVMLYILLSGVPPFWAETEKGIFDAILQGHIDFESkpWpsISNGAKDLVRKMLT 326
Cdd:PTZ00263 176 CGTPEYLAPEVIQSKgHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPN--W--FDGRARDLVKGLLQ 251
                        250       260
                 ....*....|....*....|....
gi 4336426   327 QDPKKRITA-----AQVLEHPWLR 345
Cdd:PTZ00263 252 TDHTKRLGTlkggvADVKNHPYFH 275
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
382-522 1.52e-28

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 227455 [Multi-domain]  Cd Length: 160  Bit Score: 110.86  E-value: 1.52e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426  382 NLPDEEIQGLKQMFANMDTDGSGSITYEELREGLARLGSKLTETEVKALMEAADqDGSGSIDYYEFITAtMHRY--RLER 459
Cdd:COG5126  13 QLTEEQIQELKEAFQLFDRDSDGLIDRNELGKILRSLGFNPSEAEINKLFEEID-AGNETVDFPEFLTV-MSVKlkRGDK 90
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4336426  460 DEHLYKAFQYFDKDNSGFITTDELETAMKEYGIA-DENCIAEILLEVDTDNDGRINYDEFSAMM 522
Cdd:COG5126  91 EEELREAFKLFDKDHDGYISIGELRRVLKSLGERlSDEEVEKLLKEYDEDGDGEIDYEEFKKLI 154
PTZ00184 PTZ00184
calmodulin; Provisional
379-524 1.67e-28

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 110.24  E-value: 1.67e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426   379 IAENLPDEEIQGLKQMFANMDTDGSGSITYEELREGLARLGSKLTETEVKALMEAADQDGSGSIDYYEFITaTMHRYRLE 458
Cdd:PTZ00184   1 MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLT-LMARKMKD 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426   459 RD--EHLYKAFQYFDKDNSGFITTDELETAMKEYG--IADENcIAEILLEVDTDNDGRINYDEFSAMMRS 524
Cdd:PTZ00184  80 TDseEEIKEAFKVFDRDGNGFISAAELRHVMTNLGekLTDEE-VDEMIREADVDGDGQINYEEFVKMMMS 148
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
391-521 3.20e-19

EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein (ALG-2); The family includes some homologs of mammalian apoptosis-linked gene 2 protein (ALG-2) mainly found in lower eukaryotes, such as a parasitic protist Leishmarua major and a cellular slime mold Dictyostelium discoideum. These homologs contains five EF-hand motifs. Due to the presence of unfavorable residues at the Ca2+-coordinating positions, their non-canonical EF4 and EF5 hands may not bind Ca2+. Two Dictyostelium PEF proteins are the prototypes of this family. They may bind to cytoskeletal proteins and/or signal-transducing proteins localized to detergent-resistant membranes named lipid rafts, and occur as monomers or weak homo- or heterodimers like ALG-2. They can serve as a mediator for Ca2+ signaling-related Dictyostehum programmed cell death (PCD).


Pssm-ID: 320060 [Multi-domain]  Cd Length: 163  Bit Score: 84.57  E-value: 3.20e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426  391 LKQMFANMDTDGSGSITYEELREGLARLGSKLTETEVKALMEAADQDGSGSIDYYEFitATMHRYRLErdehLYKAFQYF 470
Cdd:cd16185   2 LRQWFRAVDRDRSGSIDVNELQKALAGGGLLFSLATAEKLIRMFDRDGNGTIDFEEF--AALHQFLSN----MQNGFEQR 75
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 4336426  471 DKDNSGFITTDELETAMKEYGIA-DENCIAEILLEVDTDNDGRINYDEFSAM 521
Cdd:cd16185  76 DTSRSGRLDANEVHEALAASGFQlDPPAFQALFRKFDPDRGGSLGFDDYIEL 127
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
132-339 2.65e-14

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 [Multi-domain]  Cd Length: 1266  Bit Score: 76.04  E-value: 2.65e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426     132 RREIQIMQHMSgQPNIVEF--KGAYEDKTsVNLVMELCAGGELFDRIIAKGHYSEKAAATMLRQIVNVVHVCHFMGVMHR 209
Cdd:TIGR03903   26 RRETALCARLY-HPNIVALldSGEAPPGL-LFAVFEYVPGRTLREVLAADGALPAGETGRLMLQVLDALACAHNQGIVHR 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426     210 DLKPENFLLSSKDENSLLKATDFGLSVFI---EEGKVYR-----DIVGSAYYVAPEVLRrryGKEI----DVWSAGVMLY 277
Cdd:TIGR03903  104 DLKPQNIMVSQTGVRPHAKVLDFGIGTLLpgvRDADVATltrttEVLGTPTYCAPEQLR---GEPVtpnsDLYAWGLIFL 180
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4336426     278 ILLSGVPPFWAETEKGIFDAILqGHIDFESKPWPSiSNGAKDLVRKMLTQDPKKRITAAQVL 339
Cdd:TIGR03903  181 ECLTGQRVVQGASVAEILYQQL-SPVDVSLPPWIA-GHPLGQVLRKALNKDPRQRAASAPAL 240
EF-hand_7 pfam13499
EF-hand domain pair;
391-452 9.88e-14

EF-hand domain pair;


Pssm-ID: 338778 [Multi-domain]  Cd Length: 68  Bit Score: 65.75  E-value: 9.88e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4336426    391 LKQMFANMDTDGSGSITYEELRE---GLARLGSKLTETEVKALMEAADQDGSGSIDYYEFITATM 452
Cdd:pfam13499   4 LKEAFKLLDKDGDGYLDVEELKKllrKLFEEGEKLSDEEVEELFKEFDLDKDGRISFEEFLELYR 68
 
Name Accession Description Interval E-value
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
86-343 1.04e-139

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 [Multi-domain]  Cd Length: 258  Bit Score: 403.40  E-value: 1.04e-139
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426   86 YTLGRELGRGQFGVTYLCTDKKTGQQYACKSISKKKLVTKaDKDDMRREIQIMQHMSgQPNIVEFKGAYEDKTSVNLVME 165
Cdd:cd05117   2 YELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSE-DEEMLRREIEILKRLD-HPNIVKLYEVFEDDKNLYLVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426  166 LCAGGELFDRIIAKGHYSEKAAATMLRQIVNVVHVCHFMGVMHRDLKPENFLLSSKDENSLLKATDFGLSVFIEEGKVYR 245
Cdd:cd05117  80 LCTGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPDSPIKIIDFGLAKIFEEGEKLK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426  246 DIVGSAYYVAPEVLRRR-YGKEIDVWSAGVMLYILLSGVPPFWAETEKGIFDAILQGHIDFESKPWPSISNGAKDLVRKM 324
Cdd:cd05117 160 TVCGTPYYVAPEVLKGKgYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYSFDSPEWKNVSEEAKDLIKRL 239
                       250
                ....*....|....*....
gi 4336426  325 LTQDPKKRITAAQVLEHPW 343
Cdd:cd05117 240 LVVDPKKRLTAAEALNHPW 258
Pkinase pfam00069
Protein kinase domain;
86-344 8.56e-106

Protein kinase domain;


Pssm-ID: 333812 [Multi-domain]  Cd Length: 259  Bit Score: 316.87  E-value: 8.56e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426     86 YTLGRELGRGQFGVTYLCTDKKTGQQYACKSISKKKlVTKADKDDMRREIQIMQHMSGqPNIVEFKGAYEDKTSVNLVME 165
Cdd:pfam00069   1 YEVLEKLGEGSFGTVYKAKHKDTGKIVAIKKIKKEK-IKKKKEKNVLREIKILKKLSH-PNIVRLYDVFEDKDHLYLVLE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426    166 LCAGGELFDRIIAKGHYSEKAAATMLRQIVNVVHVCHFMGVMHRDLKPENFLLsskDENSLLKATDFGLSVFIEEGKVYR 245
Cdd:pfam00069  79 YVEGGSLFDLLSEKGVFSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENILI---DEDGNLKITDFGLAKQLSSGSKLT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426    246 DIVGSAYYVAPEVLRRR-YGKEIDVWSAGVMLYILLSGVPPFWAETEKGIF----DAILQGHIDFESKPWPSISNGAKDL 320
Cdd:pfam00069 156 TFVGTPWYMAPEVLGGNpYGPKVDVWSLGCILYELLTGKPPFPGINGDDIYelilDQLERIPEDFSSPFPSSLSEEAKDL 235
                         250       260
                  ....*....|....*....|....
gi 4336426    321 VRKMLTQDPKKRITAAQVLEHPWL 344
Cdd:pfam00069 236 LKKLLKKDPSKRLTATQALQHPWF 259
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
86-344 1.33e-105

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 316.39  E-value: 1.33e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426      86 YTLGRELGRGQFGVTYLCTDKKTGQQYACKSISKKKLvtKADKDDMRREIQIMQHMsGQPNIVEFKGAYEDKTSVNLVME 165
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKI--KKDRERILREIKILKKL-KHPNIVRLYDVFEDEDKLYLVME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426     166 LCAGGELFDRIIAKGHYSEKAAATMLRQIVNVVHVCHFMGVMHRDLKPENFLLsskDENSLLKATDFGLSVFIEEGKVYR 245
Cdd:smart00220  78 YCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILL---DEDGHVKLADFGLARQLDPGEKLT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426     246 DIVGSAYYVAPEVLRRR-YGKEIDVWSAGVMLYILLSGVPPFWA-ETEKGIFDAILQGHIDFESKPWPsISNGAKDLVRK 323
Cdd:smart00220 155 TFVGTPEYMAPEVLLGKgYGKAVDIWSLGVILYELLTGKPPFPGdDQLLELFKKIGKPKPPFPPPEWD-ISPEAKDLIRK 233
                          250       260
                   ....*....|....*....|.
gi 4336426     324 MLTQDPKKRITAAQVLEHPWL 344
Cdd:smart00220 234 LLVKDPEKRLTAEEALQHPFF 254
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
86-343 1.30e-94

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 [Multi-domain]  Cd Length: 252  Bit Score: 288.26  E-value: 1.30e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426   86 YTLGRELGRGQFGVTYLCTDKKTGQQYACKSISKKKLVTKADKDdMRREIQIMQHMSgQPNIVEFKGAYEDKTSVNLVME 165
Cdd:cd14003   2 YELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEIEEK-IKREIEIMKLLN-HPNIIKLYEVIETENKIYLVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426  166 LCAGGELFDRIIAKGHYSEKAAATMLRQIVNVVHVCHFMGVMHRDLKPENFLLsskDENSLLKATDFGLSVFIEEGKVYR 245
Cdd:cd14003  80 YASGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILL---DKNGNLKIIDFGLSNEFRGGSLLK 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426  246 DIVGSAYYVAPEVLRRR--YGKEIDVWSAGVMLYILLSGVPPFWAETEKGIFDAILQGHIDFeskpWPSISNGAKDLVRK 323
Cdd:cd14003 157 TFCGTPAYAAPEVLLGRkyDGPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKYPI----PSHLSPDARDLIRR 232
                       250       260
                ....*....|....*....|
gi 4336426  324 MLTQDPKKRITAAQVLEHPW 343
Cdd:cd14003 233 MLVVDPSKRITIEEILNHPW 252
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
82-343 2.89e-88

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 [Multi-domain]  Cd Length: 259  Bit Score: 271.94  E-value: 2.89e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426   82 VKVYYTLGRELGRGQFGVTYLCTDKKTGQQYACKSISKKKLvtKADKDDMRREIQIMQHMSgQPNIVEFKGAYEDKTSVN 161
Cdd:cd14083   1 IRDKYEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDKKAL--KGKEDSLENEIAVLRKIK-HPNIVQLLDIYESKSHLY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426  162 LVMELCAGGELFDRIIAKGHYSEKAAATMLRQIVNVVHVCHFMGVMHRDLKPENFLLSSKDENSLLKATDFGLSVfIEEG 241
Cdd:cd14083  78 LVMELVTGGELFDRIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYYSPDEDSKIMISDFGLSK-MEDS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426  242 KVYRDIVGSAYYVAPEVLRRR-YGKEIDVWSAGVMLYILLSGVPPFWAETEKGIFDAILQGHIDFESKPWPSISNGAKDL 320
Cdd:cd14083 157 GVMSTACGTPGYVAPEVLAQKpYGKAVDCWSIGVISYILLCGYPPFYDENDSKLFAQILKAEYEFDSPYWDDISDSAKDF 236
                       250       260
                ....*....|....*....|...
gi 4336426  321 VRKMLTQDPKKRITAAQVLEHPW 343
Cdd:cd14083 237 IRHLMEKDPNKRYTCEQALEHPW 259
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
88-345 3.24e-85

Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Yeast contains only one Aurora kinase while most higher eukaryotes have two. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2. Aurora-B is most active at the transition during metaphase to the end of mitosis. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. The Aurora 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: 270909 [Multi-domain]  Cd Length: 253  Bit Score: 263.95  E-value: 3.24e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426   88 LGRELGRGQFGVTYLCTDKKTGQQYACKSISKKKLVTKADKDDMRREIQIMQHMSgQPNIVEFKGAYEDKTSVNLVMELC 167
Cdd:cd14007   4 IGKPLGKGKFGNVYLAREKKSGFIVALKVISKSQLQKSGLEHQLRREIEIQSHLR-HPNILRLYGYFEDKKRIYLILEYA 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426  168 AGGELFDRIIAKGHYSEKAAATMLRQIVNVVHVCHFMGVMHRDLKPENFLLSSKDEnslLKATDFGLSVFIEEGKvyRD- 246
Cdd:cd14007  83 PNGELYKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGE---LKLADFGWSVHAPSNR--RKt 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426  247 IVGSAYYVAPEVLRRR-YGKEIDVWSAGVMLYILLSGVPPFWAETEKGIFDAILQGHIDFeskpWPSISNGAKDLVRKML 325
Cdd:cd14007 158 FCGTLDYLPPEMVEGKeYDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNVDIKF----PSSVSPEAKDLISKLL 233
                       250       260
                ....*....|....*....|
gi 4336426  326 TQDPKKRITAAQVLEHPWLR 345
Cdd:cd14007 234 QKDPSKRLSLEQVLNHPWIK 253
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
86-372 6.09e-84

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type II; 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. CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. In addition, CaMKII contains a C-terminal association domain that facilitates oligomerization. There are four CaMKII proteins (alpha, beta, gamma, delta) encoded by different genes; each gene undergoes alternative splicing to produce more than 30 isoforms. CaMKII-alpha and -beta are enriched in neurons while CaMKII-gamma and -delta are predominant in myocardium. 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. It is a major component of the postsynaptic density and is critical in regulating synaptic plasticity including long-term potentiation. It is critical in regulating ion channels and proteins involved in myocardial excitation-contraction and excitation-transcription coupling. Excessive CaMKII activity promotes processes that contribute to heart failure and arrhythmias. The CaMKII 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: 270988 [Multi-domain]  Cd Length: 292  Bit Score: 261.97  E-value: 6.09e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426   86 YTLGRELGRGQFGVTYLCTDKKTGQQYACKSISKKKLVTKaDKDDMRREIQI---MQHmsgqPNIVEFKGAYEDKTSVNL 162
Cdd:cd14086   3 YDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSAR-DHQKLEREARIcrlLKH----PNIVRLHDSISEEGFHYL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426  163 VMELCAGGELFDRIIAKGHYSEKAAATMLRQIVNVVHVCHFMGVMHRDLKPENFLLSSKDENSLLKATDFGLSVFIE-EG 241
Cdd:cd14086  78 VFDLVTGGELFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKSKGAAVKLADFGLAIEVQgDQ 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426  242 KVYRDIVGSAYYVAPEVLRRR-YGKEIDVWSAGVMLYILLSGVPPFWAETEKGIFDAILQGHIDFESKPWPSISNGAKDL 320
Cdd:cd14086 158 QAWFGFAGTPGYLSPEVLRKDpYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYDYPSPEWDTVTPEAKDL 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 4336426  321 VRKMLTQDPKKRITAAQVLEHPWL--RDGEASDKPIDSAVLLrMKQFRVMNKLK 372
Cdd:cd14086 238 INQMLTVNPAKRITAAEALKHPWIcqRDRVASMVHRQETVDC-LKKFNARRKLK 290
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
86-349 2.84e-82

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 [Multi-domain]  Cd Length: 291  Bit Score: 257.95  E-value: 2.84e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426   86 YTLGRELGRGQFGVTYLCTDKKTGQQYACKSISKKKlvtkadkDDMRREIQIMQHMSGQPNIVEFKGAYEDKTSVNLVME 165
Cdd:cd14091   2 YEIKEEIGKGSYSVCKRCIHKATGKEYAVKIIDKSK-------RDPSEEIEILLRYGQHPNIITLRDVYDDGNSVYLVTE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426  166 LCAGGELFDRIIAKGHYSEKAAATMLRQIVNVVHVCHFMGVMHRDLKPENFLLSSKDEN-SLLKATDFGLSvfieegKVY 244
Cdd:cd14091  75 LLRGGELLDRILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESGDpESLRICDFGFA------KQL 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426  245 RDIVG-------SAYYVAPEVLRRR-YGKEIDVWSAGVMLYILLSGVPPFWA---ETEKGIFDAILQGHIDFESKPWPSI 313
Cdd:cd14091 149 RAENGllmtpcyTANFVAPEVLKKQgYDAACDIWSLGVLLYTMLAGYTPFASgpnDTPEVILARIGSGKIDLSGGNWDHV 228
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 4336426  314 SNGAKDLVRKMLTQDPKKRITAAQVLEHPWLRDGEA 349
Cdd:cd14091 229 SDSAKDLVRKMLHVDPSQRPTAAQVLQHPWIRNRDS 264
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
85-380 2.80e-81

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type IV; 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. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKIV is found predominantly in neurons and immune cells. It is activated by the binding of calcium/CaM and phosphorylation by CaMKK (alpha or beta). The CaMKK-CaMKIV cascade participates in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors. It also is implicated in T-cell development and signaling, cytokine secretion, and signaling through Toll-like receptors, and is thus, pivotal in immune response and inflammation. The CaMKIV 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: 270987 [Multi-domain]  Cd Length: 294  Bit Score: 255.52  E-value: 2.80e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426   85 YYTLGRELGRGQFGVTYLCTDKKTGQQYACKSISKKklvtkADKDDMRREIQIMQHMSgQPNIVEFKGAYEDKTSVNLVM 164
Cdd:cd14085   4 FFEIESELGRGATSVVYRCRQKGTQKPYAVKKLKKT-----VDKKIVRTEIGVLLRLS-HPNIIKLKEIFETPTEISLVL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426  165 ELCAGGELFDRIIAKGHYSEKAAATMLRQIVNVVHVCHFMGVMHRDLKPENFLLSSKDENSLLKATDFGLSVFIEEGKVY 244
Cdd:cd14085  78 ELVTGGELFDRIVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPDAPLKIADFGLSKIVDQQVTM 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4336426  245 RDIV