NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|18416872|ref|NP_568281|]
View 

calmodulin-domain protein kinase 7 [Arabidopsis thaliana]

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 ...
58-316 1.17e-141

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: 408.40  E-value: 1.17e-141
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872  58 QYDLGREVGRGEFGITYLCTDKETGEKYACKSISKKKLRTAvDIEDVRREVEIMKHMpKHPNVVSLKDSFEDDDAVHIVM 137
Cdd:cd05117   1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSE-DEEMLRREIEILKRL-DHPNIVKLYEVFEDDKNLYLVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872 138 ELCEGGELFDRIVARGHYTERAAAAVMKTIVEVVQICHKQGVMHRDLKPENFLFANKKETSALKAIDFGLSVFFKPGEQF 217
Cdd:cd05117  79 ELCTGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPDSPIKIIDFGLAKIFEEGEKL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872 218 NEIVGSPYYMAPEVLRRN-YGPEIDVWSAGVILYILLCGVPPFWAETEQGVAQAIIRSVIDFKRDPWPRVSDSAKDLVRK 296
Cdd:cd05117 159 KTVCGTPYYVAPEVLKGKgYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYSFDSPEWKNVSEEAKDLIKR 238
                       250       260
                ....*....|....*....|
gi 18416872 297 MLEPDPKKRLTAAQVLEHTW 316
Cdd:cd05117 239 LLVVDPKKRLTAAEALNHPW 258
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
356-503 3.96e-27

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


:

Pssm-ID: 227455 [Multi-domain]  Cd Length: 160  Bit Score: 107.01  E-value: 3.96e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872 356 HLSVEEAAGIKEAFEMMDVNKRGKINLEELKYGLQKAGQQIADTDLQILMEATDvDGDGTLNYSEFVAV-SVHLKKMAND 434
Cdd:COG5126  13 QLTEEQIQELKEAFQLFDRDSDGLIDRNELGKILRSLGFNPSEAEINKLFEEID-AGNETVDFPEFLTVmSVKLKRGDKE 91
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18416872 435 EHLHKAFNFFDQNQSGYIEIDELREALnDELDNTSSEEVIAAIMQDVDTDKDGRISYEEFVAMMKAGTD 503
Cdd:COG5126  92 EELREAFKLFDKDHDGYISIGELRRVL-KSLGERLSDEEVEKLLKEYDEDGDGEIDYEEFKKLIKDSPT 159
 
Name Accession Description Interval E-value
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
58-316 1.17e-141

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: 408.40  E-value: 1.17e-141
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872  58 QYDLGREVGRGEFGITYLCTDKETGEKYACKSISKKKLRTAvDIEDVRREVEIMKHMpKHPNVVSLKDSFEDDDAVHIVM 137
Cdd:cd05117   1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSE-DEEMLRREIEILKRL-DHPNIVKLYEVFEDDKNLYLVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872 138 ELCEGGELFDRIVARGHYTERAAAAVMKTIVEVVQICHKQGVMHRDLKPENFLFANKKETSALKAIDFGLSVFFKPGEQF 217
Cdd:cd05117  79 ELCTGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPDSPIKIIDFGLAKIFEEGEKL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872 218 NEIVGSPYYMAPEVLRRN-YGPEIDVWSAGVILYILLCGVPPFWAETEQGVAQAIIRSVIDFKRDPWPRVSDSAKDLVRK 296
Cdd:cd05117 159 KTVCGTPYYVAPEVLKGKgYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYSFDSPEWKNVSEEAKDLIKR 238
                       250       260
                ....*....|....*....|
gi 18416872 297 MLEPDPKKRLTAAQVLEHTW 316
Cdd:cd05117 239 LLVVDPKKRLTAAEALNHPW 258
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
59-317 2.15e-109

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 326.02  E-value: 2.15e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872     59 YDLGREVGRGEFGITYLCTDKETGEKYACKSISKKKLRTavDIEDVRREVEIMKHMpKHPNVVSLKDSFEDDDAVHIVME 138
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKK--DRERILREIKILKKL-KHPNIVRLYDVFEDEDKLYLVME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872    139 LCEGGELFDRIVARGHYTERAAAAVMKTIVEVVQICHKQGVMHRDLKPENFLFANKKEtsaLKAIDFGLSVFFKPGEQFN 218
Cdd:smart00220  78 YCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGH---VKLADFGLARQLDPGEKLT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872    219 EIVGSPYYMAPEVLRRN-YGPEIDVWSAGVILYILLCGVPPFWAETEQGVAQAIIRSVIDFKRDPWPRVSDSAKDLVRKM 297
Cdd:smart00220 155 TFVGTPEYMAPEVLLGKgYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKDLIRKL 234
                          250       260
                   ....*....|....*....|
gi 18416872    298 LEPDPKKRLTAAQVLEHTWI 317
Cdd:smart00220 235 LVKDPEKRLTAEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
59-317 2.97e-108

Protein kinase domain;


Pssm-ID: 333812 [Multi-domain]  Cd Length: 259  Bit Score: 323.42  E-value: 2.97e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872    59 YDLGREVGRGEFGITYLCTDKETGEKYACKSISKKKlRTAVDIEDVRREVEIMKHMpKHPNVVSLKDSFEDDDAVHIVME 138
Cdd:pfam00069   1 YEVLEKLGEGSFGTVYKAKHKDTGKIVAIKKIKKEK-IKKKKEKNVLREIKILKKL-SHPNIVRLYDVFEDKDHLYLVLE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872   139 LCEGGELFDRIVARGHYTERAAAAVMKTIVEVVQICHKQGVMHRDLKPENFLFANKKEtsaLKAIDFGLSVFFKPGEQFN 218
Cdd:pfam00069  79 YVEGGSLFDLLSEKGVFSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENILIDEDGN---LKITDFGLAKQLSSGSKLT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872   219 EIVGSPYYMAPEVLRRN-YGPEIDVWSAGVILYILLCGVPPFWAETEQGVAQAIIR----SVIDFKRDPWPRVSDSAKDL 293
Cdd:pfam00069 156 TFVGTPWYMAPEVLGGNpYGPKVDVWSLGCILYELLTGKPPFPGINGDDIYELILDqlerIPEDFSSPFPSSLSEEAKDL 235
                         250       260
                  ....*....|....*....|....
gi 18416872   294 VRKMLEPDPKKRLTAAQVLEHTWI 317
Cdd:pfam00069 236 LKKLLKKDPSKRLTATQALQHPWF 259
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
59-317 1.30e-55

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 191.49  E-value: 1.30e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872  59 YDLGREVGRGEFGITYLCTDKEtgeKYACKSISKKKLRTAVDIEDVRREVEIMKHMPKHPNVVSLKDSFEDDDAVHIVME 138
Cdd:COG0515   2 YRILRKLGEGSFGEVYLARDRK---LVALKVLAKKLESKSKEVERFLREIQILASLNHPPNIVKLYDFFQDEGSLYLVME 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872 139 LCEGGELFDRIVARGH---YTERAAAAVMKTIVEVVQICHKQGVMHRDLKPENFLFanKKETSALKAIDFGLSVFFKPGE 215
Cdd:COG0515  79 YVDGGSLEDLLKKIGRkgpLSESEALFILAQILSALEYLHSKGIIHRDIKPENILL--DRDGRVVKLIDFGLAKLLPDPG 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872 216 Q-------FNEIVGSPYYMAPEVLR----RNYGPEIDVWSAGVILYILLCGVPPFWAETEQGVAQAIIRSV--------- 275
Cdd:COG0515 157 StssipalPSTSVGTPGYMAPEVLLglslAYASSSSDIWSLGITLYELLTGLPPFEGEKNSSATSQTLKIIlelptpsla 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 18416872 276 IDFKRDPWPRVSDSAKDLVRKMLEPDPKKRLTAAQVLEHTWI 317
Cdd:COG0515 237 SPLSPSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLL 278
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
59-306 1.10e-38

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 144.19  E-value: 1.10e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872   59 YDLGREVGRGEFGITYLCTDKETGEKYACKSISKKKLRTAVDIEDVRREVEIMKHMpKHPNVVSLKDSFEDDDAVHIVME 138
Cdd:PTZ00263  20 FEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSILMEL-SHPFIVNMMCSFQDENRVYFLLE 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872  139 LCEGGELFDRIVARGHYTERAAAAVMKTIVEVVQICHKQGVMHRDLKPENFLFANKKEtsaLKAIDFGLSVffKPGEQFN 218
Cdd:PTZ00263  99 FVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGH---VKVTDFGFAK--KVPDRTF 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872  219 EIVGSPYYMAPEVLR-RNYGPEIDVWSAGVILYILLCGVPPFWAETEQGVAQAIIRSVIDFKRdpWprVSDSAKDLVRKM 297
Cdd:PTZ00263 174 TLCGTPEYLAPEVIQsKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPN--W--FDGRARDLVKGL 249

                 ....*....
gi 18416872  298 LEPDPKKRL 306
Cdd:PTZ00263 250 LQTDHTKRL 258
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
356-503 3.96e-27

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


Pssm-ID: 227455 [Multi-domain]  Cd Length: 160  Bit Score: 107.01  E-value: 3.96e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872 356 HLSVEEAAGIKEAFEMMDVNKRGKINLEELKYGLQKAGQQIADTDLQILMEATDvDGDGTLNYSEFVAV-SVHLKKMAND 434
Cdd:COG5126  13 QLTEEQIQELKEAFQLFDRDSDGLIDRNELGKILRSLGFNPSEAEINKLFEEID-AGNETVDFPEFLTVmSVKLKRGDKE 91
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18416872 435 EHLHKAFNFFDQNQSGYIEIDELREALnDELDNTSSEEVIAAIMQDVDTDKDGRISYEEFVAMMKAGTD 503
Cdd:COG5126  92 EELREAFKLFDKDHDGYISIGELRRVL-KSLGERLSDEEVEKLLKEYDEDGDGEIDYEEFKKLIKDSPT 159
PTZ00184 PTZ00184
calmodulin; Provisional
353-498 6.05e-22

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 92.13  E-value: 6.05e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872  353 IAEHLSVEEAAGIKEAFEMMDVNKRGKINLEELKYGLQKAGQQIADTDLQILMEATDVDGDGTLNYSEFVAVSVhlKKMA 432
Cdd:PTZ00184   1 MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTLMA--RKMK 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18416872  433 N---DEHLHKAFNFFDQNQSGYIEIDELREALNDELDNTSSEEVIAAImQDVDTDKDGRISYEEFVAMM 498
Cdd:PTZ00184  79 DtdsEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMI-READVDGDGQINYEEFVKMM 146
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
80-312 2.26e-21

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: 98.38  E-value: 2.26e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872     80 ETGEKYACKSISKKKLRTAVDIEDVRREVEIMKHMpKHPNVVSLKDSFE-DDDAVHIVMELCEGGELFDRIVARGHYTER 158
Cdd:TIGR03903    1 MTGHEVAIKLLRTDAPEEEHQRARFRRETALCARL-YHPNIVALLDSGEaPPGLLFAVFEYVPGRTLREVLAADGALPAG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872    159 AAAAVMKTIVEVVQICHKQGVMHRDLKPENFLFANKKETSALKAIDFGLSVFFkPG---------EQFNEIVGSPYYMAP 229
Cdd:TIGR03903   80 ETGRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGVRPHAKVLDFGIGTLL-PGvrdadvatlTRTTEVLGTPTYCAP 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872    230 EVLR-RNYGPEIDVWSAGVILYILLCGVPPFWAETeqgVAQAIIR--SVIDFKRDPWPRvSDSAKDLVRKMLEPDPKKRL 306
Cdd:TIGR03903  159 EQLRgEPVTPNSDLYAWGLIFLECLTGQRVVQGAS---VAEILYQqlSPVDVSLPPWIA-GHPLGQVLRKALNKDPRQRA 234

                   ....*.
gi 18416872    307 TAAQVL 312
Cdd:TIGR03903  235 ASAPAL 240
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
436-499 1.34e-17

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 76.82  E-value: 1.34e-17
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18416872 436 HLHKAFNFFDQNQSGYIEIDELREALNDELDNTSSEEvIAAIMQDVDTDKDGRISYEEFVAMMK 499
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEE-IDEMIREVDKDGDGKIDFEEFLELMA 63
EF-hand_7 pfam13499
EF-hand domain pair;
434-499 5.46e-17

EF-hand domain pair;


Pssm-ID: 338778 [Multi-domain]  Cd Length: 68  Bit Score: 75.00  E-value: 5.46e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18416872   434 DEHLHKAFNFFDQNQSGYIEIDELREAL--NDELDNTSSEEVIAAIMQDVDTDKDGRISYEEFVAMMK 499
Cdd:pfam13499   1 EEKLKEAFKLLDKDGDGYLDVEELKKLLrkLFEEGEKLSDEEVEELFKEFDLDKDGRISFEEFLELYR 68
 
Name Accession Description Interval E-value
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
58-316 1.17e-141

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: 408.40  E-value: 1.17e-141
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872  58 QYDLGREVGRGEFGITYLCTDKETGEKYACKSISKKKLRTAvDIEDVRREVEIMKHMpKHPNVVSLKDSFEDDDAVHIVM 137
Cdd:cd05117   1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSE-DEEMLRREIEILKRL-DHPNIVKLYEVFEDDKNLYLVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872 138 ELCEGGELFDRIVARGHYTERAAAAVMKTIVEVVQICHKQGVMHRDLKPENFLFANKKETSALKAIDFGLSVFFKPGEQF 217
Cdd:cd05117  79 ELCTGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPDSPIKIIDFGLAKIFEEGEKL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872 218 NEIVGSPYYMAPEVLRRN-YGPEIDVWSAGVILYILLCGVPPFWAETEQGVAQAIIRSVIDFKRDPWPRVSDSAKDLVRK 296
Cdd:cd05117 159 KTVCGTPYYVAPEVLKGKgYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYSFDSPEWKNVSEEAKDLIKR 238
                       250       260
                ....*....|....*....|
gi 18416872 297 MLEPDPKKRLTAAQVLEHTW 316
Cdd:cd05117 239 LLVVDPKKRLTAAEALNHPW 258
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
59-317 2.15e-109

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 326.02  E-value: 2.15e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872     59 YDLGREVGRGEFGITYLCTDKETGEKYACKSISKKKLRTavDIEDVRREVEIMKHMpKHPNVVSLKDSFEDDDAVHIVME 138
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKK--DRERILREIKILKKL-KHPNIVRLYDVFEDEDKLYLVME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872    139 LCEGGELFDRIVARGHYTERAAAAVMKTIVEVVQICHKQGVMHRDLKPENFLFANKKEtsaLKAIDFGLSVFFKPGEQFN 218
Cdd:smart00220  78 YCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGH---VKLADFGLARQLDPGEKLT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872    219 EIVGSPYYMAPEVLRRN-YGPEIDVWSAGVILYILLCGVPPFWAETEQGVAQAIIRSVIDFKRDPWPRVSDSAKDLVRKM 297
Cdd:smart00220 155 TFVGTPEYMAPEVLLGKgYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKDLIRKL 234
                          250       260
                   ....*....|....*....|
gi 18416872    298 LEPDPKKRLTAAQVLEHTWI 317
Cdd:smart00220 235 LVKDPEKRLTAEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
59-317 2.97e-108

Protein kinase domain;


Pssm-ID: 333812 [Multi-domain]  Cd Length: 259  Bit Score: 323.42  E-value: 2.97e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872    59 YDLGREVGRGEFGITYLCTDKETGEKYACKSISKKKlRTAVDIEDVRREVEIMKHMpKHPNVVSLKDSFEDDDAVHIVME 138
Cdd:pfam00069   1 YEVLEKLGEGSFGTVYKAKHKDTGKIVAIKKIKKEK-IKKKKEKNVLREIKILKKL-SHPNIVRLYDVFEDKDHLYLVLE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872   139 LCEGGELFDRIVARGHYTERAAAAVMKTIVEVVQICHKQGVMHRDLKPENFLFANKKEtsaLKAIDFGLSVFFKPGEQFN 218
Cdd:pfam00069  79 YVEGGSLFDLLSEKGVFSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENILIDEDGN---LKITDFGLAKQLSSGSKLT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872   219 EIVGSPYYMAPEVLRRN-YGPEIDVWSAGVILYILLCGVPPFWAETEQGVAQAIIR----SVIDFKRDPWPRVSDSAKDL 293
Cdd:pfam00069 156 TFVGTPWYMAPEVLGGNpYGPKVDVWSLGCILYELLTGKPPFPGINGDDIYELILDqlerIPEDFSSPFPSSLSEEAKDL 235
                         250       260
                  ....*....|....*....|....
gi 18416872   294 VRKMLEPDPKKRLTAAQVLEHTWI 317
Cdd:pfam00069 236 LKKLLKKDPSKRLTATQALQHPWF 259
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
58-316 6.75e-95

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: 289.03  E-value: 6.75e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872  58 QYDLGREVGRGEFGITYLCTDKETGEKYACKSISKKKLRTAVDiEDVRREVEIMKHMpKHPNVVSLKDSFEDDDAVHIVM 137
Cdd:cd14003   1 NYELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEIE-EKIKREIEIMKLL-NHPNIIKLYEVIETENKIYLVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872 138 ELCEGGELFDRIVARGHYTERAAAAVMKTIVEVVQICHKQGVMHRDLKPENFLFANKKEtsaLKAIDFGLSVFFKPGEQF 217
Cdd:cd14003  79 EYASGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGN---LKIIDFGLSNEFRGGSLL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872 218 NEIVGSPYYMAPEVL-RRNY-GPEIDVWSAGVILYILLCGVPPFWAETEqgvaQAIIRSVIDFKRDPWPRVSDSAKDLVR 295
Cdd:cd14003 156 KTFCGTPAYAAPEVLlGRKYdGPKADVWSLGVILYAMLTGYLPFDDDND----SKLFRKILKGKYPIPSHLSPDARDLIR 231
                       250       260
                ....*....|....*....|.
gi 18416872 296 KMLEPDPKKRLTAAQVLEHTW 316
Cdd:cd14003 232 RMLVVDPSKRITIEEILNHPW 252
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
58-346 2.19e-90

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: 278.92  E-value: 2.19e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872  58 QYDLGREVGRGEFGITYLCTDKETGEKYACKSISKKKLrTAVDIEDVRREVEIMKhMPKHPNVVSLKDSFEDDDAVHIVM 137
Cdd:cd14086   2 EYDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINTKKL-SARDHQKLEREARICR-LLKHPNIVRLHDSISEEGFHYLVF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872 138 ELCEGGELFDRIVARGHYTERAAAAVMKTIVEVVQICHKQGVMHRDLKPENFLFANKKETSALKAIDFGLSVFFKPGEQ- 216
Cdd:cd14086  80 DLVTGGELFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKSKGAAVKLADFGLAIEVQGDQQa 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872 217 FNEIVGSPYYMAPEVLRRN-YGPEIDVWSAGVILYILLCGVPPFWAETEQGVAQAIIRSVIDFKRDPWPRVSDSAKDLVR 295
Cdd:cd14086 160 WFGFAGTPGYLSPEVLRKDpYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYDYPSPEWDTVTPEAKDLIN 239
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 18416872 296 KMLEPDPKKRLTAAQVLEHTWILNAKK-APNVSLGETVKArLKQFSVMNKLK 346
Cdd:cd14086 240 QMLTVNPAKRITAAEALKHPWICQRDRvASMVHRQETVDC-LKKFNARRKLK 290
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
58-328 3.44e-88

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: 272.97  E-value: 3.44e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872  58 QYDLGREVGRGEFGITYLCTDKETGEKYACKSISKKKlrtavdiEDVRREVEIMKHMPKHPNVVSLKDSFEDDDAVHIVM 137
Cdd:cd14091   1 EYEIKEEIGKGSYSVCKRCIHKATGKEYAVKIIDKSK-------RDPSEEIEILLRYGQHPNIITLRDVYDDGNSVYLVT 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872 138 ELCEGGELFDRIVARGHYTERAAAAVMKTIVEVVQICHKQGVMHRDLKPENFLFANKKET-SALKAIDFGlsvFFKPGEQ 216
Cdd:cd14091  74 ELLRGGELLDRILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESGDpESLRICDFG---FAKQLRA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872 217 FNEIVGSPYY----MAPEVLRRN-YGPEIDVWSAGVILYILLCGVPPFwAETEQGVAQAIIRSV----IDFKRDPWPRVS 287
Cdd:cd14091 151 ENGLLMTPCYtanfVAPEVLKKQgYDAACDIWSLGVLLYTMLAGYTPF-ASGPNDTPEVILARIgsgkIDLSGGNWDHVS 229
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 18416872 288 DSAKDLVRKMLEPDPKKRLTAAQVLEHTWILNAKKAPNVSL 328
Cdd:cd14091 230 DSAKDLVRKMLHVDPSQRPTAAQVLQHPWIRNRDSLPQRQL 270
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
55-316 1.12e-85

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: 265.39  E-value: 1.12e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872  55 ISLQYDLGREVGRGEFGITYLCTDKETGEKYACKSISKKKLRTAVDieDVRREVEIMKHMpKHPNVVSLKDSFEDDDAVH 134
Cdd:cd14083   1 IRDKYEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDKKALKGKED--SLENEIAVLRKI-KHPNIVQLLDIYESKSHLY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872 135 IVMELCEGGELFDRIVARGHYTERAAAAVMKTIVEVVQICHKQGVMHRDLKPENFLFANKKETSALKAIDFGLSVfFKPG 214
Cdd:cd14083  78 LVMELVTGGELFDRIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYYSPDEDSKIMISDFGLSK-MEDS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872 215 EQFNEIVGSPYYMAPEVLRRN-YGPEIDVWSAGVILYILLCGVPPFWAETEQGVAQAIIRSVIDFKRDPWPRVSDSAKDL 293
Cdd:cd14083 157 GVMSTACGTPGYVAPEVLAQKpYGKAVDCWSIGVISYILLCGYPPFYDENDSKLFAQILKAEYEFDSPYWDDISDSAKDF 236
                       250       260
                ....*....|....*....|...
gi 18416872 294 VRKMLEPDPKKRLTAAQVLEHTW 316
Cdd:cd14083 237 IRHLMEKDPNKRYTCEQALEHPW 259
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
59-354 7.77e-83

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: 259.37  E-value: 7.77e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872  59 YDLGREVGRGEFGITYLCTDKETGEKYACKsiskkKLRTAVDIEDVRREVEIMKHMpKHPNVVSLKDSFEDDDAVHIVME 138
Cdd:cd14085   5 FEIESELGRGATSVVYRCRQKGTQKPYAVK-----KLKKTVDKKIVRTEIGVLLRL-SHPNIIKLKEIFETPTEISLVLE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872 139 LCEGGELFDRIVARGHYTERAAAAVMKTIVEVVQICHKQGVMHRDLKPENFLFANKKETSALKAIDFGLSVFFKPGEQFN 218
Cdd:cd14085  79 LVTGGELFDRIVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPDAPLKIADFGLSKIVDQQVTMK 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872 219 EIVGSPYYMAPEVLR-RNYGPEIDVWSAGVILYILLCGVPPFWAE-TEQGVAQAIIRSVIDFKRDPWPRVSDSAKDLVRK 296
Cdd:cd14085 159 TVCGTPGYCAPEILRgCAYGPEVDMWSVGVITYILLCGFEPFYDErGDQYMFKRILNCDYDFVSPWWDDVSLNAKDLVKK 238
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 18416872 297 MLEPDPKKRLTAAQVLEHTWIlnAKKAPNVSLGETVKARLKQFSVMNKLKKRALRVIA 354
Cdd:cd14085 239 LIVLDPKKRLTTQQALQHPWV--TGKAANFAHMDTAQKKLQEFNARRKLKAAVKAVVA 294
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
58-318 4.32e-79

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: 248.16  E-value: 4.32e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872  58 QYDLGREVGRGEFGITYLCTDKETGEKYACKSISKKKLRTAVDIEDVRREVEIMKHMpKHPNVVSLKDSFEDDDAVHIVM 137
Cdd:cd14007   1 DFEIGKPLGKGKFGNVYLAREKKSGFIVALKVISKSQLQKSGLEHQLRREIEIQSHL-RHPNILRLYGYFEDKKRIYLIL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872 138 ELCEGGELFDRIVARGHYTERAAAAVMKTIVEVVQICHKQGVMHRDLKPENFLFANKKEtsaLKAIDFGLSVFFkPGEQF 217
Cdd:cd14007  80 EYAPNGELYKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGE---LKLADFGWSVHA-PSNRR 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18416872 218 NEIVGSPYYMAPE-VLRRNYGPEIDVWSAGVILYILLCGVPPFWAETEQGVAQAIIRSVIDFkrdpWPRVSDSAKDLVRK 296
Cdd:cd14007 156 KTFCGTLDYLPPEmVEGKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNVDIKF----PSSVSPEAKDLISK 231
                       250       260
                ....*....|....*....|..
gi 18416872 297 MLEPDPKKRLTAAQVLEHTWIL 318
Cdd:cd14007 232 LLQKDPSKRLSLEQVLNHPWIK 253
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
59-316 6.93e-78

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 [Multi-domain]  Cd Length: 258  Bit Score: 245.31  E-value: 6.93e-78
                        10        20        30        40        50        60        70        80
<