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Conserved domains on  [gi|6978593|ref|NP_037052.1|]
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calcium/calmodulin-dependent protein kinase type II subunit alpha

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List of domain hits

Name Accession Description Interval E-value
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
11-302 0e+00

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: 655.26  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593   11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd14086   1 DEYDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVFD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593   91 LVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAIEVEGEQQAW 170
Cdd:cd14086  81 LVTGGELFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKSKGAAVKLADFGLAIEVQGDQQAW 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593  171 FGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINK 250
Cdd:cd14086 161 FGFAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYDYPSPEWDTVTPEAKDLINQ 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 6978593  251 MLTINPSKRITAAEALKHPWISHRSTVASCMHRQETVDCLKKFNARRKLKGA 302
Cdd:cd14086 241 MLTVNPAKRITAAEALKHPWICQRDRVASMVHRQETVDCLKKFNARRKLKGA 292
CaMKII_AD pfam08332
Calcium/calmodulin dependent protein kinase II Association; This domain is found at the ...
346-473 2.02e-78

Calcium/calmodulin dependent protein kinase II Association; This domain is found at the C-terminus of the Calcium/calmodulin dependent protein kinases II (CaMKII). These proteins also have a Ser/Thr protein kinase domain (pfam00069) at their N-terminus. The function of the CaMKII association domain is the assembly of the single proteins into large (8 to 14 subunits) multimers.


:

Pssm-ID: 254736  Cd Length: 128  Bit Score: 242.73  E-value: 2.02e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593    346 RKQEIIKVTEQLIEAISNGDFESYTKMCDPGMTAFEPEALGNLVEGLDFHRFYFENLWSRNSKPVHTTILNPHIHLMGDE 425
Cdd:pfam08332   1 EEQEIIKVTERLIEAIATGDFETYTKLCDPDLTAFEPEALGNLVEGLEFHRFYFENFLGKRPKAVHTTILNPHVHLLGDD 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 6978593    426 SACIAYIRITQYLDAGGIPRTAQSEETRVWHRRDGKWQIVHFHRSGAP 473
Cdd:pfam08332  81 SACIAYVRLTQYMDKNGKAHTVQSEETRVWHKRDGKWQIVHVHRSAAP 128
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
13-271 1.27e-110

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


:

Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 330.26  E-value: 1.27e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593      13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINtKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLV 92
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIK-KKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYC 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593      93 TGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLAIEVEGEQQAWfG 172
Cdd:smart00220  80 EGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGH---VKLADFGLARQLDPGEKLT-T 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593     173 FAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQH-RLYQQIKAGAYDFPSPEWDtVTPEAKDLINKM 251
Cdd:smart00220 156 FVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLlELFKKIGKPKPPFPPPEWD-ISPEAKDLIRKL 234
                          250       260
                   ....*....|....*....|
gi 6978593     252 LTINPSKRITAAEALKHPWI 271
Cdd:smart00220 235 LVKDPEKRLTAEEALQHPFF 254
 
Name Accession Description Interval E-value
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
11-302 0e+00

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: 655.26  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593   11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd14086   1 DEYDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVFD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593   91 LVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAIEVEGEQQAW 170
Cdd:cd14086  81 LVTGGELFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKSKGAAVKLADFGLAIEVQGDQQAW 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593  171 FGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINK 250
Cdd:cd14086 161 FGFAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYDYPSPEWDTVTPEAKDLINQ 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 6978593  251 MLTINPSKRITAAEALKHPWISHRSTVASCMHRQETVDCLKKFNARRKLKGA 302
Cdd:cd14086 241 MLTVNPAKRITAAEALKHPWICQRDRVASMVHRQETVDCLKKFNARRKLKGA 292
CaMKII_AD pfam08332
Calcium/calmodulin dependent protein kinase II Association; This domain is found at the ...
346-473 2.02e-78

Calcium/calmodulin dependent protein kinase II Association; This domain is found at the C-terminus of the Calcium/calmodulin dependent protein kinases II (CaMKII). These proteins also have a Ser/Thr protein kinase domain (pfam00069) at their N-terminus. The function of the CaMKII association domain is the assembly of the single proteins into large (8 to 14 subunits) multimers.


Pssm-ID: 254736  Cd Length: 128  Bit Score: 242.73  E-value: 2.02e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593    346 RKQEIIKVTEQLIEAISNGDFESYTKMCDPGMTAFEPEALGNLVEGLDFHRFYFENLWSRNSKPVHTTILNPHIHLMGDE 425
Cdd:pfam08332   1 EEQEIIKVTERLIEAIATGDFETYTKLCDPDLTAFEPEALGNLVEGLEFHRFYFENFLGKRPKAVHTTILNPHVHLLGDD 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 6978593    426 SACIAYIRITQYLDAGGIPRTAQSEETRVWHRRDGKWQIVHFHRSGAP 473
Cdd:pfam08332  81 SACIAYVRLTQYMDKNGKAHTVQSEETRVWHKRDGKWQIVHVHRSAAP 128
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
13-271 1.27e-110

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 330.26  E-value: 1.27e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593      13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINtKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLV 92
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIK-KKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYC 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593      93 TGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLAIEVEGEQQAWfG 172
Cdd:smart00220  80 EGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGH---VKLADFGLARQLDPGEKLT-T 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593     173 FAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQH-RLYQQIKAGAYDFPSPEWDtVTPEAKDLINKM 251
Cdd:smart00220 156 FVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLlELFKKIGKPKPPFPPPEWD-ISPEAKDLIRKL 234
                          250       260
                   ....*....|....*....|
gi 6978593     252 LTINPSKRITAAEALKHPWI 271
Cdd:smart00220 235 LVKDPEKRLTAEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
13-271 1.36e-96

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 294.54  E-value: 1.36e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593     13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLV 92
Cdd:pfam00069   1 YELLRKLGSGSFGTVYKAKHKGTGKIVAVKILKKRSEKSKKDQTARREIRILRRLSHPNIVRLIDAFEDKDHLYLVMEYC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593     93 TGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLkgaAVKLADFGLAIEVEGEQQAWFG 172
Cdd:pfam00069  81 EGGDLFDYLSRGGPLSEDEAKKIALQILRGLEYLHSNGIIHRDLKPENILLDENG---VVKIADFGLAKKLTKSSSSLTT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593    173 FAGTPGYLSPEVLRK-DPYGKPVDLWACGVILYILLVGYPPFWDE---DQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLI 248
Cdd:pfam00069 158 FVGTPEYMAPEVLLGgNGYGPKVDVWSLGVILYELLTGKPPFSGEsilDQLQLIRRILGPPLEFDEPKSDSGSEEAKDLI 237
                         250       260
                  ....*....|....*....|...
gi 6978593    249 NKMLTINPSKRITAAEALKHPWI 271
Cdd:pfam00069 238 KKCLNKDPSKRPTAEEILQHPWF 260
SPS1 COG0515
Serine/threonine protein kinase [General function prediction only / Signal transduction ...
12-356 3.08e-57

Serine/threonine protein kinase [General function prediction only / Signal transduction mechanisms / Transcription / DNA replication, recombination, and repair]


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 196.12  E-value: 3.08e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593   12 EYQLFEELGKGAFSVVRRCVKVlagQEYAAKIINTKKLSARDHQKL-EREARICRLLKHP-NIVRLHDSISEEGHHYLIF 89
Cdd:COG0515   1 SYRILRKLGEGSFGEVYLARDR---KLVALKVLAKKLESKSKEVERfLREIQILASLNHPpNIVKLYDFFQDEGSLYLVM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593   90 DLVTGGEL---FEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASklKGAAVKLADFGLAIEVEGE 166
Cdd:COG0515  78 EYVDGGSLedlLKKIGRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDR--DGRVVKLIDFGLAKLLPDP 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593  167 QQAWFG------FAGTPGYLSPEVLR---KDPYGKPVDLWACGVILYILLVGYPPF----WDEDQHRLYQQIKAGAYDFP 233
Cdd:COG0515 156 GSTSSIpalpstSVGTPGYMAPEVLLglsLAYASSSSDIWSLGITLYELLTGLPPFegekNSSATSQTLKIILELPTPSL 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593  234 SPEWDTVTP-----EAKDLINKMLTINPSKRITAAEALKHPWISHRSTvascmhRQETVDCLKKFNARRKLKGAILTTML 308
Cdd:COG0515 236 ASPLSPSNPeliskAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKL------KESDLSDLLKPDDSAPLRLSLPPSLE 309
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 6978593  309 ATRNF--SGGKSGGNKKNDGVKESSESTNTTIEDEDTKVRKQEIIKVTEQ 356
Cdd:COG0515 310 ALISSlnSLAISGSDLKLDDSNFSKELAPNGVSSSPHNSSSLLLSTASSK 359
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
12-272 9.09e-49

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 171.54  E-value: 9.09e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593    12 EYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKK-LSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:PTZ00263  19 DFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREiLKMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFLLE 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593    91 LVTGGELFEDI---------VAREYYSEadashciqqILEAVLHCHQMGVVHRDLKPENLLLASKlkgAAVKLADFGLAI 161
Cdd:PTZ00263  99 FVVGGELFTHLrkagrfpndVAKFYHAE---------LVLAFEYLHSKDIIYRDLKPENLLLDNK---GHVKVTDFGFAK 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593   162 EVEGEQqawFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSpeWdtVT 241
Cdd:PTZ00263 167 KVPDRT---FTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPN--W--FD 239
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 6978593   242 PEAKDLINKMLTINPSKRITA-----AEALKHPWIS 272
Cdd:PTZ00263 240 GRARDLVKGLLQTDHTKRLGTlkggvADVKNHPYFH 275
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
6-273 1.21e-29

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 116.11  E-value: 1.21e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593     6 CTRFTEEYQLFEELG--KGAFSVVRRCVKVLAGQEYAAKIINTKKLSARD---HQklerearicrLLK-HPNIVRLHDSI 79
Cdd:PHA03390   9 LVQFLKNCEIVKKLKliDGKFGKVSVLKHKPTQKLFVQKIIKAKNFNAIEpmvHQ----------LMKdNPNFIKLYYSV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593    80 SEEGHHYLIFDLVTGGELFEDIVAREYYSEADASHCIQQILEAV--LHCHQmgVVHRDLKPENLLLASKLKgaAVKLADF 157
Cdd:PHA03390  79 TTLKGHVLIMDYIKDGDLFDLLKKEGKLSEAEVKKIIRQLVEALndLHKHN--IIHNDIKLENVLYDRAKD--RIYLCDY 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593   158 GLAiEVEGEQQAwfgFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWD--------EDQHRLYQQikaga 229
Cdd:PHA03390 155 GLC-KIIGTPSC---YDGTLDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFKEdedeeldlESLLKRQQK----- 225
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 6978593   230 yDFPSPEwdTVTPEAKDLINKMLTINPSKR-ITAAEALKHPWISH 273
Cdd:PHA03390 226 -KLPFIK--NVSKNANDFVQSMLKYNINYRlTNYNEIIKHPFLKI 267
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
36-266 2.83e-27

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: 114.56  E-value: 2.83e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593      36 GQEYAAKIINTKKLS-ARDHQKLEREARICRLLKHPNIVRLHDS-ISEEGHHYLIFDLVTGGELFEDIVAREYYSEADAS 113
Cdd:TIGR03903    3 GHEVAIKLLRTDAPEeEHQRARFRRETALCARLYHPNIVALLDSgEAPPGLLFAVFEYVPGRTLREVLAADGALPAGETG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593     114 HCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAIEVEG-----EQQAWFG--FAGTPGYLSPEVLR 186
Cdd:TIGR03903   83 RLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGVRPHAKVLDFGIGTLLPGvrdadVATLTRTteVLGTPTYCAPEQLR 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593     187 KDPYGKPVDLWACGVILYILLVGYPPFWDED-QHRLYQQIkaGAYDFPSPEWDTVTPEAkDLINKMLTINPSKRITAAEA 265
Cdd:TIGR03903  163 GEPVTPNSDLYAWGLIFLECLTGQRVVQGASvAEILYQQL--SPVDVSLPPWIAGHPLG-QVLRKALNKDPRQRAASAPA 239

                   .
gi 6978593     266 L 266
Cdd:TIGR03903  240 L 240
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
11-270 3.95e-27

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 109.52  E-value: 3.95e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593    11 EEYQLFEELGKGAFSVVRRcvkvlAGQEYAAKIINTKKLsaRDHQKLE-------REARICRLLKHPNIVRLHDSISEEG 83
Cdd:PLN00009   2 DQYEKVEKIGEGTYGVVYK-----ARDRVTNETIALKKI--RLEQEDEgvpstaiREISLLKEMQHGNIVRLQDVVHSEK 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593    84 HHYLIFdlvtggELFEDIVAREYYSEADAS---HCIQ----QILEAVLHCHQMGVVHRDLKPENLLLASKLKgaAVKLAD 156
Cdd:PLN00009  75 RLYLVF------EYLDLDLKKHMDSSPDFAknpRLIKtylyQILRGIAYCHSHRVLHRDLKPQNLLIDRRTN--ALKLAD 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593   157 FGLAIEVEGEQQAWFGFAGTPGYLSPEVLR-KDPYGKPVDLWACGVIlYILLVGYPPFWDEDQ-----HRLYQ------- 223
Cdd:PLN00009 147 FGLARAFGIPVRTFTHEVVTLWYRAPEILLgSRHYSTPVDIWSVGCI-FAEMVNQKPLFPGDSeidelFKIFRilgtpne 225
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6978593   224 QIKAGAYDFPS-----PEWD---------TVTPEAKDLINKMLTINPSKRITAAEALKHPW 270
Cdd:PLN00009 226 ETWPGVTSLPDyksafPKWPpkdlatvvpTLEPAGVDLLSKMLRLDPSKRITARAALEHEY 286
pknD PRK13184
serine/threonine-protein kinase; Reviewed
11-267 3.29e-17

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 83.28  E-value: 3.29e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593    11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINtKKLS--ARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLI 88
Cdd:PRK13184   2 QRYDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIR-EDLSenPLLKKRFLREAKIAADLIHPGIVPVYSICSDGDPVYYT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593    89 FDLVTGGELFE--------DIVAREYYSEADASHCIQ---QILEAVLHCHQMGVVHRDLKPENLLLAskLKGAAVKLaDF 157
Cdd:PRK13184  81 MPYIEGYTLKSllksvwqkESLSKELAEKTSVGAFLSifhKICATIEYVHSKGVLHRDLKPDNILLG--LFGEVVIL-DW 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593   158 GLAIEVEGEQQAWFGF------------------AGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQH 219
Cdd:PRK13184 158 GAAIFKKLEEEDLLDIdvdernicyssmtipgkiVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYRRKKGR 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 6978593   220 RLY--QQIkagaydfPSPE----WDTVTPEAKDLINKMLTINPSKRITAAEALK 267
Cdd:PRK13184 238 KISyrDVI-------LSPIevapYREIPPFLSQIAMKALAVDPAERYSSVQELK 284
 
Name Accession Description Interval E-value
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
11-302 0e+00

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: 655.26  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593   11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd14086   1 DEYDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVFD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593   91 LVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAIEVEGEQQAW 170
Cdd:cd14086  81 LVTGGELFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKSKGAAVKLADFGLAIEVQGDQQAW 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593  171 FGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINK 250
Cdd:cd14086 161 FGFAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYDYPSPEWDTVTPEAKDLINQ 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 6978593  251 MLTINPSKRITAAEALKHPWISHRSTVASCMHRQETVDCLKKFNARRKLKGA 302
Cdd:cd14086 241 MLTVNPAKRITAAEALKHPWICQRDRVASMVHRQETVDCLKKFNARRKLKGA 292
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
13-270 5.10e-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: 5.10e-141
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593   13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLV 92
Cdd:cd05117   2 YELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLVMELC 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593   93 TGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAIEVEGEQQAWfG 172
Cdd:cd05117  82 TGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPDSPIKIIDFGLAKIFEEGEKLK-T 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593  173 FAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINKML 252
Cdd:cd05117 161 VCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYSFDSPEWKNVSEEAKDLIKRLL 240
                       250
                ....*....|....*...
gi 6978593  253 TINPSKRITAAEALKHPW 270
Cdd:cd05117 241 VVDPKKRLTAAEALNHPW 258
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
9-302 2.18e-103

Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CASK belongs to the MAGUK (membrane-associated guanylate kinase) protein family, which functions as multiple domain adaptor proteins and is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The enzymatically inactive GuK domain in MAGUK proteins mediates protein-protein interactions and associates intramolecularly with the SH3 domain. In addition, CASK contains a catalytic kinase and two L27 domains. It is highly expressed in the nervous system and plays roles in synaptic protein targeting, neural development, and regulation of gene expression. Binding partners include parkin (a Parkinson's disease molecule), neurexin (adhesion molecule), syndecans, calcium channel proteins, CINAP (nucleosome assembly protein), transcription factor Tbr-1, and the cytoplasmic adaptor proteins Mint1, Veli/mLIN-7/MALS, SAP97, caskin, and CIP98. Deletion or mutations in the CASK gene have been implicated in X-linked mental retardation. The CASK 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: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 313.71  E-value: 2.18e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593    9 FTEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSAR---DHQKLEREARICRLLKHPNIVRLHDSISEEGHH 85
Cdd:cd14094   1 FEDVYELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDVAKFTSSpglSTEDLKREASICHMLKHPHIVELLETYSSDGML 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593   86 YLIFDLVTGGELFEDIVARE----YYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAI 161
Cdd:cd14094  81 YMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593  162 EVEGEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQhRLYQQIKAGAYDFPSPEWDTVT 241
Cdd:cd14094 161 QLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIKGKYKMNPRQWSHIS 239
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6978593  242 PEAKDLINKMLTINPSKRITAAEALKHPWISHRSTVASCMHRQETVDCLKKFNARRKLKGA 302
Cdd:cd14094 240 ESAKDLVRRMLMLDPAERITVYEALNHPWIKERDRYAYRIHLPETVEQLRKFNARRKLKGA 300
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
10-270 5.47e-100

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: 303.52  E-value: 5.47e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593   10 TEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDhQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIF 89
Cdd:cd14083   2 RDKYEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDKKALKGKE-DSLENEIAVLRKIKHPNIVQLLDIYESKSHLYLVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593   90 DLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAievEGEQQA 169
Cdd:cd14083  81 ELVTGGELFDRIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYYSPDEDSKIMISDFGLS---KMEDSG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593  170 WFGFA-GTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLI 248
Cdd:cd14083 158 VMSTAcGTPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPFYDENDSKLFAQILKAEYEFDSPYWDDISDSAKDFI 237
                       250       260
                ....*....|....*....|..
gi 6978593  249 NKMLTINPSKRITAAEALKHPW 270
Cdd:cd14083 238 RHLMEKDPNKRYTCEQALEHPW 259
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
13-270 1.39e-99

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: 302.13  E-value: 1.39e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593   13 YQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLV 92
Cdd:cd14003   2 YELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEIEEKIKREIEIMKLLNHPNIIKLYEVIETENKIYLVMEYA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593   93 TGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLAIEVEGEQQAwFG 172
Cdd:cd14003  82 SGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGN---LKIIDFGLSNEFRGGSLL-KT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593  173 FAGTPGYLSPEVLRKDPY-GKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSpewdTVTPEAKDLINKM 251
Cdd:cd14003 158 FCGTPAYAAPEVLLGRKYdGPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKYPIPS----HLSPDARDLIRRM 233
                       250
                ....*....|....*....
gi 6978593  252 LTINPSKRITAAEALKHPW 270
Cdd:cd14003 234 LVVDPSKRITIEEILNHPW 252
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
12-270 2.66e-92

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: 283.45  E-value: 2.66e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593   12 EYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQkLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDL 91
Cdd:cd14095   1 KYDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAKCKGKEHM-IENEVAILRRVKHPNIVQLIEEYDTDTELYLVMEL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593   92 VTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLA-SKLKGAAVKLADFGLAIEVEGeqqAW 170
Cdd:cd14095  80 VKGGDLFDAITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVeHEDGSKSLKLADFGLATEVKE---PL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593  171 FGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFW--DEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLI 248
Cdd:cd14095 157 FTVCGTPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFRspDRDQEELFDLILAGEFEFLSPYWDNISDSAKDLI 236
                       250       260
                ....*....|....*....|..
gi 6978593  249 NKMLTINPSKRITAAEALKHPW 270
Cdd:cd14095 237 SRMLVVDPEKRYSAGQVLDHPW 258
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
9-307 4.52e-89

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: 276.32  E-value: 4.52e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593    9 FTEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIIntKKLSarDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLI 88
Cdd:cd14085   1 LEDFFEIESELGRGATSVVYRCRQKGTQKPYAVKKL--KKTV--DKKIVRTEIGVLLRLSHPNIIKLKEIFETPTEISLV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593   89 FDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAIEVEgEQQ 168
Cdd:cd14085  77 LELVTGGELFDRIVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPDAPLKIADFGLSKIVD-QQV 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593  169 AWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDE--DQHrLYQQIKAGAYDFPSPEWDTVTPEAKD 246
Cdd:cd14085 156 TMKTVCGTPGYCAPEILRGCAYGPEVDMWSVGVITYILLCGFEPFYDErgDQY-MFKRILNCDYDFVSPWWDDVSLNAKD 234
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6978593  247 LINKMLTINPSKRITAAEALKHPWISHRStvASCMHRQETVDCLKKFNARRKLKGAILTTM 307
Cdd:cd14085 235 LVKKLIVLDPKKRLTTQQALQHPWVTGKA--ANFAHMDTAQKKLQEFNARRKLKAAVKAVV 293
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
9-270 2.93e-88

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). Each subunit has tissue-specific isoforms or splice variants. Vertebrates contain two isoforms of the gamma subunit (gamma 1 and gamma 2). The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG 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: 270995 [Multi-domain]  Cd Length: 272  Bit Score: 273.46  E-value: 2.93e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593    9 FTEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKII--NTKKLSA----RDHQKLEREARICRLL-KHPNIVRLHDSISE 81
Cdd:cd14093   1 FYAKYEPKEILGRGVSSTVRRCIEKETGQEFAVKIIdiTGEKSSEneaeELREATRREIEILRQVsGHPNIIELHDVFES 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593   82 EGHHYLIFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKgaaVKLADFGLAI 161
Cdd:cd14093  81 PTFIFLVFELCRKGELFDYLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLN---VKISDFGFAT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593  162 EVEgEQQAWFGFAGTPGYLSPEVLR------KDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSP 235
Cdd:cd14093 158 RLD-EGEKLRELCGTPGYLAPEVLKcsmydnAPGYGKEVDMWACGVIMYTLLAGCPPFWHRKQMVMLRNIMEGKYEFGSP 236
                       250       260       270
                ....*....|....*....|....*....|....*
gi 6978593  236 EWDTVTPEAKDLINKMLTINPSKRITAAEALKHPW 270
Cdd:cd14093 237 EWDDISDTAKDLISKLLVVDPKKRLTAEEALEHPF 271
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
11-271 8.67e-88

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


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 273.02  E-value: 8.67e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593   11 EEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIIntKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFD 90
Cdd:cd14166   3 ETFIFMEVLGSGAFSEVYLVKQRSTGKLYALKCI--KKSPLSRDSSLENEIAVLKRIKHENIVTLEDIYESTTHYYLVMQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593   91 LVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAievEGEQQAW 170
Cdd:cd14166  81 LVSGGELFDRILERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYLTPDENSKIMITDFGLS---KMEQNGI 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593  171 FGFA-GTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLIN 249
Cdd:cd14166 158 MSTAcGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFYEETESRLFEKIKEGYYEFESPFWDDISESAKDFIR 237
                       250       260
                ....*....|....*....|..
gi 6978593  250 KMLTINPSKRITAAEALKHPWI 271
Cdd:cd14166 238 HLLEKNPSKRYTCEKALSHPWI 259
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
11-272 4.78e-85

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


Pssm-ID: 271069 [Multi-domain]  Cd Length: 263  Bit Score: 264.97  E-value: 4.78e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978593   11 EEYQLFEELGKGAFSVV-----RRCVKVLAGQEYAAKIINTKKLSardhqkLEREARICRLLKHPNIVRLHDSISEEGHH 85
Cdd:cd14167   3 DIYDFREVLGTGAFSEVvlaeeKRTQKLVAIKCIAKKALEGKETS------IENEIAVLHKIKHPNIVA