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Conserved domains on  [gi|4322296|gb|AAD16002|]
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cAMP-dependent protein kinase catalytic subunit isoform 1 [Amblyomma americanum]

Protein Classification

STKc_PKA domain-containing protein (domain architecture ID 10197742)

STKc_PKA domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
62-351 0e+00

Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. The PKA 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: 271111 [Multi-domain]  Cd Length: 290  Bit Score: 639.84  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296   62 DDFDRIKTLGTGSFGRVMLVQHKQHKDYFAMKILDKQKVVKLKQVEHTLNEKRILQAVEFPFLVKLAYHFKDNSNLYMVL 141
Cdd:cd14209   1 DDFDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDKQKVVKLKQVEHTLNEKRILQAINFPFLVKLEYSFKDNSNLYMVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296  142 EYVLGGEMFSHLRKSGRFSEPHARFYGAQIVLAFQYLHSLDLIYRDLKPENLLIDHTGYIKVTDFGFAKRVRGRTWTLCG 221
Cdd:cd14209  81 EYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKRVKGRTWTLCG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296  222 TPEYLAPEIILSKGYNKAVDWWALGVLVYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFTSDLKDLLRNLLQVDLTKR 301
Cdd:cd14209 161 TPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKR 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 4322296  302 FGNLKNGVNDIKNHRWFATTDWIAIYKKEVEAPFVPKCKGPGDTSNFDEY 351
Cdd:cd14209 241 FGNLKNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKLKGPGDTSNFDDY 290
 
Name Accession Description Interval E-value
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
62-351 0e+00

Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. The PKA 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: 271111 [Multi-domain]  Cd Length: 290  Bit Score: 639.84  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296   62 DDFDRIKTLGTGSFGRVMLVQHKQHKDYFAMKILDKQKVVKLKQVEHTLNEKRILQAVEFPFLVKLAYHFKDNSNLYMVL 141
Cdd:cd14209   1 DDFDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDKQKVVKLKQVEHTLNEKRILQAINFPFLVKLEYSFKDNSNLYMVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296  142 EYVLGGEMFSHLRKSGRFSEPHARFYGAQIVLAFQYLHSLDLIYRDLKPENLLIDHTGYIKVTDFGFAKRVRGRTWTLCG 221
Cdd:cd14209  81 EYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKRVKGRTWTLCG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296  222 TPEYLAPEIILSKGYNKAVDWWALGVLVYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFTSDLKDLLRNLLQVDLTKR 301
Cdd:cd14209 161 TPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKR 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 4322296  302 FGNLKNGVNDIKNHRWFATTDWIAIYKKEVEAPFVPKCKGPGDTSNFDEY 351
Cdd:cd14209 241 FGNLKNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKLKGPGDTSNFDDY 290
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
48-371 3.33e-151

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 429.24  E-value: 3.33e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296    48 EQKWTSPSSNTASLDDFDRIKTLGTGSFGRVMLVQHKQHKDYFAMKILDKQKVVKLKQVEHTLNEKRILQAVEFPFLVKL 127
Cdd:PTZ00263   4 AYMFTKPDTSSWKLSDFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSILMELSHPFIVNM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296   128 AYHFKDNSNLYMVLEYVLGGEMFSHLRKSGRFSEPHARFYGAQIVLAFQYLHSLDLIYRDLKPENLLIDHTGYIKVTDFG 207
Cdd:PTZ00263  84 MCSFQDENRVYFLLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296   208 FAKRVRGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLVYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFTSDLK 287
Cdd:PTZ00263 164 FAKKVPDRTFTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNWFDGRAR 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296   288 DLLRNLLQVDLTKRFGNLKNGVNDIKNHRWFATTDWIAIYKKEVEAPFVPKCKGPGDTSNFDEYEEEALRISS--TEKCA 365
Cdd:PTZ00263 244 DLVKGLLQTDHTKRLGTLKGGVADVKNHPYFHGANWDKLYARYYPAPIPVRVKSPGDTSNFEKYPDSPVDRLPplTAAQQ 323

                 ....*.
gi 4322296   366 REFAEF 371
Cdd:PTZ00263 324 AEFAGF 329
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
64-318 6.78e-109

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 318.71  E-value: 6.78e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296      64 FDRIKTLGTGSFGRVMLVQHKQHKDYFAMKILDKQKvvKLKQVEHTLNEKRILQAVEFPFLVKLAYHFKDNSNLYMVLEY 143
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKK--IKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296     144 VLGGEMFSHLRKSGRFSEPHARFYGAQIVLAFQYLHSLDLIYRDLKPENLLIDHTGYIKVTDFGFAKRVR--GRTWTLCG 221
Cdd:smart00220  79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDpgEKLTTFVG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296     222 TPEYLAPEIILSKGYNKAVDWWALGVLVYEMAAGYPPFFAD-QPIQIYEKIVSGKVRFPSH---FTSDLKDLLRNLLQVD 297
Cdd:smart00220 159 TPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDdQLLELFKKIGKPKPPFPPPewdISPEAKDLIRKLLVKD 238
                          250       260
                   ....*....|....*....|.
gi 4322296     298 LTKRFgnlknGVNDIKNHRWF 318
Cdd:smart00220 239 PEKRL-----TAEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
64-318 1.86e-91

Protein kinase domain;


Pssm-ID: 333812 [Multi-domain]  Cd Length: 259  Bit Score: 274.88  E-value: 1.86e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296     64 FDRIKTLGTGSFGRVMLVQHKQHKDYFAMKILDKQKVVKLKQvEHTLNEKRILQAVEFPFLVKLAYHFKDNSNLYMVLEY 143
Cdd:pfam00069   1 YEVLEKLGEGSFGTVYKAKHKDTGKIVAIKKIKKEKIKKKKE-KNVLREIKILKKLSHPNIVRLYDVFEDKDHLYLVLEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296    144 VLGGEMFSHLRKSGRFSEPHARFYGAQIVLAFQYLHSLDLIYRDLKPENLLIDHTGYIKVTDFGFAKRVR--GRTWTLCG 221
Cdd:pfam00069  80 VEGGSLFDLLSEKGVFSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENILIDEDGNLKITDFGLAKQLSsgSKLTTFVG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296    222 TPEYLAPEIILSKGYNKAVDWWALGVLVYEMAAGYPPFFADQPIQIYEKIVSG--------KVRFPSHFTSDLKDLLRNL 293
Cdd:pfam00069 160 TPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGDDIYELILDQleripedfSSPFPSSLSEEAKDLLKKL 239
                         250       260
                  ....*....|....*....|....*
gi 4322296    294 LQVDLTKRFgnlknGVNDIKNHRWF 318
Cdd:pfam00069 240 LKKDPSKRL-----TATQALQHPWF 259
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
63-324 6.83e-54

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 182.25  E-value: 6.83e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296   63 DFDRIKTLGTGSFGRVMLVQHKQhkdYFAMKILDKQKVVKLKQVEHTLNEKRILQAV-EFPFLVKLAYHFKDNSNLYMVL 141
Cdd:COG0515   1 SYRILRKLGEGSFGEVYLARDRK---LVALKVLAKKLESKSKEVERFLREIQILASLnHPPNIVKLYDFFQDEGSLYLVM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296  142 EYVLGGEMFSHLRKSGR---FSEPHARFYGAQIVLAFQYLHSLDLIYRDLKPENLLIDHTGY-IKVTDFGFAKRVRGRTW 217
Cdd:COG0515  78 EYVDGGSLEDLLKKIGRkgpLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRvVKLIDFGLAKLLPDPGS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296  218 ---------TLCGTPEYLAPEIILSKG---YNKAVDWWALGVLVYEMAAGYPPFFADQPI----QIYEKIVSGKV----- 276
Cdd:COG0515 158 tssipalpsTSVGTPGYMAPEVLLGLSlayASSSSDIWSLGITLYELLTGLPPFEGEKNSsatsQTLKIILELPTpslas 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 4322296  277 ----RFPSHFTSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHRWFATTDWI 324
Cdd:COG0515 238 plspSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKESDLS 289
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
137-301 3.81e-09

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: 58.32  E-value: 3.81e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296     137 LYMVLEYVLGGEMFSHLRKSGRFSEPHARFYGAQIVLAFQYLHSLDLIYRDLKPENLLIDHTG---YIKVTDFGFAKRVR 213
Cdd:TIGR03903   54 LFAVFEYVPGRTLREVLAADGALPAGETGRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGvrpHAKVLDFGIGTLLP 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296     214 G----------RTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLVYEMAAGYPPFFADQPIQIYEKIVSG-KVRFPSHF 282
Cdd:TIGR03903  134 GvrdadvatltRTTEVLGTPTYCAPEQLRGEPVTPNSDLYAWGLIFLECLTGQRVVQGASVAEILYQQLSPvDVSLPPWI 213
                          170       180
                   ....*....|....*....|
gi 4322296     283 TS-DLKDLLRNLLQVDLTKR 301
Cdd:TIGR03903  214 AGhPLGQVLRKALNKDPRQR 233
 
Name Accession Description Interval E-value
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
62-351 0e+00

Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. The PKA 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: 271111 [Multi-domain]  Cd Length: 290  Bit Score: 639.84  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296   62 DDFDRIKTLGTGSFGRVMLVQHKQHKDYFAMKILDKQKVVKLKQVEHTLNEKRILQAVEFPFLVKLAYHFKDNSNLYMVL 141
Cdd:cd14209   1 DDFDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDKQKVVKLKQVEHTLNEKRILQAINFPFLVKLEYSFKDNSNLYMVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296  142 EYVLGGEMFSHLRKSGRFSEPHARFYGAQIVLAFQYLHSLDLIYRDLKPENLLIDHTGYIKVTDFGFAKRVRGRTWTLCG 221
Cdd:cd14209  81 EYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKRVKGRTWTLCG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296  222 TPEYLAPEIILSKGYNKAVDWWALGVLVYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFTSDLKDLLRNLLQVDLTKR 301
Cdd:cd14209 161 TPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKR 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 4322296  302 FGNLKNGVNDIKNHRWFATTDWIAIYKKEVEAPFVPKCKGPGDTSNFDEY 351
Cdd:cd14209 241 FGNLKNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKLKGPGDTSNFDDY 290
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
62-351 0e+00

Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the cAMP-dependent protein kinases, PKA and PRKX, and similar proteins. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. PRKX is also reulated by the R subunit and is is present in many tissues including fetal and adult brain, kidney, and lung. It is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PKA-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: 270732 [Multi-domain]  Cd Length: 290  Bit Score: 529.07  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296   62 DDFDRIKTLGTGSFGRVMLVQHKQHKDYFAMKILDKQKVVKLKQVEHTLNEKRILQAVEFPFLVKLAYHFKDNSNLYMVL 141
Cdd:cd05580   1 DDFEFLKTLGTGSFGRVRLVKHKDSGKYYALKILKKAKIIKLKQVEHVLNEKRILSEVRHPFIVNLLGSFQDDRNLYMVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296  142 EYVLGGEMFSHLRKSGRFSEPHARFYGAQIVLAFQYLHSLDLIYRDLKPENLLIDHTGYIKVTDFGFAKRVRGRTWTLCG 221
Cdd:cd05580  81 EYVPGGELFSLLRRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFAKRVKDRTYTLCG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296  222 TPEYLAPEIILSKGYNKAVDWWALGVLVYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFTSDLKDLLRNLLQVDLTKR 301
Cdd:cd05580 161 TPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKILEGKIRFPSFFDPDAKDLIKRLLVVDLTKR 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 4322296  302 FGNLKNGVNDIKNHRWFATTDWIAIYKKEVEAPFVPKCKGPGDTSNFDEY 351
Cdd:cd05580 241 LGNLKNGVEDIKNHPWFAGIDWDALLQRKIPAPYVPKVRGPGDTSNFDKY 290
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
62-353 3.49e-156

Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include human PRKX (X chromosome-encoded protein kinase), Drosophila DC2, and similar proteins. PRKX is present in many tissues including fetal and adult brain, kidney, and lung. The PRKX gene is located in the Xp22.3 subregion and has a homolog called PRKY on the Y chromosome. An abnormal interchange between PRKX aand PRKY leads to the sex reversal disorder of XX males and XY females. PRKX is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PRKX-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: 270763 [Multi-domain]  Cd Length: 292  Bit Score: 440.33  E-value: 3.49e-156
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296   62 DDFDRIKTLGTGSFGRVMLVQHKQHKDYFAMKILDKQKVVKLKQVEHTLNEKRILQAVEFPFLVKLAYHFKDNSNLYMVL 141
Cdd:cd05612   1 DDFERIKTIGTGTFGRVHLVRDRISEHYYALKVMAIPEVIRLKQEQHVHNEKRVLKEVSHPFIIRLFWTEHDQRFLYMLM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296  142 EYVLGGEMFSHLRKSGRFSEPHARFYGAQIVLAFQYLHSLDLIYRDLKPENLLIDHTGYIKVTDFGFAKRVRGRTWTLCG 221
Cdd:cd05612  81 EYVPGGELFSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAKKLRDRTWTLCG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296  222 TPEYLAPEIILSKGYNKAVDWWALGVLVYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFTSDLKDLLRNLLQVDLTKR 301
Cdd:cd05612 161 TPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFDDNPFGIYEKILAGKLEFPRHLDLYAKDLIKKLLVVDRTRR 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 4322296  302 FGNLKNGVNDIKNHRWFATTDWIAIYKKEVEAPFVPKCKGPGDTSNFDEYEE 353
Cdd:cd05612 241 LGNMKNGADDVKNHRWFKSVDWDDVPQRKLKPPIVPKVSHDGDTSNFDDYPE 292
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
48-371 3.33e-151

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 429.24  E-value: 3.33e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296    48 EQKWTSPSSNTASLDDFDRIKTLGTGSFGRVMLVQHKQHKDYFAMKILDKQKVVKLKQVEHTLNEKRILQAVEFPFLVKL 127
Cdd:PTZ00263   4 AYMFTKPDTSSWKLSDFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSILMELSHPFIVNM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296   128 AYHFKDNSNLYMVLEYVLGGEMFSHLRKSGRFSEPHARFYGAQIVLAFQYLHSLDLIYRDLKPENLLIDHTGYIKVTDFG 207
Cdd:PTZ00263  84 MCSFQDENRVYFLLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296   208 FAKRVRGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLVYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFTSDLK 287
Cdd:PTZ00263 164 FAKKVPDRTFTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNWFDGRAR 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296   288 DLLRNLLQVDLTKRFGNLKNGVNDIKNHRWFATTDWIAIYKKEVEAPFVPKCKGPGDTSNFDEYEEEALRISS--TEKCA 365
Cdd:PTZ00263 244 DLVKGLLQTDHTKRLGTLKGGVADVKNHPYFHGANWDKLYARYYPAPIPVRVKSPGDTSNFEKYPDSPVDRLPplTAAQQ 323

                 ....*.
gi 4322296   366 REFAEF 371
Cdd:PTZ00263 324 AEFAGF 329
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
70-318 3.06e-142

Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases. Members of this family include cAMP-dependent Protein Kinase (PKA), cGMP-dependent Protein Kinase (PKG), Protein Kinase C (PKC), Protein Kinase B (PKB), G protein-coupled Receptor Kinase (GRK), Serum- and Glucocorticoid-induced Kinase (SGK), and 70 kDa ribosomal Protein S6 Kinase (p70S6K or S6K), among others. AGC kinases share an activation mechanism based on the phosphorylation of up to three sites: the activation loop (A-loop), the hydrophobic motif (HM) and the turn motif. Phosphorylation at the A-loop is required of most AGC kinases, which results in a disorder-to-order transition of the A-loop. The ordered conformation results in the access of substrates and ATP to the active site. A subset of AGC kinases with C-terminal extensions containing the HM also requires phosphorylation at this site. Phosphorylation at the HM allows the C-terminal extension to form an ordered structure that packs into the hydrophobic pocket of the catalytic domain, which then reconfigures the kinase into an active bi-lobed state. In addition, growth factor-activated AGC kinases such as PKB, p70S6K, RSK, MSK, PKC, and SGK, require phosphorylation at the turn motif (also called tail or zipper site), located N-terminal to the HM at the C-terminal extension. The AGC family 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: 270693 [Multi-domain]  Cd Length: 250  Bit Score: 403.44  E-value: 3.06e-142
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296   70 LGTGSFGRVMLVQHKQHKDYFAMKILDKQKVVKLKQVEHTLNEKRILQAVEFPFLVKLAYHFKDNSNLYMVLEYVLGGEM 149
Cdd:cd05123   1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEIIKRKEVEHTLNERNILERVNHPFIVKLHYAFQTEEKLYLVLDYVPGGEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296  150 FSHLRKSGRFSEPHARFYGAQIVLAFQYLHSLDLIYRDLKPENLLIDHTGYIKVTDFGFAKRV---RGRTWTLCGTPEYL 226
Cdd:cd05123  81 FSHLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKELssdGDRTYTFCGTPEYL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296  227 APEIILSKGYNKAVDWWALGVLVYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFTSDLKDLLRNLLQVDLTKRFGNLk 306
Cdd:cd05123 161 APEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKILKSPLKFPEYVSPEAKSLISGLLQKDPTKRLGSG- 239
                       250
                ....*....|..
gi 4322296  307 nGVNDIKNHRWF 318
Cdd:cd05123 240 -GAEEIKAHPFF 250
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
70-323 7.32e-119

Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mammals have two cGK isoforms from different genes, cGKI and cGKII. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. cGK consists of an N-terminal regulatory domain containing a dimerization and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is also expressed at lower concentrations in other tissues. cGKII is a membrane-bound protein that is most abundantly expressed in the intestine. It is also present in the brain nuclei, adrenal cortex, kidney, lung, and prostate. cGKI is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. cGKII plays a role in the regulation of secretion, such as renin secretion by the kidney and aldosterone secretion by the adrenal. It also regulates bone growth and the circadian rhythm. The cGK 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: 270724 [Multi-domain]  Cd Length: 262  Bit Score: 344.59  E-value: 7.32e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296   70 LGTGSFGRVMLVQHKQHKDYFAMKILDKQKVVKLKQVEHTLNEKRILQAVEFPFLVKLAYHFKDNSNLYMVLEYVLGGEM 149
Cdd:cd05572   1 LGVGGFGRVELVQLKSKGRTFALKCVKKRHIVQTRQQEHIFSEKEILEECNSPFIVKLYRTFKDKKYLYMLMEYCLGGEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296  150 FSHLRKSGRFSEPHARFYGAQIVLAFQYLHSLDLIYRDLKPENLLIDHTGYIKVTDFGFAKRV--RGRTWTLCGTPEYLA 227
Cdd:cd05572  81 WTILRDRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAKKLgsGRKTWTFCGTPEYVA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296  228 PEIILSKGYNKAVDWWALGVLVYEMAAGYPPFFADQ--PIQIYEKIVSG--KVRFPSHFTSDLKDLLRNLLQVDLTKRFG 303
Cdd:cd05572 161 PEIILNKGYDFSVDYWSLGILLYELLTGRPPFGGDDedPMKIYNIILKGidKIEFPKYIDKNAKNLIKQLLRRNPEERLG 240
                       250       260
                ....*....|....*....|
gi 4322296  304 NLKNGVNDIKNHRWFATTDW 323
Cdd:cd05572 241 YLKGGIRDIKKHKWFEGFDW 260
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
68-371 1.66e-117

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, classical PKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. Novel PKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. Also included in this subfamily are the PKC-like proteins, called PKNs. The PKC 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: 270722 [Multi-domain]  Cd Length: 318  Bit Score: 343.04  E-value: 1.66e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296   68 KTLGTGSFGRVMLVQHKQHKDYFAMKILDKQKVVKLKQVEHTLNEKRIL-QAVEFPFLVKLAYHFKDNSNLYMVLEYVLG 146
Cdd:cd05570   1 KVLGKGSFGKVMLAERKKTDELYAIKVLKKEVIIEDDDVECTMTEKRVLaLANRHPFLTGLHACFQTEDRLYFVMEYVNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296  147 GEMFSHLRKSGRFSEPHARFYGAQIVLAFQYLHSLDLIYRDLKPENLLIDHTGYIKVTDFGFAK---RVRGRTWTLCGTP 223
Cdd:cd05570  81 GDLMFHIQRARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMCKegiWGGNTTSTFCGTP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296  224 EYLAPEIILSKGYNKAVDWWALGVLVYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFTSDLKDLLRNLLQVDLTKRFG 303
Cdd:cd05570 161 DYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFEGDDEDELFEAILNDEVLYPRWLSREAVSILKGLLTKDPARRLG 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4322296  304 NLKNGVNDIKNHRWFATTDWIAIYKKEVEAPFVPKCKGPGDTSNFD-EYEEEALRISSTEKCAR------EFAEF 371
Cdd:cd05570 241 CGPKGEADIKAHPFFRNIDWDKLEKKEVEPPFKPKVKSPRDTSNFDpEFTSESPRLTPVDSDLLtnidqeEFRGF 315
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
68-363 7.25e-114

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. There are three PKB isoforms from different genes, PKB-alpha (or Akt1), PKB-beta (or Akt2), and PKB-gamma (or Akt3). PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. It is activated downstream of phosphoinositide 3-kinase (PI3K) and plays important roles in diverse cellular functions including cell survival, growth, proliferation, angiogenesis, motility, and migration. PKB also has a central role in a variety of human cancers, having been implicated in tumor initiation, progression, and metastasis. The PKB 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 PI3K.


Pssm-ID: 270723 [Multi-domain]  Cd Length: 322  Bit Score: 333.94  E-value: 7.25e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296   68 KTLGTGSFGRVMLVQHKQHKDYFAMKILDKQKVVKLKQVEHTLNEKRILQAVEFPFLVKLAYHFKDNSNLYMVLEYVLGG 147
Cdd:cd05571   1 KVLGKGTFGKVILCREKATGELYAIKILKKEVIIAKDEVAHTLTENRVLQNTRHPFLTSLKYSFQTNDRLCFVMEYVNGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296  148 EMFSHLRKSGRFSEPHARFYGAQIVLAFQYLHSLDLIYRDLKPENLLIDHTGYIKVTDFGFAK---RVRGRTWTLCGTPE 224
Cdd:cd05571  81 ELFFHLSRERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLCKeeiSYGATTKTFCGTPE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296  225 YLAPEIILSKGYNKAVDWWALGVLVYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFTSDLKDLLRNLLQVDLTKRFGN 304
Cdd:cd05571 161 YLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNRDHEVLFELILMEEVRFPSTLSPEAKSLLAGLLKKDPKKRLGG 240
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296  305 LKNGVNDIKNHRWFATTDWIAIYKKEVEAPFVPKCKGPGDTSNFD-EYEEEALRISSTEK 363
Cdd:cd05571 241 GPRDAKEIMEHPFFASINWDDLYQKKIPPPFKPQVTSETDTRYFDeEFTAESVELTPPDR 300
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
68-355 1.15e-112

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGKs are activated by insulin and growth factors via phosphoinositide 3-kinase and PDK1. They activate ion channels, ion carriers, and the Na-K-ATPase, as well as regulate the activity of enzymes and transcription factors. SGKs play important roles in transport, hormone release, neuroexcitability, cell proliferation, and apoptosis. There are three isoforms of SGK, named SGK1, SGK2, and SGK3 (also called cytokine-independent survival kinase CISK). The SGK 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: 270727 [Multi-domain]  Cd Length: 323  Bit Score: 331.20  E-value: 1.15e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296   68 KTLGTGSFGRVMLVQHKQHKDYFAMKILDKQKVVKLKQVEHTLNEKRIL-QAVEFPFLVKLAYHFKDNSNLYMVLEYVLG 146
Cdd:cd05575   1 KVIGKGSFGKVLLARHKAEGKLYAVKVLQKKAILKRNEVKHIMAERNVLlKNVKHPFLVGLHYSFQTKDKLYFVLDYVNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296  147 GEMFSHLRKSGRFSEPHARFYGAQIVLAFQYLHSLDLIYRDLKPENLLIDHTGYIKVTDFGFAK---RVRGRTWTLCGTP 223
Cdd:cd05575  81 GELFFHLQRERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLCKegiEPSDTTSTFCGTP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296  224 EYLAPEIILSKGYNKAVDWWALGVLVYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFTSDLKDLLRNLLQVDLTKRFG 303
Cdd:cd05575 161 EYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRDTAEMYDNILHKPLRLRTNVSPSARDLLEGLLQKDRTKRLG 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 4322296  304 NlKNGVNDIKNHRWFATTDWIAIYKKEVEAPFVPKCKGPGDTSNFD-EYEEEA 355
Cdd:cd05575 241 S-GNDFLEIKNHSFFRPINWDDLEAKKIPPPFNPNVSGPLDLRNIDpEFTREP 292
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
57-354 5.32e-111

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 327.71  E-value: 5.32e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296    57 NTASLDDFDRIKTLGTGSFGRVMLVQHKqHKDY--FAMKILDKQKVVKLKQVEHTLNEKRILQAVEFPFLVKLAYHFKDN 134
Cdd:PTZ00426  25 NKMKYEDFNFIRTLGTGSFGRVILATYK-NEDFppVAIKRFEKSKIIKQKQVDHVFSERKILNYINHPFCVNLYGSFKDE 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296   135 SNLYMVLEYVLGGEMFSHLRKSGRFSEPHARFYGAQIVLAFQYLHSLDLIYRDLKPENLLIDHTGYIKVTDFGFAKRVRG 214
Cdd:PTZ00426 104 SYLYLVLEFVIGGEFFTFLRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTDFGFAKVVDT 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296   215 RTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLVYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFTSDLKDLLRNLL 294
Cdd:PTZ00426 184 RTYTLCGTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPFYANEPLLIYQKILEGIIYFPKFLDNNCKHLMKKLL 263
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296   295 QVDLTKRFGNLKNGVNDIKNHRWFATTDWIAIYKKEVEAPFVPKCKGPGDTSNFDEYEEE 354
Cdd:PTZ00426 264 SHDLTKRYGNLKKGAQNVKEHPWFGNIDWVSLLHKNVEVPYKPKYKNVFDSSNFERVQED 323
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
64-318 6.78e-109

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 318.71  E-value: 6.78e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296      64 FDRIKTLGTGSFGRVMLVQHKQHKDYFAMKILDKQKvvKLKQVEHTLNEKRILQAVEFPFLVKLAYHFKDNSNLYMVLEY 143
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKK--IKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296     144 VLGGEMFSHLRKSGRFSEPHARFYGAQIVLAFQYLHSLDLIYRDLKPENLLIDHTGYIKVTDFGFAKRVR--GRTWTLCG 221
Cdd:smart00220  79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDpgEKLTTFVG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296     222 TPEYLAPEIILSKGYNKAVDWWALGVLVYEMAAGYPPFFAD-QPIQIYEKIVSGKVRFPSH---FTSDLKDLLRNLLQVD 297
Cdd:smart00220 159 TPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDdQLLELFKKIGKPKPPFPPPewdISPEAKDLIRKLLVKD 238
                          250       260
                   ....*....|....*....|.
gi 4322296     298 LTKRFgnlknGVNDIKNHRWF 318
Cdd:smart00220 239 PEKRL-----TAEEALQHPFF 254
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
62-363 2.13e-105

Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR kinases regulate mitosis, cell growth, embryonic development, and neurological processes. They are also required for proper centrosome duplication. Higher eukaryotes contain two NDR isoforms, NDR1 and NDR2. This subfamily also contains fungal NDR-like kinases. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR kinase 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: 270750 [Multi-domain]  Cd Length: 324  Bit Score: 312.63  E-value: 2.13e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296   62 DDFDRIKTLGTGSFGRVMLVQHKQHKDYFAMKILDKQKVVKLKQVEHTLNEKRILQAVEFPFLVKLAYHFKDNSNLYMVL 141
Cdd:cd05599   1 EDFEPLKVIGRGAFGEVRLVRKKDTGHVYAMKKLRKSEMLEKEQVAHVRAERDILAEADNPWVVKLYYSFQDEENLYLIM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296  142 EYVLGGEMFSHLRKSGRFSEPHARFYGAQIVLAFQYLHSLDLIYRDLKPENLLIDHTGYIKVTDFGFAK--RVRGRTWTL 219
Cdd:cd05599  81 EFLPGGDMMTLLMKKDTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARGHIKLSDFGLCTglKKSHLAYST 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296  220 CGTPEYLAPEIILSKGYNKAVDWWALGVLVYEMAAGYPPFFADQPIQIYEKIVSGK--VRFPS--HFTSDLKDLLRNLLq 295
Cdd:cd05599 161 VGTPDYIAPEVFLQKGYGKECDWWSLGVIMYEMLIGYPPFCSDDPQETCRKIMNWRetLVFPPevPISPEAKDLIERLL- 239
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4322296  296 VDLTKRFGNlkNGVNDIKNHRWFATTDWIAIYkkEVEAPFVPKCKGPGDTSNFDEYEEEALRISSTEK 363
Cdd:cd05599 240 CDAEHRLGA--NGVEEIKSHPFFKGVDWDHIR--ERPAPILPEVKSILDTSNFDEFEEVDLQIPSSPE 303
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
67-349 8.56e-105

Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p70S6K (or S6K) contains only one catalytic kinase domain, unlike p90 ribosomal S6 kinases (RSKs). It acts as a downstream effector of the STK mTOR (mammalian Target of Rapamycin) and plays a role in the regulation of the translation machinery during protein synthesis. p70S6K also plays a pivotal role in regulating cell size and glucose homeostasis. Its targets include S6, the translation initiation factor eIF3, and the insulin receptor substrate IRS-1, among others. Mammals contain two isoforms of p70S6K, named S6K1 and S6K2 (or S6K-beta). The p70S6K 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: 270736 [Multi-domain]  Cd Length: 323  Bit Score: 311.26  E-value: 8.56e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296   67 IKTLGTGSFGRVMLVQHKQHKD---YFAMKILDKQKVVK-LKQVEHTLNEKRILQAVEFPFLVKLAYHFKDNSNLYMVLE 142
Cdd:cd05584   1 LKVLGKGGYGKVFQVRKTTGSDkgkIFAMKVLKKASIVRnQKDTAHTKAERNILEAVKHPFIVDLHYAFQTGGKLYLILE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296  143 YVLGGEMFSHLRKSGRFSEPHARFYGAQIVLAFQYLHSLDLIYRDLKPENLLIDHTGYIKVTDFGFAK-RVRG--RTWTL 219
Cdd:cd05584  81 YLSGGELFMHLEREGIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGLCKeSIHDgtVTHTF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4322296  220 CGTPEYLAPEIILSKGYNKAVDWWALGVLVYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFTSDLKDLLRNLLQVDLT 299
Cdd:cd05584 161 CGTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKILKGKLNLPPYLTNEARDLLKKLLKRNVS 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 4322296  300 KRFGNLKNGVNDIKNHRWFATTDWIAIYKKEVEAPFVPKCKGPGDTSNFD 349
Cdd:cd05584 241 SRLGSGPGDAEEIKAHPFFRHINWDDLLAKKVEPPFKPLLQSEEDVSQFD 290
STKc_ROCK_NDR_like cd05573
Cat