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Conserved domains on  [gi|22946048|gb|AAN10703|]
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protein kinase, cAMP-dependent, catalytic subunit 1, isoform B [Drosophila melanogaster]

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 ...
44-333 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: 633.29  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048  44 DDFERIKTLGTGSFGRVMIVQHKPTKDYYAMKILDKQKVVKLKQVEHTLNEKRILQAIQFPFLVSLRYHFKDNSNLYMVL 123
Cdd:cd14209   1 DDFDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDKQKVVKLKQVEHTLNEKRILQAINFPFLVKLEYSFKDNSNLYMVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048 124 EYVPGGEMFSHLRKVGRFSEPHSRFYAAQIVLAFEYLHYLDLIYRDLKPENLLIDSQGYLKVTDFGFAKRVKGRTWTLCG 203
Cdd:cd14209  81 EYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKRVKGRTWTLCG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048 204 TPEYLAPEIILSKGYNKAVDWWALGVLVYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFGSDLKDLLRNLLQVDLTKR 283
Cdd:cd14209 161 TPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKR 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 22946048 284 YGNLKAGVNDIKNQKWFASTDWIAIFQKKIEAPFIPRCKGPGDTSNFDDY 333
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 ...
44-333 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: 633.29  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048  44 DDFERIKTLGTGSFGRVMIVQHKPTKDYYAMKILDKQKVVKLKQVEHTLNEKRILQAIQFPFLVSLRYHFKDNSNLYMVL 123
Cdd:cd14209   1 DDFDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDKQKVVKLKQVEHTLNEKRILQAINFPFLVKLEYSFKDNSNLYMVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048 124 EYVPGGEMFSHLRKVGRFSEPHSRFYAAQIVLAFEYLHYLDLIYRDLKPENLLIDSQGYLKVTDFGFAKRVKGRTWTLCG 203
Cdd:cd14209  81 EYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKRVKGRTWTLCG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048 204 TPEYLAPEIILSKGYNKAVDWWALGVLVYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFGSDLKDLLRNLLQVDLTKR 283
Cdd:cd14209 161 TPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKR 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 22946048 284 YGNLKAGVNDIKNQKWFASTDWIAIFQKKIEAPFIPRCKGPGDTSNFDDY 333
Cdd:cd14209 241 FGNLKNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKLKGPGDTSNFDDY 290
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
43-353 1.62e-151

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 429.24  E-value: 1.62e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048   43 LDDFERIKTLGTGSFGRVMIVQHKPTKDYYAMKILDKQKVVKLKQVEHTLNEKRILQAIQFPFLVSLRYHFKDNSNLYMV 122
Cdd:PTZ00263  17 LSDFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048  123 LEYVPGGEMFSHLRKVGRFSEPHSRFYAAQIVLAFEYLHYLDLIYRDLKPENLLIDSQGYLKVTDFGFAKRVKGRTWTLC 202
Cdd:PTZ00263  97 LEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKVPDRTFTLC 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048  203 GTPEYLAPEIILSKGYNKAVDWWALGVLVYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFGSDLKDLLRNLLQVDLTK 282
Cdd:PTZ00263 177 GTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNWFDGRARDLVKGLLQTDHTK 256
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22946048  283 RYGNLKAGVNDIKNQKWFASTDWIAIFQKKIEAPFIPRCKGPGDTSNFDDYEEEALRISS--TEKCAKEFAEF 353
Cdd:PTZ00263 257 RLGTLKGGVADVKNHPYFHGANWDKLYARYYPAPIPVRVKSPGDTSNFEKYPDSPVDRLPplTAAQQAEFAGF 329
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
46-300 2.77e-108

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 316.78  E-value: 2.77e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048     46 FERIKTLGTGSFGRVMIVQHKPTKDYYAMKILDKQKvvKLKQVEHTLNEKRILQAIQFPFLVSLRYHFKDNSNLYMVLEY 125
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKK--IKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048    126 VPGGEMFSHLRKVGRFSEPHSRFYAAQIVLAFEYLHYLDLIYRDLKPENLLIDSQGYLKVTDFGFAKRVK--GRTWTLCG 203
Cdd:smart00220  79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDpgEKLTTFVG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048    204 TPEYLAPEIILSKGYNKAVDWWALGVLVYEMAAGYPPFFAD-QPIQIYEKIVSGKVRFPSH---FGSDLKDLLRNLLQVD 279
Cdd:smart00220 159 TPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDdQLLELFKKIGKPKPPFPPPewdISPEAKDLIRKLLVKD 238
                          250       260
                   ....*....|....*....|.
gi 22946048    280 LTKRYgnlkaGVNDIKNQKWF 300
Cdd:smart00220 239 PEKRL-----TAEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
46-300 7.07e-92

Protein kinase domain;


Pssm-ID: 333812 [Multi-domain]  Cd Length: 259  Bit Score: 275.27  E-value: 7.07e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048    46 FERIKTLGTGSFGRVMIVQHKPTKDYYAMKILDKQKVVKLKQvEHTLNEKRILQAIQFPFLVSLRYHFKDNSNLYMVLEY 125
Cdd:pfam00069   1 YEVLEKLGEGSFGTVYKAKHKDTGKIVAIKKIKKEKIKKKKE-KNVLREIKILKKLSHPNIVRLYDVFEDKDHLYLVLEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048   126 VPGGEMFSHLRKVGRFSEPHSRFYAAQIVLAFEYLHYLDLIYRDLKPENLLIDSQGYLKVTDFGFAKRVK--GRTWTLCG 203
Cdd:pfam00069  80 VEGGSLFDLLSEKGVFSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENILIDEDGNLKITDFGLAKQLSsgSKLTTFVG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048   204 TPEYLAPEIILSKGYNKAVDWWALGVLVYEMAAGYPPFFADQPIQIYEKIVSG--------KVRFPSHFGSDLKDLLRNL 275
Cdd:pfam00069 160 TPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGDDIYELILDQleripedfSSPFPSSLSEEAKDLLKKL 239
                         250       260
                  ....*....|....*....|....*
gi 22946048   276 LQVDLTKRYgnlkaGVNDIKNQKWF 300
Cdd:pfam00069 240 LKKDPSKRL-----TATQALQHPWF 259
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
45-306 2.12e-54

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 183.02  E-value: 2.12e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048  45 DFERIKTLGTGSFGRVMIVQHKPTkdyYAMKILDKQKVVKLKQVEHTLNEKRILQAIQFP-FLVSLRYHFKDNSNLYMVL 123
Cdd:COG0515   1 SYRILRKLGEGSFGEVYLARDRKL---VALKVLAKKLESKSKEVERFLREIQILASLNHPpNIVKLYDFFQDEGSLYLVM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048 124 EYVPGGEMFSHLRK---VGRFSEPHSRFYAAQIVLAFEYLHYLDLIYRDLKPENLLIDSQGY-LKVTDFGFAKRVKGRTW 199
Cdd:COG0515  78 EYVDGGSLEDLLKKigrKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRvVKLIDFGLAKLLPDPGS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048 200 ---------TLCGTPEYLAPEIILSKG---YNKAVDWWALGVLVYEMAAGYPPFFADQPI----QIYEKIVSGKV----- 258
Cdd:COG0515 158 tssipalpsTSVGTPGYMAPEVLLGLSlayASSSSDIWSLGITLYELLTGLPPFEGEKNSsatsQTLKIILELPTpslas 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 22946048 259 ----RFPSHFGSDLKDLLRNLLQVDLTKRYGNLKAGVNDIKNQKWFASTDWI 306
Cdd:COG0515 238 plspSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKESDLS 289
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
119-283 2.89e-10

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: 61.40  E-value: 2.89e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048    119 LYMVLEYVPGGEMFSHLRKVGRFSEPHSRFYAAQIVLAFEYLHYLDLIYRDLKPENLLIDSQG---YLKVTDFGFAKRVK 195
Cdd:TIGR03903   54 LFAVFEYVPGRTLREVLAADGALPAGETGRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGvrpHAKVLDFGIGTLLP 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048    196 G----------RTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLVYEMAAGYPPFFADQPIQIYEKIVSG-KVRFPSHF 264
Cdd:TIGR03903  134 GvrdadvatltRTTEVLGTPTYCAPEQLRGEPVTPNSDLYAWGLIFLECLTGQRVVQGASVAEILYQQLSPvDVSLPPWI 213
                          170       180
                   ....*....|....*....|
gi 22946048    265 -GSDLKDLLRNLLQVDLTKR 283
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 ...
44-333 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: 633.29  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048  44 DDFERIKTLGTGSFGRVMIVQHKPTKDYYAMKILDKQKVVKLKQVEHTLNEKRILQAIQFPFLVSLRYHFKDNSNLYMVL 123
Cdd:cd14209   1 DDFDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDKQKVVKLKQVEHTLNEKRILQAINFPFLVKLEYSFKDNSNLYMVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048 124 EYVPGGEMFSHLRKVGRFSEPHSRFYAAQIVLAFEYLHYLDLIYRDLKPENLLIDSQGYLKVTDFGFAKRVKGRTWTLCG 203
Cdd:cd14209  81 EYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKRVKGRTWTLCG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048 204 TPEYLAPEIILSKGYNKAVDWWALGVLVYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFGSDLKDLLRNLLQVDLTKR 283
Cdd:cd14209 161 TPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKR 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 22946048 284 YGNLKAGVNDIKNQKWFASTDWIAIFQKKIEAPFIPRCKGPGDTSNFDDY 333
Cdd:cd14209 241 FGNLKNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKLKGPGDTSNFDDY 290
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
44-333 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: 527.53  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048  44 DDFERIKTLGTGSFGRVMIVQHKPTKDYYAMKILDKQKVVKLKQVEHTLNEKRILQAIQFPFLVSLRYHFKDNSNLYMVL 123
Cdd:cd05580   1 DDFEFLKTLGTGSFGRVRLVKHKDSGKYYALKILKKAKIIKLKQVEHVLNEKRILSEVRHPFIVNLLGSFQDDRNLYMVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048 124 EYVPGGEMFSHLRKVGRFSEPHSRFYAAQIVLAFEYLHYLDLIYRDLKPENLLIDSQGYLKVTDFGFAKRVKGRTWTLCG 203
Cdd:cd05580  81 EYVPGGELFSLLRRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFAKRVKDRTYTLCG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048 204 TPEYLAPEIILSKGYNKAVDWWALGVLVYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFGSDLKDLLRNLLQVDLTKR 283
Cdd:cd05580 161 TPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKILEGKIRFPSFFDPDAKDLIKRLLVVDLTKR 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 22946048 284 YGNLKAGVNDIKNQKWFASTDWIAIFQKKIEAPFIPRCKGPGDTSNFDDY 333
Cdd:cd05580 241 LGNLKNGVEDIKNHPWFAGIDWDALLQRKIPAPYVPKVRGPGDTSNFDKY 290
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
44-335 1.11e-152

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: 430.70  E-value: 1.11e-152
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048  44 DDFERIKTLGTGSFGRVMIVQHKPTKDYYAMKILDKQKVVKLKQVEHTLNEKRILQAIQFPFLVSLRYHFKDNSNLYMVL 123
Cdd:cd05612   1 DDFERIKTIGTGTFGRVHLVRDRISEHYYALKVMAIPEVIRLKQEQHVHNEKRVLKEVSHPFIIRLFWTEHDQRFLYMLM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048 124 EYVPGGEMFSHLRKVGRFSEPHSRFYAAQIVLAFEYLHYLDLIYRDLKPENLLIDSQGYLKVTDFGFAKRVKGRTWTLCG 203
Cdd:cd05612  81 EYVPGGELFSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAKKLRDRTWTLCG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048 204 TPEYLAPEIILSKGYNKAVDWWALGVLVYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFGSDLKDLLRNLLQVDLTKR 283
Cdd:cd05612 161 TPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFDDNPFGIYEKILAGKLEFPRHLDLYAKDLIKKLLVVDRTRR 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 22946048 284 YGNLKAGVNDIKNQKWFASTDWIAIFQKKIEAPFIPRCKGPGDTSNFDDYEE 335
Cdd:cd05612 241 LGNMKNGADDVKNHRWFKSVDWDDVPQRKLKPPIVPKVSHDGDTSNFDDYPE 292
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
43-353 1.62e-151

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 429.24  E-value: 1.62e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048   43 LDDFERIKTLGTGSFGRVMIVQHKPTKDYYAMKILDKQKVVKLKQVEHTLNEKRILQAIQFPFLVSLRYHFKDNSNLYMV 122
Cdd:PTZ00263  17 LSDFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048  123 LEYVPGGEMFSHLRKVGRFSEPHSRFYAAQIVLAFEYLHYLDLIYRDLKPENLLIDSQGYLKVTDFGFAKRVKGRTWTLC 202
Cdd:PTZ00263  97 LEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKVPDRTFTLC 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048  203 GTPEYLAPEIILSKGYNKAVDWWALGVLVYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFGSDLKDLLRNLLQVDLTK 282
Cdd:PTZ00263 177 GTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNWFDGRARDLVKGLLQTDHTK 256
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22946048  283 RYGNLKAGVNDIKNQKWFASTDWIAIFQKKIEAPFIPRCKGPGDTSNFDDYEEEALRISS--TEKCAKEFAEF 353
Cdd:PTZ00263 257 RLGTLKGGVADVKNHPYFHGANWDKLYARYYPAPIPVRVKSPGDTSNFEKYPDSPVDRLPplTAAQQAEFAGF 329
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
52-300 1.07e-138

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: 393.81  E-value: 1.07e-138
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048  52 LGTGSFGRVMIVQHKPTKDYYAMKILDKQKVVKLKQVEHTLNEKRILQAIQFPFLVSLRYHFKDNSNLYMVLEYVPGGEM 131
Cdd:cd05123   1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEIIKRKEVEHTLNERNILERVNHPFIVKLHYAFQTEEKLYLVLDYVPGGEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048 132 FSHLRKVGRFSEPHSRFYAAQIVLAFEYLHYLDLIYRDLKPENLLIDSQGYLKVTDFGFAKRVKG---RTWTLCGTPEYL 208
Cdd:cd05123  81 FSHLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKELSSdgdRTYTFCGTPEYL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048 209 APEIILSKGYNKAVDWWALGVLVYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFGSDLKDLLRNLLQVDLTKRYGNLk 288
Cdd:cd05123 161 APEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKILKSPLKFPEYVSPEAKSLISGLLQKDPTKRLGSG- 239
                       250
                ....*....|..
gi 22946048 289 aGVNDIKNQKWF 300
Cdd:cd05123 240 -GAEEIKAHPFF 250
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
52-305 3.03e-116

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: 337.28  E-value: 3.03e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048  52 LGTGSFGRVMIVQHKPTKDYYAMKILDKQKVVKLKQVEHTLNEKRILQAIQFPFLVSLRYHFKDNSNLYMVLEYVPGGEM 131
Cdd:cd05572   1 LGVGGFGRVELVQLKSKGRTFALKCVKKRHIVQTRQQEHIFSEKEILEECNSPFIVKLYRTFKDKKYLYMLMEYCLGGEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048 132 FSHLRKVGRFSEPHSRFYAAQIVLAFEYLHYLDLIYRDLKPENLLIDSQGYLKVTDFGFAKRVKG--RTWTLCGTPEYLA 209
Cdd:cd05572  81 WTILRDRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAKKLGSgrKTWTFCGTPEYVA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048 210 PEIILSKGYNKAVDWWALGVLVYEMAAGYPPFFADQ--PIQIYEKIVSG--KVRFPSHFGSDLKDLLRNLLQVDLTKRYG 285
Cdd:cd05572 161 PEIILNKGYDFSVDYWSLGILLYELLTGRPPFGGDDedPMKIYNIILKGidKIEFPKYIDKNAKNLIKQLLRRNPEERLG 240
                       250       260
                ....*....|....*....|
gi 22946048 286 NLKAGVNDIKNQKWFASTDW 305
Cdd:cd05572 241 YLKGGIRDIKKHKWFEGFDW 260
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
50-331 5.43e-113

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: 5.43e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048  50 KTLGTGSFGRVMIVQHKPTKDYYAMKILDKQKVVKLKQVEHTLNEKRIL-QAIQFPFLVSLRYHFKDNSNLYMVLEYVPG 128
Cdd:cd05575   1 KVIGKGSFGKVLLARHKAEGKLYAVKVLQKKAILKRNEVKHIMAERNVLlKNVKHPFLVGLHYSFQTKDKLYFVLDYVNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048 129 GEMFSHLRKVGRFSEPHSRFYAAQIVLAFEYLHYLDLIYRDLKPENLLIDSQGYLKVTDFGFAK---RVKGRTWTLCGTP 205
Cdd:cd05575  81 GELFFHLQRERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLCKegiEPSDTTSTFCGTP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048 206 EYLAPEIILSKGYNKAVDWWALGVLVYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFGSDLKDLLRNLLQVDLTKRYG 285
Cdd:cd05575 161 EYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRDTAEMYDNILHKPLRLRTNVSPSARDLLEGLLQKDRTKRLG 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 22946048 286 NlKAGVNDIKNQKWFASTDWIAIFQKKIEAPFIPRCKGPGDTSNFD 331
Cdd:cd05575 241 S-GNDFLEIKNHSFFRPINWDDLEAKKIPPPFNPNVSGPLDLRNID 285
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
50-353 6.91e-113

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: 330.72  E-value: 6.91e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048  50 KTLGTGSFGRVMIVQHKPTKDYYAMKILDKQKVVKLKQVEHTLNEKRIL-QAIQFPFLVSLRYHFKDNSNLYMVLEYVPG 128
Cdd:cd05570   1 KVLGKGSFGKVMLAERKKTDELYAIKVLKKEVIIEDDDVECTMTEKRVLaLANRHPFLTGLHACFQTEDRLYFVMEYVNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048 129 GEMFSHLRKVGRFSEPHSRFYAAQIVLAFEYLHYLDLIYRDLKPENLLIDSQGYLKVTDFGFAKR-VKG--RTWTLCGTP 205
Cdd:cd05570  81 GDLMFHIQRARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMCKEgIWGgnTTSTFCGTP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048 206 EYLAPEIILSKGYNKAVDWWALGVLVYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFGSDLKDLLRNLLQVDLTKRYG 285
Cdd:cd05570 161 DYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFEGDDEDELFEAILNDEVLYPRWLSREAVSILKGLLTKDPARRLG 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22946048 286 NLKAGVNDIKNQKWFASTDWIAIFQKKIEAPFIPRCKGPGDTSNFD-DYEEEALRISSTEKCA------KEFAEF 353
Cdd:cd05570 241 CGPKGEADIKAHPFFRNIDWDKLEKKEVEPPFKPKVKSPRDTSNFDpEFTSESPRLTPVDSDLltnidqEEFRGF 315
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
50-345 1.01e-111

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: 327.78  E-value: 1.01e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048  50 KTLGTGSFGRVMIVQHKPTKDYYAMKILDKQKVVKLKQVEHTLNEKRILQAIQFPFLVSLRYHFKDNSNLYMVLEYVPGG 129
Cdd:cd05571   1 KVLGKGTFGKVILCREKATGELYAIKILKKEVIIAKDEVAHTLTENRVLQNTRHPFLTSLKYSFQTNDRLCFVMEYVNGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048 130 EMFSHLRKVGRFSEPHSRFYAAQIVLAFEYLHYLDLIYRDLKPENLLIDSQGYLKVTDFGFAK---RVKGRTWTLCGTPE 206
Cdd:cd05571  81 ELFFHLSRERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLCKeeiSYGATTKTFCGTPE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048 207 YLAPEIILSKGYNKAVDWWALGVLVYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFGSDLKDLLRNLLQVDLTKRYGN 286
Cdd:cd05571 161 YLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNRDHEVLFELILMEEVRFPSTLSPEAKSLLAGLLKKDPKKRLGG 240
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048 287 LKAGVNDIKNQKWFASTDWIAIFQKKIEAPFIPRCKGPGDTSNFD-DYEEEALRISSTEK 345
Cdd:cd05571 241 GPRDAKEIMEHPFFASINWDDLYQKKIPPPFKPQVTSETDTRYFDeEFTAESVELTPPDR 300
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
46-300 2.77e-108

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 316.78  E-value: 2.77e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048     46 FERIKTLGTGSFGRVMIVQHKPTKDYYAMKILDKQKvvKLKQVEHTLNEKRILQAIQFPFLVSLRYHFKDNSNLYMVLEY 125
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKK--IKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048    126 VPGGEMFSHLRKVGRFSEPHSRFYAAQIVLAFEYLHYLDLIYRDLKPENLLIDSQGYLKVTDFGFAKRVK--GRTWTLCG 203
Cdd:smart00220  79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDpgEKLTTFVG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048    204 TPEYLAPEIILSKGYNKAVDWWALGVLVYEMAAGYPPFFAD-QPIQIYEKIVSGKVRFPSH---FGSDLKDLLRNLLQVD 279
Cdd:smart00220 159 TPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDdQLLELFKKIGKPKPPFPPPewdISPEAKDLIRKLLVKD 238
                          250       260
                   ....*....|....*....|.
gi 22946048    280 LTKRYgnlkaGVNDIKNQKWF 300
Cdd:smart00220 239 PEKRL-----TAEEALQHPFF 254
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
18-336 8.22e-108

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 318.85  E-value: 8.22e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048   18 VKEFLEQAKEEFEDKWRRNPTNTAALDDFERIKTLGTGSFGRVMIVQHKpTKDY--YAMKILDKQKVVKLKQVEHTLNEK 95
Cdd:PTZ00426   4 LKNLQLHKKKDSDSTKEPKRKNKMKYEDFNFIRTLGTGSFGRVILATYK-NEDFppVAIKRFEKSKIIKQKQVDHVFSER 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048   96 RILQAIQFPFLVSLRYHFKDNSNLYMVLEYVPGGEMFSHLRKVGRFSEPHSRFYAAQIVLAFEYLHYLDLIYRDLKPENL 175
Cdd:PTZ00426  83 KILNYINHPFCVNLYGSFKDESYLYLVLEFVIGGEFFTFLRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048  176 LIDSQGYLKVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLVYEMAAGYPPFFADQPIQIYEKIVS 255
Cdd:PTZ00426 163 LLDKDGFIKMTDFGFAKVVDTRTYTLCGTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPFYANEPLLIYQKILE 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048  256 GKVRFPSHFGSDLKDLLRNLLQVDLTKRYGNLKAGVNDIKNQKWFASTDWIAIFQKKIEAPFIPRCKGPGDTSNFDDYEE 335
Cdd:PTZ00426 243 GIIYFPKFLDNNCKHLMKKLLSHDLTKRYGNLKKGAQNVKEHPWFGNIDWVSLLHKNVEVPYKPKYKNVFDSSNFERVQE 322

                 .
gi 22946048  336 E 336
Cdd:PTZ00426 323 D 323
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
44-349 3.74e-106

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: 313.78  E-value: 3.74e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048  44 DDFERIKTLGTGSFGRVMIVQHKPTKDYYAMKILDKQKVVKLKQVEHTLNEKRILQAIQFPFLVSLRYHFKDNSNLYMVL 123
Cdd:cd05599   1 EDFEPLKVIGRGAFGEVRLVRKKDTGHVYAMKKLRKSEMLEKEQVAHVRAERDILAEADNPWVVKLYYSFQDEENLYLIM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048 124 EYVPGGEMFSHLRKVGRFSEPHSRFYAAQIVLAFEYLHYLDLIYRDLKPENLLIDSQGYLKVTDFGFAKRVKGR--TWTL 201
Cdd:cd05599  81 EFLPGGDMMTLLMKKDTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARGHIKLSDFGLCTGLKKShlAYST 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048 202 CGTPEYLAPEIILSKGYNKAVDWWALGVLVYEMAAGYPPFFADQPIQIYEKIVSGK--VRFPS--HFGSDLKDLLRNLLq 277
Cdd:cd05599 161 VGTPDYIAPEVFLQKGYGKECDWWSLGVIMYEMLIGYPPFCSDDPQETCRKIMNWRetLVFPPevPISPEAKDLIERLL- 239
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22946048 278 VDLTKRYGNLkaGVNDIKNQKWFASTDWIAIFQKKieAPFIPRCKGPGDTSNFDDYEEEALRISSTEKCAKE 349
Cdd:cd05599 240 CDAEHRLGAN--GVEEIKSHPFFKGVDWDHIRERP--APILPEVKSILDTSNFDEFEEVDLQIPSSPEAGKD 307
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
44-338 8.57e-105

Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear Dbf2-Related (NDR)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include ROCK and ROCK-like proteins such as DMPK, MRCK, and CRIK, as well as NDR and NDR-like proteins such as LATS, CBK1 and Sid2p. ROCK and CRIK are effectors of the small GTPase Rho, while MRCK is an effector of the small GTPase Cdc42. NDR and NDR-like kinases contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Proteins in this subfamily are involved in regulating many cellular functions including contraction, motility, division, proliferation, apoptosis, morphogenesis, and cytokinesis. The ROCK/NDR-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: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 311.14  E-value: 8.57e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048  44 DDFERIKTLGTGSFGRVMIVQHKPTKDYYAMKILDKQKVVKLKQVEHTLNEKRILQAIQFPFLVSLRYHFKDNSNLYMVL 123
Cdd:cd05573   1 DDFEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILRKSDMLKREQIAHVRAERDILADADSPWIVRLHYAFQDEDHLYLVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048 124 EYVPGGEMFSHLRKVGRFSEPHSRFYAAQIVLAFEYLHYLDLIYRDLKPENLLIDSQGYLKVTDFGFAKRV--------- 194
Cdd:cd05573  81 EYMPGGDLMNLLIKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFGLCTKMnksgdresy 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048 195 --------------KGRTW---------TLCGTPEYLAPEIILSKGYNKAVDWWALGVLVYEMAAGYPPFFADQPIQIYE 251
Cdd:cd05573 161 lndsvntlfqdnvlARRRPhkqrrvraySAVGTPDYIAPEVLRGTGYGPECDWWSLGVILYEMLYGFPPFYSDSLVETYS 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22946048 252 KIVSGKV--RFPSHFG--SDLKDLLRNLLqVDLTKRYGNLKagvnDIKNQKWFASTDWIAIFQKKieAPFIPRCKGPGDT 327
Cdd:cd05573 241 KIMNWKEslVFPDDPDvsPEAIDLIRRLL-CDPEDRLGSAE----EIKAHPFFKGIDWENLRESP--PPFVPELSSPTDT 313
                       330
                ....*....|.
gi 2294604