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Conserved domains on  [gi|71834338|ref|NP_001025262|]
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protein kinase C zeta type [Danio rerio]

Protein Classification

C1 and STKc_aPKC_zeta domain-containing protein (domain architecture ID 10918540)

protein containing domains PB1, C1, and STKc_aPKC_zeta

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
243-599 0e+00

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC-zeta 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: 270768  Cd Length: 357  Bit Score: 744.92  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 243 DGIEGIQISQCLGLGDFDLIRVIGRGSYAKVLLVRLKKNEQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASTNPFLVG 322
Cdd:cd05617   1 DGMDGIKISQGLGLQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASSNPFLVG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 323 LHSCFQTESRLFLVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHEKGIIYRDLKLDNVLLDQDGHIKLTDY 402
Cdd:cd05617  81 LHSCFQTTSRLFLVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDY 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 403 GMCKEGIRPGDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFDIITDNPDMNTEEYLFQVILEKPI 482
Cdd:cd05617 161 GMCKEGLGPGDTTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDIITDNPDMNTEDYLFQVILEKPI 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 483 RIPRSLSVKAASVLKGFLNKDPKERLGCQVQTGFTDIKSHTFFRSIDWDQLEQKQVTPPFKPQITDDYGLENFDTQFTNE 562
Cdd:cd05617 241 RIPRFLSVKASHVLKGFLNKDPKERLGCQPQTGFSDIKSHTFFRSIDWDLLEKKQVTPPFKPQITDDYGLENFDTQFTSE 320
                       330       340       350
                ....*....|....*....|....*....|....*..
gi 71834338 563 PVQLTPDDEDVIKRIDQSEFEGFEYINPLLLSTEETV 599
Cdd:cd05617 321 PVQLTPDDEDVIKRIDQSEFEGFEYINPLLLSTEETV 357
PB1 super family cl02720
The PB1 domain is a modular domain mediating specific protein-protein interactions which play ...
16-98 1.66e-35

The PB1 domain is a modular domain mediating specific protein-protein interactions which play a role in many critical cell processes, such as osteoclastogenesis, angiogenesis, early cardiovascular development, and cell polarity. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domain, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as a noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants.


The actual alignment was detected with superfamily member cd06404:

Pssm-ID: 295447  Cd Length: 83  Bit Score: 129.39  E-value: 1.66e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338  16 VKIKAHYGGDMLISDLDLALTYTEVCKEVREMCGVRKETPITLKWIDDEGDPCTISSQMELEEAFRIYSRSRHSGLLLHV 95
Cdd:cd06404   1 VRVKAAYNGDIMITSIDPSISLEELCNEVRDMCRFHNDQPFTLKWIDEEGDPCTISSQMELEEAFRLYELNKDSELNIHV 80

                ...
gi 71834338  96 FPS 98
Cdd:cd06404  81 FPG 83
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
131-183 1.50e-19

Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain.


:

Pssm-ID: 278556  Cd Length: 53  Bit Score: 84.42  E-value: 1.50e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 71834338   131 HLFQAKRFNRKAYCGHCSERIWGLGRQGYKCINCKLLVHKRCHKLVPLTCQRH 183
Cdd:pfam00130   1 HHFVHRNFKQPTFCDHCGEFLWGLGKQGLKCSWCKLNVHKRCHEKVPPECGCD 53
 
Name Accession Description Interval E-value
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
243-599 0e+00

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC-zeta 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: 270768  Cd Length: 357  Bit Score: 744.92  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 243 DGIEGIQISQCLGLGDFDLIRVIGRGSYAKVLLVRLKKNEQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASTNPFLVG 322
Cdd:cd05617   1 DGMDGIKISQGLGLQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASSNPFLVG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 323 LHSCFQTESRLFLVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHEKGIIYRDLKLDNVLLDQDGHIKLTDY 402
Cdd:cd05617  81 LHSCFQTTSRLFLVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDY 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 403 GMCKEGIRPGDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFDIITDNPDMNTEEYLFQVILEKPI 482
Cdd:cd05617 161 GMCKEGLGPGDTTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDIITDNPDMNTEDYLFQVILEKPI 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 483 RIPRSLSVKAASVLKGFLNKDPKERLGCQVQTGFTDIKSHTFFRSIDWDQLEQKQVTPPFKPQITDDYGLENFDTQFTNE 562
Cdd:cd05617 241 RIPRFLSVKASHVLKGFLNKDPKERLGCQPQTGFSDIKSHTFFRSIDWDLLEKKQVTPPFKPQITDDYGLENFDTQFTSE 320
                       330       340       350
                ....*....|....*....|....*....|....*..
gi 71834338 563 PVQLTPDDEDVIKRIDQSEFEGFEYINPLLLSTEETV 599
Cdd:cd05617 321 PVQLTPDDEDVIKRIDQSEFEGFEYINPLLLSTEETV 357
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
259-525 2.51e-93

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


Pssm-ID: 214567  Cd Length: 254  Bit Score: 290.59  E-value: 2.51e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338    259 FDLIRVIGRGSYAKVLLVRLKKNEQIYAMKVVKKElvHDDEDIDWVQTEKHVFEQAStNPFLVGLHSCFQTESRLFLVIE 338
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKK--KIKKDRERILREIKILKKLK-HPNIVRLYDVFEDEDKLYLVME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338    339 YVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHEKGIIYRDLKLDNVLLDQDGHIKLTDYGMCKEgIRPGDTTSTF 418
Cdd:smart00220  78 YCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQ-LDPGEKLTTF 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338    419 CGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFdiitdnPDMNTEEYLFQVILEKPIRIPR---SLSVKAASV 495
Cdd:smart00220 157 VGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPF------PGDDQLLELFKKIGKPKPPFPPpewDISPEAKDL 230
                          250       260       270
                   ....*....|....*....|....*....|
gi 71834338    496 LKGFLNKDPKERLGCQvqtgftDIKSHTFF 525
Cdd:smart00220 231 IRKLLVKDPEKRLTAE------EALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
259-525 2.66e-82

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 261.76  E-value: 2.66e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338   259 FDLIRVIGRGSYAKVLLVRLKKNEQIYAMKVVKKELVhDDEDIDWVQTEKHVFEQAStNPFLVGLHSCFQTESRLFLVIE 338
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKI-KKKKDKNILREIKILKKLN-HPNIVRLYDAFEDKDNLYLVLE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338   339 YVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHEKGIIYRDLKLDNVLLDQDGHIKLTDYGMCKEGIRPGDTTsTF 418
Cdd:pfam00069  79 YVEGGSLFDLLSEKGAFSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENILIDEDGNLKITDFGLARQLNSGSSLT-SF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338   419 CGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFDIITDNPDMNteeylfQVILEKP-IRIPRSLSVKAASVLK 497
Cdd:pfam00069 158 VGTPWYMAPEVLRGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYE------KIIDQDFdSPRPSSISEEAKDLLK 231
                         250       260
                  ....*....|....*....|....*...
gi 71834338   498 GFLNKDPKERLGCqvqtgfTDIKSHTFF 525
Cdd:pfam00069 232 KLLKKDPSKRLTA------TEALQHPWF 253
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
256-585 2.82e-81

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289  Cd Length: 329  Bit Score: 262.06  E-value: 2.82e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338  256 LGDFDLIRVIGRGSYAKVLLVRLKKNEQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQAStNPFLVGLHSCFQTESRLFL 335
Cdd:PTZ00263  17 LSDFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSILMELS-HPFIVNMMCSFQDENRVYF 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338  336 VIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHEKGIIYRDLKLDNVLLDQDGHIKLTDYGMCKegiRPGDTT 415
Cdd:PTZ00263  96 LLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAK---KVPDRT 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338  416 STFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFdiiTDNPDMNTeeylFQVILEKPIRIPRSLSVKAASV 495
Cdd:PTZ00263 173 FTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPF---FDDTPFRI----YEKILAGRLKFPNWFDGRARDL 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338  496 LKGFLNKDPKERLGcQVQTGFTDIKSHTFFRSIDWDQLEQKQVTPPFKPQITDDYGLENFDtQFTNEPVQLTPddedVIK 575
Cdd:PTZ00263 246 VKGLLQTDHTKRLG-TLKGGVADVKNHPYFHGANWDKLYARYYPAPIPVRVKSPGDTSNFE-KYPDSPVDRLP----PLT 319
                        330
                 ....*....|
gi 71834338  576 RIDQSEFEGF 585
Cdd:PTZ00263 320 AAQQAEFAGF 329
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
258-548 3.41e-51

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 183.02  E-value: 3.41e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 258 DFDLIRVIGRGSYAKVLLVrlkKNEQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASTNPFLVGLHSCFQTESRLFLVI 337
Cdd:COG0515   1 SYRILRKLGEGSFGEVYLA---RDRKLVALKVLAKKLESKSKEVERFLREIQILASLNHPPNIVKLYDFFQDEGSLYLVM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 338 EYVNGGDL---MFHMQRQRKLPEEHARFYAAEICIALNFLHEKGIIYRDLKLDNVLLDQDGH-IKLTDYGMCKEGIRPGD 413
Cdd:COG0515  78 EYVDGGSLedlLKKIGRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRvVKLIDFGLAKLLPDPGS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 414 T------TSTFCGTPNYIAPEILRG---EDYGFSVDWWALGVLMFEMMAGRSPFDIITDNPDMNT------EEYLFQVIL 478
Cdd:COG0515 158 TssipalPSTSVGTPGYMAPEVLLGlslAYASSSSDIWSLGITLYELLTGLPPFEGEKNSSATSQtlkiilELPTPSLAS 237
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 479 EKPIRIPRSLSVKAASVLKGFLNKDPKERLGCqVQTGFTDIKSHTFFRSIDWDQLEQKQVTPPFKPQITD 548
Cdd:COG0515 238 PLSPSNPELISKAASDLLKKLLAKDPKNRLSS-SSDLSHDLLAHLKLKESDLSDLLKPDDSAPLRLSLPP 306
PB1_aPKC cd06404
PB1 domain is an essential modular domain of the atypical protein kinase C (aPKC) which in ...
16-98 1.66e-35

PB1 domain is an essential modular domain of the atypical protein kinase C (aPKC) which in complex with Par6 and Par3 proteins is crucial for establishment of apical-basal polarity of animal cells. PB1 domain is a modular domain mediating specific protein-protein interaction which play roles in many critical cell processes. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domains, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants. The aPKC protein contains a type I/II PB1 domain.


Pssm-ID: 99725  Cd Length: 83  Bit Score: 129.39  E-value: 1.66e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338  16 VKIKAHYGGDMLISDLDLALTYTEVCKEVREMCGVRKETPITLKWIDDEGDPCTISSQMELEEAFRIYSRSRHSGLLLHV 95
Cdd:cd06404   1 VRVKAAYNGDIMITSIDPSISLEELCNEVRDMCRFHNDQPFTLKWIDEEGDPCTISSQMELEEAFRLYELNKDSELNIHV 80

                ...
gi 71834338  96 FPS 98
Cdd:cd06404  81 FPG 83
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
131-183 1.50e-19

Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain.


Pssm-ID: 278556  Cd Length: 53  Bit Score: 84.42  E-value: 1.50e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 71834338   131 HLFQAKRFNRKAYCGHCSERIWGLGRQGYKCINCKLLVHKRCHKLVPLTCQRH 183
Cdd:pfam00130   1 HHFVHRNFKQPTFCDHCGEFLWGLGKQGLKCSWCKLNVHKRCHEKVPPECGCD 53
C1 cd00029
Protein kinase C conserved region 1 (C1) . Cysteine-rich zinc binding domain. Some members of ...
131-180 3.40e-17

Protein kinase C conserved region 1 (C1) . Cysteine-rich zinc binding domain. Some members of this domain family bind phorbol esters and diacylglycerol, some are reported to bind RasGTP. May occur in tandem arrangement. Diacylglycerol (DAG) is a second messenger, released by activation of Phospholipase D. Phorbol Esters (PE) can act as analogues of DAG and mimic its downstream effects in, for example, tumor promotion. Protein Kinases C are activated by DAG/PE, this activation is mediated by their N-terminal conserved region (C1). DAG/PE binding may be phospholipid dependent. C1 domains may also mediate DAG/PE signals in chimaerins (a family of Rac GTPase activating proteins), RasGRPs (exchange factors for Ras/Rap1), and Munc13 isoforms (scaffolding proteins involved in exocytosis).


Pssm-ID: 237996  Cd Length: 50  Bit Score: 77.53  E-value: 3.40e-17
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 71834338 131 HLFQAKRFNRKAYCGHCSERIWGLGRQGYKCINCKLLVHKRCHKLVPLTC 180
Cdd:cd00029   1 HRFVRKSFFKPTFCDVCRKSIWGLFKQGLRCSWCKVKCHKKCADKVPPSC 50
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
286-507 6.15e-17

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  Cd Length: 1266  Bit Score: 84.90  E-value: 6.15e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338    286 AMKVVKKELVHDDEDIDWVQTEKHVFEQAStNPFLVGLHSCFQTE-SRLFLVIEYVNGGDLMFHMQRQRKLPEEHARFYA 364
Cdd:TIGR03903    7 AIKLLRTDAPEEEHQRARFRRETALCARLY-HPNIVALLDSGEAPpGLLFAVFEYVPGRTLREVLAADGALPAGETGRLM 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338    365 AEICIALNFLHEKGIIYRDLKLDNVLLDQDG---HIKLTDYGMCK--EGIRPGDT-----TSTFCGTPNYIAPEILRGED 434
Cdd:TIGR03903   86 LQVLDALACAHNQGIVHRDLKPQNIMVSQTGvrpHAKVLDFGIGTllPGVRDADVatltrTTEVLGTPTYCAPEQLRGEP 165
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71834338    435 YGFSVDWWALGVLMFEMMAGRSPFDIITdnpdmnTEEYLFQVILEKPIRIPRSL-SVKAASVLKGFLNKDPKER 507
Cdd:TIGR03903  166 VTPNSDLYAWGLIFLECLTGQRVVQGAS------VAEILYQQLSPVDVSLPPWIaGHPLGQVLRKALNKDPRQR 233
PB1 smart00666
PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. ...
16-96 1.20e-16

PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. The domain adopts a beta-grasp fold, similar to that found in ubiquitin and Ras-binding domains. A motif, variously termed OPR, PC and AID, represents the most conserved region of the majority of PB1 domains, and is necessary for PB1 domain function. This function is the formation of PB1 domain heterodimers, although not all PB1 domain pairs associate.


Pssm-ID: 214770  Cd Length: 81  Bit Score: 76.86  E-value: 1.20e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338     16 VKIKAHYGGDMLISDLDLALTYTEVCKEVREMCGVRKEtPITLKWIDDEGDPCTISSQMELEEAFRIYSRSRHSGLLLHV 95
Cdd:smart00666   2 VDVKLRYGGETRRLSVPRDISFEDLRSKVAKRFGLDNQ-SFTLKYQDEDGDLVSLTSDEDLEEAIEEYDSLGSKKLRLHV 80

                   .
gi 71834338     96 F 96
Cdd:smart00666  81 F 81
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
131-180 4.77e-15

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


Pssm-ID: 197519  Cd Length: 50  Bit Score: 71.34  E-value: 4.77e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 71834338    131 HLFQAKRFNRKAYCGHCSERIWGLGRQGYKCINCKLLVHKRCHKLVPLTC 180
Cdd:smart00109   1 HKHVFRTFTKPTFCCVCRKSIWGSFKQGLRCSECKVKCHKKCADKVPKAC 50
PB1 pfam00564
PB1 domain;
16-98 1.43e-14

PB1 domain;


Pssm-ID: 278962  Cd Length: 84  Bit Score: 70.77  E-value: 1.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338    16 VKIKAHYGGDMLIS-DLDLALTYTEVCKEVREMCGVRKETpITLKWIDDEGDPCTISSQMELEEAFRIYSRSRHSGLLLH 94
Cdd:pfam00564   2 VRLKLRYGGGIRRFlSVSRGISFEELRAKVEQRFGLDDVD-FKLKYPDEDGDLVSLTSDEDLEEALEEARSLGSKSLRLH 80

                  ....
gi 71834338    95 VFPS 98
Cdd:pfam00564  81 VFPA 84
 
Name Accession Description Interval E-value
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
243-599 0e+00

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC-zeta 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: 270768  Cd Length: 357  Bit Score: 744.92  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 243 DGIEGIQISQCLGLGDFDLIRVIGRGSYAKVLLVRLKKNEQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASTNPFLVG 322
Cdd:cd05617   1 DGMDGIKISQGLGLQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASSNPFLVG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 323 LHSCFQTESRLFLVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHEKGIIYRDLKLDNVLLDQDGHIKLTDY 402
Cdd:cd05617  81 LHSCFQTTSRLFLVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDY 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 403 GMCKEGIRPGDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFDIITDNPDMNTEEYLFQVILEKPI 482
Cdd:cd05617 161 GMCKEGLGPGDTTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDIITDNPDMNTEDYLFQVILEKPI 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 483 RIPRSLSVKAASVLKGFLNKDPKERLGCQVQTGFTDIKSHTFFRSIDWDQLEQKQVTPPFKPQITDDYGLENFDTQFTNE 562
Cdd:cd05617 241 RIPRFLSVKASHVLKGFLNKDPKERLGCQPQTGFSDIKSHTFFRSIDWDLLEKKQVTPPFKPQITDDYGLENFDTQFTSE 320
                       330       340       350
                ....*....|....*....|....*....|....*..
gi 71834338 563 PVQLTPDDEDVIKRIDQSEFEGFEYINPLLLSTEETV 599
Cdd:cd05617 321 PVQLTPDDEDVIKRIDQSEFEGFEYINPLLLSTEETV 357
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
263-588 0e+00

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. aPKCs only require phosphatidylserine (PS) for activation. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The aPKC 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: 270740  Cd Length: 328  Bit Score: 711.50  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 263 RVIGRGSYAKVLLVRLKKNEQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASTNPFLVGLHSCFQTESRLFLVIEYVNG 342
Cdd:cd05588   1 RVIGRGSYAKVLMVELKKTKRIYAMKVIKKELVNDDEDIDWVQTEKHVFETASNHPFLVGLHSCFQTESRLFFVIEFVNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 343 GDLMFHMQRQRKLPEEHARFYAAEICIALNFLHEKGIIYRDLKLDNVLLDQDGHIKLTDYGMCKEGIRPGDTTSTFCGTP 422
Cdd:cd05588  81 GDLMFHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTSTFCGTP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 423 NYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFDII--TDNPDMNTEEYLFQVILEKPIRIPRSLSVKAASVLKGFL 500
Cdd:cd05588 161 NYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSPFDIVgsSDNPDQNTEDYLFQVILEKPIRIPRSLSVKAASVLKGFL 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 501 NKDPKERLGCQVQTGFTDIKSHTFFRSIDWDQLEQKQVTPPFKPQITDDYGLENFDTQFTNEPVQLTPDDEDVIKRIDQS 580
Cdd:cd05588 241 NKNPAERLGCHPQTGFADIQSHPFFRTIDWEQLEQKQVTPPYKPRIESERDLENFDPQFTNEPVQLTPDDPDVIEKIDQS 320

                ....*...
gi 71834338 581 EFEGFEYI 588
Cdd:cd05588 321 EFEGFEYV 328
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
239-599 0e+00

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-iota is directly implicated in carcinogenesis. It is critical to oncogenic signaling mediated by Ras and Bcr-Abl. The PKC-iota gene is the target of tumor-specific gene amplification in many human cancers, and has been identified as a human oncogene. In addition to its role in transformed growth, PKC-iota also promotes invasion, chemoresistance, and tumor cell survival. Expression profiling of PKC-iota is a prognostic marker of poor clinical outcome in several human cancers. PKC-iota also plays a role in establishing cell polarity, and has critical embryonic functions. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC 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: 270769  Cd Length: 364  Bit Score: 639.00  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 239 KAVVDGIEGIQISQCLGLGDFDLIRVIGRGSYAKVLLVRLKKNEQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASTNP 318
Cdd:cd05618   2 KEAMNSRESGKASSSLGLQDFDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVKKELVNDDEDIDWVQTEKHVFEQASNHP 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 319 FLVGLHSCFQTESRLFLVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHEKGIIYRDLKLDNVLLDQDGHIK 398
Cdd:cd05618  82 FLVGLHSCFQTESRLFFVIEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIK 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 399 LTDYGMCKEGIRPGDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFDII--TDNPDMNTEEYLFQV 476
Cdd:cd05618 162 LTDYGMCKEGLRPGDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFDIVgsSDNPDQNTEDYLFQV 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 477 ILEKPIRIPRSLSVKAASVLKGFLNKDPKERLGCQVQTGFTDIKSHTFFRSIDWDQLEQKQVTPPFKPQITDDYGLENFD 556
Cdd:cd05618 242 ILEKQIRIPRSLSVKAASVLKSFLNKDPKERLGCHPQTGFADIQGHPFFRNVDWDLMEQKQVVPPFKPNISGEFGLDNFD 321
                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 71834338 557 TQFTNEPVQLTPDDEDVIKRIDQSEFEGFEYINPLLLSTEETV 599
Cdd:cd05618 322 SQFTNEPVQLTPDDDDIVRKIDQSEFEGFEYINPLLMSAEECV 364
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
263-588 0e+00

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  Cd Length: 318  Bit Score: 559.91  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 263 RVIGRGSYAKVLLVRLKKNEQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASTNPFLVGLHSCFQTESRLFLVIEYVNG 342
Cdd:cd05570   1 KVLGKGSFGKVMLAERKKTDELYAIKVLKKEVIIEDDDVECTMTEKRVLALANRHPFLTGLHACFQTEDRLYFVMEYVNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 343 GDLMFHMQRQRKLPEEHARFYAAEICIALNFLHEKGIIYRDLKLDNVLLDQDGHIKLTDYGMCKEGIRPGDTTSTFCGTP 422
Cdd:cd05570  81 GDLMFHIQRARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMCKEGIWGGNTTSTFCGTP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 423 NYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFDIitdnpdmNTEEYLFQVILEKPIRIPRSLSVKAASVLKGFLNK 502
Cdd:cd05570 161 DYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFEG-------DDEDELFEAILNDEVLYPRWLSREAVSILKGLLTK 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 503 DPKERLGCqVQTGFTDIKSHTFFRSIDWDQLEQKQVTPPFKPQITDDYGLENFDTQFTNEPVQLTPDDEDVIKRIDQSEF 582
Cdd:cd05570 234 DPARRLGC-GPKGEADIKAHPFFRNIDWDKLEKKEVEPPFKPKVKSPRDTSNFDPEFTSESPRLTPVDSDLLTNIDQEEF 312

                ....*.
gi 71834338 583 EGFEYI 588
Cdd:cd05570 313 RGFSYI 318
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
262-589 2.00e-155

Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. cPKCs contain a calcium-binding C2 region in their regulatory domain. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The cPKC 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: 270739  Cd Length: 320  Bit Score: 453.00  E-value: 2.00e-155
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 262 IRVIGRGSYAKVLLVRLKKNEQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASTNPFLVGLHSCFQTESRLFLVIEYVN 341
Cdd:cd05587   1 LMVLGKGSFGKVMLAERKGTDELYAIKILKKDVIIQDDDVECTMVEKRVLALSGKPPFLTQLHSCFQTMDRLYFVMEYVN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 342 GGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHEKGIIYRDLKLDNVLLDQDGHIKLTDYGMCKEGIRPGDTTSTFCGT 421
Cdd:cd05587  81 GGDLMYHIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCKEGIFGGKTTRTFCGT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 422 PNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFdiitdnpDMNTEEYLFQVILEKPIRIPRSLSVKAASVLKGFLN 501
Cdd:cd05587 161 PDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPF-------DGEDEDELFQSIMEHNVSYPKSLSKEAVSICKGLLT 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 502 KDPKERLGCQVqTGFTDIKSHTFFRSIDWDQLEQKQVTPPFKPQITDDYGLENFDTQFTNEPVQLTPDDEDVIKRIDQSE 581
Cdd:cd05587 234 KHPAKRLGCGP-TGERDIKEHPFFRRIDWEKLERREIQPPFKPKIKSPRDAENFDKEFTKEPPVLTPTDKLVIMNIDQSE 312

                ....*...
gi 71834338 582 FEGFEYIN 589
Cdd:cd05587 313 FEGFSFVN 320
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
263-589 6.25e-148

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-epsilon 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: 270743  Cd Length: 321  Bit Score: 433.84  E-value: 6.25e-148
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 263 RVIGRGSYAKVLLVRLKKNEQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASTNPFLVGLHSCFQTESRLFLVIEYVNG 342
Cdd:cd05591   1 KVLGKGSFGKVMLAERKGTDEVYAIKVLKKDVILQDDDVDCTMTEKRILALAAKHPFLTALHSCFQTKDRLFFVMEYVNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 343 GDLMFHMQRQRKLPEEHARFYAAEICIALNFLHEKGIIYRDLKLDNVLLDQDGHIKLTDYGMCKEGIRPGDTTSTFCGTP 422
Cdd:cd05591  81 GDLMFQIQRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGKTTTTFCGTP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 423 NYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFDiiTDNpdmntEEYLFQVILEKPIRIPRSLSVKAASVLKGFLNK 502
Cdd:cd05591 161 DYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFE--ADN-----EDDLFESILHDDVLYPVWLSKEAVSILKAFMTK 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 503 DPKERLGCQVQTGFTD-IKSHTFFRSIDWDQLEQKQVTPPFKPQITDDYGLENFDTQFTNEPVQLTPDDEDVIKRIDQSE 581
Cdd:cd05591 234 NPAKRLGCVASQGGEDaIRQHPFFREIDWEALEQRKVKPPFKPKIKTKRDANNFDQDFTKEEPVLTPVDPAVIKQINQEE 313

                ....*...
gi 71834338 582 FEGFEYIN 589
Cdd:cd05591 314 FRGFSFVN 321
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
263-590 2.78e-147

Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. There are four nPKC isoforms, delta, epsilon, eta, and theta. The nPKC-theta-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: 270744  Cd Length: 320  Bit Score: 432.19  E-value: 2.78e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 263 RVIGRGSYAKVLLVRLKKNEQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASTNPFLVGLHSCFQTESRLFLVIEYVNG 342
Cdd:cd05592   1 KVLGKGSFGKVMLAELKGTNQYFAIKALKKDVVLEDDDVECTMIERRVLALASQHPFLTHLFCTFQTESHLFFVMEYLNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 343 GDLMFHMQRQRKLPEEHARFYAAEICIALNFLHEKGIIYRDLKLDNVLLDQDGHIKLTDYGMCKEGIRPGDTTSTFCGTP 422
Cdd:cd05592  81 GDLMFHIQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMCKENIYGENKASTFCGTP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 423 NYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFdiitdnpDMNTEEYLFQVILEKPIRIPRSLSVKAASVLKGFLNK 502
Cdd:cd05592 161 DYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPF-------HGEDEDELFWSICNDTPHYPRWLTKEAASCLSLLLER 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 503 DPKERLGCQVQTGfTDIKSHTFFRSIDWDQLEQKQVTPPFKPQITDDYGLENFDTQFTNEPVQLTPDDEDVIKRIDQSEF 582
Cdd:cd05592 234 NPEKRLGVPECPA-GDIRDHPFFKTIDWDKLERREIDPPFKPKVKSANDVSNFDPDFTMEKPVLTPVDKKLLASMDQEQF 312

                ....*...
gi 71834338 583 EGFEYINP 590
Cdd:cd05592 313 KGFSFTNP 320
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
258-589 2.65e-139

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. 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, cPKCs depend on calcium, DAG, and in most cases, phosphatidylserine (PS) for activation. The cPKC-beta 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: 270767  Cd Length: 323  Bit Score: 412.09  E-value: 2.65e-139
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 258 DFDLIRVIGRGSYAKVLLVRLKKNEQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASTNPFLVGLHSCFQTESRLFLVI 337
Cdd:cd05616   1 DFNFLMVLGKGSFGKVMLAERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLALSGKPPFLTQLHSCFQTMDRLYFVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 338 EYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHEKGIIYRDLKLDNVLLDQDGHIKLTDYGMCKEGIRPGDTTST 417
Cdd:cd05616  81 EYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDGVTTKT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 418 FCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFdiitdnpDMNTEEYLFQVILEKPIRIPRSLSVKAASVLK 497
Cdd:cd05616 161 FCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPF-------EGEDEDELFQSIMEHNVAYPKSMSKEAVAICK 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 498 GFLNKDPKERLGCQVQtGFTDIKSHTFFRSIDWDQLEQKQVTPPFKPQITDDyGLENFDTQFTNEPVQLTPDDEDVIKRI 577
Cdd:cd05616 234 GLMTKHPGKRLGCGPE-GERDIKEHAFFRYIDWEKLERKEIQPPYKPKACGR-NAENFDRFFTRHPPVLTPPDQEVIRNI 311
                       330
                ....*....|..
gi 71834338 578 DQSEFEGFEYIN 589
Cdd:cd05616 312 DQSEFEGFSFVN 323
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
263-590 5.85e-137

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  Cd Length: 322  Bit Score: 405.97  E-value: 5.85e-137
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 263 RVIGRGSYAKVLLVRLKKNEQIYAMKVVKKELVHDDEDIDWVQTEKHVFeQASTNPFLVGLHSCFQTESRLFLVIEYVNG 342
Cdd:cd05571   1 KVLGKGTFGKVILCREKATGELYAIKILKKEVIIAKDEVAHTLTENRVL-QNTRHPFLTSLKYSFQTNDRLCFVMEYVNG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 343 GDLMFHMQRQRKLPEEHARFYAAEICIALNFLHEKGIIYRDLKLDNVLLDQDGHIKLTDYGMCKEGIRPGDTTSTFCGTP 422
Cdd:cd05571  80 GELFFHLSRERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLCKEEISYGATTKTFCGTP 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 423 NYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFdiitDNPDmntEEYLFQVILEKPIRIPRSLSVKAASVLKGFLNK 502
Cdd:cd05571 160 EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF----YNRD---HEVLFELILMEEVRFPSTLSPEAKSLLAGLLKK 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 503 DPKERLGCQVQTGfTDIKSHTFFRSIDWDQLEQKQVTPPFKPQITDDYGLENFDTQFTNEPVQLTPDDE---DVIKRIDQ 579
Cdd:cd05571 233 DPKKRLGGGPRDA-KEIMEHPFFASINWDDLYQKKIPPPFKPQVTSETDTRYFDEEFTAESVELTPPDRgdlLGLEEEER 311
                       330
                ....*....|.
gi 71834338 580 SEFEGFEYINP 590
Cdd:cd05571 312 PHFEQFSYSAS 322
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
263-592 1.36e-134

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-eta 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: 270742  Cd Length: 323  Bit Score: 399.67  E-value: 1.36e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 263 RVIGRGSYAKVLLVRLKKNEQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASTNPFLVGLHSCFQTESRLFLVIEYVNG 342
Cdd:cd05590   1 RVLGKGSFGKVMLARLKESGRLYAVKVLKKDVILQDDDVECTMTEKRILSLARNHPFLTQLYCCFQTPDRLFFVMEFVNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 343 GDLMFHMQRQRKLPEEHARFYAAEICIALNFLHEKGIIYRDLKLDNVLLDQDGHIKLTDYGMCKEGIRPGDTTSTFCGTP 422
Cdd:cd05590  81 GDLMFHIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGIFNGKTTSTFCGTP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 423 NYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFdiitdnpDMNTEEYLFQVILEKPIRIPRSLSVKAASVLKGFLNK 502
Cdd:cd05590 161 DYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPF-------EAENEDDLFEAILNDEVVYPTWLSQDAVDILKAFMTK 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 503 DPKERLGCQVQTGFTDIKSHTFFRSIDWDQLEQKQVTPPFKPQITDDYGLENFDTQFTNEPVQLTPDDEDVIKRIDQSEF 582
Cdd:cd05590 234 NPTMRLGSLTLGGEEAILRHPFFKELDWEKLNRRQIEPPFRPRIKSREDVSNFDPDFIKEDPVLTPIEESLLPMINQDEF 313
                       330
                ....*....|
gi 71834338 583 EGFEYINPLL 592
Cdd:cd05590 314 RNFSYTAPEL 323
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
263-588 1.88e-132

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  Cd Length: 323  Bit Score: 394.38  E-value: 1.88e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 263 RVIGRGSYAKVLLVRLKKNEQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASTNPFLVGLHSCFQTESRLFLVIEYVNG 342
Cdd:cd05575   1 KVIGKGSFGKVLLARHKAEGKLYAVKVLQKKAILKRNEVKHIMAERNVLLKNVKHPFLVGLHYSFQTKDKLYFVLDYVNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834338 343 GDLMFHMQRQRKLPEEHARFYAAEICIALNFLHEKGIIYRDLKLDNVLLDQDGHIKLTDYGMCKEGIRPGDTTSTFCGTP 422
Cdd:cd05575  81 GELFFHLQRERHFPEPRARFYAAEIASAL