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Conserved domains on  [gi|11968080|ref|NP_071952|]
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protein kinase C zeta type [Rattus norvegicus]

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List of domain hits

Name Accession Description Interval E-value
STKc_aPKC_zeta cd05617
Catalytic domain of the Protein Serine/Threonine Kinase, Atypical Protein Kinase C zeta; ...
256-582 0e+00

Catalytic domain of the Protein Serine/Threonine Kinase, Atypical Protein Kinase C zeta; Serine/Threonine Kinases (STKs), Atypical Protein Kinase C (aPKC) subfamily, zeta isoform, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The aPKC 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. 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. There are two aPKC isoforms, zeta and iota. 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.


:

Pssm-ID: 173708 [Multi-domain]  Cd Length: 327  Bit Score: 690.23  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080 256 RVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASSNPFLVGLHSCFQTTSRLFLVIEYVNG 335
Cdd:cd05617   1 RVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASSNPFLVGLHSCFQTTSRLFLVIEYVNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080 336 GDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTTSTFCGTP 415
Cdd:cd05617  81 GDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTTSTFCGTP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080 416 NYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDIITDNPDMNTEDYLFQVILEKPIRIPRFLSVKASHVLKGFLNK 495
Cdd:cd05617 161 NYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDIITDNPDMNTEDYLFQVILEKPIRIPRFLSVKASHVLKGFLNK 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080 496 DPKERLGCRPQTGFSDIKSHAFFRSIDWDLLEKKQTLPPFQPQITDDYGLDNFDTQFTSEPVQLTPDDEDVIKRIDQSEF 575
Cdd:cd05617 241 DPKERLGCQPQTGFSDIKSHTFFRSIDWDLLEKKQVTPPFKPQITDDYGLENFDTQFTSEPVQLTPDDEDVIKRIDQSEF 320

                ....*..
gi 11968080 576 EGFEYIN 582
Cdd:cd05617 321 EGFEYIN 327
PB1_aPKC cd06404
PB1 domain is an essential modular domain of the atypical protein kinase C (aPKC) which in ...
16-98 4.05e-43

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: 149.42  E-value: 4.05e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080  16 VRLKAHYGGDILITSVDPTTTFQDLCEEVRDMCGLHQQHPLTLKWVDSEGDPCTVSSQMELEEAFRLACQGRDEVLIIHV 95
Cdd:cd06404   1 VRVKAAYNGDIMITSIDPSISLEELCNEVRDMCRFHNDQPFTLKWIDEEGDPCTISSQMELEEAFRLYELNKDSELNIHV 80

                ...
gi 11968080  96 FPS 98
Cdd:cd06404  81 FPG 83
C1 cd00029
Protein kinase C conserved region 1 (C1) . Cysteine-rich zinc binding domain. Some members of ...
131-180 3.91e-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: 76.38  E-value: 3.91e-17
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 11968080 131 HLFQAKRFNRRAYCGQCSERIWGLARQGYRCINCKLLVHKRCHVLVPLTC 180
Cdd:cd00029   1 HRFVRKSFFKPTFCDVCRKSIWGLFKQGLRCSWCKVKCHKKCADKVPPSC 50
PH_PKB cd01241
Protein Kinase B-like pleckstrin homology (PH) domain; PKB (also called Akt), a member of the ...
228-281 6.72e-03

Protein Kinase B-like pleckstrin homology (PH) domain; PKB (also called Akt), a member of the AGC kinase family, is a phosphatidylinositol 3'-kinase (PI3K)-dependent Ser/Thr kinase which alters the activity of the targeted protein. The name AGC is based on the three proteins that it is most similar to cAMP-dependent protein kinase 1 (PKA; also known as PKAC), cGMP-dependent protein kinase (PKG; also known as CGK1) and protein kinase C (PKC). Human Akt has three isoforms derived for distinct genes: Akt1/PKBalpha, Akt2/PKBbeta, and Akt3/PKBgamma. All Akts have an N-terminal PH domain with an activating Thr phosphorylation site, a kinase domain, and a short C-terminal regulatory tail with an activating Ser phosphorylation site. The PH domain recruits Akt to the plasma membrane by binding to phosphoinositides (PtdIns-3,4-P2) and is required for activation. The phosphorylation of Akt at its Thr and Ser phosphorylation sites leads to increased Akt activity toward forkhead transcription factors, the mammalian target of rapamycin (mTOR), and the Bcl-xL/Bcl-2-associated death promoter (BAD), all of which possess a consensus motif R-X-R-XX-ST-B (X = amino acid, B = bulky hydrophobic residue) for Akt phosphorylation. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


:

Pssm-ID: 241274 [Multi-domain]  Cd Length: 121  Bit Score: 35.81  E-value: 6.72e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 11968080 228 SEDLKPVIDGvdgIKISQGLGLQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMK 281
Cdd:cd01241  67 TEKPKEVIEN---TFIIRCLQWTTPDELKVIERTFHVKSQLEREEWTNAIYAVK 117
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
252-518 1.63e-94

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


:

Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 292.51  E-value: 1.63e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080    252 FDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKElvHDDEDIDWVQTEKHVFEQASSnPFLVGLHSCFQTTSRLFLVIE 331
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKK--KIKKDRERILREIKILKKLKH-PNIVRLYDVFEDEDKLYLVME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080    332 YVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEgLGPGDTTSTF 411
Cdd:smart00220  78 YCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQ-LDPGEKLTTF 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080    412 CGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFdiitdnPDMNTEDYLFQVILEKPIRIPRF---LSVKASHV 488
Cdd:smart00220 157 VGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPF------PGDDQLLELFKKIGKPKPPFPPPewdISPEAKDL 230
                          250       260       270
                   ....*....|....*....|....*....|
gi 11968080    489 LKGFLNKDPKERLGCRpqtgfsDIKSHAFF 518
Cdd:smart00220 231 IRKLLVKDPEKRLTAE------EALQHPFF 254
 
Name Accession Description Interval E-value
STKc_aPKC_zeta cd05617
Catalytic domain of the Protein Serine/Threonine Kinase, Atypical Protein Kinase C zeta; ...
256-582 0e+00

Catalytic domain of the Protein Serine/Threonine Kinase, Atypical Protein Kinase C zeta; Serine/Threonine Kinases (STKs), Atypical Protein Kinase C (aPKC) subfamily, zeta isoform, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The aPKC 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. 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. There are two aPKC isoforms, zeta and iota. 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.


Pssm-ID: 173708 [Multi-domain]  Cd Length: 327  Bit Score: 690.23  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080 256 RVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASSNPFLVGLHSCFQTTSRLFLVIEYVNG 335
Cdd:cd05617   1 RVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASSNPFLVGLHSCFQTTSRLFLVIEYVNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080 336 GDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTTSTFCGTP 415
Cdd:cd05617  81 GDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTTSTFCGTP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080 416 NYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDIITDNPDMNTEDYLFQVILEKPIRIPRFLSVKASHVLKGFLNK 495
Cdd:cd05617 161 NYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDIITDNPDMNTEDYLFQVILEKPIRIPRFLSVKASHVLKGFLNK 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080 496 DPKERLGCRPQTGFSDIKSHAFFRSIDWDLLEKKQTLPPFQPQITDDYGLDNFDTQFTSEPVQLTPDDEDVIKRIDQSEF 575
Cdd:cd05617 241 DPKERLGCQPQTGFSDIKSHTFFRSIDWDLLEKKQVTPPFKPQITDDYGLENFDTQFTSEPVQLTPDDEDVIKRIDQSEF 320

                ....*..
gi 11968080 576 EGFEYIN 582
Cdd:cd05617 321 EGFEYIN 327
PB1_aPKC cd06404
PB1 domain is an essential modular domain of the atypical protein kinase C (aPKC) which in ...
16-98 4.05e-43

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: 149.42  E-value: 4.05e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080  16 VRLKAHYGGDILITSVDPTTTFQDLCEEVRDMCGLHQQHPLTLKWVDSEGDPCTVSSQMELEEAFRLACQGRDEVLIIHV 95
Cdd:cd06404   1 VRVKAAYNGDIMITSIDPSISLEELCNEVRDMCRFHNDQPFTLKWIDEEGDPCTISSQMELEEAFRLYELNKDSELNIHV 80

                ...
gi 11968080  96 FPS 98
Cdd:cd06404  81 FPG 83
C1 cd00029
Protein kinase C conserved region 1 (C1) . Cysteine-rich zinc binding domain. Some members of ...
131-180 3.91e-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: 76.38  E-value: 3.91e-17
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 11968080 131 HLFQAKRFNRRAYCGQCSERIWGLARQGYRCINCKLLVHKRCHVLVPLTC 180
Cdd:cd00029   1 HRFVRKSFFKPTFCDVCRKSIWGLFKQGLRCSWCKVKCHKKCADKVPPSC 50
PB1 smart00666
PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. ...
16-96 1.42e-20

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: 86.87  E-value: 1.42e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080     16 VRLKAHYGGDILITSVDPTTTFQDLCEEVRDMCGLHQQHPlTLKWVDSEGDPCTVSSQMELEEAFRLACQGRDEVLIIHV 95
Cdd:smart00666   2 VDVKLRYGGETRRLSVPRDISFEDLRSKVAKRFGLDNQSF-TLKYQDEDGDLVSLTSDEDLEEAIEEYDSLGSKKLRLHV 80

                   .
gi 11968080     96 F 96
Cdd:smart00666  81 F 81
S_TK_X smart00133
Extension to Ser/Thr-type protein kinases;
519-582 1.39e-19

Extension to Ser/Thr-type protein kinases;


Pssm-ID: 214529  Cd Length: 64  Bit Score: 83.56  E-value: 1.39e-19
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 11968080    519 RSIDWDLLEKKQTLPPFQPQITDDYGLDNFDTQFTSEPVQLTPDDEDVIKRIDQSEFEGFEYIN 582
Cdd:smart00133   1 RGIDWDKLENKEIEPPFVPKIKSPTDTSNFDPEFTEETPVLTPVDSPLSGGIQQEPFRGFSYVF 64
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
131-180 3.26e-17

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


Pssm-ID: 249614  Cd Length: 50  Bit Score: 76.32  E-value: 3.26e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 11968080   131 HLFQAKRFNRRAYCGQCSERIWGLARQGYRCINCKLLVHKRCHVLVPLTC 180
Cdd:pfam00130   1 HHFVHRNFKQPTFCDHCGEFLWGLGKQGLKCSWCGLNVHKRCHRLVPPEC 50
PB1 pfam00564
PB1 domain;
16-98 3.61e-16

PB1 domain;


Pssm-ID: 249962  Cd Length: 84  Bit Score: 74.23  E-value: 3.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080    16 VRLKAHYGGDILIT-SVDPTTTFQDLCEEVRDMCGLHQqHPLTLKWVDSEGDPCTVSSQMELEEAFRLACQGRDEVLIIH 94
Cdd:pfam00564   2 VRVKLRYGGGIRRFlSVSPGISFEELRSKVEQRFGLDR-VDFKLKYPDEDGDLVSITSDEDLEEAIEEARSLGSKTLRLH 80

                  ....
gi 11968080    95 VFPS 98
Cdd:pfam00564  81 VFPA 84
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
131-180 1.35e-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: 71.73  E-value: 1.35e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 11968080    131 HLFQAKRFNRRAYCGQCSERIWGLARQGYRCINCKLLVHKRCHVLVPLTC 180
Cdd:smart00109   1 HKHVFRTFTKPTFCCVCRKSIWGSFKQGLRCSECKVKCHKKCADKVPKAC 50
Pkinase_C pfam00433
Protein kinase C terminal domain;
538-583 1.41e-11

Protein kinase C terminal domain;


Pssm-ID: 249854  Cd Length: 47  Bit Score: 60.37  E-value: 1.41e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 11968080   538 QITDDYGLDNFDTQFTSEPVQLTPDDEDVIKRIDQSEFEGFEYINP 583
Cdd:pfam00433   1 KVKSETDTSNFDPEFTSEPPTLTPPDPTVLSAIDQKDFRGFTYVNP 46
PH_PKB cd01241
Protein Kinase B-like pleckstrin homology (PH) domain; PKB (also called Akt), a member of the ...
228-281 6.72e-03

Protein Kinase B-like pleckstrin homology (PH) domain; PKB (also called Akt), a member of the AGC kinase family, is a phosphatidylinositol 3'-kinase (PI3K)-dependent Ser/Thr kinase which alters the activity of the targeted protein. The name AGC is based on the three proteins that it is most similar to cAMP-dependent protein kinase 1 (PKA; also known as PKAC), cGMP-dependent protein kinase (PKG; also known as CGK1) and protein kinase C (PKC). Human Akt has three isoforms derived for distinct genes: Akt1/PKBalpha, Akt2/PKBbeta, and Akt3/PKBgamma. All Akts have an N-terminal PH domain with an activating Thr phosphorylation site, a kinase domain, and a short C-terminal regulatory tail with an activating Ser phosphorylation site. The PH domain recruits Akt to the plasma membrane by binding to phosphoinositides (PtdIns-3,4-P2) and is required for activation. The phosphorylation of Akt at its Thr and Ser phosphorylation sites leads to increased Akt activity toward forkhead transcription factors, the mammalian target of rapamycin (mTOR), and the Bcl-xL/Bcl-2-associated death promoter (BAD), all of which possess a consensus motif R-X-R-XX-ST-B (X = amino acid, B = bulky hydrophobic residue) for Akt phosphorylation. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 241274 [Multi-domain]  Cd Length: 121  Bit Score: 35.81  E-value: 6.72e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 11968080 228 SEDLKPVIDGvdgIKISQGLGLQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMK 281
Cdd:cd01241  67 TEKPKEVIEN---TFIIRCLQWTTPDELKVIERTFHVKSQLEREEWTNAIYAVK 117
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
252-518 1.63e-94

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 292.51  E-value: 1.63e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080    252 FDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKElvHDDEDIDWVQTEKHVFEQASSnPFLVGLHSCFQTTSRLFLVIE 331
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKK--KIKKDRERILREIKILKKLKH-PNIVRLYDVFEDEDKLYLVME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080    332 YVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEgLGPGDTTSTF 411
Cdd:smart00220  78 YCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQ-LDPGEKLTTF 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080    412 CGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFdiitdnPDMNTEDYLFQVILEKPIRIPRF---LSVKASHV 488
Cdd:smart00220 157 VGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPF------PGDDQLLELFKKIGKPKPPFPPPewdISPEAKDL 230
                          250       260       270
                   ....*....|....*....|....*....|
gi 11968080    489 LKGFLNKDPKERLGCRpqtgfsDIKSHAFF 518
Cdd:smart00220 231 IRKLLVKDPEKRLTAE------EALQHPFF 254
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
249-578 2.20e-78

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 253.20  E-value: 2.20e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080  249 LQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFeQASSNPFLVGLHSCFQTTSRLFL 328
Cdd:PTZ00263  17 LSDFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSIL-MELSHPFIVNMMCSFQDENRVYF 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080  329 VIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEglgPGDTT 408
Cdd:PTZ00263  96 LLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKK---VPDRT 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080  409 STFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFdiiTDNPDMNTedylFQVILEKPIRIPRFLSVKASHV 488
Cdd:PTZ00263 173 FTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPF---FDDTPFRI----YEKILAGRLKFPNWFDGRARDL 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080  489 LKGFLNKDPKERLGCRPQtGFSDIKSHAFFRSIDWDLLEKKQTLPPFQPQITDDYGLDNFDtQFTSEPVQLTPddedVIK 568
Cdd:PTZ00263 246 VKGLLQTDHTKRLGTLKG-GVADVKNHPYFHGANWDKLYARYYPAPIPVRVKSPGDTSNFE-KYPDSPVDRLP----PLT 319
                        330
                 ....*....|
gi 11968080  569 RIDQSEFEGF 578
Cdd:PTZ00263 320 AAQQAEFAGF 329
Pkinase pfam00069
Protein kinase domain;
252-518 4.66e-78

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 249.86  E-value: 4.66e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080   252 FDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKElvhddeDIDWVQTEKHVFEQA----SSNPFLVGLHSCFQTTSRLF 327
Cdd:pfam00069   1 YELLRKLGSGSFGTVYKAKHKGTGKIVAVKILKKR------SEKSKKDQTARREIRilrrLSHPNIVRLIDAFEDKDHLY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080   328 LVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDT 407
Cdd:pfam00069  75 LVMEYCEGGDLFDYLSRGGPLSEDEAKKIALQILRGLEYLHSNGIIHRDLKPENILLDENGVVKIADFGLAKKLTKSSSS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080   408 TSTFCGTPNYIAPEILR-GEEYGFSVDWWALGVLMFEMMAGRSPFdiitDNPDMNTEDYLFQVILEKPIRIPRFLSVKAS 486
Cdd:pfam00069 155 LTTFVGTPEYMAPEVLLgGNGYGPKVDVWSLGVILYELLTGKPPF----SGESILDQLQLIRRILGPPLEFDEPKSDSGS 230
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 11968080   487 ----HVLKGFLNKDPKERLGCRpqtgfsDIKSHAFF 518
Cdd:pfam00069 231 eeakDLIKKCLNKDPSKRPTAE------EILQHPWF 260
SPS1 COG0515
Serine/threonine protein kinase [General function prediction only / Signal transduction ...
251-551 2.59e-51

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


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 182.25  E-value: 2.59e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080 251 DFDLIRVIGRGSYAKVLLVRLKKndqIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASSNPFLVGLHSCFQTTSRLFLVI 330
Cdd:COG0515   1 SYRILRKLGEGSFGEVYLARDRK---LVALKVLAKKLESKSKEVERFLREIQILASLNHPPNIVKLYDFFQDEGSLYLVM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080 331 EYVNGGDL---MFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGH-IKLTDYGMCKE------ 400
Cdd:COG0515  78 EYVDGGSLedlLKKIGRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRvVKLIDFGLAKLlpdpgs 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080 401 GLGPGDTTSTFCGTPNYIAPEILRG---EEYGFSVDWWALGVLMFEMMAGRSPFDIITDNPDMNT------EDYLFQVIL 471
Cdd:COG0515 158 TSSIPALPSTSVGTPGYMAPEVLLGlslAYASSSSDIWSLGITLYELLTGLPPFEGEKNSSATSQtlkiilELPTPSLAS 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080 472 EKPIRIPRFLSVKASHVLKGFLNKDPKERLGCRpQTGFSDIKSHAFFRSIDWDLLEKKQTLPPFQPQITDDYGLDNFDTQ 551
Cdd:COG0515 238 PLSPSNPELISKAASDLLKKLLAKDPKNRLSSS-SDLSHDLLAHLKLKESDLSDLLKPDDSAPLRLSLPPSLEALISSLN 316
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
261-518 2.26e-37

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 139.22  E-value: 2.26e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080  261 GSYAKVLLVRLKKNDQIYAMKVVKKElvHDDEDidwvqtEKHVFEQASSNPFLVGLHSCFQTTSRLFLVIEYVNGGDLMF 340
Cdd:PHA03390  27 GKFGKVSVLKHKPTQKLFVQKIIKAK--NFNAI------EPMVHQLMKDNPNFIKLYYSVTTLKGHVLIMDYIKDGDLFD 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080  341 HMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLD-ADGHIKLTDYGMCK-EGlgpgdTTSTFCGTPNYI 418
Cdd:PHA03390  99 LLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDrAKDRIYLCDYGLCKiIG-----TPSCYDGTLDYF 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080  419 APEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDIITDNpDMNTEDYLfqVILEKPIRIPRFLSVKASHVLKGFLNKDPK 498
Cdd:PHA03390 174 SPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFKEDEDE-ELDLESLL--KRQQKKLPFIKNVSKNANDFVQSMLKYNIN 250
                        250       260
                 ....*....|....*....|
gi 11968080  499 ERLgcrpqTGFSDIKSHAFF 518
Cdd:PHA03390 251 YRL-----TNYNEIIKHPFL 265
pknD PRK13184
serine/threonine-protein kinase; Reviewed
249-500 2.37e-18

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 87.90  E-value: 2.37e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080  249 LQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELvhddedIDWVQTEKHVFEQAS-----SNPFLVGLHSCFQTT 323
Cdd:PRK13184   1 MQRYDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDL------SENPLLKKRFLREAKiaadlIHPGIVPVYSICSDG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080  324 SRLFLVIEYVNG---GDLMFHMQRQRKLPEEHAR----------FYaaEICIALNFLHERGIIYRDLKLDNVLLDADGHI 390
Cdd:PRK13184  75 DPVYYTMPYIEGytlKSLLKSVWQKESLSKELAEktsvgaflsiFH--KICATIEYVHSKGVLHRDLKPDNILLGLFGEV 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080  391 KLTDYG------MCKEGLG------PGDTTSTF------CGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFD 452
Cdd:PRK13184 153 VILDWGaaifkkLEEEDLLdidvdeRNICYSSMtipgkiVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYR 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 11968080  453 iITDNPDMNTEDYLFQVILEKPIR-IPRFLSvkaSHVLKGfLNKDPKER 500
Cdd:PRK13184 233 -RKKGRKISYRDVILSPIEVAPYReIPPFLS---QIAMKA-LAVDPAER 276
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
240-451 2.60e-18

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 85.26  E-value: 2.60e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080  240 GIKISQGLGLQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKElvHDDEDIDWVQTEKHVFEQASsNPFLVGLHSC 319
Cdd:PLN00034  64 GSAPSAAKSLSELERVNRIGSGAGGTVYKVIHRPTGRLYALKVIYGN--HEDTVRRQICREIEILRDVN-HPNVVKCHDM 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080  320 FQTTSRLFLVIEYVNGGDLM-FHMQRQRKLPEeharfYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMC 398
Cdd:PLN00034 141 FDHNGEIQVLLEFMDGGSLEgTHIADEQFLAD-----VARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVS 215
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 11968080  399 KEGLGPGDTTSTFCGTPNYIAPEIL-----RGEEYGFSVDWWALGVLMFEMMAGRSPF 451
Cdd:PLN00034 216 RILAQTMDPCNSSVGTIAYMSPERIntdlnHGAYDGYAGDIWSLGVSILEFYLGRFPF 273
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
279-500 2.11e-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: 234389 [Multi-domain]  Cd Length: 1266  Bit Score: 84.90  E-value: 2.11e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080    279 AMKVVKKELVHDDEDIDWVQTEKHVFEQASsNPFLVGLHSCFQT-TSRLFLVIEYVNGGDLMFHMQRQRKLPEEHARFYA 357
Cdd:TIGR03903    7 AIKLLRTDAPEEEHQRARFRRETALCARLY-HPNIVALLDSGEApPGLLFAVFEYVPGRTLREVLAADGALPAGETGRLM 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080    358 AEICIALNFLHERGIIYRDLKLDNVLLDADG---HIKLTDYGMCKEGLGPGDT-------TSTFCGTPNYIAPEILRGEE 427
Cdd:TIGR03903   86 LQVLDALACAHNQGIVHRDLKPQNIMVSQTGvrpHAKVLDFGIGTLLPGVRDAdvatltrTTEVLGTPTYCAPEQLRGEP 165
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 11968080    428 YGFSVDWWALGVLMFEMMAGRSPFDIITdnpdmnTEDYLFQVILEKPIRIPrflSVKASH----VLKGFLNKDPKER 500
Cdd:TIGR03903  166 VTPNSDLYAWGLIFLECLTGQRVVQGAS------VAEILYQQLSPVDVSLP---PWIAGHplgqVLRKALNKDPRQR 233
 
Name Accession Description Interval E-value
STKc_aPKC_zeta cd05617
Catalytic domain of the Protein Serine/Threonine Kinase, Atypical Protein Kinase C zeta; ...
256-582 0e+00

Catalytic domain of the Protein Serine/Threonine Kinase, Atypical Protein Kinase C zeta; Serine/Threonine Kinases (STKs), Atypical Protein Kinase C (aPKC) subfamily, zeta isoform, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The aPKC 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. 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. There are two aPKC isoforms, zeta and iota. 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.


Pssm-ID: 173708 [Multi-domain]  Cd Length: 327  Bit Score: 690.23  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080 256 RVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASSNPFLVGLHSCFQTTSRLFLVIEYVNG 335
Cdd:cd05617   1 RVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASSNPFLVGLHSCFQTTSRLFLVIEYVNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080 336 GDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTTSTFCGTP 415
Cdd:cd05617  81 GDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTTSTFCGTP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080 416 NYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDIITDNPDMNTEDYLFQVILEKPIRIPRFLSVKASHVLKGFLNK 495
Cdd:cd05617 161 NYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDIITDNPDMNTEDYLFQVILEKPIRIPRFLSVKASHVLKGFLNK 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080 496 DPKERLGCRPQTGFSDIKSHAFFRSIDWDLLEKKQTLPPFQPQITDDYGLDNFDTQFTSEPVQLTPDDEDVIKRIDQSEF 575
Cdd:cd05617 241 DPKERLGCQPQTGFSDIKSHTFFRSIDWDLLEKKQVTPPFKPQITDDYGLENFDTQFTSEPVQLTPDDEDVIKRIDQSEF 320

                ....*..
gi 11968080 576 EGFEYIN 582
Cdd:cd05617 321 EGFEYIN 327
PB1_aPKC cd06404
PB1 domain is an essential modular domain of the atypical protein kinase C (aPKC) which in ...
16-98 4.05e-43

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: 149.42  E-value: 4.05e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080  16 VRLKAHYGGDILITSVDPTTTFQDLCEEVRDMCGLHQQHPLTLKWVDSEGDPCTVSSQMELEEAFRLACQGRDEVLIIHV 95
Cdd:cd06404   1 VRVKAAYNGDIMITSIDPSISLEELCNEVRDMCRFHNDQPFTLKWIDEEGDPCTISSQMELEEAFRLYELNKDSELNIHV 80

                ...
gi 11968080  96 FPS 98
Cdd:cd06404  81 FPG 83
C1 cd00029
Protein kinase C conserved region 1 (C1) . Cysteine-rich zinc binding domain. Some members of ...
131-180 3.91e-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: 76.38  E-value: 3.91e-17
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 11968080 131 HLFQAKRFNRRAYCGQCSERIWGLARQGYRCINCKLLVHKRCHVLVPLTC 180
Cdd:cd00029   1 HRFVRKSFFKPTFCDVCRKSIWGLFKQGLRCSWCKVKCHKKCADKVPPSC 50
STKc_aPKC cd05588
Catalytic domain of the Protein Serine/Threonine Kinase, Atypical Protein Kinase C; Serine ...
256-582 0e+00

Catalytic domain of the Protein Serine/Threonine Kinase, Atypical Protein Kinase C; Serine/Threonine Kinases (STKs), Atypical Protein Kinase C (aPKC) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The aPKC 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. 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. 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.


Pssm-ID: 173679 [Multi-domain]  Cd Length: 329  Bit Score: 690.02  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080 256 RVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASSNPFLVGLHSCFQTTSRLFLVIEYVNG 335
Cdd:cd05588   1 RVIGRGSYAKVLLVELKKTRRIYAMKVIKKELVNDDEDIDWVQTEKHVFETASNHPFLVGLHSCFQTESRLFFVIEFVSG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080 336 GDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTTSTFCGTP 415
Cdd:cd05588  81 GDLMFHMQRQRKLPEEHARFYSAEISLALNFLHERGIIYRDLKLDNVLLDAEGHIKLTDYGMCKEGIRPGDTTSTFCGTP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080 416 NYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDII--TDNPDMNTEDYLFQVILEKPIRIPRFLSVKASHVLKGFL 493
Cdd:cd05588 161 NYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFDIVgmSDNPDQNTEDYLFQVILEKQIRIPRSLSVKASSVLKGFL 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080 494 NKDPKERLGCRPQTGFSDIKSHAFFRSIDWDLLEKKQTLPPFQPQITDDYGLDNFDTQFTSEPVQLTPDDEDVIKRIDQS 573
Cdd:cd05588 241 NKDPKERLGCHPQTGFRDIKSHPFFRNIDWDLLEQKQVLPPYKPNIESDRDLDNFDPQFTDEPVQLTPDDPDVIARIDQS 320

                ....*....
gi 11968080 574 EFEGFEYIN 582
Cdd:cd05588 321 EFEGFEYIN 329
STKc_aPKC_iota cd05618
Catalytic domain of the Protein Serine/Threonine Kinase, Atypical Protein Kinase C iota; ...
256-582 0e+00

Catalytic domain of the Protein Serine/Threonine Kinase, Atypical Protein Kinase C iota; Serine/Threonine Kinases (STKs), Atypical Protein Kinase C (aPKC) subfamily, iota isoform, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The aPKC 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. 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. There are two aPKC isoforms, zeta and iota. 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.


Pssm-ID: 88519 [Multi-domain]  Cd Length: 329  Bit Score: 603.59  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080 256 RVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASSNPFLVGLHSCFQTTSRLFLVIEYVNG 335
Cdd:cd05618   1 RVIGRGSYAKVLLVRLKKTERIYAMKVVKKELVNDDEDIDWVQTEKHVFEQASNHPFLVGLHSCFQTESRLFFVIEYVNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080 336 GDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTTSTFCGTP 415
Cdd:cd05618  81 GDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTSTFCGTP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080 416 NYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDII--TDNPDMNTEDYLFQVILEKPIRIPRFLSVKASHVLKGFL 493
Cdd:cd05618 161 NYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFDIVgsSDNPDQNTEDYLFQVILEKQIRIPRSLSVKAASVLKSFL 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080 494 NKDPKERLGCRPQTGFSDIKSHAFFRSIDWDLLEKKQTLPPFQPQITDDYGLDNFDTQFTSEPVQLTPDDEDVIKRIDQS 573
Cdd:cd05618 241 NKDPKERLGCHPQTGFADIQGHPFFRNVDWDLMEQKQVVPPFKPNISGEFGLDNFDAQFTNEPVQLTPDDDDIVRKIDQS 320

                ....*....
gi 11968080 574 EFEGFEYIN 582
Cdd:cd05618 321 EFEGFEYIN 329
STKc_PKC cd05570
Catalytic domain of the Protein Serine/Threonine Kinase, Protein Kinase C; Serine/Threonine ...
256-581 0e+00

Catalytic domain of the Protein Serine/Threonine Kinase, Protein Kinase C; Serine/Threonine Kinases (STKs), Protein Kinase C (PKC) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKC 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. 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.


Pssm-ID: 173661 [Multi-domain]  Cd Length: 318  Bit Score: 550.06  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080 256 RVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASSNPFLVGLHSCFQTTSRLFLVIEYVNG 335
Cdd:cd05570   1 KVLGKGSFGKVLLAELKGTDELYAVKVLKKDVILQDDDVECTMTEKRVLALAGKHPFLTQLHSCFQTKDRLFFVMEYVNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080 336 GDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTTSTFCGTP 415
Cdd:cd05570  81 GDLMFHIQRSGRFDEPRARFYAAEIVLGLQFLHERGIIYRDLKLDNVLLDSEGHIKIADFGMCKEGILGGVTTSTFCGTP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080 416 NYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDIitDNpdmntEDYLFQVILEKPIRIPRFLSVKASHVLKGFLNK 495
Cdd:cd05570 161 DYIAPEILSYQPYGPAVDWWALGVLLYEMLAGQSPFEG--DD-----EDELFQSILEDEVRYPRWLSKEAKSILKSFLTK 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080 496 DPKERLGCRPqTGFSDIKSHAFFRSIDWDLLEKKQTLPPFQPQITDDYGLDNFDTQFTSEPVQLTPDDEDVIKRIDQSEF 575
Cdd:cd05570 234 NPEKRLGCLP-TGEQDIKGHPFFREIDWDKLERKEIKPPFKPKIKGRFDVSNFDDEFTKEKPVLTPPDEAIIRNIDQEEF 312

                ....*.
gi 11968080 576 EGFEYI 581
Cdd:cd05570 313 RGFSYI 318
STKc_cPKC cd05587
Catalytic domain of the Protein Serine/Threonine Kinase, Classical Protein Kinase C; Serine ...
251-582 3.50e-150

Catalytic domain of the Protein Serine/Threonine Kinase, Classical Protein Kinase C; Serine/Threonine Kinases (STKs), Classical (or Conventional) Protein Kinase C (cPKC) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The cPKC 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 (PI3K). 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 (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. cPKCs are potent kinases for histones, myelin basic protein, and protamine. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia.


Pssm-ID: 173678 [Multi-domain]  Cd Length: 324  Bit Score: 438.44  E-value: 3.50e-150
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080 251 DFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASSNPFLVGLHSCFQTTSRLFLVI 330
Cdd:cd05587   1 DFNFLMVLGKGSFGKVMLAERKGTDELYAIKILKKDVIIQDDDVECTMVEKRVLALPGKPPFLTQLHSCFQTMDRLYFVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080 331 EYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTTST 410
Cdd:cd05587  81 EYVNGGDLMYHIQQVGKFKEPHAVFYAAEIAIGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCKENIFGGKTTRT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080 411 FCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDIItdnpdmnTEDYLFQVILEKPIRIPRFLSVKASHVLK 490
Cdd:cd05587 161 FCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQPPFDGE-------DEDELFQSIMEHNVSYPKSLSKEAVSICK 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080 491 GFLNKDPKERLGCRPqTGFSDIKSHAFFRSIDWDLLEKKQTLPPFQPQITDDYGLDNFDTQFTSEPVQLTPDDEDVIKRI 570
Cdd:cd05587 234 GLLTKHPAKRLGCGP-TGERDIREHAFFRRIDWEKLERREIQPPFKPKVKGRRSAENFDKFFTREPPVLTPPDKLVIANI 312
                       330
                ....*....|..
gi 11968080 571 DQSEFEGFEYIN 582
Cdd:cd05587 313 DQSEFQGFSFVN 324
STKc_nPKC_epsilon cd05591
Catalytic domain of the Protein Serine/Threonine Kinase, Novel Protein Kinase C epsilon; ...
256-582 9.56e-145

Catalytic domain of the Protein Serine/Threonine Kinase, Novel Protein Kinase C epsilon; Serine/Threonine Kinases (STKs), Novel Protein Kinase C (nPKC), epsilon isoform, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The nPKC 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. 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. 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.


Pssm-ID: 173682 [Multi-domain]  Cd Length: 321  Bit Score: 424.64  E-value: 9.56e-145
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080 256 RVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASSNPFLVGLHSCFQTTSRLFLVIEYVNG 335
Cdd:cd05591   1 KVLGKGSFGKVMLAELKGTDEVYAIKVLKKDVILQDDDVDCTMTEKRILALAAKHPFLTALHCCFQTKDRLFFVMEYVNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080 336 GDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTTSTFCGTP 415
Cdd:cd05591  81 GDLMFQIQRSRKFDEPRSRFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFCGTP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080 416 NYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDiiTDNpdmntEDYLFQVILEKPIRIPRFLSVKASHVLKGFLNK 495
Cdd:cd05591 161 DYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFE--ADN-----EDDLFESILHDDVLYPVWLSKEAVSILKAFMTK 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080 496 DPKERLGCRPQTGFSD-IKSHAFFRSIDWDLLEKKQTLPPFQPQITDDYGLDNFDTQFTSEPVQLTPDDEDVIKRIDQSE 574
Cdd:cd05591 234 NPNKRLGCVASQGGEDaIKQHPFFKEIDWVLLEQRKIKPPFKPKIKTKRDVNNFDQDFTKEEPVLTPVDPAVIKQINQEE 313

                ....*...
gi 11968080 575 FEGFEYIN 582
Cdd:cd05591 314 FRGFSFFN 321
STKc_cPKC_beta cd05616
Catalytic domain of the Protein Serine/Threonine Kinase, Classical Protein Kinase C beta; ...
251-582 2.49e-138

Catalytic domain of the Protein Serine/Threonine Kinase, Classical Protein Kinase C beta; Serine/Threonine Kinases (STKs), Classical Protein Kinase C (cPKC) subfamily, beta isoforms, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The cPKC 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. 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 (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG 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.


Pssm-ID: 173707 [Multi-domain]  Cd Length: 323  Bit Score: 408.24  E-value: 2.49e-138
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080 251 DFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASSNPFLVGLHSCFQTTSRLFLVI 330
Cdd:cd05616   1 DFNFLMVLGKGSFGKVMLAERKGTDELYAIKILKKDVVIQDDDVECTMVEKRVLALSGKPPFLTQLHSCFQTMDRLYFVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080 331 EYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTTST 410
Cdd:cd05616  81 EYVNGGDLMYQIQQVGRFKEPHAVFYAAEIAIGLFFLHSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENMWDGVTTKT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080 411 FCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFdiitdnpDMNTEDYLFQVILEKPIRIPRFLSVKASHVLK 490
Cdd:cd05616 161 FCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPF-------EGEDEDELFQSIMEHNVAYPKSMSKEAVAICK 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080 491 GFLNKDPKERLGCRPQtGFSDIKSHAFFRSIDWDLLEKKQTLPPFQPQITDDyGLDNFDTQFTSEPVQLTPDDEDVIKRI 570
Cdd:cd05616 234 GLMTKHPGKRLGCGPE-GERDIKEHAFFRYIDWEKLERKEVQPPYKPKACGR-DAENFDKFFTRHPPVLTPPDQEVIMNL 311
                       330
                ....*....|..
gi 11968080 571 DQSEFEGFEYIN 582
Cdd:cd05616 312 DQSEFEGFSYVN 323
STKc_cPKC_alpha cd05615
Catalytic domain of the Protein Serine/Threonine Kinase, Classical Protein Kinase C alpha; ...
251-582 1.03e-133

Catalytic domain of the Protein Serine/Threonine Kinase, Classical Protein Kinase C alpha; Serine/Threonine Kinases (STKs), Classical Protein Kinase C (cPKC) subfamily, alpha isoform, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The cPKC 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. 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 (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility. It plays a role in the signaling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumors. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion.


Pssm-ID: 173706 [Multi-domain]  Cd Length: 323  Bit Score: 396.29  E-value: 1.03e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080 251 DFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASSNPFLVGLHSCFQTTSRLFLVI 330
Cdd:cd05615   1 DFNFLMVLGKGSFGKVMLAERKGTDELYAIKILKKDVVIQDDDVECTMVEKRVLALQDKPPFLTQLHSCFQTVDRLYFVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080 331 EYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTTST 410
Cdd:cd05615  81 EYVNGGDLMYHIQQVGKFKEPQAVFYAAEISVGLFFLHRRGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMVDGVTTRT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080 411 FCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFdiitdnpDMNTEDYLFQVILEKPIRIPRFLSVKASHVLK 490
Cdd:cd05615 161 FCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPF-------DGEDEDELFQSIMEHNVSYPKSLSKEAVSICK 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080 491 GFLNKDPKERLGCRPQtGFSDIKSHAFFRSIDWDLLEKKQTLPPFQPQITDDyGLDNFDTQFTSEPVQLTPDDEDVIKRI 570
Cdd:cd05615 234 GLMTKHPSKRLGCGPE-GERDIREHAFFRRIDWDKLENREIQPPFKPKVCGK-GAENFDKFFTRGQPVLTPPDQLVIANI 311
                       330
                ....*....|..
gi 11968080 571 DQSEFEGFEYIN 582
Cdd:cd05615 312 DQADFEGFSYVN 323
STKc_nPKC_eta cd05590
Catalytic domain of the Protein Serine/Threonine Kinase, Novel Protein Kinase C eta; Serine ...
256-581 1.55e-133

Catalytic domain of the Protein Serine/Threonine Kinase, Novel Protein Kinase C eta; Serine/Threonine Kinases (STKs), Novel Protein Kinase C (nPKC), eta isoform, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The nPKC 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. 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. 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.


Pssm-ID: 173681 [Multi-domain]  Cd Length: 320  Bit Score: 395.81  E-value: 1.55e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968080 256 RVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASSNPFLVGLHSCFQTTSRLFLVIEYVNG 335
Cdd:cd05590   1 RVLGKGSFGKVMLARLKESGRLYAVKVLKKDVILQDDDVECTMTEKRILSLARNHPFLTQLYCCFQTPDRLFFVMEFVNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi