ID A0A093FRP4_GAVST Unreviewed; 574 AA.
AC A0A093FRP4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=protein kinase C {ECO:0000256|ARBA:ARBA00012429};
DE EC=2.7.11.13 {ECO:0000256|ARBA:ARBA00012429};
DE Flags: Fragment;
GN ORFNames=N328_09490 {ECO:0000313|EMBL:KFV56994.1};
OS Gavia stellata (Red-throated diver) (Colymbus stellatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gaviiformes; Gaviidae; Gavia.
OX NCBI_TaxID=37040 {ECO:0000313|EMBL:KFV56994.1, ECO:0000313|Proteomes:UP000054313};
RN [1] {ECO:0000313|EMBL:KFV56994.1, ECO:0000313|Proteomes:UP000054313}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N328 {ECO:0000313|EMBL:KFV56994.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.13;
CC Evidence={ECO:0000256|ARBA:ARBA00000946};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.13; Evidence={ECO:0000256|ARBA:ARBA00000569};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Cytoplasm
CC {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. PKC subfamily. {ECO:0000256|ARBA:ARBA00005490}.
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DR EMBL; KK633359; KFV56994.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093FRP4; -.
DR Proteomes; UP000054313; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004697; F:diacylglycerol-dependent serine/threonine kinase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd20834; C1_nPKC_theta-like_rpt1; 1.
DR CDD; cd20837; C1_nPKC_theta-like_rpt2; 1.
DR Gene3D; 3.30.60.20; -; 2.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR020454; DAG/PE-bd.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR014376; Prot_kin_PKC_delta.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24356:SF181; PROTEIN KINASE C THETA TYPE; 1.
DR PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF21494; PKC_C2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF000551; PKC_delta; 1.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000551-
KW 51}; Kinase {ECO:0000313|EMBL:KFV56994.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000551-51};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000054313};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000313|EMBL:KFV56994.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1..107
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 158..208
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 230..280
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 385..574
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT ACT_SITE 509
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000551-50"
FT BINDING 391..399
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000551-51"
FT BINDING 414
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000551-51,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT NON_TER 574
FT /evidence="ECO:0000313|EMBL:KFV56994.1"
SQ SEQUENCE 574 AA; 65191 MW; 3F7B80829DBD6D6A CRC64;
MSPFLRIGLS NYDSGPYLPS QGEVINPYCA VMVKEAVESE NGQVYVQKKP TMYPPWNSTF
DAHINNGRVM HIVVKDKSAE MVSETTVELK VLAERCKKSN GKTEIWLELK PQGRMLMNAR
YFLEINAKDL ADCETEGFFS LHQRRGAIKQ AKIHNVKCHE FTATFFPQPT FCSVCHEFVW
GLNKQGYQCR QCNAAIHKKC IDKVIAKCTG SAINSRETMF HKERFKIDMP HRFKVYNYKS
PTFCEHCGTL LWGLARQGLK CDACGMNVHH KCQTKVANLC GVNQKLMAEA LAMIESTQQA
RCQRDTEQIS RDGPLEIGFP VPVEVTPIQA LPASTTGKKE PQGISWETPV EGTVKGESLI
ESDLGEQTQE QEEHQVQLKL TIEDFVLHKM LGKGSFGKVF LAELKSTDQY FAVKALKKDV
VLMDDDVECT MVEKRVLSLA WEHPFLTHVF CTFQTKENLF FVMEYLNGGD LMFHIQSCHK
FDLPRATFYA AEIICGLQFL HSKGIIYRDL KLDNVLLDNE GHIKIADFGM CKENMFGDAK
TSTFCGTPDY IAPEVGVRSR EVIKLLWDSR MHLK
//
