ID H3A5S9_LATCH Unreviewed; 392 AA.
AC H3A5S9;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Protein kinase C alpha {ECO:0000313|Ensembl:ENSLACP00000005000.1};
GN Name=PRKCA {ECO:0000313|Ensembl:ENSLACP00000005000.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000005000.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000005000.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; AFYH01050958; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01050959; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01050960; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01050961; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01050962; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01050963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01050964; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01050965; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01050966; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01050967; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3A5S9; -.
DR Ensembl; ENSLACT00000005044.1; ENSLACP00000005000.1; ENSLACG00000004445.1.
DR GeneTree; ENSGT00940000156104; -.
DR Proteomes; UP000008672; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR CDD; cd20836; C1_cPKC_rpt2; 1.
DR CDD; cd04026; C2_PKC_alpha_gamma; 1.
DR Gene3D; 3.30.60.20; -; 1.
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; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR PANTHER; PTHR24356:SF193; PROTEIN KINASE C ALPHA TYPE; 1.
DR PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00360; C2DOMAIN.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
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; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000008672};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 23..73
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 80..197
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 262..392
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 291
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 392 AA; 44768 MW; 8831A7056D4E249C CRC64;
HEFVTFSCPG ADKGPDTDDP RSKHKFKIHT YGSPTFCDHC GSLLYGLIHQ GMKCETCDMN
VHKQCVINVP SLCGTDHTER RGRLFLKIEI NDEKMYVTVG EAKNLIPMDP NGLSDPYVKL
KLIPDPKNES KQKTRTIRSS LNPNFNESFT FKLKASDKDR RLSVEAWDWD RTTRNDFMGS
LSFGVSELMK QPVCGWYKLL NQEEGEYYNV PISEADDGNV ELRQKFEKAK LGPAGNKVIS
PVEERKSSTP SNNLDRVKLT DFNFLMVLGK GSFGKVMLAE RKGTEELYAI KILKKDVVIQ
DDDVECTMIE KRVLALHDKP PFLTQLHSCF QTVDRLYFVM EYVNGGDLMY HIQHVGKFKE
PQAVFYAAEI AIGLFFLHKE GIIYRDLKLD NV
//
