ID A0A091FWW7_9AVES Unreviewed; 162 AA.
AC A0A091FWW7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Protein kinase C epsilon type {ECO:0000313|EMBL:KFO74103.1};
DE Flags: Fragment;
GN ORFNames=N303_06712 {ECO:0000313|EMBL:KFO74103.1};
OS Cuculus canorus (common cuckoo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO74103.1, ECO:0000313|Proteomes:UP000053760};
RN [1] {ECO:0000313|EMBL:KFO74103.1, ECO:0000313|Proteomes:UP000053760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO74103.1};
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};
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DR EMBL; KL447479; KFO74103.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091FWW7; -.
DR STRING; 55661.A0A091FWW7; -.
DR Proteomes; UP000053760; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd20838; C1_nPKC_epsilon-like_rpt2; 1.
DR Gene3D; 3.30.60.20; -; 2.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR020454; DAG/PE-bd.
DR InterPro; IPR002219; PE/DAG-bd.
DR PANTHER; PTHR22968:SF27; PROTEIN KINASE C; 1.
DR PANTHER; PTHR22968; PROTEIN KINASE C, MU; 1.
DR Pfam; PF00130; C1_1; 2.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 2.
DR SUPFAM; SSF57889; Cysteine-rich domain; 2.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:KFO74103.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000053760};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 16..67
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 90..140
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO74103.1"
FT NON_TER 162
FT /evidence="ECO:0000313|EMBL:KFO74103.1"
SQ SEQUENCE 162 AA; 18463 MW; C08D1E237FCD0810 CRC64;
RKRQGAVRRR VHQVNGHKFM ATYLRQPTYC SHCRDFIWGV IGKQGYQCQV CTCVVHKRCH
ELIITKCAGL KKQETHDEQV GSQRFSVNMP HKFSIHNYKV PTFCDHCGSL LWGLLRQGLQ
CKVCKMNVHR RCETNVAPNC GVDARGIAKV LADLGVTPDK IT
//
