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Database: UniProt
Entry: A0A093QJC5_9PASS
LinkDB: A0A093QJC5_9PASS
Original site: A0A093QJC5_9PASS 
ID   A0A093QJC5_9PASS        Unreviewed;       610 AA.
AC   A0A093QJC5;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-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=N305_00951 {ECO:0000313|EMBL:KFW89033.1};
OS   Manacus vitellinus (golden-collared manakin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Pipridae; Manacus.
OX   NCBI_TaxID=328815 {ECO:0000313|EMBL:KFW89033.1, ECO:0000313|Proteomes:UP000053258};
RN   [1] {ECO:0000313|EMBL:KFW89033.1, ECO:0000313|Proteomes:UP000053258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N305 {ECO:0000313|EMBL:KFW89033.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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   -!- 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; KL761277; KFW89033.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093QJC5; -.
DR   STRING; 328815.ENSMVIP00005007804; -.
DR   Proteomes; UP000053258; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004697; F:diacylglycerol-dependent serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd20835; C1_nPKC_epsilon-like_rpt1; 1.
DR   CDD; cd20838; C1_nPKC_epsilon-like_rpt2; 1.
DR   CDD; cd05591; STKc_nPKC_epsilon; 1.
DR   Gene3D; 3.30.60.20; -; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR020454; DAG/PE-bd.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR034669; nPKC_epsilon.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR017892; Pkinase_C.
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; PTHR24351:SF182; PROTEIN KINASE C EPSILON TYPE; 1.
DR   PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   Pfam; PF00130; C1_1; 2.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   PIRSF; PIRSF000551; PKC_delta; 1.
DR   PRINTS; PR00008; DAGPEDOMAIN.
DR   SMART; SM00109; C1; 2.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 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:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KFW89033.1};
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:UP000053258};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          36..87
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          110..160
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          281..541
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          542..610
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   REGION          193..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          236..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        200..219
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        405
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000551-50"
FT   BINDING         287..295
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000551-51"
FT   BINDING         310
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         1
FT                   /evidence="ECO:0000313|EMBL:KFW89033.1"
FT   NON_TER         610
FT                   /evidence="ECO:0000313|EMBL:KFW89033.1"
SQ   SEQUENCE   610 AA;  69548 MW;  5B95EFDF509E9DA7 CRC64;
     SSVSAPKDNE ERVFRERMRP RKRQGAVRRR VHQVNGHKFM ATYLRQPTYC SHCRDFIWGV
     IGKQGYQCQV CTCVVHKRCH ELIITKCAGL KKQETHDEQV GSQRFSVNMP HKFSIHNYKV
     PTFCDHCGSL LWGLLRQGLQ CKVCKMNVHR RCETNVAPNC GVDARGIAKV LADLGVTPDK
     ITNSGQRRKK LIAGAETQPP VPGSASSEED RSKSAPTSPC DQEIKELENN IRKALSFDNR
     GEEHRATATT STDNQLNKPG ENGENGEVKQ AQGKRIGLEE FNFIKVLGKG SFGKVMLAEL
     KGKDEVYAVK VLKKDVILQD DDVDCTMTEK RILALARKHP YLTQLYCCFQ TKDRLFFVME
     YVNGGDLMFQ IQRSRKFDEP RSRFYAAEVT SALMFLHQHG VIYRDLKLDN ILLDAEGHCK
     LADFGMCKEG ILNGVTTTTF CGTPDYIAPE ILQELEYGPS VDWWALGVLM YEMMAGQPPF
     EADNEDDLFE SILHDDVLYP VWLSKEAVSI LKAFMTKNPN KRLGCVASQN GEDAIKQHPF
     FKEIDWVLLE QRKIKPPFKP RIKTKRDVNN FDQDFTREEP VLTLVDETII KQINQEEFKG
     FSYFGEELLP
//
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