ID A0A091ILG0_CALAN Unreviewed; 604 AA.
AC A0A091ILG0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Protein kinase C {ECO:0000256|ARBA:ARBA00012429, ECO:0000256|PIRNR:PIRNR000554};
DE EC=2.7.11.13 {ECO:0000256|ARBA:ARBA00012429, ECO:0000256|PIRNR:PIRNR000554};
GN ORFNames=N300_05889 {ECO:0000313|EMBL:KFP08338.1};
OS Calypte anna (Anna's hummingbird) (Archilochus anna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Apodiformes;
OC Trochilidae; Calypte.
OX NCBI_TaxID=9244 {ECO:0000313|EMBL:KFP08338.1, ECO:0000313|Proteomes:UP000054308};
RN [1] {ECO:0000313|EMBL:KFP08338.1, ECO:0000313|Proteomes:UP000054308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N300 {ECO:0000313|EMBL:KFP08338.1};
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 ECO:0000256|PIRNR:PIRNR000554};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. PKC subfamily. {ECO:0000256|ARBA:ARBA00005490,
CC ECO:0000256|PIRNR:PIRNR000554}.
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DR EMBL; KL218792; KFP08338.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091ILG0; -.
DR STRING; 9244.A0A091ILG0; -.
DR Proteomes; UP000054308; 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-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd21095; C1_aPKC_zeta; 1.
DR CDD; cd06404; PB1_aPKC; 1.
DR CDD; cd05617; STKc_aPKC_zeta; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR034662; aPKC_zeta.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR047314; C1_aPKC_zeta.
DR InterPro; IPR020454; DAG/PE-bd.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR034877; PB1_aPKC.
DR InterPro; IPR000270; PB1_dom.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR012233; PKC.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24351:SF241; PROTEIN KINASE C; 1.
DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00564; PB1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR PIRSF; PIRSF000554; PKC_zeta; 1.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 1.
DR SMART; SM00666; PB1; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF54277; CAD & PB1 domains; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS51745; PB1; 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; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000554};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000554};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000554};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000054308};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|PIRNR:PIRNR000554};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000554};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 15..98
FT /note="PB1"
FT /evidence="ECO:0000259|PROSITE:PS51745"
FT DOMAIN 142..192
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 264..530
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 531..602
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 201..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 388
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000554-1"
FT BINDING 270..278
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000554-2"
FT BINDING 293
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000554-2"
FT BINDING 297
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 604 AA; 69666 MW; 89A3401B495F2931 CRC64;
MPSRMGSKID LNKDFIRVKT HYSGDILITN LDASMSYDEL CDEVHKMCNL QQEQPITLKW
IDDEGDPCTI SSQMELEEAF RLYCQNRDEG LIIHGKYYTA QRPPCAFFPS IPEKPGMPCP
GEDKSIYRRG ARRWRKLYRV NGHLFQAKRF NRRAYCGQCS ERIWGLGRQG YKCINCKLLV
HKRCHILVPL TCKRHMDSVM PSQEPQLDDK NDEVDLPSEE TDGISYIPST RKHDNLKDDS
EDIKPVIDGM DGIKISQGLG LQDFDLIRVI GRGSYAKVLL VRLKKNDQIY AMKVVKKELV
HDDEDIDWVQ TEKHVFEQAS SNPFLVGLHS CFQTTSRLFL VIEYVNGGDL MFHMQRQRKL
PEEHARFYAA EICIALNFLH ERGIIYRDLK LDNVLLDAEG HIKLTDYGMC KEGLGPGDTT
STFCGTPNYI APEILRGEEY GFSVDWWALG VLMFEMMAGR SPFDIITDNP DMNTEDYLFQ
VILEKPIRIP RFLSVKASHV LKGFLNKDPK ERLGCQPQTG FSDIKSHTFF RSIDWDLLEK
KQTTPPFQPQ ITDDYGLDNF DTQFTSEPVQ LTPDDEDIIK RIDQSEFEGF EYINPLLLST
EETV
//
