ID A0A1S3I5L1_LINUN Unreviewed; 562 AA.
AC A0A1S3I5L1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=protein kinase C {ECO:0000256|ARBA:ARBA00012429};
DE EC=2.7.11.13 {ECO:0000256|ARBA:ARBA00012429};
GN Name=LOC106161221 {ECO:0000313|RefSeq:XP_013393565.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013393565.1};
RN [1] {ECO:0000313|RefSeq:XP_013393565.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013393565.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_013393565.1; XM_013538111.1.
DR AlphaFoldDB; A0A1S3I5L1; -.
DR EnsemblMetazoa; XM_013538111.1; XP_013393565.1; LOC106161221.
DR GeneID; 106161221; -.
DR OrthoDB; 841660at2759; -.
DR Proteomes; UP000085678; Unplaced.
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:0007163; P:establishment or maintenance of cell polarity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd20794; C1_aPKC; 1.
DR CDD; cd05588; STKc_aPKC; 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; IPR034659; Atypical_PKC.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR020454; DAG/PE-bd.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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:SF216; PROTEIN KINASE C; 1.
DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR Pfam; PF00130; C1_1; 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; 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; 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|PIRSR:PIRSR000554-
KW 2};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|RefSeq:XP_013393565.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000554-2};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000085678};
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 91..141
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 220..488
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 489..560
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 152..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 344
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000554-1"
FT BINDING 226..234
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000554-2"
FT BINDING 249
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000554-2"
FT BINDING 253
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 562 AA; 64373 MW; 8EEAD323C9F2502F CRC64;
MASIAFLLWD EVVYRLSCCN YGNTSGDPCT VSSQIELEEA IRLYEVNKDS EITIHIFPNV
PEKPGYPCIG EDRNMYRRGA RRWRKLYRVN GHLFQAKRFS RRAFCAYCSD RIWGLGRQGY
KCITCKLLVH KKCHKLVQIT CQAQLEHTIR PLTSSSSLPP MPGHNGTEAT PRGHSPSKSM
DDASEAPETT KVETVENSES LEDETTATET ATGAISLRDF ELLRVIGRGS YAKVLQVELK
KTKRIYAMKV IKKELVNDDE DIDWVQTEKH VFETASNHPF LVGLHSCFQT PSRLFFVIEF
VNGGDLMFHM QRQRRLPEEH ARFYAAEIIL GLNFLHERGI IYRDLKLDNV LLDSEGHIKL
TDYGMCKEGI RPGDSTSTFC GTPNYIAPEM LRGEDYDFSV DWWALGVLMY EMMAGRSPFD
IVGGAENPDQ NTEDYLFQVI LEKTIRIPRS LSVKAASVLK GFLNKNPQER LGCHPQTGFA
DIQSHPFYRP IDWDLLEKKQ VTPPYKPHVK DERDLEHFDP QFTNEPVQLT PDDTKIISKI
DQTEFEGFEY INPLLMSMED CV
//
