ID A0A091MSD0_CARIC Unreviewed; 562 AA.
AC A0A091MSD0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Protein kinase C iota type {ECO:0000256|ARBA:ARBA00019159};
DE EC=2.7.11.13 {ECO:0000256|ARBA:ARBA00012429};
DE AltName: Full=nPKC-iota {ECO:0000256|ARBA:ARBA00031507};
DE Flags: Fragment;
GN ORFNames=N322_05934 {ECO:0000313|EMBL:KFP64365.1};
OS Cariama cristata (Red-legged seriema).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Cariamiformes; Cariamidae; Cariama.
OX NCBI_TaxID=54380 {ECO:0000313|EMBL:KFP64365.1, ECO:0000313|Proteomes:UP000054116};
RN [1] {ECO:0000313|EMBL:KFP64365.1, ECO:0000313|Proteomes:UP000054116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N322 {ECO:0000313|EMBL:KFP64365.1};
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. PKC subfamily. {ECO:0000256|ARBA:ARBA00005490}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KK514728; KFP64365.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091MSD0; -.
DR Proteomes; UP000054116; 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; cd20794; C1_aPKC; 1.
DR CDD; cd06404; PB1_aPKC; 1.
DR CDD; cd05618; STKc_aPKC_iota; 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; IPR034661; aPKC_iota.
DR InterPro; IPR046349; C1-like_sf.
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:SF236; PROTEIN KINASE C IOTA TYPE; 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|PIRSR:PIRSR000554-
KW 2}; Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KFP64365.1};
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:UP000054116};
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 1..74
FT /note="PB1"
FT /evidence="ECO:0000259|PROSITE:PS51745"
FT DOMAIN 106..156
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 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"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP64365.1"
FT NON_TER 562
FT /evidence="ECO:0000313|EMBL:KFP64365.1"
SQ SEQUENCE 562 AA; 64519 MW; 7AE0DFEB4BA80510 CRC64;
DIMITYFEPS ISFEGLCNEV RDMCSFDNEQ LFTMKWIDEE GDPCTVSSQL ELEEAFRLYE
LNKDSELLIH VFPCVPERPG MPCPGEDKSI YRRGARRWRK LYCANGHTFQ AKRFNRRAHC
AICTDRIWGL GRQGYKCINC KLLVHKKCHK LVSIECGRHT LQPEPIMPMD SSSVHPDNVE
SVIPYNPSSH ESLDHVGEEK EAMSIRESGK ASSSLGLQDF DLLRVIGRGS YAKVLLVRLK
KTERIYAMKV VKKELVNDDE DIDWVQTEKH VFEQASNHPF LVGLHSCFQT ESRLFFVIEY
VNGGDLMFHM QRQRKLPEEH ARFYSAEISL ALNYLHERGI IYRDLKLDNV LLDSEGHIKL
TDYGMCKEGL RPGDTTSTFC GTPNYIAPEI LRGEDYGFSV DWWALGVLMF EMMAGRSPFD
IVGSSDNPDQ NTEDYLFQVI LEKQIRIPRS LSVKAAGVLK SFLNKDPKER LGCHPQTGFA
DIQGHPFFRN VDWDLMEQKQ VVPPFKPNIS GEFGLDNFDS QFTNEPVQLT PDDDDIVKKI
DQSEFEGFEY INPLLMSAEE CV
//
