ID A0A099ZEE9_TINGU Unreviewed; 429 AA.
AC A0A099ZEE9;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=N309_13591 {ECO:0000313|EMBL:KGL80127.1};
OS Tinamus guttatus (White-throated tinamou).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Tinamiformes; Tinamidae; Tinamus.
OX NCBI_TaxID=94827 {ECO:0000313|EMBL:KGL80127.1, ECO:0000313|Proteomes:UP000053641};
RN [1] {ECO:0000313|EMBL:KGL80127.1, ECO:0000313|Proteomes:UP000053641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N309 {ECO:0000313|EMBL:KGL80127.1};
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-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=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
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=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00009903}.
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DR EMBL; KL892793; KGL80127.1; -; Genomic_DNA.
DR RefSeq; XP_010217090.1; XM_010218788.1.
DR AlphaFoldDB; A0A099ZEE9; -.
DR STRING; 94827.A0A099ZEE9; -.
DR GeneID; 104571671; -.
DR KEGG; tgt:104571671; -.
DR CTD; 6446; -.
DR OrthoDB; 3028764at2759; -.
DR Proteomes; UP000053641; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05575; STKc_SGK; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR PANTHER; PTHR24351:SF184; SERINE_THREONINE-PROTEIN KINASE SGK1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KGL80127.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000053641};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|RuleBase:RU000304};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 96..353
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 354..429
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 63..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 134
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 429 AA; 48725 MW; DB4EC9BE00826958 CRC64;
MTVKAAGPAL SYAKMRGMVA ILIAFMKQRR MGLNDFIQKI ATNSYACKHP EVQSILKISQ
PQEPELMNTN PSPPPSPSQQ INLGPSSNPH AKPSDFHFLK VIGKGSFGKV LLARHKAEEQ
FYAVKVLQKK AILKKKEEKH IMFERNVLLQ NVKHPFLVGL HFSFQTADKL YFVLDYINGG
ELFYHLQRER CFLEPRARFY AAEIASALGY LHSLNIVYRD LKPENILLDS QGHIVLTDFG
LCKENIEHNG TTSTFCGTPE YLAPEVLHKQ PYDRTVDWWC LGAVLYEMLY GLPPFYSRNT
AEMYDNILNK PLQLKPNITN SARHLLEGLL QKDRTKRLGA KEDFMEIKNH IFFSPINWDD
LINKKITPPF NPNVSGPSDL RHFDPEFTDE PVPNSIGQSP DSILITASVK EAAEAFLGFS
YAPPMDSFL
//
