ID E2AWE1_CAMFO Unreviewed; 489 AA.
AC E2AWE1;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 57.
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=EAG_12404 {ECO:0000313|EMBL:EFN62241.1};
OS Camponotus floridanus (Florida carpenter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Camponotus.
OX NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN [1] {ECO:0000313|EMBL:EFN62241.1, ECO:0000313|Proteomes:UP000000311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
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. TKL Ser/Thr
CC protein kinase family. Pelle subfamily.
CC {ECO:0000256|ARBA:ARBA00008718}.
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DR EMBL; GL443286; EFN62241.1; -; Genomic_DNA.
DR RefSeq; XP_011265220.1; XM_011266918.2.
DR AlphaFoldDB; E2AWE1; -.
DR STRING; 104421.E2AWE1; -.
DR EnsemblMetazoa; XM_011266918.3; XP_011265220.1; LOC105256733.
DR GeneID; 105256733; -.
DR KEGG; cfo:105256733; -.
DR InParanoid; E2AWE1; -.
DR OMA; CLCAIEV; -.
DR OrthoDB; 2999496at2759; -.
DR Proteomes; UP000000311; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0048583; P:regulation of response to stimulus; IEA:UniProt.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd08307; Death_Pelle; 1.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 1.10.533.10; Death Domain, Fas; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR000488; Death_domain.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR037924; Pelle_death.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR47989:SF35; LRR RECEPTOR-LIKE SERINE_THREONINE-PROTEIN KINASE RKF3-RELATED; 1.
DR PANTHER; PTHR47989; OS01G0750732 PROTEIN; 1.
DR Pfam; PF00531; Death; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF47986; DEATH domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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}; Kinase {ECO:0000313|EMBL:EFN62241.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000000311};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|RuleBase:RU000304}; Transferase {ECO:0000313|EMBL:EFN62241.1}.
FT DOMAIN 213..489
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 241
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 489 AA; 55962 MW; E13DCF9D9E36BC1E CRC64;
MTTTESLKYI YHLPFSERSE FCKIMNQNDK WEELAGNWMK YDVLTIQSLR KEKNPTDELL
TLWGHHNHTI TELFVLLSKM QHYQSMVPLL NFVDQKFHRL LHSGEANLQN IPRKQLINKN
TKDLKIGTQN FNQRASPQQS VDKILNQPVQ LAISPSNSNN LLVASPGAAV VFLPSSQNTG
SNAKKINESS LPKTETTLPH ASYSELAIAT NGWNPHNILG KGGFGTVYRG TWKNTDVAIK
KIRQKGPDSD ESYILQLQQS LKEIKILNSR AHENILPLYA YSFGGEAPCL VYQLMKNGSL
EDRLLLRQKT KPLTWIQRHE IAKGIARGLQ YLHIIGDKPL IHGDIKSANI LLDKNFEPRI
GDFGLAREGP ERDSMKISKI HGTRPYLPEE FLFDKKLSTK IDTYSYGIVL FEMATGLRAY
DDSRPEKKFL RDLIDAWEDK DLFLLIDKKA GEKDKQVYKN LISLGKWCAN KLAQNRPEME
FVFRKLNDL
//
