ID G1WZF5_ARTOA Unreviewed; 339 AA.
AC G1WZF5;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGX53678.1};
GN ORFNames=AOL_s00006g6 {ECO:0000313|EMBL:EGX53678.1};
OS Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX NCBI_TaxID=756982 {ECO:0000313|EMBL:EGX53678.1, ECO:0000313|Proteomes:UP000008784};
RN [1] {ECO:0000313|EMBL:EGX53678.1, ECO:0000313|Proteomes:UP000008784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491
RC {ECO:0000313|Proteomes:UP000008784};
RX PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT provide insights into nematode-trap formation.";
RL PLoS Pathog. 7:E1002179-E1002179(2011).
CC -!- SIMILARITY: Belongs to the protein kinase superfamily.
CC {ECO:0000256|RuleBase:RU000304}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGX53678.1}.
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DR EMBL; ADOT01000009; EGX53678.1; -; Genomic_DNA.
DR RefSeq; XP_011117617.1; XM_011119315.1.
DR AlphaFoldDB; G1WZF5; -.
DR STRING; 756982.G1WZF5; -.
DR GeneID; 22889145; -.
DR eggNOG; KOG0694; Eukaryota.
DR HOGENOM; CLU_000288_63_5_1; -.
DR InParanoid; G1WZF5; -.
DR OMA; RGCQIMA; -.
DR OrthoDB; 21591at2759; -.
DR PHI-base; PHI:123295; -.
DR Proteomes; UP000008784; 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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05570; STKc_PKC; 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:SF228; PROTEIN KINASE C; 1.
DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 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}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000008784};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|RuleBase:RU000304};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 14..273
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 274..339
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT BINDING 43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 339 AA; 39050 MW; 00C57DE93A1F93E5 CRC64;
MRPESARKIG LDHFNFLAVL GKGNFGKVML AETKATKQLY AIKVLKKEFI IENDEVESIR
SEKRVFLIAN KERHPFLLNL HACFQTETRV YFVMEYISGG DLMLHIQRGQ FGTKRAQFYA
AEVCLALKYF HENGVIYRDL KLDNILLTLD GHIKIGDYGL CKEEMWYGST TSTFCGTPEF
MAPEILLDKR YGRAVDWWAF GVLIYQMLLQ QSPFRGEDED EIYDAILSDE PLYPIHMPRD
SVSILQKLLT REPELRLGSG PTDAQEIMSH AFFRNVNWDD IYNKRVPSPF LPQISSPTDT
SNFDQEFTSV TPVLTPVQSV LTQAMQEEFR GFSYTADFV
//