ID A0A2G8RLX5_9APHY Unreviewed; 276 AA.
AC A0A2G8RLX5;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=GSI_15204 {ECO:0000313|EMBL:PIL22515.1};
OS Ganoderma sinense ZZ0214-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Ganoderma.
OX NCBI_TaxID=1077348 {ECO:0000313|EMBL:PIL22515.1, ECO:0000313|Proteomes:UP000230002};
RN [1] {ECO:0000313|EMBL:PIL22515.1, ECO:0000313|Proteomes:UP000230002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZZ0214-1 {ECO:0000313|EMBL:PIL22515.1,
RC ECO:0000313|Proteomes:UP000230002};
RX PubMed=26046933; DOI=10.1038/srep11087;
RA Zhu Y., Xu J., Sun C., Zhou S., Xu H., Nelson D.R., Qian J., Song J.,
RA Luo H., Xiang L., Li Y., Xu Z., Ji A., Wang L., Lu S., Hayward A., Sun W.,
RA Li X., Schwartz D.C., Wang Y., Chen S.;
RT "Chromosome-level genome map provides insights into diverse defense
RT mechanisms in the medicinal fungus Ganoderma sinense.";
RL Sci. Rep. 5:11087-11087(2015).
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 -!- 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:PIL22515.1}.
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DR EMBL; AYKW01000069; PIL22515.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G8RLX5; -.
DR STRING; 1077348.A0A2G8RLX5; -.
DR OrthoDB; 5481355at2759; -.
DR Proteomes; UP000230002; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR000687; RIO_kinase.
DR PANTHER; PTHR45723; SERINE/THREONINE-PROTEIN KINASE RIO1; 1.
DR PANTHER; PTHR45723:SF2; SERINE_THREONINE-PROTEIN KINASE RIO1; 1.
DR Pfam; PF01163; RIO1; 1.
DR SMART; SM00090; RIO; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000230002};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 192..276
FT /note="RIO kinase"
FT /evidence="ECO:0000259|SMART:SM00090"
FT REGION 14..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..66
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 276 AA; 30911 MW; 591C85AACEE2C520 CRC64;
MPNTAAFAAQ EIVEAGQFDD APGDDSTAAS NPRRGHSFID DEGLLEWSSG SSEDESEPDE
FQEEEDALEA EAFQMLRAED EDWEIAEGDF TKQYNRIRQH VAVRTGEAQG VASALNSKAA
VASLPAVNRP HPPKPTSTQP SQQQQQHARD KTENQLQALS KYSSRLRNLD IRYDLGVGVN
RKGPSATANM KDKSDRATSE QVLDPRTRII LFKMIGRGLI YEVNGCVSTG KEANVYHALT
PEYKHLALKI YKTSILVFKD RDRYVSGEFR FRRGYR
//