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Database: UniProt
Entry: A0A2G8RLX5_9APHY
LinkDB: A0A2G8RLX5_9APHY
Original site: A0A2G8RLX5_9APHY 
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
//
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