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Database: UniProt
Entry: A0A3M2S595_9HYPO
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Original site: A0A3M2S595_9HYPO 
ID   A0A3M2S595_9HYPO        Unreviewed;       400 AA.
AC   A0A3M2S595;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, 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=CDV36_007968 {ECO:0000313|EMBL:RMJ12365.1};
OS   Fusarium kuroshium.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium solani species complex.
OX   NCBI_TaxID=2010991 {ECO:0000313|EMBL:RMJ12365.1, ECO:0000313|Proteomes:UP000277212};
RN   [1] {ECO:0000313|EMBL:RMJ12365.1, ECO:0000313|Proteomes:UP000277212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCR3666 {ECO:0000313|EMBL:RMJ12365.1};
RA   Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA   Kasson M.;
RT   "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL   Submitted (JUN-2017) 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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. RIO-type Ser/Thr
CC       kinase family. {ECO:0000256|ARBA:ARBA00009196}.
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:RMJ12365.1}.
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DR   EMBL; NKUJ01000138; RMJ12365.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M2S595; -.
DR   STRING; 2010991.A0A3M2S595; -.
DR   Proteomes; UP000277212; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion 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   CDD; cd05144; RIO2_C; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR030484; Rio2.
DR   InterPro; IPR015285; RIO2_wHTH_N.
DR   InterPro; IPR000687; RIO_kinase.
DR   InterPro; IPR018935; RIO_kinase_CS.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR45852; SER/THR-PROTEIN KINASE RIO2; 1.
DR   PANTHER; PTHR45852:SF1; SERINE_THREONINE-PROTEIN KINASE RIO2; 1.
DR   Pfam; PF01163; RIO1; 1.
DR   Pfam; PF09202; Rio2_N; 1.
DR   SMART; SM00090; RIO; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS01245; RIO1; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000277212};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          67..310
FT                   /note="RIO kinase"
FT                   /evidence="ECO:0000259|SMART:SM00090"
FT   REGION          339..400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        346..371
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   400 AA;  44868 MW;  64AB5391F02C3D03 CRC64;
     MKLDTRAMRH LASEDWRVLT AVEMGSKNHE LVPTPLIEKI SRLRGGASGV HRSISALAKV
     GLIARVKEAK YDGYRLTYGG LDYLALHTHA KRKDVYSVGN RIGVGKESDI MVVADETGTQ
     RVLKIHRLGR ISFRTVKSNR DYLKNRQSGS WMYLSRLAAM KEFAFMKALR EEGFPVPEPI
     AQSRHTIVMS LIDAFPLRQI SDVPDPASLY ADLIGLILRL AKHGLIHGDF NEFNILVKEE
     RTKSEDGQEV VSLEPIIIDF PQMVSMEHQN AEMYFDRDVN CIKRFFERRF HFVTTQPGPF
     FKNAKKTVGK DGVTRLDATV EASGFTKKML KDLEAAIKDK AETKEQAADD EDEDDDDEED
     EDEDEDEEGD GSSNSGGLLG EDAKNSPDEG VEEGMSKLAV
//
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