ID A0A2C5XNA5_9PEZI Unreviewed; 417 AA.
AC A0A2C5XNA5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=rio2 {ECO:0000313|EMBL:PHH56274.1};
GN ORFNames=CFIMG_000406RA {ECO:0000313|EMBL:PHH56274.1};
OS Ceratocystis fimbriata CBS 114723.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Ceratocystidaceae; Ceratocystis.
OX NCBI_TaxID=1035309 {ECO:0000313|EMBL:PHH56274.1, ECO:0000313|Proteomes:UP000222788};
RN [1] {ECO:0000313|EMBL:PHH56274.1, ECO:0000313|Proteomes:UP000222788}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114723 {ECO:0000313|EMBL:PHH56274.1,
RC ECO:0000313|Proteomes:UP000222788};
RX PubMed=23931120; DOI=10.1016/j.funbio.2013.06.004;
RA Simpson M.C., Wilken P.M., Coetzee M.P., Wingfield M.J., Wingfield B.D.;
RT "Analysis of microsatellite markers in the genome of the plant pathogen
RT Ceratocystis fimbriata.";
RL Fungal Biol. 117:545-555(2013).
RN [2] {ECO:0000313|EMBL:PHH56274.1, ECO:0000313|Proteomes:UP000222788}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114723 {ECO:0000313|EMBL:PHH56274.1,
RC ECO:0000313|Proteomes:UP000222788};
RX PubMed=24563841; DOI=10.5598/imafungus.2013.04.02.14;
RA Wilken P.M., Steenkamp E.T., Wingfield M.J., de Beer Z.W., Wingfield B.D.;
RT "IMA Genome-F 1: Ceratocystis fimbriata: Draft nuclear genome sequence for
RT the plant pathogen, Ceratocystis fimbriata.";
RL IMA Fungus 4:357-358(2013).
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:PHH56274.1}.
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DR EMBL; APWK03000001; PHH56274.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C5XNA5; -.
DR STRING; 1035309.A0A2C5XNA5; -.
DR OrthoDB; 21899at2759; -.
DR Proteomes; UP000222788; 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, ECO:0000313|EMBL:PHH56274.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000222788};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 67..312
FT /note="RIO kinase"
FT /evidence="ECO:0000259|SMART:SM00090"
FT REGION 340..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..380
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 417 AA; 46621 MW; BC3274A3261C045D CRC64;
MLLDSKALRH LTSDDWRVLA AAEQGSKNHE LVPTSLIEKL SRLRGGASGV RRSISALAKV
GLIAKVKEAK YDGYRLTYGG LDYLALHTYT TRKEIYSVGS RIGVGKESDI MVVADQTGKQ
LVLKIHRLGR ISFRTVKSNR DYLRNRSSAS WMYLSRLAAM KEFAFMKALR AEGFPVPEPL
GQSRHTVLMS LIDAFPLRQI SSVPDPASLY SDLIDLLLRL AKHGLIHGDF NEFNILIKEE
EVEGVDEEGQ ANLKLTPIII DFPQMVSMDH QNAEMYFDRD VNCVKRYFKR RFGFTPTSRG
PFFKDAKKLV GQDGATRLDI AEAASGFTKK MNRDLEAAVN QEATNESGNE EEDDDSDEYD
SEYEGEGGED EEDEEEEEEA LPKPEGKQGA GEDTQEPKVG SKSILDGVKL EKLEIAD
//
