ID A5DMC0_PICGU Unreviewed; 480 AA.
AC A5DMC0;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=Serine/threonine-protein kinase RIO1 {ECO:0000256|ARBA:ARBA00016038};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=PGUG_04421 {ECO:0000313|EMBL:EDK40323.1};
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746 {ECO:0000313|EMBL:EDK40323.1, ECO:0000313|Proteomes:UP000001997};
RN [1] {ECO:0000313|EMBL:EDK40323.1, ECO:0000313|Proteomes:UP000001997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL
RC Y-324 {ECO:0000313|Proteomes:UP000001997};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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 ECO:0000256|PIRSR:PIRSR038147-3};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. RIO-type Ser/Thr
CC kinase family. {ECO:0000256|ARBA:ARBA00009196}.
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DR EMBL; CH408159; EDK40323.1; -; Genomic_DNA.
DR RefSeq; XP_001483692.1; XM_001483642.1.
DR AlphaFoldDB; A5DMC0; -.
DR STRING; 294746.A5DMC0; -.
DR GeneID; 5125470; -.
DR KEGG; pgu:PGUG_04421; -.
DR VEuPathDB; FungiDB:PGUG_04421; -.
DR eggNOG; KOG2270; Eukaryota.
DR HOGENOM; CLU_018693_4_1_1; -.
DR InParanoid; A5DMC0; -.
DR OMA; HPMSLDF; -.
DR OrthoDB; 5481355at2759; -.
DR Proteomes; UP000001997; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; 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 GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR CDD; cd05147; RIO1_euk; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000687; RIO_kinase.
DR InterPro; IPR018935; RIO_kinase_CS.
DR InterPro; IPR017407; Ser/Thr_kinase_Rio1.
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 PIRSF; PIRSF038147; Ser/Thr_PK_RIO1; 1.
DR SMART; SM00090; RIO; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS01245; RIO1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR038147-
KW 2}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR038147-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000001997};
KW Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 95..333
FT /note="RIO kinase"
FT /evidence="ECO:0000259|SMART:SM00090"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..425
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..480
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 271
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038147-1"
FT ACT_SITE 288
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR038147-1"
FT BINDING 153
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR038147-2"
FT BINDING 225
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR038147-2"
FT BINDING 276
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR038147-3"
FT BINDING 288
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR038147-3"
SQ SEQUENCE 480 AA; 55527 MW; DD8E32AA2F4BDEE9 CRC64;
MGSNLAPLSN LEGEKAVEGE PTGPRMTGND FESAKTSEDD STTDSDSDSD TEFDNGTHNP
PATAPKTLTD RGDIIDRYGS KIADSSIKGP KTTKDRANRA TVEQVLDPRT MRFLGKIFNK
GIITRINGCI STGKEANVYH GEHEEKNLEY AVKIYKTSIL VFKDRERYVD GEFRFRNQKN
QSNPRKMVKM WAEKEFRNLK RLYLNGIPCP EPIELKSHVL VMQYLTKGKG QPSPKLKDHP
FADEEEVVHY YHQMLFYMRR MYQECRLVHA DLSEYNSIVH DNKLYIIDVS QSVEPEHPMA
LDFLRMDIKN VNDFFKKKIN VYPERMLFQY ITDNTLRDNS DESLTKYLEA IPLKNEDHDQ
EVEDEIFRSV YLVRSLNQLD ERDFNDFSLG KLNVLNDLLG EAEKEEDSSD SESEYSDESD
EDSDSYDDER AAKIPKGKKF EDKDEKKARK EAAKTAKAEK RKTKMKKNVK KKLVNKRKTK
//
