ID R7SB80_TREMS Unreviewed; 549 AA.
AC R7SB80;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=TREMEDRAFT_35119 {ECO:0000313|EMBL:EIW66263.1};
OS Tremella mesenterica (strain ATCC 24925 / CBS 8224 / DSM 1558 / NBRC 9311 /
OS NRRL Y-6157 / RJB 2259-6 / UBC 559-6) (Jelly fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Tremellaceae; Tremella.
OX NCBI_TaxID=578456 {ECO:0000313|EMBL:EIW66263.1, ECO:0000313|Proteomes:UP000054539};
RN [1] {ECO:0000313|Proteomes:UP000054539}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fries {ECO:0000313|Proteomes:UP000054539};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
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}.
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DR EMBL; JH711542; EIW66263.1; -; Genomic_DNA.
DR RefSeq; XP_007007700.1; XM_007007638.1.
DR AlphaFoldDB; R7SB80; -.
DR GeneID; 18492664; -.
DR KEGG; tms:TREMEDRAFT_35119; -.
DR VEuPathDB; FungiDB:TREMEDRAFT_35119; -.
DR eggNOG; KOG2268; Eukaryota.
DR OrthoDB; 21899at2759; -.
DR Proteomes; UP000054539; 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:UP000054539};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 65..294
FT /note="RIO kinase"
FT /evidence="ECO:0000259|SMART:SM00090"
FT REGION 299..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 438..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..403
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..494
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..529
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 549 AA; 62294 MW; 6F11D3391DBBBF09 CRC64;
MRLDATDLRY ITNDEFKVLT AVEVGSRDHE VVPTSSIAEI SGLRGGNVNK ALSDLAKRNL
VARVQGAKYE GFRLTYGGLD YLALRTFSRR KPPSVYAVGQ KIGVGKESDI HVVVDESDHR
RVLKMHRLGR ISFRQVKSKR DYLGNRTSAS WMQLSRLAAQ KEFAFMKVLH ANDFPVPVPI
DQVRHCIVMS LIDGYPLRQI QAVESPSDLY AKLMELIVRL ANHGLIHGDF NEFNIIVKKD
GEPVVIDFPQ MVSTRHRNAE YFFNRDVNCI RRYFRRRYKY EGLSWPTWAD VLANQDDTST
SFEQVGPEGA SEPTQGEVQG SANNTTGLAS TSRGNNKRLD LEVEASGFGG TLARELEDHM
IRMMDVPEQD NSDDDEDSDF EEEEDEEEEE VVEIDEDQKE EDTTFDEDHF QRQLAIKLER
MRLNKALGND VNEELYTNLG GQMEEQVRDV GSEGNEGESD EENSIAISDE TPVSEYPTGT
RKRDAQHRIN LKTSSRDEVQ AAIRAEVGKH RSKEERKHHS RKAPVKAGNV KGHKWKQSTG
HLVEKNGGW
//
