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Database: UniProt
Entry: A0A194SDH0_RHOGW
LinkDB: A0A194SDH0_RHOGW
Original site: A0A194SDH0_RHOGW 
ID   A0A194SDH0_RHOGW        Unreviewed;       824 AA.
AC   A0A194SDH0;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
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=RHOBADRAFT_49210 {ECO:0000313|EMBL:KPV78642.1};
OS   Rhodotorula graminis (strain WP1).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=578459 {ECO:0000313|EMBL:KPV78642.1, ECO:0000313|Proteomes:UP000053890};
RN   [1] {ECO:0000313|EMBL:KPV78642.1, ECO:0000313|Proteomes:UP000053890}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WP1 {ECO:0000313|EMBL:KPV78642.1,
RC   ECO:0000313|Proteomes:UP000053890};
RX   PubMed=26441909; DOI=10.3389/fmicb.2015.00978;
RA   Firrincieli A., Otillar R., Salamov A., Schmutz J., Khan Z., Redman R.S.,
RA   Fleck N.D., Lindquist E., Grigoriev I.V., Doty S.L.;
RT   "Genome sequence of the plant growth promoting endophytic yeast Rhodotorula
RT   graminis WP1.";
RL   Front. Microbiol. 6:978-978(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};
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DR   EMBL; KQ474073; KPV78642.1; -; Genomic_DNA.
DR   RefSeq; XP_018274691.1; XM_018415232.1.
DR   AlphaFoldDB; A0A194SDH0; -.
DR   STRING; 578459.A0A194SDH0; -.
DR   GeneID; 28975680; -.
DR   OMA; THTINRT; -.
DR   OrthoDB; 5491350at2759; -.
DR   Proteomes; UP000053890; Unassembled WGS sequence.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR024604; GSG2_C.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   PANTHER; PTHR24419; INTERLEUKIN-1 RECEPTOR-ASSOCIATED KINASE; 1.
DR   PANTHER; PTHR24419:SF18; SERINE_THREONINE-PROTEIN KINASE HASPIN; 1.
DR   Pfam; PF12330; Haspin_kinase; 1.
DR   SMART; SM01331; DUF3635; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053890};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          594..691
FT                   /note="Serine/threonine-protein kinase haspin C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01331"
FT   REGION          1..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          652..751
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..55
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..135
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        159..173
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        213..230
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        652..666
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   824 AA;  86534 MW;  9384706FCEBDC325 CRC64;
     MPPTALSGST QHYRAYGKRK TNVINRRQPL GAWNASPVAA PAADGTTSSS DDSETTTDDS
     SSDDDDEPRV TLATRTEAAP CRRKPAKQPA FAVVVESRRS SSTRPPPGAR TTASTSASKE
     NGPAAVWTSS VSGKVQGKAV ELVKGGATSG DEAARRSPLG GASSSSSSRR RPAQSGKKAV
     YGARRARATV VLSSGSSSEE EERLPTPPGV RRTPVVVQSS GSATSSPLTS LQATPQAVVV
     LSDEESEGED ELVDDRAALV LEDEASSLSV AESSDANDLV VVDSASSRAA PRSAGRFPPQ
     LASLRSSLLS PNLFSFSSFV ASPPAPFSAT RPATAAPWRK IGEASYSEVF ATTDDAGRDM
     VVKIIPVAAP SRSRTGTRGG SALRSDVPLP FVSSCDAVRR EIEVSGVLGG REGGIDGFVR
     FRGAFLVQGS YPDELLSAWD DFKRAQGPAC DEQVRPDVLP ETQLFALLLL DNAGSALETF
     KLKSWVEAAG VLGQVVEALG KAEEECGFEH RDLHWGNILL QSVAARRAPA SSLSHRLASL
     SLGQPSSPAL SPLALLDPTS CGVRATLIDF TLSRCCVSTS ADADQVVFDP FEDDDLFEGE
     GEYQFEVYRR MRALVERAQG EQGDKAWRAS EPRTNVLWLH YLVDKLLHSS RLRLPPPPPP
     SPSSATPSSP HRQSGPAASP RRAPLAHRPV TRRTSTAFAP SLSSPARARA RASVGGGVGR
     PAAFGSPLKP RARTLPTPTT ASARAAAATE ARERAAHDAL VRAERALEAA VEGWGLGSGT
     GTGGRGAAKG RGRARKVVKV PAGRDAGLAF ASAGEFARWW FGGF
//
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