ID Q6BTI4_DEBHA Unreviewed; 650 AA.
AC Q6BTI4;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 04-NOV-2008, sequence version 2.
DT 27-MAR-2024, entry version 106.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN OrderedLocusNames=DEHA2D00352g {ECO:0000313|EMBL:CAG86581.2};
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG86581.2, ECO:0000313|Proteomes:UP000000599};
RN [1] {ECO:0000313|EMBL:CAG86581.2, ECO:0000313|Proteomes:UP000000599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC
RC 2968 {ECO:0000313|Proteomes:UP000000599};
RX PubMed=15229592; DOI=10.1038/nature02579;
RG Genolevures;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA Wincker P., Souciet J.L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382136; CAG86581.2; -; Genomic_DNA.
DR RefSeq; XP_458485.2; XM_458485.1.
DR AlphaFoldDB; Q6BTI4; -.
DR GeneID; 2900886; -.
DR KEGG; dha:DEHA2D00352g; -.
DR VEuPathDB; FungiDB:DEHA2D00352g; -.
DR HOGENOM; CLU_432121_0_0_1; -.
DR InParanoid; Q6BTI4; -.
DR OrthoDB; 2062123at2759; -.
DR Proteomes; UP000000599; Chromosome D.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR Pfam; PF01163; RIO1; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 4: Predicted;
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000000599};
KW Telomere {ECO:0000256|ARBA:ARBA00022895};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 431..650
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
SQ SEQUENCE 650 AA; 75991 MW; 1CB5ECC8860201C4 CRC64;
MNNNTFRNNI RRYILGDDED TGMDIDIDID KFEITKFDYR SIFGKSEHQN MSHLEMVSKF
FRTNKKSEMD MVTLKHKLYF DDHPDEWKEL FIFFCVMPFT EYEFQGKDGK LLNPTTLHAI
GSSHGTDNVL IETFSELEFE SFNEIISEGR LAFNLENILK TDIFSSNFNK DESKRIITNL
LFLGLHMKHI LVTDVLSTDE DTYKENFKKY LFDPICEYVA ALLNFEINIR TKNTAGRTGV
NTKVPHQSND IFHSHPDVVA YYKWKHRRSL AIVEVKKLPI LKGEKVVDFT EPRMVSFMIQ
VVAEMFSDHT NKGMLTDSYT TILIEIDIER SMEIVNQKLT GPENCKFIAL NYRLLDCQSS
GLTLRGGLIS FIYEAFSANE YQLNDVKRGL DAIYDYVRKS DEEYLTYLDG LGEKVDKIFK
NNYNSFMRQL HVIEPKIGLG EFKRIDVQSG VTFNSQLFKV NSKDVKMYLK EDIDETVELV
VKVFDPAKAK RDHNKYVIKK HDMFDNCRRA YLCEKRAYER LLLNFKFNSV YIAQEPVYGR
FFIGNYYHAL GPFIVLKYLA KETLPRDEET YEKAKEQLNI IHLYNIIHGD ISPRNILYSQ
GKVYFIDFGY SEYTEDKLGS NPVSANPERI KSEHQQLCGI FGQPTPNEYE
//
