ID Q6BI24_DEBHA Unreviewed; 704 AA.
AC Q6BI24;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 04-NOV-2008, sequence version 2.
DT 27-MAR-2024, entry version 122.
DE SubName: Full=DEHA2G13970p {ECO:0000313|EMBL:CAG90633.2};
GN OrderedLocusNames=DEHA2G13970g {ECO:0000313|EMBL:CAG90633.2};
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:CAG90633.2, ECO:0000313|Proteomes:UP000000599};
RN [1] {ECO:0000313|EMBL:CAG90633.2, 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).
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DR EMBL; CR382139; CAG90633.2; -; Genomic_DNA.
DR RefSeq; XP_462147.2; XM_462147.1.
DR AlphaFoldDB; Q6BI24; -.
DR STRING; 284592.Q6BI24; -.
DR GeneID; 2905061; -.
DR KEGG; dha:DEHA2G13970g; -.
DR VEuPathDB; FungiDB:DEHA2G13970g; -.
DR eggNOG; KOG0598; Eukaryota.
DR HOGENOM; CLU_000288_120_1_1; -.
DR InParanoid; Q6BI24; -.
DR OMA; SWKRLLM; -.
DR OrthoDB; 10768at2759; -.
DR Proteomes; UP000000599; Chromosome G.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd11651; YPK1_N_like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR PANTHER; PTHR24351:SF243; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000000599};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 382..636
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 637..704
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 411
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 704 AA; 78569 MW; FF7AA68B7CA57B73 CRC64;
MLKFKNKFKF GSSNGNQEPT SPTGGKRSPK TSSESRRTIS GNVLSDNLSK LSMTDQETTH
SDLSGYQSSV QSGSKMTGQL QGTDKAGQVN VQPMTVQSPR QAGAQGGQGG AVMASTGTSS
KSTSPSSGVS DTDQPNTTVS STPGLLTVKI YNSANLQLPI KINNNKQILH TLATNANNDV
TSQQLIKNLN ALATKEEEEE AGHAHLPGSI STNFLPSTIT IPNGENLIKA LLYLTVEFDN
NVLVIEPQKG TVNQSVWNQV VSFDVTKKST SSGTGSNFLN LNLFIRLPNI LIPDSEKSSQ
ENLFTKNESA KNSNNIGDLL IGTIKLPLNL NFHIKPIRLM NHEYLSFANF NLSDDTKKAL
GEIMLTIDFK PILKSHLSIN DFDLLKVIGK GSFGKVMQVV KKDTKQIYAL KTLRKQHIIS
RMEVTHTLAE RTVLARITNP FIVPLKFSFQ SPEKLYLVLS FINGGELFWH LQKEGKFSMN
RSRFYIAELL TALESLHELN VIYRDLKPEN ILLDYQGHIA LCDFGLCKLN MTNNDKTNTF
CGTPEYLAPE LLLNQGYTRS VDWWTLGILL YEMLTGLPPF YDDDVPTMYR KILQNELKFP
TWLENTDAQD LLIKLIQKDP SKRLNDAQVI KNHSFFKDID WQKLLSKNYL PPFKPNVENL
LDTSNFDQDF TSEKPQDSVV DDFLSESVQK QFGGWTYNGD NILS
//
