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Database: UniProt
Entry: G0WF47_NAUDC
LinkDB: G0WF47_NAUDC
Original site: G0WF47_NAUDC 
ID   G0WF47_NAUDC            Unreviewed;       706 AA.
AC   G0WF47;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   Name=NDAI0H02340 {ECO:0000313|EMBL:CCD26408.1};
GN   OrderedLocusNames=NDAI_0H02340 {ECO:0000313|EMBL:CCD26408.1};
OS   Naumovozyma dairenensis (strain ATCC 10597 / BCRC 20456 / CBS 421 / NBRC
OS   0211 / NRRL Y-12639) (Saccharomyces dairenensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX   NCBI_TaxID=1071378 {ECO:0000313|EMBL:CCD26408.1, ECO:0000313|Proteomes:UP000000689};
RN   [1] {ECO:0000313|EMBL:CCD26408.1, ECO:0000313|Proteomes:UP000000689}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10597 / BCRC 20456 / CBS 421 / NBRC 0211 / NRRL Y-12639
RC   {ECO:0000313|Proteomes:UP000000689};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT   accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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DR   EMBL; HE580274; CCD26408.1; -; Genomic_DNA.
DR   RefSeq; XP_003671651.1; XM_003671603.1.
DR   AlphaFoldDB; G0WF47; -.
DR   STRING; 1071378.G0WF47; -.
DR   GeneID; 11495939; -.
DR   KEGG; ndi:NDAI_0H02340; -.
DR   eggNOG; KOG0598; Eukaryota.
DR   HOGENOM; CLU_000288_120_2_1; -.
DR   OMA; HHWITLE; -.
DR   OrthoDB; 10768at2759; -.
DR   Proteomes; UP000000689; Chromosome 8.
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:UP000000689};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          374..629
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          630..700
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          47..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          93..133
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..33
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         407
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   706 AA;  80077 MW;  63E9F062FC6625C9 CRC64;
     MNAWKKFKLG KWKDENENKE KEVGKDRDRG EKAELENNTR LFHFHHSNHD HHHHHKHQNS
     QSSVTSDDFF VDRKKTIVKS PSSIAPVRLS SEVLSSTSTM KDTSIAADSR SESSRSESTA
     PTTGTATSNH HTNTSAGIMT IKVYNGEDFT LPIPITSKEQ ILSRLLGSGI NSLHHNLSNE
     VNTLISQLSK IQLEAHEGRS SSSLGSPDEN LIDGKLATNY IPATVMLPAS TKLNPLLYFT
     IEFDNTVATI EPEYGLMSNP IFNKISTFDV TRKLPFLKID VFARIPSILL PPKMWQQIKI
     EEDRKMKKIL EKINSNQDIH LGSVEVPVNL KINSAANIRL YNHHWISLDN GMGKINISID
     YKPSRNKPLS IDDFDLLKVI GKGSFGKVMQ VRKKDTQKIY ALKAIRKSYI VSKSEVTHTL
     AERTVLARVN CPFIVPLKFS FQSSEKLYLV LACINGGELF YHLQREGRFD LSRARFYTAE
     LLCALETLHN LNVIYRDLKP ENILLDYQGH IALCDFGLCK LNMKDDDKTD TFCGTPEYLA
     PELLLGQGYT KVVDWWTLGI LLYEMLTGLP PYYDEDVPRM YRKILQDPLR FPDGFDQDAK
     DLLIQLLNRD PLRRLGCNGA DEIKSHPFFS QLSWKRLVSK GYIPPYKPPV ASSVDTRNFD
     QEFTSEKPVD SVVDEYLSES VQKQFGGWTY VGNEQLGSSM VGDNNI
//
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