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
//