ID A6ZMG0_YEAS7 Unreviewed; 677 AA.
AC A6ZMG0;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:EDN64490.1};
GN Name=YPK2 {ECO:0000313|EMBL:EDN64490.1};
GN ORFNames=SCY_4272 {ECO:0000313|EMBL:EDN64490.1};
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796 {ECO:0000313|EMBL:EDN64490.1, ECO:0000313|Proteomes:UP000007060};
RN [1] {ECO:0000313|EMBL:EDN64490.1, ECO:0000313|Proteomes:UP000007060}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789 {ECO:0000313|EMBL:EDN64490.1,
RC ECO:0000313|Proteomes:UP000007060};
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EDN64490.1}.
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DR EMBL; AAFW02000020; EDN64490.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZMG0; -.
DR HOGENOM; CLU_000288_120_2_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
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};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EDN64490.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000313|EMBL:EDN64490.1}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 344..599
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 600..670
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 1..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 373
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 677 AA; 76720 MW; F52A3C24D3F4C677 CRC64;
MHSWRISKFK LGRSKEDDGS SEDENEKSWG NGLFHFHHGE KHHDGSPKNH NHEHEHHIRK
INTNETLPSS LSSPKLRNDA SFKNPSGIGN DNSKASERKA SQSSTETQGP SSESGLMTVK
VYSGKDFTLP FPITSNSTIL QKLLSSGILT SSSNDASEVA AIMRQLPRYK RVDQDSAGEG
LIDRAFATKF IPSSILLPGS TNSSPLLYFT IEFDNSITTI SPDMGTMEQP VFNKISTFDV
TRKLRFLKID VFARIPSLLL PSKNWQQEIG EQDEVLREIL KKINTNQDIH LDSFHLPLNL
KIDSAAQIRL YNHHWISLER GYGKLNITVD YKPSKNKPLS IDDFDLLKVI GRGSFGKVMQ
VRKKDTQKIY ALKALRKAYI VSKCEVTHTL AERTVLARVD CPFIVPLKFS FQSPEKLYLV
LAFINGGELF YHLQHEGRFS LARSRFYIAE LLCALDSLHK LDVIYRDLKP ENILLDYQGH
IALCDFGLCK LNMKDNDKTD TFCGTPEYLA PEILLGQGYT KTVDWWTLGI LLYEMMTGLP
PYYDENVPVM YKKILQQPLL FPDGFDPAAK DLLIGLLSRD PSRRLGVNGT DEIRNHPFFK
DISWKKLLLK GYIPPYKPLV KSEIDTANFD QEFTKEKPID SVVDEYLSAS IQKQFGGWTY
IGDEQLGDSP SQGRSIS
//
