ID A6ZTB2_YEAS7 Unreviewed; 824 AA.
AC A6ZTB2;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:EDN62443.1};
GN Name=SCH9 {ECO:0000313|EMBL:EDN62443.1};
GN ORFNames=SCY_2596 {ECO:0000313|EMBL:EDN62443.1};
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:EDN62443.1, ECO:0000313|Proteomes:UP000007060};
RN [1] {ECO:0000313|EMBL:EDN62443.1, ECO:0000313|Proteomes:UP000007060}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789 {ECO:0000313|EMBL:EDN62443.1,
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:EDN62443.1}.
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DR EMBL; AAFW02000082; EDN62443.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZTB2; -.
DR HOGENOM; CLU_000288_52_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; cd05586; STKc_Sck1_like; 1.
DR CDD; cd11651; YPK1_N_like; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
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:SF245; AGC_AKT PROTEIN KINASE SCK2; 1.
DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50004; C2; 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:EDN62443.1};
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:EDN62443.1}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 166..378
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 412..671
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 672..748
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 451
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 824 AA; 91828 MW; C657857530A2EF9E CRC64;
MMNFFTSKSS NQDTGFSSQH QHPNGQNNGN NNSSTAGNDN GYPCKLVSSG PCASSNNGAL
FTNFTLQTAT PTTAISQDLY AMGTTGITSE NALFQMKSMN NGISSVNNNN SNTPTIITTS
QEETNAGNVH GDTGGNSLQN SEDDNFSSSS TTKCLLSSTS SLSINQREAA AAAYGPDTDI
PRGKLEVTII EARDLVTRSK DSQPYVVCTF ESSEFISNGP ESLGAINNNN NNNNNNQHNQ
NQHINNNNEN TNPDAASQHH NNNSGWNGSQ LPSIKEHLKK KPLYTHRSSS QLDQLNSCSS
VTDPSKRSSN SSSGSSNGPK NDSSHPIWHH KTTFDVLGSH SELDISVYDA AHDHMFLGQV
RLYPMIHNLA HASQHQWHSL KPRVIDEVVS GDILIKWTYK QTKKRHYGPQ DFEVLRLLGK
GTFGQVYQVK KKDTQRIYAM KVLSKKVIVK KNEIAHTIGE RNILVTTASK SSPFIVGLKF
SFQTPTDLYL VTDYMSGGEL FWHLQKEGRF SEDRAKFYIA ELVLALEHLH DNDIVYRDLK
PENILLDANG NIALCDFGLS KADLKDRTNT FCGTTEYLAP ELLLDETGYT KMVDFWSLGV
LIFEMCCGWS PFFAENNQKM YQKIAFGKVK FPRDVLSQEG RSFVKGLLNR NPKHRLGSID
DGRELRAHPF FADIDWEALK QKKIPPPFKP HLVSETDTSN FDPEFTTAST SYMNKHQPMM
TATPLSPAMQ AKFAGFTFVD ESAIDEHVNN NRKFLQNSYF MEPGSFIPGN PNLPPDEDVI
DDDGDEDIND GFNQEKNMNN SHSQMDFDGD QHMDDEFVSG RFEI
//
