GenomeNet

Database: UniProt
Entry: H0GXE4_SACCK
LinkDB: H0GXE4_SACCK
Original site: H0GXE4_SACCK 
ID   H0GXE4_SACCK            Unreviewed;       680 AA.
AC   H0GXE4;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Ypk1p {ECO:0000313|EMBL:EHN01520.1};
GN   ORFNames=VIN7_8298 {ECO:0000313|EMBL:EHN01520.1};
OS   Saccharomyces cerevisiae x Saccharomyces kudriavzevii (strain VIN7)
OS   (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=1095631 {ECO:0000313|EMBL:EHN01520.1, ECO:0000313|Proteomes:UP000009009};
RN   [1] {ECO:0000313|EMBL:EHN01520.1, ECO:0000313|Proteomes:UP000009009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VIN7 {ECO:0000313|EMBL:EHN01520.1,
RC   ECO:0000313|Proteomes:UP000009009};
RX   PubMed=22136070; DOI=10.1111/j.1567-1364.2011.00773.x;
RA   Borneman A.R., Desany B.A., Riches D., Affourtit J.P., Forgan A.H.,
RA   Pretorius I.S., Egholm M., Chambers P.J.;
RT   "The genome sequence of the wine yeast VIN7 reveals an allotriploid hybrid
RT   genome with Saccharomyces cerevisiae and Saccharomyces kudriavzevii
RT   origins.";
RL   FEMS Yeast Res. 12:88-96(2012).
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:EHN01520.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AGVY01000290; EHN01520.1; -; Genomic_DNA.
DR   AlphaFoldDB; H0GXE4; -.
DR   HOGENOM; CLU_000288_120_1_1; -.
DR   PhylomeDB; H0GXE4; -.
DR   Proteomes; UP000009009; 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}; Kinase {ECO:0000256|ARBA:ARBA00022777};
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   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          347..602
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          603..673
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   REGION          1..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..38
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..116
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         380
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   680 AA;  76342 MW;  1BEEB9F06BC785AE CRC64;
     MYSWKSKFKF GKSKEEKEAK HSGFFHSSKK EESQNSQEIA GDHDASVTRS SLDRKGTINP
     SNSSVVPVRV SYDASSSTST VRDSNGGNLE NINSPQNLDD TANIGSTGTP NDATSSSGMM
     TIKVYNGDGF ILPFPITSSE QILNKLLASG VPPPHKEIAK EVDALIAQLS RVQLKNQGPA
     DEDLISSESA AKFIPSTIML PGSSTLNPLL YFTIEFDNTV ATIEAEYGTI ANPGFNKIST
     FDVTRKLPYL KIDVFARIPS ILLPSKSWQQ EMGVQDEKLQ AIFDKINSNQ DIHLDSFHLP
     INLSFDSAAS IRLYNHHWIT LDNGLGKINI SIDYKPSRNK PLSIDDFDLL KVIGKGSFGK
     VMQVRKKDTQ KVYALKAIRK SYIVSKSEVT HTLAERTVLA RVDCPFIVPL KFSFQSPEKL
     YFVLAFINGG ELFYHLQKEG RFDLSRARFY TAELLCALDN LHKLDVIYRD LKPENILLDY
     QGHIALCDFG LCKLNMKDDD KTDTFCGTPE YLAPELLLGL GYSKAVDWWT LGVLLYEMLT
     GLPPYYDEDV PKMYKKILQE PLVFPDGFDR DAKDLLIGLL SRDPTRRLGY NGADEIRNHP
     FFSQLSWKRL LMKGYIPPYK PAVSNSMDTS NFDEEFTREK PIDSVVDEYL SESVQKQFGG
     WTYVGNEQLG SSMVQGRSIR
//
DBGET integrated database retrieval system