YJV8_YEAST
ID YJV8_YEAST Reviewed; 196 AA.
AC P40892; D6VVX8;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Putative acetyltransferase YJL218W {ECO:0000305};
DE EC=2.3.1.-;
GN OrderedLocusNames=YJL218W; ORFNames=HRA196, J0224;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7725802; DOI=10.1002/yea.320101216;
RA Vandenbol M., Durand P., Bolle P.-A., Dion C., Portetelle D., Hilger F.;
RT "Sequence analysis of a 40.2 kb DNA fragment located near the left telomere
RT of yeast chromosome X.";
RL Yeast 10:1657-1662(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P77791}.
CC -!- INTERACTION:
CC P40892; P39940: RSP5; NbExp=2; IntAct=EBI-26263, EBI-16219;
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC {ECO:0000305}.
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DR EMBL; Z34098; CAA83992.1; -; Genomic_DNA.
DR EMBL; Z49493; CAA89515.1; -; Genomic_DNA.
DR EMBL; AY692672; AAT92691.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08594.1; -; Genomic_DNA.
DR PIR; S50709; S50709.
DR RefSeq; NP_012317.1; NM_001181651.1.
DR AlphaFoldDB; P40892; -.
DR SMR; P40892; -.
DR BioGRID; 33563; 36.
DR DIP; DIP-1828N; -.
DR IntAct; P40892; 8.
DR MINT; P40892; -.
DR STRING; 4932.YJL218W; -.
DR MaxQB; P40892; -.
DR PaxDb; P40892; -.
DR PRIDE; P40892; -.
DR EnsemblFungi; YJL218W_mRNA; YJL218W; YJL218W.
DR GeneID; 853237; -.
DR KEGG; sce:YJL218W; -.
DR SGD; S000003754; YJL218W.
DR VEuPathDB; FungiDB:YJL218W; -.
DR eggNOG; KOG4750; Eukaryota.
DR HOGENOM; CLU_051638_3_0_1; -.
DR InParanoid; P40892; -.
DR OMA; YHIHIGD; -.
DR PRO; PR:P40892; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P40892; protein.
DR GO; GO:0016407; F:acetyltransferase activity; ISS:SGD.
DR GO; GO:0008870; F:galactoside O-acetyltransferase activity; IBA:GO_Central.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR018357; Hexapep_transf_CS.
DR InterPro; IPR039369; LacA-like.
DR InterPro; IPR024688; Mac_dom.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR PANTHER; PTHR43017; PTHR43017; 1.
DR Pfam; PF14602; Hexapep_2; 1.
DR Pfam; PF12464; Mac; 1.
DR SMART; SM01266; Mac; 1.
DR SUPFAM; SSF51161; SSF51161; 1.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Reference proteome; Repeat; Transferase.
FT CHAIN 1..196
FT /note="Putative acetyltransferase YJL218W"
FT /id="PRO_0000068743"
FT ACT_SITE 114
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P07464"
FT BINDING 84
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P07464"
FT BINDING 141
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P07464"
FT BINDING 159
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P07464"
FT BINDING 164..165
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P07464"
FT BINDING 179
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P07464"
FT BINDING 182
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P07464"
FT SITE 84
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P07464"
SQ SEQUENCE 196 AA; 21480 MW; FDE9036757112E84 CRC64;
MGVLENIVPG ELYDANYDPD LLKIRKETKI KLHEYNTLSP ADENKKSQVI RELLGSCTDN
FIIEPPFYCD YGSNIYIGDN FYANHNLVIL DGAKVVIGDN VFIAPNVGIY TAGHPIDVER
RLQGLEYAMP VTIGDNVWIG GGVSIIPGVN IGKNSVIAAG SVVIRDIPEN VVAAGNPCKV
IRKITEKDST TTNYRK
