FSH1_YEAST
ID FSH1_YEAST Reviewed; 243 AA.
AC P38777; D3DKZ7;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Family of serine hydrolases 1;
DE EC=3.1.-.-;
GN Name=FSH1; OrderedLocusNames=YHR049W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [2]
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 [3]
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).
RN [4]
RP FUNCTION.
RX PubMed=14645503; DOI=10.1074/mcp.m300082-mcp200;
RA Baxter S.M., Rosenblum J.S., Knutson S., Nelson M.R., Montimurro J.S.,
RA Di Gennaro J.A., Speir J.A., Burbaum J.J., Fetrow J.S.;
RT "Synergistic computational and experimental proteomics approaches for more
RT accurate detection of active serine hydrolases in yeast.";
RL Mol. Cell. Proteomics 3:209-225(2004).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=15802654; DOI=10.1110/ps.051415905;
RA Quevillon-Cheruel S., Leulliot N., Graille M., Hervouet N., Coste F.,
RA Benedetti H., Zelwer C., Janin J., Van Tilbeurgh H.;
RT "Crystal structure of yeast YHR049W/FSH1, a member of the serine hydrolase
RT family.";
RL Protein Sci. 14:1350-1356(2005).
CC -!- FUNCTION: Serine hydrolase of unknown specificity.
CC {ECO:0000269|PubMed:14645503}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 14600 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the AB hydrolase 3 family. {ECO:0000305}.
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DR EMBL; U00062; AAB68901.1; -; Genomic_DNA.
DR EMBL; AY558283; AAS56609.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06741.1; -; Genomic_DNA.
DR PIR; S46732; S46732.
DR RefSeq; NP_011915.1; NM_001179179.1.
DR PDB; 1YCD; X-ray; 1.70 A; A/B=1-243.
DR PDBsum; 1YCD; -.
DR AlphaFoldDB; P38777; -.
DR SMR; P38777; -.
DR BioGRID; 36481; 66.
DR DIP; DIP-5101N; -.
DR STRING; 4932.YHR049W; -.
DR ESTHER; yeast-FSH1; FSH1.
DR iPTMnet; P38777; -.
DR MaxQB; P38777; -.
DR PaxDb; P38777; -.
DR PRIDE; P38777; -.
DR EnsemblFungi; YHR049W_mRNA; YHR049W; YHR049W.
DR GeneID; 856445; -.
DR KEGG; sce:YHR049W; -.
DR SGD; S000001091; FSH1.
DR VEuPathDB; FungiDB:YHR049W; -.
DR eggNOG; KOG2551; Eukaryota.
DR GeneTree; ENSGT00390000003541; -.
DR HOGENOM; CLU_051938_2_3_1; -.
DR InParanoid; P38777; -.
DR OMA; FEHPGGH; -.
DR BioCyc; YEAST:G3O-31104-MON; -.
DR EvolutionaryTrace; P38777; -.
DR PRO; PR:P38777; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38777; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IBA:GO_Central.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR005645; FSH_dom.
DR Pfam; PF03959; FSH1; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Nucleus; Reference proteome;
KW Serine esterase.
FT CHAIN 1..243
FT /note="Family of serine hydrolases 1"
FT /id="PRO_0000212580"
FT ACT_SITE 110
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:15802654"
FT ACT_SITE 183
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:15802654"
FT ACT_SITE 218
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:15802654"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:1YCD"
FT HELIX 18..24
FT /evidence="ECO:0007829|PDB:1YCD"
FT HELIX 26..34
FT /evidence="ECO:0007829|PDB:1YCD"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:1YCD"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:1YCD"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:1YCD"
FT HELIX 59..67
FT /evidence="ECO:0007829|PDB:1YCD"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:1YCD"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:1YCD"
FT HELIX 87..100
FT /evidence="ECO:0007829|PDB:1YCD"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:1YCD"
FT HELIX 111..126
FT /evidence="ECO:0007829|PDB:1YCD"
FT STRAND 134..140
FT /evidence="ECO:0007829|PDB:1YCD"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:1YCD"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:1YCD"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:1YCD"
FT TURN 162..165
FT /evidence="ECO:0007829|PDB:1YCD"
FT STRAND 174..180
FT /evidence="ECO:0007829|PDB:1YCD"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:1YCD"
FT HELIX 188..201
FT /evidence="ECO:0007829|PDB:1YCD"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:1YCD"
FT TURN 206..208
FT /evidence="ECO:0007829|PDB:1YCD"
FT STRAND 209..219
FT /evidence="ECO:0007829|PDB:1YCD"
FT HELIX 224..238
FT /evidence="ECO:0007829|PDB:1YCD"
SQ SEQUENCE 243 AA; 27339 MW; C4B379487695426F CRC64;
MTVQIPKLLF LHGFLQNGKV FSEKSSGIRK LLKKANVQCD YIDAPVLLEK KDLPFEMDDE
KWQATLDADV NRAWFYHSEI SHELDISEGL KSVVDHIKAN GPYDGIVGFS QGAALSSIIT
NKISELVPDH PQFKVSVVIS GYSFTEPDPE HPGELRITEK FRDSFAVKPD MKTKMIFIYG
ASDQAVPSVR SKYLYDIYLK AQNGNKEKVL AYEHPGGHMV PNKKDIIRPI VEQITSSLQE
ASE
