ID   FUN19_YEAST             Reviewed;         413 AA.
AC   P28003; D6VPI4;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 3.
DT   27-MAR-2024, entry version 158.
DE   RecName: Full=SWIRM domain-containing protein FUN19;
GN   Name=FUN19; OrderedLocusNames=YAL034C;
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].
RX   PubMed=1583694; DOI=10.1016/0022-2836(92)91025-k;
RA   Harris S.D., Cheng J., Pugh T.A., Pringle J.R.;
RT   "Molecular analysis of Saccharomyces cerevisiae chromosome I. On the number
RT   of genes and the identification of essential genes using temperature-
RT   sensitive-lethal mutations.";
RL   J. Mol. Biol. 225:53-65(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA   Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA   Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA   Storms R.K.;
RT   "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
RN   [3]
RP   SEQUENCE REVISION.
RA   Vo D.T.;
RL   Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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   [5]
RP   IDENTIFICATION OF PROBABLE INITIATION SITE.
RX   PubMed=12748633; DOI=10.1038/nature01644;
RA   Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT   "Sequencing and comparison of yeast species to identify genes and
RT   regulatory elements.";
RL   Nature 423:241-254(2003).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-194; SER-207 AND SER-211, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- MISCELLANEOUS: FUN19 is a non-essential gene.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC04998.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAA44456.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; X62577; CAA44456.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; U12980; AAC04998.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BK006935; DAA06954.1; -; Genomic_DNA.
DR   PIR; S23410; S23410.
DR   RefSeq; NP_009368.2; NM_001180035.1.
DR   AlphaFoldDB; P28003; -.
DR   SMR; P28003; -.
DR   BioGRID; 31732; 132.
DR   DIP; DIP-6766N; -.
DR   IntAct; P28003; 26.
DR   MINT; P28003; -.
DR   STRING; 4932.YAL034C; -.
DR   iPTMnet; P28003; -.
DR   MaxQB; P28003; -.
DR   PaxDb; 4932-YAL034C; -.
DR   PeptideAtlas; P28003; -.
DR   TopDownProteomics; P28003; -.
DR   EnsemblFungi; YAL034C_mRNA; YAL034C; YAL034C.
DR   GeneID; 851199; -.
DR   KEGG; sce:YAL034C; -.
DR   AGR; SGD:S000002134; -.
DR   SGD; S000002134; FUN19.
DR   VEuPathDB; FungiDB:YAL034C; -.
DR   eggNOG; ENOG502R6VN; Eukaryota.
DR   GeneTree; ENSGT00940000176451; -.
DR   HOGENOM; CLU_042442_0_0_1; -.
DR   InParanoid; P28003; -.
DR   OMA; YRYATHG; -.
DR   OrthoDB; 1380889at2759; -.
DR   BioCyc; YEAST:G3O-28891-MONOMER; -.
DR   BioGRID-ORCS; 851199; 1 hit in 10 CRISPR screens.
DR   PRO; PR:P28003; -.
DR   Proteomes; UP000002311; Chromosome I.
DR   RNAct; P28003; Protein.
DR   GO; GO:1990483; C:Clr6 histone deacetylase complex I''; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0070210; C:Rpd3L-Expanded complex; IBA:GO_Central.
DR   GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR   GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR   GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR007526; SWIRM.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR12374:SF21; SWIRM DOMAIN-CONTAINING PROTEIN FUN19-RELATED; 1.
DR   PANTHER; PTHR12374; TRANSCRIPTIONAL ADAPTOR 2 ADA2 -RELATED; 1.
DR   Pfam; PF04433; SWIRM; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   PROSITE; PS50934; SWIRM; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..413
FT                   /note="SWIRM domain-containing protein FUN19"
FT                   /id="PRO_0000202417"
FT   DOMAIN          316..413
FT                   /note="SWIRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00247"
FT   REGION          35..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          189..211
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          249..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..211
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        252..271
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         194
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         207
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         211
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   CONFLICT        255
FT                   /note="T -> S (in Ref. 1; CAA44456)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        369
FT                   /note="L -> S (in Ref. 1)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   413 AA;  47068 MW;  B588358DBCF7A9AB CRC64;
     MGLYSPESEK SQLNMNYIGK DDSQSIFRRL NQNLKASNNN NDSNKNGLNM SDYSNNSPYG
     RSYDVRINQN SQNNGNGCFS GSIDSLVDEH IIPSPPLSPK LESKISHNGS PRMASSVLVG
     STPKGAVENV LFVKPVWPNG LSRKRYRYAT YGFLSQYKIF SNLAQPYSKN IINRYNNLAY
     NARHKYSKYN DDMTPPPLPS SSSRLPSPLA SPNLNRQARY NMRKQALYNN NLGKFESDTE
     WIPRKRKVYS PQRRTMTTSP HRAKKFSPSA STPHTNIASI EAIHDAPQYI PNVSWKKLPD
     YSPPLSTLPT DSNKSLKIEW KGSPMDLSTD PLRNELHPAE LVLAQTLRLP CDLYLDSKRR
     LFLEKVYRLK KGLPFRRTDA QKACRIDVNK ASRLFQAFEK VGWLQDSNFT KYL
//