ID   SGF73_YEAST             Reviewed;         657 AA.
AC   P53165; D6VU75;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 184.
DE   RecName: Full=SAGA-associated factor 73;
DE   AltName: Full=73 kDa SAGA-associated factor;
DE   AltName: Full=SAGA histone acetyltransferase complex 73 kDa subunit;
GN   Name=SGF73; OrderedLocusNames=YGL066W;
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=9290212;
RX   DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA   Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT   "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT   chromosome VII.";
RL   Yeast 13:1077-1090(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 115-657.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9234674;
RX   DOI=10.1002/(sici)1097-0061(199707)13:9<861::aid-yea125>3.0.co;2-9;
RA   Feuermann M., de Montigny J., Potier S., Souciet J.-L.;
RT   "The characterization of two new clusters of duplicated genes suggests a
RT   'Lego' organization of the yeast Saccharomyces cerevisiae chromosomes.";
RL   Yeast 13:861-869(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
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 IN THE SAGA COMPLEX.
RX   PubMed=12052880; DOI=10.1128/mcb.22.13.4723-4738.2002;
RA   Sanders S.L., Jennings J., Canutescu A., Link A.J., Weil P.A.;
RT   "Proteomics of the eukaryotic transcription machinery: identification of
RT   proteins associated with components of yeast TFIID by multidimensional mass
RT   spectrometry.";
RL   Mol. Cell. Biol. 22:4723-4738(2002).
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   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   [8]
RP   IDENTIFICATION BY 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).
RN   [9]
RP   3D-STRUCTURE MODELING OF THE SAGA COMPLEX.
RX   PubMed=15260971; DOI=10.1016/j.molcel.2004.06.005;
RA   Wu P.Y., Ruhlmann C., Winston F., Schultz P.;
RT   "Molecular architecture of the S. cerevisiae SAGA complex.";
RL   Mol. Cell 15:199-208(2004).
CC   -!- FUNCTION: Functions as a component of the transcription regulatory
CC       histone acetylation (HAT) complex SAGA. SAGA is involved in RNA
CC       polymerase II-dependent transcriptional regulation of approximately 10%
CC       of yeast genes. At the promoters, SAGA is required for recruitment of
CC       the basal transcription machinery. It influences RNA polymerase II
CC       transcriptional activity through different activities such as TBP
CC       interaction (SPT3, SPT8 and SPT20) and promoter selectivity,
CC       interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1),
CC       and chromatin modification through histone acetylation (GCN5) and
CC       deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some
CC       extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts
CC       with DNA via upstream activating sequences (UASs).
CC   -!- SUBUNIT: Component of the 1.8 MDa SAGA complex, which consists of at
CC       least of TRA1, CHD1, SPT7, TAF5, ADA3, SGF73, SPT20/ADA5, SPT8, TAF12,
CC       TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10, TAF9, SGF11 and
CC       SUS1. TAF5, TAF6, TAF9, TAF19, TAF12 and ADA1 seem to be present in 2
CC       copies. SAGA is built of 5 distinct domains with specialized functions.
CC       Domain I (containing TRA1) probably represents the activator
CC       interaction surface. Domain II (containing TAF5 and TAF6, and probably
CC       TAF9 and TAF10), domain III (containing GCN5, TAF10, SPT7, TAF5 and
CC       ADA1, and probably ADA2, ADA3 and TAF12), and domain IV (containing
CC       HFI1/ADA1 and TAF6, and probably TAF9) are believed to play primarily
CC       an architectural role. Domain III also harbors the HAT activity. Domain
CC       V (containing SPT3 and SPT20, and probably SPT8) represents the TBP-
CC       interacting module, which may be associated transiently with SAGA.
CC       {ECO:0000269|PubMed:12052880}.
CC   -!- INTERACTION:
CC       P53165; P50875: SPT20; NbExp=7; IntAct=EBI-23812, EBI-17751;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- MISCELLANEOUS: Present with 486 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the ataxin-7 family. {ECO:0000305}.
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DR   EMBL; Z72588; CAA96770.1; -; Genomic_DNA.
DR   EMBL; Z72587; CAA96769.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08036.1; -; Genomic_DNA.
DR   PIR; S64073; S64073.
DR   RefSeq; NP_011449.1; NM_001180931.1.
DR   PDB; 2LO3; NMR; -; A=59-102.
DR   PDB; 3M99; X-ray; 2.70 A; D=1-104.
DR   PDB; 3MHH; X-ray; 2.45 A; E=1-96.
DR   PDB; 3MHS; X-ray; 1.89 A; E=1-96.
DR   PDB; 4FIP; X-ray; 2.69 A; D/H=1-96.
DR   PDB; 4FJC; X-ray; 2.83 A; D/H=1-96.
DR   PDB; 4FK5; X-ray; 2.03 A; E=1-96.
DR   PDB; 4W4U; X-ray; 2.80 A; E/H=1-96.
DR   PDB; 4WA6; X-ray; 2.36 A; E/H=1-96.
DR   PDB; 4ZUX; X-ray; 3.82 A; Y/d/i/n=1-104.
DR   PDB; 6AQR; X-ray; 2.10 A; E=1-96.
DR   PDB; 6T9I; EM; 3.90 A; Q=1-657.
DR   PDB; 6T9K; EM; 3.30 A; Q=1-657.
DR   PDB; 6T9L; EM; 3.60 A; N=1-657.
DR   PDBsum; 2LO3; -.
DR   PDBsum; 3M99; -.
DR   PDBsum; 3MHH; -.
DR   PDBsum; 3MHS; -.
DR   PDBsum; 4FIP; -.
DR   PDBsum; 4FJC; -.
DR   PDBsum; 4FK5; -.
DR   PDBsum; 4W4U; -.
DR   PDBsum; 4WA6; -.
DR   PDBsum; 4ZUX; -.
DR   PDBsum; 6AQR; -.
DR   PDBsum; 6T9I; -.
DR   PDBsum; 6T9K; -.
DR   PDBsum; 6T9L; -.
DR   AlphaFoldDB; P53165; -.
DR   BMRB; P53165; -.
DR   EMDB; EMD-10412; -.
DR   EMDB; EMD-10414; -.
DR   EMDB; EMD-10415; -.
DR   SMR; P53165; -.
DR   BioGRID; 33181; 718.
DR   ComplexPortal; CPX-656; SAGA complex.
DR   ComplexPortal; CPX-675; SLIK (SAGA-like) complex.
DR   DIP; DIP-5211N; -.
DR   IntAct; P53165; 95.
DR   MINT; P53165; -.
DR   STRING; 4932.YGL066W; -.
DR   iPTMnet; P53165; -.
DR   MaxQB; P53165; -.
DR   PaxDb; 4932-YGL066W; -.
DR   PeptideAtlas; P53165; -.
DR   EnsemblFungi; YGL066W_mRNA; YGL066W; YGL066W.
DR   GeneID; 852814; -.
DR   KEGG; sce:YGL066W; -.
DR   AGR; SGD:S000003034; -.
DR   SGD; S000003034; SGF73.
DR   VEuPathDB; FungiDB:YGL066W; -.
DR   eggNOG; KOG4140; Eukaryota.
DR   GeneTree; ENSGT00940000173477; -.
DR   HOGENOM; CLU_032226_0_0_1; -.
DR   InParanoid; P53165; -.
DR   OMA; GRSLTCK; -.
DR   OrthoDB; 1385477at2759; -.
DR   BioCyc; YEAST:G3O-30571-MONOMER; -.
DR   BioGRID-ORCS; 852814; 2 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; P53165; -.
DR   PRO; PR:P53165; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P53165; Protein.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0071819; C:DUBm complex; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0000124; C:SAGA complex; IDA:SGD.
DR   GO; GO:0046695; C:SLIK (SAGA-like) complex; IPI:SGD.
DR   GO; GO:0008047; F:enzyme activator activity; IDA:SGD.
DR   GO; GO:0005198; F:structural molecule activity; IMP:SGD.
DR   GO; GO:0006325; P:chromatin organization; IMP:SGD.
DR   GO; GO:0006338; P:chromatin remodeling; IEA:GOC.
DR   GO; GO:0006406; P:mRNA export from nucleus; IMP:SGD.
DR   GO; GO:0045899; P:positive regulation of RNA polymerase II transcription preinitiation complex assembly; IMP:SGD.
DR   GO; GO:0065003; P:protein-containing complex assembly; IMP:SGD.
DR   GO; GO:0046822; P:regulation of nucleocytoplasmic transport; IDA:SGD.
DR   GO; GO:1905634; P:regulation of protein localization to chromatin; IDA:SGD.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR   GO; GO:1904802; P:RITS complex assembly; IBA:GO_Central.
DR   Gene3D; 6.10.140.670; -; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR   InterPro; IPR013243; SCA7_dom.
DR   InterPro; IPR037804; SGF73.
DR   InterPro; IPR041251; Znf_C2H2_13.
DR   PANTHER; PTHR47805; SAGA-ASSOCIATED FACTOR 73; 1.
DR   PANTHER; PTHR47805:SF1; SAGA-ASSOCIATED FACTOR 73; 1.
DR   Pfam; PF08313; SCA7; 1.
DR   Pfam; PF18508; zf_C2H2_13; 1.
DR   PROSITE; PS51505; SCA7; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..657
FT                   /note="SAGA-associated factor 73"
FT                   /id="PRO_0000202764"
FT   DOMAIN          220..286
FT                   /note="SCA7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00838"
FT   REGION          98..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          287..353
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          469..532
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          572..636
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        119..133
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        135..162
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        168..211
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        287..312
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        316..353
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   STRAND          7..11
FT                   /evidence="ECO:0007829|PDB:4FK5"
FT   HELIX           13..18
FT                   /evidence="ECO:0007829|PDB:3MHS"
FT   TURN            19..22
FT                   /evidence="ECO:0007829|PDB:4FJC"
FT   STRAND          28..30
FT                   /evidence="ECO:0007829|PDB:4FJC"
FT   HELIX           32..35
FT                   /evidence="ECO:0007829|PDB:3MHS"
FT   HELIX           36..41
FT                   /evidence="ECO:0007829|PDB:3MHS"
FT   STRAND          47..49
FT                   /evidence="ECO:0007829|PDB:3MHS"
FT   HELIX           51..57
FT                   /evidence="ECO:0007829|PDB:3MHS"
FT   STRAND          70..72
FT                   /evidence="ECO:0007829|PDB:3MHS"
FT   STRAND          76..78
FT                   /evidence="ECO:0007829|PDB:3MHS"
FT   TURN            79..81
FT                   /evidence="ECO:0007829|PDB:3MHS"
FT   STRAND          84..86
FT                   /evidence="ECO:0007829|PDB:4FK5"
FT   HELIX           87..89
FT                   /evidence="ECO:0007829|PDB:3MHS"
FT   TURN            90..92
FT                   /evidence="ECO:0007829|PDB:3MHS"
FT   HELIX           354..365
FT                   /evidence="ECO:0007829|PDB:6T9K"
FT   HELIX           382..397
FT                   /evidence="ECO:0007829|PDB:6T9K"
FT   TURN            410..412
FT                   /evidence="ECO:0007829|PDB:6T9K"
FT   STRAND          420..422
FT                   /evidence="ECO:0007829|PDB:6T9K"
SQ   SEQUENCE   657 AA;  72878 MW;  4618E2E47824321D CRC64;
     MRSGDAEIKG IKPKVIEEYS LSQGSGPSND SWKSLMSSAK DTPLQYDHMN RESLKKYFNP
     NAQLIEDPLD KPIQYRVCEK CGKPLALTAI VDHLENHCAG ASGKSSTDPR DESTRETIRN
     GVESTGRNNN DDDNSNDNNN DDDDDDDNDD NEDDDDADDD DDNSNGANYK KNDSSFNPLK
     RSTSMESANT PNMDTKRSKT GTPQTFSSSI KKQKKVKQRN PTEKHLIDFN KQCGVELPEG
     GYCARSLTCK SHSMGAKRAV SGRSKPYDVL LADYHREHQT KIGAAAEKRA KQQELQKLQK
     QIQKEQKKHT QQQKQGQRSK QRNVNGGKSA KNGGKSTVHN GNNINEIGHV NLTPEEETTQ
     VLNGVSRSFP LPLESTVLSS VRYRTKYFRM REMFASSFSV KPGYTSPGYG AIHSRVGCLD
     LDRTTDYKFR VRTPQPINHL TNQNLNPKQI QRLQQQRALQ AQLLSQQQQQ QQQQQQHHSP
     QAQAQASTQQ PTQGMVPNHF PGGATNSSFN ANVSSKQIQQ QQQQQQHKSQ DTGLTPLEIQ
     SQQQKLRQQQ LQQQKFEAAA SYLANATKLM QESNQDSHLS GTHNNNSSKN GNNNLMTMKA
     SISSPNTSVN SIQSPPSVNS VNGSGQGVST GINVSGNNGR IEVGIGNSVN PYNGRIN
//