SGF73_YEAST
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 03-AUG-2022, entry version 176.
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 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 SMR; P53165; -.
DR BioGRID; 33181; 711.
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; P53165; -.
DR PRIDE; P53165; -.
DR EnsemblFungi; YGL066W_mRNA; YGL066W; YGL066W.
DR GeneID; 852814; -.
DR KEGG; sce:YGL066W; -.
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 BioCyc; YEAST:G3O-30571-MON; -.
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:0016573; P:histone acetylation; IDA:ComplexPortal.
DR GO; GO:0016578; P:histone deubiquitination; IMP:SGD.
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 InterPro; IPR013243; SCA7_dom.
DR InterPro; IPR037804; SGF73.
DR InterPro; IPR041251; Znf_C2H2_13.
DR PANTHER; PTHR47805; PTHR47805; 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
