SGF73_SCHPO
ID SGF73_SCHPO Reviewed; 344 AA.
AC O94397;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=SAGA-associated factor 73;
GN Name=sgf73; ORFNames=SPCC126.04c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Functions as component of the transcription regulatory
CC histone acetylation (HAT) complex SAGA. At the promoters, SAGA is
CC required for recruitment of the basal transcription machinery. It
CC influences RNA polymerase II transcriptional activity through different
CC activities such as TBP interaction and promoter selectivity,
CC interaction with transcription activators, and chromatin modification
CC through histone acetylation and deubiquitination. SAGA acetylates
CC nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac
CC and H3K23ac). SAGA interacts with DNA via upstream activating sequences
CC (UASs). Sgf11 is involved in transcriptional regulation of a subset of
CC SAGA-regulated genes and is required for histone H2B deubiquitination
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the SAGA complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the ataxin-7 family. {ECO:0000305}.
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DR EMBL; CU329672; CAA22473.1; -; Genomic_DNA.
DR PIR; T40908; T40908.
DR RefSeq; NP_588447.1; NM_001023438.2.
DR AlphaFoldDB; O94397; -.
DR SMR; O94397; -.
DR BioGRID; 275352; 254.
DR IntAct; O94397; 2.
DR MINT; O94397; -.
DR STRING; 4896.SPCC126.04c.1; -.
DR iPTMnet; O94397; -.
DR MaxQB; O94397; -.
DR PaxDb; O94397; -.
DR PRIDE; O94397; -.
DR EnsemblFungi; SPCC126.04c.1; SPCC126.04c.1:pep; SPCC126.04c.
DR GeneID; 2538769; -.
DR KEGG; spo:SPCC126.04c; -.
DR PomBase; SPCC126.04c; sgf73.
DR VEuPathDB; FungiDB:SPCC126.04c; -.
DR eggNOG; KOG4140; Eukaryota.
DR HOGENOM; CLU_044734_0_0_1; -.
DR InParanoid; O94397; -.
DR OMA; MQVTGTI; -.
DR PhylomeDB; O94397; -.
DR PRO; PR:O94397; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0000124; C:SAGA complex; IDA:PomBase.
DR GO; GO:0031048; P:heterochromatin assembly by small RNA; IMP:PomBase.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:GOC.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; EXP:PomBase.
DR GO; GO:1904802; P:RITS complex assembly; IMP:PomBase.
DR InterPro; IPR013243; SCA7_dom.
DR InterPro; IPR037804; SGF73.
DR PANTHER; PTHR47805; PTHR47805; 1.
DR Pfam; PF08313; SCA7; 1.
DR PROSITE; PS51505; SCA7; 1.
PE 3: Inferred from homology;
KW Nucleus; Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..344
FT /note="SAGA-associated factor 73"
FT /id="PRO_0000343136"
FT DOMAIN 190..256
FT /note="SCA7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00838"
FT REGION 123..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 344 AA; 38581 MW; C4ACEEEF10DD5AA1 CRC64;
MLTEQQTLEL FPENWERNEQ VLLKYPDGLP KDVLADQRVD NTESQVKDEI TSNITNQTQI
LLPADSFPQY GSYPNNSELD YVVCTKCDRP FLSEYIEDHH SSCNGIKPPK PQFEPVANSQ
VLNKDVNNGN NAPIKNGVKS TAKGSAGNHE KNSVNGQKNP EMPPKRRKTE ENKKPTKSAL
PKKEASKKKN PKVKGPVDVE KQCGVLLPNG QMCARSLTCK THSMSSKRAV PGRSQPYDVL
LAACQKKNQV KIQRQILETA KESEDNQHQA PVDSDEEVSF IMNVLQKSGN QPLEQKVFLP
VKRRHSYFRT RELIAAAFRH GEQGMQVTGT ILGRVIPFSA RQPL
