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Database: UniProt
Entry: Q9UTR9
LinkDB: Q9UTR9
Original site: Q9UTR9 
ID   ASA1_SCHPO              Reviewed;         368 AA.
AC   Q9UTR9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 141.
DE   RecName: Full=ASTRA-associated protein 1;
GN   Name=asa1; ORFNames=SPAC1006.02;
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).
RN   [3]
RP   IDENTIFICATION IN THE ASTRA COMPLEX, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=19040720; DOI=10.1186/gb-2008-9-11-r167;
RA   Shevchenko A., Roguev A., Schaft D., Buchanan L., Habermann B., Sakalar C.,
RA   Thomas H., Krogan N.J., Shevchenko A., Stewart A.F.;
RT   "Chromatin Central: towards the comparative proteome by accurate mapping of
RT   the yeast proteomic environment.";
RL   Genome Biol. 9:R167.1-R167.22(2008).
CC   -!- FUNCTION: Component of the ASTRA complex probably involved in chromatin
CC       remodeling.
CC   -!- SUBUNIT: Component of the ASTRA chromatin-remodeling machinery complex.
CC       {ECO:0000269|PubMed:19040720}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the WD repeat ASA1 family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB60232.1; -; Genomic_DNA.
DR   RefSeq; NP_594849.1; NM_001020278.2.
DR   AlphaFoldDB; Q9UTR9; -.
DR   SMR; Q9UTR9; -.
DR   BioGRID; 279683; 1.
DR   IntAct; Q9UTR9; 1.
DR   MINT; Q9UTR9; -.
DR   STRING; 284812.Q9UTR9; -.
DR   SwissPalm; Q9UTR9; -.
DR   MaxQB; Q9UTR9; -.
DR   PaxDb; 4896-SPAC1006-02-1; -.
DR   EnsemblFungi; SPAC1006.02.1; SPAC1006.02.1:pep; SPAC1006.02.
DR   GeneID; 2543255; -.
DR   KEGG; spo:SPAC1006.02; -.
DR   PomBase; SPAC1006.02; asa1.
DR   VEuPathDB; FungiDB:SPAC1006.02; -.
DR   eggNOG; KOG0322; Eukaryota.
DR   HOGENOM; CLU_041940_0_1_1; -.
DR   InParanoid; Q9UTR9; -.
DR   OMA; NSLCFQE; -.
DR   PhylomeDB; Q9UTR9; -.
DR   PRO; PR:Q9UTR9; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0110078; C:TTT Hsp90 cochaperone complex; IDA:PomBase.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR19854:SF1; GUANINE NUCLEOTIDE-BINDING PROTEIN SUBUNIT BETA-LIKE PROTEIN 1; 1.
DR   PANTHER; PTHR19854; TRANSDUCIN BETA-LIKE 3; 1.
DR   Pfam; PF00400; WD40; 2.
DR   SMART; SM00320; WD40; 5.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE   1: Evidence at protein level;
KW   Chromatin regulator; Cytoplasm; Nucleus; Reference proteome; Repeat;
KW   WD repeat.
FT   CHAIN           1..368
FT                   /note="ASTRA-associated protein 1"
FT                   /id="PRO_0000316564"
FT   REPEAT          12..50
FT                   /note="WD 1"
FT   REPEAT          53..91
FT                   /note="WD 2"
FT   REPEAT          246..283
FT                   /note="WD 3"
FT   REPEAT          294..333
FT                   /note="WD 4"
FT   REPEAT          336..368
FT                   /note="WD 5"
SQ   SEQUENCE   368 AA;  40846 MW;  6BBB7C670E80A0EB CRC64;
     MVVPTPFYVL RGHSSSVTSV LFDANEYLYS GDEAGFVICW CLTSMRPKCA WRAHTKTILG
     MQIVKGGALC THGRDCRLVT WKIDFNCMTD NFMSLSKLAE LQNYGPEASS ETEKSSAFIS
     IHSNIVVNSL TFCPFSYSPQ SKIVVLCNTL NFEELDVYDD ESLYHPQTHK EDCGKRLQTR
     IQPEESVGKT GSVMSTSVTV TDEKYVLLAA GYESGHVVQY ICSLENVKTV TLDFKAVWKM
     VYAYKSHSQP VLSVEYAGSK LFSTGADDCI CLHPTPSSIA DDLGSLPHPI FRKTKHCGQQ
     NIRIRSDNKI LATAGWDGRG RVYSCQTLAP LAVLKYHSDG INSLAFHPGS NVIALASKDT
     RISLWKLY
//
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