ID   IQW1_SCHPO              Reviewed;         809 AA.
AC   O94527;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=WD repeat protein iqw1;
GN   Name=iqw1; ORFNames=SPBC609.03;
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 BY MASS SPECTROMETRY, AND INTERACTION WITH DDB1.
RX   PubMed=18794354; DOI=10.1128/mcb.00757-08;
RA   Fukumoto Y., Dohmae N., Hanaoka F.;
RT   "Schizosaccharomyces pombe Ddb1 recruits substrate-specific adaptor
RT   proteins through a novel protein motif, the DDB-box.";
RL   Mol. Cell. Biol. 28:6746-6756(2008).
CC   -!- FUNCTION: Ligand-dependent coactivator of nuclear receptors that may
CC       function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein
CC       ligase complex. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with ddb1. {ECO:0000269|PubMed:18794354}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
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DR   EMBL; CU329671; CAA22832.1; -; Genomic_DNA.
DR   PIR; T40574; T40574.
DR   RefSeq; NP_596313.1; NM_001022235.2.
DR   AlphaFoldDB; O94527; -.
DR   SMR; O94527; -.
DR   BioGRID; 277636; 33.
DR   STRING; 4896.SPBC609.03.1; -.
DR   MaxQB; O94527; -.
DR   PaxDb; O94527; -.
DR   EnsemblFungi; SPBC609.03.1; SPBC609.03.1:pep; SPBC609.03.
DR   GeneID; 2541121; -.
DR   KEGG; spo:SPBC609.03; -.
DR   PomBase; SPBC609.03; iqw1.
DR   VEuPathDB; FungiDB:SPBC609.03; -.
DR   eggNOG; KOG1310; Eukaryota.
DR   HOGENOM; CLU_012381_3_1_1; -.
DR   InParanoid; O94527; -.
DR   OMA; HIYSFDI; -.
DR   PhylomeDB; O94527; -.
DR   Reactome; R-SPO-8951664; Neddylation.
DR   PRO; PR:O94527; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; ISS:PomBase.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   Gene3D; 2.130.10.10; -; 2.
DR   InterPro; IPR045151; DCAF8.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR15574; PTHR15574; 1.
DR   Pfam; PF00400; WD40; 2.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE   1: Evidence at protein level;
KW   Cytoplasm; Reference proteome; Repeat; WD repeat.
FT   CHAIN           1..809
FT                   /note="WD repeat protein iqw1"
FT                   /id="PRO_0000316550"
FT   REPEAT          43..82
FT                   /note="WD 1"
FT   REPEAT          87..128
FT                   /note="WD 2"
FT   REPEAT          141..180
FT                   /note="WD 3"
FT   REPEAT          193..233
FT                   /note="WD 4"
FT   REPEAT          241..295
FT                   /note="WD 5"
FT   REPEAT          668..708
FT                   /note="WD 6"
FT   REPEAT          711..750
FT                   /note="WD 7"
FT   REGION          599..644
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        609..636
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   809 AA;  92499 MW;  4877443546BD057E CRC64;
     MSGISLSLRQ LDYRDWFQRK ISRDIYGNST WLTGIDLQKE LTGHTGCVNT LDWSADGEFL
     LSGSDDTRLI VWDVFNEYKP RHLISTGHVQ NIFSAKFVPY SNNRQILSAS GDKLIKLFDL
     DSSKEGGMDH GMETQTRCWS CALDSVKNIV PCDNGHTFLV CSEDGTARQY DIREPHVCNQ
     DLDCPSILVN YNPYRINLYT ITMSPSNPYY FAIGGTHPYA FLYDRRMVKK SFRDDWTMNT
     SPEKDCRCVR KFSPDGSCNS QGILDRYITC CQFSAANPNE LLVSWNSDYV YLFHVHEDKS
     YTPTFNKIED SNKKPSKPSL LQTQPLKRKN YSPWYKNNFG ASTPASRVSR NPYTAAQPRK
     HTFYQMYENI EKFFTTENGG LYESIVSGRL SHFSRSIQYV KDAIYFLENY NYIPDSNGLN
     HSIRVSALRY WRACVSILAL MDDTVSLEPN TIIQAGWGWL YDFMNWVTRY LLGISDHWAL
     QMSPPTNVAR QNFVLCDPDE PSRVLFSNPS EMIRAFARID TNDLSSVRRF FWIHKVLRGC
     LLLISSDIYW EQFQPWDSST SDVTSSQRLD DENGFLTLLE PPVNYENEVE SSSGENIVSM
     YTGHSDLNDD DDDYQDEESY SYASDDDDES DEDSDEGPTL LSLRMKKRKA VEPNVPVNTH
     VKSYYGHCNV ESIKNVNFYG QNDEYVMSGS DDGRFFIWDK LNASILAIIH GDSEAVNVIE
     GHPRCPTLAV SGIDSTVKIF NTENTPPSGC SRNHTSNSYK IIATNEMNRQ QGSRDSYITS
     RMLSHLAYRA HLDDGFGHEV LDTDACSIM