WDR59_SCHPO
ID WDR59_SCHPO Reviewed; 1323 AA.
AC O13686;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Uncharacterized RWD, RING finger and WD repeat-containing protein C11E3.05;
GN ORFNames=SPAC11E3.05;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: May be involved in telomere capping. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the WD repeat WDR59 family. {ECO:0000305}.
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DR EMBL; CU329670; CAB11184.1; -; Genomic_DNA.
DR PIR; T37533; T37533.
DR RefSeq; NP_594930.1; NM_001020361.2.
DR AlphaFoldDB; O13686; -.
DR SMR; O13686; -.
DR BioGRID; 278367; 3.
DR STRING; 4896.SPAC11E3.05.1; -.
DR iPTMnet; O13686; -.
DR MaxQB; O13686; -.
DR PaxDb; O13686; -.
DR PRIDE; O13686; -.
DR EnsemblFungi; SPAC11E3.05.1; SPAC11E3.05.1:pep; SPAC11E3.05.
DR GeneID; 2541877; -.
DR KEGG; spo:SPAC11E3.05; -.
DR PomBase; SPAC11E3.05; -.
DR VEuPathDB; FungiDB:SPAC11E3.05; -.
DR eggNOG; KOG0309; Eukaryota.
DR HOGENOM; CLU_001497_3_0_1; -.
DR InParanoid; O13686; -.
DR OMA; HDACIPF; -.
DR PhylomeDB; O13686; -.
DR PRO; PR:O13686; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000329; C:fungal-type vacuole membrane; ISO:PomBase.
DR GO; GO:1990130; C:GATOR1 complex; IMP:PomBase.
DR GO; GO:0061700; C:GATOR2 complex; IPI:PomBase.
DR GO; GO:0035859; C:Seh1-associated complex; IMP:PomBase.
DR GO; GO:0005774; C:vacuolar membrane; EXP:PomBase.
DR GO; GO:0035591; F:signaling adaptor activity; IPI:PomBase.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISM:PomBase.
DR GO; GO:0008270; F:zinc ion binding; ISM:PomBase.
DR GO; GO:0034198; P:cellular response to amino acid starvation; IBA:GO_Central.
DR GO; GO:1904262; P:negative regulation of TORC1 signaling; IMP:PomBase.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IBA:GO_Central.
DR GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR006575; RWD-domain.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR SMART; SM00591; RWD; 1.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50908; RWD; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; WD repeat; Zinc;
KW Zinc-finger.
FT CHAIN 1..1323
FT /note="Uncharacterized RWD, RING finger and WD repeat-
FT containing protein C11E3.05"
FT /id="PRO_0000310741"
FT REPEAT 271..314
FT /note="WD 1"
FT REPEAT 320..360
FT /note="WD 2"
FT REPEAT 364..403
FT /note="WD 3"
FT REPEAT 409..449
FT /note="WD 4"
FT REPEAT 453..494
FT /note="WD 5"
FT REPEAT 502..551
FT /note="WD 6"
FT DOMAIN 671..779
FT /note="RWD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00179"
FT ZN_FING 1265..1309
FT /note="RING-type; degenerate"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 879..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1323 AA; 149063 MW; 610D4590AA78BF69 CRC64;
MRELQGDDSS RKSPPSDSVV KNSSPIDYEH SLKSLQDERT LNYPNKQFNS ENPSSYYNMD
DSGELCNFEL EKDSLESMIH ESSTALSAQS NTAQDGDQLA SSSTISKDHS ETLDNKLNDS
KILIKKASNS FANFSESVRS STIVAYSQTP TQRLQGLTSI SSSSFDDGSY GSRRISFNSQ
GVSGRLRRNM DSTVIIPSED EDLQLPSNSN SNVEYGPFDS TTFDRQLSIE VNQPVGAMSL
SPCGRDIALA SRYGLLVLDL DNPYNPPRML RHSTPWEVAD TQWNVHAARD QWVVSTSSQK
TIVWNLALPN DRAIEFMLHG HTRAVTDMNW HRQNPDVLAT CSIDSSVHCW DLRSPRFPVN
SFYDWHNGAT QVKWNYKNPH ILASSHGRLV RIWDDRYGSA PLHTIKTSEN ITKINGLEFN
RACETRLLTC AMDRTVKFWN YEKSTEEPEH LITTDSPVWK ARFTPFGDGV ILMPQRGDNS
VHMYDCRNLD KEGPRAVHRF AGHTDQVKEF LWRCRGEDVF DRDLRDFQLI TWSKDHHVRL
WPIGNDILNS MGHDRTKPVP FKLTRLGAKY RTYSREPLKQ SLINTECDSS DAMNSFDSNF
GAERANTSDL SRGFVAFANR KKSKYNLPGS SGFMTRSTKS TNPMTPLNWL RGISMGRLGN
ADWEVPQNLG EELSWIGQKY SNVSFEKIDV AERTCTISLN APILPDDGYA YIRLHVYFPN
NYPISATPVF QLERSSAFND EQFNYVFNTL TSISDQCISS HKYCMDACLS YLSGNLSVDE
IWKLGFQKDN SDSSSESSAD IFQDVFPSMP DFRGGDRGLS HKHQNIPLPK TCAAIFCGND
ELVCFFTIKA DESAAQATAN RETHGRQKLF ESFGVLDSSN SVADSDSTNY DDENSLNRGG
TSESDSEFIW DVDESNSGSI VFPKSKTSIN LNNINSASAS IMGSRFGAAD IFMSKRPSTK
GSNRPSILLS KPSHDFHVVR IISMSKYLPV KRALAAEYVV DTGDKVTVCN KNAEVSAKHN
YYRLAKVWLM LGRLLGHLSR TENKDHINDE EAFPWLKSPL AKWVVNSLLD YYASQCNTQM
LAMLACVLDI PNPKKQSGNT SADQVLFNQP KQVTEKLGVQ LNLPKTKILE KVSSHSLAQI
TALREKEPKD ADSTYSKEKI FSATSTVHLQ LMDYDKQNND FVDAQEIAYT KLLQQKFIQW
RATYAEQLDL WGFFIPKLEM LKFNAHEFSS PSEKTLVNHC NSCNSTTSNT RICEKCYSLV
PRMSCTFCCL SIHGLCIVCG LCLHVMHEDC YKEWFSNGDS ISQSCSSGCG CKCQFQHMSL
EKV
