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ERB1_SCHPO
ID   ERB1_SCHPO              Reviewed;         740 AA.
AC   O74399;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 2.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=Ribosome biogenesis protein erb1 {ECO:0000255|HAMAP-Rule:MF_03027};
DE   AltName: Full=Eukaryotic ribosome biogenesis protein 1 {ECO:0000255|HAMAP-Rule:MF_03027};
GN   Name=erb1; ORFNames=SPBC4F6.13c;
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   REVISION OF GENE MODEL.
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
RN   [3]
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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-434, 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: Component of the NOP7 complex, which is required for
CC       maturation of the 25S and 5.8S ribosomal RNAs and formation of the 60S
CC       ribosome. {ECO:0000255|HAMAP-Rule:MF_03027}.
CC   -!- SUBUNIT: Component of the NOP7 complex, composed of erb1, ppp1/nop7 and
CC       ytm1/SPAC890.04c. The complex is held together by erb1, which interacts
CC       with ppp1/nop7 via its N-terminal domain and with ytm1/SPAC890.04c via
CC       a high-affinity interaction between the seven-bladed beta-propeller
CC       domains of the 2 proteins. The NOP7 complex associates with the 66S
CC       pre-ribosome. {ECO:0000255|HAMAP-Rule:MF_03027}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000255|HAMAP-
CC       Rule:MF_03027, ECO:0000269|PubMed:16823372}. Nucleus, nucleoplasm
CC       {ECO:0000255|HAMAP-Rule:MF_03027}.
CC   -!- SIMILARITY: Belongs to the WD repeat BOP1/ERB1 family.
CC       {ECO:0000255|HAMAP-Rule:MF_03027}.
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DR   EMBL; CU329671; CAA20733.2; -; Genomic_DNA.
DR   PIR; T40510; T40510.
DR   RefSeq; NP_596113.2; NM_001022030.2.
DR   AlphaFoldDB; O74399; -.
DR   SMR; O74399; -.
DR   BioGRID; 277405; 5.
DR   STRING; 4896.SPBC4F6.13c.1; -.
DR   iPTMnet; O74399; -.
DR   MaxQB; O74399; -.
DR   PaxDb; O74399; -.
DR   PRIDE; O74399; -.
DR   EnsemblFungi; SPBC4F6.13c.1; SPBC4F6.13c.1:pep; SPBC4F6.13c.
DR   GeneID; 2540888; -.
DR   KEGG; spo:SPBC4F6.13c; -.
DR   PomBase; SPBC4F6.13c; erb1.
DR   VEuPathDB; FungiDB:SPBC4F6.13c; -.
DR   eggNOG; KOG0650; Eukaryota.
DR   HOGENOM; CLU_011390_0_1_1; -.
DR   InParanoid; O74399; -.
DR   OMA; MRPAKGE; -.
DR   Reactome; R-SPO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   PRO; PR:O74399; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005730; C:nucleolus; HDA:PomBase.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0070545; C:PeBoW complex; ISO:PomBase.
DR   GO; GO:0030687; C:preribosome, large subunit precursor; IBA:GO_Central.
DR   GO; GO:0043021; F:ribonucleoprotein complex binding; IBA:GO_Central.
DR   GO; GO:0000466; P:maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:UniProtKB-UniRule.
DR   GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR   Gene3D; 2.130.10.10; -; 1.
DR   HAMAP; MF_03027; BOP1; 1.
DR   InterPro; IPR028598; BOP1/Erb1.
DR   InterPro; IPR012953; BOP1_N_dom.
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; PTHR17605; PTHR17605; 1.
DR   Pfam; PF08145; BOP1NT; 1.
DR   Pfam; PF00400; WD40; 2.
DR   SMART; SM01035; BOP1NT; 1.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 2.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE   1: Evidence at protein level;
KW   Nucleus; Phosphoprotein; Reference proteome; Repeat; Ribosome biogenesis;
KW   rRNA processing; WD repeat.
FT   CHAIN           1..740
FT                   /note="Ribosome biogenesis protein erb1"
FT                   /id="PRO_0000316569"
FT   REPEAT          381..420
FT                   /note="WD 1"
FT   REPEAT          526..568
FT                   /note="WD 2"
FT   REPEAT          571..609
FT                   /note="WD 3"
FT   REPEAT          612..651
FT                   /note="WD 4"
FT   REPEAT          655..694
FT                   /note="WD 5"
FT   REPEAT          710..740
FT                   /note="WD 6"
FT   REGION          1..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          251..304
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..34
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..60
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..104
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        251..279
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         434
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   740 AA;  82945 MW;  D352AF12C7A1D0BE CRC64;
     METGMNRKRS RSKRANSNVG VEKDKEKEKS KGVSNVPNEV ETESSSHEPS FKKDVDEEIP
     SLTAELSEEE EGEYSSESGR STPELSPDDF EDADDEEEFE EIDAGYSSDS STEDVAPGLY
     ESPYDENLYI NYDIDGKKIT RPATPAALDS LIASIDKDKG WTGIVDPMTG KPVNLTTEEL
     GLLKRLAQSE IPDENFDPYP DYDDFFTNTV RETPLSSAPE PKRRFAPSKH EQKRILQLAY
     AIRKGRILTS EQRAERERES QSNYADHDLW ADDDQATVNQ RKLDYAPAPK LPPPSHEESY
     NPPEEYLKQS SDFPKKYKSL RVVPAYSNLI KEKFERCLDL YLAPRVRRTK LNIDPESLLP
     KLPTPSELRP FPTRCTNVFI GHKGRVRCLS VHVSGNWLAS GGDDGVLRIW EVMTGRCVWK
     CSLDSFGNAH NIDSDEDAVN ESLSHSTKSS IIQSLAWGPL SDSPVLAVAV DETVYFITPP
     IFSDEQIEAS KELFTSAPYQ ESSAIWRRGA KQSLQLHGGI VHATVSTPSS IKSLSWHRRG
     DYLATSSPTS SSQAVLIHQL SRGASQSPFS KSKGSVQAVT FHPTMPYLLV ATQRYVRIYN
     LVKQELVKTL LTGVKWVSSL SVHSSGDHVI IGSYDKRLCW FDLDFSSKPY KNLRYHSRAL
     RDVSYHPSLP LFCSGSDDGD VQVFHGRVYS DLLANPLIVP LKILRNHKVV DNVGVLSTCW
     HPKEAWLFSA GAGGEIRMWT
 
 
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