YTM1_SCHPO
ID YTM1_SCHPO Reviewed; 440 AA.
AC Q9URY0;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Ribosome biogenesis protein ytm1 {ECO:0000255|HAMAP-Rule:MF_03029};
GN Name=ytm1; ORFNames=SPAC890.04c;
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 [MRNA].
RC STRAIN=972 / ATCC 24843;
RA Matsumoto S.;
RT "Schizosaccharomyces pombe homolog of the Saccharomyces cerevisiae YTM1.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-140 AND SER-242, AND
RP IDENTIFICATION BY 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_03029}.
CC -!- SUBUNIT: Component of the NOP7 complex, composed of erb1, ppp1/nop7 and
CC ytm1. The complex is held together by erb1, which interacts with
CC ppp1/nop7 via its N-terminal domain and with ytm1 via a high-affinity
CC interaction between the seven-bladed beta-propeller domains of the 2
CC proteins. The NOP7 complex associates with the 66S pre-ribosome.
CC Interacts (via UBL domain) with mdn1 (via VWFA/MIDAS domain).
CC {ECO:0000255|HAMAP-Rule:MF_03029}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000255|HAMAP-
CC Rule:MF_03029}. Nucleus, nucleoplasm {ECO:0000255|HAMAP-Rule:MF_03029}.
CC -!- SIMILARITY: Belongs to the WD repeat WDR12/YTM1 family.
CC {ECO:0000255|HAMAP-Rule:MF_03029}.
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DR EMBL; AF237708; AAF40218.1; -; mRNA.
DR EMBL; CU329670; CAB63495.1; -; Genomic_DNA.
DR PIR; T50260; T50260.
DR RefSeq; NP_594822.1; NM_001020251.2.
DR AlphaFoldDB; Q9URY0; -.
DR SMR; Q9URY0; -.
DR BioGRID; 279966; 8.
DR STRING; 4896.SPAC890.04c.1; -.
DR iPTMnet; Q9URY0; -.
DR MaxQB; Q9URY0; -.
DR PaxDb; Q9URY0; -.
DR PRIDE; Q9URY0; -.
DR EnsemblFungi; SPAC890.04c.1; SPAC890.04c.1:pep; SPAC890.04c.
DR GeneID; 2543549; -.
DR KEGG; spo:SPAC890.04c; -.
DR PomBase; SPAC890.04c; ytm1.
DR VEuPathDB; FungiDB:SPAC890.04c; -.
DR eggNOG; KOG0313; Eukaryota.
DR HOGENOM; CLU_000288_57_0_1; -.
DR InParanoid; Q9URY0; -.
DR OMA; VDCTRTK; -.
DR PhylomeDB; Q9URY0; -.
DR Reactome; R-SPO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:Q9URY0; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000785; C:chromatin; HDA:PomBase.
DR GO; GO:0005730; C:nucleolus; IDA: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; IEA:UniProtKB-UniRule.
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); IEA:UniProtKB-UniRule.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 1.
DR HAMAP; MF_03029; WDR12; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR012972; NLE.
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 InterPro; IPR028599; WDR12/Ytm1.
DR Pfam; PF08154; NLE; 1.
DR Pfam; PF00400; WD40; 3.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Ribosome biogenesis;
KW rRNA processing; WD repeat.
FT CHAIN 1..440
FT /note="Ribosome biogenesis protein ytm1"
FT /id="PRO_0000051465"
FT REPEAT 102..139
FT /note="WD 1"
FT REPEAT 141..180
FT /note="WD 2"
FT REPEAT 195..234
FT /note="WD 3"
FT REPEAT 267..306
FT /note="WD 4"
FT REPEAT 308..347
FT /note="WD 5"
FT REPEAT 353..393
FT /note="WD 6"
FT REPEAT 403..440
FT /note="WD 7"
FT REGION 11..90
FT /note="Ubiquitin-like (UBL) domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03029"
FT MOD_RES 140
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 440 AA; 48334 MW; 825FDB62CDAFA1D8 CRC64;
MDAQSAPSGQ VQVRFTTRNE DLAVGDTPIF VPTSLKRYGL SQIVNHLLKT EKPTPFDFLV
QGQLLKTTLD EYIVQNGLST ESILDIEYIQ STLPPAYLAS FSHDDWISGI QLTSDTILTS
SYDGIARVWD KSGEIKFQST GCGSSLKSAS WHIPNQSFLT ASLDQKIFHW VIEEPESMLD
AEKKSSGILQ TLFVGHKDIV ERVRSLESSS VFISASADNT VGIWDFERSP ETTLESFSSS
ISKKRRRKNA EFTPQAGARS PLILCEGHTG PVMDIVFSDD PSVAYSVGQD HTIKTWDLIT
GQNVDSKITK APLLCVEKLT DLHLVICGSS ARHIVVHDPR AGSDKIVSHT LSGHKNLVSG
LSASPENPYM FASVSHDNTC RVWDVRATSG SIYTISRAEK TGSQWDKLFA VDWNKSIGIV
TGGTDKQLQI NQSSSFGKSE
