SNU13_SCHPO
ID SNU13_SCHPO Reviewed; 125 AA.
AC O74690;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=13 kDa ribonucleoprotein-associated protein;
GN Name=snu13; ORFNames=SPAC607.03c;
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 [GENOMIC DNA].
RA Stiefel J., Hoffman C.S.;
RT "Fission yeast RS6/L7A ribosomal protein homolog rph1.";
RL Submitted (AUG-1998) 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 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).
CC -!- FUNCTION: Common component of the spliceosome and rRNA processing
CC machinery. In association with the spliceosomal U4/U6.U5 tri-snRNP
CC particle, required for splicing of pre-mRNA. In association with box
CC C/D snoRNPs, required for processing of pre-ribosomal RNA (rRNA) and
CC site-specific 2'-O-methylation of substrate RNAs. Essential for the
CC accumulation and stability of U4 snRNA, U6 snRNA, and box C/D snoRNAs
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the U3 snoRNP particle. Binds to the C'/D and B/C
CC motifs in U3 snoRNA. Component of the 25S U4/U6.U5 tri-snRNP particle,
CC a subcomplex of the spliceosome. Binds to the 5' stem-loop of U4 snRNA
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL8 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF087136; AAC62085.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB63790.1; -; Genomic_DNA.
DR PIR; T50223; T50223.
DR RefSeq; NP_593592.1; NM_001019023.2.
DR AlphaFoldDB; O74690; -.
DR SMR; O74690; -.
DR BioGRID; 279116; 10.
DR STRING; 4896.SPAC607.03c.1; -.
DR MaxQB; O74690; -.
DR PaxDb; O74690; -.
DR EnsemblFungi; SPAC607.03c.1; SPAC607.03c.1:pep; SPAC607.03c.
DR GeneID; 2542663; -.
DR KEGG; spo:SPAC607.03c; -.
DR PomBase; SPAC607.03c; snu13.
DR VEuPathDB; FungiDB:SPAC607.03c; -.
DR eggNOG; KOG3387; Eukaryota.
DR HOGENOM; CLU_084513_4_1_1; -.
DR InParanoid; O74690; -.
DR OMA; KPFYVRF; -.
DR PhylomeDB; O74690; -.
DR Reactome; R-SPO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-SPO-72165; mRNA Splicing - Minor Pathway.
DR PRO; PR:O74690; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0031428; C:box C/D RNP complex; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; HDA:PomBase.
DR GO; GO:0071011; C:precatalytic spliceosome; IBA:GO_Central.
DR GO; GO:0032040; C:small-subunit processome; ISO:PomBase.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; ISO:PomBase.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0000470; P:maturation of LSU-rRNA; IBA:GO_Central.
DR GO; GO:0030490; P:maturation of SSU-rRNA; ISO:PomBase.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; ISO:PomBase.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR Gene3D; 3.30.1330.30; -; 1.
DR InterPro; IPR002415; H/ACA_rnp_Nhp2-like.
DR InterPro; IPR029064; L30e-like.
DR InterPro; IPR004038; Ribosomal_L7Ae/L30e/S12e/Gad45.
DR InterPro; IPR018492; Ribosomal_L7Ae/L8/Nhp2.
DR InterPro; IPR004037; Ribosomal_L7Ae_CS.
DR Pfam; PF01248; Ribosomal_L7Ae; 1.
DR PRINTS; PR00881; L7ARS6FAMILY.
DR PRINTS; PR00883; NUCLEARHMG.
DR SUPFAM; SSF55315; SSF55315; 1.
DR PROSITE; PS01082; RIBOSOMAL_L7AE; 1.
PE 3: Inferred from homology;
KW mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW Ribonucleoprotein; Ribosome biogenesis; RNA-binding; rRNA processing;
KW Spliceosome.
FT CHAIN 1..125
FT /note="13 kDa ribonucleoprotein-associated protein"
FT /id="PRO_0000290662"
SQ SEQUENCE 125 AA; 13535 MW; AAE05D2194DAEB9C CRC64;
MSVNPKAFPL ADSGLTQQIL DLVQQASHYK QLRKGANEAT KTLNRGISEF IVMAADTEPI
EILLHLPLLC EDKNVPYVFV PSKAALGRAC GVSRPVISAS ITTNEASDLL PQIQAIKLAI
EKLLI
