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RIA1_SCHPO
ID   RIA1_SCHPO              Reviewed;        1000 AA.
AC   O74945;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Ribosome assembly protein 1;
DE            EC=3.6.5.-;
DE   AltName: Full=EF-2 like GTPase;
DE   AltName: Full=Elongation factor-like 1;
GN   Name=ria1; ORFNames=SPCC553.08c;
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).
CC   -!- FUNCTION: GTPase involved in the biogenesis of the 60S ribosomal
CC       subunit and translational activation of ribosomes. Together with sdo1,
CC       may trigger the GTP-dependent release of tif6 from 60S pre-ribosomes in
CC       the cytoplasm, thereby activating ribosomes for translation competence
CC       by allowing 80S ribosome assembly and facilitating tif6 recycling to
CC       the nucleus, where it is required for 60S rRNA processing and nuclear
CC       export. Inhibits GTPase activity of ribosome-bound EF-2 (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC   -!- ACTIVITY REGULATION: GTPase activity is stimulated in the presence of
CC       60S subunits. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01059}.
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DR   EMBL; CU329672; CAA19260.1; -; Genomic_DNA.
DR   PIR; T41396; T41396.
DR   RefSeq; NP_587766.1; NM_001022759.2.
DR   AlphaFoldDB; O74945; -.
DR   SMR; O74945; -.
DR   BioGRID; 275861; 30.
DR   STRING; 4896.SPCC553.08c.1; -.
DR   MaxQB; O74945; -.
DR   PaxDb; O74945; -.
DR   PRIDE; O74945; -.
DR   EnsemblFungi; SPCC553.08c.1; SPCC553.08c.1:pep; SPCC553.08c.
DR   GeneID; 2539293; -.
DR   KEGG; spo:SPCC553.08c; -.
DR   PomBase; SPCC553.08c; ria1.
DR   VEuPathDB; FungiDB:SPCC553.08c; -.
DR   eggNOG; KOG0467; Eukaryota.
DR   HOGENOM; CLU_002794_3_1_1; -.
DR   InParanoid; O74945; -.
DR   OMA; ERFARCE; -.
DR   PhylomeDB; O74945; -.
DR   PRO; PR:O74945; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; ISM:PomBase.
DR   GO; GO:0003924; F:GTPase activity; ISO:PomBase.
DR   GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR   GO; GO:0042256; P:mature ribosome assembly; IBA:GO_Central.
DR   GO; GO:0042254; P:ribosome biogenesis; ISO:PomBase.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR041095; EFG_II.
DR   InterPro; IPR035647; EFG_III/V.
DR   InterPro; IPR000640; EFG_V-like.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   Pfam; PF00679; EFG_C; 1.
DR   Pfam; PF14492; EFG_III; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SMART; SM00838; EFG_C; 1.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF54980; SSF54980; 2.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; GTP-binding; Hydrolase; Nucleotide-binding; Reference proteome;
KW   Ribosome biogenesis.
FT   CHAIN           1..1000
FT                   /note="Ribosome assembly protein 1"
FT                   /id="PRO_0000315632"
FT   DOMAIN          17..246
FT                   /note="tr-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   BINDING         26..33
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         100..104
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         154..157
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1000 AA;  112129 MW;  E0B3624D52560702 CRC64;
     MPVIPPEKLV SLQKNQENIR NFTLLAHVDH GKTTLADSLL ASNGIISSKL AGTVRFLDFR
     EDEITRGITM KSSAISLFFK VISQNDEKRV EKDYLINLID SPGHVDFSSE VSSASRLCDG
     AFVLVDAVEG VCSQTITVLR QAWIDRIKVI LVINKMDRLI TELKLSPIEA HYHLLRLVEQ
     VNAVIGTFYT GELMQLADND EVISDEGIYF APEQGNVVFA SAYDGWAFCL DQFSEFYEKK
     LGLKQKALTK CLWGDYYLDP KTKRVLQPKH LQGRRLKPMF VQFVLENLWA VYESAVSNRN
     LENIEKIIKA LNIKVLPRDI KSKDPRNLLL AIFQQWLPLS TAILLTAIRE IPSPINAQAN
     RARKVLSSTP HYEMIDPDIT LAMESCDASK EQPVLVYISK MVAFSERDLP NHRRKQLSAE
     EMKLIRSKLS ESIESGINTI SIEENVSSTN SDNLEGSTTD MDDDKDILIG FARIYSGTIS
     VGQEVYVYGP KYDPVNPEKH ITKVTVESLY LMMGQELVYL ETVPAGNVFA IGGLAGTVLR
     TATLCSSPNG PNLVGVTQQM EPIVRVALEP VRPFEMNKLV TGLDMLNQAD PCVQIAVEEN
     GEHVIMCAGE IHLERCLKDL RERFAKIEIQ ASQPLVPYRE TTIATPDLLA KNKELSIGFV
     TATLPVGGVT IGITVTPLSG SVVDFLLKHS KTIENVSSNF SKKNRNVVVS ESLTKSMEEV
     LTPEKFYERL SKLLEEENSD LGELKNHLDS IIAFGPKRVG PNILFDKTKK MRDFRRQSDE
     TKLIPSDLSE YVVTAFQLIT HQGPLCAEPV QGICVSIDQF DISDDSEDSK LLTINNPQIP
     GQVISVVKES IRHGFLGWSP RLMLAMYSCD VQATSEVLGR VYGVVSKRRG RVIDEEMKEG
     TPFFIVKALI PVVESFGFAV EILKRTSGAA YPQLIFHGFE MLDENPFWVP TTEEELEDLG
     ELADRENIAK RYMLNVRKRK GLLVEQKIVE KAEKQRTLKH
 
 
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