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 27-MAR-2024, entry version 155.
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; 284812.O74945; -.
DR MaxQB; O74945; -.
DR PaxDb; 4896-SPCC553-08c-1; -.
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; FARCDIQ; -.
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; IBA:GO_Central.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0042256; P:cytosolic ribosome assembly; IBA:GO_Central.
DR GO; GO:0042254; P:ribosome biogenesis; ISO:PomBase.
DR CDD; cd01681; aeEF2_snRNP_like_IV; 1.
DR CDD; cd04096; eEF2_snRNP_like_C; 1.
DR CDD; cd01885; EF2; 1.
DR CDD; cd16268; EF2_II; 1.
DR CDD; cd16261; EF2_snRNP_III; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.240; -; 1.
DR Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR041095; EFG_II.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_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 NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR42908:SF3; ELONGATION FACTOR-LIKE GTPASE 1; 1.
DR PANTHER; PTHR42908; TRANSLATION ELONGATION FACTOR-RELATED; 1.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF14492; EFG_III; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SMART; SM00838; EFG_C; 1.
DR SUPFAM; SSF54980; EF-G C-terminal domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF50447; Translation proteins; 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
//
