TSR1_YEAST
ID TSR1_YEAST Reviewed; 788 AA.
AC Q07381; D6VRT6; Q03128;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Ribosome biogenesis protein TSR1;
DE AltName: Full=20S rRNA accumulation protein 1;
GN Name=TSR1; OrderedLocusNames=YDL060W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 570-788.
RX PubMed=8769646; DOI=10.1101/gad.10.16.2025;
RA Bai Y., Symington L.S.;
RT "A Rad52 homolog is required for RAD51-independent mitotic recombination in
RT Saccharomyces cerevisiae.";
RL Genes Dev. 10:2025-2037(1996).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11565749; DOI=10.1017/s1355838201013073;
RA Gelperin D., Horton L., Beckman J., Hensold J., Lemmon S.K.;
RT "Bms1p, a novel GTP-binding protein, and the related Tsr1p are required for
RT distinct steps of 40S ribosome biogenesis in yeast.";
RL RNA 7:1268-1283(2001).
RN [5]
RP FUNCTION, INTERACTION WITH RIO2, AND SUBCELLULAR LOCATION.
RX PubMed=12628929; DOI=10.1093/emboj/cdg121;
RA Schaefer T., Strauss D., Petfalski E., Tollervey D., Hurt E.;
RT "The path from nucleolar 90S to cytoplasmic 40S pre-ribosomes.";
RL EMBO J. 22:1370-1380(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15167894; DOI=10.1038/sj.emboj.7600252;
RA Leger-Silvestre I., Milkereit P., Ferreira-Cerca S., Saveanu C.,
RA Rousselle J.-C., Choesmel V., Guinefoleau C., Gas N., Gleizes P.-E.;
RT "The ribosomal protein Rps15p is required for nuclear exit of the 40S
RT subunit precursors in yeast.";
RL EMBO J. 23:2336-2347(2004).
RN [8]
RP FUNCTION.
RX PubMed=16159874; DOI=10.1074/jbc.m506916200;
RA Leger-Silvestre I., Caffrey J.M., Dawaliby R., Alvarez-Arias D.A., Gas N.,
RA Bertolone S.J., Gleizes P.E., Ellis S.R.;
RT "Specific role for yeast homologs of the Diamond Blackfan anemia-associated
RT Rps19 protein in ribosome synthesis.";
RL J. Biol. Chem. 280:38177-38185(2005).
CC -!- FUNCTION: Required for 40S ribosomal subunit synthesis. Required for
CC normal export of the pre-40S particles from the nucleus to the
CC cytoplasm. Its subcellular location and association with pre-40S
CC subunitshifts from mixed cytoplasm/nucleus to all nuclear in RPS19
CC disruptions, suggesting it acts after the ribosomal protein.
CC {ECO:0000269|PubMed:11565749, ECO:0000269|PubMed:12628929,
CC ECO:0000269|PubMed:15167894, ECO:0000269|PubMed:16159874}.
CC -!- SUBUNIT: Interacts with RIO2. {ECO:0000269|PubMed:12628929}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus.
CC -!- MISCELLANEOUS: Present with 1390 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Bms1-like GTPase family. TSR1 subfamily. {ECO:0000305}.
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DR EMBL; Z74108; CAA98623.1; -; Genomic_DNA.
DR EMBL; U53668; AAB66661.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11796.1; -; Genomic_DNA.
DR PIR; S67595; S67595.
DR RefSeq; NP_010223.1; NM_001180119.1.
DR PDB; 5IW7; X-ray; 3.60 A; A/B/C/D=46-409, A/B/C/D=477-788.
DR PDB; 5WWN; X-ray; 2.81 A; A=80-788.
DR PDB; 6EML; EM; 3.60 A; t=1-788.
DR PDB; 6FAI; EM; 3.40 A; k=1-788.
DR PDB; 6RBD; EM; 3.47 A; k=1-788.
DR PDB; 6WDR; EM; 3.70 A; k=1-788.
DR PDB; 6Y7C; EM; 3.80 A; t=1-788.
DR PDBsum; 5IW7; -.
DR PDBsum; 5WWN; -.
DR PDBsum; 6EML; -.
DR PDBsum; 6FAI; -.
DR PDBsum; 6RBD; -.
DR PDBsum; 6WDR; -.
DR PDBsum; 6Y7C; -.
DR AlphaFoldDB; Q07381; -.
DR SMR; Q07381; -.
DR BioGRID; 31998; 186.
DR DIP; DIP-6294N; -.
DR IntAct; Q07381; 40.
DR MINT; Q07381; -.
DR STRING; 4932.YDL060W; -.
DR iPTMnet; Q07381; -.
DR MaxQB; Q07381; -.
DR PaxDb; Q07381; -.
DR PRIDE; Q07381; -.
DR EnsemblFungi; YDL060W_mRNA; YDL060W; YDL060W.
DR GeneID; 851499; -.
DR KEGG; sce:YDL060W; -.
DR SGD; S000002218; TSR1.
DR VEuPathDB; FungiDB:YDL060W; -.
DR eggNOG; KOG1980; Eukaryota.
DR GeneTree; ENSGT00940000153195; -.
DR HOGENOM; CLU_009858_1_0_1; -.
DR InParanoid; Q07381; -.
DR OMA; KTPHQQV; -.
DR BioCyc; YEAST:G3O-29476-MON; -.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:Q07381; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q07381; protein.
DR GO; GO:0030686; C:90S preribosome; HDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0030688; C:preribosome, small subunit precursor; IDA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; IDA:SGD.
DR GO; GO:0034511; F:U3 snoRNA binding; IBA:GO_Central.
DR GO; GO:0000479; P:endonucleolytic cleavage of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0000461; P:endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR InterPro; IPR012948; AARP2CN.
DR InterPro; IPR039761; Bms1/Tsr1.
DR InterPro; IPR007034; BMS1_TSR1_C.
DR InterPro; IPR030387; G_Bms1/Tsr1_dom.
DR PANTHER; PTHR12858; PTHR12858; 1.
DR Pfam; PF08142; AARP2CN; 1.
DR Pfam; PF04950; RIBIOP_C; 1.
DR SMART; SM00785; AARP2CN; 1.
DR SMART; SM01362; DUF663; 1.
DR PROSITE; PS51714; G_BMS1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Nucleus; Reference proteome; Ribosome biogenesis.
FT CHAIN 1..788
FT /note="Ribosome biogenesis protein TSR1"
FT /id="PRO_0000065671"
FT DOMAIN 82..248
FT /note="Bms1-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01051"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 51..72
FT /evidence="ECO:0007829|PDB:6FAI"
FT STRAND 84..92
FT /evidence="ECO:0007829|PDB:5WWN"
FT HELIX 97..106
FT /evidence="ECO:0007829|PDB:5WWN"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:6FAI"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:5WWN"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:6RBD"
FT STRAND 123..127
FT /evidence="ECO:0007829|PDB:5WWN"
FT TURN 129..132
FT /evidence="ECO:0007829|PDB:6FAI"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:5WWN"
FT HELIX 145..153
FT /evidence="ECO:0007829|PDB:5WWN"
FT STRAND 156..162
FT /evidence="ECO:0007829|PDB:5WWN"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:5WWN"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:5WWN"
FT HELIX 173..182
FT /evidence="ECO:0007829|PDB:5WWN"
FT STRAND 187..193
FT /evidence="ECO:0007829|PDB:5WWN"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:5WWN"
FT HELIX 202..217
FT /evidence="ECO:0007829|PDB:5WWN"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:5WWN"
FT HELIX 232..244
FT /evidence="ECO:0007829|PDB:5WWN"
FT HELIX 251..254
FT /evidence="ECO:0007829|PDB:5WWN"
FT STRAND 256..260
FT /evidence="ECO:0007829|PDB:5WWN"
FT STRAND 262..268
FT /evidence="ECO:0007829|PDB:5WWN"
FT STRAND 270..284
FT /evidence="ECO:0007829|PDB:5WWN"
FT STRAND 291..295
FT /evidence="ECO:0007829|PDB:5WWN"
FT TURN 296..298
FT /evidence="ECO:0007829|PDB:5WWN"
FT STRAND 299..307
FT /evidence="ECO:0007829|PDB:5WWN"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:6FAI"
FT HELIX 353..356
FT /evidence="ECO:0007829|PDB:6FAI"
FT TURN 375..377
FT /evidence="ECO:0007829|PDB:6FAI"
FT STRAND 393..395
FT /evidence="ECO:0007829|PDB:6FAI"
FT HELIX 398..401
FT /evidence="ECO:0007829|PDB:6FAI"
FT TURN 402..404
FT /evidence="ECO:0007829|PDB:6FAI"
FT HELIX 466..481
FT /evidence="ECO:0007829|PDB:5WWN"
FT STRAND 484..486
FT /evidence="ECO:0007829|PDB:6FAI"
FT STRAND 490..492
FT /evidence="ECO:0007829|PDB:6FAI"
FT HELIX 494..497
FT /evidence="ECO:0007829|PDB:5WWN"
FT TURN 498..500
FT /evidence="ECO:0007829|PDB:5WWN"
FT HELIX 507..509
FT /evidence="ECO:0007829|PDB:5WWN"
FT STRAND 514..516
FT /evidence="ECO:0007829|PDB:6FAI"
FT HELIX 523..527
FT /evidence="ECO:0007829|PDB:6FAI"
FT HELIX 534..547
FT /evidence="ECO:0007829|PDB:5WWN"
FT STRAND 556..564
FT /evidence="ECO:0007829|PDB:5WWN"
FT HELIX 565..567
FT /evidence="ECO:0007829|PDB:5WWN"
FT TURN 568..570
FT /evidence="ECO:0007829|PDB:5WWN"
FT TURN 574..576
FT /evidence="ECO:0007829|PDB:5WWN"
FT STRAND 580..583
FT /evidence="ECO:0007829|PDB:5WWN"
FT TURN 586..589
FT /evidence="ECO:0007829|PDB:5WWN"
FT STRAND 590..600
FT /evidence="ECO:0007829|PDB:5WWN"
FT STRAND 609..612
FT /evidence="ECO:0007829|PDB:6FAI"
FT STRAND 614..618
FT /evidence="ECO:0007829|PDB:5WWN"
FT STRAND 621..625
FT /evidence="ECO:0007829|PDB:5WWN"
FT STRAND 628..630
FT /evidence="ECO:0007829|PDB:5WWN"
FT STRAND 638..645
FT /evidence="ECO:0007829|PDB:5WWN"
FT STRAND 648..650
FT /evidence="ECO:0007829|PDB:5WWN"
FT STRAND 652..659
FT /evidence="ECO:0007829|PDB:5WWN"
FT STRAND 666..672
FT /evidence="ECO:0007829|PDB:5WWN"
FT STRAND 679..691
FT /evidence="ECO:0007829|PDB:5WWN"
FT STRAND 696..711
FT /evidence="ECO:0007829|PDB:5WWN"
FT STRAND 714..720
FT /evidence="ECO:0007829|PDB:5WWN"
FT HELIX 724..729
FT /evidence="ECO:0007829|PDB:5WWN"
FT TURN 730..732
FT /evidence="ECO:0007829|PDB:5WWN"
FT STRAND 735..737
FT /evidence="ECO:0007829|PDB:5WWN"
FT TURN 738..740
FT /evidence="ECO:0007829|PDB:6FAI"
FT STRAND 742..749
FT /evidence="ECO:0007829|PDB:5WWN"
FT TURN 750..753
FT /evidence="ECO:0007829|PDB:5WWN"
FT STRAND 754..761
FT /evidence="ECO:0007829|PDB:5WWN"
FT STRAND 769..777
FT /evidence="ECO:0007829|PDB:5WWN"
FT STRAND 782..784
FT /evidence="ECO:0007829|PDB:6RBD"
SQ SEQUENCE 788 AA; 90748 MW; 71BA5461E8A858C7 CRC64;
MAGHSHRSSL KNGHKSYKSK HASKGALKRL YKGKVEKEPV GTGKPDKQVS KLQRKNKAKQ
LRAQRILDSI ENRKLFEGKN GAAKIITIVP LVNDLDPLDI LYKLLKCADD EGIMVQEVDS
KRIFNVHIKK FKSNLKIIIP DMTNFLNILD CAKVADFVVF GLSGVQEVDE EFGEQIIRAL
ELQGIASYIG VISNLSAVHE KEKFQLDVKQ SLESYFKHFF PSEERVYNLE KNSDALNVLR
TLCQRLPRSI NWRDNRGYVV ADFVDFVETS PDSGDLVIEG TVRGIGFNAN RLVHIPDFGD
FQLNKIEKIS ESSQKRKIIK EKATDSLSLE LDLQTVFESN MNRDTLDEYA PEGTEDWSDY
DEDFEYDGLT TARYDDHGFL PGREQTSKKA AVPKGTSDYQ AKWYLDDVID ANEEEEAEQT
NGKDETMMEI DDEMMVEQDN EEVAGDEEYD IEDNEGFEEL SPEEEERQLR EFRDMEKEDR
EFPDEIELEP SESAIERLKR YRGLKNLYNC DWQVDEKDPS SPAEWKRLLR IGNYKNTKNR
IIKETKNEAQ AIAGDRIRMF IRFPKFLLEK IQDPKQLLFA VYGLLLHEHK NAVVNFSLQR
WEQYDKPVPS QEPIVVQYGV RRYTIQPLFS QGSNSPNNVH KYERFLHPDT VSVATCIAPV
DFTQSPAIFF KPSPTDAKNI ELIGHGTFLN ADHSRILAKR AILTGHPFRF HKTVVTVRYM
FFRPEDVEWF KSIPLFTKSG RSGFIKESLG THGYFKATFD GKLSAQDVVA MSLYKRMWPM
PSLPWNGM
