TSR3_YEAST
ID TSR3_YEAST Reviewed; 313 AA.
AC Q12094; D6W272;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=18S rRNA aminocarboxypropyltransferase {ECO:0000305};
DE EC=2.5.1.- {ECO:0000269|PubMed:27084949};
DE AltName: Full=20S rRNA accumulation protein 3 {ECO:0000303|PubMed:27084949};
DE Short=ScTsr3 {ECO:0000303|PubMed:27084949};
GN Name=TSR3 {ECO:0000255|HAMAP-Rule:MF_03146, ECO:0000303|PubMed:27084949};
GN OrderedLocusNames=YOR006C; ORFNames=UND313;
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 [GENOMIC DNA].
RX PubMed=8896276;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1091::aid-yea22>3.0.co;2-i;
RA Sterky F., Holmberg A., Pettersson B., Uhlen M.;
RT "The sequence of a 30 kb fragment on the left arm of chromosome XV from
RT Saccharomyces cerevisiae reveals 15 open reading frames, five of which
RT correspond to previously identified genes.";
RL Yeast 12:1091-1095(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
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 [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [7]
RP FUNCTION.
RX PubMed=19806183; DOI=10.1371/journal.pbio.1000213;
RA Li Z., Lee I., Moradi E., Hung N.J., Johnson A.W., Marcotte E.M.;
RT "Rational extension of the ribosome biogenesis pathway using network-guided
RT genetics.";
RL PLoS Biol. 7:E1000213-E1000213(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-286 AND SER-289, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF ARG-60; SER-62; LYS-65; GLU-111 AND ARG-131.
RX PubMed=27084949; DOI=10.1093/nar/gkw244;
RA Meyer B., Wurm J.P., Sharma S., Immer C., Pogoryelov D., Koetter P.,
RA Lafontaine D.L., Woehnert J., Entian K.D.;
RT "Ribosome biogenesis factor Tsr3 is the aminocarboxypropyl transferase
RT responsible for 18S rRNA hypermodification in yeast and humans.";
RL Nucleic Acids Res. 44:4304-4316(2016).
CC -!- FUNCTION: Aminocarboxypropyltransferase that catalyzes the
CC aminocarboxypropyl transfer on pseudouridine at position 1191 (Psi1191)
CC in 18S rRNA (PubMed:27084949). It constitutes the last step in
CC biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-
CC carboxypropyl) pseudouridine (m1acp3-Psi) conserved in eukaryotic 18S
CC rRNA (PubMed:27084949). Required for processing 35S pre-rRNA at site D
CC (PubMed:19806183). {ECO:0000269|PubMed:19806183,
CC ECO:0000269|PubMed:27084949}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(1)-methylpseudouridine(1191) in yeast 18S rRNA + S-adenosyl-
CC L-methionine = H(+) + N(1)-methyl-N(3)-[(3S)-3-amino-3-
CC carboxypropyl]pseudouridine(1191) in yeast 18S rRNA + S-methyl-5'-
CC thioadenosine; Xref=Rhea:RHEA:63300, Rhea:RHEA-COMP:13852, Rhea:RHEA-
CC COMP:16309, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74890, ChEBI:CHEBI:146234; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03146, ECO:0000269|PubMed:27084949};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63301;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03146,
CC ECO:0000269|PubMed:27084949};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03146,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:27084949}. Nucleus
CC {ECO:0000255|HAMAP-Rule:MF_03146, ECO:0000269|PubMed:14562095}.
CC -!- DISRUPTION PHENOTYPE: Minor growth defect caused by late 18S rRNA
CC processing defects, leading to a ribosomal subunit imbalance with a
CC reduced 40S to 60S ratio. {ECO:0000269|PubMed:27084949}.
CC -!- MISCELLANEOUS: Present with 3610 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TDD superfamily. TSR3 family.
CC {ECO:0000255|HAMAP-Rule:MF_03146}.
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DR EMBL; U43491; AAC49486.1; -; Genomic_DNA.
DR EMBL; Z74914; CAA99194.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10788.1; -; Genomic_DNA.
DR PIR; S61990; S61990.
DR RefSeq; NP_014648.1; NM_001183425.1.
DR AlphaFoldDB; Q12094; -.
DR SMR; Q12094; -.
DR BioGRID; 34409; 141.
DR DIP; DIP-1251N; -.
DR IntAct; Q12094; 6.
DR MINT; Q12094; -.
DR STRING; 4932.YOR006C; -.
DR iPTMnet; Q12094; -.
DR MaxQB; Q12094; -.
DR PaxDb; Q12094; -.
DR PRIDE; Q12094; -.
DR EnsemblFungi; YOR006C_mRNA; YOR006C; YOR006C.
DR GeneID; 854167; -.
DR KEGG; sce:YOR006C; -.
DR SGD; S000005532; TSR3.
DR VEuPathDB; FungiDB:YOR006C; -.
DR eggNOG; KOG3154; Eukaryota.
DR GeneTree; ENSGT00390000014665; -.
DR HOGENOM; CLU_035060_0_0_1; -.
DR InParanoid; Q12094; -.
DR OMA; HHIRKGR; -.
DR BioCyc; MetaCyc:G3O-33556-MON; -.
DR BioCyc; YEAST:G3O-33556-MON; -.
DR PRO; PR:Q12094; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12094; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0106388; F:18S rRNA aminocarboxypropyltransferase activity; IMP:SGD.
DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000455; P:enzyme-directed rRNA pseudouridine synthesis; IDA:UniProtKB.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IMP:SGD.
DR HAMAP; MF_01116; TSR3; 1.
DR InterPro; IPR007209; RNaseL-inhib-like_metal-bd_dom.
DR InterPro; IPR022968; Tsr3-like.
DR InterPro; IPR007177; Tsr3_C.
DR PANTHER; PTHR20426; PTHR20426; 1.
DR Pfam; PF04034; Ribo_biogen_C; 1.
DR Pfam; PF04068; RLI; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW Ribosome biogenesis; rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..313
FT /note="18S rRNA aminocarboxypropyltransferase"
FT /id="PRO_0000094426"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 62
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:E1QU22"
FT BINDING 110
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:E1QU22"
FT BINDING 133
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:E1QU22"
FT BINDING 148
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:E1QU22"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 60
FT /note="R->A: Decreased aminocarboxypropyltransferase
FT activity; when associated with A-65 and A-131."
FT /evidence="ECO:0000269|PubMed:27084949"
FT MUTAGEN 62
FT /note="S->A: Does not affect S-adenosyl-L-methionine-
FT binding."
FT /evidence="ECO:0000269|PubMed:27084949"
FT MUTAGEN 62
FT /note="S->D: Decreased S-adenosyl-L-methionine-binding."
FT /evidence="ECO:0000269|PubMed:27084949"
FT MUTAGEN 65
FT /note="K->A: Decreased aminocarboxypropyltransferase
FT activity; when associated with A-60 and A-131."
FT /evidence="ECO:0000269|PubMed:27084949"
FT MUTAGEN 111
FT /note="E->A: Reduced aminocarboxypropyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:27084949"
FT MUTAGEN 131
FT /note="R->A: Decreased aminocarboxypropyltransferase
FT activity; when associated with A-60 and A-65."
FT /evidence="ECO:0000269|PubMed:27084949"
SQ SEQUENCE 313 AA; 35686 MW; 6DF4703EA7252910 CRC64;
MGKGKNKMHE PKNGRPQRGA NGHSSRQNHR RMEMKYDNSE KMKFPVKLAM WDFDHCDPKR
CSGKKLERLG LIKSLRVGQK FQGIVVSPNG KGVVCPDDLE IVEQHGASVV ECSWARLEEV
PFNKIGGKHE RLLPYLVAAN QVNYGRPWRL NCVEALAACF AIVGRMDWAS ELLSHFSWGM
GFLELNKELL EIYQQCTDCD SVKRAEEEWL QKLEKETQER KSRAKEEDIW MMGNINRRGN
GSQSDTSESE ENSEQSDLEG NNQCIEYDSL GNAIRIDNMK SREAQSEESE DEESGSKENG
EPLSYDPLGN LIR
