TSR3_SCHPO
ID TSR3_SCHPO Reviewed; 288 AA.
AC Q10409;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=18S rRNA aminocarboxypropyltransferase {ECO:0000305};
DE EC=2.5.1.- {ECO:0000250|UniProtKB:Q12094};
GN Name=tsr3 {ECO:0000312|PomBase:SPAC1F3.04c}; ORFNames=SPAC1F3.04c;
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).
CC -!- FUNCTION: Aminocarboxypropyltransferase that catalyzes the
CC aminocarboxypropyl transfer on pseudouridine at position 1191 (Psi1191)
CC in 18S rRNA. It constitutes the last step in biosynthesis of the
CC hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine
CC (m1acp3-Psi) conserved in eukaryotic 18S rRNA. Required for processing
CC 35S pre-rRNA at site D. {ECO:0000250|UniProtKB:Q12094}.
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;
CC Evidence={ECO:0000250|UniProtKB:Q12094, ECO:0000255|HAMAP-
CC Rule:MF_03146};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63301;
CC Evidence={ECO:0000250|UniProtKB:Q12094, ECO:0000255|HAMAP-
CC Rule:MF_03146};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03146}.
CC Nucleus {ECO:0000255|HAMAP-Rule:MF_03146}.
CC -!- SIMILARITY: Belongs to the TDD superfamily. TSR3 family.
CC {ECO:0000255|HAMAP-Rule:MF_03146}.
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DR EMBL; CU329670; CAA94622.1; -; Genomic_DNA.
DR PIR; T38075; T38075.
DR RefSeq; NP_593007.1; NM_001018406.2.
DR AlphaFoldDB; Q10409; -.
DR SMR; Q10409; -.
DR STRING; 4896.SPAC1F3.04c.1; -.
DR MaxQB; Q10409; -.
DR PaxDb; Q10409; -.
DR PRIDE; Q10409; -.
DR EnsemblFungi; SPAC1F3.04c.1; SPAC1F3.04c.1:pep; SPAC1F3.04c.
DR GeneID; 2542142; -.
DR KEGG; spo:SPAC1F3.04c; -.
DR PomBase; SPAC1F3.04c; tsr3.
DR VEuPathDB; FungiDB:SPAC1F3.04c; -.
DR eggNOG; KOG3154; Eukaryota.
DR HOGENOM; CLU_035060_2_1_1; -.
DR InParanoid; Q10409; -.
DR OMA; GRECMNL; -.
DR PhylomeDB; Q10409; -.
DR PRO; PR:Q10409; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; ISO:PomBase.
DR GO; GO:0005634; C:nucleus; ISO:PomBase.
DR GO; GO:0106388; F:18S rRNA aminocarboxypropyltransferase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; ISM:PomBase.
DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000455; P:enzyme-directed rRNA pseudouridine synthesis; IEA:UniProtKB-UniRule.
DR GO; GO:0030490; P:maturation of SSU-rRNA; ISO:PomBase.
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 3: Inferred from homology;
KW Cytoplasm; Nucleus; Reference proteome; Ribosome biogenesis;
KW rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..288
FT /note="18S rRNA aminocarboxypropyltransferase"
FT /id="PRO_0000094427"
FT REGION 209..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 43
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:E1QU22"
FT BINDING 91
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:E1QU22"
FT BINDING 114
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:E1QU22"
FT BINDING 129
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:E1QU22"
SQ SEQUENCE 288 AA; 32606 MW; 99DA85DF7B014220 CRC64;
MGPRSSNRRS NAKDGFKGSN KASKFPLPLA MWDFGHCNPN ACSGKRLERL GCVRNLRIGQ
KFRGVVITPN GKVPVSPADK EYFDNGGASV VECSWARIEE IPFSRIGGRC ERLLPYLVAS
NPVNYGRPWR LNCAEALAAC MYIVGYPNEA RLLMDNFKWG HSFFEVNEEL LDIYAQCHDA
QDIQEKEKKY LEEMEASYQE QRNQTTDDIW SAGNLNHKPT LNTSSTHSNS EESRSPLHEP
SEASLAHDEH SIPTDDNEET LTNLQANDVD EDEVWRKIVR MKVHSTDT
