TSR3_SACS2
ID TSR3_SACS2 Reviewed; 166 AA.
AC Q9UWV6;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=16S rRNA aminocarboxypropyltransferase {ECO:0000255|HAMAP-Rule:MF_01116, ECO:0000305};
DE EC=2.5.1.- {ECO:0000255|HAMAP-Rule:MF_01116};
DE AltName: Full=20S S rRNA accumulation protein 3 homolog {ECO:0000303|PubMed:27084949};
DE Short=SsTsr3 {ECO:0000303|PubMed:27084949};
GN OrderedLocusNames=SSO0551; ORFNames=C21_048;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=10701121; DOI=10.1139/g99-108;
RA Charlebois R.L., Singh R.K., Chan-Weiher C.C.-Y., Allard G., Chow C.,
RA Confalonieri F., Curtis B., Duguet M., Erauso G., Faguy D., Gaasterland T.,
RA Garrett R.A., Gordon P., Jeffries A.C., Kozera C., Kushwaha N., Lafleur E.,
RA Medina N., Peng X., Penny S.L., She Q., St Jean A., van der Oost J.,
RA Young F., Zivanovic Y., Doolittle W.F., Ragan M.A., Sensen C.W.;
RT "Gene content and organization of a 281-kbp contig from the genome of the
RT extremely thermophilic archaeon, Sulfolobus solfataricus P2.";
RL Genome 43:116-136(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [3] {ECO:0007744|PDB:5AP8}
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS), S-ADENOSYL-L-METHIONINE-BINDING,
RP RRNA-BINDING, AND MUTAGENESIS OF ASP-63 AND TRP-66.
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 corresponding to position
CC 914 in M.jannaschii 16S rRNA. It constitutes the last step in
CC biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-
CC carboxypropyl) pseudouridine (m1acp3-Psi). {ECO:0000255|HAMAP-
CC Rule:MF_01116}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N(1)-methylpseudouridine in 16S/18S rRNA + S-adenosyl-L-
CC methionine = H(+) + N(1)-methyl-N(3)[(3S)-3-amino-3-
CC carboxypropyl]pseudouridine in 16S/18S rRNA + S-methyl-5'-
CC thioadenosine; Xref=Rhea:RHEA:63296, Rhea:RHEA-COMP:11634, Rhea:RHEA-
CC COMP:16310, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74890, ChEBI:CHEBI:146234; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01116};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01116}.
CC -!- SIMILARITY: Belongs to the TDD superfamily. TSR3 family.
CC {ECO:0000255|HAMAP-Rule:MF_01116}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK40868.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAB57748.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Y18930; CAB57748.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE006641; AAK40868.1; ALT_INIT; Genomic_DNA.
DR PIR; E90201; E90201.
DR RefSeq; WP_009991056.1; NC_002754.1.
DR PDB; 5AP8; X-ray; 2.25 A; A/B/C=1-166.
DR PDBsum; 5AP8; -.
DR AlphaFoldDB; Q9UWV6; -.
DR SMR; Q9UWV6; -.
DR STRING; 273057.SSO0551; -.
DR PRIDE; Q9UWV6; -.
DR EnsemblBacteria; AAK40868; AAK40868; SSO0551.
DR GeneID; 44129554; -.
DR KEGG; sso:SSO0551; -.
DR PATRIC; fig|273057.12.peg.560; -.
DR eggNOG; arCOG04733; Archaea.
DR HOGENOM; CLU_035060_4_1_2; -.
DR InParanoid; Q9UWV6; -.
DR OMA; DCSWESA; -.
DR PhylomeDB; Q9UWV6; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0106388; F:18S rRNA aminocarboxypropyltransferase activity; IEA:InterPro.
DR GO; GO:0019843; F:rRNA binding; IDA:UniProtKB.
DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; IDA:UniProtKB.
DR GO; GO:0000455; P:enzyme-directed rRNA pseudouridine synthesis; IEA:UniProtKB-UniRule.
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 3D-structure; Cytoplasm; Reference proteome; Ribosome biogenesis;
KW rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..166
FT /note="16S rRNA aminocarboxypropyltransferase"
FT /id="PRO_0000094422"
FT BINDING 17
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:E1QU22, ECO:0000255|HAMAP-
FT Rule:MF_01116"
FT BINDING 62
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:E1QU22, ECO:0000255|HAMAP-
FT Rule:MF_01116"
FT BINDING 84
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:E1QU22, ECO:0000255|HAMAP-
FT Rule:MF_01116"
FT BINDING 99
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:E1QU22, ECO:0000255|HAMAP-
FT Rule:MF_01116"
FT BINDING 103
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:E1QU22, ECO:0000255|HAMAP-
FT Rule:MF_01116"
FT MUTAGEN 63
FT /note="D->A: Does not affect S-adenosyl-L-methionine-
FT binding."
FT /evidence="ECO:0000269|PubMed:27084949"
FT MUTAGEN 66
FT /note="W->A: Decreased S-adenosyl-L-methionine-binding."
FT /evidence="ECO:0000269|PubMed:27084949"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:5AP8"
FT HELIX 19..23
FT /evidence="ECO:0007829|PDB:5AP8"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:5AP8"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:5AP8"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:5AP8"
FT HELIX 51..56
FT /evidence="ECO:0007829|PDB:5AP8"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:5AP8"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:5AP8"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:5AP8"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:5AP8"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:5AP8"
FT TURN 92..96
FT /evidence="ECO:0007829|PDB:5AP8"
FT HELIX 103..113
FT /evidence="ECO:0007829|PDB:5AP8"
FT HELIX 117..122
FT /evidence="ECO:0007829|PDB:5AP8"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:5AP8"
FT HELIX 130..136
FT /evidence="ECO:0007829|PDB:5AP8"
FT HELIX 138..144
FT /evidence="ECO:0007829|PDB:5AP8"
FT HELIX 149..159
FT /evidence="ECO:0007829|PDB:5AP8"
FT HELIX 161..164
FT /evidence="ECO:0007829|PDB:5AP8"
SQ SEQUENCE 166 AA; 19197 MW; 41B644E0B04AECFB CRC64;
MKVYIIDYHK DDPKRCTGKK LVKLKIAEFT RVGKGVVLDP FAQITLSNKD KDIVRRIGIT
IVDTSWNNTS QSEFKNIRGE HRRIPILFAG NPIHYGIAYK LSSIEALIAT LYIVDEVEEA
IKLSNVVKWG HTFIELNKEL LEAYKNKTEE DIKKIEREII EKILEK
