TSR3_VULDI
ID TSR3_VULDI Reviewed; 185 AA.
AC E1QU22;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 61.
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=VdTsr3 {ECO:0000303|PubMed:27084949};
GN OrderedLocusNames=Vdis_0418 {ECO:0000312|EMBL:ADN49819.1};
OS Vulcanisaeta distributa (strain DSM 14429 / JCM 11212 / NBRC 100878 /
OS IC-017).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Vulcanisaeta.
OX NCBI_TaxID=572478;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14429 / JCM 11212 / NBRC 100878 / IC-017;
RX DOI=10.4056/sigs.1113067;
RA Mavromatis K., Sikorski J., Pabst E., Teshima H., Lapidus A., Lucas S.,
RA Nolan M., Glavina Del Rio T., Cheng J., Bruce D., Goodwin L., Pitluck S.,
RA Liolios K., Ivanova N., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y., Jeffries C., Rohde M., Spring S., Goker M.,
RA Wirth R., Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P.,
RA Klenk H., Kyrpides N.;
RT "Complete genome sequence of Vulcanisaeta distributa type strain (IC-
RT 017T).";
RL Stand. Genomic Sci. 3:117-125(2010).
RN [2] {ECO:0007744|PDB:5APG}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH
RP S-ADENOSYL-L-METHIONINE.
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, ECO:0000305}.
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DR EMBL; CP002100; ADN49819.1; -; Genomic_DNA.
DR PDB; 5APG; X-ray; 1.60 A; A/B/C=1-185.
DR PDBsum; 5APG; -.
DR AlphaFoldDB; E1QU22; -.
DR SMR; E1QU22; -.
DR STRING; 572478.Vdis_0418; -.
DR EnsemblBacteria; ADN49819; ADN49819; Vdis_0418.
DR KEGG; vdi:Vdis_0418; -.
DR eggNOG; arCOG04733; Archaea.
DR HOGENOM; CLU_035060_4_2_2; -.
DR OMA; DCSWESA; -.
DR Proteomes; UP000006681; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0106388; F:18S rRNA aminocarboxypropyltransferase activity; IEA:InterPro.
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; IPR022968; Tsr3-like.
DR InterPro; IPR007177; Tsr3_C.
DR PANTHER; PTHR20426; PTHR20426; 1.
DR Pfam; PF04034; Ribo_biogen_C; 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..185
FT /note="16S rRNA aminocarboxypropyltransferase"
FT /id="PRO_0000450352"
FT BINDING 19
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:27084949,
FT ECO:0007744|PDB:5APG"
FT BINDING 69
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:27084949,
FT ECO:0007744|PDB:5APG"
FT BINDING 93
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:27084949,
FT ECO:0007744|PDB:5APG"
FT BINDING 108
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:27084949,
FT ECO:0007744|PDB:5APG"
FT BINDING 112
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:27084949,
FT ECO:0007744|PDB:5APG"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:5APG"
FT HELIX 19..25
FT /evidence="ECO:0007829|PDB:5APG"
FT STRAND 28..34
FT /evidence="ECO:0007829|PDB:5APG"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:5APG"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:5APG"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:5APG"
FT HELIX 58..63
FT /evidence="ECO:0007829|PDB:5APG"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:5APG"
FT HELIX 73..83
FT /evidence="ECO:0007829|PDB:5APG"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:5APG"
FT TURN 101..105
FT /evidence="ECO:0007829|PDB:5APG"
FT HELIX 112..122
FT /evidence="ECO:0007829|PDB:5APG"
FT HELIX 126..133
FT /evidence="ECO:0007829|PDB:5APG"
FT HELIX 141..153
FT /evidence="ECO:0007829|PDB:5APG"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:5APG"
FT HELIX 160..165
FT /evidence="ECO:0007829|PDB:5APG"
FT HELIX 170..182
FT /evidence="ECO:0007829|PDB:5APG"
SQ SEQUENCE 185 AA; 20927 MW; EED58D68245D9CD5 CRC64;
MIPRVFIYRL PQDDPRKNTA IKLVRFGFAQ LVDSIKALPS GSIILDPTVK TPLTPSDRVI
AESRGLSLID CSWKRAVDVH TKFIRGKFIR RRLPLLIAAN PTHYGKPYIL STIEAVAAAL
YIMGFKDEAM EVLRLYKWGP NFIIINQKYL ERYAAGDLSP ERELLGVDDV DNGLEQLMRV
LTNGD
