TSR3_HALSA
ID TSR3_HALSA Reviewed; 165 AA.
AC Q9HNJ6;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 3.
DT 03-AUG-2022, entry version 91.
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};
GN OrderedLocusNames=VNG_2075C;
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
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=AAG20224.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE004437; AAG20224.1; ALT_INIT; Genomic_DNA.
DR PIR; D84357; D84357.
DR RefSeq; WP_012289427.1; NC_002607.1.
DR AlphaFoldDB; Q9HNJ6; -.
DR SMR; Q9HNJ6; -.
DR STRING; 64091.VNG_2075C; -.
DR PaxDb; Q9HNJ6; -.
DR EnsemblBacteria; AAG20224; AAG20224; VNG_2075C.
DR GeneID; 5953226; -.
DR GeneID; 62887383; -.
DR KEGG; hal:VNG_2075C; -.
DR PATRIC; fig|64091.14.peg.1582; -.
DR HOGENOM; CLU_035060_4_1_2; -.
DR InParanoid; Q9HNJ6; -.
DR OrthoDB; 113131at2157; -.
DR PhylomeDB; Q9HNJ6; -.
DR Proteomes; UP000000554; 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; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Cytoplasm; Reference proteome; Ribosome biogenesis; rRNA processing;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..165
FT /note="16S rRNA aminocarboxypropyltransferase"
FT /id="PRO_0000094416"
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:0000255|HAMAP-Rule:MF_01116"
FT BINDING 83
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 102
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"
SQ SEQUENCE 165 AA; 18405 MW; F2AA37ACFD3C115D CRC64;
MELHVRYEGD DDPEKCTARK LARFDLAALH RTGRETPAGV VLNPHAERAL SPADDTDMLV
ALDCSWETAG RAMFEIDGEH RALPFLVAAN PVNYGQPFQL NTVEAFAGAL AILGRWERAE
ELLSKFTWGH TFLELNEEPL RRYADCEDSS EVVAVQQAYL DAGED
