ARLMC_PYRAB
ID ARLMC_PYRAB Reviewed; 410 AA.
AC Q9UZK1; G8ZKB9;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=23S rRNA (uracil(747)-C(5))-methyltransferase;
DE EC=2.1.1.189;
DE AltName: Full=23S rRNA(m5U747)-methyltransferase;
GN OrderedLocusNames=PYRAB11450; ORFNames=PAB0760;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=21051506; DOI=10.1261/rna.2323411;
RA Auxilien S., Rasmussen A., Rose S., Brochier-Armanet C., Husson C.,
RA Fourmy D., Grosjean H., Douthwaite S.;
RT "Specificity shifts in the rRNA and tRNA nucleotide targets of archaeal and
RT bacterial m5U methyltransferases.";
RL RNA 17:45-53(2011).
CC -!- FUNCTION: Catalyzes the formation of 5-methyl-uridine at position
CC equivalent to 747 (m5U747) in 23S rRNA (m5U859 in the P.abyssi
CC numbering). {ECO:0000269|PubMed:21051506}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + uridine(747) in 23S rRNA = 5-
CC methyluridine(747) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42628, Rhea:RHEA-COMP:10154, Rhea:RHEA-COMP:10155,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74447; EC=2.1.1.189;
CC Evidence={ECO:0000269|PubMed:21051506};
CC -!- ACTIVITY REGULATION: Activated by magnesium ions.
CC {ECO:0000269|PubMed:21051506}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RNA M5U methyltransferase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01024}.
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DR EMBL; AJ248286; CAB50056.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE70562.1; -; Genomic_DNA.
DR PIR; C75094; C75094.
DR RefSeq; WP_010868262.1; NC_000868.1.
DR AlphaFoldDB; Q9UZK1; -.
DR SMR; Q9UZK1; -.
DR STRING; 272844.PAB0760; -.
DR EnsemblBacteria; CAB50056; CAB50056; PAB0760.
DR GeneID; 1496508; -.
DR KEGG; pab:PAB0760; -.
DR PATRIC; fig|272844.11.peg.1203; -.
DR eggNOG; arCOG00122; Archaea.
DR HOGENOM; CLU_014689_8_1_2; -.
DR OMA; YCGVGGF; -.
DR OrthoDB; 33103at2157; -.
DR PhylomeDB; Q9UZK1; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070041; F:rRNA (uridine-C5-)-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0031167; P:rRNA methylation; IDA:UniProtKB.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR030390; MeTrfase_TrmA_AS.
DR InterPro; IPR030391; MeTrfase_TrmA_CS.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR015985; TehB-like_dom.
DR InterPro; IPR010280; U5_MeTrfase_fam.
DR PANTHER; PTHR11061; PTHR11061; 1.
DR Pfam; PF03848; TehB; 1.
DR Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR PROSITE; PS01230; TRMA_1; 1.
DR PROSITE; PS01231; TRMA_2; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Methyltransferase;
KW rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..410
FT /note="23S rRNA (uracil(747)-C(5))-methyltransferase"
FT /id="PRO_0000162054"
FT ACT_SITE 367
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT BINDING 61
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 253
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT BINDING 279
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT BINDING 300
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT BINDING 341
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 410 AA; 46442 MW; 5315A0A418E34024 CRC64;
MRGIIKGVSN DGLGVLGEVL VPFAYPGDVV EVISTRERFG RTIARDFKLV KSSPIRVPGK
CRYFGRCGGC LWQGLKYREQ LKLKEEIFKR VTGVEAEIKG SPRIWFFRNI SNFIVTVNGI
GFKEFGMPRT VVSVDECPVF SERTKLYIRA MKRFLRETGL NPWNWKNGDV HYLQVREGKF
TGEVMINVIA HIPPSGREEL TEAFGFADSV YWSLKRDKRD DPKGIPTLIK GNEFIRESIE
GLVYLIHPST FFQTNSYALP ILLKAVESFA EGSKVLDLYS GVGTFSLYLA KKGFEVTGVE
VNEESVRVAK KSAEVNSLDV SFIPGRAEDA KLKGYETLIV DPPRKGLKDF SKRIAKEGPE
NLIYVSCNPS KFVLDYRNYL SKAYKIEDAV LIDMFPHTPH VEAVVKLRRR
