ID   ARLMC_PYRFU             Reviewed;         409 AA.
AC   Q8U2K7;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=PF0827;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
CC   -!- FUNCTION: Catalyzes the formation of 5-methyl-uridine at position
CC       equivalent to 747 (m5U747) in 23S rRNA. {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RNA M5U methyltransferase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01024}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE009950; AAL80951.1; -; Genomic_DNA.
DR   RefSeq; WP_011011956.1; NZ_CP023154.1.
DR   AlphaFoldDB; Q8U2K7; -.
DR   SMR; Q8U2K7; -.
DR   STRING; 186497.PF0827; -.
DR   PRIDE; Q8U2K7; -.
DR   EnsemblBacteria; AAL80951; AAL80951; PF0827.
DR   GeneID; 41712630; -.
DR   KEGG; pfu:PF0827; -.
DR   PATRIC; fig|186497.12.peg.875; -.
DR   eggNOG; arCOG00122; Archaea.
DR   HOGENOM; CLU_014689_8_1_2; -.
DR   OMA; YCGVGGF; -.
DR   OrthoDB; 33103at2157; -.
DR   PhylomeDB; Q8U2K7; -.
DR   Proteomes; UP000001013; 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; ISS:UniProtKB.
DR   GO; GO:0031167; P:rRNA methylation; ISS: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; IPR010280; U5_MeTrfase_fam.
DR   PANTHER; PTHR11061; PTHR11061; 1.
DR   Pfam; PF05958; tRNA_U5-meth_tr; 2.
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   3: Inferred from homology;
KW   4Fe-4S; Iron; Iron-sulfur; Metal-binding; Methyltransferase;
KW   Reference proteome; rRNA processing; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..409
FT                   /note="23S rRNA (uracil(747)-C(5))-methyltransferase"
FT                   /id="PRO_0000162055"
FT   ACT_SITE        365
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         251
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         277
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         298
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         339
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   409 AA;  46868 MW;  F6049CC3DAF85D5E CRC64;
     MRGIIEDLSQ DGLGVINGIE VPFCYPGDEV RITRTRDRFG RKMASEFSLI TPSPLRQRPR
     CRHYGKCGGC LWQGMKYEEQ LKFKKELFRR ITGIEAEILG SPRIWEFRNI SNFIVSVNGI
     GLKEFARPKT VVDLKECPVF SNRTPLYIRA MKEFLRESGL KPWNWKEGDV HYLQVREGKF
     TGEVMVNIIA HRPPEETILE YFPFADSVYW SIKRDKRDDP SGEPIHLGEK EFISEKIFGI
     KYLLRPGIFF QTNSYALPLL LKAVEGFLDG SKVLDLYSGI GTFSLYLTKK GFNVVGVEIN
     KTAVEVAKLS AELNSLNVEF KAKRAEEENI EGYDALILDP PRKGLGEFAG VVEKKGPENV
     VYVSCNPKRF ILDFKNYLSR SYKVEDAILI DMFPHTPHVE AVIKLRKYS