Y1713_FUSNN
ID Y1713_FUSNN Reviewed; 464 AA.
AC Q8R5Z8;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Uncharacterized RNA methyltransferase FN1713;
DE EC=2.1.1.-;
GN OrderedLocusNames=FN1713;
OS Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 /
OS BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355).
OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium.
OX NCBI_TaxID=190304;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC 2640 / LMG 13131 / VPI 4355;
RX PubMed=11889109; DOI=10.1128/jb.184.7.2005-2018.2002;
RA Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O.,
RA Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M.,
RA Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N.C.,
RA Overbeek R.;
RT "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum
RT strain ATCC 25586.";
RL J. Bacteriol. 184:2005-2018(2002).
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; AE009951; AAL93828.1; -; Genomic_DNA.
DR RefSeq; NP_602529.1; NC_003454.1.
DR AlphaFoldDB; Q8R5Z8; -.
DR SMR; Q8R5Z8; -.
DR STRING; 190304.FN1713; -.
DR EnsemblBacteria; AAL93828; AAL93828; FN1713.
DR KEGG; fnu:FN1713; -.
DR PATRIC; fig|190304.8.peg.202; -.
DR eggNOG; COG2265; Bacteria.
DR HOGENOM; CLU_014689_7_1_0; -.
DR InParanoid; Q8R5Z8; -.
DR OMA; SIIHVMN; -.
DR BioCyc; FNUC190304:G1FZS-214-MON; -.
DR Proteomes; UP000002521; Chromosome.
DR GO; GO:0070041; F:rRNA (uridine-C5-)-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0070475; P:rRNA base methylation; IBA:GO_Central.
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; IPR002792; TRAM_dom.
DR InterPro; IPR010280; U5_MeTrfase_fam.
DR PANTHER; PTHR11061; PTHR11061; 1.
DR Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR PROSITE; PS50926; TRAM; 1.
DR PROSITE; PS01230; TRMA_1; 1.
DR PROSITE; PS01231; TRMA_2; 1.
PE 3: Inferred from homology;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..464
FT /note="Uncharacterized RNA methyltransferase FN1713"
FT /id="PRO_0000161980"
FT DOMAIN 13..71
FT /note="TRAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00208"
FT ACT_SITE 420
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT BINDING 295
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT BINDING 324
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT BINDING 345
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT BINDING 393
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 464 AA; 53230 MW; F8B7A5F51C5F00ED CRC64;
MMRSSTLKLR NKMLKVSDII QIKIDKIVFG GEGLGYYNGF AVFVPMSIPE DELEIEIISI
KKTYARGLIK NIIKASPERI DNHKFTFEDF YGCDFAMLKY ESQLKYKRFM VEEVIRKIAG
LSDIEISDVL ASEDIYNYRN KIIEPFSVYA NKIITGFFKR KSHEVFEVDE NILNSKLGNK
IIKELKEILN KNKISVYDEN THKGILRNIM IRTNSNNEAM VVLIINSNKI TENIKKLLFK
LRENIEEIKS IYISLNSKKT NTVIGEKNIL IYGEKSIKEN INRIEFHISP TSFFQINVKQ
AKRLYDIAIS FFDNIDNKYI VDAYSGTGTI GMIIAKKAKK VYAIEIVKSA SEDGEKTAKE
NGIENIEFIN GAVEKELVKL VNNNQKIDTI IFDPPRKGLE TSIIDKVAEL NLKEVVYISC
NPSTFARDVK LFSEKGYVLK KLQAVDMFPQ TSHIECVGLI ERKI