ID   Y2977_LEPIN             Reviewed;         454 AA.
AC   Q8F201;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Uncharacterized RNA methyltransferase LA_2977;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=LA_2977;
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS   56601).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=189518;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=56601;
RX   PubMed=12712204; DOI=10.1038/nature01597;
RA   Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X.,
RA   Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X.,
RA   Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F.,
RA   Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y.,
RA   Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I.,
RA   Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
RT   "Unique physiological and pathogenic features of Leptospira interrogans
RT   revealed by whole-genome sequencing.";
RL   Nature 422:888-893(2003).
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; AE010300; AAN50175.1; -; Genomic_DNA.
DR   RefSeq; NP_713157.1; NC_004342.2.
DR   RefSeq; WP_000884774.1; NC_004342.2.
DR   AlphaFoldDB; Q8F201; -.
DR   SMR; Q8F201; -.
DR   EnsemblBacteria; AAN50175; AAN50175; LA_2977.
DR   KEGG; lil:LA_2977; -.
DR   PATRIC; fig|189518.3.peg.2955; -.
DR   HOGENOM; CLU_014689_8_1_12; -.
DR   InParanoid; Q8F201; -.
DR   OMA; SIIHVMN; -.
DR   Proteomes; UP000001408; Chromosome I.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0008083; F:growth factor activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR000072; PDGF/VEGF_dom.
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; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR   PROSITE; PS01230; TRMA_1; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Iron; Iron-sulfur; Metal-binding; Methyltransferase;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..454
FT                   /note="Uncharacterized RNA methyltransferase LA_2977"
FT                   /id="PRO_0000161996"
FT   ACT_SITE        408
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         73
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         79
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         82
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         154
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         279
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         307
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         328
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         381
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   454 AA;  52406 MW;  0DAD76282BB783A5 CRC64;
     MLDKNTNLTH QSKIEFVNSN LRGIGFVNNT KIEVPYSLPG DVYNVTFFKK KRRKPSAKLE
     LVSQTQRSFI PPCSAFTKCG GCCAQHISYQ DQFRYKTSSL LESYKKDFEI VPTLYPAQKT
     FYYRNRMDFA VFPGPIVGQR EAGSFRHIVD LETCLIQSKE SNEELYRFRN LISKFPNLPY
     DRKSDSGFLK YFTLRKAKNT SELMTILTFV EEFKNTIEEK EFENVCLKSL KADHILFCFN
     RRKGEISATG EIKILKGMDS YKELVCGKEF RVPFDSFFQP NPEGFQPILD FIEKEIPDSF
     DHLVDLFCGS GFFSRIFAHK FLKITGIDSI ESSLEIARKQ MSLDFPKIDS SYLKVDLFSK
     NSSSKLKVLF SSSDKDVLIA DPPRAGLGEF VLDALKDSKV SYFFYVSCNP TSQKSDLWKL
     KDFFQIQKIL ITDPYPQTPH LESVAFLKRK NFTT