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Y924_DESVH
ID   Y924_DESVH              Reviewed;         468 AA.
AC   Q72DK5;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Uncharacterized RNA methyltransferase DVU_0924;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=DVU_0924;
OS   Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS   B-1760 / Hildenborough).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough;
RX   PubMed=15077118; DOI=10.1038/nbt959;
RA   Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA   Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M.,
RA   Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA   Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J.,
RA   Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G.,
RA   Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V.,
RA   Wall J.D., Voordouw G., Fraser C.M.;
RT   "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT   Desulfovibrio vulgaris Hildenborough.";
RL   Nat. Biotechnol. 22:554-559(2004).
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; AE017285; AAS95404.1; -; Genomic_DNA.
DR   RefSeq; WP_010938223.1; NC_002937.3.
DR   RefSeq; YP_010145.1; NC_002937.3.
DR   AlphaFoldDB; Q72DK5; -.
DR   SMR; Q72DK5; -.
DR   IntAct; Q72DK5; 1.
DR   STRING; 882.DVU_0924; -.
DR   PaxDb; Q72DK5; -.
DR   EnsemblBacteria; AAS95404; AAS95404; DVU_0924.
DR   KEGG; dvu:DVU_0924; -.
DR   PATRIC; fig|882.5.peg.868; -.
DR   eggNOG; COG2265; Bacteria.
DR   HOGENOM; CLU_014689_7_2_7; -.
DR   OMA; YCGVGGF; -.
DR   PhylomeDB; Q72DK5; -.
DR   Proteomes; UP000002194; 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:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0034470; P:ncRNA processing; IEA:UniProt.
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; PF01938; TRAM; 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   4Fe-4S; Iron; Iron-sulfur; Metal-binding; Methyltransferase;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..468
FT                   /note="Uncharacterized RNA methyltransferase DVU_0924"
FT                   /id="PRO_0000161977"
FT   DOMAIN          3..61
FT                   /note="TRAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00208"
FT   ACT_SITE        416
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         74
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         80
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         83
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         162
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         288
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         317
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         338
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         389
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   468 AA;  51206 MW;  737D9BE1F8A74118 CRC64;
     METFANGMTL DVTVDALAPG GKAVCRHEGR VIFVDRGLPG QQLHVRLTTV RKRFAEAECL
     AVVTHTADEC DPFCPHFGDC GGCTWQNLPY PAQLAWKERF VRDSLQRIGR IEAPNVLPTL
     PSPLQQGFRN KMEFAFTTDD REMLHLGLRR RGGHEVVDVT SCGLQTATTC RVVTTARDIA
     RASGLPGWDD AAHRGFWRFL VVREPARGGQ CLVQCITAPH PEAEHVARAF FTALRQAVPE
     VTGCVHSIRS QNSQVAYGDA TVFTEGEIVL TEKLGAIELD FGHDTFLQTN TRATELLYGE
     VERMAGLSGR EHVWDLYCGV GSIALWLAEH AATICGMEAT PASVEAAQRN AQAAGCTHCD
     FVAGDVRALL RSRSKGKAQE PIPDVVVTDP PRAGMHPDVI DALLQTAPAR IVYVSCDPAT
     MARDVGLLMQ RYTLHEARPV DLFPHTPHVE TVVLLSNKEV DDTISTTV
 
 
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