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Database: UniProt
Entry: W8VXA7_9FLAO
LinkDB: W8VXA7_9FLAO
Original site: W8VXA7_9FLAO 
ID   W8VXA7_9FLAO            Unreviewed;       473 AA.
AC   W8VXA7;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=RNA methyltransferase, TrmA family {ECO:0000313|EMBL:BAO55597.1};
GN   ORFNames=NMS_1588 {ECO:0000313|EMBL:BAO55597.1};
OS   Nonlabens marinus S1-08.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Nonlabens.
OX   NCBI_TaxID=1454201 {ECO:0000313|EMBL:BAO55597.1, ECO:0000313|Proteomes:UP000031760};
RN   [1] {ECO:0000313|EMBL:BAO55597.1, ECO:0000313|Proteomes:UP000031760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S1-08 {ECO:0000313|EMBL:BAO55597.1,
RC   ECO:0000313|Proteomes:UP000031760};
RX   PubMed=24706784; DOI=10.1073/pnas.1403051111;
RA   Yoshizawa S., Kumagai Y., Kim H., Ogura Y., Hayashi T., Iwasaki W.,
RA   DeLong E.F., Kogure K.;
RT   "Functional characterization of flavobacteria rhodopsins reveals a unique
RT   class of light-driven chloride pump in bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:6732-6737(2014).
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RNA M5U methyltransferase family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01024}.
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DR   EMBL; AP014548; BAO55597.1; -; Genomic_DNA.
DR   RefSeq; WP_041496178.1; NZ_AP014548.1.
DR   AlphaFoldDB; W8VXA7; -.
DR   STRING; 1454201.NMS_1588; -.
DR   HOGENOM; CLU_014689_7_2_10; -.
DR   OrthoDB; 9804590at2; -.
DR   Proteomes; UP000031760; Chromosome.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0034470; P:ncRNA processing; IEA:UniProt.
DR   GO; GO:0009451; P:RNA modification; IEA:UniProt.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 2.40.50.1070; -; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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   NCBIfam; TIGR00479; rumA; 1.
DR   PANTHER; PTHR11061; RNA M5U METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR11061:SF30; TRNA (URACIL(54)-C(5))-METHYLTRANSFERASE; 1.
DR   Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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 {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01024};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU01024};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU01024}.
FT   DOMAIN          5..65
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        431
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        431
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         305
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         334
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         355
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         404
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   473 AA;  53685 MW;  3F71B4016418C4EC CRC64;
     MSKRRRRANQ TFENVPVVDA GARGKSVAKT EEGAVIFLTD AVPGDVVDIT TFKKRKSFYE
     GKVTKYHTLS DRRTTPVCKH YDTCGGCKWQ SMAYESQLYF KQKEVLENLT RIGHLELPEI
     TPIKGSDEQY YYRNKMEFSF SANRWLTLKE IQSDVQLEDD DKKALGFHIP GMWDKILHLD
     ECHLHPAVGE QIRLAVHAFA KAEHISYFSP REKSGTLRTL MLRMSSTGEV MVVIQFFQDH
     EEHRIALLEH LKESFPQITS LQYIINEKAN DTIYDQDVIL YDGVDHIMEE MEGLQFKISA
     KSFYQTNSAQ AYELYKITRD FAGLDGTQTV YDLYTGTGTI AQFVAGKAAK VVGIESVPQA
     IEDAQANALH NKVENAEFYV GDMKEVFTAD FIAEHGTPDV VITDPPRDGM HKDVVAQLLQ
     LAAPRIVYVS CNSATQARDL ALLDAQYKVI KVQPVDMFPQ THHVENVVLL ELK
//
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