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Database: UniProt
Entry: C7M3S5_CAPOD
LinkDB: C7M3S5_CAPOD
Original site: C7M3S5_CAPOD 
ID   C7M3S5_CAPOD            Unreviewed;       471 AA.
AC   C7M3S5;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   SubName: Full=RNA methyltransferase, TrmA family {ECO:0000313|EMBL:ACU93701.1};
GN   OrderedLocusNames=Coch_2157 {ECO:0000313|EMBL:ACU93701.1};
OS   Capnocytophaga ochracea (strain ATCC 27872 / DSM 7271 / JCM 12966 / NCTC
OS   12371 / VPI 2845) (Bacteroides ochraceus).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Capnocytophaga.
OX   NCBI_TaxID=521097 {ECO:0000313|EMBL:ACU93701.1, ECO:0000313|Proteomes:UP000006650};
RN   [1] {ECO:0000313|EMBL:ACU93701.1, ECO:0000313|Proteomes:UP000006650}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27872 / DSM 7271 / JCM 12966 / VPI 2845
RC   {ECO:0000313|Proteomes:UP000006650};
RX   PubMed=21304645; DOI=10.4056/sigs.15195;
RA   Mavrommatis K., Gronow S., Saunders E., Land M., Lapidus A., Copeland A.,
RA   Glavina Del Rio T., Nolan M., Lucas S., Chen F., Tice H., Cheng J.F.,
RA   Bruce D., Goodwin L., Pitluck S., Pati A., Ivanova N., Chen A.,
RA   Palaniappan K., Chain P., Hauser L., Chang Y.J., Jeffries C.D., Brettin T.,
RA   Detter J.C., Han C., Bristow J., Goker M., Rohde M., Eisen J.A.,
RA   Markowitz V., Kyrpides N.C., Klenk H.P., Hugenholtz P.;
RT   "Complete genome sequence of Capnocytophaga ochracea type strain (VPI
RT   2845).";
RL   Stand. Genomic Sci. 1:101-109(2009).
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; CP001632; ACU93701.1; -; Genomic_DNA.
DR   RefSeq; WP_015783112.1; NC_013162.1.
DR   AlphaFoldDB; C7M3S5; -.
DR   STRING; 521097.Coch_2157; -.
DR   GeneID; 29676221; -.
DR   KEGG; coc:Coch_2157; -.
DR   eggNOG; COG2265; Bacteria.
DR   HOGENOM; CLU_014689_7_2_10; -.
DR   Proteomes; UP000006650; 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; PF01938; TRAM; 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}; Reference proteome {ECO:0000313|Proteomes:UP000006650};
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          1..62
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        425
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        425
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         299
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         328
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         349
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         398
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   471 AA;  53440 MW;  0EDB2EDF74FEE96B CRC64;
     MSKNKHITIE NVTVIDAGAK GKSIAKAPDG RVIFISNAIP GDVVDVQTTK KKSAYYEGFV
     TKYHQLSEQR VTPVCSHFGY CGGCKWQDMN YQSQLFYKQK EVENNLVRLG RIEIPAVMPI
     IGSDETYYYR NKMEFSFSDM RWLTPDEIKK ADEIDNRNAL GFHIAGAWDK ILDIDKCYLQ
     ADPSNAIRLE VKRFALANEM PFYSPRQQTG LLRTMMIRIS SIGQIMVVIQ FFRNDPKITL
     LLDHIAETFP MITSLQYCIN SKGNDAIYDQ ELICYKGTDC IYEEMEGLRF KINAKSFYQT
     NSAQAYKLYQ VARNFADLKG DELVYDLYTG TGTIAQFVAK KAKKVIGVEA VPEAIADAKD
     NAFANGIENV TFYVGDMKNI FNDTFIEENG TPDVIITDPP RDGMHKDVVA KILQIAPKKI
     VYVSCNSATQ ARDLSLLDVT YKVTKVQPVD MFPQTYHVEN VVLLEKRNEK S
//
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