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Database: UniProt
Entry: C0XSM6_CORLD
LinkDB: C0XSM6_CORLD
Original site: C0XSM6_CORLD 
ID   C0XSM6_CORLD            Unreviewed;       410 AA.
AC   C0XSM6;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=TRAM domain protein {ECO:0000313|EMBL:EEI16764.1};
GN   ORFNames=HMPREF0298_1446 {ECO:0000313|EMBL:EEI16764.1};
OS   Corynebacterium lipophiloflavum (strain ATCC 700352 / DSM 44291 / CCUG
OS   37336 / JCM 10383 / DMMZ 1944).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=525263 {ECO:0000313|EMBL:EEI16764.1, ECO:0000313|Proteomes:UP000006196};
RN   [1] {ECO:0000313|EMBL:EEI16764.1, ECO:0000313|Proteomes:UP000006196}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700352 / DSM 44291 / CCUG 37336 / JCM 10383 / DMMZ 1944
RC   {ECO:0000313|Proteomes:UP000006196};
RA   Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA   Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA   Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA   Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA   Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA   Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA   Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA   Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA   Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA   Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RNA M5U methyltransferase family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01024}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EEI16764.1}.
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DR   EMBL; ACHJ01000117; EEI16764.1; -; Genomic_DNA.
DR   RefSeq; WP_006840173.1; NZ_GG667192.1.
DR   AlphaFoldDB; C0XSM6; -.
DR   STRING; 525263.HMPREF0298_1446; -.
DR   eggNOG; COG2265; Bacteria.
DR   HOGENOM; CLU_014689_7_0_11; -.
DR   OrthoDB; 9804590at2; -.
DR   Proteomes; UP000006196; Unassembled WGS sequence.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
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; 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; 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.
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..64
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        362
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        362
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         241
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         271
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         295
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         335
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   410 AA;  43291 MW;  DCDA9091CB98786E CRC64;
     MRVSAIADNT TLELDVTAMA HGGEGIARDS DGRVVFVGGA IPGDKVRAEL TKVKKMWARA
     QLTEVVSASP DRVSPTCPVA ARGGGCCDYS HIAPAAQPGI KREVLIGQLG AFSNSAEALG
     DTVVLEPATR WRSRVRLGVD SSGRAGVRTA RSTQLITDVA CSQVVPGLLD GIVGPGARTF
     TPGAEVIAVL DSTGQRHVVE STRAQRGRRV EKVDRVVEGS GVVEQNVGKH AFRFPATAFW
     QAHVAAPAAY SEVIRSWGKA DYERATGWDL YGGVGAFVPA IDEALGGAAH IDSVDYSVSA
     TRAAQDTLAG FALRVHNSPV EKAGELTPPG LVVLDPPRSG AGEDVVRRVA GAAPERIIHV
     GCDPATFARD LGYWAAHGFG VRRMVLIDAF PNTHHFEMIA QLEPDGQMQR
//
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