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Database: UniProt
Entry: C2E582_LACJH
LinkDB: C2E582_LACJH
Original site: C2E582_LACJH 
ID   C2E582_LACJH            Unreviewed;       459 AA.
AC   C2E582;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   SubName: Full=23S rRNA (Uracil-5-)-methyltransferase RumA {ECO:0000313|EMBL:EEJ59957.1};
DE            EC=2.1.1.- {ECO:0000313|EMBL:EEJ59957.1};
GN   Name=rumA {ECO:0000313|EMBL:EEJ59957.1};
GN   ORFNames=HMPREF0528_0906 {ECO:0000313|EMBL:EEJ59957.1};
OS   Lactobacillus johnsonii ATCC 33200.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=525330 {ECO:0000313|EMBL:EEJ59957.1, ECO:0000313|Proteomes:UP000003491};
RN   [1] {ECO:0000313|EMBL:EEJ59957.1, ECO:0000313|Proteomes:UP000003491}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33200 {ECO:0000313|EMBL:EEJ59957.1,
RC   ECO:0000313|Proteomes:UP000003491};
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:EEJ59957.1}.
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DR   EMBL; ACGR01000032; EEJ59957.1; -; Genomic_DNA.
DR   RefSeq; WP_004893786.1; NZ_GG670120.1.
DR   PATRIC; fig|525330.7.peg.1020; -.
DR   HOGENOM; CLU_014689_7_1_9; -.
DR   Proteomes; UP000003491; 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   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; 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:SF45; -; 1.
DR   PANTHER; PTHR11061; RNA M5U 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   ACT_SITE        414
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        414
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         289
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         318
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         339
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         387
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   459 AA;  52284 MW;  71B0E65B4D97DDC9 CRC64;
     MTKFTKNKQE KNIIITIKRL GINGEGIGYY KKKIIFIPGA LPNEIVVAKI VDRHPHYLEG
     ELVRIKEKSP DRVTFPKGVD PAVGGLELAH LSYPKQLEFK QHLILESLRK YHPRDYIKYK
     VKKTIPAPNA WNYRNKAQYQ IEFNKGKSKL GLYAPNSRRL INLPDMPTQT KETQKVEREI
     KKLVDKLHIR IADFRRHTYG IKTIAVRQSN ATGEIQVTLI TIGKKIKDLK LLASHIMKLP
     NVVSVFQNET QWQNPQVWGN KTIKLFGKSH ITEEILGKKF KLSPRAFFQL NPEQTTTLYS
     EALKYLDLTP DQTLIDAYAG VGTLGILASD QVRQVIGIES IPEAVIDAQE NCRLNHVRNA
     EYIQGNVEKL LPELKNQGVP INALIVDPPR TGLSKKLIKT LLEVKPETFV YVSCNPATLA
     KDLVLLSEAY DVRVIQPVDM MPQTPRWEGV AKLVLRKNK
//
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