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Database: UniProt
Entry: E6XAH3_CELAD
LinkDB: E6XAH3_CELAD
Original site: E6XAH3_CELAD 
ID   E6XAH3_CELAD            Unreviewed;       472 AA.
AC   E6XAH3;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   SubName: Full=23S rRNA m(5)U-1939 methyltransferase {ECO:0000313|EMBL:ADV49889.1};
DE            EC=2.1.1.- {ECO:0000313|EMBL:ADV49889.1};
GN   OrderedLocusNames=Celal_2604 {ECO:0000313|EMBL:ADV49889.1};
OS   Cellulophaga algicola (strain DSM 14237 / IC166 / ACAM 630).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Cellulophaga.
OX   NCBI_TaxID=688270 {ECO:0000313|EMBL:ADV49889.1, ECO:0000313|Proteomes:UP000008634};
RN   [1] {ECO:0000313|EMBL:ADV49889.1, ECO:0000313|Proteomes:UP000008634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14237 / IC166 / ACAM 630
RC   {ECO:0000313|Proteomes:UP000008634};
RX   PubMed=21475589; DOI=10.4056/sigs.1543845;
RA   Abt B., Lu M., Misra M., Han C., Nolan M., Lucas S., Hammon N.,
RA   Deshpande S., Cheng J.F., Tapia R., Goodwin L., Pitluck S., Liolios K.,
RA   Pagani I., Ivanova N., Mavromatis K., Ovchinikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA   Brambilla E., Rohde M., Tindall B.J., Goker M., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA   Lapidus A.;
RT   "Complete genome sequence of Cellulophaga algicola type strain (IC166).";
RL   Stand. Genomic Sci. 4:72-80(2010).
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; CP002453; ADV49889.1; -; Genomic_DNA.
DR   RefSeq; WP_013551360.1; NC_014934.1.
DR   AlphaFoldDB; E6XAH3; -.
DR   STRING; 688270.Celal_2604; -.
DR   KEGG; cao:Celal_2604; -.
DR   eggNOG; COG2265; Bacteria.
DR   HOGENOM; CLU_014689_7_2_10; -.
DR   OrthoDB; 9804590at2; -.
DR   Proteomes; UP000008634; 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};
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          2..65
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        429
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        429
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         303
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         332
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         353
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         402
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   472 AA;  54212 MW;  C52685ED2343B605 CRC64;
     MRRKSNKTKT IFENVTVVDA GAKGKTIGKA PDGRVIFLNN TVPGDVVDVQ TTKKRKAYFE
     GTAINFHTLS DKRVTPVCQH FGTCGGCKWQ DMGYDHQLFY KQKEVENNLR RIGHLELPEI
     TPILGSKKQY FYRNKMEFSF SDSRWLSLDE IKSDEEIKDR NALGFHIPGM WDKILDIEKC
     HLQEDPSNAI RLETKDFALK NDMSFFNPRN QHGLLRTMMI RTTSTGEIMV MVQFFENDKN
     KRELLLNHLQ LKFPEITALL YVVNEKQNDT IYDQEIVCFA GRDHIFEEME GLKFKINAKS
     FYQTNSDQAY ELYKITRDFA GLTGNELVYD LYTGTGTIAQ FVAKKAKKVV GIEAVPEAIE
     DAKANAIFNK IENTSFFAGD MKNIFNEEFI RENGTPDIII TDPPRDGMHK DVVAQILAIA
     PQKVVYVSCN SATQARDLEL MKDDYKITKT QAVDMFPQTH HVENVVLLEK RY
//
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