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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//