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Database: UniProt
Entry: F4H1H0_CELFA
LinkDB: F4H1H0_CELFA
Original site: F4H1H0_CELFA 
ID   F4H1H0_CELFA            Unreviewed;       429 AA.
AC   F4H1H0;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Deoxyribonuclease/rho motif-related TRAM {ECO:0000313|EMBL:AEE46269.1};
GN   OrderedLocusNames=Celf_2141 {ECO:0000313|EMBL:AEE46269.1};
OS   Cellulomonas fimi (strain ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 /
OS   NCIMB 8980 / NCTC 7547).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=590998 {ECO:0000313|EMBL:AEE46269.1, ECO:0000313|Proteomes:UP000008460};
RN   [1] {ECO:0000313|EMBL:AEE46269.1, ECO:0000313|Proteomes:UP000008460}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 /
RC   NCTC 7547 {ECO:0000313|Proteomes:UP000008460};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Mead D., Brumm P.,
RA   Woyke T.;
RT   "Complete sequence of Cellulomonas fimi ATCC 484.";
RL   Submitted (APR-2011) 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}.
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DR   EMBL; CP002666; AEE46269.1; -; Genomic_DNA.
DR   RefSeq; WP_013771295.1; NC_015514.1.
DR   AlphaFoldDB; F4H1H0; -.
DR   STRING; 590998.Celf_2141; -.
DR   KEGG; cfi:Celf_2141; -.
DR   eggNOG; COG2265; Bacteria.
DR   HOGENOM; CLU_014689_7_0_11; -.
DR   Proteomes; UP000008460; Chromosome.
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; 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.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01024}; Reference proteome {ECO:0000313|Proteomes:UP000008460};
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          15..75
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        387
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         259
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         288
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         311
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         360
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   429 AA;  45658 MW;  13F06E6EEF5860E3 CRC64;
     MVTEPPATPP APADRPDPDA LVELEVGPVA HGGHCVARHE GRVVFVRHTL PGERVRARLT
     DAGESASFWR ADAVEVLEAS PDRVASAWPE AGAGGVGGGE LAHVALPAQR RWKEAVLAEQ
     LRRLARDERA VTVHAAPGDD DRGGLHWRTR IDLVADARGR AGMRGHRSHD VRALDAMPLA
     TEAIEALGLF ERRWSGGARI EAVAPAAGDT PLVLQDGAPF DLGRGRTDKR PNARTSVREE
     VRRGDVTYTY RVAAAGFWQV HREAPGLLVG AVLDALGDVD GAVVLDLYAG AGLFTLPLAD
     AVGDGEVVSV EGDARAVRDA RRNVHDRPNV ELHAGDVARV LTGRQDADSD VVHADAVVLD
     PPRTGAGRRV VDAVAALRPE RVVYVACDPA ALARDVALLG EAGYALDDVQ GYDLFPHTHH
     LEAVAVFTR
//
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