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YR405_MIMIV
ID   YR405_MIMIV             Reviewed;         389 AA.
AC   Q5UQK3;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Putative RNA methyltransferase R405;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MIMI_R405;
OS   Acanthamoeba polyphaga mimivirus (APMV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Imitervirales; Mimiviridae; Mimivirus.
OX   NCBI_TaxID=212035;
OH   NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rowbotham-Bradford;
RX   PubMed=15486256; DOI=10.1126/science.1101485;
RA   Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA   La Scola B., Susan M., Claverie J.-M.;
RT   "The 1.2-megabase genome sequence of Mimivirus.";
RL   Science 306:1344-1350(2004).
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RNA M5U methyltransferase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01024}.
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DR   EMBL; AY653733; AAV50674.1; -; Genomic_DNA.
DR   RefSeq; YP_003986909.1; NC_014649.1.
DR   SMR; Q5UQK3; -.
DR   GeneID; 9925026; -.
DR   KEGG; vg:9925026; -.
DR   Proteomes; UP000001134; Genome.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR030390; MeTrfase_TrmA_AS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR045850; TRM2_euk.
DR   InterPro; IPR010280; U5_MeTrfase_fam.
DR   PANTHER; PTHR45904; PTHR45904; 1.
DR   Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR   PROSITE; PS01230; TRMA_1; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..389
FT                   /note="Putative RNA methyltransferase R405"
FT                   /id="PRO_0000162061"
FT   ACT_SITE        342
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         207
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         261
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         314
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   389 AA;  44942 MW;  BE67F5AB758F24FF CRC64;
     MESINDVSEI CLQLVNLNYS DQLDFKLNLI KQYIPNLLTN QVIASPLVDN YRNKLRFDIG
     LSNHDLITIG YSLPKKKNTH RYVYSSISMK HLHPKMIQIV SKIELFLRTH EQSWYSIKHG
     ETLLPSMTIR TSFHTEDVMI IFKFKGPQNE TVINYFSSDI FYEIIESIEI NIVIEFSDCR
     KIVKGHNYIH EKLDDYIFKI TDESFFQVNT LATEVLYNKV LELTMKYIKP TGQDILFDLC
     CGTGTIGIYL SKIFTKVFGI DIKQSSIIDA NHNKLLNNIP NIEFICNPIE NVLEKLISEC
     LEKNPDSTFF AVVDPPRTGM HGGVQNTINN CPNLEYLIYV SCNVVTFKRD MEILGKQFEA
     IETICLDLFP HTPHCELIVV LKKIDLSIY
 
 
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