ID I0YUW9_COCSC Unreviewed; 484 AA.
AC I0YUW9;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=S-adenosyl-L-methionine-dependent methyltransferase {ECO:0000313|EMBL:EIE22188.1};
DE Flags: Fragment;
GN ORFNames=COCSUDRAFT_2897 {ECO:0000313|EMBL:EIE22188.1};
OS Coccomyxa subellipsoidea (strain C-169) (Green microalga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Trebouxiophyceae incertae sedis; Elliptochloris clade; Coccomyxa;
OC Coccomyxa subellipsoidea.
OX NCBI_TaxID=574566 {ECO:0000313|EMBL:EIE22188.1, ECO:0000313|Proteomes:UP000007264};
RN [1] {ECO:0000313|EMBL:EIE22188.1, ECO:0000313|Proteomes:UP000007264}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C-169 {ECO:0000313|EMBL:EIE22188.1,
RC ECO:0000313|Proteomes:UP000007264};
RX PubMed=22630137; DOI=10.1186/gb-2012-13-5-r39;
RA Blanc G., Agarkova I., Grimwood J., Kuo A., Brueggeman A., Dunigan D.,
RA Gurnon J., Ladunga I., Lindquist E., Lucas S., Pangilinan J., Proschold T.,
RA Salamov A., Schmutz J., Weeks D., Yamada T., Claverie J.M., Grigoriev I.,
RA Van Etten J., Lomsadze A., Borodovsky M.;
RT "The genome of the polar eukaryotic microalga coccomyxa subellipsoidea
RT reveals traits of cold adaptation.";
RL Genome Biol. 13:R39-R39(2012).
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:EIE22188.1}.
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DR EMBL; AGSI01000010; EIE22188.1; -; Genomic_DNA.
DR RefSeq; XP_005646732.1; XM_005646675.1.
DR AlphaFoldDB; I0YUW9; -.
DR STRING; 574566.I0YUW9; -.
DR GeneID; 17040174; -.
DR KEGG; csl:COCSUDRAFT_2897; -.
DR eggNOG; KOG2187; Eukaryota.
DR OrthoDB; 120922at2759; -.
DR Proteomes; UP000007264; 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: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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000007264};
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 1..51
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
FT ACT_SITE 440
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 440
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 313
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 342
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 363
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 413
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EIE22188.1"
FT NON_TER 484
FT /evidence="ECO:0000313|EMBL:EIE22188.1"
SQ SEQUENCE 484 AA; 52425 MW; 75A6E909DEE82C2C CRC64;
LICQSLAFGG QGVCKLPEGY TIFCDRALPG EHLRARITAV KKTHASAVKV ASMQQHSHAV
EAPCKHYSEG CGGCSVQNLA YSAQLAAKEQ QVVDALGRIG KVEGARALVK PILPCAKPFR
YRNKMGFSFA QDVPQLPRAA GFGLRHISNP KEVPILSFTV GNSQMHCSVQ VLPVWDCWLQ
DEGANRILQV LTTAVQTKRD SQELPMLQPW TKIKVFQPTV SKVTIRSGLN PDTGNRAYLV
ILHTAGERPK ALIPIVDHLR REVPEIAGIL QYTGLGRKAE DSADGLALIS GKDRIMERLC
GLEFAITPLS FFQTNPKQTE TLYKAVADAA GLSGSEVLLD LYSGTGTIAL CLARKCSKVF
GVESNQHAVD DAMENARHNR VTNATFLQAD LSKPSDVAHV AERVPQPDVV VADPARAGLG
KPVIEYLMGC GASTLVYVSC NPATQARDIQ LLTDTAAPNS FCLESVQPVD MFPHTEHIES
VVML
//
