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Database: UniProt
Entry: A0A150JAX4_9EURY
LinkDB: A0A150JAX4_9EURY
Original site: A0A150JAX4_9EURY 
ID   A0A150JAX4_9EURY        Unreviewed;       321 AA.
AC   A0A150JAX4;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=tRNA (Cytosine(48)-C(5))-methyltransferase {ECO:0000313|EMBL:KYC54228.1};
DE            EC=2.1.1.- {ECO:0000313|EMBL:KYC54228.1};
GN   Name=trm4 {ECO:0000313|EMBL:KYC54228.1};
GN   ORFNames=AMQ74_00095 {ECO:0000313|EMBL:KYC54228.1};
OS   Candidatus Methanofastidiosum methylthiophilus.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Candidatus Methanofastidiosa;
OC   Methanofastidiosum.
OX   NCBI_TaxID=1705564 {ECO:0000313|EMBL:KYC54228.1, ECO:0000313|Proteomes:UP000075578};
RN   [1] {ECO:0000313|EMBL:KYC54228.1, ECO:0000313|Proteomes:UP000075578}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U1lsi0528_Bin089 {ECO:0000313|EMBL:KYC54228.1};
RX   PubMed=26943620;
RA   Nobu M.K., Narihiro T., Kuroda K., Mei R., Liu W.T.;
RT   "Chasing the elusive Euryarchaeota class WSA2: genomes reveal a uniquely
RT   fastidious methyl-reducing methanogen.";
RL   ISME J. 0:0-0(2016).
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RsmB/NOP family. {ECO:0000256|PROSITE-ProRule:PRU01023}.
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:KYC54228.1}.
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DR   EMBL; LNGD01000003; KYC54228.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A150JAX4; -.
DR   Proteomes; UP000075578; Unassembled WGS sequence.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR031341; Methyltr_RsmF_N.
DR   InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR   InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR   InterPro; IPR011023; Nop2p.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR00446; nop2p; 1.
DR   PANTHER; PTHR22807:SF30; 28S RRNA (CYTOSINE(4447)-C(5))-METHYLTRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   Pfam; PF17125; Methyltr_RsmF_N; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01023};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU01023};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU01023};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU01023}.
FT   DOMAIN          36..320
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        246
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         125..131
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         149
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         176
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         193
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   321 AA;  36341 MW;  FAB022E34F570741 CRC64;
     MFVDLMKLSD LAKEYGYSFD NLKRYNEMFG DKLPLFLEAN EVQNKDSIRI NTIKISREEL
     YERLTKNGFV IKEINDFGYI IEESKFAISS TQENLLGYCY IQGVAEMHVA PILSPDKNDF
     VVDMCAAPGG KTTHLSAIMK NEGTIYAFDV NKRRLSALKN NISRLGCMNI AVFNLDGLEI
     SKLKNKPDKI LLDAPCTGSG IMRKDSLRKS LKSTHDIIFL SEIQKKLLKA AIENLNTGGT
     LLYTTCSLEP EENEFVVQWA LDNFNIRLLN INTEIGGIPL QSGFTEIFNR KLSDEIKLCK
     RSFPHVHNTN GLFMAKIIKS E
//
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