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Database: UniProt
Entry: F6BF16_METIK
LinkDB: F6BF16_METIK
Original site: F6BF16_METIK 
ID   F6BF16_METIK            Unreviewed;       264 AA.
AC   F6BF16;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=RNA methylase, NOL1/NOP2/sun family {ECO:0000313|EMBL:AEF95752.1};
GN   OrderedLocusNames=Metig_0195 {ECO:0000313|EMBL:AEF95752.1};
OS   Methanotorris igneus (strain DSM 5666 / JCM 11834 / Kol 5).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanotorris.
OX   NCBI_TaxID=880724 {ECO:0000313|Proteomes:UP000009227};
RN   [1] {ECO:0000313|EMBL:AEF95752.1, ECO:0000313|Proteomes:UP000009227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5666 / JCM 11834 / Kol 5
RC   {ECO:0000313|Proteomes:UP000009227};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Chertkov O., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Pagani I., Sieprawska-Lupa M.,
RA   Whitman W., Woyke T.;
RT   "Complete sequence of Methanotorris igneus Kol 5.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RsmB/NOP family. {ECO:0000256|ARBA:ARBA00007494,
CC       ECO:0000256|PROSITE-ProRule:PRU01023}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01023}.
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DR   EMBL; CP002737; AEF95752.1; -; Genomic_DNA.
DR   RefSeq; WP_013798361.1; NC_015562.1.
DR   AlphaFoldDB; F6BF16; -.
DR   STRING; 880724.Metig_0195; -.
DR   GeneID; 10643030; -.
DR   KEGG; mig:Metig_0195; -.
DR   HOGENOM; CLU_005316_7_0_2; -.
DR   OrthoDB; 14725at2157; -.
DR   Proteomes; UP000009227; Chromosome.
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   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
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   PRINTS; PR02008; RCMTFAMILY.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS01153; NOL1_NOP2_SUN; 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}; Reference proteome {ECO:0000313|Proteomes:UP000009227};
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          1..262
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        201
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         84..90
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         108
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         152
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   264 AA;  29542 MW;  918400939C3782F1 CRC64;
     MNLQYIRVNT LKINPETLKN RLENKGVMLK ETFLPYAFEV LESPFSVGAT PEYLFGYYFV
     QSISSMIPPI VLNPSKDDLV LDMCAAPGGK TTHLAQLMNN EGAIIAVEIK SSRMKSLKAN
     INRMGIANVI MLNMNVLHLK EKDLKFDKIL LDAPCSGNVI KDKSRSVTKE DIIYCSNRQK
     ELIDAGIDLL KEGGVLVYST CSAEEEENEG VIEYILNKRD DVELLPIENN FKGINVIEGG
     IEGTLRVIPP NEPFFIAKLM KIKD
//
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