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Database: UniProt
Entry: D3ALK3_9CLOT
LinkDB: D3ALK3_9CLOT
Original site: D3ALK3_9CLOT 
ID   D3ALK3_9CLOT            Unreviewed;       474 AA.
AC   D3ALK3;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=NOL1/NOP2/sun family protein {ECO:0000313|EMBL:EFC97302.1};
GN   ORFNames=CLOSTHATH_04499 {ECO:0000313|EMBL:EFC97302.1};
OS   Hungatella hathewayi DSM 13479.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Hungatella.
OX   NCBI_TaxID=566550 {ECO:0000313|EMBL:EFC97302.1, ECO:0000313|Proteomes:UP000004968};
RN   [1] {ECO:0000313|EMBL:EFC97302.1, ECO:0000313|Proteomes:UP000004968}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13479 {ECO:0000313|EMBL:EFC97302.1,
RC   ECO:0000313|Proteomes:UP000004968};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RsmB/NOP family. {ECO:0000256|PROSITE-ProRule:PRU01023}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {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:EFC97302.1}.
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DR   EMBL; ACIO01000408; EFC97302.1; -; Genomic_DNA.
DR   RefSeq; WP_006774938.1; NZ_GG667705.1.
DR   AlphaFoldDB; D3ALK3; -.
DR   HOGENOM; CLU_005316_6_1_9; -.
DR   Proteomes; UP000004968; 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:0001510; P:RNA methylation; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   CDD; cd21147; RsmF_methylt_CTD1; 1.
DR   Gene3D; 2.30.130.60; -; 1.
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; IPR027391; Nol1_Nop2_Fmu_2.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR031340; RsmF_methylt_CI.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
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   Pfam; PF13636; Methyltranf_PUA; 1.
DR   Pfam; PF17126; RsmF_methylt_CI; 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          18..303
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        232
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         110..116
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         134
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         179
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   474 AA;  54035 MW;  904A0E43236B5E1C CRC64;
     MTELPEAFKE KMKNLLGTEY EAFLESYEKE RVQGLRLNPG KTDEKEFLAK VPFHLTKIPW
     AREGYYYDSS DRPGKHPYHE AGLYYIQEPS AMAVVELLDP KPGDCVLDLC AAPGGKTTQI
     AGRLMGEGFL LSNEIHPARA KILSQNVERM GIRNAVVANE TPERLAERFP EFFDGMVVDA
     PCSGEGMFRK DEEACRQWSP DHVVMCAARQ RQILDSAARM LKAGGRMVYS TCTFSPEEDE
     QTIEMFLSEH PEFEIEDMGV REGLSPGKPE WGISAAETLR GTYRIWPHLS EGEGHYLAVL
     RKTGEDCGTW KRKAPAYLKD KAVHKEYEGF CRNLFTDPER YLDREEYILF GDQLYLLPPQ
     MIDLAGLKIV RPGLHMGTMK KNRFEPSHAL ALSMKKEEAV RRFPMKAEGQ EAGRYLKGET
     LRIDDWLRPE ESENCRLNGQ KGWVLMTVDG WPLGFSKLAG GILKNHYPRG LRWL
//
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