ID A0A0U5HYV8_9PROT Unreviewed; 440 AA.
AC A0A0U5HYV8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Putative tRNA and rRNA cytosine-C5-methylase(Bacterial Fmu (Sun)/eukaryotic nucleolar NOL1/Nop2p,166-435) {ECO:0000313|EMBL:CUW38646.1};
DE EC=2.1.1.- {ECO:0000313|EMBL:CUW38646.1};
GN ORFNames=XM1_1577 {ECO:0000313|EMBL:CUW38646.1};
OS Magnetospirillum sp. XM-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=1663591 {ECO:0000313|EMBL:CUW38646.1, ECO:0000313|Proteomes:UP000063191};
RN [1] {ECO:0000313|Proteomes:UP000063191}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wang Y.;
RL Submitted (DEC-2015) 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; LN997848; CUW38646.1; -; Genomic_DNA.
DR RefSeq; WP_068432038.1; NZ_LN997848.1.
DR AlphaFoldDB; A0A0U5HYV8; -.
DR STRING; 1663591.XM1_1577; -.
DR KEGG; magx:XM1_1577; -.
DR PATRIC; fig|1663591.3.peg.1570; -.
DR OrthoDB; 9810297at2; -.
DR Proteomes; UP000063191; Chromosome I.
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 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; IPR023267; RCMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR22807:SF77; SUN PROTEIN; 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};
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 159..438
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT ACT_SITE 373
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 273
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 320
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 440 AA; 49043 MW; 4AB938B6D3DF9097 CRC64;
MTPAARLQAA IEVLSEIEKS AKPADSVASF YFKQRRYIGA KDRRAVAETV WRVLRRRARL
DWWLEHLEHP ERPDAEGRGG ARARVLADMV FEGIRPEPDL FKGPHSAYPP EPPERRVLDM
LAGQKSLFHR DMPPHVRGEY PEWMTPRLAA LFGERLESEM GAMRDEAPLD LRVNTLKATR
EDAIRALAKE GIKSEPTALS PIGLRLYARV PLVQVQAWRN GLIEVQDEGS QLVALLTDPK
PGQAVVDYCA GAGGKTLALA ASMQNKGRLV ACDVAEWRVD RAQDRLRRAG VHNVTRRVIE
GESDKWIKRS AGSFDRVLVD APCTGTGTWR RNPDAKWQFA ETDLLELVAR QGAILESAAR
LTKPGGRLIY ATCSIMREEN EERVEAFLAA HPDYRPVPVP EIWTELAGTP CPVPGPWLRL
SPLAHGTDGF FAAVLEKAIS
//
