ID A4YH70_METS5 Unreviewed; 346 AA.
AC A4YH70;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=tRNA (cytosine(72)-C(5))-methyltransferase {ECO:0000256|HAMAP-Rule:MF_02237};
DE Short=tRNA:m(5)C72 MTase {ECO:0000256|HAMAP-Rule:MF_02237};
DE EC=2.1.1.- {ECO:0000256|HAMAP-Rule:MF_02237};
GN OrderedLocusNames=Msed_1617 {ECO:0000313|EMBL:ABP95772.1};
OS Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509
OS / TH2).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Metallosphaera.
OX NCBI_TaxID=399549 {ECO:0000313|EMBL:ABP95772.1, ECO:0000313|Proteomes:UP000000242};
RN [1] {ECO:0000313|EMBL:ABP95772.1, ECO:0000313|Proteomes:UP000000242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2
RC {ECO:0000313|Proteomes:UP000000242};
RX PubMed=18083856; DOI=10.1128/AEM.02019-07;
RA Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.;
RT "The genome sequence of the metal-mobilizing, extremely thermoacidophilic
RT archaeon Metallosphaera sedula provides insights into bioleaching-
RT associated metabolism.";
RL Appl. Environ. Microbiol. 74:682-692(2008).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC specifically methylates the C5 position of cytosine 72 in several
CC tRNAs. {ECO:0000256|HAMAP-Rule:MF_02237}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(72) in tRNA + S-adenosyl-L-methionine = 5-
CC methylcytidine(72) in tRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:61988, Rhea:RHEA-COMP:15996, Rhea:RHEA-COMP:15997,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74483, ChEBI:CHEBI:82748; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_02237};
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. {ECO:0000256|HAMAP-Rule:MF_02237}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02237}.
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DR EMBL; CP000682; ABP95772.1; -; Genomic_DNA.
DR AlphaFoldDB; A4YH70; -.
DR STRING; 399549.Msed_1617; -.
DR KEGG; mse:Msed_1617; -.
DR eggNOG; arCOG00973; Archaea.
DR eggNOG; arCOG00986; Archaea.
DR HOGENOM; CLU_005316_1_0_2; -.
DR Proteomes; UP000000242; Chromosome.
DR GO; GO:0016428; F:tRNA (cytidine-5-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-UniRule.
DR CDD; cd07953; PUA; 1.
DR Gene3D; 2.30.130.10; PUA domain; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_02237; NSUN6; 1.
DR InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR InterPro; IPR043699; NSUN6.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR036974; PUA_sf.
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:SF78; TRNA (CYTOSINE(72)-C(5))-METHYLTRANSFERASE; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 1.
DR PRINTS; PR02008; RCMTFAMILY.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS50890; PUA; 1.
DR PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_02237}; Reference proteome {ECO:0000313|Proteomes:UP000000242};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_02237};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_02237};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_02237}.
FT DOMAIN 84..346
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT ACT_SITE 304
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02237"
FT BINDING 209
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02237"
FT BINDING 214
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02237"
FT BINDING 235
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02237"
FT BINDING 254
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02237"
FT BINDING 281
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02237"
SQ SEQUENCE 346 AA; 39886 MW; 6B6FD7C801A174EB CRC64;
MNGPELIYDE FVMEELRRVY GSSLNEYLEY LGRPNPRLYI RLNTLRKQEL KEELHEFKQD
EDFEEAYFVE VRGPNFLEMR DTKVVVDKKT AESAMLGSNV YKPGIKRIEG NGSRVSVVSE
TGNHVANGIL RRDNMIVEVT ESLYSSIKVA ELDVVKRGLA ISQGKASMYV AKLLDPRPDE
IIVDMNAYPG GKLTHVYQLQ PKAKIMGFDH TRKKIDKLRN ILDTLKMKMD VYVADSRYLY
EDLGIRNVDK VMIDPPCSAL GVRPKIFDRK TKEDIQNFSS YQKQFLNSAY KILKPGGTVI
YSTCTTTLAE NEEVITDPRF EIEFMIRFHP NVHQMTGFFI AKLIKR
//
