ID A0A0F2L7H0_9CREN Unreviewed; 396 AA.
AC A0A0F2L7H0;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
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 ORFNames=TU36_06475 {ECO:0000313|EMBL:KJR71701.1};
OS Vulcanisaeta sp. AZ3.
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Vulcanisaeta.
OX NCBI_TaxID=1609231 {ECO:0000313|EMBL:KJR71701.1, ECO:0000313|Proteomes:UP000054362};
RN [1] {ECO:0000313|EMBL:KJR71701.1, ECO:0000313|Proteomes:UP000054362}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Servin-Garciduenas L.E., Martinez-Romero E.;
RT "Metagenome Sequencing of an Archaeal-Dominated Microbial Community from a
RT Hot Spring at the Los Azufres Geothermal Field, Mexico.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KJR71701.1}.
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DR EMBL; JZWU01000248; KJR71701.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2L7H0; -.
DR PATRIC; fig|1609231.3.peg.813; -.
DR Proteomes; UP000054362; Unassembled WGS sequence.
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; IPR002478; PUA.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR036974; PUA_sf.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR004521; Uncharacterised_CHP00451.
DR NCBIfam; TIGR00451; unchar_dom_2; 1.
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 Pfam; PF01472; PUA; 1.
DR PRINTS; PR02008; RCMTFAMILY.
DR SMART; SM00359; PUA; 1.
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 Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_02237};
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 106..395
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT ACT_SITE 333
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02237"
FT BINDING 234
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02237"
FT BINDING 239
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02237"
FT BINDING 262
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02237"
FT BINDING 283
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02237"
FT BINDING 310
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02237"
SQ SEQUENCE 396 AA; 44322 MW; 46F61976A6B48323 CRC64;
MASWIEIVKG HRLDHELYGY LLQYFSEGEL INIFEAIRRP PSRYYVRVNT LRISPEDLAD
RLHNRGLEVH IDEELSEALW FPVGGPNKIP SARKLVLADK RAAESVYVGA NLYVPGVVRF
EDSIKKGDEV NVLAPNGEVV AFGVAEIGSD EVRKVNGGVA VRVLTSTYSA PKIRELPEYE
AGLLYDQSLP AQWVARLVNP GPGEVIVDMN AAPGGKTSHI IQLSGGKAIV HSFDRSPAKV
QEIMRILERL GMREYCRVEA RDTRYLDIDR TDLVGVVDKV VIDPPCTDMG VRPRLFDNKT
MNLVRSMSNY QRQFIKVAWK LLKPGGILIY STCTLPPLED EDNIAYAESL GFKVVDTSVP
NASGGLVDRY ENSVVRFYPH IHDTPGFFIA RLMKPE
//
