ID I3TE07_THEC1 Unreviewed; 392 AA.
AC I3TE07;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=TCELL_0570 {ECO:0000313|EMBL:AFK50995.1};
OS Thermogladius calderae (strain DSM 22663 / VKM B-2946 / 1633).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Thermogladius.
OX NCBI_TaxID=1184251 {ECO:0000313|EMBL:AFK50995.1, ECO:0000313|Proteomes:UP000005270};
RN [1] {ECO:0000313|EMBL:AFK50995.1, ECO:0000313|Proteomes:UP000005270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22663 / VKM B-2946 / 1633
RC {ECO:0000313|Proteomes:UP000005270};
RX PubMed=22843584; DOI=10.1128/JB.00894-12;
RA Mardanov A.V., Kochetkova T.V., Beletsky A.V., Bonch-Osmolovskaya E.A.,
RA Ravin N.V., Skryabin K.G.;
RT "Complete genome sequence of the hyperthermophilic cellulolytic
RT Crenarchaeon 'Thermogladius cellulolyticus' 1633.";
RL J. Bacteriol. 194:4446-4447(2012).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003531; AFK50995.1; -; Genomic_DNA.
DR AlphaFoldDB; I3TE07; -.
DR STRING; 1184251.TCELL_0570; -.
DR KEGG; thg:TCELL_0570; -.
DR eggNOG; arCOG00973; Archaea.
DR eggNOG; arCOG00986; Archaea.
DR HOGENOM; CLU_005316_1_0_2; -.
DR InParanoid; I3TE07; -.
DR Proteomes; UP000005270; 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; 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 PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR22807:SF34; TRNA (CYTOSINE(72)-C(5))-METHYLTRANSFERASE NSUN6; 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}; Reference proteome {ECO:0000313|Proteomes:UP000005270};
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 112..392
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT ACT_SITE 330
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02237"
FT BINDING 232
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02237"
FT BINDING 237
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02237"
FT BINDING 260
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02237"
FT BINDING 280
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02237"
FT BINDING 307
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02237"
SQ SEQUENCE 392 AA; 44068 MW; D153B1500883614E CRC64;
MHKYEGDEVQ ATRIDHGLYM ELRGVYGSLT DRLLEMLTYP PKRLYLRVNT LRTRREEVVE
SLRRRGVEVR PDDLLEEAIY IELEGPYQVR DHGRRIVVDD IAAESLMMGA NLYRPGVVAY
DMFKRGDVLT AVTKNGFVVA ELEASVSSDQ LKSMRKGLVA VNTRSVYKAP PIAELPEFKE
GLVYPQSFPS MVAGRLVFPG SELVVDMNAS PGGKTGHIVQ LSRGKALVLA VDRSVGKVEK
LVENLARLGL TSNVLPLPFD SRFLDLVTLL ENRVDKVLID PPCTNLGVRP KLSFKKTLRD
AINLADYQRQ FMKVAGRLLR PGGVLVYSTC TLTRVENEEN VLYATRSLGL EPLDLGWVPR
ADKVYLDETA AYRFHPLKDD MPGFFIAVFR KP
//
