ID H3ZJN9_THELN Unreviewed; 383 AA.
AC H3ZJN9;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 63.
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=OCC_11035 {ECO:0000313|EMBL:EHR79831.1};
OS Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=523849 {ECO:0000313|EMBL:EHR79831.1, ECO:0000313|Proteomes:UP000015502};
RN [1] {ECO:0000313|EMBL:EHR79831.1, ECO:0000313|Proteomes:UP000015502}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51850 / DSM 5473 / JCM 8560 / NS-C
RC {ECO:0000313|Proteomes:UP000015502};
RX PubMed=22493191; DOI=10.1128/JB.00123-12;
RA Gardner A.F., Kumar S., Perler F.B.;
RT "Genome sequence of the model hyperthermophilic archaeon Thermococcus
RT litoralis NS-C.";
RL J. Bacteriol. 194:2375-2376(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 ECO:0000256|PROSITE-ProRule:PRU01023}.
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DR EMBL; CP006670; EHR79831.1; -; Genomic_DNA.
DR RefSeq; WP_004066170.1; NC_022084.1.
DR AlphaFoldDB; H3ZJN9; -.
DR STRING; 523849.OCC_11035; -.
DR PaxDb; 523849-OCC_11035; -.
DR GeneID; 16549729; -.
DR KEGG; tlt:OCC_11035; -.
DR HOGENOM; CLU_005316_1_0_2; -.
DR OrthoDB; 14725at2157; -.
DR Proteomes; UP000015502; 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; cd02440; AdoMet_MTases; 1.
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; IPR031341; Methyltr_RsmF_N.
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; PF17125; Methyltr_RsmF_N; 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 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 101..382
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT ACT_SITE 323
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02237,
FT ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 205..211
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02237,
FT ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 229
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02237,
FT ECO:0000256|PROSITE-ProRule:PRU01023"
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 256
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02237,
FT ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 273
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02237,
FT ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 300
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02237"
SQ SEQUENCE 383 AA; 43539 MW; 16B733ADEF1B9574 CRC64;
MYKEAFPEEL QRYYYNLFGS EAEEIMKKLR EPVEKYYIRV NTLKISRQKL MEELRKEGLK
PKRSPYLEEG IYFEREGPNF PDDYEPKLPK VVANKFAAES VYQGAQLYAP GVLKADKGIK
EGDEVQIRDP KGLLVGIGIA RMSAKEMVVA TRGIAVEVTL PKFKLPSLNE LKAYEKGYFY
AQSLPSMVVA HILEPQEEDL IIDMAAAPGG KTSHIAQLLE NRGEIIAIDK SRNRLAKMEK
ELKRLGVKNV KLVQMDSRNL PGLGIKADKI LLDAPCTALG VRPKLWETRT PKDIEATVRY
QRHFINAAIK SLRKGGILVY STCTLSYEEN EGNVQYMLKK GLKLEEQKIF IGSPGLGIKE
VQRFYPHKHL TQGFFIAKLR KVS
//
