ID V4K1F3_9CREN Unreviewed; 384 AA.
AC V4K1F3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=OSP8Acid_12500 {ECO:0000313|EMBL:ESQ24684.1};
OS uncultured Acidilobus sp. OSP8.
OC Archaea; Thermoproteota; Thermoprotei; Acidilobales; Acidilobaceae;
OC Acidilobus; environmental samples.
OX NCBI_TaxID=1410575 {ECO:0000313|EMBL:ESQ24684.1, ECO:0000313|Proteomes:UP000018061};
RN [1] {ECO:0000313|EMBL:ESQ24684.1, ECO:0000313|Proteomes:UP000018061}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Jay Z.J., Rusch D.B., Tringe S.G., Bailey C., Jennings R.M., Inskeep W.P.;
RT "Predominant Acidilobus-like populations from geothermal environments of
RT Yellowstone National Park exhibit similar metabolic potential in different
RT hypoxic microbial communities.";
RL Submitted (OCT-2013) 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:ESQ24684.1}.
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DR EMBL; AYMC01000015; ESQ24684.1; -; Genomic_DNA.
DR AlphaFoldDB; V4K1F3; -.
DR PATRIC; fig|1410575.3.peg.1179; -.
DR Proteomes; UP000018061; 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; 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; 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 108..377
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT ACT_SITE 320
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02237"
FT BINDING 224
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02237"
FT BINDING 228
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02237"
FT BINDING 250
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02237"
FT BINDING 270
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02237"
FT BINDING 297
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02237"
SQ SEQUENCE 384 AA; 42129 MW; 7288D5EC45F7C3AD CRC64;
MSLSYDNELL ENLEPVSKRG VKALLEALTR PPRRYYVRVN TLKATTEEVL QRLELLGLKF
HRDEEIDCAI YSEVEGPYKI DVEGKIVVAD KRSSEAVYVG SDLYAPGVIR AEGVRKGDRV
TVVTPEGMPV GVGIAMMDSK EIFSKRAGLA VKVERSVYVA PKVGALKEVH EGLIYSQSLP
SMWAVMTANP RPGELIVDMN AAPGGKVSMV AQIAGPSAKI IAIDRESKAE RLKQNLKTLG
ADWITVIGGD SRYASDTLNL REAVDLVLID PPCTNLGVVP KLSDKKTLQD AVTLARYQVQ
FVREAWRLLK PGGRLVYSTC TLTDVENEGV VAQAEDIGFE VERPERVSRW ASYNGVGLRF
SPEDGVPGFF IALLRKPVKG SDKV
//
