ID   TMG10_PYRAB             Reviewed;         329 AA.
AC   Q9UY84; G8ZJX8;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 2.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=tRNA (guanine(10)-N2)-dimethyltransferase;
DE            EC=2.1.1.213;
DE   AltName: Full=(Pab)Trm-G10;
DE   AltName: Full=tRNA:G10 dimethyltransferase;
GN   Name=trmG10; OrderedLocusNames=PYRAB16240; ORFNames=PAB1283;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, TRNA-BINDING, GENE NAME, TEMPERATURE
RP   DEPENDENCE, AND SUBUNIT.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=15210688; DOI=10.1074/jbc.m403845200;
RA   Armengaud J., Urbonavicius J., Fernandez B., Chaussinand G., Bujnicki J.M.,
RA   Grosjean H.;
RT   "N2-methylation of guanosine at position 10 in tRNA is catalyzed by a THUMP
RT   domain-containing, S-adenosylmethionine-dependent methyltransferase,
RT   conserved in Archaea and Eukaryota.";
RL   J. Biol. Chem. 279:37142-37152(2004).
CC   -!- FUNCTION: Catalyzes the adenosylmethionine-dependent methylation of the
CC       exocyclic amino group (N(2)) of guanosine at position 10 of various
CC       tRNAs. Acts via a two-step process that leads to the formation of
CC       either N(2)-monomethyl (m(2)G) or N(2)-dimethylguanosine (m(2)(2)G).
CC       {ECO:0000269|PubMed:15210688}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(10) in tRNA + 2 S-adenosyl-L-methionine = 2 H(+) +
CC         N(2)-dimethylguanosine(10) in tRNA + 2 S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:43124, Rhea:RHEA-COMP:10355, Rhea:RHEA-COMP:10358,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74269, ChEBI:CHEBI:74513; EC=2.1.1.213;
CC         Evidence={ECO:0000269|PubMed:15210688};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Hyperthermostable. Remains fully active after 2 hours of incubation
CC         at 80 degrees Celsius. {ECO:0000269|PubMed:15210688};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15210688}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. Trm-G10
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB50528.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AJ248288; CAB50528.1; ALT_INIT; Genomic_DNA.
DR   EMBL; HE613800; CCE71085.1; -; Genomic_DNA.
DR   PIR; B75011; B75011.
DR   AlphaFoldDB; Q9UY84; -.
DR   SMR; Q9UY84; -.
DR   STRING; 272844.PAB1283; -.
DR   EnsemblBacteria; CAB50528; CAB50528; PAB1283.
DR   KEGG; pab:PAB1283; -.
DR   PATRIC; fig|272844.11.peg.1734; -.
DR   eggNOG; arCOG00047; Archaea.
DR   HOGENOM; CLU_057819_1_0_2; -.
DR   BioCyc; MetaCyc:MON-16615; -.
DR   BRENDA; 2.1.1.213; 5242.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004809; F:tRNA (guanine-N2-)-methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0000049; F:tRNA binding; IDA:UniProtKB.
DR   GO; GO:0030488; P:tRNA methylation; IDA:UniProtKB.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR000241; RNA_methylase_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR004114; THUMP_dom.
DR   InterPro; IPR005885; TrmG10.
DR   Pfam; PF02926; THUMP; 1.
DR   Pfam; PF01170; UPF0020; 1.
DR   SMART; SM00981; THUMP; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR01177; TIGR01177; 1.
DR   PROSITE; PS51165; THUMP; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Methyltransferase; RNA-binding; S-adenosyl-L-methionine;
KW   Transferase; tRNA processing; tRNA-binding.
FT   CHAIN           1..329
FT                   /note="tRNA (guanine(10)-N2)-dimethyltransferase"
FT                   /id="PRO_0000406916"
FT   DOMAIN          40..143
FT                   /note="THUMP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00529"
SQ   SEQUENCE   329 AA;  37250 MW;  337C7C98E2967EFC CRC64;
     MFYVEILGLL PEMAEAEVKA LAELRNGTIK ERDYLLVVGN VENVEIFERL GLAHEYGILL
     GSGDDVRDIL DLVRGLEWKE IIKGTFAVRK EVMVNCAHEV KNLEKIIGGI IHSQGLRVNL
     SKPDTIIKVY CGRKLWIGIR IREFRGKEFD ERKADRRPFS RPIALPPRIA RAMVNLTRAT
     REILDPFMGT GGMLIEAGLM GLKVYGIDIR EDMVEGAKIN LEYYGVKDYV VKVGDATKIK
     EAFPGKTFEA IATDPPYGTS TTLPMDRDEL YKRALESMYS VLEGRLAIAF PSDFDALDVA
     ETIGFKVIGR FYQRVHSSLS RYFYIMEAR