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TRM1_PYRHO
ID   TRM1_PYRHO              Reviewed;         381 AA.
AC   O59493;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=tRNA (guanine(26)-N(2))-dimethyltransferase {ECO:0000255|HAMAP-Rule:MF_00290};
DE            EC=2.1.1.216 {ECO:0000255|HAMAP-Rule:MF_00290};
DE   AltName: Full=tRNA 2,2-dimethylguanosine-26 methyltransferase {ECO:0000255|HAMAP-Rule:MF_00290};
DE   AltName: Full=tRNA(guanine-26,N(2)-N(2)) methyltransferase {ECO:0000255|HAMAP-Rule:MF_00290};
DE   AltName: Full=tRNA(m(2,2)G26)dimethyltransferase {ECO:0000255|HAMAP-Rule:MF_00290};
GN   Name=trm1 {ECO:0000255|HAMAP-Rule:MF_00290}; OrderedLocusNames=PH1829;
OS   Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS   100139 / OT-3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=70601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX   PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA   Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA   Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA   Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA   Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA   Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT   "Complete sequence and gene organization of the genome of a hyper-
RT   thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL   DNA Res. 5:55-76(1998).
CC   -!- FUNCTION: Dimethylates a single guanine residue at position 26 of a
CC       number of tRNAs using S-adenosyl-L-methionine as donor of the methyl
CC       groups. {ECO:0000255|HAMAP-Rule:MF_00290}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(26) in tRNA + 2 S-adenosyl-L-methionine = 2 H(+) +
CC         N(2)-dimethylguanosine(26) in tRNA + 2 S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:43140, Rhea:RHEA-COMP:10359, Rhea:RHEA-COMP:10360,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74269, ChEBI:CHEBI:74513; EC=2.1.1.216;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00290};
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Trm1 family. {ECO:0000255|HAMAP-Rule:MF_00290}.
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DR   EMBL; BA000001; BAA30948.1; -; Genomic_DNA.
DR   PIR; E71194; E71194.
DR   PDB; 2DUL; X-ray; 1.90 A; A=4-381.
DR   PDB; 2EJT; X-ray; 2.20 A; A=4-381.
DR   PDB; 2EJU; X-ray; 1.95 A; A=4-381.
DR   PDB; 2YTZ; X-ray; 2.65 A; A/B=4-381.
DR   PDBsum; 2DUL; -.
DR   PDBsum; 2EJT; -.
DR   PDBsum; 2EJU; -.
DR   PDBsum; 2YTZ; -.
DR   AlphaFoldDB; O59493; -.
DR   SMR; O59493; -.
DR   STRING; 70601.3258265; -.
DR   PRIDE; O59493; -.
DR   EnsemblBacteria; BAA30948; BAA30948; BAA30948.
DR   KEGG; pho:PH1829; -.
DR   eggNOG; arCOG01219; Archaea.
DR   OMA; VFYNPVM; -.
DR   BRENDA; 2.1.1.216; 5244.
DR   EvolutionaryTrace; O59493; -.
DR   Proteomes; UP000000752; Chromosome.
DR   GO; GO:0004809; F:tRNA (guanine-N2-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.56.70; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_00290; tRNA_dimethyltr_TRM1; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR002905; Trm1.
DR   InterPro; IPR022923; TRM1_arc_bac.
DR   InterPro; IPR042296; tRNA_met_Trm1_C.
DR   PANTHER; PTHR10631; PTHR10631; 2.
DR   Pfam; PF02005; TRM; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00308; TRM1; 1.
DR   PROSITE; PS51626; SAM_MT_TRM1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Methyltransferase; RNA-binding; S-adenosyl-L-methionine;
KW   Transferase; tRNA processing; tRNA-binding.
FT   CHAIN           1..381
FT                   /note="tRNA (guanine(26)-N(2))-dimethyltransferase"
FT                   /id="PRO_0000147690"
FT   DOMAIN          7..378
FT                   /note="Trm1 methyltransferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00290"
FT   STRAND          7..11
FT                   /evidence="ECO:0007829|PDB:2DUL"
FT   STRAND          14..18
FT                   /evidence="ECO:0007829|PDB:2DUL"
FT   TURN            24..26
FT                   /evidence="ECO:0007829|PDB:2YTZ"
FT   STRAND          27..29
FT                   /evidence="ECO:0007829|PDB:2YTZ"
FT   HELIX           33..35
FT                   /evidence="ECO:0007829|PDB:2DUL"
FT   HELIX           36..49
FT                   /evidence="ECO:0007829|PDB:2DUL"
FT   STRAND          52..58
FT                   /evidence="ECO:0007829|PDB:2DUL"
FT   HELIX           63..71
FT                   /evidence="ECO:0007829|PDB:2DUL"
FT   STRAND          75..82
FT                   /evidence="ECO:0007829|PDB:2DUL"
FT   HELIX           84..97
FT                   /evidence="ECO:0007829|PDB:2DUL"
FT   STRAND          103..105
FT                   /evidence="ECO:0007829|PDB:2YTZ"
FT   STRAND          106..122
FT                   /evidence="ECO:0007829|PDB:2DUL"
FT   HELIX           124..130
FT                   /evidence="ECO:0007829|PDB:2DUL"
FT   STRAND          135..140
FT                   /evidence="ECO:0007829|PDB:2DUL"
FT   HELIX           147..156
FT                   /evidence="ECO:0007829|PDB:2DUL"
FT   STRAND          157..167
FT                   /evidence="ECO:0007829|PDB:2DUL"
FT   HELIX           170..173
FT                   /evidence="ECO:0007829|PDB:2DUL"
FT   HELIX           178..185
FT                   /evidence="ECO:0007829|PDB:2DUL"
FT   STRAND          186..188
FT                   /evidence="ECO:0007829|PDB:2DUL"
FT   HELIX           195..212
FT                   /evidence="ECO:0007829|PDB:2DUL"
FT   TURN            213..215
FT                   /evidence="ECO:0007829|PDB:2DUL"
FT   STRAND          216..226
FT                   /evidence="ECO:0007829|PDB:2DUL"
FT   STRAND          229..239
FT                   /evidence="ECO:0007829|PDB:2DUL"
FT   HELIX           240..247
FT                   /evidence="ECO:0007829|PDB:2DUL"
FT   STRAND          250..255
FT                   /evidence="ECO:0007829|PDB:2DUL"
FT   TURN            257..259
FT                   /evidence="ECO:0007829|PDB:2DUL"
FT   STRAND          262..269
FT                   /evidence="ECO:0007829|PDB:2DUL"
FT   STRAND          272..274
FT                   /evidence="ECO:0007829|PDB:2DUL"
FT   STRAND          276..280
FT                   /evidence="ECO:0007829|PDB:2DUL"
FT   HELIX           287..298
FT                   /evidence="ECO:0007829|PDB:2DUL"
FT   HELIX           305..317
FT                   /evidence="ECO:0007829|PDB:2DUL"
FT   HELIX           327..334
FT                   /evidence="ECO:0007829|PDB:2DUL"
FT   HELIX           341..350
FT                   /evidence="ECO:0007829|PDB:2DUL"
FT   STRAND          355..358
FT                   /evidence="ECO:0007829|PDB:2DUL"
FT   STRAND          361..369
FT                   /evidence="ECO:0007829|PDB:2DUL"
FT   HELIX           371..378
FT                   /evidence="ECO:0007829|PDB:2DUL"
SQ   SEQUENCE   381 AA;  43271 MW;  7D28AB17F805450E CRC64;
     MVNLELIEVQ EGKAKILIPK AESIYDSPVF YNPRMALNRD IVVVLLNILN PKIVLDALSA
     TGIRGIRFAL ETPAEEVWLN DISEDAYELM KRNVMLNFDG ELRESKGRAI LKGEKTIVIN
     HDDANRLMAE RHRYFHFIDL DPFGSPMEFL DTALRSAKRR GILGVTATDG APLCGAHPRA
     CLRKYLAVPL RGELCHEVGT RILVGVIARY AAKYDLGIDV ILAYYKDHYF RAFVKLKDGA
     RKGDETLEKL GYIYFDDKTG KFELEQGFLP TRPNAYGPVW LGPLKDEKIV SKMVKEAESL
     SLARKKQALK LLKMIDQELD IPLFYDTHAI GRRLKIETKK VEEIISALRE QGYEATRTHF
     SPTGIKTSAP YEVFIETIKR I
 
 
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