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Database: UniProt
Entry: A0A1G2LVR8_9BACT
LinkDB: A0A1G2LVR8_9BACT
Original site: A0A1G2LVR8_9BACT 
ID   A0A1G2LVR8_9BACT        Unreviewed;       232 AA.
AC   A0A1G2LVR8;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   26-FEB-2020, entry version 13.
DE   RecName: Full=tRNA (guanine-N(1)-)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_00605, ECO:0000256|RuleBase:RU003464, ECO:0000256|SAAS:SAAS01166819};
DE            EC=2.1.1.228 {ECO:0000256|HAMAP-Rule:MF_00605, ECO:0000256|RuleBase:RU003464, ECO:0000256|SAAS:SAAS01166822};
DE   AltName: Full=M1G-methyltransferase {ECO:0000256|HAMAP-Rule:MF_00605};
DE   AltName: Full=tRNA [GM37] methyltransferase {ECO:0000256|HAMAP-Rule:MF_00605};
GN   Name=trmD {ECO:0000256|HAMAP-Rule:MF_00605};
GN   ORFNames=A3A10_02880 {ECO:0000313|EMBL:OHA15738.1};
OS   Candidatus Tagabacteria bacterium RIFCSPLOWO2_01_FULL_42_9.
OC   Bacteria; Candidatus Tagabacteria.
OX   NCBI_TaxID=1802296 {ECO:0000313|EMBL:OHA15738.1, ECO:0000313|Proteomes:UP000178116};
RN   [1] {ECO:0000313|EMBL:OHA15738.1, ECO:0000313|Proteomes:UP000178116}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
CC   -!- FUNCTION: Specifically methylates guanosine-37 in various tRNAs.
CC       {ECO:0000256|HAMAP-Rule:MF_00605, ECO:0000256|RuleBase:RU003464,
CC       ECO:0000256|SAAS:SAAS01166823}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-
CC         methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:36899, Rhea:RHEA-COMP:10145, Rhea:RHEA-COMP:10147,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:73542, ChEBI:CHEBI:74269; EC=2.1.1.228;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00605,
CC         ECO:0000256|RuleBase:RU003464, ECO:0000256|SAAS:SAAS01166817};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00605,
CC       ECO:0000256|RuleBase:RU003464, ECO:0000256|SAAS:SAAS01166828}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00605,
CC       ECO:0000256|RuleBase:RU003464, ECO:0000256|SAAS:SAAS01085120}.
CC   -!- SIMILARITY: Belongs to the RNA methyltransferase TrmD family.
CC       {ECO:0000256|HAMAP-Rule:MF_00605, ECO:0000256|RuleBase:RU003464,
CC       ECO:0000256|SAAS:SAAS01166827}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00605}.
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:OHA15738.1}.
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DR   EMBL; MHRA01000013; OHA15738.1; -; Genomic_DNA.
DR   Proteomes; UP000178116; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0052906; F:tRNA (guanine(37)-N(1))-methyltransferase activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.10.1270.20; -; 1.
DR   Gene3D; 3.40.1280.10; -; 1.
DR   HAMAP; MF_00605; TrmD; 1.
DR   InterPro; IPR029028; Alpha/beta_knot_MTases.
DR   InterPro; IPR002649; tRNA_m1G_MeTrfase_bac.
DR   InterPro; IPR023148; tRNA_m1G_MeTrfase_C.
DR   InterPro; IPR029026; tRNA_m1G_MTases_N.
DR   InterPro; IPR016009; tRNA_MeTrfase_TRMD/TRM10.
DR   PANTHER; PTHR46417; PTHR46417; 1.
DR   Pfam; PF01746; tRNA_m1G_MT; 1.
DR   PIRSF; PIRSF000386; tRNA_mtase; 1.
DR   SUPFAM; SSF75217; SSF75217; 1.
DR   TIGRFAMs; TIGR00088; trmD; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00605, ECO:0000256|RuleBase:RU003464,
KW   ECO:0000256|SAAS:SAAS01085106};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00605,
KW   ECO:0000256|RuleBase:RU003464, ECO:0000256|SAAS:SAAS00436078,
KW   ECO:0000313|EMBL:OHA15738.1};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00605,
KW   ECO:0000256|PIRSR:PIRSR000386-1, ECO:0000256|RuleBase:RU003464,
KW   ECO:0000256|SAAS:SAAS00436073};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00605,
KW   ECO:0000256|RuleBase:RU003464, ECO:0000256|SAAS:SAAS00436122,
KW   ECO:0000313|EMBL:OHA15738.1};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_00605,
KW   ECO:0000256|RuleBase:RU003464, ECO:0000256|SAAS:SAAS01085083}.
FT   DOMAIN          24..228
FT                   /note="tRNA_m1G_MT"
FT                   /evidence="ECO:0000259|Pfam:PF01746"
FT   BINDING         116
FT                   /note="S-adenosyl-L-methionine; via amide nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00605,
FT                   ECO:0000256|PIRSR:PIRSR000386-1"
SQ   SEQUENCE   232 AA;  26829 MW;  EBBA921E7924010A CRC64;
     MTTFHIFTIF PESFKSYFNV SILKRAQKKR IIKIKIYNIR DFAKDKHKTV DDRPYGGGAG
     MLMKPLPIIK AVDKIVSKIN RKKMKIIVFS AKGRQFNQKM AFDWSKKYKD IIMICGRYEG
     IDERVKNVLK AQEISIGPYV LTDGEIPAMI LVSGLSRLLP GAIRWDSLQE ESFSGKNIKN
     EKKGLLEYPQ YTRPDFFKHP SVGGKKYSVP KVLLRGDHKK ISEWRKKHGK MT
//
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