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Database: UniProt
Entry: D9QRM9_ACEAZ
LinkDB: D9QRM9_ACEAZ
Original site: D9QRM9_ACEAZ 
ID   D9QRM9_ACEAZ            Unreviewed;       244 AA.
AC   D9QRM9;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   26-FEB-2020, entry version 56.
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   OrderedLocusNames=Acear_1665 {ECO:0000313|EMBL:ADL13170.1};
OS   Acetohalobium arabaticum (strain ATCC 49924 / DSM 5501 / Z-7288).
OC   Bacteria; Firmicutes; Clostridia; Halanaerobiales; Halobacteroidaceae;
OC   Acetohalobium.
OX   NCBI_TaxID=574087 {ECO:0000313|EMBL:ADL13170.1, ECO:0000313|Proteomes:UP000001661};
RN   [1] {ECO:0000313|EMBL:ADL13170.1, ECO:0000313|Proteomes:UP000001661}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49924 / DSM 5501 / Z-7288
RC   {ECO:0000313|Proteomes:UP000001661};
RX   PubMed=21304692;
RA   Sikorski J., Lapidus A., Chertkov O., Lucas S., Copeland A.,
RA   Glavina Del Rio T., Nolan M., Tice H., Cheng J.F., Han C., Brambilla E.,
RA   Pitluck S., Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A.,
RA   Bruce D., Detter C., Tapia R., Goodwin L., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Goker M.,
RA   Spring S., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Acetohalobium arabaticum type strain (Z-
RT   7288).";
RL   Stand. Genomic Sci. 3:57-65(2010).
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}.
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DR   EMBL; CP002105; ADL13170.1; -; Genomic_DNA.
DR   RefSeq; WP_013278615.1; NC_014378.1.
DR   STRING; 574087.Acear_1665; -.
DR   EnsemblBacteria; ADL13170; ADL13170; Acear_1665.
DR   KEGG; aar:Acear_1665; -.
DR   eggNOG; ENOG4105D6X; Bacteria.
DR   eggNOG; COG0336; LUCA.
DR   HOGENOM; CLU_047363_0_1_9; -.
DR   KO; K00554; -.
DR   OMA; ILCGHYK; -.
DR   OrthoDB; 525632at2; -.
DR   BioCyc; AARA574087:G1GMC-1727-MONOMER; -.
DR   Proteomes; UP000001661; Chromosome.
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:ADL13170.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001661};
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:ADL13170.1};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_00605,
KW   ECO:0000256|RuleBase:RU003464, ECO:0000256|SAAS:SAAS01085083}.
FT   DOMAIN          24..219
FT                   /note="tRNA_m1G_MT"
FT                   /evidence="ECO:0000259|Pfam:PF01746"
FT   REGION          131..136
FT                   /note="S-adenosyl-L-methionine binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00605,
FT                   ECO:0000256|PIRSR:PIRSR000386-1"
FT   BINDING         111
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   244 AA;  27831 MW;  51216AAECF6F681F CRC64;
     MLKFHILTIF PEMFTGPLNE SILKRAQNEE LIKIDITDIR SFAQNKHNNV DDAPYGGGAG
     MVMKPEPIFR AVEDVESDES KVIFLSPQGK TFDQKIAKEL AEEEHLVLLC GRYEGVDERV
     RKEVVDEEIS IGDYVLTGGE LSAMVVIDAV ARMIPGVLGT HQSAVEDSFY HGILDYPHYT
     RPRKYRSLEV PEVLLSGDHQ KIADWRKKQA LKRTLLRRPD LLEEVELSDE ERELLSNIKK
     ELDK
//
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