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Database: UniProt
Entry: A0A1Q5PKP4_9ACTO
LinkDB: A0A1Q5PKP4_9ACTO
Original site: A0A1Q5PKP4_9ACTO 
ID   A0A1Q5PKP4_9ACTO        Unreviewed;       418 AA.
AC   A0A1Q5PKP4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=tRNA (guanine-N(1)-)-methyltransferase {ECO:0000256|ARBA:ARBA00014679, ECO:0000256|HAMAP-Rule:MF_00605};
DE            EC=2.1.1.228 {ECO:0000256|ARBA:ARBA00012807, ECO:0000256|HAMAP-Rule:MF_00605};
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=BSR29_06170 {ECO:0000313|EMBL:OKL47202.1};
OS   Boudabousia liubingyangii.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Boudabousia.
OX   NCBI_TaxID=1921764 {ECO:0000313|EMBL:OKL47202.1, ECO:0000313|Proteomes:UP000186785};
RN   [1] {ECO:0000313|EMBL:OKL47202.1, ECO:0000313|Proteomes:UP000186785}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VUL4_2 {ECO:0000313|EMBL:OKL47202.1,
RC   ECO:0000313|Proteomes:UP000186785};
RA   Meng X.;
RT   "Actinomyces gypaetusis sp. nov. isolated from the vulture Gypaetus
RT   barbatus in Qinghai Tibet Plateau China.";
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Specifically methylates guanosine-37 in various tRNAs.
CC       {ECO:0000256|ARBA:ARBA00002634, ECO:0000256|HAMAP-Rule:MF_00605,
CC       ECO:0000256|RuleBase:RU003464}.
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|ARBA:ARBA00001189, ECO:0000256|HAMAP-
CC         Rule:MF_00605, ECO:0000256|RuleBase:RU003464};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC       Rule:MF_00605, ECO:0000256|RuleBase:RU003464}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00605, ECO:0000256|RuleBase:RU003464}.
CC   -!- SIMILARITY: Belongs to the RNA methyltransferase TrmD family.
CC       {ECO:0000256|ARBA:ARBA00007630, ECO:0000256|HAMAP-Rule:MF_00605,
CC       ECO:0000256|RuleBase:RU003464}.
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:OKL47202.1}.
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DR   EMBL; MQSV01000004; OKL47202.1; -; Genomic_DNA.
DR   RefSeq; WP_073709436.1; NZ_MQSV01000004.1.
DR   AlphaFoldDB; A0A1Q5PKP4; -.
DR   STRING; 1921764.BSR28_08110; -.
DR   OrthoDB; 9807416at2; -.
DR   Proteomes; UP000186785; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0052906; F:tRNA (guanine(37)-N1)-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-UniRule.
DR   CDD; cd18080; TrmD-like; 1.
DR   Gene3D; 3.40.1280.10; -; 1.
DR   Gene3D; 1.10.1270.20; tRNA(m1g37)methyltransferase, domain 2; 1.
DR   HAMAP; MF_00605; TrmD; 1.
DR   InterPro; IPR029028; Alpha/beta_knot_MTases.
DR   InterPro; IPR023148; tRNA_m1G_MeTrfase_C_sf.
DR   InterPro; IPR002649; tRNA_m1G_MeTrfase_TrmD.
DR   InterPro; IPR029026; tRNA_m1G_MTases_N.
DR   InterPro; IPR016009; tRNA_MeTrfase_TRMD/TRM10.
DR   NCBIfam; TIGR00088; trmD; 1.
DR   PANTHER; PTHR46417; TRNA (GUANINE-N(1)-)-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR46417:SF1; TRNA (GUANINE-N(1)-)-METHYLTRANSFERASE; 1.
DR   Pfam; PF01746; tRNA_m1G_MT; 1.
DR   SUPFAM; SSF75217; alpha/beta knot; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00605};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW   Rule:MF_00605}; Reference proteome {ECO:0000313|Proteomes:UP000186785};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW   Rule:MF_00605};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00605};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_00605}.
FT   DOMAIN          22..237
FT                   /note="tRNA methyltransferase TRMD/TRM10-type"
FT                   /evidence="ECO:0000259|Pfam:PF01746"
FT   BINDING         122
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00605"
FT   BINDING         148..153
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00605"
SQ   SEQUENCE   418 AA;  45362 MW;  C4DE0E21C7DF2986 CRC64;
     MRIDIFTIFP DFFKVLDVSL LGKAQTSGTL EIQTHNLRDW AEGPHRSVDD TPYGGGAGMV
     MRADIWLNAL ESVLSSLPEN SSEEHASGSQ QAILVPSPSG VRLTQELAQR LSTYQQLTFC
     CGRYEGIDAR FVEALKDQEG PEVIEFSLGD YVLNGGESAT VVAIEAIARL VPEVIGNQES
     LTEESHGESG LLEYPIYTRP AEVAGLGIPE VLKSGNHADI NAWRHDRALE KTAEVRPDLL
     QIGGKARANL STYDRLFLAL RGYAFAIESA NQAHSERLSN VTEAALKQTG GFKTTHSPVI
     TKLIHKKKNY VLLLAHPCGD LISAFEVLEA AADIRHTLFG EGQVFVAAPQ AETGATPALN
     ALLDAGFKRA SNSQRRNLRS LLSSEIPGED LQVLELDAAL MARLTPPRAA ASKDLLEK
//
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