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Database: UniProt
Entry: F4WIR9_ACREC
LinkDB: F4WIR9_ACREC
Original site: F4WIR9_ACREC 
ID   F4WIR9_ACREC            Unreviewed;       250 AA.
AC   F4WIR9;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   RecName: Full=tRNA (guanine-N(7)-)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_03055};
DE            EC=2.1.1.33 {ECO:0000256|HAMAP-Rule:MF_03055};
DE   AltName: Full=tRNA (guanine(46)-N(7))-methyltransferase {ECO:0000256|HAMAP-Rule:MF_03055};
DE   AltName: Full=tRNA(m7G46)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_03055};
GN   ORFNames=G5I_05594 {ECO:0000313|EMBL:EGI65865.1};
OS   Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS   echinatior).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Acromyrmex.
OX   NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN   [1] {ECO:0000313|EMBL:EGI65865.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Nygaard S., Zhang G.;
RT   "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT   adaptations to social evolution and fungus farming.";
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the formation of N(7)-methylguanine at position 46
CC       (m7G46) in tRNA. {ECO:0000256|HAMAP-Rule:MF_03055}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-
CC         methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:42708, Rhea:RHEA-COMP:10188, Rhea:RHEA-COMP:10189,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269,
CC         ChEBI:CHEBI:74480; EC=2.1.1.33; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_03055};
CC   -!- PATHWAY: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_03055}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|HAMAP-Rule:MF_03055}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. TrmB family. {ECO:0000256|HAMAP-Rule:MF_03055}.
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DR   EMBL; GL888177; EGI65865.1; -; Genomic_DNA.
DR   RefSeq; XP_011053646.1; XM_011055344.1.
DR   RefSeq; XP_011053647.1; XM_011055345.1.
DR   RefSeq; XP_011053648.1; XM_011055346.1.
DR   RefSeq; XP_011053649.1; XM_011055347.1.
DR   AlphaFoldDB; F4WIR9; -.
DR   STRING; 103372.F4WIR9; -.
DR   EnsemblMetazoa; XM_011055344.1; XP_011053646.1; LOC105145645.
DR   EnsemblMetazoa; XM_011055345.1; XP_011053647.1; LOC105145645.
DR   EnsemblMetazoa; XM_011055346.1; XP_011053648.1; LOC105145645.
DR   EnsemblMetazoa; XM_011055347.1; XP_011053649.1; LOC105145645.
DR   GeneID; 105145645; -.
DR   KEGG; aec:105145645; -.
DR   eggNOG; KOG3115; Eukaryota.
DR   InParanoid; F4WIR9; -.
DR   OrthoDB; 116813at2759; -.
DR   UniPathway; UPA00989; -.
DR   Proteomes; UP000007755; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008176; F:tRNA (guanine(46)-N7)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   HAMAP; MF_03055; tRNA_methyltr_TrmB_euk; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR025763; Trm8_euk.
DR   InterPro; IPR003358; tRNA_(Gua-N-7)_MeTrfase_Trmb.
DR   NCBIfam; TIGR00091; tRNA (guanosine(46)-N7)-methyltransferase TrmB; 1.
DR   PANTHER; PTHR23417; 3-DEOXY-D-MANNO-OCTULOSONIC-ACID TRANSFERASE/TRNA GUANINE-N 7 - -METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR23417:SF16; TRNA (GUANINE-N(7)-)-METHYLTRANSFERASE; 1.
DR   Pfam; PF02390; Methyltransf_4; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51625; SAM_MT_TRMB; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW   Rule:MF_03055};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|HAMAP-Rule:MF_03055};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007755};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_03055};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW   Rule:MF_03055};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_03055};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_03055};
KW   tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP-
KW   Rule:MF_03055}.
FT   ACT_SITE        145
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
FT   BINDING         66
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
FT   BINDING         89..90
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
FT   BINDING         122..123
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
FT   BINDING         142
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
FT   BINDING         220..222
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
SQ   SEQUENCE   250 AA;  29186 MW;  02ADE7DF07DA42E0 CRC64;
     MTTTLALPQK KYYRQRAHSN PIADHCIEYP IKPELMDWST LYPQYFQSND EQTLERQKHV
     EFADVGCGYG GLLVTLSPMF PDNLILGMEI RVKVSDYVMD RIAALRSQNP GQYQNIACLR
     TNAMKYLPNY FYKGQLKKMF FLYPDPHFKK SKHKWRIINK SLLAEYAYVL AEGAIVYTVT
     DVEDLHKWIL QHFQEHPLFE EVTKQDLAAD PVVEKLYEST EEGKKVTRNE GDKFLAVFRR
     IADPYIATNS
//
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