ID A4MY53_HAEIF Unreviewed; 232 AA.
AC A4MY53;
DT 15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 15-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=tRNA1(Val) (adenine(37)-N6)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01872};
DE EC=2.1.1.223 {ECO:0000256|HAMAP-Rule:MF_01872};
DE AltName: Full=tRNA m6A37 methyltransferase {ECO:0000256|HAMAP-Rule:MF_01872};
GN ORFNames=CGSHi22121_07225 {ECO:0000313|EMBL:EDJ88945.1};
OS Haemophilus influenzae 22.1-21.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=374927 {ECO:0000313|EMBL:EDJ88945.1, ECO:0000313|Proteomes:UP000004131};
RN [1] {ECO:0000313|EMBL:EDJ88945.1, ECO:0000313|Proteomes:UP000004131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22.1-21 {ECO:0000313|EMBL:EDJ88945.1,
RC ECO:0000313|Proteomes:UP000004131};
RX PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103;
RA Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C.,
RA Ehrlich G.D.;
RT "Characterization and modeling of the Haemophilus influenzae core and
RT supragenomes based on the complete genomic sequences of Rd and 12 clinical
RT nontypeable strains.";
RL Genome Biol. 8:R103.1-R103.18(2007).
CC -!- FUNCTION: Specifically methylates the adenine in position 37 of
CC tRNA(1)(Val) (anticodon cmo5UAC). {ECO:0000256|HAMAP-Rule:MF_01872}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(37) in tRNA1(Val) + S-adenosyl-L-methionine = H(+) +
CC N(6)-methyladenosine(37) in tRNA1(Val) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43160, Rhea:RHEA-COMP:10369, Rhea:RHEA-COMP:10370,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74449; EC=2.1.1.223;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01872};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01872}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. tRNA
CC (adenine-N(6)-)-methyltransferase family. {ECO:0000256|HAMAP-
CC Rule:MF_01872}.
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DR EMBL; AAZD01000002; EDJ88945.1; -; Genomic_DNA.
DR AlphaFoldDB; A4MY53; -.
DR Proteomes; UP000004131; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0016430; F:tRNA (adenine-N6)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-UniRule.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_01872; tRNA_methyltr_YfiC; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR007848; Small_mtfrase_dom.
DR InterPro; IPR022882; tRNA_adenine-N6_MeTrfase.
DR PANTHER; PTHR47739; TRNA1(VAL) (ADENINE(37)-N6)-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR47739:SF1; TRNA1(VAL) (ADENINE(37)-N6)-METHYLTRANSFERASE; 1.
DR Pfam; PF05175; MTS; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01872};
KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01872};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_01872};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01872}; tRNA processing {ECO:0000256|HAMAP-Rule:MF_01872}.
FT DOMAIN 34..121
FT /note="Methyltransferase small"
FT /evidence="ECO:0000259|Pfam:PF05175"
SQ SEQUENCE 232 AA; 26510 MW; F4EC9F431C5A40CE CRC64;
MNGFTFKQFH INQNSCAMKV STDGILLGAW ADVKHCKNIL DMGSGTGLLA LMLAQRTEEN
CQIQAVELDP IAAKQAQENI NNSVWKNHIQ LIQTDIQHFL QTTEQTFDLI VANPPYFEQG
IACKNEEREL ARYTKQSHLN WLEWAATRLS ENGRISFVLP YEAGKTLIKS TALFCIKQTN
VITKIGKTPQ RMLLTFAKQP QVLMQDQLVI YDADNQYTEA FIELTKDFYL KF
//
