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Database: UniProt
Entry: E6KV21_9PAST
LinkDB: E6KV21_9PAST
Original site: E6KV21_9PAST 
ID   E6KV21_9PAST            Unreviewed;       235 AA.
AC   E6KV21;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 60.
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   Name=smtA {ECO:0000313|EMBL:EFU68586.1};
GN   ORFNames=HMPREF9064_0003 {ECO:0000313|EMBL:EFU68586.1};
OS   Aggregatibacter segnis ATCC 33393.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Aggregatibacter.
OX   NCBI_TaxID=888057 {ECO:0000313|EMBL:EFU68586.1, ECO:0000313|Proteomes:UP000032871};
RN   [1] {ECO:0000313|EMBL:EFU68586.1, ECO:0000313|Proteomes:UP000032871}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33393 {ECO:0000313|EMBL:EFU68586.1,
RC   ECO:0000313|Proteomes:UP000032871};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
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}.
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:EFU68586.1}.
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DR   EMBL; AEPS01000001; EFU68586.1; -; Genomic_DNA.
DR   RefSeq; WP_005715539.1; NZ_LS483443.1.
DR   AlphaFoldDB; E6KV21; -.
DR   STRING; 739.GCA_001059425_00792; -.
DR   GeneID; 60799399; -.
DR   HOGENOM; CLU_061983_0_0_6; -.
DR   OrthoDB; 5383291at2; -.
DR   Proteomes; UP000032871; 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   Reference proteome {ECO:0000313|Proteomes:UP000032871};
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          36..161
FT                   /note="Methyltransferase small"
FT                   /evidence="ECO:0000259|Pfam:PF05175"
SQ   SEQUENCE   235 AA;  26331 MW;  7F37AE0DD45104BF CRC64;
     MSKTGFRFKQ FQVNHERCAM KVGTDGILLG AWADVTQANQ ILDLGSGSGL IALMLAQRSS
     AESRICAVEI DHAAAQQACE NVLISPWKNK IQVYQQDIDS FCTQTAERFD LIVANPPYFQ
     TGVDCRNEER NTARYFAAQS HLHWLETAAA CLAPKGKISF VLPFDAGETL LKSTALYCVV
     RCDVITKQGK APQRMLLTFA TQPQTLLYDE LIIYDTQNQY HADFVALTQD FYLNF
//
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