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tRNA (guanine(37)-N1)-methyltransferase (EC 2.1.1.228) (M1G-methyltransferase) (tRNA [GM37] methyltransferase) (tRNA methyltransferase 5 homolog)

 A0A1X1BQ67_9APIC        Unreviewed;       528 AA.
A0A1X1BQ67;
05-JUL-2017, integrated into UniProtKB/TrEMBL.
05-JUL-2017, sequence version 1.
20-DEC-2017, entry version 5.
RecName: Full=tRNA (guanine(37)-N1)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_03152};
EC=2.1.1.228 {ECO:0000256|HAMAP-Rule:MF_03152};
AltName: Full=M1G-methyltransferase {ECO:0000256|HAMAP-Rule:MF_03152};
AltName: Full=tRNA [GM37] methyltransferase {ECO:0000256|HAMAP-Rule:MF_03152};
AltName: Full=tRNA methyltransferase 5 homolog {ECO:0000256|HAMAP-Rule:MF_03152};
ORFNames=BXIN_1099 {ECO:0000313|EMBL:ORM42272.1};
Babesia sp. Xinjiang.
Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
Babesiidae; Babesia.
NCBI_TaxID=462227 {ECO:0000313|EMBL:ORM42272.1, ECO:0000313|Proteomes:UP000193856};
[1] {ECO:0000313|EMBL:ORM42272.1, ECO:0000313|Proteomes:UP000193856}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Xinjiang {ECO:0000313|EMBL:ORM42272.1,
ECO:0000313|Proteomes:UP000193856};
PubMed=27784333; DOI=.1186/s13071-016-1846-1;
Guan G., Korhonen P.K., Young N.D., Koehler A.V., Wang T., Li Y.,
Liu Z., Luo J., Yin H., Gasser R.B.;
"Genomic resources for a unique, low-virulence Babesia taxon from
China.";
Parasit. Vectors 9:564-564(2016).
-!- FUNCTION: Specifically methylates the N1 position of guanosine-37
in various cytoplasmic and mitochondrial tRNAs. Methylation is not
dependent on the nature of the nucleoside 5' of the target
nucleoside. This is the first step in the biosynthesis of
wybutosine (yW), a modified base adjacent to the anticodon of
tRNAs and required for accurate decoding. {ECO:0000256|HAMAP-
Rule:MF_03152}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + guanine(37) in tRNA
= S-adenosyl-L-homocysteine + N(1)-methylguanine(37) in tRNA.
{ECO:0000256|HAMAP-Rule:MF_03152, ECO:0000256|SAAS:SAAS00629542}.
-!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_03152,
ECO:0000256|SAAS:SAAS00629546}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03152,
ECO:0000256|SAAS:SAAS00629555}. Mitochondrion matrix
{ECO:0000256|HAMAP-Rule:MF_03152}. Nucleus {ECO:0000256|HAMAP-
Rule:MF_03152, ECO:0000256|SAAS:SAAS00629556}. Note=Predominantly
in the mitochondria and in the nucleus. {ECO:0000256|HAMAP-
Rule:MF_03152}.
-!- SIMILARITY: Belongs to the TRM5 / TYW2 family. {ECO:0000256|HAMAP-
Rule:MF_03152}.
-!- SIMILARITY: Belongs to the class I-like SAM-binding
methyltransferase superfamily. TRM5/TYW2 family.
{ECO:0000256|SAAS:SAAS00629553}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:ORM42272.1}.
-----------------------------------------------------------------------
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EMBL; MBFZ01000006; ORM42272.1; -; Genomic_DNA.
Proteomes; UP000193856; Unassembled WGS sequence.
GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005840; C:ribosome; IEA:InterPro.
GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
GO; GO:0052906; F:tRNA (guanine(37)-N(1))-methyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0006412; P:translation; IEA:InterPro.
Gene3D; 1.10.60.20; -; 1.
HAMAP; MF_00511; Ribosomal_S17e; 1.
HAMAP; MF_03152; TRM5; 1.
InterPro; IPR030382; MeTrfase_TRM5/TYW2.
InterPro; IPR001210; Ribosomal_S17e.
InterPro; IPR018273; Ribosomal_S17e_CS.
InterPro; IPR036401; RPS17e-like_sf.
InterPro; IPR029063; SAM-dependent_MTases.
InterPro; IPR025792; tRNA_Gua_MeTrfase_euk.
Pfam; PF02475; Met_10; 1.
Pfam; PF00833; Ribosomal_S17e; 1.
SUPFAM; SSF116820; SSF116820; 1.
SUPFAM; SSF53335; SSF53335; 1.
PROSITE; PS00712; RIBOSOMAL_S17E; 1.
PROSITE; PS51684; SAM_MT_TRM5_TYW2; 1.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000193856};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03152,
ECO:0000256|SAAS:SAAS00629558};
Methyltransferase {ECO:0000256|HAMAP-Rule:MF_03152,
ECO:0000256|SAAS:SAAS00629543, ECO:0000313|EMBL:ORM42272.1};
Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03152,
ECO:0000256|SAAS:SAAS00629547};
Nucleus {ECO:0000256|HAMAP-Rule:MF_03152,
ECO:0000256|SAAS:SAAS00629549};
Reference proteome {ECO:0000313|Proteomes:UP000193856};
S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_03152,
ECO:0000256|SAAS:SAAS00415313};
Transferase {ECO:0000256|HAMAP-Rule:MF_03152,
ECO:0000256|SAAS:SAAS00629543, ECO:0000313|EMBL:ORM42272.1};
tRNA processing {ECO:0000256|HAMAP-Rule:MF_03152,
ECO:0000256|SAAS:SAAS00629554}.
DOMAIN 142 414 SAM_MT_TRM5_TYW2.
{ECO:0000259|PROSITE:PS51684}.
REGION 269 270 S-adenosyl-L-methionine binding.
{ECO:0000256|HAMAP-Rule:MF_03152}.
REGION 297 298 S-adenosyl-L-methionine binding.
{ECO:0000256|HAMAP-Rule:MF_03152}.
BINDING 231 231 S-adenosyl-L-methionine.
{ECO:0000256|HAMAP-Rule:MF_03152}.
BINDING 334 334 S-adenosyl-L-methionine.
{ECO:0000256|HAMAP-Rule:MF_03152}.
SEQUENCE 528 AA; 60506 MW; 6D723142B968AB92 CRC64;
MGDRRVKRRL EGSTAWSPAV SALPEIKSPE DLENYAIKED CVFVALRPED QKTFAEKGFF
RKLVRNYKKS LNTACLKDVE LPDDARRFVV SGWETLNSDL QALIQTKAIA FRNFTHIRRY
EDLSLDECLR LLGDSHGVMV SFETVGHIAH LNLPSERLWA KHIIAKILLD KHKHIRTVVN
KVKEVDNEFR TMELELLGGS DDFVAVQHEN GYTFKIDFRK VYWNSRLIRE RERISETFNM
GDVVVDMFAG VGPFAVYAAG KGCLVFANDL NPVGTRYIEI NANLNKIANM VFPYNLDARD
FVKNFANYGI MDKAATAFRD HVLKPENKVH FVMNLPKDAI EFLDVLVGLA KGVSSANVRT
CMVHCYCFSD AEDVEADIDE RMAKVLKEHI GEKKIINGRV RTKTVKRAAR QIVEKYYAKL
GLDFHFNKKV AEEVAQIPSK RMRNKVAGFI THLMRRIQKG PVRGISLKLQ EEERERRMDF
VPERSEVDVP LIQVDQDTAD MLSFLKLNIP NVKVITANMH GDAMHQRF


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