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Database: UniProt
Entry: U6GSG8_9EIME
LinkDB: U6GSG8_9EIME
Original site: U6GSG8_9EIME 
ID   U6GSG8_9EIME            Unreviewed;       389 AA.
AC   U6GSG8;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=tRNA (guanine(37)-N1)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_03152};
DE            EC=2.1.1.228 {ECO:0000256|HAMAP-Rule:MF_03152};
DE   AltName: Full=M1G-methyltransferase {ECO:0000256|HAMAP-Rule:MF_03152};
DE   AltName: Full=tRNA [GM37] methyltransferase {ECO:0000256|HAMAP-Rule:MF_03152};
DE   AltName: Full=tRNA methyltransferase 5 homolog {ECO:0000256|HAMAP-Rule:MF_03152};
GN   ORFNames=EPH_0010490 {ECO:0000313|EMBL:CDI82228.1};
OS   Eimeria praecox.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX   NCBI_TaxID=51316 {ECO:0000313|EMBL:CDI82228.1};
RN   [1] {ECO:0000313|EMBL:CDI82228.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Houghton {ECO:0000313|EMBL:CDI82228.1};
RA   Reid A.J., Blake D., Billington K., Browne H., Dunn M., Hung S.,
RA   Kawahara F., Miranda-Saavedra D., Mourier T., Nagra H., Otto T.D.,
RA   Rawlings N., Sanchez A., Sanders M., Subramaniam C., Tay Y., Dear P.,
RA   Doerig C., Gruber A., Parkinson J., Shirley M., Wan K.L., Berriman M.,
RA   Tomley F., Pain A.;
RT   "Genomic analysis of the causative agents of coccidiosis in chickens.";
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDI82228.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Houghton {ECO:0000313|EMBL:CDI82228.1};
RA   Aslett M.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Specifically methylates the N1 position of guanosine-37 in
CC       various cytoplasmic and mitochondrial tRNAs. Methylation is not
CC       dependent on the nature of the nucleoside 5' of the target nucleoside.
CC       This is the first step in the biosynthesis of wybutosine (yW), a
CC       modified base adjacent to the anticodon of tRNAs and required for
CC       accurate decoding. {ECO:0000256|HAMAP-Rule:MF_03152}.
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|HAMAP-Rule:MF_03152};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_03152}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000256|HAMAP-
CC       Rule:MF_03152}. Nucleus {ECO:0000256|HAMAP-Rule:MF_03152}. Cytoplasm
CC       {ECO:0000256|HAMAP-Rule:MF_03152}. Note=Predominantly in the
CC       mitochondria and in the nucleus. {ECO:0000256|HAMAP-Rule:MF_03152}.
CC   -!- SIMILARITY: Belongs to the TRM5 / TYW2 family. {ECO:0000256|HAMAP-
CC       Rule:MF_03152}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. TRM5/TYW2 family. {ECO:0000256|ARBA:ARBA00009775}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_03152}.
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DR   EMBL; HG692247; CDI82228.1; -; Genomic_DNA.
DR   AlphaFoldDB; U6GSG8; -.
DR   EnsemblProtists; CDI82228; CDI82228; EPH_0010490.
DR   VEuPathDB; ToxoDB:EPH_0010490; -.
DR   OrthoDB; 276346at2759; -.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0052906; F:tRNA (guanine(37)-N1)-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030488; P:tRNA methylation; IEA:UniProtKB-UniRule.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.30.300.110; Met-10+ protein-like domains; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   HAMAP; MF_03152; TRM5; 1.
DR   InterPro; IPR030382; MeTrfase_TRM5/TYW2.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR025792; tRNA_Gua_MeTrfase_euk.
DR   PANTHER; PTHR23245:SF36; TRNA (GUANINE(37)-N1)-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR23245; TRNA METHYLTRANSFERASE; 1.
DR   Pfam; PF02475; Met_10; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51684; SAM_MT_TRM5_TYW2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03152};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW   Rule:MF_03152};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128, ECO:0000256|HAMAP-
KW   Rule:MF_03152};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|HAMAP-Rule:MF_03152};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW   Rule:MF_03152};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_03152};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_03152}.
FT   DOMAIN          59..368
FT                   /note="SAM-dependent methyltransferase TRM5/TYW2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51684"
FT   BINDING         147
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03152"
FT   BINDING         213..214
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03152"
FT   BINDING         265
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03152"
SQ   SEQUENCE   389 AA;  42898 MW;  26742CAD3A3FB8EC CRC64;
     MIVCCLAELE GLPDSLQSLL KEKGIQVLRH RVSLGYDNLS VVECLAQLLP EGVETPHRFE
     CVGHIAHLNL PAPLLKFKYA IGQVVLDKHP QLRTVVLKTG IGSKWRELQF ELIAGEPVYV
     AKVKESDLVF EVDYSKVFWN SRLSCERQRI TATIPRHAVV LDAFAGVGAF AVFLARGGCV
     VAANDGNPAS AANMQTNVKR NGVESLVEVH NQDARDFLRS QAKPAAIAAL LQKRMQAGGK
     QPKTEGAVAE RNGDQSTVEV HVLMNLPELA VEFLDVFPAI FNESEPQPKR HRPDEEVLSN
     NAATGEALQI SKWRIHCYAF CRDPQPEREL KPRVEAALGC WPEPVEIQEV RDVAPHKRMY
     CLAFDLPLAL LRGECSSSTE QAAAASAPH
//
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