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Database: UniProt
Entry: I2GY76_TETBL
LinkDB: I2GY76_TETBL
Original site: I2GY76_TETBL 
ID   I2GY76_TETBL            Unreviewed;       306 AA.
AC   I2GY76;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=tRNA (guanine(9)-N1)-methyltransferase {ECO:0000256|ARBA:ARBA00020451};
DE            EC=2.1.1.221 {ECO:0000256|ARBA:ARBA00012797};
DE   AltName: Full=tRNA methyltransferase 10 {ECO:0000256|ARBA:ARBA00032166};
DE   AltName: Full=tRNA(m1G9)-methyltransferase {ECO:0000256|ARBA:ARBA00031792};
GN   Name=TBLA0B02360 {ECO:0000313|EMBL:CCH59078.1};
GN   ORFNames=TBLA_0B02360 {ECO:0000313|EMBL:CCH59078.1};
OS   Tetrapisispora blattae (strain ATCC 34711 / CBS 6284 / DSM 70876 / NBRC
OS   10599 / NRRL Y-10934 / UCD 77-7) (Yeast) (Kluyveromyces blattae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX   NCBI_TaxID=1071380 {ECO:0000313|EMBL:CCH59078.1, ECO:0000313|Proteomes:UP000002866};
RN   [1] {ECO:0000313|EMBL:CCH59078.1, ECO:0000313|Proteomes:UP000002866}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 34711 / CBS 6284 / DSM 70876 / NBRC 10599 / NRRL Y-10934 /
RC   UCD 77-7 {ECO:0000313|Proteomes:UP000002866};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT   accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-
CC         methylguanosine(9) in tRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:43156, Rhea:RHEA-COMP:10367, Rhea:RHEA-COMP:10368,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:73542, ChEBI:CHEBI:74269; EC=2.1.1.221;
CC         Evidence={ECO:0000256|ARBA:ARBA00000855};
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DR   EMBL; HE806317; CCH59078.1; -; Genomic_DNA.
DR   RefSeq; XP_004178597.1; XM_004178549.1.
DR   AlphaFoldDB; I2GY76; -.
DR   STRING; 1071380.I2GY76; -.
DR   GeneID; 14494097; -.
DR   KEGG; tbl:TBLA_0B02360; -.
DR   eggNOG; KOG2967; Eukaryota.
DR   HOGENOM; CLU_034384_1_0_1; -.
DR   InParanoid; I2GY76; -.
DR   OMA; FKKNDGW; -.
DR   OrthoDB; 2908056at2759; -.
DR   Proteomes; UP000002866; Chromosome 2.
DR   GO; GO:0052905; F:tRNA (guanosine(9)-N1)-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd18089; SPOUT_Trm10-like; 1.
DR   Gene3D; 3.40.1280.30; -; 1.
DR   InterPro; IPR028564; MT_TRM10-typ.
DR   InterPro; IPR038459; MT_TRM10-typ_sf.
DR   InterPro; IPR016653; TRM10/TRM10A.
DR   InterPro; IPR007356; tRNA_m1G_MeTrfase_euk.
DR   InterPro; IPR016009; tRNA_MeTrfase_TRMD/TRM10.
DR   PANTHER; PTHR13563; TRNA (GUANINE-9-) METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR13563:SF13; TRNA METHYLTRANSFERASE 10 HOMOLOG A; 1.
DR   Pfam; PF01746; tRNA_m1G_MT; 1.
DR   PIRSF; PIRSF016323; tRNA_m1G_mtfrase_met; 1.
DR   PROSITE; PS51675; SAM_MT_TRM10; 1.
PE   4: Predicted;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002866};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          81..276
FT                   /note="SAM-dependent MTase TRM10-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51675"
FT   REGION          283..306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        290..306
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        207
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016323-1"
FT   BINDING         183
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016323-2"
FT   BINDING         203
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016323-2"
FT   BINDING         215
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016323-2"
FT   BINDING         229
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016323-2"
SQ   SEQUENCE   306 AA;  36045 MW;  7EC6ACFB23B37E2D CRC64;
     MMTEPIGKNT EIKRITLPPI PDGISKSQWK KICKRKRWEE TKAEYSKVRR DKRKAARAKR
     RAIIQGYLDR GEELPDEYKS TPKLNHNQSD SGIKIIMDCA FDELMNDKEI TSMTTQITRS
     YASNRRENHY ADIKITSFNK RVKARFDKEL KSSRYETWDH FEFLPDDSLI TGKDVDKSKM
     IYLTADTDDT LETLEPGMTY IVGGIVDKNR HKFLCYNKAK ELGIRTKRLP IDEYVKISSV
     KVLTTTHVIH LMLKYFDNKD WKEAFESILP TRKLEDWDTI DKEDDNVEKE QEVLEVEESD
     EEKEQE
//
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