ID A0A194UX93_9PEZI Unreviewed; 444 AA.
AC A0A194UX93;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
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 ORFNames=VP1G_03742 {ECO:0000313|EMBL:KUI56315.1};
OS Valsa mali var. pyri (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=694573 {ECO:0000313|EMBL:KUI56315.1, ECO:0000313|Proteomes:UP000078576};
RN [1] {ECO:0000313|Proteomes:UP000078576}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SXYL134 {ECO:0000313|Proteomes:UP000078576};
RA Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific Adaption of
RT Colonization on Woody Bark.";
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
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; KN714688; KUI56315.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A194UX93; -.
DR STRING; 694573.A0A194UX93; -.
DR OrthoDB; 2908056at2759; -.
DR Proteomes; UP000078576; Unassembled WGS sequence.
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; 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 PROSITE; PS51675; SAM_MT_TRM10; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:KUI56315.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000078576};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KUI56315.1}.
FT DOMAIN 144..398
FT /note="SAM-dependent MTase TRM10-type"
FT /evidence="ECO:0000259|PROSITE:PS51675"
FT REGION 1..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..426
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 444 AA; 49572 MW; 6F83EB0B6300E8CD CRC64;
METGPTPPAI EAAPPSAELP MDDAPTQVEE NPRKRQRGQD DGDQEPVLDN DAAEPSTEDN
AAAPAVDGAE DQPKLSKNQL RKLKRQKVWE ERRQDRKIQR KEKRHEKTAQ NRLRREEKAA
ALAQAEGIDK AEAIKRVVAQ EKKDQKRNKK TYVVPVSFII DCDFEKYMHE NEIVSLGAQI
TRSYSMNRQG DYQAHILVSS WGGKLKERYE TVLKNAHKNW KGVSFVDGDF VEAGKVAWNI
MHGPRGGKPC PTLGGDVQDE QQQSDDVAAA DVEQQAQDDA PESGQETALS DKPVPEFTTD
SVIYLSADSP HTLEKLEPNT SYVIGGLVDR NREKLLCQRR AEGKNIRTAK LPIGDYMQMA
SRQVLATNHV VEIMSKWLET GDWGKAFMEV IPKRKGGRLK GEDGDEDHDE DHDEAADADA
DDQNIELGNE DGEKQGDFTA NPEA
//
