ID A0A1E3I737_9TREE Unreviewed; 387 AA.
AC A0A1E3I737;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=L202_00177 {ECO:0000313|EMBL:ODN84175.1};
OS Cryptococcus amylolentus CBS 6039.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus.
OX NCBI_TaxID=1295533 {ECO:0000313|EMBL:ODN84175.1, ECO:0000313|Proteomes:UP000094065};
RN [1] {ECO:0000313|EMBL:ODN84175.1, ECO:0000313|Proteomes:UP000094065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 6039 {ECO:0000313|EMBL:ODN84175.1,
RC ECO:0000313|Proteomes:UP000094065};
RA Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT "Evolution of pathogenesis and genome organization in the Tremellales.";
RL Submitted (JUN-2016) 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};
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:ODN84175.1}.
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DR EMBL; AWGJ01000001; ODN84175.1; -; Genomic_DNA.
DR RefSeq; XP_018997978.1; XM_019133273.1.
DR AlphaFoldDB; A0A1E3I737; -.
DR STRING; 1295533.A0A1E3I737; -.
DR GeneID; 30151486; -.
DR OrthoDB; 2908056at2759; -.
DR Proteomes; UP000094065; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000094065};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 89..340
FT /note="SAM-dependent MTase TRM10-type"
FT /evidence="ECO:0000259|PROSITE:PS51675"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 73..104
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 36..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..387
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 387 AA; 42768 MW; 02C523AD1E6BFC71 CRC64;
MDIDEEAAMN AGPSTTPTTA GDKSAAGLSK KAQKRAAKQA KMEALKPLKR AAEKERRRIR
NAELHEGYAA GTLSEADKAI VERRRQIERE RKEAKKRLDK GEQGDDWKGG VVVDLGFDEL
MADQEIASTA QQLGYLYSAN RTAQHPFRTV IHTTFSPTAS PRLWARMGSS NWDKWTRCHW
WNEGLDVLQG QLQGSVAQEG QTQGKSLGAG GEAEGNTMLE KTMLSRLTGP NLPPDLIPGK
HTLVYLSADA EEEITTLSED EVYIIGGIVD RNRYKNLCQD KAEKIGIRTA RLPIGSYIAN
LPTRKVLTVN QVFDILVQYL KFKDWAVAFE AVIPTRKYAA TGGRKKRRRA RLSKHAGEEG
GDTEGGEDDE EGSETDEEPD GEPADES
//
