ID A0A165A9T4_9AGAM Unreviewed; 475 AA.
AC A0A165A9T4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=tRNA guanosine-2'-O-methyltransferase {ECO:0000313|EMBL:KZS98675.1};
GN ORFNames=SISNIDRAFT_435911 {ECO:0000313|EMBL:KZS98675.1};
OS Sistotremastrum niveocremeum HHB9708.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Trechisporales; Trechisporales incertae sedis; Sistotremastrum.
OX NCBI_TaxID=1314777 {ECO:0000313|EMBL:KZS98675.1, ECO:0000313|Proteomes:UP000076722};
RN [1] {ECO:0000313|EMBL:KZS98675.1, ECO:0000313|Proteomes:UP000076722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB9708 {ECO:0000313|EMBL:KZS98675.1,
RC ECO:0000313|Proteomes:UP000076722};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- FUNCTION: Catalytic subunit of an S-adenosyl-L-methionine-dependent
CC tRNA methyltransferase complex that mediates the methylation of the
CC guanosine nucleotide at position 10 (m2G10) in tRNAs.
CC {ECO:0000256|ARBA:ARBA00002425}.
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DR EMBL; KV419395; KZS98675.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165A9T4; -.
DR STRING; 1314777.A0A165A9T4; -.
DR OrthoDB; 5488599at2759; -.
DR Proteomes; UP000076722; Unassembled WGS sequence.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0009451; P:RNA modification; IEA:UniProt.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR000241; RlmKL-like_Mtase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016691; tRNA_mtfrase_TRM11.
DR PANTHER; PTHR13370; RNA METHYLASE-RELATED; 1.
DR PANTHER; PTHR13370:SF3; TRNA (GUANINE(10)-N2)-METHYLTRANSFERASE HOMOLOG; 1.
DR Pfam; PF01170; UPF0020; 1.
DR PIRSF; PIRSF017259; tRNA_mtfrase_TRM11; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
DR PROSITE; PS51627; SAM_MT_TRM11; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:KZS98675.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076722};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022555};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KZS98675.1};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT DOMAIN 191..325
FT /note="UPF0020"
FT /evidence="ECO:0000259|Pfam:PF01170"
SQ SEQUENCE 475 AA; 53567 MW; 1FACCFF0D03054C8 CRC64;
MTLPCLIQFA QVHEQFRLPE LRSIAELNGI QLDIPEEVDV KRPFMIINLS SEDDAKILAA
RCILIKNVLE LWGHGESYEV LHGRNKENMP LWQRYATDTT FKFLVTAYNH SIHKARQKSI
METFDYMAWE GRIDLASPEV TLLCTEEYRD RGNSHTRAKH EGEGSFRQVY FGRLLAEGTA
RDLIQKFDVK QRAYYGNTSM ESEISLLMAN QALSAPGRLI YDPFVGTGST LYTCAQFGSY
VCGSDIDGRQ MRGKGGVWLL QLSERRLMGL DVTPGIMRSA AQYGVASLIL DLFTFDVTRH
PWRSGGIFDA IITDPPYGVR AGAKRLGKKD KAVINDKPPK PGNADAPAHL RPNYIPPTKP
YELSELAVDL VALSVHLLKP GGRLVFFLPT VNEAYQDVDI PLHPHMKLVS NSLQDFGNWG
RRLVTMEKLS GPATTDPAIA TTIHVPAHKD FREKYFSGFR HAMNLKDPNM MNERR
//
