ID A0A177D0G3_9PLEO Unreviewed; 484 AA.
AC A0A177D0G3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=tRNA guanosine-2'-O-methyltransferase {ECO:0000313|EMBL:OAG12620.1};
GN ORFNames=CC84DRAFT_1183224 {ECO:0000313|EMBL:OAG12620.1};
OS Paraphaeosphaeria sporulosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC Paraphaeosphaeria.
OX NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG12620.1, ECO:0000313|Proteomes:UP000077069};
RN [1] {ECO:0000313|EMBL:OAG12620.1, ECO:0000313|Proteomes:UP000077069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG12620.1,
RC ECO:0000313|Proteomes:UP000077069};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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; KV441548; OAG12620.1; -; Genomic_DNA.
DR RefSeq; XP_018042985.1; XM_018180675.1.
DR AlphaFoldDB; A0A177D0G3; -.
DR STRING; 1460663.A0A177D0G3; -.
DR GeneID; 28764161; -.
DR InParanoid; A0A177D0G3; -.
DR OrthoDB; 5488599at2759; -.
DR Proteomes; UP000077069; 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 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:OAG12620.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077069};
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:OAG12620.1};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT DOMAIN 177..227
FT /note="UPF0020"
FT /evidence="ECO:0000259|Pfam:PF01170"
FT REGION 456..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..475
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 484 AA; 54319 MW; 590EDBAB305D75EB CRC64;
MPNYLVRLVQ MHESFRQAEL QALADVAEVS IEFVKYEEES PFCIVRLPSD AAAKTVISRS
LLSQGIYELW GQGATYDALH ESVKDISSAK WVQYESAPFR FTLDCFRGTR DNAQQRDIIE
SFSYMGFKGP IRMRDAEASF KVFEEYEEKA TGPKYAYLGR FVAASGRDAK TTYDLKKRHY
ISTTSMDAEL ALVTANMALA APGKLFYDPF MGTGGFPIAC AHFGAMVCGS DIDGRSIRGT
GGSARKGQTG KFDVQGNFKQ YGLESRYLGA FVSDLTNTPF RLLQHSNSAS RGGYLDGIVC
DPPYGIREGL KVLGSRDILN EQERATHGNR YKDPGYIPPK KPYSFTAIQD DILAFAVSTL
VENGRLSMWM PTANDEDVEL IIPTHPCLEI VSVCVQTFNK WSRRLLTYRR RAESEVPEGA
LETVKKEYEK GVKADELNNF RKKYFEGFKE FERLRQEPSA EDANHKADRS KGVSGPWREK
SGAN
//
