ID F9FVA6_FUSOF Unreviewed; 709 AA.
AC F9FVA6;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=tRNA (guanine(26)-N(2))-dimethyltransferase {ECO:0000256|ARBA:ARBA00039099};
DE EC=2.1.1.216 {ECO:0000256|ARBA:ARBA00039099};
GN ORFNames=FOXB_10337 {ECO:0000313|EMBL:EGU79177.1};
OS Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU79177.1};
RN [1] {ECO:0000313|EMBL:EGU79177.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176 {ECO:0000313|EMBL:EGU79177.1};
RX PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT "A highly conserved effector in Fusarium oxysporum is required for full
RT virulence on Arabidopsis.";
RL Mol. Plant Microbe Interact. 25:180-190(2012).
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Trm1 family. {ECO:0000256|PROSITE-ProRule:PRU00958}.
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:EGU79177.1}.
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DR EMBL; AFQF01002710; EGU79177.1; -; Genomic_DNA.
DR AlphaFoldDB; F9FVA6; -.
DR STRING; 660025.F9FVA6; -.
DR PaxDb; 5507-FOXG_08363P0; -.
DR GO; GO:0160102; F:tRNA (guanine(10)-N2)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006400; P:tRNA modification; IEA:UniProt.
DR Gene3D; 3.30.56.70; N2,N2-dimethylguanosine tRNA methyltransferase, C-terminal domain; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR002905; Trm1.
DR InterPro; IPR042296; tRNA_met_Trm1_C.
DR NCBIfam; TIGR00308; TRM1; 1.
DR PANTHER; PTHR10631; N 2 ,N 2 -DIMETHYLGUANOSINE TRNA METHYLTRANSFERASE; 1.
DR PANTHER; PTHR10631:SF3; TRNA (GUANINE(26)-N(2))-DIMETHYLTRANSFERASE; 1.
DR Pfam; PF02005; TRM; 2.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51626; SAM_MT_TRM1; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU00958};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00958};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU00958};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00958}; tRNA processing {ECO:0000256|PROSITE-ProRule:PRU00958};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|PROSITE-
KW ProRule:PRU00958}.
FT REGION 138..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..649
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 709 AA; 78774 MW; A78594B571E0A223 CRC64;
MQILSKQHSY MFRVFWRSRS NFGAGAILDL TNRFSKTRTL STNRNYRALC DKPIAHRQFS
TTAKMAEEKV NVETVTVEGK EFRTVTEGKA TILVPQGAKI GEDRGEVQQV FYNPIQQYNR
DLSVLAIKTY GEMSLERRKE QYESRMNKQG KKRKRGDDEQ KPTEAVNPPP QDKPQATEEA
AKPNDAEAQQ PKKEIKPSFR ILDALSASGL RALRYAHELP FVTSVKANDL SDTAAESIRM
NAKHNGLEDK ITVTQGDALA LMYRGIADDL SNRDKGGNPG KANKFDVIDL DPYGTAAPFF
DAAVQSIRDD GGLLCITCTD SAVWAGHSYC EKTFALYGGI PIKGMHSHEA GLRLVLNAVA
TSAARYGLAI EPLLSLSIDF YTKFFIKVTK SPQSVKFLAS KTMLVYSCDS GCGAWETQPM
LRSKPAPNKK GSGAFYKHTM AQGPSADRHC EHCGMKMHIN GPMYGGHIHS QEFIERLLAQ
IPKADPSIYG TMPRLEGMLR TALEEYLPGP EVKEPVDPKD AQLATVDHYP FFIIPSRLAN
VVSCVTPSED MVRGALIHLG YRTARSHCRP GSIKTDAPWS TIWWIITEWI RQKSPIKESS
IKKNSAAWKI LTDAGIIGQE KPEAAEETAK DGSAMEGVEQ QTSEAPVEGT AGATNGDDKP
VPSEMELRKT LVFDENLARL ARRRGEQKLV RYQMNPRENW GPLAKASRR
//