ID A0A2T4AGP2_TRIHA Unreviewed; 1464 AA.
AC A0A2T4AGP2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=tRNA (guanine-N(7)-)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_03055};
DE EC=2.1.1.33 {ECO:0000256|HAMAP-Rule:MF_03055};
DE AltName: Full=Transfer RNA methyltransferase 8 {ECO:0000256|HAMAP-Rule:MF_03055};
DE AltName: Full=tRNA (guanine(46)-N(7))-methyltransferase {ECO:0000256|HAMAP-Rule:MF_03055};
DE AltName: Full=tRNA(m7G46)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_03055};
GN Name=TRM8 {ECO:0000256|HAMAP-Rule:MF_03055};
GN ORFNames=M431DRAFT_82085 {ECO:0000313|EMBL:PTB56260.1};
OS Trichoderma harzianum CBS 226.95.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=983964 {ECO:0000313|EMBL:PTB56260.1, ECO:0000313|Proteomes:UP000241690};
RN [1] {ECO:0000313|EMBL:PTB56260.1, ECO:0000313|Proteomes:UP000241690}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 226.95 {ECO:0000313|EMBL:PTB56260.1,
RC ECO:0000313|Proteomes:UP000241690};
RG DOE Joint Genome Institute;
RA Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT "Multiple horizontal gene transfer events from other fungi enriched the
RT ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT plant biomass.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the formation of N(7)-methylguanine at position 46
CC (m7G46) in tRNA. {ECO:0000256|HAMAP-Rule:MF_03055}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-
CC methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42708, Rhea:RHEA-COMP:10188, Rhea:RHEA-COMP:10189,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269,
CC ChEBI:CHEBI:74480; EC=2.1.1.33; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_03055};
CC -!- PATHWAY: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_03055}.
CC -!- SUBUNIT: Forms a complex with TRM82. {ECO:0000256|HAMAP-Rule:MF_03055}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|HAMAP-Rule:MF_03055}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. TrmB family. {ECO:0000256|HAMAP-Rule:MF_03055}.
CC -!- SIMILARITY: Belongs to the sorting nexin family.
CC {ECO:0000256|ARBA:ARBA00010883}.
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DR EMBL; KZ679678; PTB56260.1; -; Genomic_DNA.
DR STRING; 983964.A0A2T4AGP2; -.
DR OrthoDB; 5392990at2759; -.
DR UniPathway; UPA00989; -.
DR Proteomes; UP000241690; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0008176; F:tRNA (guanine(46)-N7)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd06876; PX_MDM1p; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_03055; tRNA_methyltr_TrmB_euk; 1.
DR InterPro; IPR003114; Phox_assoc.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR044926; RGS_subdomain_2.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR013937; Sorting_nexin_C.
DR InterPro; IPR025763; Trm8_euk.
DR InterPro; IPR003358; tRNA_(Gua-N-7)_MeTrfase_Trmb.
DR NCBIfam; TIGR00091; tRNA (guanosine(46)-N7)-methyltransferase TrmB; 1.
DR PANTHER; PTHR22775; SORTING NEXIN; 1.
DR PANTHER; PTHR22775:SF3; SORTING NEXIN-13; 1.
DR Pfam; PF02390; Methyltransf_4; 1.
DR Pfam; PF08628; Nexin_C; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF02194; PXA; 1.
DR Pfam; PF00615; RGS; 1.
DR SMART; SM00312; PX; 1.
DR SMART; SM00313; PXA; 1.
DR SMART; SM00315; RGS; 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS50195; PX; 1.
DR PROSITE; PS51207; PXA; 1.
DR PROSITE; PS50132; RGS; 1.
DR PROSITE; PS51625; SAM_MT_TRMB; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_03055};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|HAMAP-Rule:MF_03055};
KW Reference proteome {ECO:0000313|Proteomes:UP000241690};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_03055}; S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_03055};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03055};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_03055};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP-
KW Rule:MF_03055}.
FT TRANSMEM 274..292
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 298..319
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 365..554
FT /note="PXA"
FT /evidence="ECO:0000259|PROSITE:PS51207"
FT DOMAIN 680..818
FT /note="RGS"
FT /evidence="ECO:0000259|PROSITE:PS50132"
FT DOMAIN 1132..1250
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 870..890
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 169
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
FT BINDING 89
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
FT BINDING 112..113
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
FT BINDING 146..147
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
FT BINDING 166
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
FT BINDING 244..246
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
SQ SEQUENCE 1464 AA; 166230 MW; 2A14A018BD736111 CRC64;
MGNQTNKKER RDRFRERRGQ DGVVLLPRKK LYRQRAHANP FSDHMLEYPI SPEYMDWSSY
YPSYVDEEAP RDESKPPRMK QDVEIVDIGC GFGGLLVGLA PIFPDKLILG LEIRTTVTQF
VQEKIWALRA QSSEKLYQNA ACIRANTMKF LPNFFKKSQL SKIFICFPDP HFKTKKHKAR
IVSTTLNSEY AYALRPGGIV YTITDVEALH EWMVEHLDAH PSFERVSKEE EENDECVKIM
LNETEEGKKV ERNKGHKFVA LFRPATMALK RRDVALAGVA YFIAWGYAVS WFSALRWVGY
AFVGGIVISF LSLIAALVLT TQHPRGDRPA RPARVSFLSS QRWRAEAEAL RQRQTYHKEP
FDPSFPQASE ALDEVLDLIF RDFVRSWYSH ISQNPTFEHE VDKAIRQALF SLVGSLRNKD
LADLVTSRFV PILTAHFHDF YEAEKSVRGR KLNRSVTESE ELDLAIASKF RDGRLHPAAS
LSFPDTKMVQ QDYLRSLVER LLSKILPKKM LSSRAVSIIV REIVGCAVLF PVVQLLSDPD
MWNQLIENLG RSMLQDRSTV RKLRAALDQH ASPTPRSNKL AMAPRLAPGD NERKFEKFIR
AIRRVNNLSD ARRFRSEVAS QLKRDSLQEN QDPVYLRRLE MGKRLLDERV HNLAAGGNRH
SPMPASSAPP VSTSKLENAS LVELLRDPAG LSYFMEYMDR QRLMPMVQFW LVVDGFRNPL
EEDGQDDELP STLPMWTDSD RLDLLQIHQA YLSKPELNVP EVAKKAVKEF LQAGVSATPA
EYYKARRAIL RAQSGVLETM RSQYFEGFKK SDLYYKCLAS QEMSRATMSP PPPTHQAPSV
SSRTQSYQSK PKPAPRFAPL AAGPSRRLSG SISDLRSVNS NGNGSDPLTS SRRSLDDDRS
ANPLFDDDDV DNYGMMDSVQ SLDQALSRQQ TPDKQVVQAV EQALTNILED DRPQTAEDLR
ASLFDNEDNV SSLFGNDNES NRGSFDAGKP LIPAKEAGKP TLSSLGLVSA ASRIGVFVDD
DLFGDEDKYL PGERDDIDEE AQSDEEDEIH EAAPGDLGLA EAITALTNDI DRLVAQDAVI
ESLTKKAELT NNAAELRILK KSRTSLQREI RRKELQRQQY VIQESDNSLY GRSEIRIKSI
QVGREDDGRE FALYVIEVQR NAGEQMPASS WAVMRRYSEF HELHQKLRSM YPSVRNLDFP
RRRVVMKFQS DFLRKRRTAL EKYLRELLLL PEVCRSRELR AFLSQSTIAQ GEDPMSRENK
KDMMTRLYDS VADGMEDILG NIPVLDQISV AGQNLIAAAT NQLNTMPLNV SEETFPAAEA
EAELDAFENK ELEPFIKPIC DIFLEVFELN KGNNWLRGRA VVVVLQQLLG GTIEKRVREN
IKMAVQEDSL VRYVAMLRNA LWPDGEFARD RKPRTTAEKK KTRTEASLML ATLVPDLAGN
VVGRVNAQAA SRRLFATFNN SRLK
//
