ID A0A010S564_9PEZI Unreviewed; 1522 AA.
AC A0A010S564;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 44.
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=CFIO01_10915 {ECO:0000313|EMBL:EXF79743.1};
OS Colletotrichum fioriniae PJ7.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF79743.1, ECO:0000313|Proteomes:UP000020467};
RN [1] {ECO:0000313|EMBL:EXF79743.1, ECO:0000313|Proteomes:UP000020467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PJ7 {ECO:0000313|EMBL:EXF79743.1,
RC ECO:0000313|Proteomes:UP000020467};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum fioriniae PJ7.";
RL Submitted (FEB-2014) 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}.
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:EXF79743.1}.
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DR EMBL; JARH01000509; EXF79743.1; -; Genomic_DNA.
DR RefSeq; XP_007596621.1; XM_007596559.1.
DR STRING; 1445577.A0A010S564; -.
DR KEGG; cfj:CFIO01_10915; -.
DR eggNOG; KOG2101; Eukaryota.
DR eggNOG; KOG3115; Eukaryota.
DR HOGENOM; CLU_002131_1_1_1; -.
DR OrthoDB; 5392990at2759; -.
DR UniPathway; UPA00989; -.
DR Proteomes; UP000020467; 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 Coiled coil {ECO:0000256|SAM:Coils}; 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:UP000020467};
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 316..334
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 340..361
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 410..599
FT /note="PXA"
FT /evidence="ECO:0000259|PROSITE:PS51207"
FT DOMAIN 728..867
FT /note="RGS"
FT /evidence="ECO:0000259|PROSITE:PS50132"
FT DOMAIN 1190..1308
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 12..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 874..968
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1026..1055
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1085..1105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1147..1181
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 929..946
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1089..1104
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 130
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
FT BINDING 49
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
FT BINDING 72..73
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
FT BINDING 107..108
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
FT BINDING 127
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
FT BINDING 205..207
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
SQ SEQUENCE 1522 AA; 170581 MW; 7B99DD425D84718F CRC64;
MNWTQYYPAF AANEETPSTN PTTTESMTLD ASKPKTRSLT KDVEVVDIGC GFGGLTVALS
PILPETLILG LEIRTSVTEY VQERIKALRV QNQETSGYQN ISCLRANSMK FLPNFFKKAQ
LSKIFICFPD PHFKARKHKA RIVSTTLNSE YAFALRPGGI VYTITDVEPL HQWMVGHFNA
HPAFERVSEE EQEADECVKV MASETEESKK VTRNQGQKHI ALFRRLEDPP CFPVKGKRIS
SIRRYLKWQG PTETHLMHPT LRRACNGKSV AKAASTLRFP NPAASENTAI FDDVRCSDSL
SPLTTDLDMA LQGRELILAA ITCFIAWGYA VSWVPVLRWV GYALVGGVIL TVVAFLALVL
VTSRGFGRGL RHRSPRPNGP AFLAPKAWAR QVSSLQTRQA YTKVALNPNS KRISKALDDL
LELIIRDFVS SWYSNISKNP VFSNEVDKVV RDALINIRER LLELDLVDIV TTRIVPMLNA
HFRDFYEAER AVRGKKLNRS VTESEELDLA IASKYKDGKL HPAASLSFPD TKLVQQDYLR
KMVSGILPKV LPPNILASRA VSSIIREIVA CAVLFPVMQI LAEPDTWNQV MENYGRSMLQ
DRSTVRKLRA ALDQHASPAP RSGKAAIIPR LSPTDSERKF EKFIRAIRKV GNLSDARRLR
SEVASQLKRD SLEENQDQVY LRRLEMGKRL LDERVQLLAA GGSRQSSATL PARPSGAPQA
PSKLEHASLV DLLRDASGLS YFMEFMDRHH MMPLVQFWLV VDGFRNPLED EGQDDEHLPS
NLPMWTSSDR EDLGQIDHAY LSKPELKVSK ASRDEVRAFL NAGKTATPEQ YYRARRAILR
AQTAVLDAMQ AQFFQAFKKS DLFYKCLASQ EASAKSAPLP VAEPSASTAA PPAHPPTHRS
SHSFQFKPSP VTRIAPRLTR PLSRRAGSAS DLASLTLNGN GSESLSKQRR SFEEDVSTPL
FDDDDFDQEG MMDSVASLDQ DTGKPPVPDT NVVQAMEEAL NNIMEDNRPQ TAEEFRESLF
GADDQVDRSS LFSGDNESLR GSLEMPRPAA SSKEIDKPSL ASLGLVSAAS RIGVFVDDDL
FGDEEKYLSD ERDDPEEETK GDVEDEIQEA APGDLGLAEA ITALSNDIDR LIAQDAIVES
LTKKADLTNN TAELRILRKS KASLQREIRR KELQRQQYVV QESDNSLYGR STIKIKAIQV
GKEDDGREFA LYVIEVQRDA GEKMPAATWM VTRRYSEFHD LHQRLRSRYP SVRNLEFPRR
RMVMKFQSEF LRKRRTALEK YLRDLLQLPE ACRSRDLRAF LSQSVIAQGQ DLVDREDKKD
MITRFYDSVT DGMEDILGNI PVLDQLSVAG QNLIAAATNQ LNAMPLPVNE DGVSAAEAEA
ELNAFENKEL ESFIKPICDI FLEVFELNRG NNWLRGRAVV VVLQQLLGGT IERKVRDNVK
MLVQEDAIIK YIALLKDSMW PGGEMNKNKQ PRTASEKKKT RTEASLMLAT LIPDLAGSVV
GRVNAQAASR RVFATLNNSR LK
//