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Database: UniProt
Entry: A0A010S564_9PEZI
LinkDB: A0A010S564_9PEZI
Original site: A0A010S564_9PEZI 
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
//
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