ID A0A366S9C4_9HYPO Unreviewed; 1501 AA.
AC A0A366S9C4;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=FIESC28_01206 {ECO:0000313|EMBL:RBR25933.1};
OS Fusarium coffeatum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium incarnatum-equiseti species complex.
OX NCBI_TaxID=231269 {ECO:0000313|EMBL:RBR25933.1, ECO:0000313|Proteomes:UP000253153};
RN [1] {ECO:0000313|EMBL:RBR25933.1, ECO:0000313|Proteomes:UP000253153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FIESC_28 {ECO:0000313|EMBL:RBR25933.1,
RC ECO:0000313|Proteomes:UP000253153};
RA Gardiner D.M.;
RT "Fusarium incarnatum-equiseti species complex species 28.";
RL Submitted (JUN-2018) 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:RBR25933.1}.
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DR EMBL; QKXC01000031; RBR25933.1; -; Genomic_DNA.
DR OrthoDB; 5392990at2759; -.
DR UniPathway; UPA00989; -.
DR Proteomes; UP000253153; 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; 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 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 282..299
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 305..328
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 372..561
FT /note="PXA"
FT /evidence="ECO:0000259|PROSITE:PS51207"
FT DOMAIN 690..828
FT /note="RGS"
FT /evidence="ECO:0000259|PROSITE:PS50132"
FT DOMAIN 1150..1268
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 853..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 983..1021
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1041..1069
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1107..1141
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 7..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..897
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 983..1006
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1055..1069
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 170
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
FT BINDING 90
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
FT BINDING 113..114
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
FT BINDING 147..148
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
FT BINDING 167
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
FT BINDING 245..247
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
SQ SEQUENCE 1501 AA; 168878 MW; 4B67A40477FB4CA0 CRC64;
MTAELPNKQR GREKDRAKRT KDGVTQLPRK KFYRQRAHAN PFSDHMLEYP KSPDDMDWSS
YFPHYVQEGT PEDSSKPPRL TKDVEIVDIG CGFGGLTVAL APKMPDTLTL GLEIRTQVAG
YVQERIKALR SQSSDNMYQN VACIRANTMK FLPNFFKKAQ LSKIFICFPD PHFKARKHKA
RIVSTTLNSE YAYALRPGGI VYTITDVEDL HLWMVQHLEA HPAFERISKE EEEADECVQV
MSTETEESKK HHRLHHLHLS IFVQECGFEV NILVMALKRR DAIVAGLAAF IAWGFAASWS
PILRWAGHAF VAGSFVTLIL LLAGLFLVSR HPNDRTLPPN GVTFLNLKSW RSEVQALRQR
QLYTPTQIQP ESPRVAKAID DLLGLIIRDF VSSWYSNISR NPAFTNQVDK AVRDALLSLC
DILRDKDLAD LLTSRLVPLL TAHFRDFYEA EKSVRGKKLN RSVTESEELD LAIASKFRDG
RLHPAASLSF PDTKMVQQDY LRSLVAKIVP QILPENMLSS RAVSIIIREI VSCAVLFPVV
QLLAEPDTWN QLMENMGRSM LQDRSTVRKL RAALDQHAPS TPKNNKLASM PRVAPGDSER
KFEKFIRAIR KVNNLSDARR FRSEVASQLK RDSLEDSQDQ VYLRRLEMGK RLLDQRVTHL
AAGGERRPPG PLPLPSTTST TSQSKLESAP LVDILRDPSA LSYFMEYMDR QNVMPLVQFW
LVVDGFRNPL EDDGPDDELP STLPMWTDSD RQDLQQINQA YLSRPELKVP DHSKNEVKEF
IKAGKSATPM QYFRARRAIL KAQSAVLEEM RARFFQGFKK SDLFYKCLAA EEAASIQTLR
STPQPEVQAV AANRASKTLP AKPRPVSRLT TQLSNTSKRT GSASDLRSLT SNGNGRGHRA
RRSLDEGSTN PLFEDDDIDT DGLGDSVQSL DPEANSQQLP DTQVVQAVEE AFTNIMEDDR
PQTAEDLRAS LFGGAGGSSI GGLDDNTSSL FSGQDNDSNR GSLDMGVRPS TFSKEGEKPS
LSSLGLVSAA SRIGVFVDDD LFGDNNKDLP DEGDPDEGPP PDDEDEVHEA APGDLGLAEA
ITALSNDIDR LVAQEAVVES LTRKAELTNN TAELRILRKS KASLQREIRR KELQRQQYVI
QESDNSLYGR STIKIKSIQV GREEDGREFA LYVVEVQRDA GEQMPAASWV ISRRYSEFHE
LHQKLRSRYP SVRNLDFPRR RMVMKFQSEF LRKRRTALEQ YLQDLLLLPE VCRSRELRAF
LSQSVITQGQ DILDREDKKD MMTRLYDSVA DGMDDILGNI PVLDQISEAG QNLIAAATNQ
LNTVPLNANE DNFPAAEAEA ELNAFENKEL EPFIKPICDI FLEIFELNKG NNWLRGRAVV
VVLQQLLGGT IERKVRDNVK MFAQDENILK CISLVQDSLW PGGQMQRDKK PRTAAEKKKT
RTEASLMLAT LVPDLAGSVV GRVNAQAASR RIFATLNNSR LNAHLVFTMI DEIISVLFEE
P
//
