ID A0A0C4F9D9_PUCT1 Unreviewed; 486 AA.
AC A0A0C4F9D9;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
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};
OS Puccinia triticina (isolate 1-1 / race 1 (BBBD)) (Brown leaf rust fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=630390 {ECO:0000313|EnsemblFungi:PTTG_09815P0, ECO:0000313|Proteomes:UP000005240};
RN [1] {ECO:0000313|Proteomes:UP000005240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate 1-1 / race 1 (BBBD)
RC {ECO:0000313|Proteomes:UP000005240};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Fellers J., Bakkeren G., Szabo L., Young S., Zeng Q.,
RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Walk T., White J., Yandava C., Haas B., Nusbaum C., Birren B.;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblFungi:PTTG_09815P0}
RP IDENTIFICATION.
RC STRAIN=isolate 1-1 / race 1 (BBBD)
RC {ECO:0000313|EnsemblFungi:PTTG_09815P0};
RG EnsemblFungi;
RL Submitted (JUN-2015) to UniProtKB.
RN [3] {ECO:0000313|Proteomes:UP000005240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate 1-1 / race 1 (BBBD)
RC {ECO:0000313|Proteomes:UP000005240};
RA Cuomo C.A., Bakkeren G., Szabo L., Khalil H., Joly D., Goldberg J.,
RA Young S., Zeng Q., Fellers J.;
RT "Comparative analysis highlights variable genome content of wheat rusts and
RT divergence of the mating loci.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EnsemblFungi:PTTG_09815P0}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=isolate 1-1 / race 1 (BBBD)
RC {ECO:0000313|EnsemblFungi:PTTG_09815P0};
RX PubMed=27913634; DOI=10.1534/g3.116.032797;
RA Cuomo C.A., Bakkeren G., Khalil H.B., Panwar V., Joly D., Linning R.,
RA Sakthikumar S., Song X., Adiconis X., Fan L., Goldberg J.M., Levin J.Z.,
RA Young S., Zeng Q., Anikster Y., Bruce M., Wang M., Yin C., McCallum B.,
RA Szabo L.J., Hulbert S., Chen X., Fellers J.P.;
RT "Comparative analysis highlights variable genome content of wheat rusts and
RT divergence of the mating loci.";
RL G3 (Bethesda) 7:361-376(2017).
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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03055}.
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DR EMBL; ADAS01011968; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A0C4F9D9; -.
DR STRING; 630390.A0A0C4F9D9; -.
DR EnsemblFungi; PTTG_09815T0; PTTG_09815P0; PTTG_09815.
DR UniPathway; UPA00989; -.
DR Proteomes; UP000005240; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_03055; tRNA_methyltr_TrmB_euk; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR025763; Trm8_euk.
DR InterPro; IPR003358; tRNA_(Gua-N-7)_MeTrfase_Trmb.
DR PANTHER; PTHR23417; 3-DEOXY-D-MANNO-OCTULOSONIC-ACID TRANSFERASE/TRNA GUANINE-N 7 - -METHYLTRANSFERASE; 1.
DR PANTHER; PTHR23417:SF16; TRNA (GUANINE-N(7)-)-METHYLTRANSFERASE; 1.
DR Pfam; PF02390; Methyltransf_4; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51625; SAM_MT_TRMB; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_03055};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|HAMAP-Rule:MF_03055};
KW Reference proteome {ECO:0000313|Proteomes:UP000005240};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_03055};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_03055};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03055};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_03055};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP-
KW Rule:MF_03055}.
FT REGION 102..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 347
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
FT BINDING 228..229
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
FT BINDING 324..325
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
FT BINDING 344
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
FT BINDING 427..429
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
SQ SEQUENCE 486 AA; 55601 MW; 780FA6240C1F63F5 CRC64;
MSLFSSGLNI SRRSNLAKTP TIIGVLMLTQ RDESFVADLV PRTWCRPGVK IMPCFPSARE
LQLDINSPIT TSKLFAISRL VCSSLLFARL RMGANHKKRN FSAVDTSNQP VKASKMDQSS
EPAKEKLPHI MPRRKWIGQN TILSSFGAKT QIQPTNKTRK RAQIVIRKSG RIRRCWVRLR
RIVDCHGTFV SRKIDASTLP LSLAIYLCQR ILKQTSLTDR HVWFSGLEIR PHVCQYVEDK
ILALRAQQKI IQQQNSSGVE GAEFVFELPS LPKQMPKFVK DIHQDQVASQ VPNEPAPDDE
LDDEAPIWVP KPGRFENVSV IRANAMKFSP NFFYKHQLSK MFFLFPDPHF KARKHKARII
SPTLLSEYGY ILKPNGIIYT ITDVKDLNVW MVKHLTEHPL FKPIEAEELI KADPLEDQLI
KSIYNLTEEG KKSPGIRAIS SWPSSEESLK KKNNPCYYPD SQIELFKASS TMAQNKEYTS
IVQWIE
//