GenomeNet

Database: UniProt
Entry: A0A0C4F9D9_PUCT1
LinkDB: A0A0C4F9D9_PUCT1
Original site: A0A0C4F9D9_PUCT1 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system