(data stored in ACNUC7421 zone)

SWISSPROT: A2Q7B7_ASPNC

ID   A2Q7B7_ASPNC            Unreviewed;       552 AA.
AC   A2Q7B7;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   11-DEC-2019, entry version 67.
DE   RecName: Full=tRNA (guanine(26)-N(2))-dimethyltransferase {ECO:0000256|PROSITE-ProRule:PRU00958};
DE            EC=2.1.1.216 {ECO:0000256|PROSITE-ProRule:PRU00958};
GN   ORFNames=An01g00070 {ECO:0000313|EMBL:CAK36858.1};
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=425011 {ECO:0000313|Proteomes:UP000006706};
RN   [1] {ECO:0000313|EMBL:CAK36858.1, ECO:0000313|Proteomes:UP000006706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 {ECO:0000313|Proteomes:UP000006706};
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA   Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA   van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA   Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA   Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA   Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA   Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA   van Ooyen A.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(26) in tRNA + 2 S-adenosyl-L-methionine = 2 H(+) +
CC         N(2)-dimethylguanosine(26) in tRNA + 2 S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:43140, Rhea:RHEA-COMP:10359, Rhea:RHEA-COMP:10360,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74269, ChEBI:CHEBI:74513; EC=2.1.1.216;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU00958};
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Trm1 family. {ECO:0000256|PROSITE-ProRule:PRU00958}.
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DR   EMBL; AM269949; CAK36858.1; -; Genomic_DNA.
DR   PaxDb; A2Q7B7; -.
DR   EnsemblFungi; CAK36858; CAK36858; An01g00070.
DR   HOGENOM; HOG000177995; -.
DR   Proteomes; UP000006706; Chromosome 2R.
DR   GO; GO:0004809; F:tRNA (guanine-N2-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.56.70; -; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   InterPro; IPR002905; Trm1.
DR   InterPro; IPR042296; tRNA_met_Trm1_C.
DR   PANTHER; PTHR10631; PTHR10631; 1.
DR   Pfam; PF02005; TRM; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00308; TRM1; 1.
DR   PROSITE; PS51626; SAM_MT_TRM1; 1.
PE   3: Inferred from homology;
DR   PRODOM; A2Q7B7.
DR   SWISS-2DPAGE; A2Q7B7.
KW   Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU00958,
KW   ECO:0000313|EMBL:CAK36858.1};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00958};
KW   S-adenosyl-L-methionine {ECO:0000256|PROSITE-ProRule:PRU00958};
KW   Transferase {ECO:0000256|PROSITE-ProRule:PRU00958,
KW   ECO:0000313|EMBL:CAK36858.1};
KW   tRNA processing {ECO:0000256|PROSITE-ProRule:PRU00958};
KW   tRNA-binding {ECO:0000256|PROSITE-ProRule:PRU00958}.
FT   REGION          78..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        82..106
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        107..127
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   552 AA;  60943 MW;  4AC799EB1ADFBE69 CRC64;
     MAEQLIQYDG TEYRAVKEGL AYILNPPAQA PGTKRDRKAD EQSQSVFYNP IQQFNRDLSV
     LAIRAYGEHL LALKKQKAEK KKQKAAANDS AKGKKRKREE VDGKEQTQDQ NQGQGDQTAA
     QQAEQDTAPS FTILDALSAT GLRALRYASE IPFTSCVVAN DLSPSAIESM KTNIKYNSLG
     EKIRPNTGDA RSYIHLGKFD VIDLDPYGSA APFMDAAVQG VKDGGLLCVT CTDAGVWASY
     GYPEKSFALY GGIPVKGPHC HEGGLRLILH GLAASAAKYG LAIEPLLSLS IDFYARVFVR
     VHRSPAEVKY ISGNMMMVYN CDAGCGAWST QPITQTKQKL DKKGNPFYHF GFAQGPVADS
     RCGHCGSRTH LSGPMWAGPL HNAQFIRRIL DMLPQADRNV YHTIDRIEGM LTTAMEEDLN
     LGISKYPFYF SLSALSKVLH TSTISIDAMR GAIRHLGYRS TRSHARPNTI RTDAPWEVIW
     EIMREWVRQK SPIREGALKP GSPGAVIIPH PSTLEVVFDE ALGRETAKKR LVRYQINPRE
     NWGPLSRASG GK
//

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