位置:首页 > 蛋白库 > TRM10_CRYNJ
TRM10_CRYNJ
ID   TRM10_CRYNJ             Reviewed;         429 AA.
AC   P0CS10; Q55WD7; Q5KJW1;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=tRNA (guanine(9)-N1)-methyltransferase {ECO:0000250|UniProtKB:Q12400};
DE            EC=2.1.1.221 {ECO:0000250|UniProtKB:Q12400};
DE   AltName: Full=tRNA methyltransferase 10 {ECO:0000250|UniProtKB:Q12400};
DE   AltName: Full=tRNA(m1G9)-methyltransferase {ECO:0000250|UniProtKB:Q12400};
DE            Short=tRNA(m1G9)MTase {ECO:0000250|UniProtKB:Q12400};
GN   Name=TRM10 {ECO:0000250|UniProtKB:Q12400}; OrderedLocusNames=CNC05170;
OS   Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS   MYA-565) (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=214684;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEC21 / ATCC MYA-565;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
CC   -!- FUNCTION: S-adenosyl-L-methionine-dependent guanine N(1)-
CC       methyltransferase that catalyzes the formation of N(1)-methylguanine at
CC       position 9 (m1G9) in cytoplasmic tRNA. {ECO:0000250|UniProtKB:Q12400}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-
CC         methylguanosine(9) in tRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:43156, Rhea:RHEA-COMP:10367, Rhea:RHEA-COMP:10368,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:73542, ChEBI:CHEBI:74269; EC=2.1.1.221;
CC         Evidence={ECO:0000250|UniProtKB:Q12400};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:O14214}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q12400}. Nucleus
CC       {ECO:0000250|UniProtKB:Q12400}.
CC   -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC       superfamily. TRM10 family. {ECO:0000255|PROSITE-ProRule:PRU01012}.
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; AE017343; AAW42557.1; -; Genomic_DNA.
DR   RefSeq; XP_569864.1; XM_569864.1.
DR   AlphaFoldDB; P0CS10; -.
DR   SMR; P0CS10; -.
DR   STRING; 5207.AAW42557; -.
DR   PaxDb; P0CS10; -.
DR   EnsemblFungi; AAW42557; AAW42557; CNC05170.
DR   GeneID; 3256197; -.
DR   KEGG; cne:CNC05170; -.
DR   eggNOG; KOG2967; Eukaryota.
DR   HOGENOM; CLU_034384_1_1_1; -.
DR   InParanoid; P0CS10; -.
DR   OMA; TAWTETR; -.
DR   OrthoDB; 1396299at2759; -.
DR   Proteomes; UP000002149; Chromosome 3.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0052905; F:tRNA (guanine(9)-N(1))-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009019; F:tRNA (guanine-N1-)-methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR   GO; GO:0002939; P:tRNA N1-guanine methylation; IBA:GO_Central.
DR   Gene3D; 3.40.1280.30; -; 1.
DR   InterPro; IPR028564; MT_TRM10-typ.
DR   InterPro; IPR038459; MT_TRM10-typ_sf.
DR   InterPro; IPR016653; TRM10/TRM10A.
DR   InterPro; IPR007356; tRNA_m1G_MeTrfase_euk.
DR   InterPro; IPR016009; tRNA_MeTrfase_TRMD/TRM10.
DR   PANTHER; PTHR13563; PTHR13563; 1.
DR   PANTHER; PTHR13563:SF13; PTHR13563:SF13; 1.
DR   Pfam; PF01746; tRNA_m1G_MT; 1.
DR   PROSITE; PS51675; SAM_MT_TRM10; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; Nucleus; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase; tRNA processing.
FT   CHAIN           1..429
FT                   /note="tRNA (guanine(9)-N1)-methyltransferase"
FT                   /id="PRO_0000060513"
FT   DOMAIN          131..379
FT                   /note="SAM-dependent MTase TRM10-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01012"
FT   REGION          47..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          382..429
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        383..399
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        400..422
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        309
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:O14214"
FT   BINDING         285..286
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q12400"
FT   BINDING         305
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q12400"
FT   BINDING         309..313
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q12400"
FT   BINDING         317
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q12400"
FT   BINDING         331
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q12400"
FT   BINDING         344..346
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q12400"
SQ   SEQUENCE   429 AA;  48581 MW;  ABCE7096151DB626 CRC64;
     MKFHLGLTEA LQEREPNINA SSKDLSPLHF ELYRRSEPIM DIDEESYLNA GPSAPSKIPQ
     GGEGDRLQGM SKKAMKRAAK QARLEEIKPL KRAAERERRR QRTAQLAEGY AAGTLSEADK
     ELVERRRRVE KERKEAQRRI ESGDQANDWL GGVVIDLGFD DLMTDQEIAS MAQQLGYLYS
     SNRTAEKPVR TVIHTTFSPA ASPRLWQRME NFNWHKWSRC HWWEQGLETL KSQLDPSTSI
     LSVQSVVSKE TQDKAGIDTK SLLSRLTGPQ VPVDLQAGKH KLVYLSADAE DELLSLSEDE
     IYIIGGIVDR NRHKNLCQGK AEQLGIRTAR LPIGTFLEML PTRKVLTVNQ VFDILVKYLH
     LGDWAAAFEA VIPIRKYAPG RKTKRAKTET KRNEKEEEEV ECTSAEGEED IGVIEESAEV
     DPEDVFSNQ
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024