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TRM61_ASHGO
ID   TRM61_ASHGO             Reviewed;         406 AA.
AC   Q755M8;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=tRNA (adenine(58)-N(1))-methyltransferase catalytic subunit TRM61;
DE            EC=2.1.1.220;
DE   AltName: Full=tRNA(m1A58)-methyltransferase subunit TRM61;
DE            Short=tRNA(m1A58)MTase subunit TRM61;
GN   Name=TRM61; OrderedLocusNames=AFL214C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Catalytic subunit of tRNA (adenine-N(1)-)-methyltransferase,
CC       which catalyzes the formation of N(1)-methyladenine at position 58
CC       (m1A58) in initiator methionyl-tRNA. {ECO:0000250|UniProtKB:P46959}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine(58) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-
CC         methyladenosine(58) in tRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:43152, Rhea:RHEA-COMP:10365, Rhea:RHEA-COMP:10366,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74411, ChEBI:CHEBI:74491; EC=2.1.1.220;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00952};
CC   -!- SUBUNIT: Heterotetramer; composed of two copies of TRM6 and two copies
CC       of TRM61. {ECO:0000250|UniProtKB:P46959}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P46959}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. TRM61 family. {ECO:0000255|PROSITE-ProRule:PRU00952}.
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DR   EMBL; AE016819; AAS53160.1; -; Genomic_DNA.
DR   RefSeq; NP_985336.1; NM_210690.1.
DR   AlphaFoldDB; Q755M8; -.
DR   SMR; Q755M8; -.
DR   STRING; 33169.AAS53160; -.
DR   EnsemblFungi; AAS53160; AAS53160; AGOS_AFL214C.
DR   GeneID; 4621560; -.
DR   KEGG; ago:AGOS_AFL214C; -.
DR   eggNOG; KOG2915; Eukaryota.
DR   HOGENOM; CLU_025402_4_0_1; -.
DR   InParanoid; Q755M8; -.
DR   OMA; VVYPKDA; -.
DR   Proteomes; UP000000591; Chromosome VI.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0031515; C:tRNA (m1A) methyltransferase complex; IBA:GO_Central.
DR   GO; GO:0016429; F:tRNA (adenine-N1-)-methyltransferase activity; IEA:EnsemblFungi.
DR   GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR014816; tRNA_MeTrfase_Gcd14.
DR   PANTHER; PTHR12133; PTHR12133; 1.
DR   Pfam; PF08704; GCD14; 1.
DR   PIRSF; PIRSF017269; GCD14; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51620; SAM_TRM61; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; Nucleus; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase; tRNA processing.
FT   CHAIN           1..406
FT                   /note="tRNA (adenine(58)-N(1))-methyltransferase catalytic
FT                   subunit TRM61"
FT                   /id="PRO_0000256167"
FT   REGION          281..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          385..406
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        290..310
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         119..121
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT   BINDING         137
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q96FX7,
FT                   ECO:0000255|PROSITE-ProRule:PRU00952"
FT   BINDING         142
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT   BINDING         167..168
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT   BINDING         202
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q96FX7,
FT                   ECO:0000255|PROSITE-ProRule:PRU00952"
SQ   SEQUENCE   406 AA;  46214 MW;  D20B41703BD32459 CRC64;
     MSYFTEYKDL IAEGDLVLVW ISRGNVKQLR IKSGEVFNTR YGSFAHDDIV GRPYGSQIGV
     RTKGSNRFGF IHVLQPTPEL WTLSLPHRTQ IVYTPDSSYI MQRLGCSPQS RVIEAGTGSG
     SFSHAFARTV GQLFSYEFHH MRYEQALAEF QEHGLIADGN VTITHRDVCQ KGFLIKAGDT
     TSYEFLEGQD SVSVNADCIF LDLPAPWEAI PHLDAVIAKD RTARLCCFSP CIEQVDKTLE
     ALELHGWEEI ETVEIQGRQY ESRRQMVRQL DDALERLRDV KRRKQHGTER RKRLGEQLGS
     VEELTDDVRP KTPKTSYNPF GKGSRVKEGD NGFEWKQVAK VESEIKSHTS YLTFASKILF
     KSRDENTVSQ LLEQYKDFNP NVKAASKLDK RPQETSFEES QASNSV
 
 
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