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DIM1_KLULA
ID   DIM1_KLULA              Reviewed;         320 AA.
AC   P78697; Q6CSJ1;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2004, sequence version 3.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Dimethyladenosine transferase;
DE            EC=2.1.1.183;
DE   AltName: Full=18S rRNA (adenine(1779)-N(6)/adenine(1780)-N(6))-dimethyltransferase;
DE   AltName: Full=18S rRNA dimethylase;
DE   AltName: Full=S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase;
GN   Name=DIM1; OrderedLocusNames=KLLA0D00594g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9219342;
RX   DOI=10.1002/(sici)1097-0061(19970630)13:8<777::aid-yea140>3.0.co;2-1;
RA   Housen I., Demonte D., Lafontaine D., Vandenhaute J.;
RT   "Cloning and characterization of the KlDIM1 gene from Kluyveromyces lactis
RT   encoding the m2(6)A dimethylase of the 18S rRNA.";
RL   Yeast 13:777-781(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Specifically dimethylates two adjacent adenosines in the loop
CC       of a conserved hairpin near the 3'-end of 18S rRNA in the 40S particle.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine(1779)/adenosine(1780) in 18S rRNA + 4 S-adenosyl-L-
CC         methionine = 4 H(+) + N(6)-dimethyladenosine(1779)/N(6)-
CC         dimethyladenosine(1780) in 18S rRNA + 4 S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:42780, Rhea:RHEA-COMP:10234, Rhea:RHEA-COMP:10236,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74411, ChEBI:CHEBI:74493; EC=2.1.1.183;
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. rRNA adenine N(6)-methyltransferase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01026}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA92586.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; Z68294; CAA92586.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; CR382124; CAH00194.1; -; Genomic_DNA.
DR   PIR; T09625; T09625.
DR   RefSeq; XP_453098.1; XM_453098.1.
DR   AlphaFoldDB; P78697; -.
DR   SMR; P78697; -.
DR   STRING; 28985.XP_453098.1; -.
DR   EnsemblFungi; CAH00194; CAH00194; KLLA0_D00594g.
DR   GeneID; 2893296; -.
DR   KEGG; kla:KLLA0_D00594g; -.
DR   eggNOG; KOG0820; Eukaryota.
DR   HOGENOM; CLU_041220_2_0_1; -.
DR   InParanoid; P78697; -.
DR   OMA; VNAQMWA; -.
DR   BRENDA; 2.1.1.183; 2825.
DR   Proteomes; UP000000598; Chromosome D.
DR   GO; GO:0030688; C:preribosome, small subunit precursor; IEA:EnsemblFungi.
DR   GO; GO:0052909; F:18S rRNA (adenine(1779)-N(6)/adenine(1780)-N(6))-dimethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:EnsemblFungi.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR001737; KsgA/Erm.
DR   InterPro; IPR020596; rRNA_Ade_Mease_Trfase_CS.
DR   InterPro; IPR020598; rRNA_Ade_methylase_Trfase_N.
DR   InterPro; IPR011530; rRNA_adenine_dimethylase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR11727; PTHR11727; 1.
DR   Pfam; PF00398; RrnaAD; 1.
DR   SMART; SM00650; rADc; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00755; ksgA; 1.
DR   PROSITE; PS01131; RRNA_A_DIMETH; 1.
DR   PROSITE; PS51689; SAM_RNA_A_N6_MT; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; Reference proteome; RNA-binding; rRNA processing;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..320
FT                   /note="Dimethyladenosine transferase"
FT                   /id="PRO_0000101461"
FT   BINDING         38
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         40
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         65
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         86
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         114
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         129
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   CONFLICT        248
FT                   /note="V -> D (in Ref. 1; CAA92586)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   320 AA;  35763 MW;  FF5150C93E8D9AE5 CRC64;
     MGKAVKKKYS GASSGGKEVD AEKHLTTVFK FNTDLGQHIL KNPLVAQGIV DKAQIKPSDI
     VLEIGPGTGN LTVRILEQAR KVVAVEFDPR MAAELTKRVH GTPVEKKLEI LLGDFMKTEL
     PYFDVCISNT PYQISSPLVF KLINQPKPPR VSILMFQREF AMRLLARPGD SLYCRLSANV
     QMWANVTHIM KVGKNNFRPP PKVESSVVRI EIKNPRPQVD FNEWDGLLRI VFVRKNRTIA
     AGFKSTTVLE ILEKNYKAFL ATQSAVPTTS SGDSLINEVK EKIEQVLSET GLAEKRAGKC
     DQTDFLKLLY GFHQVGIHFA
 
 
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