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DIM1_MACFA
ID   DIM1_MACFA              Reviewed;         313 AA.
AC   Q95KJ0;
DT   13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Probable dimethyladenosine transferase;
DE            EC=2.1.1.183 {ECO:0000250|UniProtKB:Q9UNQ2};
DE   AltName: Full=DIM1 dimethyladenosine transferase 1 homolog;
DE   AltName: Full=DIM1 dimethyladenosine transferase 1-like;
DE   AltName: Full=Probable 18S rRNA (adenine(1779)-N(6)/adenine(1780)-N(6))-dimethyltransferase;
DE   AltName: Full=Probable 18S rRNA dimethylase;
DE   AltName: Full=Probable S-adenosylmethionine-6-N',N'-adenosyl(rRNA) dimethyltransferase;
GN   Name=DIMT1; Synonyms=DIMT1L; ORFNames=QtrA-10945;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Temporal cortex;
RA   Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K.,
RA   Suzuki Y., Sugano S., Hashimoto K.;
RT   "Isolation of full-length cDNA clones from macaque brain cDNA libraries.";
RL   Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
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       Involved in the pre-rRNA processing steps leading to small-subunit rRNA
CC       production independently of its RNA-modifying catalytic activity.
CC       {ECO:0000250|UniProtKB:Q9UNQ2}.
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         Evidence={ECO:0000250|UniProtKB:Q9UNQ2};
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC       {ECO:0000250|UniProtKB:Q9UNQ2}. Nucleus, nucleolus
CC       {ECO:0000250|UniProtKB:Q9UNQ2}.
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}.
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DR   EMBL; AB060843; BAB46866.1; -; mRNA.
DR   RefSeq; NP_001270420.1; NM_001283491.1.
DR   AlphaFoldDB; Q95KJ0; -.
DR   SMR; Q95KJ0; -.
DR   STRING; 9541.XP_005557033.1; -.
DR   GeneID; 102115642; -.
DR   CTD; 27292; -.
DR   eggNOG; KOG0820; Eukaryota.
DR   OrthoDB; 963506at2759; -.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
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:0000179; F:rRNA (adenine-N6,N6-)-dimethyltransferase activity; ISS:UniProtKB.
DR   GO; GO:2000234; P:positive regulation of rRNA processing; ISS:UniProtKB.
DR   GO; GO:0031167; P:rRNA methylation; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Methyltransferase; Nucleus; Reference proteome; RNA-binding;
KW   rRNA processing; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..313
FT                   /note="Probable dimethyladenosine transferase"
FT                   /id="PRO_0000101466"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         37
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         39
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         64
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         85
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         113
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         128
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
SQ   SEQUENCE   313 AA;  35221 MW;  CB08294AB0847F08 CRC64;
     MPKVKSGAIG RRRGRQEQRR ELKSAGGLMF NTGIGQHILK NPLIINSIID KAALRPTDVV
     LEVGPGTGNM TVKLLEKAKK VVACELDPRL VAELRKRVQG TPVASKLQVL VGDVLKTDLP
     FFDTCVANLP YQISSPFVFK LLLHRPFFRC AILMFQRELA LRLVAKPGDK LYCRLSINTQ
     LLARVDHLMK VGKNNFRPPP KVESSVVRIE PKNPPPPINF QEWDGLVRIT FVRKNKTLSA
     AFKSSAVQQL LEKNYRIHCS VHNIIIPEDF SIADKIQQIL TSTGFSDKRA RSMDIDDFIR
     LLHGFNAEGI HFS
 
 
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