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MRNC_DESHY
ID   MRNC_DESHY              Reviewed;         157 AA.
AC   Q250Q5;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Mini-ribonuclease 3 {ECO:0000255|HAMAP-Rule:MF_01468};
DE            Short=Mini-3 {ECO:0000255|HAMAP-Rule:MF_01468};
DE            Short=Mini-RNase 3 {ECO:0000255|HAMAP-Rule:MF_01468};
DE            EC=3.1.26.- {ECO:0000255|HAMAP-Rule:MF_01468};
DE   AltName: Full=Mini-RNase III {ECO:0000255|HAMAP-Rule:MF_01468};
DE            Short=Mini-III {ECO:0000255|HAMAP-Rule:MF_01468};
GN   Name=mrnC {ECO:0000255|HAMAP-Rule:MF_01468}; OrderedLocusNames=DSY0448;
OS   Desulfitobacterium hafniense (strain Y51).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfitobacterium.
OX   NCBI_TaxID=138119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y51;
RX   PubMed=16513756; DOI=10.1128/jb.188.6.2262-2274.2006;
RA   Nonaka H., Keresztes G., Shinoda Y., Ikenaga Y., Abe M., Naito K.,
RA   Inatomi K., Furukawa K., Inui M., Yukawa H.;
RT   "Complete genome sequence of the dehalorespiring bacterium
RT   Desulfitobacterium hafniense Y51 and comparison with Dehalococcoides
RT   ethenogenes 195.";
RL   J. Bacteriol. 188:2262-2274(2006).
CC   -!- FUNCTION: Involved in correct processing of both the 5' and 3' ends of
CC       23S rRNA precursor. Processes 30S rRNA precursor transcript even in
CC       absence of ribonuclease 3 (Rnc); Rnc processes 30S rRNA into smaller
CC       rRNA precursors. {ECO:0000255|HAMAP-Rule:MF_01468}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01468};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01468}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01468}.
CC   -!- SIMILARITY: Belongs to the MrnC RNase family. {ECO:0000255|HAMAP-
CC       Rule:MF_01468}.
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DR   EMBL; AP008230; BAE82237.1; -; Genomic_DNA.
DR   RefSeq; WP_011459085.1; NC_007907.1.
DR   AlphaFoldDB; Q250Q5; -.
DR   SMR; Q250Q5; -.
DR   STRING; 138119.DSY0448; -.
DR   EnsemblBacteria; BAE82237; BAE82237; DSY0448.
DR   KEGG; dsy:DSY0448; -.
DR   eggNOG; COG1939; Bacteria.
DR   HOGENOM; CLU_091169_2_1_9; -.
DR   OMA; AYMGDAI; -.
DR   OrthoDB; 1939897at2; -.
DR   Proteomes; UP000001946; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004525; F:ribonuclease III activity; IEA:InterPro.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.1520.10; -; 1.
DR   HAMAP; MF_01468; RNase_Mini_III; 1.
DR   InterPro; IPR008226; Mini3_fam.
DR   InterPro; IPR000999; RNase_III_dom.
DR   InterPro; IPR036389; RNase_III_sf.
DR   Pfam; PF00636; Ribonuclease_3; 1.
DR   SMART; SM00535; RIBOc; 1.
DR   SUPFAM; SSF69065; SSF69065; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Endonuclease; Hydrolase; Magnesium; Nuclease;
KW   Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing;
KW   rRNA-binding.
FT   CHAIN           1..157
FT                   /note="Mini-ribonuclease 3"
FT                   /id="PRO_0000415983"
FT   REGION          126..157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..145
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        18
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01468"
SQ   SEQUENCE   157 AA;  17902 MW;  C5F870C2833ADE9A CRC64;
     MPRSWQEMNA LTLAYLGDVV YELWVRTHLL NNGYEKVNEL HRLATQYVRA GTQAKLLHHI
     LPHLDEQELS VVHRGRNAKG GHPKSTDVVT YRYATGFEAL VGYWQLTGRT ERMLWAFEQV
     DQFVGEEDEG KGKGETAKEE ESITDALSPA EQSEIDC
 
 
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