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Database: UniProt
Entry: A0A1I2CMJ7_9FIRM
LinkDB: A0A1I2CMJ7_9FIRM
Original site: A0A1I2CMJ7_9FIRM 
ID   A0A1I2CMJ7_9FIRM        Unreviewed;       146 AA.
AC   A0A1I2CMJ7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   31-JAN-2018, entry version 3.
DE   RecName: Full=Mini-ribonuclease 3 {ECO:0000256|HAMAP-Rule:MF_01468};
DE            Short=Mini-3 {ECO:0000256|HAMAP-Rule:MF_01468};
DE            Short=Mini-RNase 3 {ECO:0000256|HAMAP-Rule:MF_01468};
DE            EC=3.1.26.- {ECO:0000256|HAMAP-Rule:MF_01468};
DE   AltName: Full=Mini-RNase III {ECO:0000256|HAMAP-Rule:MF_01468};
DE            Short=Mini-III {ECO:0000256|HAMAP-Rule:MF_01468};
GN   Name=mrnC {ECO:0000256|HAMAP-Rule:MF_01468};
GN   ORFNames=SAMN02910278_01484 {ECO:0000313|EMBL:SFE69454.1};
OS   Peptostreptococcus sp. D1.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales;
OC   Peptostreptococcaceae; Peptostreptococcus.
OX   NCBI_TaxID=72304 {ECO:0000313|EMBL:SFE69454.1, ECO:0000313|Proteomes:UP000199190};
RN   [1] {ECO:0000313|EMBL:SFE69454.1, ECO:0000313|Proteomes:UP000199190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D1 {ECO:0000313|EMBL:SFE69454.1,
RC   ECO:0000313|Proteomes:UP000199190};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in correct processing of both the 5' and 3'
CC       ends of 23S rRNA precursor. Processes 30S rRNA precursor
CC       transcript even in absence of ribonuclease 3 (Rnc); Rnc processes
CC       30S rRNA into smaller rRNA precursors. {ECO:0000256|HAMAP-
CC       Rule:MF_01468}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01468};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01468}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01468}.
CC   -!- SIMILARITY: Belongs to the MrnC RNase family. {ECO:0000256|HAMAP-
CC       Rule:MF_01468}.
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DR   EMBL; FONP01000008; SFE69454.1; -; Genomic_DNA.
DR   Proteomes; UP000199190; Unassembled WGS sequence.
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   PIRSF; PIRSF005520; UCP005520; 1.
DR   SMART; SM00535; RIBOc; 1.
DR   SUPFAM; SSF69065; SSF69065; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000199190};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01468};
KW   Endonuclease {ECO:0000256|HAMAP-Rule:MF_01468};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01468};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01468};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_01468};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199190};
KW   Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_01468};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01468};
KW   rRNA processing {ECO:0000256|HAMAP-Rule:MF_01468};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01468}.
FT   DOMAIN        6    145       RNase III. {ECO:0000259|SMART:SM00535}.
FT   ACT_SITE     35     35       {ECO:0000256|HAMAP-Rule:MF_01468}.
SQ   SEQUENCE   146 AA;  16730 MW;  4E9768D2CB2DA650 CRC64;
     MEKDVAMEKD GINLRELSKE ELLRISPLTL AYLGDTIYET YIREYLIKKS IYTKINELHR
     SAIMYVSAAA QSKAIKSMEG ILSEEETTIY KRGRNHKKST GAKNASIIDY RHATGFESLI
     GYLYLKGDTD RLEFIVLMAI QAIENR
//
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