ID Q2EUS3_SHIFL Unreviewed; 178 AA.
AC Q2EUS3;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Ribonuclease 3 {ECO:0000256|ARBA:ARBA00017706};
DE EC=3.1.26.3 {ECO:0000256|ARBA:ARBA00012177};
DE AltName: Full=Ribonuclease III {ECO:0000256|ARBA:ARBA00032486};
DE Flags: Fragment;
GN Name=rnc {ECO:0000313|EMBL:ABD19999.1};
OS Shigella flexneri.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623 {ECO:0000313|EMBL:ABD19999.1};
RN [1] {ECO:0000313|EMBL:ABD19999.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=577 {ECO:0000313|EMBL:ABD19999.1};
RX PubMed=17160643; DOI=10.1007/s00239-006-0052-8;
RA Yang J., Nie H., Chen L., Zhang X., Yang F., Xu X., Zhu Y., Yu J., Jin Q.;
RT "Revisiting the molecular evolutionary history of Shigella spp.";
RL J. Mol. Evol. 64:71-79(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.3;
CC Evidence={ECO:0000256|ARBA:ARBA00000109};
CC -!- SIMILARITY: Belongs to the ribonuclease III family.
CC {ECO:0000256|ARBA:ARBA00010183}.
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DR EMBL; DQ362296; ABD19999.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2EUS3; -.
DR GO; GO:0004525; F:ribonuclease III activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0006364; P:rRNA processing; IEA:InterPro.
DR CDD; cd10845; DSRM_RNAse_III_family; 1.
DR CDD; cd00593; RIBOc; 1.
DR Gene3D; 3.30.160.20; -; 1.
DR Gene3D; 1.10.1520.10; Ribonuclease III domain; 1.
DR InterPro; IPR014720; dsRBD_dom.
DR InterPro; IPR011907; RNase_III.
DR InterPro; IPR000999; RNase_III_dom.
DR InterPro; IPR036389; RNase_III_sf.
DR NCBIfam; TIGR02191; RNaseIII; 1.
DR PANTHER; PTHR11207:SF0; RIBONUCLEASE 3; 1.
DR PANTHER; PTHR11207; RIBONUCLEASE III; 1.
DR Pfam; PF00035; dsrm; 1.
DR Pfam; PF14622; Ribonucleas_3_3; 1.
DR SMART; SM00358; DSRM; 1.
DR SMART; SM00535; RIBOc; 1.
DR SUPFAM; SSF54768; dsRNA-binding domain-like; 1.
DR SUPFAM; SSF69065; RNase III domain-like; 1.
DR PROSITE; PS50137; DS_RBD; 1.
DR PROSITE; PS50142; RNASE_3_2; 1.
PE 3: Inferred from homology;
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00266}.
FT DOMAIN 1..80
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT DOMAIN 107..177
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABD19999.1"
SQ SEQUENCE 178 AA; 19922 MW; 6015C5496A9748AE CRC64;
SYVIANALYH RFPRADEGDM SRMRATLVRG NTLAELAREF ELGECLRLGP GELKSGGFRR
ESILADTVEA LIGGVFLDSD IQTVEKLILN WYQTRLDEIS PGDKQKDPKT RLQEYLQGRH
LPLPTYLVVQ VRGEAHDQEF TIHCQVSGLS EPVVGTGSSR RKAEQAAAEQ ALKKLELE
//
