ID   A0A519M5A6_9BACT        Unreviewed;       199 AA.
AC   A0A519M5A6;
DT   16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2019, sequence version 1.
DT   13-NOV-2019, entry version 2.
DE   RecName: Full=Ribonuclease 3 {ECO:0000256|HAMAP-Rule:MF_00104};
DE            EC=3.1.26.3 {ECO:0000256|HAMAP-Rule:MF_00104};
DE   AltName: Full=Ribonuclease III {ECO:0000256|HAMAP-Rule:MF_00104};
DE            Short=RNase III {ECO:0000256|HAMAP-Rule:MF_00104};
GN   Name=rnc {ECO:0000256|HAMAP-Rule:MF_00104,
GN   ECO:0000313|EMBL:RZJ56747.1};
GN   ORFNames=EOO55_04665 {ECO:0000313|EMBL:RZJ56747.1};
OS   Hymenobacter sp.
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Hymenobacter.
OX   NCBI_TaxID=1898978 {ECO:0000313|EMBL:RZJ56747.1};
RN   [1] {ECO:0000313|EMBL:RZJ56747.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PMG_005 {ECO:0000313|EMBL:RZJ56747.1};
RX   PubMed=30498029; DOI=.1073/pnas.1812668115;
RA   Crombie A.T., Larke-Mejia N.L., Emery H., Dawson R., Pratscher J.,
RA   Murphy G.P., McGenity T.J., Murrell J.C.;
RT   "Poplar phyllosphere harbors disparate isoprene-degrading bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 115:13081-13086(2018).
RN   [2] {ECO:0000313|EMBL:RZJ56747.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PMG_005 {ECO:0000313|EMBL:RZJ56747.1};
RA   Crombie A.;
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Digests double-stranded RNA. Involved in the processing
CC       of primary rRNA transcript to yield the immediate precursors to
CC       the large and small rRNAs (23S and 16S). Processes some mRNAs, and
CC       tRNAs when they are encoded in the rRNA operon. Processes pre-
CC       crRNA and tracrRNA of type II CRISPR loci if present in the
CC       organism. {ECO:0000256|HAMAP-Rule:MF_00104}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.;
CC         EC=3.1.26.3; Evidence={ECO:0000256|HAMAP-Rule:MF_00104,
CC         ECO:0000256|SAAS:SAAS01115986};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00104, ECO:0000256|SAAS:SAAS00751453};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00104,
CC       ECO:0000256|SAAS:SAAS00751513}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00104,
CC       ECO:0000256|SAAS:SAAS00751438}.
CC   -!- SIMILARITY: Belongs to the ribonuclease III family.
CC       {ECO:0000256|SAAS:SAAS00809456}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:RZJ56747.1}.
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DR   EMBL; SEBX01000183; RZJ56747.1; -; Genomic_DNA.
DR   CDD; cd00048; DSRM; 1.
DR   CDD; cd00593; RIBOc; 1.
DR   Gene3D; 1.10.1520.10; -; 1.
DR   HAMAP; MF_00104; RNase_III; 1.
DR   InterPro; IPR014720; dsRBD_dom.
DR   InterPro; IPR011907; RNase_III.
DR   InterPro; IPR000999; RNase_III_dom.
DR   InterPro; IPR036389; RNase_III_sf.
DR   Pfam; PF00035; dsrm; 1.
DR   Pfam; PF14622; Ribonucleas_3_3; 1.
DR   SMART; SM00358; DSRM; 1.
DR   SMART; SM00535; RIBOc; 1.
DR   SUPFAM; SSF69065; SSF69065; 1.
DR   TIGRFAMs; TIGR02191; RNaseIII; 1.
DR   PROSITE; PS50137; DS_RBD; 1.
DR   PROSITE; PS00517; RNASE_3_1; 1.
DR   PROSITE; PS50142; RNASE_3_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00104,
KW   ECO:0000256|SAAS:SAAS00751501};
KW   Endonuclease {ECO:0000256|HAMAP-Rule:MF_00104,
KW   ECO:0000256|SAAS:SAAS00751464};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00104,
KW   ECO:0000256|SAAS:SAAS00751448, ECO:0000313|EMBL:RZJ56747.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00104,
KW   ECO:0000256|SAAS:SAAS00751488};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00104,
KW   ECO:0000256|SAAS:SAAS00751459};
KW   mRNA processing {ECO:0000256|HAMAP-Rule:MF_00104,
KW   ECO:0000256|SAAS:SAAS00751469};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_00104,
KW   ECO:0000256|SAAS:SAAS00751483};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00104, ECO:0000256|PROSITE-
KW   ProRule:PRU00266, ECO:0000256|SAAS:SAAS00880466};
KW   rRNA processing {ECO:0000256|HAMAP-Rule:MF_00104,
KW   ECO:0000256|SAAS:SAAS00751509};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_00104,
KW   ECO:0000256|SAAS:SAAS00745773};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_00104,
KW   ECO:0000256|SAAS:SAAS00751473}.
FT   DOMAIN        8    103       RNase III. {ECO:0000259|PROSITE:PS50142}.
FT   DOMAIN      131    199       DRBM. {ECO:0000259|PROSITE:PS50137}.
FT   ACT_SITE     22     22       {ECO:0000256|HAMAP-Rule:MF_00104}.
FT   ACT_SITE     92     92       {ECO:0000256|HAMAP-Rule:MF_00104}.
FT   METAL        18     18       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00104}.
FT   METAL        89     89       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00104}.
FT   METAL        92     92       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00104}.
SQ   SEQUENCE   199 AA;  21839 MW;  7D81A78ABDE9D454 CRC64;
     MVRAEPGAGR HQSNERLEFL GDAVLGTVVA EYLFRKFPYE QEGFLTETRS RIVNRESLNA
     IALKLGLDRL VQLDAAQTRV ARSRSVNGNA LEALVGAVYL DLGYKAARKF VLKGLIKPFV
     DVNTLTTTTS NYKSKLIEWA QRNGKAVRYD ISGEPRPGGV MEFTATVILN EEVIATGMGL
     NKKQAEQLAA ERALVALGV
//