ID   RNAS6_CHLAE             Reviewed;         150 AA.
AC   O46534;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Ribonuclease K6;
DE            Short=RNase K6;
DE            EC=3.1.27.-;
DE   Flags: Precursor;
GN   Name=RNASE6;
OS   Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Chlorocebus.
OX   NCBI_TaxID=9534;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9647635; DOI=10.1101/gr.8.6.599;
RA   Deming M.S., Dyer K.D., Bankier A.T., Piper M.B., Dear P.H.,
RA   Rosenberg H.F.;
RT   "Ribonuclease k6: chromosomal mapping and divergent rates of evolution
RT   within the RNase A gene superfamily.";
RL   Genome Res. 8:599-607(1998).
CC   -!- FUNCTION: Ribonuclease which shows a preference for the pyrimidines
CC       uridine and cytosine. Has potent antibacterial activity against a range
CC       of Gram-positive and Gram-negative bacteria, including P.aeruginosa,
CC       A.baumanii, M.luteus, S.aureus, E.faecalis, E.faecium, S.saprophyticus
CC       and E.coli. Causes loss of bacterial membrane integrity, and also
CC       promotes agglutination of Gram-negative bacteria. Probably contributes
CC       to urinary tract sterility. Bactericidal activity is independent of
CC       RNase activity. {ECO:0000250|UniProtKB:Q93091}.
CC   -!- SUBUNIT: Interacts (via N-terminus) with bacterial lipopolysaccharide
CC       (LPS). {ECO:0000250|UniProtKB:Q93091}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q93091}. Lysosome
CC       {ECO:0000250|UniProtKB:Q93091}. Cytoplasmic granule
CC       {ECO:0000250|UniProtKB:Q93091}.
CC   -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF037090; AAB94752.1; -; Genomic_DNA.
DR   AlphaFoldDB; O46534; -.
DR   SMR; O46534; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0016070; P:RNA metabolic process; IEA:UniProt.
DR   Gene3D; 3.10.130.10; -; 1.
DR   InterPro; IPR001427; RNaseA.
DR   InterPro; IPR036816; RNaseA-like_dom_sf.
DR   InterPro; IPR023411; RNaseA_AS.
DR   InterPro; IPR023412; RNaseA_domain.
DR   PANTHER; PTHR11437; PTHR11437; 1.
DR   Pfam; PF00074; RnaseA; 1.
DR   PRINTS; PR00794; RIBONUCLEASE.
DR   SMART; SM00092; RNAse_Pc; 1.
DR   SUPFAM; SSF54076; SSF54076; 1.
DR   PROSITE; PS00127; RNASE_PANCREATIC; 1.
PE   3: Inferred from homology;
KW   Antibiotic; Antimicrobial; Disulfide bond; Endonuclease; Glycoprotein;
KW   Hydrolase; Lysosome; Nuclease; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000250"
FT   CHAIN           24..150
FT                   /note="Ribonuclease K6"
FT                   /id="PRO_0000030890"
FT   ACT_SITE        38
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q64438"
FT   ACT_SITE        145
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q64438"
FT   BINDING         61..65
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         86
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         105
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            59
FT                   /note="Facilitates cleavage of polynucleotide substrates"
FT                   /evidence="ECO:0000250|UniProtKB:Q93091"
FT   SITE            61
FT                   /note="Critical for catalytic activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H1E1"
FT   CARBOHYD        55
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        100
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        46..104
FT                   /evidence="ECO:0000250|UniProtKB:Q93091"
FT   DISULFID        60..114
FT                   /evidence="ECO:0000250|UniProtKB:Q93091"
FT   DISULFID        78..129
FT                   /evidence="ECO:0000250|UniProtKB:Q93091"
FT   DISULFID        85..92
FT                   /evidence="ECO:0000250|UniProtKB:Q93091"
SQ   SEQUENCE   150 AA;  17178 MW;  0424428106EB8E07 CRC64;
     MVLCFPLLLL LLVLWGPVCL LHAWPKHLTR AHWFEIQHIQ PSPLQCNRAM SGINNYTQHC
     KHQNTFLHDS FQNVAAVCDL LSIICKNRQH NCHQSSKPVN MTDCRLTSGK YPQCRYSAAG
     LYKFFIVACD PPQKSDPPYK LVPVHLDSIL