ID   FAU1_NATPD              Reviewed;         461 AA.
AC   Q3ITR7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Probable ribonuclease FAU-1 {ECO:0000255|HAMAP-Rule:MF_01910};
DE            EC=3.1.26.- {ECO:0000255|HAMAP-Rule:MF_01910};
DE   AltName: Full=RNA-binding protein FAU-1 {ECO:0000255|HAMAP-Rule:MF_01910};
GN   Name=fau-1 {ECO:0000255|HAMAP-Rule:MF_01910}; OrderedLocusNames=NP_0750A;
OS   Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS   8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Natronomonas.
OX   NCBI_TaxID=348780;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB
RC   2260 / Gabara;
RX   PubMed=16169924; DOI=10.1101/gr.3952905;
RA   Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA   Oesterhelt D.;
RT   "Living with two extremes: conclusions from the genome sequence of
RT   Natronomonas pharaonis.";
RL   Genome Res. 15:1336-1343(2005).
CC   -!- FUNCTION: Probable RNase involved in rRNA stability through maturation
CC       and/or degradation of precursor rRNAs. Binds to RNA in loop regions
CC       with AU-rich sequences. {ECO:0000255|HAMAP-Rule:MF_01910}.
CC   -!- SIMILARITY: Belongs to the FAU-1 family. {ECO:0000255|HAMAP-
CC       Rule:MF_01910}.
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DR   EMBL; CR936257; CAI48466.1; -; Genomic_DNA.
DR   RefSeq; WP_011322102.1; NC_007426.1.
DR   AlphaFoldDB; Q3ITR7; -.
DR   SMR; Q3ITR7; -.
DR   STRING; 348780.NP_0750A; -.
DR   EnsemblBacteria; CAI48466; CAI48466; NP_0750A.
DR   GeneID; 3700951; -.
DR   KEGG; nph:NP_0750A; -.
DR   eggNOG; arCOG04307; Archaea.
DR   HOGENOM; CLU_044303_0_0_2; -.
DR   OMA; GTYVNVC; -.
DR   OrthoDB; 83570at2157; -.
DR   Proteomes; UP000002698; Chromosome.
DR   GO; GO:0016891; F:endoribonuclease activity, producing 5'-phosphomonoesters; IEA:UniProtKB-UniRule.
DR   GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.40.380.10; -; 1.
DR   HAMAP; MF_01910; RNA_binding_AU_1; 1.
DR   InterPro; IPR007295; DUF402.
DR   InterPro; IPR035930; FomD-like_sf.
DR   InterPro; IPR016730; RNA-bd_FAU-1.
DR   InterPro; IPR003029; S1_domain.
DR   Pfam; PF04167; DUF402; 1.
DR   PIRSF; PIRSF018644; RNA-binding_FAU-1; 1.
DR   SUPFAM; SSF159234; SSF159234; 1.
DR   PROSITE; PS50126; S1; 1.
PE   3: Inferred from homology;
KW   Endonuclease; Hydrolase; Nuclease; Reference proteome; RNA-binding;
KW   rRNA processing.
FT   CHAIN           1..461
FT                   /note="Probable ribonuclease FAU-1"
FT                   /id="PRO_0000334201"
FT   DOMAIN          89..158
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01910"
SQ   SEQUENCE   461 AA;  49556 MW;  CD523053114DEF3B CRC64;
     MNVRVRGIYT TALTELLGGE YDIVQASPPI QRRFEASFPV AVADATVRTS DDRLGAGIAG
     TADAVDAVGE TLSALGRDTF RWTDPAPRGA VFYGEVTETL GSGAVVDLGT VDGDSVEGFL
     PYNRVEGYVD EGDSYRVQVA SPEPPWGDAR PSLATALRIP GGLVELRRGS EGGLSETARM
     ADLLPVDPPE GWTPNWSRAA DDASLEAMEA ALRRASDRAE TVMEAVVDAD RDEPGRIVAP
     QAGAWLLFGR ESRFELDEYR RQIETTMPGH HRTKAATTAA SAAVDFAEAL CEPDGAFPFD
     VVTRQFGPTE GDDVTISHGK PDGRTISLGR GEVTDRDPEA ESITVEREMS GGGTYDAIGV
     KREAGDIATT TFVEGRWWYP TVYCSADGER RGTYVNICTP LEVFPDTVRY VDLHVDVVKG
     PDGDVRRVDD DELDAAVEAG EISEPLAERA REVAAAIKKA L