ID   FAU1_HYPBU              Reviewed;         473 AA.
AC   A2BN82;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 67.
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=Hbut_1628;
OS   Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC   Hyperthermus.
OX   NCBI_TaxID=415426;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5456 / JCM 9403 / PLM1-5;
RX   PubMed=17350933; DOI=10.1155/2007/745987;
RA   Bruegger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M.,
RA   She Q., Garrett R.A., Klenk H.-P.;
RT   "The genome of Hyperthermus butylicus: a sulfur-reducing, peptide
RT   fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.";
RL   Archaea 2:127-135(2007).
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; CP000493; ABM81443.1; -; Genomic_DNA.
DR   RefSeq; WP_011822761.1; NC_008818.1.
DR   AlphaFoldDB; A2BN82; -.
DR   SMR; A2BN82; -.
DR   STRING; 415426.Hbut_1628; -.
DR   EnsemblBacteria; ABM81443; ABM81443; Hbut_1628.
DR   GeneID; 4781637; -.
DR   KEGG; hbu:Hbut_1628; -.
DR   eggNOG; arCOG04307; Archaea.
DR   HOGENOM; CLU_044303_0_0_2; -.
DR   OMA; GTYVNVC; -.
DR   OrthoDB; 83570at2157; -.
DR   Proteomes; UP000002593; 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; IPR019307; RNA-bd_AU-1/RNase_E/G.
DR   InterPro; IPR016730; RNA-bd_FAU-1.
DR   Pfam; PF04167; DUF402; 1.
DR   Pfam; PF10150; RNase_E_G; 1.
DR   PIRSF; PIRSF018644; RNA-binding_FAU-1; 1.
DR   SUPFAM; SSF159234; SSF159234; 1.
PE   3: Inferred from homology;
KW   Endonuclease; Hydrolase; Nuclease; Reference proteome; RNA-binding;
KW   rRNA processing.
FT   CHAIN           1..473
FT                   /note="Probable ribonuclease FAU-1"
FT                   /id="PRO_0000334198"
SQ   SEQUENCE   473 AA;  52982 MW;  11ACCACCB7DDDA36 CRC64;
     MATPARRIPR VRVRGIYATA LTKLVIDMGF QVVQPSRIIA DRFSLPMLTL PADVTIKDSD
     NNPSELLIVG YEWAVNIILE KLRDTLPYSF YWRSSLPLHS TVKARVIGLR DNRCIARVGD
     VEAELLVDRS ECIEDREVVG GVVRPGVKPR ETPRIVPGAR VIGDYAILIE SSEPRVTISE
     HVRSPEKRAL LAAIATSFTE QGYAVHWRSS SQHAEREELE KHLRQLREAL AEARKRAEEG
     PPGVYSEGEA VVLVHLSSAD KQKLDEIRDS VVATIPYHHT VKSLQPSLSK VIDYAEKVKA
     LGVDSEKLVR ALLELVAEDL ASRRRIRILH VKPSGEYIEL GKAEIKSVYV EDKSLVIVLE
     RTVKSRGVYD GLGVEKEPGD RIVTEVRTDE WIVKHTYYAP DGTVKGTYIN INTPPEIAED
     AIVYLDLEID IVKKPGKKPK IVDAEELDKY HEQGIVTTKL KEKALEIARK LAG