ID   FAU1_THEGJ              Reviewed;         471 AA.
AC   C5A2F3;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 66.
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=TGAM_2070;
OS   Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=593117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15229 / JCM 11827 / EJ3;
RX   PubMed=19558674; DOI=10.1186/gb-2009-10-6-r70;
RA   Zivanovic Y., Armengaud J., Lagorce A., Leplat C., Guerin P., Dutertre M.,
RA   Anthouard V., Forterre P., Wincker P., Confalonieri F.;
RT   "Genome analysis and genome-wide proteomics of Thermococcus gammatolerans,
RT   the most radioresistant organism known amongst the Archaea.";
RL   Genome Biol. 10:R70.1-R70.23(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; CP001398; ACS34572.1; -; Genomic_DNA.
DR   RefSeq; WP_015859675.1; NC_012804.1.
DR   AlphaFoldDB; C5A2F3; -.
DR   SMR; C5A2F3; -.
DR   STRING; 593117.TGAM_2070; -.
DR   PaxDb; C5A2F3; -.
DR   EnsemblBacteria; ACS34572; ACS34572; TGAM_2070.
DR   GeneID; 7988636; -.
DR   KEGG; tga:TGAM_2070; -.
DR   PATRIC; fig|593117.10.peg.2079; -.
DR   eggNOG; arCOG04307; Archaea.
DR   HOGENOM; CLU_044303_0_0_2; -.
DR   OMA; GTYVNVC; -.
DR   OrthoDB; 83570at2157; -.
DR   Proteomes; UP000001488; 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; RNA-binding; rRNA processing.
FT   CHAIN           1..471
FT                   /note="Probable ribonuclease FAU-1"
FT                   /id="PRO_1000216191"
SQ   SEQUENCE   471 AA;  54625 MW;  9EBDF023F19FD350 CRC64;
     MSTDTGVSVR VRGIYSTALT KLFLDRGFRI SQPSQKIAER LGIEKTYDEF DVDIYDKRDH
     HGVILVGTEV EKVKEVFEEE FIDVLFRKLP YQLYGIYKGL VIKRDERYVY VDIGNAIGTI
     PVEEGKNLHE GDEVLVQVKK HNLLPHLSTM LTIPGDYAVL IPKPVGVQRH VKISRKIRDS
     SERERLRILG LSIDMGEWGI LWRTAAAYKD WNTLRDEIIR LSKIADRLKE AEKKSAPEQI
     VEGRNIYEVE FGGGAKKKLD EIRNRVVPTV EGHHMLKAYD VEFSFAVEIA EGILAKVPGQ
     RIKVNQGFWE ALLDSKGPKK GWLFFLEHNK PDGQRYKLGP GEIVEVTFNP LRITLRRNLK
     PGKFYDGLDL PIEFGDYAIT EIEAGKWWFV HRYYDRNGNL KGEYYNINTP VEIYPDRARY
     IDLEIDIVKW PDGEKEIIDK DKLREHYEDG IISEKLYKAV LRITQEVYER I