ID   FAU1_PYRAB              Reviewed;         469 AA.
AC   Q9V2F9; G8ZFV0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   25-MAY-2022, entry version 105.
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=PYRAB01150;
GN   ORFNames=PAB0071;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB49039.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AJ248283; CAB49039.1; ALT_INIT; Genomic_DNA.
DR   EMBL; HE613800; CCE69491.1; -; Genomic_DNA.
DR   PIR; H75198; H75198.
DR   RefSeq; WP_048146488.1; NC_000868.1.
DR   AlphaFoldDB; Q9V2F9; -.
DR   SMR; Q9V2F9; -.
DR   STRING; 272844.PAB0071; -.
DR   PRIDE; Q9V2F9; -.
DR   EnsemblBacteria; CAB49039; CAB49039; PAB0071.
DR   GeneID; 1495002; -.
DR   KEGG; pab:PAB0071; -.
DR   PATRIC; fig|272844.11.peg.128; -.
DR   eggNOG; arCOG04307; Archaea.
DR   HOGENOM; CLU_044303_0_0_2; -.
DR   OrthoDB; 83570at2157; -.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; 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..469
FT                   /note="Probable ribonuclease FAU-1"
FT                   /id="PRO_0000334206"
SQ   SEQUENCE   469 AA;  53800 MW;  9D51996D586C9D6E CRC64;
     MSTESEISVR IRGIYSTALT KLFLDKGFKI VQPSDVIAER LGIEKSYEDF DVDIYDRNHG
     ITIVGTKVEE VRKALEEELV DVFFRKLPYK LYGVYKGIVV KRDDRYVYVD IGNAIGTVLV
     EELPDAVEGD EVVVQVKKHN VLPHLSIMIT IPGDYAVLIP KPIGVQRHVK ISRKIRDPEE
     RERLRILGLS VNLGEWGILW RTAAAYKEWS LLRDELVRLS KIADKLKEAD KYSAPAEIIE
     GRSIYEVEFG GGAKKKLDEI RNRVVPTIEG HHQYKSYDPE FTLAVEVAEG ILAKMPSQRQ
     KISEGFVEAI TNSKGPRVGW IFTLNHVKPD GQVIKIGPGE VIEVSSRPLR VKIRRNLRPG
     RVYDGLEVPI EPGDYAITEI EAGKWWFVHR YYDRNGNLKG EFYNINTPVE IYPDKARYVD
     LEVDIVKWPD GKKEIIDKEK LKEHYEDGII SEKLYKAVLR IVQEVYERV