ID   FAU1_METKA              Reviewed;         484 AA.
AC   Q8TY07;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 97.
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=MK0499;
OS   Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC   Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC   Methanopyrus.
OX   NCBI_TaxID=190192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX   PubMed=11930014; DOI=10.1073/pnas.032671499;
RA   Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA   Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA   Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA   Koonin E.V., Kozyavkin S.A.;
RT   "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT   monophyly of archaeal methanogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
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; AE009439; AAM01714.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8TY07; -.
DR   SMR; Q8TY07; -.
DR   STRING; 190192.MK0499; -.
DR   EnsemblBacteria; AAM01714; AAM01714; MK0499.
DR   KEGG; mka:MK0499; -.
DR   PATRIC; fig|190192.8.peg.529; -.
DR   HOGENOM; CLU_044303_0_0_2; -.
DR   OMA; GTYVNVC; -.
DR   Proteomes; UP000001826; 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; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR019307; RNA-bd_AU-1/RNase_E/G.
DR   InterPro; IPR016730; RNA-bd_FAU-1.
DR   InterPro; IPR003029; S1_domain.
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.
DR   SUPFAM; SSF50249; SSF50249; 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..484
FT                   /note="Probable ribonuclease FAU-1"
FT                   /id="PRO_0000334200"
FT   DOMAIN          92..153
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01910"
SQ   SEQUENCE   484 AA;  54156 MW;  076EDE9AB5857D9F CRC64;
     MPCKVRIRGI YSTALTKICL DHGFIVTQPS DDIRRRFPDA EFDSGSPDVD VRDTRNRHGI
     EIQGPADDVR ELVDILQSEV WATVTADKIG EGSVFKGVVR EIDDRAGVAV VDLGNGLQGF
     LSEDESEVVE EGEELVVQVA KSVSDGPLKL TTEVTVAGEY AVLVPVEGIR VSRKIRDERE
     RERLKRLGEA LVPEGWGLIW RTAAEGKSGE ELAEEIDDLI EERKQLFKRA EEMSEPGPIR
     DVREMELEIH SLAKSRLDSV RSEVLPTMVG HHYFKCRSLA GSVAVDTVEP FLDDLDEEVV
     AERLIRCLTR SEGPSEGDRI DIVHVKPGQG VKKLGGNPKV VEYDPVEGIL KVRREMRGPG
     FYDGIDKPIE KGDYAISILP DGSMVTVHQY FNKDGELKGR YYNIGTPLEV FKNCVRYVDL
     EVDVVEPEEG EREIIDEEDL ERAVDSGLIP EELAELALET AKRVEKRGMK EVKPYPVWKG
     FEHG