ID   FAU1_CALMQ              Reviewed;         471 AA.
AC   A8M8Y9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   25-MAY-2022, entry version 68.
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=Cmaq_1382;
OS   Caldivirga maquilingensis (strain ATCC 700844 / DSM 13496 / JCM 10307 /
OS   IC-167).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Caldivirga.
OX   NCBI_TaxID=397948;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700844 / DSM 13496 / JCM 10307 / IC-167;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., Lowe T.M.,
RA   Saltikov C., House C.H., Richardson P.;
RT   "Complete sequence of Caldivirga maquilingensis IC-167.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000852; ABW02208.1; -; Genomic_DNA.
DR   RefSeq; WP_012186427.1; NC_009954.1.
DR   AlphaFoldDB; A8M8Y9; -.
DR   STRING; 397948.Cmaq_1382; -.
DR   EnsemblBacteria; ABW02208; ABW02208; Cmaq_1382.
DR   GeneID; 5709315; -.
DR   KEGG; cma:Cmaq_1382; -.
DR   eggNOG; arCOG04307; Archaea.
DR   HOGENOM; CLU_044303_0_0_2; -.
DR   OMA; GTYVNVC; -.
DR   OrthoDB; 83570at2157; -.
DR   Proteomes; UP000001137; 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   Pfam; PF04167; DUF402; 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..471
FT                   /note="Probable ribonuclease FAU-1"
FT                   /id="PRO_0000334193"
SQ   SEQUENCE   471 AA;  52266 MW;  9B6FB282A2F8E703 CRC64;
     MTKVRVRGIY ATALTKIMLE DGYDIVQATD TILSRFNILH STEPPDVTIK DDENIPGALF
     IIGKCSEVNK VLESILRRVG DVAYNKPPVP LYSVIMGVVA DNGHIEVAPG VLALLEGSNY
     FRPGDKLPVT MVNVTGQLRA SPYIMPTTSY LRVIDSPTVR LSRHIKDPDA KMMLVRVGLS
     KINQLGGLGI RWRSSAQYLS EEDAEKALDE AISLVNAIRV KIAEARDYDM LFEGECIVSV
     ILDAEARWVL DDIRNTIVPT VKGHHALKIT MKNTEILDYT EYLVGELKMR DELGRALANY
     ALSNLSTINV HHVKVNGEHI NLGPGERVHY SNGLLIIRRE LKPGGTLDGL NVAKEYGDAA
     YSVINIGERH LTHIYVSHDG SFKGAYVNIN TPIEVTWDGV IYIDLEVDLT VDKGFNVNII
     DEDKLSSIPS RRLINEAEEE LSRLKGDVVN LVRNHIDTLS KLGLSIHYQG P