ID   FAU1_THEPD              Reviewed;         491 AA.
AC   A1RXN7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 69.
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=Tpen_0561;
OS   Thermofilum pendens (strain DSM 2475 / Hrk 5).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermofilales; Thermofilaceae;
OC   Thermofilum.
OX   NCBI_TaxID=368408;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2475 / Hrk 5;
RX   PubMed=18263724; DOI=10.1128/jb.01949-07;
RA   Anderson I., Rodriguez J., Susanti D., Porat I., Reich C., Ulrich L.E.,
RA   Elkins J.G., Mavromatis K., Lykidis A., Kim E., Thompson L.S., Nolan M.,
RA   Land M., Copeland A., Lapidus A., Lucas S., Detter C., Zhulin I.B.,
RA   Olsen G.J., Whitman W., Mukhopadhyay B., Bristow J., Kyrpides N.;
RT   "Genome sequence of Thermofilum pendens reveals an exceptional loss of
RT   biosynthetic pathways without genome reduction.";
RL   J. Bacteriol. 190:2957-2965(2008).
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; CP000505; ABL77967.1; -; Genomic_DNA.
DR   RefSeq; WP_011752232.1; NC_008698.1.
DR   AlphaFoldDB; A1RXN7; -.
DR   STRING; 368408.Tpen_0561; -.
DR   EnsemblBacteria; ABL77967; ABL77967; Tpen_0561.
DR   GeneID; 4600604; -.
DR   KEGG; tpe:Tpen_0561; -.
DR   eggNOG; arCOG04307; Archaea.
DR   HOGENOM; CLU_044303_0_0_2; -.
DR   OMA; GTYVNVC; -.
DR   OrthoDB; 83570at2157; -.
DR   Proteomes; UP000000641; 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..491
FT                   /note="Probable ribonuclease FAU-1"
FT                   /id="PRO_0000334214"
SQ   SEQUENCE   491 AA;  54025 MW;  E29B5317C99C0A40 CRC64;
     MIRVRGIHST AIAGLLDEAG FRFADLSQEL LARIPQLRVE ERVLVTVKDT DDRSGVVVLG
     DRAVVEKVAY LLRAVIPGAL VSYVGEGPYT TYAVRLLSRV EGDVYEAEYS PGKRTTVKLR
     RPHVEGEVIM AHVIRASPEA PLLKEGVAIT GSLVRLVQFD RHSVSEHIRD ENLRLQLLTL
     AMTSAPTGWG VHFRSASKRA SIVDVMAEIK ALSEKAEKIL KEVAPKEPGV VVPGEAIAIV
     EIPADASIRM DALRSRYYPT LPLHHLLKRL GDDELSRAVD FSERLLAGCE KCLSSTGAIE
     VFLERLSSLK GRQVSVLHRK VAGAGHVWSA EVESVKRMTV VLKRVVSSPG LYDGFEGLKR
     EPGDVIRSYT WLFGRAVVHF YTSARGELKG VYVNINAPVF FAGNANTLGY VDLGVDVTRA
     ADEEPKVVDL AEFLDLVERG VLDKQLAGSY LEFAESVKHL LEKDIGEDLP ARIMQAQKSI
     FSFETDKLLA V