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 23-FEB-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=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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000505; ABL77967.1; -; Genomic_DNA. DR RefSeq; WP_011752232.1; NC_008698.1. 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 //