FAU1_HALMA
ID FAU1_HALMA Reviewed; 466 AA.
AC Q5V0I9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 83.
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=rrnAC2113;
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=272569;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT Dead Sea.";
RL Genome Res. 14:2221-2234(2004).
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; AY596297; AAV46964.1; -; Genomic_DNA.
DR RefSeq; WP_011224036.1; NZ_CP039138.1.
DR AlphaFoldDB; Q5V0I9; -.
DR SMR; Q5V0I9; -.
DR STRING; 272569.rrnAC2113; -.
DR EnsemblBacteria; AAV46964; AAV46964; rrnAC2113.
DR GeneID; 40153027; -.
DR KEGG; hma:rrnAC2113; -.
DR PATRIC; fig|272569.17.peg.2761; -.
DR eggNOG; arCOG04307; Archaea.
DR HOGENOM; CLU_044303_0_0_2; -.
DR OMA; GTYVNVC; -.
DR Proteomes; UP000001169; Chromosome I.
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; IPR016730; RNA-bd_FAU-1.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR Pfam; PF04167; DUF402; 1.
DR Pfam; PF00575; S1; 1.
DR PIRSF; PIRSF018644; RNA-binding_FAU-1; 1.
DR SMART; SM00316; S1; 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..466
FT /note="Probable ribonuclease FAU-1"
FT /id="PRO_0000334194"
FT DOMAIN 90..152
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01910"
SQ SEQUENCE 466 AA; 49462 MW; 0F2202C56C8FDAFF CRC64;
MTVRVRGIYA TALTRLLREA GHEVVQASGP IEDRFDGEFA DERAAVTVTT TDDQQGVGVI
GDHDAAAAVT DRLTELGRDT LHWSDPTPEG AIYAGTVTDT LGSGAVVDLG DGEGFLPYSS
SDERVETGDT LRVQVVEASA PWTDGRPVLD TTVAVRGSLL SLVRGETAST PGTGGPAMLD
LIAAEPRDGW GVSWESASED ASFDALAAAL DAANDRAAAI DASLDGADAP EDCAPTRYDE
GRSTVWLWFG RESRFALDEV RREVTSTMPG HHRVKAGDRA ASAAVDYVEA LCDDPETGET
DFPFAVTTRQ FGPQVGGSLS LGHGKPDGRL ITLGNGEVQS VDDDGTVTIE REMSPGGTYD
ALGVPKEAGD IAETKVKEGR WWYPTVYRDS DGEKKGTYVN VCTPVEIFPD TARYVDLHVD
VVKHADGAVE RVDDDELDAA VERGHISEPL AERARSVAAA VKSALE
