FAU1_PYRFU
ID FAU1_PYRFU Reviewed; 469 AA.
AC Q8U4Q7; Q8NKW7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Probable ribonuclease FAU-1 {ECO:0000255|HAMAP-Rule:MF_01910, ECO:0000305};
DE EC=3.1.26.- {ECO:0000255|HAMAP-Rule:MF_01910, ECO:0000269|PubMed:28978920};
DE AltName: Full=FAU-1 protein {ECO:0000303|PubMed:12614195};
DE AltName: Full=P.furiosus AU-binding {ECO:0000303|PubMed:12614195};
DE AltName: Full=RNA-binding protein AU-1 {ECO:0000305};
DE AltName: Full=RNA-binding protein FAU-1 {ECO:0000255|HAMAP-Rule:MF_01910, ECO:0000303|PubMed:12614195};
GN Name=fau-1 {ECO:0000255|HAMAP-Rule:MF_01910, ECO:0000303|PubMed:12614195};
GN Synonyms=aubA {ECO:0000305}; OrderedLocusNames=PF0022;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-8, FUNCTION,
RP RNA-BINDING, ACTIVITY REGULATION, AND SUBUNIT.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=12614195; DOI=10.1042/bj20021968;
RA Kanai A., Oida H., Matsuura N., Doi H.;
RT "Expression cloning and characterization of a novel gene that encodes the
RT RNA-binding protein FAU-1 from Pyrococcus furiosus.";
RL Biochem. J. 372:253-261(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [3]
RP FUNCTION AS A RNASE, AND ACTIVITY REGULATION.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=28978920; DOI=10.1038/s41598-017-13062-3;
RA Ikeda Y., Okada Y., Sato A., Kanai T., Tomita M., Atomi H., Kanai A.;
RT "An archaeal RNA binding protein, FAU-1, is a novel ribonuclease related to
RT rRNA stability in Pyrococcus and Thermococcus.";
RL Sci. Rep. 7:12674-12674(2017).
CC -!- FUNCTION: Probable RNase involved in rRNA stability through maturation
CC and/or degradation of precursor rRNAs. Preferentially cleaves UA
CC sequences in the 5' precursor region of 5S rRNA (PubMed:28978920).
CC Binds to RNA in loop regions with AU-rich sequences. Binds to the
CC consensus sequence GGC(U/A)(U/A)U(U/C) in vitro (PubMed:12614195).
CC {ECO:0000269|PubMed:12614195, ECO:0000269|PubMed:28978920}.
CC -!- ACTIVITY REGULATION: Activity increases in the presence of Mg(2+)
CC (PubMed:28978920). RNA-binding is heat stable (PubMed:12614195).
CC {ECO:0000269|PubMed:12614195, ECO:0000269|PubMed:28978920}.
CC -!- SUBUNIT: Mainly homotrimer, but may form homohexamer, and homononamer.
CC {ECO:0000269|PubMed:12614195}.
CC -!- SIMILARITY: Belongs to the FAU-1 family. {ECO:0000255|HAMAP-
CC Rule:MF_01910, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB91152.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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; AB055587; BAB91152.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE009950; AAL80146.1; -; Genomic_DNA.
DR RefSeq; WP_011011134.1; NZ_CP023154.1.
DR AlphaFoldDB; Q8U4Q7; -.
DR SMR; Q8U4Q7; -.
DR STRING; 186497.PF0022; -.
DR EnsemblBacteria; AAL80146; AAL80146; PF0022.
DR GeneID; 41711808; -.
DR KEGG; pfu:PF0022; -.
DR PATRIC; fig|186497.12.peg.24; -.
DR eggNOG; arCOG04307; Archaea.
DR HOGENOM; CLU_044303_0_0_2; -.
DR OMA; GTYVNVC; -.
DR OrthoDB; 83570at2157; -.
DR PhylomeDB; Q8U4Q7; -.
DR Proteomes; UP000001013; 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; IPR019307; RNA-bd_AU-1/RNase_E/G.
DR InterPro; IPR016730; RNA-bd_FAU-1.
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.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Endonuclease; Hydrolase; Nuclease;
KW Reference proteome; RNA-binding; rRNA processing.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12614195"
FT CHAIN 2..469
FT /note="Probable ribonuclease FAU-1"
FT /id="PRO_0000334207"
FT DOMAIN 90..148
FT /note="S1 motif"
SQ SEQUENCE 469 AA; 53671 MW; C1D3D15FB9F65AA8 CRC64;
MSTESEIAVR IRGIYSTALT KLLMDRGFKI VQPSDVIAER FGIEKSYEDF DVDIYDKNHG
VTIVGTKVEA VKKVFEEEFI DVFFRKLPYK LHGIYKGLVV KRDDRFVYVD IGNVIGTVLI
EELPDAAEGD EVVVQVKKHN VLPHLSTLIT IPGDYAVLIP KPIGVQRHVK ISRKIKDPEE
RERLRILGLS VDLGEWGVLW RTAAAYKDWN TLRDELVRLS KIADKLKEAE KFSAPAEIIE
GREIYEIEFG GGVKKKLDEI RNEVVPTIEG HHQFKSYDPE FTLAVDVAEG ILAKLPSQRQ
KISKGFLEAI ITSKGPKVGW IFTLNHVKPD GQIIKIGPGE VIEVSTDPLK VTIKRYLRPG
KFYDGLEVPI ESGDYAITEI EAGKWWFVHR YYDKDGNLKG EFYNINTPVE IYPDKARYVD
LEVDIVRWPD GKKEIIDKEK LKEHYEEGII SEKLYKATLR IAQEVYDRL
