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FAU1_SULAC
ID   FAU1_SULAC              Reviewed;         418 AA.
AC   Q4J9H1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   25-MAY-2022, entry version 78.
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=Saci_1213;
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS   15157 / NCIMB 11770).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=330779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
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; CP000077; AAY80559.1; -; Genomic_DNA.
DR   RefSeq; WP_011278061.1; NC_007181.1.
DR   AlphaFoldDB; Q4J9H1; -.
DR   STRING; 330779.Saci_1213; -.
DR   EnsemblBacteria; AAY80559; AAY80559; Saci_1213.
DR   GeneID; 3473558; -.
DR   KEGG; sai:Saci_1213; -.
DR   PATRIC; fig|330779.12.peg.1175; -.
DR   eggNOG; arCOG04307; Archaea.
DR   HOGENOM; CLU_044303_0_0_2; -.
DR   OMA; GTYVNVC; -.
DR   Proteomes; UP000001018; 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   PIRSF; PIRSF018644; RNA-binding_FAU-1; 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..418
FT                   /note="Probable ribonuclease FAU-1"
FT                   /id="PRO_0000334211"
SQ   SEQUENCE   418 AA;  48447 MW;  3870F1167C8D3F3B CRC64;
     MRVRIRGIYA TALTYLFLKN GFEIVQQTPQ IAERFFMDII RSPADVTVKD GIDKGEIVSV
     GEDIYNFMRS IFKYSPIWRS PIKLYSVVST EDCKFMNFIV EPCLSEGLVI KPPVEGKIIL
     SSPRAVGKFA MVWKGDGRTF FSEHIDERDS QRLLSVSIPF NKKGYNVKWR SNAAMATTAE
     LKEELENLTM RYSYNDFREQ GEDFLKVTLS LEDKLFLDDI RSLVINTMKF HHMLKMTYSN
     EVDIEEGKVN PSPEKLLTSL IGDNMIEAIE HVKPNGKRVL LKGGTIVQKE IGRDYYWLKI
     RREFKSGGIY DGLNLKIEDG DYDLVELDSR NWYQIHRYHD RNNNLKGLYV NISTPPELLK
     NRIRYLDLEV DVVKVNNTVN IIDLEELEAN KPILGEFLYK KALEIAQNIK DKLNEDKI
 
 
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