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ESF2_YARLI
ID   ESF2_YARLI              Reviewed;         324 AA.
AC   Q6CFT1;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Pre-rRNA-processing protein ESF2;
DE   AltName: Full=18S rRNA factor 2;
GN   Name=ESF2; OrderedLocusNames=YALI0B04136g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Involved in the small subunit (SSU) processome assembly and
CC       function, and in the 18S rRNA synthesis. Required for the early
CC       cleavages at sites A0, A1 and A2 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ESF2/ABP1 family. {ECO:0000305}.
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DR   EMBL; CR382128; CAG82708.1; -; Genomic_DNA.
DR   RefSeq; XP_500481.1; XM_500481.1.
DR   AlphaFoldDB; Q6CFT1; -.
DR   SMR; Q6CFT1; -.
DR   STRING; 4952.CAG82708; -.
DR   EnsemblFungi; CAG82708; CAG82708; YALI0_B04136g.
DR   GeneID; 2907052; -.
DR   KEGG; yli:YALI0B04136g; -.
DR   VEuPathDB; FungiDB:YALI0_B04136g; -.
DR   HOGENOM; CLU_054086_0_0_1; -.
DR   InParanoid; Q6CFT1; -.
DR   OMA; TRKHNDF; -.
DR   Proteomes; UP000001300; Chromosome B.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR   GO; GO:0032040; C:small-subunit processome; IEA:EnsemblFungi.
DR   GO; GO:0001671; F:ATPase activator activity; IEA:EnsemblFungi.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0000480; P:endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR   GO; GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR   GO; GO:0000472; P:endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR   GO; GO:0034462; P:small-subunit processome assembly; IBA:GO_Central.
DR   CDD; cd12263; RRM_ABT1_like; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR039119; ABT1/Esf2.
DR   InterPro; IPR034353; ABT1/ESF2_RRM.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   PANTHER; PTHR12311; PTHR12311; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
PE   3: Inferred from homology;
KW   Nucleus; Reference proteome; Ribosome biogenesis; RNA-binding;
KW   rRNA processing.
FT   CHAIN           1..324
FT                   /note="Pre-rRNA-processing protein ESF2"
FT                   /id="PRO_0000285381"
FT   DOMAIN          126..216
FT                   /note="RRM"
FT   REGION          1..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          248..324
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..38
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..71
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..91
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        92..116
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        248..264
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        265..313
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   324 AA;  36936 MW;  33593DB700704514 CRC64;
     MARAKAVDFF STKNNSSDSE EEEDKPAVDP RFVLADSDSE GEEEQEDGDE DEEEKGRTSK
     KKTKDFFELA GKTDDGDDEE EDEEDEEEEE EEKEKKPVKT SSTKAKTKPM TKEEIEKHNK
     KIAKTGVVYF SRIPPLMDPG KLRMLLQRFG IVDRIYLVPE DPKAQAVRIR HGGNRALAYT
     EGWAEFTKKR YAKTCASTLN GNTIGGKKGS QHYDDIMNAK YLPKFKWSDL SEQLAQETHN
     RQARLRTEIS QATRENQTYI QSLEKSKAAE RRRQRQEEEG GETEEKPAKK VHRDFYQGKT
     HSARAKEGKK ELDGSVGSIL GSVM
 
 
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