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PESC_ASHGO
ID   PESC_ASHGO              Reviewed;         596 AA.
AC   Q75EI5;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Pescadillo homolog {ECO:0000255|HAMAP-Rule:MF_03028};
DE   AltName: Full=Nucleolar protein 7 homolog {ECO:0000255|HAMAP-Rule:MF_03028};
GN   Name=NOP7 {ECO:0000255|HAMAP-Rule:MF_03028}; OrderedLocusNames=AAR094W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Component of the NOP7 complex, which is required for
CC       maturation of the 25S and 5.8S ribosomal RNAs and formation of the 60S
CC       ribosome. {ECO:0000255|HAMAP-Rule:MF_03028}.
CC   -!- SUBUNIT: Component of the NOP7 complex, composed of ERB1, NOP7 and
CC       YTM1. The complex is held together by ERB1, which interacts with NOP7
CC       via its N-terminal domain and with YTM1 via a high-affinity interaction
CC       between the seven-bladed beta-propeller domains of the 2 proteins. The
CC       NOP7 complex associates with the 66S pre-ribosome. {ECO:0000255|HAMAP-
CC       Rule:MF_03028}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000255|HAMAP-
CC       Rule:MF_03028}. Nucleus, nucleoplasm {ECO:0000255|HAMAP-Rule:MF_03028}.
CC   -!- SIMILARITY: Belongs to the pescadillo family. {ECO:0000255|HAMAP-
CC       Rule:MF_03028}.
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DR   EMBL; AE016814; AAS50459.1; -; Genomic_DNA.
DR   RefSeq; NP_982635.1; NM_207988.1.
DR   AlphaFoldDB; Q75EI5; -.
DR   SMR; Q75EI5; -.
DR   STRING; 33169.AAS50459; -.
DR   EnsemblFungi; AAS50459; AAS50459; AGOS_AAR094W.
DR   GeneID; 4618625; -.
DR   KEGG; ago:AGOS_AAR094W; -.
DR   eggNOG; KOG2481; Eukaryota.
DR   HOGENOM; CLU_019619_1_1_1; -.
DR   InParanoid; Q75EI5; -.
DR   OMA; TWIVPHY; -.
DR   Proteomes; UP000000591; Chromosome I.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0070545; C:PeBoW complex; IBA:GO_Central.
DR   GO; GO:0030687; C:preribosome, large subunit precursor; IEA:UniProtKB-UniRule.
DR   GO; GO:0070180; F:large ribosomal subunit rRNA binding; IEA:EnsemblFungi.
DR   GO; GO:0043021; F:ribonucleoprotein complex binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0000466; P:maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:UniProtKB-UniRule.
DR   GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR   GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:EnsemblFungi.
DR   Gene3D; 3.40.50.10190; -; 1.
DR   HAMAP; MF_03028; Pescadillo; 1.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR036420; BRCT_dom_sf.
DR   InterPro; IPR010613; PES.
DR   PANTHER; PTHR12221; PTHR12221; 1.
DR   Pfam; PF16589; BRCT_2; 1.
DR   Pfam; PF06732; Pescadillo_N; 1.
DR   SMART; SM00292; BRCT; 1.
DR   SUPFAM; SSF52113; SSF52113; 1.
DR   PROSITE; PS50172; BRCT; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Nucleus; Reference proteome; Ribosome biogenesis;
KW   rRNA processing.
FT   CHAIN           1..596
FT                   /note="Pescadillo homolog"
FT                   /id="PRO_0000370477"
FT   DOMAIN          347..440
FT                   /note="BRCT"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03028"
FT   REGION          449..552
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          460..596
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03028"
FT   COMPBIAS        460..501
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        534..552
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   596 AA;  67752 MW;  BDDFAC4C450973E5 CRC64;
     MRVKKKNTTG NARNFVTRSQ AVRKLQISLA DFRRLCIFKG IYPREPRNKK KANKGSTAPT
     TFYYYKDIQY LQHEPVLAKF REHKTFAKKL TRALGRGEVS SAKKLEENKS HYKLDHIIKE
     RYPSFADALR DLDDALNMLF LFANLPATDQ VSTRVTKDAQ ELCNQWLALI ARERLVRKVF
     VSIKGVYYQA NVRGEEVRWL VPYKFPENIP SDVDFRIMLT FLEFYSTLLH FVLYKLYTDN
     GLVYPPKLDI KKNKLIGGIS AYILESKDAP FLSSVDGSAD SENQEVQVLD KKALRHAMKA
     DDKAGSEADE GDADSNEQVT NIELDDFEDK NKNHGDILEQ PSQYDSPTST LFSEFVFYIG
     REVPVDILEF LIVSCGGSVI SEAALDQADA ANVDVSKVTH QLVDRPVVKN KVAGRTYIQP
     QWVFDSINKG ELVPANLYLP GESLPPHLSP WGDSVGYDPA AELAEEEAES EEEEEVSDEA
     EGDEEATLAA EEDEEDEAEA EELRAQKELE LEAQGVTYSE AADSAAPSKK ASKQKKRKTE
     EEEEKDLKLI MMSNKQRKLF KKMKYSNQQK EQEIETLKQK KKQIAKTKAK LKKLEN
 
 
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