PESC_ASPOR
ID PESC_ASPOR Reviewed; 681 AA.
AC Q2UGQ8;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 86.
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; ORFNames=AO090023000752;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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; AP007157; BAE59257.1; -; Genomic_DNA.
DR RefSeq; XP_001821259.1; XM_001821207.2.
DR AlphaFoldDB; Q2UGQ8; -.
DR SMR; Q2UGQ8; -.
DR STRING; 510516.Q2UGQ8; -.
DR EnsemblFungi; BAE59257; BAE59257; AO090023000752.
DR GeneID; 5993261; -.
DR KEGG; aor:AO090023000752; -.
DR VEuPathDB; FungiDB:AO090023000752; -.
DR HOGENOM; CLU_019619_1_1_1; -.
DR OMA; TWIVPHY; -.
DR Proteomes; UP000006564; Chromosome 3.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IEA:UniProtKB-UniRule.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; IEA:UniProtKB-UniRule.
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); IEA:UniProtKB-UniRule.
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; PF06732; Pescadillo_N; 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..681
FT /note="Pescadillo homolog"
FT /id="PRO_0000370481"
FT DOMAIN 350..469
FT /note="BRCT"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03028"
FT REGION 489..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 491..527
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03028"
FT COILED 574..681
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03028"
FT COMPBIAS 499..519
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..583
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..681
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 681 AA; 76305 MW; 0EE906647C1C844E CRC64;
MAKIKKKGTS GQAKNYITRT QAVRKLQISL PDFRRLCIFK GIYPREPRNK KKAAKNSTAS
TTFYYTKDIQ YLLHEPLLRK FRDQKALSKK IARSLGRGEV SDAARLEKNH APQLTLDHII
KERYPTFIDA LRDLDDALSL LFLFANLPST AHVPPKTIAL CQRLCHEFQH YLIVTNSLRK
SFLSIKGIYY QATIQGQDIM WLVPYRFVQR VNGDVDYRIM ATFVDFYTTL LGFVNFRLYS
TLGLRYPPKF DTRSDENGAE LAAFTLEGRA VGETTKAIEG TKQTSSTANK EVSQDVQAKV
DKVIKSAGLD QTKDDQAVQA TEESTEEIDK FEPAAPEADT LLQPDISGDT AGALFAPFTF
YISREAPKAP LEFILRSFGC KRIGWDAVLG DGAFTHDETD TRITHQIVDR PALPESSLPA
VPAASENGAG AVQKVKPGTR IPGRTYIQPQ WIWDCINEGK LLRPDLYAPG ATLPPHLSPW
VKPTRGAYDP RASLAEQEEE GEAEIAAEEE EEDSDEEMEE ATDGKKVDAK AEDSAEEENE
DEDDSVDGGM DVAGTDDDED ESEEEMEDEF GGFEEEAASE SEDEEESART QHQKELEAEA
AGLPFSSSSA GGDSTKKKSS QAKKVASKKR KEEEELERQK MMMSRKKRKL LEKMMYSNKK
QSEEAAKLRS KRRKLEKGAE K
