ID   PESC_ASPTN              Reviewed;         676 AA.
AC   Q0CLP9;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 73.
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=ATEG_05385;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476600; EAU34454.1; -; Genomic_DNA.
DR   RefSeq; XP_001214563.1; XM_001214563.1.
DR   AlphaFoldDB; Q0CLP9; -.
DR   SMR; Q0CLP9; -.
DR   STRING; 341663.Q0CLP9; -.
DR   EnsemblFungi; EAU34454; EAU34454; ATEG_05385.
DR   GeneID; 4321179; -.
DR   VEuPathDB; FungiDB:ATEG_05385; -.
DR   eggNOG; KOG2481; Eukaryota.
DR   HOGENOM; CLU_019619_1_1_1; -.
DR   OMA; TWIVPHY; -.
DR   OrthoDB; 777920at2759; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
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..676
FT                   /note="Pescadillo homolog"
FT                   /id="PRO_0000370482"
FT   DOMAIN          351..467
FT                   /note="BRCT"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03028"
FT   REGION          277..296
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          471..676
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          571..676
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03028"
FT   COMPBIAS        277..295
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        497..517
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        531..578
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        606..676
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   676 AA;  75945 MW;  67D43E70678B273A CRC64;
     MAKIKKKGTS GQAKNYITRT QAVRKLQISL PDFRRLCIFK GIYPREPRNK KKASKTSTPN
     TTFYYTKDIQ YLLHEPLLRK FRDQKAVAKK IARSLGRGEV GDASRLEKNH APKLTLDHII
     KERYPTFIDA LRDLDDALSL LFLFANLPST SHVPPKTIAL CQRLCHEFQH YLITTNSLRK
     SFLSIKGIYY QATIQGQDIM WLVPYRFVQR VNGDVDYRIM ATFVEFYTTL LGFVNFRLYS
     SIGLRYPPKF DTRSDENGAE LAAFTLEGRA VANAAKTIEG SNKQSNNSSN QEVSRDVQAK
     VDKVIKTAGL DKTKDEQTVE ATDENTDAID RFEPAAPEAD TLPQPDISGE EAGALFAPFT
     FYISREAPKA PLEFILRAFG CKRIGWDAVM GDGAFTHNEA DTRITHQIVD RPSLPEGALP
     AVPAAKEGAV PAVRPGTRIP GRTYIQPQWV WDCINEGKLL RPDLYAPGET LPPHLSPWVK
     PSKGAYDPRA TLAEQEEEGE AEMAGEEEEE ESDEEMEEAP ETKKADAKAD ESESEDEDES
     VDGGMDVADS DDDESESGQE EEDFGGFDDN EAASESEDEE EAARTQHQKE LEAEAAGLPF
     SSNGATDDAK KKKSSQAKKI AAKKRKEEEE LERQKMMMSR KKRKLLEKMM YSNKKQSEEA
     AKLRSKRRKL EKTGEK