ID   PESC_EMENI              Reviewed;         677 AA.
AC   Q5B6K3; C8V6R0;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   25-MAY-2022, entry version 90.
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=AN3827;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAA59092.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AACD01000062; EAA59092.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001302; CBF75294.1; -; Genomic_DNA.
DR   RefSeq; XP_661431.1; XM_656339.1.
DR   AlphaFoldDB; Q5B6K3; -.
DR   SMR; Q5B6K3; -.
DR   STRING; 162425.CADANIAP00004881; -.
DR   PRIDE; Q5B6K3; -.
DR   EnsemblFungi; CBF75294; CBF75294; ANIA_03827.
DR   EnsemblFungi; EAA59092; EAA59092; AN3827.2.
DR   GeneID; 2873249; -.
DR   KEGG; ani:AN3827.2; -.
DR   VEuPathDB; FungiDB:AN3827; -.
DR   eggNOG; KOG2481; Eukaryota.
DR   HOGENOM; CLU_019619_1_1_1; -.
DR   InParanoid; Q5B6K3; -.
DR   OMA; TWIVPHY; -.
DR   OrthoDB; 777920at2759; -.
DR   Proteomes; UP000000560; Chromosome II.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
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: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   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..677
FT                   /note="Pescadillo homolog"
FT                   /id="PRO_0000370491"
FT   DOMAIN          359..468
FT                   /note="BRCT"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03028"
FT   REGION          472..677
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          609..650
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03028"
FT   COMPBIAS        498..518
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        529..578
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        611..677
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   677 AA;  75554 MW;  6D1E2CE2E560C307 CRC64;
     MAKIKKKGTS GQAKNYITRT QAVRKLQISL PDFRRLCIFK GIYPREPRNK KKASKSATQS
     TTFYYTKDIQ YLLHEPLLRK FREQKALAKK IARSLGRGEV SDAARLEKNH APKLTLDHVI
     KERYPTFIDA LRDLDDALSL LFLFANLPST SHVPPKTIAL CQRVTHEFQH YLITTNSLRK
     SFLSIKGIYY QATIQGQDIM WLVPYRFVQR VNGDVDYRIM ATFVEFYTTL LGFVNYRLYS
     SIGLRYPPKF DTRLDENGAE LAAFTLEGRT VGDAPKAIEP AKSSSDAANQ EVSAEVQKKV
     DNVIKKAGLD QASSEQPTET AEEVTDAIDK FETTAPEADT LPQPDMSGDQ AGSLFAPFTF
     YISREAPKTP LEFILRAFGC KRIGWDTVLG GGAFTHNEAD PRITHQIVDR PSLPESSLPS
     IPAAATDGGA VQKVKPGTRV PGRTYVQPQW VWDCINEGKL LRPDLYAPGA TLPPHLSPWV
     NPKKGGYDPR ASLAEQEEDG EADIDAEEES DEEMEEAGEE KPAPTAANES EDSEDESVDG
     GMDVAETDDD DSESEEEEEE EDEFAGIDDE DAGSESEDEE ETARTQHQKE LEAEAAGLPF
     SSSGAGDDAA AKKKSQAKKR AAKKRQEEEE LERQKMMMSR KKRKLLEKMM YSNKKTAEES
     AKLRSKRRKI EKGAAGK