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Database: UniProt
Entry: A0A167CFD0_9HYPO
LinkDB: A0A167CFD0_9HYPO
Original site: A0A167CFD0_9HYPO 
ID   A0A167CFD0_9HYPO        Unreviewed;       656 AA.
AC   A0A167CFD0;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   22-FEB-2023, entry version 28.
DE   RecName: Full=Pescadillo homolog {ECO:0000256|HAMAP-Rule:MF_03028};
DE   AltName: Full=Nucleolar protein 7 homolog {ECO:0000256|HAMAP-Rule:MF_03028};
GN   Name=NOP7 {ECO:0000256|HAMAP-Rule:MF_03028};
GN   ORFNames=BBO_05675 {ECO:0000313|EMBL:OAA41139.1};
OS   Beauveria brongniartii RCEF 3172.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria;
OC   Beauveria brongniartii.
OX   NCBI_TaxID=1081107 {ECO:0000313|EMBL:OAA41139.1, ECO:0000313|Proteomes:UP000076863};
RN   [1] {ECO:0000313|EMBL:OAA41139.1, ECO:0000313|Proteomes:UP000076863}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCEF 3172 {ECO:0000313|EMBL:OAA41139.1,
RC   ECO:0000313|Proteomes:UP000076863};
RX   PubMed=27071652; DOI=10.1093/gbe/evw082;
RA   Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT   "Divergent and convergent evolution of fungal pathogenicity.";
RL   Genome Biol. Evol. 8:1374-1387(2016).
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:0000256|HAMAP-Rule:MF_03028}.
CC   -!- SUBUNIT: Component of the NOP7 complex, composed of ERB1, NOP7 and
CC       YTM1. Within the NOP7 complex ERB1 appears to interact directly with
CC       NOP7 and YTM1. The NOP7 complex also associates with the 66S pre-
CC       ribosome. {ECO:0000256|HAMAP-Rule:MF_03028}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000256|HAMAP-
CC       Rule:MF_03028}. Nucleus, nucleoplasm {ECO:0000256|HAMAP-Rule:MF_03028}.
CC   -!- SIMILARITY: Belongs to the pescadillo family. {ECO:0000256|HAMAP-
CC       Rule:MF_03028}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OAA41139.1}.
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DR   EMBL; AZHA01000017; OAA41139.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A167CFD0; -.
DR   OrthoDB; 169151at2759; -.
DR   Proteomes; UP000076863; 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   CDD; cd17709; BRCT_pescadillo_like; 1.
DR   Gene3D; 3.40.50.10190; BRCT domain; 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; PESCADILLO - RELATED; 1.
DR   PANTHER; PTHR12221:SF6; PESCADILLO HOMOLOG; 1.
DR   Pfam; PF00533; BRCT; 1.
DR   Pfam; PF06732; Pescadillo_N; 1.
DR   SMART; SM00292; BRCT; 1.
DR   SUPFAM; SSF52113; BRCT domain; 1.
DR   PROSITE; PS50172; BRCT; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|HAMAP-Rule:MF_03028};
KW   Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517, ECO:0000256|HAMAP-
KW   Rule:MF_03028};
KW   rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP-
KW   Rule:MF_03028}.
FT   DOMAIN          356..469
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   REGION          310..345
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          495..656
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        495..563
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        566..580
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        581..624
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        632..656
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   656 AA;  73794 MW;  1EE08AFDB0B3D31B CRC64;
     MARIKRRGET GASKNFVTRN QAIRKLQLSL PDFRKLCIWK GIYPREPRSK KKVSKSSTAS
     TTFYYHKDIQ YLLHEPLVQK FRDTKALEKK ISKALGRGDV GDAARLDSNA ARPEKTGKPN
     YTLDHVVRER YPTFVDALRD LDDCLSMLFL FANLPSTSTV PAKMIARCER LCLEFQHYLI
     VSRSLTKSFL SIKGIYYQAN IQGEEILWLV PYKFTQRVVG DVDFRIMGTF IEFYMTLLGF
     INFRLYTSVG LKYPPKFDLV KDENAAELGA FTLEGKTLVG GEEQKQLEDI AHRPDPNVQA
     AVNKVVKTLT SGETNGDGNE AAAEEDEEDN SGALDKFEPA APGGDVLLQP TAGAKGQGAL
     FSNFTFYLSR ETPRQPLEFI LKAFGCKRVG WDATLGDGAF TTNELDPAIT HHIVDRPIVP
     VEDVDGEDNQ TSQKLTQNQR VPGRIYVQPQ WVWDSINDGE LKEAHLYAPG ASLPPHLSPF
     VKNVQGAYDP TVPLEEQEPE NEALEADSDE EVGDADADET AEGMDIADED DEDTDEDDDA
     EDDEDVDEDE DKEDEEEDEA TQRQQELEAE MNGTSLDSKK VNAKTKAKAD ARKAYSKKSR
     EEAEDLERAK GMLSKKKRKL FEQMQYTNNK KSAADEKLRA KRRRLEKEKA KKEASA
//
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