PESC_BOTFB
ID PESC_BOTFB Reviewed; 680 AA.
AC A6SK81;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 76.
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=BC1G_13323;
OS Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=332648;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B05.10;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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; CH476953; EDN19066.1; -; Genomic_DNA.
DR RefSeq; XP_001548387.1; XM_001548337.1.
DR AlphaFoldDB; A6SK81; -.
DR SMR; A6SK81; -.
DR GeneID; 5428842; -.
DR KEGG; bfu:BCIN_01g04710; -.
DR VEuPathDB; FungiDB:Bcin01g04710; -.
DR OMA; TWIVPHY; -.
DR OrthoDB; 777920at2759; -.
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; Ribosome biogenesis; rRNA processing.
FT CHAIN 1..680
FT /note="Pescadillo homolog"
FT /id="PRO_0000370483"
FT DOMAIN 359..476
FT /note="BRCT"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03028"
FT REGION 312..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 609..673
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03028"
FT COMPBIAS 312..329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..525
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..562
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..680
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 680 AA; 77009 MW; 89F340CEF8BFD611 CRC64;
MGRIKKKGTS GQAKNFITRT QAVRKLQISL PDFRKLCIWK GIYPREPRNK KKASKSSTHS
TTFYYTKDIQ WLLHEKIVDA FREQKALERK ISKALGRGDA SDAARLERNA SRPEKTGKTK
YNLDHIIRER YPTFIDALRD LDDCLSMLFL FANLPSTSTV PAKMIARCEK LCLEFEHYLI
VSNSLRKSFL SIKGIYYQAT IQGQDILWLV PYRFNQRVTG DVDFRIMGTF VEFYQTLLGF
VNFRLYTSVG LVYPPKFDAA RDDQDAGLGA FSLEGNGIGA IEQPKQITNG DASKPDPKLQ
AEIDKLMLQL NAPEKEVEET TKTSPDGEDE EQATETIDKF EPAAPGGDIL MQPSYSATDP
STLFSKFTFF LSRETPRQPL EFILRAFGCK RIGWDAVLGE GAFTHNESDP SITHQVVDRP
PVQVQPEEDE EVKEDNQTAQ RLRPGARVPG RIYIQPQWIW DCINDEELKR PDLYAPGAQL
PPHLSPFVKK VRGQYDPSAP LEDQEREDEE LEMDSGSEDE ADVSDEEAAV QKQDLVTAMD
VDETAEGMDV AGSDDESDEA PDKVDESFGG FSEAEDSEDE EETAALRRQR ELEAELSGVA
LQEKEVDPRA KAKTDAKKKA AKKAKEEDEE LERSKMMMSR KKRKILEKMV YSNKKKDAEA
EALRAKRRKI EKSGKAAPRE
