PESC_AJECN
ID PESC_AJECN Reviewed; 723 AA.
AC A6RBB0;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 25-MAY-2022, entry version 62.
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 {ECO:0000255|HAMAP-Rule:MF_03028}; ORFNames=HCAG_06248;
OS Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma;
OC unclassified Histoplasma.
OX NCBI_TaxID=2059318;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAm1 / WU24;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(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=EDN10445.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CH476661; EDN10445.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_001538643.1; XM_001538593.1.
DR AlphaFoldDB; A6RBB0; -.
DR SMR; A6RBB0; -.
DR STRING; 339724.A6RBB0; -.
DR EnsemblFungi; EDN10445; EDN10445; HCAG_06248.
DR GeneID; 5444824; -.
DR KEGG; aje:HCAG_06248; -.
DR HOGENOM; CLU_019619_1_1_1; -.
DR OrthoDB; 777920at2759; -.
DR Proteomes; UP000009297; 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..723
FT /note="Pescadillo homolog"
FT /id="PRO_0000370476"
FT DOMAIN 380..497
FT /note="BRCT"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03028"
FT REGION 440..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 522..551
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03028"
FT COILED 656..723
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03028"
FT COMPBIAS 529..548
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..619
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..723
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 723 AA; 81815 MW; F7E512ADC8C298CC CRC64;
MAGRLREERK YRQKNRGLVQ ERIRLSLVVW ESRKQGTSGQ AKNFITRTQA VRKLQISLPD
FRRLCIFKGI YPREPRNKKK ASKAATPSTT FYYTRDIQYL LHEPLLKKFR EQKALSKKIA
RALGRGEVGN AARLEKNNAP KLSLDHIIKE RYPTFIDALR DLDDALSLLF LFANLPSTTS
VPAKTITLCQ RLCHEFQHYL IATNSLRKSF LSIKGIYYQA TILGQDIMWL VPYRFVQRVT
GDVDYRIMGT FVEFYTTLLG FVNYKLYTSI GLVYPPKFDK SSDERGAELA AFTLEGRYFG
EAHKAIETSR QPNGSAEKAA TTSKELQAKV DNILEKTQLD TDPTDQSTED QEENIEAIDK
FEPIAPEADS LPQPQISGDE AGSLFATFTF YISREAPRAP LEFLLRSFGC KRIGWDSVLG
DGAFTHDELD ARITHQIVDR PQLPQASLPP LPKNPEDGTE AAPRPGTRVP GRTYIQPQWV
WDCINEGKLL RPDLYAPGAT LPPHLSPWVK PSERGYDPRA SLADQEEEGE AERAAEAEEY
ENDEQEESGE ESTKSKQSKE LLANLARDSG DENTSGDESV NGGMDIAMAE DTDESSDDGD
GADKFEGFDQ DEDMSSESED EEEKARSQHQ KELEAEAAGL PFSASSQAES GTIRGKKQQA
PLAKKRAAQK KKEEEELERQ KMMMSRKKRK LLDKMIYSNK KQDAEAEKLR QKRRKIEQGL
NKK