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Database: UniProt
Entry: A0A238FB22_9BASI
LinkDB: A0A238FB22_9BASI
Original site: A0A238FB22_9BASI 
ID   A0A238FB22_9BASI        Unreviewed;       703 AA.
AC   A0A238FB22;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   22-FEB-2023, entry version 17.
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=BQ2448_1799 {ECO:0000313|EMBL:SCV70405.1};
OS   Microbotryum intermedium.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX   NCBI_TaxID=269621 {ECO:0000313|EMBL:SCV70405.1, ECO:0000313|Proteomes:UP000198372};
RN   [1] {ECO:0000313|Proteomes:UP000198372}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Jeantristanb JTB J.-T., Ricardo R.;
RL   Submitted (SEP-2016) 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: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}.
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DR   EMBL; FMSP01000005; SCV70405.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A238FB22; -.
DR   STRING; 269621.A0A238FB22; -.
DR   OrthoDB; 169151at2759; -.
DR   Proteomes; UP000198372; 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; PF16589; BRCT_2; 1.
DR   Pfam; PF06732; Pescadillo_N; 2.
DR   SMART; SM00292; BRCT; 1.
DR   SUPFAM; SSF52113; BRCT domain; 1.
DR   PROSITE; PS50172; BRCT; 1.
PE   3: Inferred from homology;
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|HAMAP-Rule:MF_03028};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198372};
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          396..494
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   REGION          348..372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          508..589
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        534..566
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   703 AA;  78308 MW;  663C9904CEE46430 CRC64;
     MARITRAHNG MKKKGEAGAA KNYITRNQAI KKLQCTLSDF RRLCILKGIY PREPKSRKKA
     NKGSTIPASF YYAKDIQYLL HEPVLGKLRE HKAFAKKLSR AIGRGEWHLA KNLEESKPVY
     RLDHIIKERC DTRQAYPTFT DSLRDLDDAL CLIVLFASLP ATTTIPAAII SNCTQLAAQW
     QLYVMRTRSL RKVFLSIKGI YFQAEVQGQT VTWLVPYMFT QTVSYLGFAP KGTLWEGWWL
     RFDLLFSQIP SDLDYRIMLT FLELYQTLLG FVFYKLYTDI NLIYPPKLDQ VLDEHGAGIG
     ALLLEENGQG LVVVRDDAAQ APESIGTERR KPNAKDVRKQ IKQIGLGGNE AQPALEDDEQ
     RASAAASNDA SAAQELDVFP SNGAGDEALQ PEATSAATSL FEGYFFYLSR EVTRPTLEFV
     IRSLGGQVGW DAVLGAGSPF EENDVRITHH VVDRPVVAGA PPRSHPGKRA YIQPQWVVDC
     INRRTLLPTD QYAPGQVLPP HLSPFVDEDE VRERDGYVPM EARRIGGINT VDADMDAEQE
     EEEDEDEDDA EEGEGEDEEM DEDEGADEVA TKGKKGKKPA PALLAAAKDP KNAALLHAAE
     LEAESRGVEP AQFEAELASE TKKAKKDAAG AGGKVIKAPK KVLRSQEEQL ASIMLTGKQK
     KLYSKMVYSK DRRAEETAKL VARKRELEKK QQKRGIKGSQ VGL
//
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