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Database: UniProt
Entry: A0A0A8L4W6_9SACH
LinkDB: A0A0A8L4W6_9SACH
Original site: A0A0A8L4W6_9SACH 
ID   A0A0A8L4W6_9SACH        Unreviewed;       603 AA.
AC   A0A0A8L4W6;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   22-FEB-2023, entry version 35.
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=KLDO_g2230 {ECO:0000313|EMBL:CDO93942.1};
OS   Kluyveromyces dobzhanskii CBS 2104.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=1427455 {ECO:0000313|EMBL:CDO93942.1, ECO:0000313|Proteomes:UP000031516};
RN   [1] {ECO:0000313|EMBL:CDO93942.1, ECO:0000313|Proteomes:UP000031516}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS2104 {ECO:0000313|Proteomes:UP000031516};
RA   Nystedt B., Astrom S.;
RT   "The genome of Kluyveromyces dobzhanskii.";
RL   Submitted (MAR-2014) 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}.
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:CDO93942.1}.
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DR   EMBL; CCBQ010000027; CDO93942.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A8L4W6; -.
DR   OrthoDB; 169151at2759; -.
DR   Proteomes; UP000031516; 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; 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          346..440
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   REGION          300..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          443..603
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        459..508
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        528..558
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        570..603
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   603 AA;  69231 MW;  C370886F441B83D8 CRC64;
     MRIKKRNTRG NARNFITRSQ AVRKLQISLA DFRRLCIFKG IYPREPRNKK KANKGSTAPT
     TFYYYKDIQY LMHEPVLAKF REHKTFSKKL TKALGRGEVS AAKRLEENRP NYELDHIIKE
     RYPSFADALR DVDDALNMLF LFANLPATDQ VSSRITQSAQ QLCNQWAAYI AKERCVRKVF
     VSIKGVYYQA SVKGEDVRWL VPYKFPENIP SDVDFRIMLT FLEFYSTLLH FVLFRLYVDS
     GLVYPPKLDT KKNKLIGGLS AYILESNDEK SSLALHPKEI SEDAAVQELG AKALKTALNA
     DSKKHDEEEE DQEDQEDVED VELDRFEDNN KNQGDLLEQP SKFDSPTATL FSDFVFYVGR
     EVPLDIVEFL ILSCGGSVVS EATLDQIADK KDIDLSKVTH QIVDRPVLKN KVANRTYIQP
     QWIFDSINKV ELVPANLYLP GEPLPPHLSP WGDATGYDPT AEDDQEDEDS EEEDVDESAD
     EAVDIDEESA EAIALNEDDD EDEDELRQQK ELELEAQGVS YSEGKDTIQG EGSEKKAKKN
     KRKATEEEEE KDLKLIMMSN KQRKLYKKMK YSNEKKDEKI EQLKQKKKQI AKTKSKLAKL
     DKK
//
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