PESC_YEAS7
ID PESC_YEAS7 Reviewed; 605 AA.
AC A6ZV85;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Pescadillo homolog {ECO:0000255|HAMAP-Rule:MF_03028};
DE AltName: Full=Nucleolar protein 7;
DE AltName: Full=Ribosomal RNA-processing protein 13;
GN Name=NOP7 {ECO:0000255|HAMAP-Rule:MF_03028}; Synonyms=RRP13, YPH1;
GN ORFNames=SCY_2318;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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; AAFW02000102; EDN61693.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZV85; -.
DR SMR; A6ZV85; -.
DR IntAct; A6ZV85; 2.
DR MINT; A6ZV85; -.
DR PRIDE; A6ZV85; -.
DR EnsemblFungi; EDN61693; EDN61693; SCY_2318.
DR HOGENOM; CLU_019619_1_1_1; -.
DR Proteomes; UP000007060; 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; PF16589; BRCT_2; 1.
DR Pfam; PF06732; Pescadillo_N; 1.
DR SMART; SM00292; BRCT; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR PROSITE; PS50172; BRCT; 1.
PE 3: Inferred from homology;
KW Coiled coil; Nucleus; Phosphoprotein; Ribosome biogenesis; rRNA processing.
FT CHAIN 1..605
FT /note="Pescadillo homolog"
FT /id="PRO_0000370506"
FT DOMAIN 355..449
FT /note="BRCT"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03028"
FT REGION 51..484
FT /note="Sufficient for interaction with ERB1"
FT /evidence="ECO:0000250"
FT REGION 297..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 294..342
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03028"
FT COILED 530..605
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03028"
FT COMPBIAS 310..340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..513
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..558
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..587
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53261"
FT MOD_RES 308
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P53261"
SQ SEQUENCE 605 AA; 69877 MW; 131001C956787BE5 CRC64;
MRIKKKNTRG NARNFITRSQ AVRKLQVSLA DFRRLCIFKG IYPREPRNKK KANKGSTAPT
TFYYAKDIQY LMHEPVLAKF REHKTFARKL TRALGRGEVS SAKRLEENRD SYTLDHIIKE
RYPSFPDAIR DIDDALNMLF LFSNLPSTNQ VSSKIINDAQ KICNQWLAYV AKERLVRKVF
VSIKGVYYQA NIKGEEVRWL VPFKFPENIP SDVDFRIMLT FLEFYSTLLH FVLYKLYTDS
GLIYPPKLDL KKDKIISGLS SYILESRQED SLLKLDPTEI EEDVKVESLD ASTLKSALNA
DEANTDETEK EEEQEKKQEK EQEKEQNEET ELDTFEDNNK NKGDILIQPS KYDSPVASLF
SAFVFYVSRE VPIDILEFLI LSCGGNVISE AAMDQIENKK DIDMSKVTHQ IVDRPVLKNK
VAGRTYIQPQ WIFDCINKGE LVPANKYLPG EALPPHLSPW GDAIGYDPTA PVEEGEEEES
ESESESEDQV EEEDQEVVAG EEDDDDDEEL QAQKELELEA QGIKYSETSE ADKDVNKSKN
KKRKVDEEEE EKKLKMIMMS NKQKKLYKKM KYSNAKKEEQ AENLKKKKKQ IAKQKAKLNK
LDSKK
