PESC_MALGO
ID PESC_MALGO Reviewed; 684 AA.
AC A8Q1F0;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
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=MGL_1778;
OS Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated
OS fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=425265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4612 / CBS 7966;
RX PubMed=18000048; DOI=10.1073/pnas.0706756104;
RA Xu J., Saunders C.W., Hu P., Grant R.A., Boekhout T., Kuramae E.E.,
RA Kronstad J.W., DeAngelis Y.M., Reeder N.L., Johnstone K.R., Leland M.,
RA Fieno A.M., Begley W.M., Sun Y., Lacey M.P., Chaudhary T., Keough T.,
RA Chu L., Sears R., Yuan B., Dawson T.L. Jr.;
RT "Dandruff-associated Malassezia genomes reveal convergent and divergent
RT virulence traits shared with plant and human fungal pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18730-18735(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; AAYY01000006; EDP43565.1; -; Genomic_DNA.
DR RefSeq; XP_001730779.1; XM_001730727.1.
DR AlphaFoldDB; A8Q1F0; -.
DR SMR; A8Q1F0; -.
DR STRING; 425265.A8Q1F0; -.
DR EnsemblFungi; EDP43565; EDP43565; MGL_1778.
DR GeneID; 5855086; -.
DR KEGG; mgl:MGL_1778; -.
DR VEuPathDB; FungiDB:MGL_1778; -.
DR InParanoid; A8Q1F0; -.
DR OMA; TWIVPHY; -.
DR OrthoDB; 777920at2759; -.
DR Proteomes; UP000008837; 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 Nucleus; Reference proteome; Ribosome biogenesis; rRNA processing.
FT CHAIN 1..684
FT /note="Pescadillo homolog"
FT /id="PRO_0000370496"
FT DOMAIN 387..486
FT /note="BRCT"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03028"
FT REGION 284..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 612..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..352
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..524
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..545
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..572
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..674
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 684 AA; 76672 MW; 72AA7DE257EE0061 CRC64;
MARIKKRGES GAAKNYITRN QSLKKLQITL AEFRRLCILK GIFPRQPRHV KRANKGSTAP
TTFYYTKDIA YLQHEPVLQA FRDHKAFAKK VNRAIARREW HAAKNLDENR PKYRLDHIIK
ERYPTFVDSL RDLDDALSTL FLFANIPSQK SMAPEITAHC ARLCAEWQLY VMRTHCLSKV
FLSIKGIYFQ AVVHGQEITW LVPYMFTQTI PTDVDFRVMM TFLELYQTLM GFVLFKLYTD
ENLVYPPKLD ESLDNQGAGF GSLMLMAADA DVLTGKHSLR PMDDAAAAEA SSNAITRKDG
KKLSTRDVKR QIAQLTRSED KAEHEPEDDE SMPALDATMQ DQDSDEEADD EAGAADAFVA
HASKTQGAGA DQLTTLRDLQ KQAGEDPLPM LFSRYVFYIS REVPRTVFEF ILRSFGASPS
NVGWDPVAGA GSQVAVDDER VTHHILDRPV DGMSLDHAGH RVYIQPQWVV DCVNARQILP
TDPYRPGQTL PPHLSPFVDD REVARKGGYV PEEAREKLGL EAEYVGGADE DEDEDEDEDE
DEDKAGSGRG DDKNVAAREQ DAVEKHDKTP ARPALEALLA DPTGAGLLEA AELEAEATGG
EDALLDLRAK HAASLKSHKK KKRTSTTQSP QLSEEAEARD MAKTLLSNKQ RKLYTRMGQA
TGKKKEEKMR LEAKKRALSK NKKP
