PESC_PHANO
ID PESC_PHANO Reviewed; 676 AA.
AC Q0V577;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 79.
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=SNOG_00837;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(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; CH445325; EAT92332.1; -; Genomic_DNA.
DR RefSeq; XP_001791508.1; XM_001791456.1.
DR AlphaFoldDB; Q0V577; -.
DR SMR; Q0V577; -.
DR STRING; 13684.SNOT_00837; -.
DR EnsemblFungi; SNOT_00837; SNOT_00837; SNOG_00837.
DR GeneID; 5968567; -.
DR KEGG; pno:SNOG_00837; -.
DR eggNOG; KOG2481; Eukaryota.
DR HOGENOM; CLU_019619_1_1_1; -.
DR InParanoid; Q0V577; -.
DR OMA; TWIVPHY; -.
DR OrthoDB; 777920at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070545; C:PeBoW complex; IBA:GO_Central.
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:0003723; F:RNA binding; IBA:GO_Central.
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); IBA:GO_Central.
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..676
FT /note="Pescadillo homolog"
FT /id="PRO_0000370499"
FT DOMAIN 351..466
FT /note="BRCT"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03028"
FT REGION 298..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 298..327
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03028"
FT COILED 568..676
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03028"
FT COMPBIAS 302..328
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..574
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..676
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 676 AA; 75588 MW; 4A0F459DAD139F4A CRC64;
MAGRSKKKGT SGAAKNYITR TRAVKKLQIS LPDFRRLCIF KGIYPREPRN KKKVSKGSTA
QTTFYYTKDI QYLLHEPLLA KFREHKSVAK KIGRALGRGE AGDAARLEKN LMPKVKLDHI
IKERYPTFVD ALRDLDDALS MLFLFANLPS SDHIPAKTIA LCQRLTREFE HYVITSHALR
KSFLSIKGIY YQATIQGQDI LWLVPYRFVQ RTGGDIDFRI MGTFVEFYTT LLGFVNYRLY
TSVGLVYPPK FNAKSDEQGG ELAAFQLEGK ANATNGASND HDDDVEINPE AQAKADKIAA
MADDEDEQEV EMAEADAEDD DEEENTEGID KFEPTAPDAD ILPQPQASSA EIASLFAPFT
FYLAREVPRA SLEFILKAFG CKRVGWDSIL GDGAFTTNES DPNITHQIVD RPPLANGASA
AGAEDAATPQ VQWPHSTKPG RTYVQPQWVW DCINQGKLLR PDLYAPGAEL PPHLSPWVKP
KKGEYDPNLP LAAQQPDGEA EAFEDLADED EDAFEVDDDE DMDAVADREG SVEVGEGMDV
ADSDDDDEDD SESDAEGGAD GFAGFDDESE AESDISEGEA ARLQHQRELE AEATGKKLDV
KAPTKKEQNA AIRKKFDKKK RAEEEERDRQ KMMLSNKKRK LLKRIEYGEN KRDTESENLR
RKRTRLEKAK AAAERA
