PESC_PYRTR
ID PESC_PYRTR Reviewed; 679 AA.
AC B2WBA7;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 25-MAY-2022, entry version 46.
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; ORFNames=PTRG_06919;
OS Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS (Drechslera tritici-repentis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=426418;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pt-1C-BFP;
RX PubMed=23316438; DOI=10.1534/g3.112.004044;
RA Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT repentis, reveals transduplication and the impact of repeat elements on
RT pathogenicity and population divergence.";
RL G3 (Bethesda) 3:41-63(2013).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDU49839.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DS231621; EDU49839.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001937252.1; XM_001937217.1.
DR AlphaFoldDB; B2WBA7; -.
DR SMR; B2WBA7; -.
DR STRING; 45151.EDU49839; -.
DR GeneID; 6345188; -.
DR eggNOG; KOG2481; Eukaryota.
DR InParanoid; B2WBA7; -.
DR OrthoDB; 777920at2759; -.
DR Proteomes; UP000001471; 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 Coiled coil; Nucleus; Reference proteome; Ribosome biogenesis;
KW rRNA processing.
FT CHAIN 1..679
FT /note="Pescadillo homolog"
FT /id="PRO_0000370502"
FT DOMAIN 351..471
FT /note="BRCT"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03028"
FT REGION 413..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 573..679
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03028"
FT COMPBIAS 504..528
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..577
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..679
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 679 AA; 75743 MW; BA2D58AFA229D79F CRC64;
MHILTPTQAP LVPNPPHELM YTSSPLQISL PDFRRLCIFK GIYPPREPRN KKKVSKGSTA
ATTFYYTKDI QYLLHEPLLA KFREHKAVAK KIGRALGRGE SGDASRLEKN LMPKVKLDHI
IKERYPTFVD ALRDLDDALS MLFLFANLPS SDHIPAKTIA LCQRLTREFE HYVITSHSLR
KSFLSIKGIY YQATIQGQDI LWLVPYRFVQ RTGGDIDFRI MGTFVEFYTT LLGFVNYRLY
TSIGLVYPPK FNARSDEQGG ELAAFQLEGK ATATNGASNG HAEDAEINPE AQAIADRIGA
MPDVEEEEAT TAVAKTGAED DEEEANEEID KFEPTAPDAD ILPQPQASSA EVASLFAPFT
FYLSRETPRG SLEFILKAFG CKRVGWDGVL GDGAFTTNES DPAITHQIVD RPALSNGAPA
SNVQETENGG AAAPKAQWPY SMMPGRTYVQ PQWVWDSINQ GKLLRADHYS PGADLPPHLS
PWVKPKKGEY DPNLPLAAQQ PEGEAEAFED EGDEETAFDV DGDEDMEAIV DREGSVEVGE
GMDVADDSED DSDDDESDEE DGPAGDEDDL DSDAESDISE GEAARLQHQR ELEAEATGKK
LEVKKPTRKE ENATIRKKAE KKKRAEEEER ERQKMMLSNK KRKLLKRIEY GENKRDNESE
NLRRKRARVE KAKAAAEAV