PESC_DEBHA
ID PESC_DEBHA Reviewed; 600 AA.
AC Q6BXL7;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 91.
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};
GN OrderedLocusNames=DEHA2B01958g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382134; CAG85038.1; -; Genomic_DNA.
DR RefSeq; XP_457052.1; XM_457052.1.
DR AlphaFoldDB; Q6BXL7; -.
DR SMR; Q6BXL7; -.
DR STRING; 4959.XP_457052.1; -.
DR PRIDE; Q6BXL7; -.
DR EnsemblFungi; CAG85038; CAG85038; DEHA2B01958g.
DR GeneID; 2913744; -.
DR KEGG; dha:DEHA2B01958g; -.
DR VEuPathDB; FungiDB:DEHA2B01958g; -.
DR eggNOG; KOG2481; Eukaryota.
DR HOGENOM; CLU_019619_1_1_1; -.
DR InParanoid; Q6BXL7; -.
DR OMA; TWIVPHY; -.
DR OrthoDB; 777920at2759; -.
DR Proteomes; UP000000599; Chromosome B.
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; Reference proteome; Ribosome biogenesis;
KW rRNA processing.
FT CHAIN 1..600
FT /note="Pescadillo homolog"
FT /id="PRO_0000370490"
FT DOMAIN 351..450
FT /note="BRCT"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03028"
FT REGION 454..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 478..600
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03028"
FT COMPBIAS 476..512
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..555
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..600
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 600 AA; 68400 MW; 028055D2B9277B42 CRC64;
MRIKKKGTSG NAKNFITRTQ AVKKLQVSLA DFRRLCIFKG IYPREPRNKK KANKGSTAPV
TFYYTKDIQY LLHEPVLGKF REHKTFAKKL QRALGRGEVS DAQKLEGNRP KYTLEHIIKE
RYPTFLDALR DIDDPLNMLF LFANMPATDK VSHRITKEAE KLTNQWLAYV AKERLIKKVF
VSIKGVYYQA NVKGQEVRWL VPFKFPTNIP TDVDFRIMLT FLEFYSTLLH FVLFRLYNDA
NLIYPPTIDT EKLKGIGGLS SYVLQSKDQG VKALLPNAKK AADSKDESKK VKETKLSKEE
ISKAVAADKS LNENAEDNVS ENVEDVELDE FSSTNKTAGD LLSQPSKFAS PTSTLLSKFI
FYVGREVPLD ILEFCILSCG GSIISEIALD ELQLNQPEEY KKLDLSNITH QIVDRPTVAS
KVAGRTYVQP QWVFDCLNKS ELLPVSQYAP GETLPPHLSP WGDAGGYNPD AEVKPTEQGE
EEEEEEEEIE GDEIEEDVEE EDEEEDEDLQ AQKELELEAA GVKSADAQKK DKKSSKGKKR
SAEDEEKDLK KIMMSNKQRK LYKKMQYGID KKEARQDDLT KKRRKLEKTK AELGKLNKKN
