ERB1_MALGO
ID ERB1_MALGO Reviewed; 864 AA.
AC A8QD31;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Ribosome biogenesis protein ERB1 {ECO:0000255|HAMAP-Rule:MF_03027};
DE AltName: Full=Eukaryotic ribosome biogenesis protein 1 {ECO:0000255|HAMAP-Rule:MF_03027};
GN Name=ERB1 {ECO:0000255|HAMAP-Rule:MF_03027}; ORFNames=MGL_4099;
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_03027}.
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_03027}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000255|HAMAP-
CC Rule:MF_03027}. Nucleus, nucleoplasm {ECO:0000255|HAMAP-Rule:MF_03027}.
CC -!- SIMILARITY: Belongs to the WD repeat BOP1/ERB1 family.
CC {ECO:0000255|HAMAP-Rule:MF_03027}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDP41550.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AAYY01000020; EDP41550.1; ALT_FRAME; Genomic_DNA.
DR RefSeq; XP_001728764.1; XM_001728712.1.
DR AlphaFoldDB; A8QD31; -.
DR SMR; A8QD31; -.
DR STRING; 425265.A8QD31; -.
DR EnsemblFungi; EDP41550; EDP41550; MGL_4099.
DR GeneID; 5853105; -.
DR KEGG; mgl:MGL_4099; -.
DR InParanoid; A8QD31; -.
DR OrthoDB; 759498at2759; -.
DR Proteomes; UP000008837; Unassembled WGS sequence.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070545; C:PeBoW complex; IEA:EnsemblFungi.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IEA:UniProtKB-UniRule.
DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; IEA:EnsemblFungi.
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; 2.130.10.10; -; 1.
DR HAMAP; MF_03027; BOP1; 1.
DR InterPro; IPR028598; BOP1/Erb1.
DR InterPro; IPR012953; BOP1_N_dom.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR17605; PTHR17605; 1.
DR Pfam; PF08145; BOP1NT; 1.
DR Pfam; PF00400; WD40; 4.
DR SMART; SM01035; BOP1NT; 1.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 3: Inferred from homology;
KW Nucleus; Reference proteome; Repeat; Ribosome biogenesis; rRNA processing;
KW WD repeat.
FT CHAIN 1..864
FT /note="Ribosome biogenesis protein ERB1"
FT /id="PRO_0000370434"
FT REPEAT 509..549
FT /note="WD 1"
FT REPEAT 559..599
FT /note="WD 2"
FT REPEAT 694..732
FT /note="WD 3"
FT REPEAT 735..774
FT /note="WD 4"
FT REPEAT 778..817
FT /note="WD 5"
FT REPEAT 833..864
FT /note="WD 6"
FT REGION 1..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..71
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..151
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 864 AA; 97424 MW; DCC280A8ADCDCE32 CRC64;
MAVDKGRRPV PPERRAQGRK RAEPGDVTIR ETRTRPVHTP EPEPELLAKD GILELEDDDD
NDDDDDDDDD DKSNHHDGAP KNEDDMEAFP ELVSGKDKDD DGDEDEEEDD EDEDEDASDD
EAFDSDDLEN WDEEADAKYG DADLSDDDDV KEGDAALERM IARARVKPDE SERTTNKLGI
DTGVAARFYD ESRNDDGSKR GRVVQSHVTG MPKVEYPPIE PEYDSDSSTE DVPNRIGQVP
LSWYDDLPHI GYDINGRRVL RPAQGDELDK FLDSVEGEGD GWFSAHDKTS GQDVKLTDEE
LDIIQRLERA QIPVEAYDPY EPATDWFTQH QQTTPLTARP EPKRRFVPSK WEHKKIMKIV
RAIRQGRIVA HAPGRERPAF YNLWSDADEA RADHPMHMPA PKLPLPSHVE SYNPPAEYLF
GDDEKAEWEA AEPEDRKLPF LPAKYAALRL VPGYDQALHE RFQRCLDLYM APRMRRKRLD
IDDPDQLLPK LPAPRDLRPF PTHTDVVYAH APWRIRTVSI DPSGAWLLTG PDDGHVRLWD
AALGRCVATW DMNAGVARAD RSPVYCVQWC PNRTFGIAAA VSVGRVTLLA PPQCGKTMYE
ASLAHLTTPH AAEDAATAQW TRASEADRAA GVCVRIDVRN NKHASLVPKY VRWHARGDYF
ATVSPEAAGE AVLIHQVSKH RSQAPFRRTR RAGNSAMAVQ CVCFHPSRPW LFVATQRYVR
VYDLVQQSLV KTLQPGVRWI SSLDVHPSGD HVIIGSYDRR VLWFDLDLSE RPYKALRYHS
RAVRAVAYHP RFPLFASAAD DGTVHVYHGT VYSDLLQNAL LVPLKILRGH AVQDALGVLS
IAWHPTLPWL VSAGADGDAR LWTP