ERB1_YEAS7
ID ERB1_YEAS7 Reviewed; 807 AA.
AC A6ZMA9;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 65.
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=SCY_4221;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(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}.
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DR EMBL; AAFW02000020; EDN64439.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZMA9; -.
DR SMR; A6ZMA9; -.
DR IntAct; A6ZMA9; 2.
DR MINT; A6ZMA9; -.
DR PRIDE; A6ZMA9; -.
DR EnsemblFungi; EDN64439; EDN64439; SCY_4221.
DR HOGENOM; CLU_011390_0_1_1; -.
DR Proteomes; UP000007060; 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; 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; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR17605; PTHR17605; 1.
DR Pfam; PF08145; BOP1NT; 1.
DR Pfam; PF00400; WD40; 3.
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; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 3: Inferred from homology;
KW Isopeptide bond; Nucleus; Phosphoprotein; Repeat; Ribosome biogenesis;
KW rRNA processing; Ubl conjugation; WD repeat.
FT CHAIN 1..807
FT /note="Ribosome biogenesis protein ERB1"
FT /id="PRO_0000370444"
FT REPEAT 435..474
FT /note="WD 1"
FT REPEAT 483..523
FT /note="WD 2"
FT REPEAT 592..634
FT /note="WD 3"
FT REPEAT 637..675
FT /note="WD 4"
FT REPEAT 678..717
FT /note="WD 5"
FT REPEAT 721..760
FT /note="WD 6"
FT REPEAT 776..807
FT /note="WD 7"
FT REGION 1..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..383
FT /note="Required for interaction with NOP7"
FT /evidence="ECO:0000250"
FT REGION 383..419
FT /note="Required for interaction with YTM1"
FT /evidence="ECO:0000250"
FT COMPBIAS 41..58
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..100
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04660"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04660"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04660"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04660"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04660"
FT MOD_RES 418
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04660"
FT CROSSLNK 127
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q04660"
SQ SEQUENCE 807 AA; 91703 MW; 5DA602CB016FF6FB CRC64;
MMAKNNKTTE AKMSKKRAAS EESDVEEDED KLLSVDGLID AEASESDEDD DEYESAVEEK
ESSSDKEAQD DSDDDSDAEL NKLLAEEEGD EEEDYDSSEF SDDTTSLTDR LSGVKLQTIV
DPNIYSKYAD GSDRIIKPEI NPVYDSDDSD AETQNTIGNI PLSAYDEMPH IGYDINGKRI
MRPAKGSALD QLLDSIELPE GWTGLLDKNS GSSLNLTKEE LELISKIQRN EQTDDSINPY
EPLIDWFTRH EEVMPLTAVP EPKRRFVPSK NEAKRVMKIV RAIREGRIIP PKKLKEMKEK
EKTENYQYDL WGDSTETNDH VMHLRAPKLP PPTNEESYNP PEEYLLSPEE KEAWENTEYS
ERERNFVPQK YSALRKVPGY GESIRERFER SLDLYLAPRV RKNKLNIDPN SLIPELPSPK
DLRPFPIRCS TIYAGHKGKV RTLSIDPSGL WLATGSDDGT VRVWEILTGR EVYRTTLIDD
EENPDDHIEC IEWNPDANNG ILAVAVGENI HLIVPPIFGY DIENNGKTKI EDGFGYDTFG
TVKKSNLEVN ENGDGDEDGE NESAKNAVKK QVAQWNKPSQ KQLEKDICIT ISCKKTVKKL
SWHRKGDYFV TVQPDSGNTS VLIHQVSKHL TQSPFKKSKG IIMDAKFHPF KPQLFVCSQR
YVRIYDLSQQ ILVKKLLPGA RWLSKIDIHP RGDNLIASSF DKRVLWHDLD LASTPYKTLR
YHEKAVRSVN FHKKLPLFSS AADDGTIHVF HATVYDDMMK NPMIVPLKKL TGHKVINSLG
VLDAIWHPRE AWLFSAGADN TARLWTT
