ERB1_CHATD
ID ERB1_CHATD Reviewed; 801 AA.
AC G0SCK6;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 25-MAY-2022, entry version 49.
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=CTHT_0057570;
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=759272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719;
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 433-801 IN COMPLEX WITH YTM1, AND
RP MUTAGENESIS OF ARG-486.
RX PubMed=26476442; DOI=10.1093/nar/gkv1043;
RA Wegrecki M., Rodriguez-Galan O., de la Cruz J., Bravo J.;
RT "The structure of Erb1-Ytm1 complex reveals the functional importance of a
RT high-affinity binding between two beta-propellers during the assembly of
RT large ribosomal subunits in eukaryotes.";
RL Nucleic Acids Res. 43:11017-11030(2015).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.67 ANGSTROMS) OF 423-801.
RX PubMed=26657628; DOI=10.1093/nar/gkv1365;
RA Thoms M., Ahmed Y.L., Maddi K., Hurt E., Sinning I.;
RT "Concerted removal of the Erb1-Ytm1 complex in ribosome biogenesis relies
RT on an elaborate interface.";
RL Nucleic Acids Res. 44:926-939(2016).
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; GL988045; EGS19132.1; -; Genomic_DNA.
DR RefSeq; XP_006696077.1; XM_006696014.1.
DR PDB; 5CXB; X-ray; 2.10 A; B=433-801.
DR PDB; 5CXC; X-ray; 3.10 A; B=433-801.
DR PDB; 5CYK; X-ray; 3.00 A; B=433-801.
DR PDB; 5EM2; X-ray; 2.67 A; A/C=423-801.
DR PDBsum; 5CXB; -.
DR PDBsum; 5CXC; -.
DR PDBsum; 5CYK; -.
DR PDBsum; 5EM2; -.
DR AlphaFoldDB; G0SCK6; -.
DR SMR; G0SCK6; -.
DR STRING; 759272.G0SCK6; -.
DR EnsemblFungi; EGS19132; EGS19132; CTHT_0057570.
DR GeneID; 18259795; -.
DR KEGG; cthr:CTHT_0057570; -.
DR eggNOG; KOG0650; Eukaryota.
DR HOGENOM; CLU_011390_0_1_1; -.
DR OrthoDB; 759498at2759; -.
DR Proteomes; UP000008066; 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; 2.
DR SMART; SM01035; BOP1NT; 1.
DR SMART; SM00320; WD40; 6.
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 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Nucleus; Reference proteome; Repeat;
KW Ribosome biogenesis; rRNA processing; WD repeat.
FT CHAIN 1..801
FT /note="Ribosome biogenesis protein ERB1"
FT /id="PRO_0000435843"
FT REPEAT 451..490
FT /note="WD 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03027"
FT REPEAT 494..534
FT /note="WD 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03027"
FT REPEAT 586..628
FT /note="WD 3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03027"
FT REPEAT 631..669
FT /note="WD 4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03027"
FT REPEAT 672..711
FT /note="WD 5"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03027"
FT REPEAT 715..755
FT /note="WD 6"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03027"
FT REPEAT 771..801
FT /note="WD 7"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03027"
FT REGION 1..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..86
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..377
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 486
FT /note="R->A: Weakens, but does not disrupt the interaction
FT with YTM1."
FT /evidence="ECO:0000269|PubMed:26476442"
FT MUTAGEN 486
FT /note="R->E: Disrupts the interaction with YTM1."
FT /evidence="ECO:0000269|PubMed:26476442"
FT HELIX 435..438
FT /evidence="ECO:0007829|PDB:5CXB"
FT STRAND 444..449
FT /evidence="ECO:0007829|PDB:5CXB"
FT STRAND 456..461
FT /evidence="ECO:0007829|PDB:5CXB"
FT STRAND 465..472
FT /evidence="ECO:0007829|PDB:5CXB"
FT STRAND 475..481
FT /evidence="ECO:0007829|PDB:5CXB"
FT TURN 482..484
FT /evidence="ECO:0007829|PDB:5CXB"
FT STRAND 487..493
FT /evidence="ECO:0007829|PDB:5CXB"
FT STRAND 495..497
FT /evidence="ECO:0007829|PDB:5EM2"
FT STRAND 499..504
FT /evidence="ECO:0007829|PDB:5CXB"
FT TURN 508..510
FT /evidence="ECO:0007829|PDB:5CYK"
FT STRAND 513..517
FT /evidence="ECO:0007829|PDB:5CXB"
FT STRAND 520..524
FT /evidence="ECO:0007829|PDB:5CXB"
FT HELIX 533..544
FT /evidence="ECO:0007829|PDB:5CXB"
FT TURN 545..548
FT /evidence="ECO:0007829|PDB:5EM2"
FT STRAND 568..570
FT /evidence="ECO:0007829|PDB:5CXB"
FT HELIX 574..578
FT /evidence="ECO:0007829|PDB:5CXB"
FT STRAND 581..586
FT /evidence="ECO:0007829|PDB:5CXB"
FT STRAND 593..596
FT /evidence="ECO:0007829|PDB:5CXB"
FT STRAND 600..606
FT /evidence="ECO:0007829|PDB:5CXB"
FT HELIX 608..610
FT /evidence="ECO:0007829|PDB:5CXB"
FT HELIX 611..613
FT /evidence="ECO:0007829|PDB:5EM2"
FT STRAND 615..619
FT /evidence="ECO:0007829|PDB:5CXB"
FT TURN 620..623
FT /evidence="ECO:0007829|PDB:5CXB"
FT STRAND 624..626
FT /evidence="ECO:0007829|PDB:5CXB"
FT STRAND 636..641
FT /evidence="ECO:0007829|PDB:5CXB"
FT STRAND 643..654
FT /evidence="ECO:0007829|PDB:5CXB"
FT STRAND 656..660
FT /evidence="ECO:0007829|PDB:5CXB"
FT TURN 661..664
FT /evidence="ECO:0007829|PDB:5CXB"
FT STRAND 667..670
FT /evidence="ECO:0007829|PDB:5CXB"
FT STRAND 675..682
FT /evidence="ECO:0007829|PDB:5CXB"
FT STRAND 686..693
FT /evidence="ECO:0007829|PDB:5CXB"
FT STRAND 698..702
FT /evidence="ECO:0007829|PDB:5CXB"
FT TURN 703..705
FT /evidence="ECO:0007829|PDB:5CXB"
FT STRAND 710..713
FT /evidence="ECO:0007829|PDB:5CXB"
FT STRAND 720..725
FT /evidence="ECO:0007829|PDB:5CXB"
FT STRAND 727..729
FT /evidence="ECO:0007829|PDB:5EM2"
FT STRAND 731..737
FT /evidence="ECO:0007829|PDB:5CXB"
FT STRAND 740..748
FT /evidence="ECO:0007829|PDB:5CXB"
FT STRAND 751..755
FT /evidence="ECO:0007829|PDB:5CXC"
FT STRAND 758..766
FT /evidence="ECO:0007829|PDB:5CXB"
FT STRAND 776..781
FT /evidence="ECO:0007829|PDB:5CXB"
FT STRAND 783..786
FT /evidence="ECO:0007829|PDB:5CXB"
FT STRAND 788..792
FT /evidence="ECO:0007829|PDB:5CXB"
FT STRAND 797..801
FT /evidence="ECO:0007829|PDB:5CXB"
SQ SEQUENCE 801 AA; 90721 MW; 728B27240CE0F620 CRC64;
MGSKIVEKKR KSRDSDSESD NELGDGLFDG VLSQSEDEED YIPSSEVDED DDDDADESAS
EDSDDSNDSE DDEVEEDDEA LLSDEIPSEG ESEKDQDLAE SKESKQDQDK EPSEPEILEP
FVDPPRKEDE ELEDRNYRIE KDANGGIRYV YDEIDPVYDS DDTDYNVPVN TIGNIPLSFY
DSYPHIGYDI NGKKIMRPAT GDALQNLLDS IEVPEGWTGL TDPNTGKPLN LSRDELELIR
KVQQGLIPDD VEDPYPDTVE WFTSVEEKMP LSAAPEPKRR FIPSKNEAKQ IMKLVRAIRE
GRILPYKPPE EREREELEKE EEFYDLWQNE EPQPPNPMHI PAPKLPPPGY DLSYNPPPEY
LPTKEEREEW EKMDPEDREK DYLPTKYDSL RKVPAWGNFV KERFERCMDL YLAPRVRKNR
LNIDPNSLLP KLPSPDELKP FPTVQQTIFR GHEGRVRSVA IDPTGVALAT GGDDGTVRVW
ELLTGRQVWS VKLNGDEAVN TVRWRPTKDT FILAAAAGED IFLMIPTHPS VTPALDQASR
DILNAGFGHA TNGKQQANLP PGKEPPGKWA RPGTRLEDEG VLLRITVRST IKAISWHRRG
DHFATVSPSG QRSSVAIHTL SKHLTQIPFR KLNGLAQTAS FHPLRPLFFV ATQRSIRCYD
LQKLELVKIV QPGAKWISSF DVHPGGDNLV VGSYDKRLLW HDLDLSNRPY KTMRFHTEAI
RAVRFHKGGL PLFADASDDG SLQIFHGKVP NDQLENPTIV PVKMLKGHKV VNKLGVLDID
WHPREPWCVS AGADGTARLW M
