BOP1A_XENLA
ID BOP1A_XENLA Reviewed; 728 AA.
AC Q7T0W1;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Ribosome biogenesis protein bop1-A {ECO:0000255|HAMAP-Rule:MF_03027};
DE AltName: Full=Block of proliferation 1 protein A {ECO:0000255|HAMAP-Rule:MF_03027};
GN Name=bop1-a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the PeBoW complex, which is required for
CC maturation of 28S and 5.8S ribosomal RNAs and formation of the 60S
CC ribosome. {ECO:0000255|HAMAP-Rule:MF_03027}.
CC -!- SUBUNIT: Component of the PeBoW complex, composed of bop1, pes1 and
CC wdr12. The complex is held together by bop1, which interacts with pes1
CC via its N-terminal domain and with wdr12 via a high-affinity
CC interaction between the seven-bladed beta-propeller domains of the 2
CC proteins. The PeBoW complex associates with the 66S pre-ribosome.
CC {ECO:0000255|HAMAP-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; BC056015; AAH56015.1; -; mRNA.
DR RefSeq; NP_001079852.1; NM_001086383.1.
DR AlphaFoldDB; Q7T0W1; -.
DR SMR; Q7T0W1; -.
DR PRIDE; Q7T0W1; -.
DR DNASU; 379542; -.
DR GeneID; 379542; -.
DR KEGG; xla:379542; -.
DR CTD; 379542; -.
DR Xenbase; XB-GENE-6255479; bop1.S.
DR OrthoDB; 759498at2759; -.
DR Proteomes; UP000186698; Chromosome 6S.
DR Bgee; 379542; Expressed in oocyte and 19 other tissues.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070545; C:PeBoW complex; ISS:UniProtKB.
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); ISS:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
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; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 2: Evidence at transcript level;
KW Nucleus; Reference proteome; Repeat; Ribosome biogenesis; rRNA processing;
KW WD repeat.
FT CHAIN 1..728
FT /note="Ribosome biogenesis protein bop1-A"
FT /id="PRO_0000370388"
FT REPEAT 393..432
FT /note="WD 1"
FT REPEAT 434..474
FT /note="WD 2"
FT REPEAT 514..556
FT /note="WD 3"
FT REPEAT 559..597
FT /note="WD 4"
FT REPEAT 600..639
FT /note="WD 5"
FT REPEAT 643..682
FT /note="WD 6"
FT REPEAT 698..728
FT /note="WD 7"
FT REGION 1..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 728 AA; 83459 MW; 90373430ECBA6A8E CRC64;
MKRGSQGEAG SPQTEEPEPL FSEEDRSLRD GNALDESDSE ESQYSGLEDS GTDRSDDEED
HWSEEEENPG KSPKEIIKVP NRSSKSPADS AADEEDRPNE IKEYENDSSD EEDIRNTVGN
IPMEWYKDLP HIGYDLDGRK IFKPLRSKDQ LEEFLDKMEN PDYWRTIHDK KTGQDIKLTD
EQVDLVERLQ KGQFGDINYD PYQPAIDFFT HETMIHPVTN RPADKRSFIP SLIEKEKVSK
LVHAIKMGWI QPRKPREDTA TYYDLWAKED PNSILGRHKM HVPAPKLPLP GHEQSYNPPP
EYLMSEEERL SWEQQDPEDR KLPFLPQRFN CLRAVPGYAR FIHERFERCL DLYLCPRQRK
MRVNVDPEDL IPKLPKPRDL QPFPTIQSLI YKGHKDLVRC ISVSPSGQWL VSGSDDCSVR
FWEVSTGRCM KSVVLEGAVK SISWNPNPGL VLVAACVDRS VVLINPGLGD RLLCSATDQH
ISGYQPPEEE VQQPVTWEEV EGAQYSNGLR LCIKHQKEVK QVTFHARGDY FAVVLPDNGN
SQVLIHQLSR RRSQNPFRKN KGQVQKVLFH PTRPFFFVAT QRYVRVYNLL KQELTKKLLT
NCKWVSSIAV HPAGDNLICG SYDSKLAWFD MDLSTKPYKV LRHHKKALRA VSFHKSYPLF
ASGSDDGSVI VCHGMVYNDL LQNPLIVPVK VLRGHAIHRD LGVLDVTFHP TQPWVFSSGA
DATIRLFT