CDC48_ENCCU
ID CDC48_ENCCU Reviewed; 780 AA.
AC Q8SSJ5;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Cell division control protein 48;
GN Name=CDC48; OrderedLocusNames=ECU01_1230;
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11157783; DOI=10.1101/gr.164301;
RA Peyret P., Katinka M.D., Duprat S., Duffieux F., Barbe V., Barbazanges M.,
RA Weissenbach J., Saurin W., Vivares C.P.;
RT "Sequence and analysis of chromosome I of the amitochondriate intracellular
RT parasite Encephalitozoon cuniculi (Microspora).";
RL Genome Res. 11:198-207(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP DEVELOPMENTAL STAGE.
RX PubMed=16691553; DOI=10.1002/pmic.200500796;
RA Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.;
RT "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi
RT (microsporidia): a reference map for proteins expressed in late sporogonial
RT stages.";
RL Proteomics 6:3625-3635(2006).
CC -!- FUNCTION: Involved in spindle disassembly, degradation of ubiquitinated
CC proteins and protein export from the endoplasmic reticulum to the
CC cytoplasm. Acts as a chaperone that collects ubiquitinated substrates.
CC Has a role in the endoplasmic reticulum-associated degradation (ERAD)
CC pathway. Component of the ribosome quality control complex (RQC), a
CC ribosome-associated complex that mediates ubiquitination and extraction
CC of incompletely synthesized nascent chains for proteasomal degradation.
CC CDC48 may provide the mechanical force that dislodges the
CC polyubiquitinated nascent peptides from the exit channel.
CC {ECO:0000250|UniProtKB:P25694}.
CC -!- SUBUNIT: Component of the ribosome quality control complex (RQC),
CC composed of the E3 ubiquitin ligase LTN1, RQC1 and RQC2, as well as
CC CDC48 and its ubiquitin-binding cofactors. RQC forms a stable complex
CC with 60S ribosomal subunits. {ECO:0000250|UniProtKB:P25694}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages.
CC {ECO:0000269|PubMed:16691553}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; AL391737; CAD24996.1; -; Genomic_DNA.
DR RefSeq; XP_965961.1; XM_960868.1.
DR AlphaFoldDB; Q8SSJ5; -.
DR SMR; Q8SSJ5; -.
DR STRING; 284813.Q8SSJ5; -.
DR PRIDE; Q8SSJ5; -.
DR GeneID; 860302; -.
DR KEGG; ecu:ECU01_1230; -.
DR VEuPathDB; MicrosporidiaDB:ECU01_1230; -.
DR HOGENOM; CLU_000688_12_3_1; -.
DR InParanoid; Q8SSJ5; -.
DR OMA; HACHDIK; -.
DR OrthoDB; 194195at2759; -.
DR Proteomes; UP000000819; Chromosome I.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR029067; CDC48_domain_2-like_sf.
DR InterPro; IPR003338; CDC4_N-term_subdom.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00004; AAA; 2.
DR Pfam; PF17862; AAA_lid_3; 2.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01073; CDC48_N; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF54585; SSF54585; 1.
DR PROSITE; PS00674; AAA; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Endoplasmic reticulum; Nucleotide-binding;
KW Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1..780
FT /note="Cell division control protein 48"
FT /id="PRO_0000382903"
FT BINDING 251..257
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P55072"
FT BINDING 352
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P55072"
FT BINDING 388
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P55072"
SQ SEQUENCE 780 AA; 87267 MW; C9D7E6FA78108128 CRC64;
MAAAANEKDF STAILESKTK NTLIVCDKDC SKLRTYQVGL HPTTLNELEL FESDYVRILG
KKKAELIFST VALESVPPRH IAIVRDGRFN LRIRITDTVK LYRVDKDIPV VSKLNFLPIK
DTVENIRGNI FDEFVRPFLD FNFMPLTTGS IYGVTSGLGR VEFKVTKMID AQDMEIKHGS
VTSTTSVYCD ETISREEVEK EFNMVGYDDV GGCRAQMAKI RELVELPLRH SQLYSKIGVK
PPKGILLYGP PGTGKTLIAR AIANETGAFL FLINGPEIMS KMAGESESNL RKAFEEAEKN
SPAIIFIDEI DALAPKREKS QGEVERRIVS QLLTLMDGMK ARSNVIVLGA TNRPNSIDPA
LRRYGRFDRE IEIGVPDETG RLEILRIHTK NMKMSEDVDL VAINKELHGF TGSDLASLCS
EAALQQIREK LPQIDLDSEK IDAKVLASLK VNSENFRYAI EHTDPSSLRE TVIQSPNVKW
SDIGGLEQVK QELRETVQYP VEYPEKFIKF GMTPAKGVLF YGPPGCGKTL LAKAVATECK
ANFISIKGPE LLSMWVGESE SNIRDLFARA RGAAPCVLFF DEIDSIAKAR SGNDGSSGAT
DRMLNQLLSE MDGINQKKNV FVIGATNRPD QLDSALMRPG RLDQLVYIPL PDLDSRVSIL
QATLKKTPLS PEIDLRQLAE ATDKFSGADL SEICQRACKL AIRETIEYEL EQKKKGSEMM
DLEDPVPYLR PDHLVQSLKT ARRSVSEKEV ERYEAFARSM KVDVRKFDKK NDINDDGLYE
