CDC48_EMENI
ID CDC48_EMENI Reviewed; 823 AA.
AC Q5AWS6; C8VCV6;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Cell division control protein 48;
GN Name=cdc48; ORFNames=AN7254;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [3]
RP INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17258477; DOI=10.1016/j.fgb.2006.12.001;
RA Kim Y., Nandakumar M.P., Marten M.R.;
RT "Proteome map of Aspergillus nidulans during osmoadaptation.";
RL Fungal Genet. Biol. 44:886-895(2007).
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 -!- INDUCTION: Up-regulated when grown with elevated levels of potassium
CC chloride. {ECO:0000269|PubMed:17258477}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAA61160.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AACD01000124; EAA61160.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001304; CBF78760.1; -; Genomic_DNA.
DR RefSeq; XP_680523.1; XM_675431.1.
DR AlphaFoldDB; Q5AWS6; -.
DR SMR; Q5AWS6; -.
DR STRING; 162425.CADANIAP00000188; -.
DR PRIDE; Q5AWS6; -.
DR EnsemblFungi; EAA61160; EAA61160; AN7254.2.
DR GeneID; 2869922; -.
DR KEGG; ani:AN7254.2; -.
DR eggNOG; KOG0730; Eukaryota.
DR HOGENOM; CLU_000688_12_2_1; -.
DR InParanoid; Q5AWS6; -.
DR OrthoDB; 194195at2759; -.
DR Proteomes; UP000000560; Chromosome IV.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0034098; C:VCP-NPL4-UFD1 AAA ATPase complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IBA:GO_Central.
DR GO; GO:0097352; P:autophagosome maturation; IBA:GO_Central.
DR GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IBA:GO_Central.
DR GO; GO:0051228; P:mitotic spindle disassembly; IBA:GO_Central.
DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IBA:GO_Central.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR005938; AAA_ATPase_CDC48.
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; IPR004201; Cdc48_dom2.
DR InterPro; IPR029067; CDC48_domain_2-like_sf.
DR InterPro; IPR003338; CDC4_N-term_subdom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015415; Vps4_C.
DR Pfam; PF00004; AAA; 2.
DR Pfam; PF17862; AAA_lid_3; 2.
DR Pfam; PF02933; CDC48_2; 1.
DR Pfam; PF02359; CDC48_N; 1.
DR Pfam; PF09336; Vps4_C; 1.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01072; CDC48_2; 1.
DR SMART; SM01073; CDC48_N; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF54585; SSF54585; 1.
DR TIGRFAMs; TIGR01243; CDC48; 1.
DR PROSITE; PS00674; AAA; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Nucleotide-binding; Protein transport;
KW Reference proteome; Repeat; Stress response; Transport.
FT CHAIN 1..823
FT /note="Cell division control protein 48"
FT /id="PRO_0000348277"
FT REGION 729..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 799..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 268..274
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P55072"
FT BINDING 369
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P55072"
FT BINDING 405
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P55072"
SQ SEQUENCE 823 AA; 90541 MW; 326CF8350DD54E19 CRC64;
MSSEEHKKKL LYGVHFLQFL DASGAEKKEE LDTSTAILKK KKKPNSLIVT DAVNDDNSTI
SLSNNTMDTL GLFRGDTVTV RGKKRKETVL IVLADDDLDD GSARINRVVR HNLRVKHGDI
ITVHPCPDIK YAKRIAVLPI ADTVEGLTGS LFDVYLAPYF RDGYRPVKQG DLFTVRGGMR
QVEFKVVEVD PPEFGIVAPD TIIHSEGEPI QREDEENNLN EVGYDDIGGC RKQMAQIREL
VELPLRHPQL FKSIGIKPPR GILMYGPPGT GKTLMARAVA NETGAFFFLI NGPEIMSKMA
GESESNLRKA FEEAEKNSPA IIFIDEIDSI APKREKTNGE VERRVVSQLL TLMDGMKARS
NVVVMAATNR PNSIDPALRR FGRFDREVDI GIPDPTGRLE ILSIHTKNMK LGEDVDLETI
AAETHGYVGS DLASLCSEAA MQQIREKMDL IDLDEDTIDA EVLDSLGVTM ENFRYALGVS
NPSALREVAV VEVPNVRWED IGGLEEVKRE LIESVQYPVD HPEKFQKFGL SPSRGVLFYG
PPGTGKTMLA KAVANECAAN FISVKGPELL SMWFGESESN IRDIFDKARA AAPCVVFLDE
LDSIAKSRGG SVGDAGGASD RVVNQLLTEM DGMTSKKNVF VIGATNRPEQ LDAALVRPGR
LDTLVYVPLP DQASREGILK AQLRKTPVAS DVDIEFIASK THGFSGADLG FVTQRAVKLA
IKESISAEIE RQKQREAAGE DVKMEDEEEG EDPVPELTRA HFEEAMKTAR RSVSDVEIRR
YEAFAQSLKN SGGSSFFRFP SANEAADSGN TFGEAGNDDS LYD
