ID A0A0A0AVD5_CHAVO Unreviewed; 802 AA.
AC A0A0A0AVD5;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Transitional endoplasmic reticulum ATPase {ECO:0000256|ARBA:ARBA00019970};
DE EC=3.6.4.6 {ECO:0000256|ARBA:ARBA00012674};
DE AltName: Full=Valosin-containing protein {ECO:0000256|ARBA:ARBA00031860};
DE Flags: Fragment;
GN ORFNames=N301_01046 {ECO:0000313|EMBL:KGL98524.1};
OS Charadrius vociferus (Killdeer) (Aegialitis vocifera).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Charadriiformes; Charadriidae; Charadrius.
OX NCBI_TaxID=50402 {ECO:0000313|EMBL:KGL98524.1, ECO:0000313|Proteomes:UP000053858};
RN [1] {ECO:0000313|EMBL:KGL98524.1, ECO:0000313|Proteomes:UP000053858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N301 {ECO:0000313|EMBL:KGL98524.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.6;
CC Evidence={ECO:0000256|ARBA:ARBA00000161};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000256|ARBA:ARBA00004240}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|ARBA:ARBA00006914}.
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DR EMBL; KL873369; KGL98524.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A0AVD5; -.
DR STRING; 50402.A0A0A0AVD5; -.
DR Proteomes; UP000053858; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0033554; P:cellular response to stress; IEA:UniProt.
DR CDD; cd19519; RecA-like_CDC48_r1-like; 1.
DR CDD; cd19528; RecA-like_CDC48_r2-like; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.10.330.10; -; 1.
DR Gene3D; 6.10.20.150; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR01243; CDC48; 1.
DR PANTHER; PTHR23077; AAA-FAMILY ATPASE; 1.
DR PANTHER; PTHR23077:SF69; TRANSITIONAL ENDOPLASMIC RETICULUM ATPASE; 1.
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 SMART; SM00382; AAA; 2.
DR SMART; SM01072; CDC48_2; 1.
DR SMART; SM01073; CDC48_N; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF54585; Cdc48 domain 2-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00674; AAA; 2.
PE 3: Inferred from homology;
KW Autophagy {ECO:0000256|ARBA:ARBA00023006};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Reference proteome {ECO:0000313|Proteomes:UP000053858}.
FT DOMAIN 21..104
FT /note="CDC48 N-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01073"
FT DOMAIN 121..187
FT /note="CDC48"
FT /evidence="ECO:0000259|SMART:SM01072"
FT DOMAIN 233..369
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 506..645
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 704..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 763..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..790
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KGL98524.1"
FT NON_TER 802
FT /evidence="ECO:0000313|EMBL:KGL98524.1"
SQ SEQUENCE 802 AA; 88964 MW; 4ABA9932049D4CC2 CRC64;
ASSKADDLST AILKQKNRPN RLIVDEAINE DNSVVSLSQA KMDELQLFRG DTVLLKGKKR
REAVCIVLSD DTCSDEKIRM NRVVRNNLRV RLGDVISIQP CPDVKYGKRI HVLPIDDTVE
GITGNLFEVY LKPYFLEAYR PIRKGDIFLV RGGMRAVEFK VVETDPSPYC IVAPDTVIHC
EGEPIKREDE EESLNEVGYD DIGGCRKQLA QIKEMVELPL RHPALFKAIG VKPPRGILLY
GPPGTGKTLI ARAVANETGA FFFLINGPEI MSKLAGESES NLRKAFEEAE KNAPAIIFID
ELDAIAPKRE KTHGEVERRI VSQLLTLMDG LKQRAHVIVM AATNRPNSID PALRRFGRFD
REVDIGIPDA TGRLEILQIH TKNMKLADDV DLEQVANETH GHVGADLAAL CSEAALQAIR
KKMDLIDLED ETIDAEVMNS LAVTMDDFRW ALSQSNPSAL RETVVEVPQV TWEDIGGLED
VKRELQELVQ YPVEHPDKFL KFGMTPSKGV LFYGPPGCGK TLLAKAIANE CQANFISIKG
PELLTMWFGE SEANVREIFD KARQAAPCVL FFDELDSIAK ARGGNIGDGG GAADRVINQI
LTEMDGMSTK KNVFIIGATN RPDIIDPAIL RPGRLDQLIY IPLPDEKSRV AILKANLRKS
PVAKDVDLDF LAKMTNGFSG ADLTEICQRA CKLAIRESIE SEIRRERERQ TNPSAMEVEE
DDPVPEIRRD HFEEAMRFAR RSVSDNDIRK YEMFAQTLQQ SRGFGSFRFP SGNQGGTGPS
QGTGGGSGGN VYSEDNDDDL YG
//
