ID A0A443S2P8_9ACAR Unreviewed; 435 AA.
AC A0A443S2P8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Transitional endoplasmic reticulum ATPase-like protein {ECO:0000313|EMBL:RWS21795.1};
DE Flags: Fragment;
GN ORFNames=B4U80_03061 {ECO:0000313|EMBL:RWS21795.1};
OS Leptotrombidium deliense.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Trombidiformes; Prostigmata; Anystina; Parasitengona;
OC Trombiculoidea; Trombiculidae; Leptotrombidium.
OX NCBI_TaxID=299467 {ECO:0000313|EMBL:RWS21795.1, ECO:0000313|Proteomes:UP000288716};
RN [1] {ECO:0000313|EMBL:RWS21795.1, ECO:0000313|Proteomes:UP000288716}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UoL-UT {ECO:0000313|EMBL:RWS21795.1};
RA Dong X., Chaisiri K., Xia D., Armstrong S.D., Fang Y., Donnelly M.J.,
RA Kadowaki T., McGarry J.W., Darby A.C., Makepeace B.L.;
RT "Genomes of trombidid mites reveal novel predicted allergens and laterally-
RT transferred genes associated with secondary metabolism.";
RL Gigascience 0:0-0(2018).
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|RuleBase:RU003651}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RWS21795.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NCKV01010814; RWS21795.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A443S2P8; -.
DR STRING; 299467.A0A443S2P8; -.
DR EnsemblMetazoa; LDEU010245-RA; LDEU010245-PA; LDEU010245.
DR VEuPathDB; VectorBase:LDEU010245; -.
DR Proteomes; UP000288716; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd19528; RecA-like_CDC48_r2-like; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 6.10.20.150; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015415; Spast_Vps4_C.
DR PANTHER; PTHR23077; AAA-FAMILY ATPASE; 1.
DR PANTHER; PTHR23077:SF171; ATPASE FAMILY PROTEIN 2 HOMOLOG; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 2.
DR Pfam; PF09336; Vps4_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003651};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003651};
KW Reference proteome {ECO:0000313|Proteomes:UP000288716}.
FT DOMAIN 143..282
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 402..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RWS21795.1"
SQ SEQUENCE 435 AA; 48246 MW; AF7160D1EDF0E01E CRC64;
DIGIPDATGR LEILRIHTKN MKLADDVDLE RIAAETHGFV GADLAALCSE AALQQIREKM
DLIDLEDDQI DAEVLSSLAV TMENFKWALG KSSPSALRET VVEVPNVTWD DIGGLTNVKR
ELQEMVQYPV EFPDKFLKFG MTPSRGVLFY GPPGCGKTLL AKAIANECQA NFISIKGPEL
LTMWFGESEA NVRDVFDKAR AAAPCILFFD ELDSIAKARG GSVGDAGGAA DRVINQILTE
MDGMSSKKNV FIIGATNRPD IIDPAILRPG RLDQLIYIPL PDEKSRESIL KANLRKSPIA
KEVDLTFLAR VTNGFSGADL TEICQRACKL AIRESIEQEI KREKERRAKT DAAMDVEEPD
PVPNIRREHF EEAMKFARRS VSDNDIRKYE MFSQTLQQSR GFGTNFRFPA SQASTDNPGA
PNQGNFHEED DDLYS
//