ID A0A0R3RFL3_9BILA Unreviewed; 418 AA.
AC A0A0R3RFL3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=AAA domain-containing protein {ECO:0000313|WBParaSite:EEL_0000015601-mRNA-1};
OS Elaeophora elaphi.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Elaeophora.
OX NCBI_TaxID=1147741 {ECO:0000313|Proteomes:UP000050640, ECO:0000313|WBParaSite:EEL_0000015601-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:EEL_0000015601-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|ARBA:ARBA00006914, ECO:0000256|RuleBase:RU003651}.
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DR AlphaFoldDB; A0A0R3RFL3; -.
DR STRING; 1147741.A0A0R3RFL3; -.
DR WBParaSite; EEL_0000015601-mRNA-1; EEL_0000015601-mRNA-1; EEL_0000015601.
DR Proteomes; UP000050640; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032501; Prot_ATP_ID_OB_2nd.
DR PANTHER; PTHR23073; 26S PROTEASOME REGULATORY SUBUNIT; 1.
DR PANTHER; PTHR23073:SF7; 26S PROTEASOME REGULATORY SUBUNIT 6A; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF16450; Prot_ATP_ID_OB_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU003651};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942}.
FT DOMAIN 198..337
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 418 AA; 46788 MW; 767FB36FDA52DFE1 CRC64;
MTSTQGEQQT SKAGNDGTEK KEEKMEVEDQ PLDEEILRMS ADDLKSRTHL VENEIRIMRS
EIQRISHVID TLTSHVKENT ERIKVNKTLP YLVSNVVELL LLEELQEDEG ANVDLDAHKT
KCAVIKTSTR ATYFLPVVGL VDPSELKPGD LVGVNKVLTY FIWQYDIGGC DKQIQELIEA
VVLPMTHKDR FLNLGIHPPK GVLLYGPPGT GKTMMARAVA AQTKSTFLKL AGPQLVQMFI
GDGAKLVRDA FALAKEKAPA IIFIDELDAI GTKRFDSEKA GDREVQRTML ELLNQLDGFQ
PNDDIKVIAA TNRVDVLDPA LLRSGRLDRK IELPSPTEDA RARIMQIHSR KMNVHKDVNF
EELARCTDDF NGAQCKAVCV EAGMIALRRD AVEVMHEDFM DAILEVQAKK KASLYYYA
//
