ID A0A3B0JRS0_DROGU Unreviewed; 685 AA.
AC A0A3B0JRS0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 28-JUN-2023, entry version 17.
DE SubName: Full=Blast:ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial {ECO:0000313|EMBL:SPP83693.1};
GN ORFNames=DGUA_6G016154 {ECO:0000313|EMBL:SPP83693.1};
OS Drosophila guanche (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7266 {ECO:0000313|EMBL:SPP83693.1, ECO:0000313|Proteomes:UP000268350};
RN [1] {ECO:0000313|Proteomes:UP000268350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Alioto T., Alioto T.;
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; OUUW01000008; SPP83693.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B0JRS0; -.
DR STRING; 7266.A0A3B0JRS0; -.
DR OMA; HRSDFTN; -.
DR OrthoDB; 452393at2759; -.
DR Proteomes; UP000268350; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd19497; RecA-like_ClpX; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR48102:SF7; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR48102; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000313|EMBL:SPP83693.1};
KW Hydrolase {ECO:0000313|EMBL:SPP83693.1};
KW Nucleotide-binding {ECO:0000313|EMBL:SPP83693.1};
KW Protease {ECO:0000313|EMBL:SPP83693.1}.
FT DOMAIN 326..478
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 546..637
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT REGION 82..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 685 AA; 72600 MW; E824581B8A3B8998 CRC64;
MSMVRRIILL GPKYSVWAKG GGVPTTQHTA KCVILSRRNA AAAEGAGPGV CGGRRFHLAT
HQCAANRQIV LEPVMNIPAY IDITNGTTQP PEDTSDSGSG GNSSASSGGT SKIPGAGSSA
GGASTTSGGD PPGGGDKFLS CPKCGSACTQ VETFVSSTRF VKCAKCNYFF VVLSEVETKQ
RVKDEPKNQR KPPPPPQKIM EYLDKHVVGQ DFAKKVLAVA VYNHYKRIHH NLPQLQQQQG
GGHGGQGGSG LDGIPRPDLL HITGIGHTLN STPGNELPPK PAQMGMGGGM GGGLGSSLGN
HSGRGGGDNR AGSEILDNKS TDVKLEKSNI IMLGPTGSGK TLIAQTIARC LDVPFAICDC
TTLTQAGYVG EDIESVISKL LQDANYNVDR AQTGIVFLDE VDKIGAVPGI HQLRDVGGEG
VQQGMLKMLE GTVVNVPERN SPRKLRGETV QVDTTNILFV ASGAYTGLDR LIGRRLNEKY
LGFGMPSSSS GSGNRRAVQS VAAPMDNDQE ERDKCLTKVQ ARDLVEFGMI PEFVGRFPVI
VPFHSLNVSM LVRILTEPRN ALVPQYKALL GLDEVDLTFD EDAVESIAKL AMERHTGARG
LRSIMEQLLL DPMFIVPGSD IRGVHITGEY VRGQSTPVYS RDTDATANSS SGAGSSSDSE
NTNDNDKNFE DSEKSFVNDT LAGTP
//