ID A0A103Y8V7_CYNCS Unreviewed; 564 AA.
AC A0A103Y8V7;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 13-SEP-2023, entry version 24.
DE SubName: Full=AAA+ ATPase domain-containing protein {ECO:0000313|EMBL:KVI04662.1};
GN ORFNames=Ccrd_017021 {ECO:0000313|EMBL:KVI04662.1};
OS Cynara cardunculus var. scolymus (Globe artichoke) (Cynara scolymus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Carduoideae; Cardueae;
OC Carduinae; Cynara.
OX NCBI_TaxID=59895 {ECO:0000313|EMBL:KVI04662.1, ECO:0000313|Proteomes:UP000243975};
RN [1] {ECO:0000313|EMBL:KVI04662.1, ECO:0000313|Proteomes:UP000243975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2C {ECO:0000313|EMBL:KVI04662.1};
RX PubMed=26786968; DOI=10.1038/srep19427;
RA Scaglione D., Reyes-Chin-Wo S., Acquadro A., Froenicke L., Portis E.,
RA Beitel C., Tirone M., Mauro R., Lo Monaco A., Mauromicale G., Faccioli P.,
RA Cattivelli L., Rieseberg L., Michelmore R., Lanteri S.;
RT "The genome sequence of the outbreeding globe artichoke constructed de novo
RT incorporating a phase-aware low-pass sequencing strategy of F1 progeny.";
RL Sci. Rep. 6:19427-19427(2016).
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:KVI04662.1}.
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DR EMBL; LEKV01001944; KVI04662.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A103Y8V7; -.
DR STRING; 59895.A0A103Y8V7; -.
DR EnsemblPlants; KVI04662; KVI04662; Ccrd_017021.
DR Gramene; KVI04662; KVI04662; Ccrd_017021.
DR OMA; LTAPECC; -.
DR Proteomes; UP000243975; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:EnsemblPlants.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
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; IPR004487; Clp_protease_ATP-bd_su_ClpX.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00382; clpX; 1.
DR PANTHER; PTHR48102; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR48102:SF6; CLP PROTEASE REGULATORY SUBUNIT CLPX1, MITOCHONDRIAL; 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 Reference proteome {ECO:0000313|Proteomes:UP000243975}.
FT DOMAIN 218..370
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 419..509
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT REGION 127..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 564 AA; 60481 MW; C3E8D715195D37FE CRC64;
MAAAALRSKS SKATASLSSI SQFKYFILTH RMHAGRIPNF PITSSIPTTS KLDEYLPHYH
HQHQSFKPFS LPAEVVDKGC GFSKSSNNKR RLITLSGSGG YGDPPEVWQP PGDGIVPQPG
LKVVQVSGGD DPSTGGFGSD SGDGSWGGSS LGISFPTPKE ICKGLDKFVI GQDRAKKVLA
VAVYNHYKRI SIDSTKKPAG HSRNDKKNVM DEDAVELEKS NILLMGPTGS GKTLLAKTLA
RLVNVPFAGY VGEDVESILY KLLTVADYNV AAAQQGIVYI DEVDKITKKA ESVNISRDVS
GEGVQQALLK MLEGTVVNVP EKGARKHPRG DNIQIDTKDI LFICGGAFID LEKTISERRQ
DSSIGFGAPV RANMRTGGVT TASVTSSLLE TVESSDLIAY GLIPEFVGRF PILVSLLALT
EDQLVQVLTE PKNALGKQYK KLFQMNDVKL HYTESALRLI ARKAITKNTG ARGLRAILEN
ILMDAMYEIP DARTGKDIID AVVVDEEAVG VEGQGCGAKI LHGEGALDCY LSQHTVKDLE
MGVGRAADGG AEAEVEAELP SVAL
//