ID A0A1A8ZT16_9APIC Unreviewed; 1199 AA.
AC A0A1A8ZT16;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=ATP-dependent Clp protease, putative {ECO:0000313|EMBL:SBT47021.1};
GN ORFNames=POVWA1_053820 {ECO:0000313|EMBL:SBT46434.1}, POVWA2_053080
GN {ECO:0000313|EMBL:SBT47021.1};
OS Plasmodium ovale wallikeri.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=864142 {ECO:0000313|EMBL:SBT47021.1, ECO:0000313|Proteomes:UP000078550};
RN [1] {ECO:0000313|Proteomes:UP000078550, ECO:0000313|Proteomes:UP000078555}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Naeem Raeece;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SBT47021.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lavstsen T., Jespersen J.S.;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FLRD01000139; SBT46434.1; -; Genomic_DNA.
DR EMBL; FLRE01000187; SBT47021.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1A8ZT16; -.
DR Proteomes; UP000078550; Unassembled WGS sequence.
DR Proteomes; UP000078555; 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; cd00009; AAA; 1.
DR CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR Gene3D; 1.10.8.60; -; 2.
DR Gene3D; 1.10.1780.10; Clp, N-terminal domain; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR036628; Clp_N_dom_sf.
DR InterPro; IPR004176; Clp_R_dom.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 78, MITOCHONDRIAL; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF81923; Double Clp-N motif; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51903; CLP_R; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000313|EMBL:SBT47021.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000313|EMBL:SBT47021.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000078555};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 76..356
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 235..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..765
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1199 AA; 138523 MW; 0CD9A70EDCDAB31E CRC64;
MYTYHTPCEV VTNQRSTVKQ TYRHTCEYSY RLSIHIRRKP HFLFNTNRVS KHRILEKMRN
YSRVKRRRNK LYGSIFDEYD EKCIKALIMA REVAKNDNKN EIMVKHILMA IIKIDFPRFE
HILKYLNVSV TQFLEKFNVE IKKKVQHEND SKEEDEEGNI SYNLNTKRIT DKNENKEYNL
KDTIDKMGKK IGDSIQEYNK EKEGKKILNE FIDKHIQNIE EKMILLKSLN EKDENMNSED
NFTDDAVKTK DINQSETNNK NQTSSHSKKY TNKISKENSD IKFSKNCKTL LQNALLEARK
KKRIFVSVTD ILISLINLSQ ESENSDFVNY LNEHNISISE LKKYLASYDD CESSGSKDSN
ENHNGSDSDS TTASSSENRR KADIENFRLG NQGNEHSGQL MHGLNNEYLN QGRELRNNEE
NNLIHNNNFV SSSFVKDCVV DMVKLAEEKT DDDFFGRKKE IQRIIEILGR KKKSNPLLIG
EAGVGKTAIV EQLSYLILKN KVPFHLKNCK IYQLNVGNIV AGTRYRGEFE EKMKFLLSNM
NKKKKNILFI DEIHIIIGAG SGEGSLDASN LLKPFLSSDN LQCIGATTFQ EYSKYIDRDK
ALRRRFNCVS IEPFTTKETY LLLKKIKHTY EKYHNVYYTN EALKSIIHLT DEYLPTSNFP
DKAIDILDEA GVYQKIKYEN FIRKKLRNER ISSMKIPSAA TLPIQAKKSQ GGVELQGGVE
PQGGVELQGG VEPQGGEELQ GGEEPQGGVK AEWDNSDELS KGEINGEEIV TDASSGMNSF
EERNKSGEKL AEEVNRTNLL RDLQMQYVTS DVIENIVSKK SSVSYIKKNK REEEKIVRLK
EKLSDVIIGQ EKVIDILSKY LFKAITNIKD PNKPIGTLLL CGTSGVGKTL CAQVISKYLF
NENNLILINM SEYIDKYAVT RLFGSYPGYI GYREGGELTE KVKKKPFSII LFDEIEKAHK
EVLNVLLQIL DNGVLTDSKG NTVSFKNSFI FMTTNVGADI ITDYFKLYNK NYSNLGFKYY
MKNKQSKGER DLNTSANRSS NDITIDSFEQ FEEKLRTNKW YEELQPEIEE ELKKQFLPEF
LNRIDEKIIF RQFLKRDIVN ILQNMIKDLK RRMKKRKNLN LIIDQDVIKH ICSDENNIYD
MNYGARSIRR ALYKYIEDPV ASFLVYNICE PNDSIRLTLT SDNKIDVHLV RTSISQLSS
//
