ID A0A1D3TN22_9APIC Unreviewed; 1195 AA.
AC A0A1D3TN22;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=ATP-dependent Clp protease, putative {ECO:0000313|EMBL:SCP06343.1};
DE EC=3.4.21.92 {ECO:0000313|EMBL:SCP06343.1};
GN Name=ClpC {ECO:0000313|EMBL:SCP06343.1};
GN ORFNames=POCGH01_13053000 {ECO:0000313|EMBL:SCP06343.1};
OS Plasmodium ovale (malaria parasite P. ovale).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=36330 {ECO:0000313|EMBL:SCP06343.1, ECO:0000313|Proteomes:UP000242942};
RN [1] {ECO:0000313|EMBL:SCP06343.1, ECO:0000313|Proteomes:UP000242942}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PocGH01 {ECO:0000313|EMBL:SCP06343.1};
RG Pathogen Informatics;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; LT594594; SCP06343.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D3TN22; -.
DR VEuPathDB; PlasmoDB:PocGH01_13053000; -.
DR VEuPathDB; PlasmoDB:POWCR01_130049900; -.
DR Proteomes; UP000242942; Chromosome 13.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
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; 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.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000313|EMBL:SCP06343.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000313|EMBL:SCP06343.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000242942};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1195
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008921693"
FT DOMAIN 456..600
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 870..1009
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 1089..1183
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT REGION 237..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 763..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1195 AA; 137992 MW; B1094A92DDE1809B CRC64;
MNTLYIFVVI LILKIVVSIH IRTKPHFLFN TNQVSKHKIL EKMRNYSRVN RRRNKLYGSI
FDEYDEKCIK ALIMAREVAK NDNQNEIMVK HILMAIIKID FPRFEHILKY LNVSLTQFLE
KFNMEINKVK HENDIKEENE EGNISYNLNT KRITDKNEHK EKNWKHTIDK MDKKIGDSIQ
EYNKQKEGNK ILNDFIDKHI QNIEEKMILL KSLNEKDENM NSEDNFTDDA VKTKDINQSE
ANNKNQTSSH SKKNTNKISK ENSDIKFSKN CKTLLQNALL EARKKKRIFV SVTDILISLI
NLSQESENSD FVKYLNEHNI NINDLKKYLA SYDDCESSGS KDSNENHHGS DSDSTTASSS
ENQRKADIEN FRLGNQGNEH SGQLMHGLNN EYLNQGRELR NNEENNLIHN NNFVSSSFVK
DCVVDMVKLA EEKMDDDFFG RKKEIQRIIE ILGRKKKSNP LLIGEAGVGK TAIVEQLSYL
ILKNKVPFHL KNCRIYQLNV GNIVAGTRYR GEFEEKMKFL LSNMNKKKKN ILFIDEIHII
IGAGSGEGSL DASNLLKPFL SSDNLQCIGA TTFQEYSKYI DRDKALRRRF NCVSIEPFTT
KQTYLLLKKI KHTYEKYHNI YYTNDALKSI ILLTDEYLPT SNFPDKAIDI LDEAGVYQKI
KYENFIRKKL RNERISNMKI SSAATLSSQA KKSQGRVESE RRVETNGMVE ADGMVEADGR
VETNGMVEAD GMVEADGMVE ADGRVKAEWD NVDELSKGQI NEEEKVTDAS GGVNPFEDGN
QSKGKLAEEV NRINLLRDLQ MQYVTSDVIE NIVSKKSSVS YIKKNKREEE KIVRLKEKLS
NVIIGQEKVI DILSKYLFKA ITNIKDPNKP IGTLLLCGTS GVGKTLCAQV ICKYLFNENN
LILINMSEYI DKYAVTRLFG SYPGYIGYRE GGELTEKVKK KPFSIILFDE IEKAHKEVLN
VLLQILDNGV LTDSKGNTVS FKNTFIFMTT NVGADIITDY FKLYNKNYSN LGFKYYMKNK
QSKGERDINA SENGSSNGIT ADSFEQFEEK LRTNKWYEEL QPEIEEELRK QFLPEFLNRI
DEKIIFRQFL KRDIVNILQN MIKDLKRRMK KRKNLNLIID QDVIKHICSD ENNIYDMNYG
ARSIRRALYK YIEDPLASFL VYNICEPNDS IRLTLTSDKK IDVHLVRTPI SQLSS
//
