ID J4C485_THEOR Unreviewed; 895 AA.
AC J4C485;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Endopeptidase ATP-binding subunit {ECO:0000313|EMBL:BAM41746.1};
GN ORFNames=TOT_040000128 {ECO:0000313|EMBL:BAM41746.1};
OS Theileria orientalis strain Shintoku.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=869250 {ECO:0000313|EMBL:BAM41746.1, ECO:0000313|Proteomes:UP000003786};
RN [1] {ECO:0000313|EMBL:BAM41746.1, ECO:0000313|Proteomes:UP000003786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shintoku {ECO:0000313|EMBL:BAM41746.1,
RC ECO:0000313|Proteomes:UP000003786};
RX PubMed=22951932;
RA Hayashida K., Hara Y., Abe T., Yamasaki C., Toyoda A., Kosuge T.,
RA Suzuki Y., Sato Y., Kawashima S., Katayama T., Wakaguri H., Inoue N.,
RA Homma K., Tada-Umezaki M., Yagi Y., Fujii Y., Habara T., Kanehisa M.,
RA Watanabe H., Ito K., Gojobori T., Sugawara H., Imanishi T., Weir W.,
RA Gardner M., Pain A., Shiels B., Hattori M., Nene V., Sugimoto C.;
RT "Comparative genome analysis of three eukaryotic parasites with differing
RT abilities to transform leukocytes reveals key mediators of Theileria-
RT induced leukocyte transformation.";
RL MBio 3:e00204-e00212(2012).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP011949; BAM41746.1; -; Genomic_DNA.
DR RefSeq; XP_009692047.1; XM_009693752.1.
DR AlphaFoldDB; J4C485; -.
DR STRING; 869250.J4C485; -.
DR EnsemblProtists; BAM41746; BAM41746; TOT_040000128.
DR GeneID; 20716222; -.
DR KEGG; tot:TOT_040000128; -.
DR VEuPathDB; PiroplasmaDB:TOT_040000128; -.
DR eggNOG; KOG1051; Eukaryota.
DR OrthoDB; 275944at2759; -.
DR Proteomes; UP000003786; Chromosome 4.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; 1.
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; IPR018368; ClpA/B_CS1.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 104; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF02861; Clp_N; 2.
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; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51903; CLP_R; 1.
DR PROSITE; PS00870; CLPAB_1; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:BAM41746.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000003786};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 70..214
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 141..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..512
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 895 AA; 100313 MW; B454BBB85B4C1026 CRC64;
MKPMYSVINI LLIFQINIFV SVYRINCFKN FNGRSKISEQ FGFCKSSISQ SSTNSFHSHP
YRDSRLYLDF HNFSDNAIKV LMLSLEEARQ SKHPNVESSH IFQGLVCLSQ GLAFKVLKEF
GVTANSAREA TMSTFPIDES KRQRGIPTFS PSAKTALEHS SSEAERLGNS TIETEHLLLG
VLNDKSGEMA TFYKHLKLDV PLVIDTTIRT INKIKELNEA SVLNNSADEH TPNYVYLSPS
LKHDESSNTC LSQFTIDLTE KAKKGLLPKV IHRDNEIDRA IITLSRKTKS NPLLVGEPGV
GKTAIVEGIA NRISQGFTLP HMAEKRIVQL QFGLLIAGTK FRGQFEERLT KLIDEIITAG
NIILVIDEAH MLIGAGAGDG SIDAANLLKP ALSRGEIQCI AITTPKEYKK HFEKDMALSR
RFHTIYVDEP SDSDTLKILN GISSTYGEFH NVEYTPEAIN LASKLERMQR IEKQFSEIFE
AKREEETKED EESSRTYLEV NSEGDAPESK DPGNKRLILG QVKPEHVAEV MSIWTGIPLK
KLSRGEMEII RHMEDDIHKM VIGQDEAVKN VCKAIRRAKT NIKNPHRPIG SFLFCGPPGV
GKSEVARSLT KYLFAKENLI RIDMSEYKEP HSISRILGSP PGYKGHDTGG QLTEKVKNNP
YSVVMFDEIE KAHHDVLNIL LQILEDGKLT DAKNQTVSFK NTIIIMTSNT GSNVIQRSSK
GVHTFGFTVE KNDSSDYLKI KALVMEELKS HFLPELINRI DDVILFKPLS DEEMREIAKL
MLNELTSRAN AAGILIEIDN TFTEHILKLP RDDKCGARPL RRIITSVLED KLADLVISEN
FDSKTTYVVS VNKEGEVKIH PKEEFESYAS LGAQTIDFDA PGDIDHIPGD ENPDS
//