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Database: UniProt
Entry: J4C485_THEOR
LinkDB: J4C485_THEOR
Original site: J4C485_THEOR 
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).
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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
//
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