ID A0A061DBN2_BABBI Unreviewed; 1008 AA.
AC A0A061DBN2;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 03-MAY-2023, entry version 36.
DE SubName: Full=Clp amino terminal domain containing protein, putative {ECO:0000313|EMBL:CDR97352.1};
GN ORFNames=BBBOND_0312550 {ECO:0000313|EMBL:CDR97352.1};
OS Babesia bigemina.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Babesiidae; Babesia.
OX NCBI_TaxID=5866 {ECO:0000313|EMBL:CDR97352.1, ECO:0000313|Proteomes:UP000033188};
RN [1] {ECO:0000313|Proteomes:UP000033188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bond {ECO:0000313|Proteomes:UP000033188};
RX PubMed=24799432; DOI=10.1093/nar/gku322;
RA Jackson A.P., Otto T.D., Darby A., Ramaprasad A., Xia D., Echaide I.E.,
RA Farber M., Gahlot S., Gamble J., Gupta D., Gupta Y., Jackson L.,
RA Malandrin L., Malas T.B., Moussa E., Nair M., Reid AJ., Sanders M.,
RA Sharma J., Tracey A., Quail M.A., Weir W., Wastling J.M., Hall N.,
RA Willadsen P., Lingelbach K., Shiels B., Tait A., Berriman M., Allred D.R.,
RA Pain A.;
RT "The evolutionary dynamics of variant antigen genes in Babesia reveal a
RT history of genomic innovation underlying host-parasite interaction.";
RL Nucleic Acids Res. 42:7113-7131(2014).
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DR EMBL; LK391709; CDR97352.1; -; Genomic_DNA.
DR RefSeq; XP_012769538.1; XM_012914084.1.
DR AlphaFoldDB; A0A061DBN2; -.
DR STRING; 5866.A0A061DBN2; -.
DR EnsemblProtists; CDR97352; CDR97352; BBBOND_0312550.
DR GeneID; 24565893; -.
DR KEGG; bbig:BBBOND_0312550; -.
DR VEuPathDB; PiroplasmaDB:BBBOND_0312550; -.
DR OMA; SCKRVFE; -.
DR OrthoDB; 275944at2759; -.
DR Proteomes; UP000033188; Chromosome 3.
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 Gene3D; 4.10.860.10; UVR domain; 1.
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; 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 104; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000033188};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 59..207
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 494..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 580..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1008 AA; 111414 MW; 8C5BFBEDE3B65E18 CRC64;
MKHRGQHITA EAFRNDATSS SCRRFGSLLP SSNIRRRCYS TGDSSGQARS PDKRALLNFN
NFSDNAVKVL MLSQEEARRA STTQIAARHI FQGLVCLDSG LAAHVLREFG VTVNTIRAAA
DNIFRVDTSN SNEALDTKLM TFSDEAKEAL ELSSVEAELL GHSAIETEHI LLGLLRCRSE
EVARLLNTLS LNPDEVRKLT LKYITEHKEK PEEVQQSDTW KQALSQYSYM PAQGRSVDVM
KETYTSPLAT FTVDITAKAE LGKLPKVLCR DAEIDRAIRT LCRKHKRNPI LIGEPGVGKT
AVIEGLAMQL LKGGATPSLR HKRLRQLDLG LLVAGARFRG QFEERLTKLI EEVKTMKDVI
LVIDEAHMLV GAGAGEGALD AANLFKPSLA RGEIQCVAIT TPKEYRKYFE KDAALSRRFQ
PIYVNEPTDE DTKTILNATT EEYGKYHKVS YNPEAVAAAL KFSKQFIQDR FLPDKAIDIL
DEAGALAKIR FHARTKSHQE DAGNSATTQD ANNERSQTET AANTTQSDSQ CSIDAGGMRG
AESNGSTTQE TNALSGISYG FAVKGDVDLQ QTGSAGNEGG MCATISDSDG ASGSSSSADS
YYTEDSELES DMAEQSPAAP VCEVNTEHVA EVVSTWTGIP LQRLSEDEIE GLRNMESELH
KRIIGHEEAV KHICKAIRRA KTNIKNPERP IGSFLFCGPP GVGKSEIAKA LTNLLFASEK
NIIKLDMSEY NEPHSISRIL GSPPGYKGHD SGGQLTEKLR KNPYSVVMFD EIEKAHPNVI
NILLQVLEDG KLTDSKNQTV SFKNAVIIMT SNTGSNVIER ASRGSHTFGF NIQDKPADES
KNYSEIKSLV CEELKSQFKP ELVDRIDDII IFRPLTDQQL RQISKLMIEE TLKRARDAGM
DIVVDDSFVD FVLKLPRDEK GGARPIRRLI TSNLEDKLAE FVINKDYEPG KRYRVAVDDQ
KHIVIRADND TGKVYQKEPP QPVSPIVITE DNVENPLCVL HTLNEVEV
//