ID A0A2A9MC09_9APIC Unreviewed; 930 AA.
AC A0A2A9MC09;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Putative heat shock protein {ECO:0000313|EMBL:PFH33203.1};
GN ORFNames=BESB_084020 {ECO:0000313|EMBL:PFH33203.1};
OS Besnoitia besnoiti.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Besnoitia.
OX NCBI_TaxID=94643 {ECO:0000313|EMBL:PFH33203.1, ECO:0000313|Proteomes:UP000224006};
RN [1] {ECO:0000313|EMBL:PFH33203.1, ECO:0000313|Proteomes:UP000224006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bb-Ger1 {ECO:0000313|EMBL:PFH33203.1,
RC ECO:0000313|Proteomes:UP000224006};
RA Schares G., Venepally P., Lorenzi H.A.;
RT "Genome sequencing of Besnoitia besnoiti strain Bb-Ger1.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|RuleBase:RU004432}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PFH33203.1}.
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; NWUJ01000009; PFH33203.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A9MC09; -.
DR STRING; 94643.A0A2A9MC09; -.
DR VEuPathDB; ToxoDB:BESB_084020; -.
DR OrthoDB; 35211at2759; -.
DR Proteomes; UP000224006; Chromosome viii.
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; -; 1.
DR Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
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; IPR028299; ClpA/B_CS2.
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.
DR PROSITE; PS00871; CLPAB_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000224006};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000313|EMBL:PFH33203.1}.
FT DOMAIN 3..145
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 875..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 470..524
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 898..924
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 930 AA; 104337 MW; D2FFA14594390C46 CRC64;
MDPESWTTLV KKAFLAGQEL CKERKNPQLD PAHVFDAMLR DKQSFATQVL TQSTGDFAQC
QEEVHKLVLK FPQQTPPPDF PSPNHAMMSV LRQAQDFQKQ MNDTHMSIDS LFLALVADKT
LKRAVTEAGF TLKQLEEKAK AVRGSRAVSS AEDDATFDAL KKYGVDFTDL AEKGKLDPVI
GREDEIRRVI RILCRRTKNN PVLIGEPGVG KSAVVEGLAR RIVEKDVPSS LHCRLISLDV
GALISGAKYR GEFEERLKAV LQEVRDAEGK VILFIDEIHT ILGAGKTDGA LDAANLLKPM
LARGELRCIG ATTLDEYRKY VEKDAAFERR FQQVHVHEPS VQATISILRG LKDRYATHHG
VRILDTALVE AAQLADRYIT TRFLPDKAID LMDEACAIAR VQVDSKPEAL DVLERQKVQL
EIEVLALEKE RDPASQKRLA EVKQHLATIE DDLRPLYLQY TQEKSRIDEL GKLAQKQDEL
KAKIERAQRM GDLDLVAELK YDALPGVEAR FKKLQQEQEE YERTHKPLLT EVVGPEQIAD
VVHRWTNIPV HKLTQSETDR LLSLRETLAE QVIGQSQAVE AVTQAILRSA AGLSKRNKPI
GSFLFLGPTG VGKTELCKRV AESLFDTKDR LVRLDMSEYM EQHSVSRLIG APPGYVGHDE
GGQLTEEIRR NPYSVVLFDE VEKAHAQVWN VLLQVLDDGR LTDSQGRTVD FSNTILILTS
NLGATYLLEA AQRAGTDEHA AAEAAAKEMV MMEVRKFFRP EMLNRLDDIV LFKALTNLNL
RQVMSLQMQD VRERLAEKRI DLVTTDRACD HVVHEAFDPA YGARPLKRFI ERHIVSELSL
KLLKGEVVAD SRVVCDWDPE ARKWLWTTTV VAPPTGAQST RKGPGLAADA DMDDGSLTPD
SRTLSIGSRT ESYTNRSSAM HTTNAKKFRY
//