ID J9DQJ9_EDHAE Unreviewed; 887 AA.
AC J9DQJ9;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=ATP-dependent chaperone ClpB {ECO:0008006|Google:ProtNLM};
GN ORFNames=EDEG_00977 {ECO:0000313|EMBL:EJW04840.1};
OS Edhazardia aedis (strain USNM 41457) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Edhazardia.
OX NCBI_TaxID=1003232 {ECO:0000313|EMBL:EJW04840.1, ECO:0000313|Proteomes:UP000003163};
RN [1] {ECO:0000313|EMBL:EJW04840.1, ECO:0000313|Proteomes:UP000003163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USNM 41457 {ECO:0000313|EMBL:EJW04840.1,
RC ECO:0000313|Proteomes:UP000003163};
RA Liu Z.J., Shi F.L., Lu J.Q., Li M., Wang Z.L.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000003163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USNM 41457 {ECO:0000313|Proteomes:UP000003163};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cuomo C.A., Sanscrainte N.D., Goldberg J.M., Heiman D., Young S., Zeng Q.,
RA Becnel J.J., Birren B.W.;
RT "Contrasting host-pathogen interactions and genome evolution in two
RT generalist and specialist microsporidian pathogens of mosquitoes.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675}.
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:EJW04840.1}.
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DR EMBL; AFBI03000013; EJW04840.1; -; Genomic_DNA.
DR AlphaFoldDB; J9DQJ9; -.
DR STRING; 1003232.J9DQJ9; -.
DR VEuPathDB; MicrosporidiaDB:EDEG_00977; -.
DR HOGENOM; CLU_005070_4_0_1; -.
DR InParanoid; J9DQJ9; -.
DR OMA; GRVIQEH; -.
DR OrthoDB; 35211at2759; -.
DR Proteomes; UP000003163; Unassembled WGS sequence.
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; 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 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; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00870; CLPAB_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000003163}.
FT DOMAIN 180..324
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 612..787
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 786..875
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT REGION 121..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 487..521
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 887 AA; 99314 MW; 6D626FFDE6460F23 CRC64;
MDIQFTKQAE EVLLKVVELA ESSTHSIIIP EHMVKVLIDD IPLDSVQKRE LLSEVNAELA
RVGISTTKPS YSQGYLSLIN SIPIIAKKFN DKYCSIDHIM LALCESPPNL KTFMKNLKEI
ESEVRRSKTP SDSRGEKKGD GELPAFAVEM VQLARDGKFD PVMGRENEIR SVIEILSKKT
KCNPILIGNP GVGKTAIVNE IATMIANNQL KTLEGYKIYS IDIGSIVAGT GVRGEFEERF
KRIIKEACSS PRVILFIDEI HMIVSAGSCG GSIDAANMLK PGLASGEIKC IGATTYYEYR
KYVEKDPALV RRFVRVNVGE PLMEDSITML RGLRERIEAF HGTRIMDQAI VAAVKMAKKY
VPGRMLPDSA IDLLDTACAS AVISVETEPQ EALRIRAKMW SLGLEKASLE LDFRRKIEAL
SQEDIEKYGL REVSGNKKGA FSPDLASSFP ELSADLSAIQ AKIASLNESL ETCKSSLRPI
EEQYRTKKEL LESRRSIQKR IDEYNNKYNE AVRNRDEYQA AEIKNHIVPN LQQALREIKF
STVTEINQNN IAEIVSRWTG IPVSRLNITE NERLLRMEER IRKKIFGQEN AVSHVCDAII
TNRTGLSEPN KPIGSFLFLG PTGVGKTELA KALCYEMFDN NQGVVIDMSD YSTEISVTKL
IGVSAGYVGY DEGGRLTEPV KNKPYNLVIF DEIDLAHPSV FNILYQLLDE GRVVDGKGAE
INFTNCVVIM TSNLGYKQSQ SMYNETKIDA HNYLVKLKKS AENEALNKFG PALINRIDAI
VHFNPLSIES TNYILDTQII KINERLAENN ITIQISDSAR AEILRNCVSE QFGARPLKKY
LQRNIVNALA KLILMNKDHK IPEIVLVNLD NKGVLIGDYF FQRTPIE
//
