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Database: UniProt
Entry: A0A2P8A4D1_9PEZI
LinkDB: A0A2P8A4D1_9PEZI
Original site: A0A2P8A4D1_9PEZI 
ID   A0A2P8A4D1_9PEZI        Unreviewed;       731 AA.
AC   A0A2P8A4D1;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Hsp78-like protein {ECO:0000313|EMBL:PSK55321.1};
GN   ORFNames=B9Z65_2710 {ECO:0000313|EMBL:PSK55321.1};
OS   Elsinoe australis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Myriangiales; Elsinoaceae; Elsinoe.
OX   NCBI_TaxID=40998 {ECO:0000313|EMBL:PSK55321.1, ECO:0000313|Proteomes:UP000243723};
RN   [1] {ECO:0000313|EMBL:PSK55321.1, ECO:0000313|Proteomes:UP000243723}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NL1 {ECO:0000313|EMBL:PSK55321.1,
RC   ECO:0000313|Proteomes:UP000243723};
RA   Cheng Q.;
RT   "Draft genome sequence of Elsinoe australis.";
RL   Submitted (MAY-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:PSK55321.1}.
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DR   EMBL; NHZQ01000067; PSK55321.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P8A4D1; -.
DR   STRING; 40998.A0A2P8A4D1; -.
DR   Proteomes; UP000243723; 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; 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; 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:SF176; 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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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:UP000243723}.
FT   DOMAIN          49..192
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          465..618
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          636..725
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   REGION          363..392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          262..349
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        378..392
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   731 AA;  81028 MW;  137C7FFE5AB96495 CRC64;
     MNLGREEEKP ALEQYGVDLT ARAKDGKLDP VIGRDSEIHR TIQILSRRTK NNPVLIGNAG
     TGKTAILEGL AQRIVRGDVP ESIKEKRVIS LDLGQLIAGA KFRGDFEERL KKVLKEVEEA
     QGGVILFVDE LHILLGLGKA EGSIDASNLL KPALSRGELQ CCGATTLNEY RQIEKDVALA
     RRFQPIQVGE PTVQDTISIL RGIKDKYEVH HGVRITDGAL VAAATYSNRY ITDRFLPDKA
     IDLVDEAASA LRLQQESKPD AIQELDRSIM TIQIELESLR KETDIASRER RESLESSLKK
     KQEEVRVLTE RWERERAEIE EIKQAKQKLE DARTELEQVQ RQGDLARASE LRYSIIPELQ
     KKLPDEAPEK YPASSGSLAA PSGGSSTAAG SDTLVHDSVT ADDIANVVSR TTGIPVNKLM
     SGEVEKLIRM EDTLRQSVRG QDEALTSVAN AVRLQRAGLS GENRPLASFM FLGPTGTGKT
     ELCKKIAGFL FSTESAVVRF DMSEFQEKHT VSRLIGSPAG YVGYDDAGQL TEAIRRKPYA
     VLLFDEFEKA HKDISTLLLQ VLDDGFLTDA QGHKVDFRNT IIVLTSNLGA EALLMDESGS
     AEISARVKNE VMDVVQGSYP PEFLNRIDEF IVFKRLSREA LKDITDIRLK ELQSRLDDRR
     ITLNVPDDVK SWLCEKGYDP RYGARPLNRL IQKQIGNSLA DKIIRGQIKT GDTATVAIKE
     GGEALEVLDP K
//
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