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Database: UniProt
Entry: A0A0F4GXF5_9PEZI
LinkDB: A0A0F4GXF5_9PEZI
Original site: A0A0F4GXF5_9PEZI 
ID   A0A0F4GXF5_9PEZI        Unreviewed;       812 AA.
AC   A0A0F4GXF5;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Heat shock protein 78 {ECO:0000313|EMBL:KJY00901.1};
GN   ORFNames=TI39_contig307g00093 {ECO:0000313|EMBL:KJY00901.1};
OS   Zymoseptoria brevis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX   NCBI_TaxID=1047168 {ECO:0000313|EMBL:KJY00901.1, ECO:0000313|Proteomes:UP000033647};
RN   [1] {ECO:0000313|EMBL:KJY00901.1, ECO:0000313|Proteomes:UP000033647}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zb18110 {ECO:0000313|EMBL:KJY00901.1,
RC   ECO:0000313|Proteomes:UP000033647};
RA   Grandaubert J., Bhattacharyya A., Stukenbrock E.H.;
RT   "RNA-seq based gene annotation and comparative genomics of four
RT   Zymoseptoria species reveal species-specific pathogenicity related genes
RT   and transposable element activity.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|ARBA:ARBA00008675, 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:KJY00901.1}.
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DR   EMBL; LAFY01000299; KJY00901.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F4GXF5; -.
DR   STRING; 1047168.A0A0F4GXF5; -.
DR   OrthoDB; 35211at2759; -.
DR   Proteomes; UP000033647; 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: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; 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|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:UP000033647};
KW   Stress response {ECO:0000313|EMBL:KJY00901.1}.
FT   DOMAIN          144..288
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          546..718
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          717..808
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   COILED          357..444
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   812 AA;  90264 MW;  5D8227D82196B650 CRC64;
     MNIQTAARNR IDHLVFTVSI MLQHSGRGAA RRIASVRHPI PRFALRASGR LEANSTPTTF
     QRSILNSIQR SIPVATTQCR SYANGPPRPP GGTHRMNMSG DPEKPALEQY GVDLTARARD
     GKLDPVIGRD NEVHRTIQIL SRRTKNNPVL IGNAGTGKTA ILEGLAQRIV KGDCPESVKE
     KRVISLDLGS LIAGAKFRGD FEERLKSVLK EVEDAKGGVI LFVDELHTLL GLGKAEGSID
     ASNLLKPALS RGELQCCGAT TLNEYRQIEK DVALARRFQP IVVNEPTVQD TVSILRGIKE
     KYEVHHGVRI TDGALVAAAA YSNRYITDRF LPDKAIDLVD EAASALRLQQ ESKPDAIREL
     DRAIMTIQIE LESLRKETDI ASKERREQLE RQLTLKQDEV GALTEKWEQE RKELELIKQA
     KEELEQARID LDQAQREGNF ARASELRYAR IPELQKKLNE EESSETPSGE AKETLIHDSV
     TADDIALVVA KATGIPVTKL MAGELEKLIH LEDTLRQSVR GQDEALTAVA NAVRMQRAGL
     SGENRPLASF LFLGPTGVGK TELCKKLAGF LFSTESAVIR FDMSEFQEKH TVSRLIGSPA
     GYVGYDDAGQ LTEAVRRKPY AVLLFDEFEK AHKDISTLLL QVLDEGFLTD AQGRKVDFRN
     TMIVLTSNLG ASALLESADE NSEVSPDVKR QVLDIVTASF APEFINRIDE MIIFKRLSKE
     ALRDIVDIRL RELQARLDDR RIVLDVEDDV KTWLCEKAYD PRYGARPLNR LIQREVGNSL
     ADRIIRGQVK VGSRAKIVVD ETGEHLGVVE AE
//
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