ID F9F702_FUSOF Unreviewed; 789 AA.
AC F9F702;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Heat shock protein 78, mitochondrial {ECO:0008006|Google:ProtNLM};
GN ORFNames=FOXB_02177 {ECO:0000313|EMBL:EGU87301.1};
OS Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU87301.1};
RN [1] {ECO:0000313|EMBL:EGU87301.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176 {ECO:0000313|EMBL:EGU87301.1};
RX PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT "A highly conserved effector in Fusarium oxysporum is required for full
RT virulence on Arabidopsis.";
RL Mol. Plant Microbe Interact. 25:180-190(2012).
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:EGU87301.1}.
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DR EMBL; AFQF01000695; EGU87301.1; -; Genomic_DNA.
DR AlphaFoldDB; F9F702; -.
DR STRING; 660025.F9F702; -.
DR PaxDb; 5507-FOXG_00378P0; -.
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}.
FT DOMAIN 113..257
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 513..653
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 691..782
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT COILED 326..406
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 789 AA; 87721 MW; 31DD3D3A631A1BE3 CRC64;
MQARKQIITS TQRIAASART RSVQPLTRVL ATQPLRPTSL RLIPSLAIRS YANGRPHPPG
GTHRMNMGGE EEKPALEQFG IDLTARAKDG KLDPVIGRDA EIQRTIQILS RRTKNNPVLI
GNAGTGKTAI LEGLALRIVR GDVPESIKNK RVISLDLGSL IAGAKFRGDF EERLKKVLTE
VEQAQGEVIL FIDELHTLLG LGKAEGSIDA SNLLKPALAR GELQCCGATT LNEYRQIEKD
VALARRFQPI IVSEPSVEDT ISILRGIKDK YEVHHGVRIT DGALVAAATL SNRYITDRFL
PDKAIDLMDE AASHLKLQHE SKPEDIMRLD HKIMTIQIEL ESLRKESDIA SKERREKLES
DLKKLNEEIS ELNARWEKER AEIESVKKIQ EDLDKAKFEL EQAQREGNFG RASELRFGVI
PNLEKKLPKE GEAKEAKSSD TLIHDSVSPD DIANVVSRIT GIPVSKLTSG HIEKLVHMED
SLREAVKGQD EAIKAVSNAV RLQRAGLSGE NKPLASFFFL GPTGVGKTEL CKKLAGFLFS
TESAVVRFDM SEFQEKHTIS RLIGAPSGYV GYEDAGQLTE AVRRKPYAVL LFDEFEKAHR
DISALLLQVL DEGYLTDAQG HKVDFKNTII VLTSNLGADI LVGQNHLHPY TETPDGEMDP
SVRKAVMDVV ASAYPPEFLN RIDSFIIFKR LARSAIRDIV DIRLKELQQR LDDRRIILSV
PGDVRDWLAE RGYDPKFGAR PLNRLITNEI GNGLADQIIK GQLKMGETAE VKIRDDKEGL
DIIIKSKDA
//
