GenomeNet

Database: UniProt
Entry: W9INI7_FUSOX
LinkDB: W9INI7_FUSOX
Original site: W9INI7_FUSOX 
ID   W9INI7_FUSOX            Unreviewed;       797 AA.
AC   W9INI7;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Heat shock protein 78, mitochondrial {ECO:0000313|EMBL:EWY94086.1};
GN   ORFNames=FOYG_06976 {ECO:0000313|EMBL:EWY94086.1};
OS   Fusarium oxysporum NRRL 32931.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=660029 {ECO:0000313|EMBL:EWY94086.1, ECO:0000313|Proteomes:UP000030753};
RN   [1] {ECO:0000313|EMBL:EWY94086.1, ECO:0000313|Proteomes:UP000030753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FOSC 3-a {ECO:0000313|Proteomes:UP000030753};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA   Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusarium oxysporum FOSC 3-a.";
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; JH717842; EWY94086.1; -; Genomic_DNA.
DR   AlphaFoldDB; W9INI7; -.
DR   HOGENOM; CLU_005070_4_0_1; -.
DR   OrthoDB; 35211at2759; -.
DR   Proteomes; UP000030753; 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:UP000030753};
KW   Stress response {ECO:0000313|EMBL:EWY94086.1}.
FT   DOMAIN          121..265
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          521..661
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          699..788
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   COILED          334..414
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   797 AA;  88636 MW;  F5A1A576E3CB644E CRC64;
     MPSITVPNMQ ARKQIITSTQ RMAASARTRS VQPLTRVLAT QPLRPTSLRL IPSLAIRSYA
     NGRPHPPGGT HRMNMGGEEE KPALEQFGID LTARAKDGKL DPVIGRDAEI QRTIQILSRR
     TKNNPVLIGN AGTGKTAILE GLALRIVRGD VPESIKNKRV ISLDLGSLIA GAKFRGDFEE
     RLKKVLTEVE QAQGEVILFI DELHTLLGLG KAEGSIDASN LLKPALARGE LQCCGATTLN
     EYRQIEKDVA LARRFQPIIV SEPSVEDTIS ILRGIKDKYE VHHGVRITDG ALVAAATLSN
     RYITDRFLPD KAIDLMDEAA SHLKLQHESK PEDIMRLDHK IMTIQIELES LRKESDIASK
     ERREKLESDL KKLNEEISEL NARWEKERAE IESVKKIQED LDKAKFELEQ AQREGNFGRA
     SELRFGVIPN LEKKLPKEGE AKEAKSSDTL IHDSVSPDDI ANVVSRITGI PVSKLTSGHI
     EKLVHMEDSL REAVKGQDEA IKAVSNAVRL QRAGLSGENK PLASFFFLGP TGVGKTELCK
     KLAGFLFSTE SAVVRFDMSE FQEKHTISRL IGAPSGYVGY EDAGQLTEAV RRKPYAVLLF
     DEFEKAHRDI SALLLQVLDE GYLTDAQGHK VDFKNTIIVL TSNLGADILV GQNHLHPYTE
     TPDGEMDPSV RKAVMDVVAS AYPPEFLNRI DSFIIFKRLA RSAIRDIVDI RLKELQQRLD
     DRRIILSVPG DVRDWLAERG YDPKFGARPL NRLITNEIGN GLADQIIKGQ LKMGETAEVK
     IRDDREGLDI IIKSKDV
//
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