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Database: UniProt
Entry: A0A4U6XC81_9PEZI
LinkDB: A0A4U6XC81_9PEZI
Original site: A0A4U6XC81_9PEZI 
ID   A0A4U6XC81_9PEZI        Unreviewed;       786 AA.
AC   A0A4U6XC81;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Heat shock protein 78, mitochondrial {ECO:0000313|EMBL:TKW53195.1};
GN   Name=hsp78 {ECO:0000313|EMBL:TKW53195.1};
GN   ORFNames=CTA1_5783 {ECO:0000313|EMBL:TKW53195.1};
OS   Colletotrichum tanaceti.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum destructivum species complex.
OX   NCBI_TaxID=1306861 {ECO:0000313|EMBL:TKW53195.1, ECO:0000313|Proteomes:UP000310108};
RN   [1] {ECO:0000313|EMBL:TKW53195.1, ECO:0000313|Proteomes:UP000310108}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRIP57314 {ECO:0000313|EMBL:TKW53195.1};
RX   PubMed=31150449; DOI=10.1371/journal.pone.0212248;
RA   Lelwala R.V., Korhonen P.K., Young N.D., Scott J.B., Ades P.A.,
RA   Gasser R.B., Taylor P.W.J.;
RT   "Comparative genome analysis indicates high evolutionary potential of
RT   pathogenicity genes in Colletotrichum tanaceti.";
RL   PLoS ONE 14:e0212248-e0212248(2019).
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:TKW53195.1}.
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DR   EMBL; PJEX01000197; TKW53195.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4U6XC81; -.
DR   STRING; 1306861.A0A4U6XC81; -.
DR   Proteomes; UP000310108; 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:UP000310108};
KW   Stress response {ECO:0000313|EMBL:TKW53195.1}.
FT   DOMAIN          114..258
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          510..661
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          688..779
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          327..407
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   786 AA;  86805 MW;  A728C7A3671BC4A1 CRC64;
     MQARKQVISS ARRIVGSSSP RPTRLISRAI LTESAALKSS SRLLPTISIR TYANGRPHPS
     GGTHRMNMGG EPEKPALEQF GIDLTAKAKD GKLDPVIGRD AEIQRTIQIL SRRTKNNPVV
     IGKAGTGKTA ILEGLALRIV RGDVPESIKN KRVIALDLGS LIAGAKFRGD FEERLKKVLT
     EVQQAEGEVI LFIDELHTLL GLGKAEGSID ASNLLKPALA RGELQCCGAT TLEEYRLIEK
     DVALARRFQP IIVNEPTVQD TISILRGIKD KYEVHHGVRI TDGALVAAAT YSNRYITDRF
     LPDKAIDLMD EAASHLKLEH ESKPENIMAL DQKIMTIQIE LESLRKEKDV ASQERREKLQ
     TDLKKYEQEI SELTKRWEAE RAEIEAVKKT QEELDKARIE LDQAQREGNF GRASELRYSV
     IPSLEEKIPK EGEKAGDTLV HDAVTADDIA AVVSRVTGIP ISKLTSGHIE KLVHMEDTLR
     EAVRGQDEAI KAVSNAVRLQ RAGLSGENRP LASFFFLGPT GVGKTELCKK LAGFLFSTES
     AVVRFDMSEF QEKHTISRLI GAPSGYVGYE DAGQLTEAVR RKPYAVLLFD EFEKAHRDIS
     ALLLQVLDEG YLTDAQGHKV DFRNTIIVLT SNLGADILVG ANPSHPYKET ADGDIDPSVR
     KAVMDVVAAN YPPEFLNRID SFIVFKRLAL SALRDIVDIR LRELQHRLDD KRIVLNVGGE
     VRDWLAERGY DPKFGARPLN RLITNEIGNG LADKIIGGEL RSGDTAVVHI KEDDSGLEVA
     PEAKTA
//
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