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Database: UniProt
Entry: V5GCV9_BYSSN
LinkDB: V5GCV9_BYSSN
Original site: V5GCV9_BYSSN 
ID   V5GCV9_BYSSN            Unreviewed;       794 AA.
AC   V5GCV9;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=Heat shock protein/chaperonin HSP78, putative {ECO:0000313|EMBL:GAD99871.1};
GN   ORFNames=PVAR5_8599 {ECO:0000313|EMBL:GAD99871.1};
OS   Byssochlamys spectabilis (strain No. 5 / NBRC 109023) (Paecilomyces
OS   variotii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX   NCBI_TaxID=1356009 {ECO:0000313|EMBL:GAD99871.1, ECO:0000313|Proteomes:UP000018001};
RN   [1] {ECO:0000313|Proteomes:UP000018001}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=No. 5 / NBRC 109023 {ECO:0000313|Proteomes:UP000018001};
RX   PubMed=24407650; DOI=10.1128/genomeA.01162-13;
RA   Oka T., Ekino K., Fukuda K., Nomura Y.;
RT   "Draft genome sequence of the formaldehyde-resistant fungus Byssochlamys
RT   spectabilis No. 5 (anamorph Paecilomyces variotii No. 5) (NBRC109023).";
RL   Genome Announc. 2:E0116213-E0116213(2014).
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:GAD99871.1}.
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DR   EMBL; BAUL01000333; GAD99871.1; -; Genomic_DNA.
DR   AlphaFoldDB; V5GCV9; -.
DR   eggNOG; KOG1051; Eukaryota.
DR   HOGENOM; CLU_005070_4_0_1; -.
DR   InParanoid; V5GCV9; -.
DR   OrthoDB; 35211at2759; -.
DR   Proteomes; UP000018001; 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:UP000018001};
KW   Stress response {ECO:0000313|EMBL:GAD99871.1}.
FT   DOMAIN          119..263
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          521..681
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          699..790
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   COILED          332..412
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   794 AA;  88174 MW;  E6809D77C1AB0A4C CRC64;
     MASRLQLGRG RLIRPSTLAS PDRLSIAQRP RFPAALAPRL LPYRRTVLPS ISSVRHYANG
     RPHPPGGTHR MNMSGEQEKP ALEQYGVDLT AKAKSGKLDP VIGRDAEIHR TIQVLSRRTK
     NNPVLIGAAG TGKTAILEGL AQRIVQGDVP ESIKNKRVIA LDLGSLIAGA KFRGDFEERL
     KAVLKEVEDA QGGVILFIDE LHTLLGLGKA EGSIDASNLL KPALSRGELQ CCGATTLNEY
     RMIEKDVALA RRFQPIQVGE PSVAATISIL RGIKNKYEVH HGVRITDAAL VAAATYSNRY
     ITDRFLPDKA IDLVDEAASA LRLQQESKPD AIQELDREIT TIQIELESLR KETDVTSRER
     REKLQETLKQ KQEEVGKLME VWNKEKAEIE EIKRTKEELE RARFELEQAQ REGNFAKAGE
     LRYSTIPSLE KKLPQEGSEV QTTTEGRQTL IHDSVTPDDI AAVVSRTTGI PVNKLMAGEV
     EKLIRMEDTL RQSVKGQDEA LSAVANAVRM QRAGLSGENK PLASFMFLGP TGVGKTELCK
     KMAGFLFSTE SAVLRFDMSE FQEKHTVSRL IGSPAGYVGY DDAGQLTEAV RRKPYAVLLF
     DEFEKAHRDI SALLLQVLDE GFLTDAQGHK VDFRNTIIVL TSNLGADILV GADPLHSYKD
     LDSGEVSPEI KKAVMDVVQA SYPPEFLNRI DEFIIFKRLS KEALRDIVDI RLRELQSRLD
     DRRMTLKVDD EIKDWLCEKG YDPRYGARPL NRLIAKEIGN RLADKIIRGE VVSGQTARVS
     FNADKSGLEV TSEA
//
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