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Database: UniProt
Entry: A0A4U0UTC7_9PEZI
LinkDB: A0A4U0UTC7_9PEZI
Original site: A0A4U0UTC7_9PEZI 
ID   A0A4U0UTC7_9PEZI        Unreviewed;       813 AA.
AC   A0A4U0UTC7;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Heat shock protein 78, mitochondrial {ECO:0000313|EMBL:TKA39244.1};
GN   ORFNames=B0A54_08553 {ECO:0000313|EMBL:TKA39244.1};
OS   Friedmanniomyces endolithicus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Friedmanniomyces.
OX   NCBI_TaxID=329885 {ECO:0000313|EMBL:TKA39244.1, ECO:0000313|Proteomes:UP000310066};
RN   [1] {ECO:0000313|EMBL:TKA39244.1, ECO:0000313|Proteomes:UP000310066}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCFEE 5311 {ECO:0000313|EMBL:TKA39244.1,
RC   ECO:0000313|Proteomes:UP000310066};
RA   Coleine C., Masonjones S., Stajich J.E.;
RT   "Genomes of endolithic fungi from Antarctica.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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:TKA39244.1}.
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DR   EMBL; NAJP01000040; TKA39244.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4U0UTC7; -.
DR   STRING; 329885.A0A4U0UTC7; -.
DR   Proteomes; UP000310066; 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:UP000310066};
KW   Stress response {ECO:0000313|EMBL:TKA39244.1}.
FT   DOMAIN          139..282
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          543..701
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          719..808
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          450..471
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          352..432
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        457..471
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   813 AA;  89350 MW;  4FE0139D6165B3E2 CRC64;
     MSSATGRSAA RRIAGTRYTL PRQASRAPLS ALGPPAAFPY ALPQQVSRVP VSVLRSPASL
     PPVHHVLAPA ISHRRGYASS RPHPPGGTHR MNLGGEPEKS ALEQYGIDLT AKAKSGRLDP
     VIGRDGEIHR TIQILSRRTK NNPVLIGAAG TGKTAILEGL AQRITRGDVP ESIKDKKVIS
     LDLGSLIAGA KFRGDFEERL KAVLKEVEDA HGKVILFIDE LHTLLGLGKA EGSIDASNLL
     KPALARGELQ CCGATTLSEY RIIEKDAALA RRFQPIQVGE PTVQDTISIL RGIKERYEVH
     HGVRITDSAL VAAATYSNRY ITDRFLPDKA IDLVDEAASA LRLQQESKPD AIQELDRQIM
     TIQIELESLR KETDIASKER REQLEKNLTL KQDEAGLLTE KWDKERAEIE TIKKTKEDLE
     QARIDLETAQ REGNFARASE LRYAKIPELQ KALPSEEGGE STPTSSTGSE TLIHDSVTAD
     DIAWVVAKAT GIPVTKLMAG EIQKLVHMED TLRQTIRGQD EALTAVANAV RLQRAGLSGE
     NRPLASFMFL GPTGVGKTEL CKQVAAFLFS TPQAVVRFDM SEFQEKHTIS RLIGSPAGYV
     GYEDAGQLTE AVRRKPYAVL LFDEFEKAHK DISTLLLQVL DEGFLTDAQG HRVDFRNTMV
     VLTSNLAAEA IVADDSNNST SGSGEISPDV KQHVMDVVQS TYPPEFLNRI DEFILFRRLS
     KPALRDIVDL RLRELQTRLD DRRITLRVSD EVKTWLCDKG YDPRYGARPL NRLIAKEVGN
     GLADKIIRGL IKGGESAEVV VREGGEHLDV VAV
//
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