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
//