ID B2AAM4_PODAN Unreviewed; 803 AA.
AC B2AAM4;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE SubName: Full=Mitochondrial heat shock protein 78 {ECO:0000313|EMBL:CDP22777.1};
DE SubName: Full=Podospora anserina S mat+ genomic DNA chromosome 1, supercontig 1 {ECO:0000313|EMBL:CAP60136.1};
GN ORFNames=PODANS_1_4520 {ECO:0000313|EMBL:CAP60136.1};
OS Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS (Pleurage anserina).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC Podospora anserina.
OX NCBI_TaxID=515849 {ECO:0000313|EMBL:CAP60136.1};
RN [1] {ECO:0000313|EMBL:CAP60136.1, ECO:0000313|Proteomes:UP000001197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197}, and S mat+
RC {ECO:0000313|EMBL:CAP60136.1};
RX PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL Genome Biol. 9:R77.1-R77.22(2008).
RN [2] {ECO:0000313|EMBL:CAP60136.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S mat+ {ECO:0000313|EMBL:CAP60136.1};
RA Genoscope - CEA;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000001197}
RP GENOME REANNOTATION.
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197};
RX PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Genetics 197:421-432(2014).
RN [4] {ECO:0000313|EMBL:CDP22777.1}
RP NUCLEOTIDE SEQUENCE.
RA Grognet P., Bidard F., Kuchly C., Chan Ho Tong L., Coppin E.,
RA Ait Benkhali J., Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Submitted (APR-2015) 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; CU633438; CAP60136.1; -; Genomic_DNA.
DR EMBL; FO904936; CDP22777.1; -; Genomic_DNA.
DR RefSeq; XP_001912654.1; XM_001912619.1.
DR AlphaFoldDB; B2AAM4; -.
DR STRING; 515849.B2AAM4; -.
DR GeneID; 6197038; -.
DR KEGG; pan:PODANSg09703; -.
DR VEuPathDB; FungiDB:PODANS_1_4520; -.
DR eggNOG; KOG1051; Eukaryota.
DR HOGENOM; CLU_005070_4_0_1; -.
DR OrthoDB; 35211at2759; -.
DR Proteomes; UP000001197; Chromosome 1.
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:UP000001197};
KW Stress response {ECO:0000313|EMBL:CDP22777.1}.
FT DOMAIN 119..262
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 516..667
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 694..785
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT REGION 56..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 784..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 332..412
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 803 AA; 89267 MW; EE5CDF31E512AF5E CRC64;
MQARSRLLTA ASRRMAAVSR GATRQRQFPQ ALATTTPQTA ALVNSLRLVP SVAARHYSNG
RPHPPGGTHR MNMGGEPEKP ALEQYGVDLT AKARDGKLDP VIGRSAEIQR TIQILSRRTK
NNPVLIGNAG VGKTAILEGL ALEIVRGAVP ESIKNKRVIS LDLGSLIAGA KFRGDFEERL
KKVLTEVEQA NGEVILFIDE LHTLLGLGKA EGSIDASNLL KPALSRGELQ CCGATTLAEY
RLIEKDVALA RRFQPIIVSE PTVQDTISIL RGIKDKYEVH HGVRITDGAL VAAATYSNRY
ITDRFLPDKA IDLMDEAASS LRLQQESKPD DIQRLDQKIM TIQIELESLR KEKDIASKER
REKLEADLKT YEDEVKVLTE KWEKEKAELD AIKQAQAELD RARVELEVAQ RVGNFGRASE
LRFGIIPQLE QKLPKEDEKK SETTLIHDSV TADDIANVVS RITGIPISKL TSGHTERLIH
MEDILRESIR GQDEALKAVA DAVRMQRAGL SGENRPLASF FFLGPTGVGK TELCKKLAGF
LFSTESAVVR FDMSEFQEKH TISRLIGAPS GYVGYEDAGQ LTEAVRRKPY AVLLFDEFEK
AHRDISALLL QVLDEGYLTD AQGHKVDFKN TIIVLTSNLG AEILVGADML HPYKETPDGD
IHPDVKRAVM DVVHSQYPPE FLNRIDSFII FKRLALEALR DIVDIRLKEL QQRLDDRRIT
LEVPGDVRQW LAERGYDPKF GARPLNRLIT TEIGNGLADK IIRGEIRKGD HAVVRVNEEK
TGLVIEGQPG KGEEGRKEEG KEK
//
