ID A8HR89_PODAS Unreviewed; 926 AA.
AC A8HR89;
DT 04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT 04-DEC-2007, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=Heat shock protein HSP104 {ECO:0000313|EMBL:ABV71346.1};
OS Podospora anserina (Pleurage anserina).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora.
OX NCBI_TaxID=2587412 {ECO:0000313|EMBL:ABV71346.1};
RN [1] {ECO:0000313|EMBL:ABV71346.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=17881723; DOI=10.1091/mbc.E07-07-0657;
RA Malato L., Dos Reis S., Benkemoun L., Sabate R., Saupe S.J.;
RT "Role of Hsp104 in the propagation and inheritance of the [Het-s] prion.";
RL Mol. Biol. Cell 18:4803-4812(2007).
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|RuleBase:RU004432}.
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DR EMBL; EU128751; ABV71346.1; -; Genomic_DNA.
DR AlphaFoldDB; A8HR89; -.
DR VEuPathDB; FungiDB:PODANS_7_8800; -.
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; 1.10.1780.10; Clp, N-terminal domain; 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; IPR036628; Clp_N_dom_sf.
DR InterPro; IPR004176; Clp_R_dom.
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:SF194; HEAT SHOCK PROTEIN 104; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF02861; Clp_N; 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; SSF81923; Double Clp-N motif; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51903; CLP_R; 1.
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 Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000313|EMBL:ABV71346.1}.
FT DOMAIN 1..162
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 431..545
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 926 AA; 103091 MW; 51B0E078F20B9785 CRC64;
MNSKMEFTDR AKKALEDAMA LAEQYAHSQL LPVHLAVALL DPLPDQSKDL QNAPPGTTQT
LLRQVVERAH GDPQLFDRAL KKMLVRLPSQ DPPPESVSMA PSFNNVLRKA MELQKVQKDT
YIAVDHLIQA LSEDVSIQGA LKEANIPKPK LVQEAVQQIR GTKRVDSRNA DTEQENENLA
KFTIDMTAMA REGKIDPVIG REEEIRRVVR ILSRRTKNNP VLIGEPGVGK TTVVEGLAQR
IVNNDVPDNL AACKLLSLDV GALVAGSKYR GEFEERMKGV LKEIQESKEM IVLFVDEIHL
LMGAGSSGEG GMDAANLLKP MLARGQLHCI GATTLAEYRK YIEKDAAFER RFQQVLVKEP
TIPETISILR GLKEKYEVHH GVNIADAAIV ASANLAARYL TSRRLPDSAV DLIDEAAAAV
RVARESQPEI IDSLERRLRQ LKIEIHALSR EKDEASKTRL AQARQDAENV EEELRPLREK
YERERQRGKD IQEAKLKLEA LRVKAEDASR VGDHSRAADL QYYAIPEQEA VIRRLEKEKA
AADAALNANG GDSGGSMITD VVGPDQINEI VARWTGIPVT RLKTTEREKL LHMEKALGKI
VVGQKEAVQS VSNAIRLQRS GLANPNQPPS FLFCGPSGTG KTLLTKALAE FLFDDPKSMI
RFDMSEYQER HSLSRMIGAP PGYVGHDSGG QLTEALRRKP FSILLFDEVE KAAKEVLTVL
LQLMDDGRIT DGQGRVVDAK NCIVVMTSNL GAEYLARPNG KDGKIDPTTR ELVMNALRNY
FLPEFLNRIN SIVIFNRLTR KEIRRIVDLR ISEIQKRLSD NDRNVIIKVS EAAKDKLGAQ
GYSPAYGARP LQRLLEKEVL NRMAILILRG SIRDGEVARV DLVDNKVTVL PNHQESEASD
EEMMIDSDDA LDEIAPDSMD EDLYND
//
