ID Q5BF22_EMENI Unreviewed; 927 AA.
AC Q5BF22; C8VQ12;
DT 26-APR-2005, integrated into UniProtKB/TrEMBL.
DT 26-APR-2005, sequence version 1.
DT 24-JAN-2024, entry version 129.
DE SubName: Full=Heat shock protein (Eurofung) {ECO:0000313|EMBL:CBF88645.1};
GN ORFNames=ANIA_00858 {ECO:0000313|EMBL:CBF88645.1};
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321 {ECO:0000313|EMBL:CBF88645.1, ECO:0000313|Proteomes:UP000000560};
RN [1] {ECO:0000313|Proteomes:UP000000560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC {ECO:0000313|Proteomes:UP000000560};
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.J., Wortman J.R., Batzoglou S.,
RA Lee S.I., Basturkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M., Hynes M., Paoletti M., Fischer R., Miller B.,
RA Dyer P., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2] {ECO:0000313|Proteomes:UP000000560}
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC {ECO:0000313|Proteomes:UP000000560};
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|RuleBase:RU004432}.
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DR EMBL; BN001308; CBF88645.1; -; Genomic_DNA.
DR RefSeq; XP_658462.1; XM_653370.1.
DR AlphaFoldDB; Q5BF22; -.
DR STRING; 227321.Q5BF22; -.
DR EnsemblFungi; CBF88645; CBF88645; ANIA_00858.
DR GeneID; 2876634; -.
DR KEGG; ani:AN0858.2; -.
DR VEuPathDB; FungiDB:AN0858; -.
DR eggNOG; KOG1051; Eukaryota.
DR HOGENOM; CLU_005070_4_0_1; -.
DR InParanoid; Q5BF22; -.
DR OMA; ERMKAVM; -.
DR OrthoDB; 35211at2759; -.
DR Proteomes; UP000000560; Chromosome VIII.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0140602; C:nucleolar peripheral inclusion body; IEA:EnsemblFungi.
DR GO; GO:0140453; C:protein aggregate center; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0051787; F:misfolded protein binding; IEA:EnsemblFungi.
DR GO; GO:0051087; F:protein-folding chaperone binding; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0070370; P:cellular heat acclimation; IBA:GO_Central.
DR GO; GO:0071218; P:cellular response to misfolded protein; IEA:EnsemblFungi.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0043335; P:protein unfolding; IBA:GO_Central.
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:SF18; 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|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000000560};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000313|EMBL:CBF88645.1}.
FT DOMAIN 3..162
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 479..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..517
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..555
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 927 AA; 103528 MW; B0BC764D9D46A2EB CRC64;
MNTDKYTDKA NKALQDALEL TIEHSNAELY PVHLAVALLD PSQNEDDGPS LHPSHGDSTS
LFRQVVERAH GDVQLLHRGL MKRLVKLPSQ DPPPETRSIS APFRKVLTAA ADLSKTQKDS
YIAVDHLIQA VCQDSTVQAA LKDANVPNVK LIDNAIQQIR GTRRVDSKTA DAESENENLK
KFTIDMTALA REGKIDPVIG REEEIRRVIR ILSRRTKNNP VLIGEPGVGK TTIVEGLARR
IVNADIPASL SQCKLLSLDV GSLVAGSKYR GEFEERLKGV LKEIEESKET IVLFVDEIHL
LMGAGASGEG GMDAANLLKP MLARGQLHCI GATTLGEYRK YIEKDAAFER RFQQVLVKEP
TVSETISILR GLKEKYEVHH GSVRILDAAI VTAATLAARY LTARRLPDSA VDLIDEAAAA
VRVARESEPE ALDNLERKHR QLQIEIHALK REKDEASKAR LQAAEQEAAN VIEELRPMRQ
KYESEKQRNK AIQDAKTKLD NLKNKQEEAE RSGDTETAAD LKYYAIPETQ QHIEMLEKQR
AEADEERRNR QGDAGEPLLA DEVGPDQINE IVARWTGIPV TRLKTSEKDK LLEMEKHLGK
IVVGQREAVK SISDAIRLQR SGLSNPNSPP SFLFCGPSGT GKTLLTKALA EFLFDDPKSM
IRFDMSEYQE RHSLSRMIGA PPGYVGHDAG GQLTESLRRR PFSILLFDEV EKAAKEVLTV
LLQLMDDGRI TDGQGRVVDA RNCIVVMTSN LGAEYLARPT TKDGKIDPQT RELVMGALRN
YFLPEFLNRI SSIVIFNRLT KKEIRKIVDL RLDEVQRRLE QNGRNVVIEC TEEVKDYLGQ
SGYSPAYGAR PLGRIIEREV LNRLAVLILR GSIQDGEVAR VVMRDGRIDV IPNHEMAIDE
DQDMTDEDDF DAMAEMEDNG GDMDLYE
//