ID D5GKG4_TUBMM Unreviewed; 683 AA.
AC D5GKG4;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 24-JAN-2024, entry version 64.
DE SubName: Full=(Perigord truffle) hypothetical protein {ECO:0000313|EMBL:CAZ85007.1};
GN ORFNames=GSTUM_00009533001 {ECO:0000313|EMBL:CAZ85007.1};
OS Tuber melanosporum (strain Mel28) (Perigord black truffle).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Tuberaceae; Tuber.
OX NCBI_TaxID=656061 {ECO:0000313|EMBL:CAZ85007.1, ECO:0000313|Proteomes:UP000006911};
RN [1] {ECO:0000313|EMBL:CAZ85007.1, ECO:0000313|Proteomes:UP000006911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mel28 {ECO:0000313|EMBL:CAZ85007.1,
RC ECO:0000313|Proteomes:UP000006911};
RX PubMed=20348908; DOI=10.1038/nature08867;
RA Martin F., Kohler A., Murat C., Balestrini R., Coutinho P.M., Jaillon O.,
RA Montanini B., Morin E., Noel B., Percudani R., Porcel B., Rubini A.,
RA Amicucci A., Amselem J., Anthouard V., Arcioni S., Artiguenave F.,
RA Aury J.M., Ballario P., Bolchi A., Brenna A., Brun A., Buee M.,
RA Cantarel B., Chevalier G., Couloux A., Da Silva C., Denoeud F.,
RA Duplessis S., Ghignone S., Hilselberger B., Iotti M., Marcais B., Mello A.,
RA Miranda M., Pacioni G., Quesneville H., Riccioni C., Ruotolo R.,
RA Splivallo R., Stocchi V., Tisserant E., Viscomi A.R., Zambonelli A.,
RA Zampieri E., Henrissat B., Lebrun M.H., Paolocci F., Bonfante P.,
RA Ottonello S., Wincker P.;
RT "Perigord black truffle genome uncovers evolutionary origins and mechanisms
RT of symbiosis.";
RL Nature 464:1033-1038(2010).
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|RuleBase:RU004432}.
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DR EMBL; FN430338; CAZ85007.1; -; Genomic_DNA.
DR RefSeq; XP_002840816.1; XM_002840770.1.
DR AlphaFoldDB; D5GKG4; -.
DR STRING; 656061.D5GKG4; -.
DR EnsemblFungi; CAZ85007; CAZ85007; GSTUM_00009533001.
DR GeneID; 9182027; -.
DR KEGG; tml:GSTUM_00009533001; -.
DR eggNOG; KOG1051; Eukaryota.
DR HOGENOM; CLU_005070_4_0_1; -.
DR InParanoid; D5GKG4; -.
DR OMA; GPEHILM; -.
DR OrthoDB; 35211at2759; -.
DR Proteomes; UP000006911; Unassembled WGS sequence.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:EnsemblFungi.
DR GO; GO:0051787; F:misfolded protein binding; IEA:EnsemblFungi.
DR GO; GO:0034605; P:cellular response to heat; IEA:EnsemblFungi.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IEA:EnsemblFungi.
DR GO; GO:0042026; P:protein refolding; IEA:EnsemblFungi.
DR GO; GO:0050821; P:protein stabilization; IEA:EnsemblFungi.
DR GO; GO:0043335; P:protein unfolding; IEA:EnsemblFungi.
DR CDD; cd00009; AAA; 1.
DR CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR Gene3D; 1.10.8.60; -; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000006911}.
FT DOMAIN 122..266
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 408..551
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 579..670
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT REGION 54..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 683 AA; 75276 MW; 8B40BB3073CEF4BD CRC64;
MLSRSIAITR AFRPAANTAN LRIRSVNRIN LPPLIGLNSF LRGSPVSTIR GYATARGGGG
PQGPFPPGGT HSMDLGGSGE EESALGKFGT DLTARARDGK LDPVIGRNEE IRRTIQVLSR
RTKNNPVLIG SAGTGKTAIL EGLAQRIVSG EVPESMKDKR VVSLDLGQLI AGAKYRGDFE
ERFKGVLKEV SGAQGKVILF IDELHTLLGL GKTEGSVDAS NLLKPQLSRG ELQCCGATTL
NEYRQIEKDV ALARRFQPIL VDEPSVQDTI SILRGIKDRY EVHHGVRITD NALVSAAILS
NRYITDRFLP DKAIDLVDEA ASALRLQQES QKANLQKIKT TKEELEQARV VSKATGIPTT
KLMSGEVEKL VHLEDTLRQS VRGQDDALKS VADAVRLQRA GLANDHRPTA SFMFLGPTGV
GKTELCKALA TTLFASENAV IRFDMSEFQE KHTISRLIGS PAGYVGYEDA GQLTEAVRRK
PYAVLLFDEF EKAHKDLSSL LLQVLDEGFL TDAHGRKVDF RSTIIVLTSN IGQDILINDP
SSDVAISPAI KQQVIDIVQH SYPPEFLNRI DEFIIFQRLS KDAIRDIVDI RLRELQEKLD
DRRIKLDVDA KAKDWLSEKG YDTRYGARPL NRLIGKKLLN PLAERLIRGE IRNSEVARTR
VAQEGTELEV LPNHQPSTSS NQR
//