ID A0A067LTK8_9AGAM Unreviewed; 798 AA.
AC A0A067LTK8;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 13-SEP-2023, entry version 33.
DE RecName: Full=Clp R domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BOTBODRAFT_39437 {ECO:0000313|EMBL:KDQ06633.1};
OS Botryobasidium botryosum FD-172 SS1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Botryobasidiaceae; Botryobasidium.
OX NCBI_TaxID=930990 {ECO:0000313|EMBL:KDQ06633.1, ECO:0000313|Proteomes:UP000027195};
RN [1] {ECO:0000313|Proteomes:UP000027195}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FD-172 SS1 {ECO:0000313|Proteomes:UP000027195};
RX PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA Hibbett D.S., Grigoriev I.V.;
RT "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT white-rot/brown-rot paradigm for wood decay fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
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DR EMBL; KL198128; KDQ06633.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067LTK8; -.
DR STRING; 930990.A0A067LTK8; -.
DR HOGENOM; CLU_005070_4_0_1; -.
DR InParanoid; A0A067LTK8; -.
DR OrthoDB; 35211at2759; -.
DR Proteomes; UP000027195; 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; 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.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000027195}.
FT DOMAIN 113..258
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 511..686
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 685..776
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT COILED 326..406
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 798 AA; 88230 MW; 7EF3B3A06E4CA5F2 CRC64;
MLRLSAAAAR ARARFLTLQL ERGAPSSART LGPLKFPLHV QPKQLAHALR RGYAQYPGGF
PGVQFKQEQP QKGQALKEYS VDLTELAKAG KLDPVIGRDE EIRRTIQILS RRTKSNPVLL
GQPGTGKTAI LEGLASRIVA KEVPESLHGK RVLSLDLAAL LAGSGIRGQF EERFKALLKD
IEEEAGGVIC FIDELHTLLN LGKAEGSVDA GNMIKPALAR GLQLVGATTP DEYAKTIGKD
RALERRFQPV TIEEPTVEST ISILRGLKSR YERHHGVQIS DAALVTAAVY GARYISDRFL
PDKAIDLVDE AASSLRLAQE SKPDELEALD REIVTLQIER ESLKAETDIF SVERRAQVET
ELERKKDEAQ RLSSIWHAER SRLQAIKELK QKIDDARHYL EVAQREGDYE KASQLRFATI
PELERKVEKL GKEKDDDGAL LHDRVTSSDI AKVVAKATGI PVQNLLKRER EKLVHMEEVL
RERVVGQDHV VASVSDAIRI SRAGLQNANR PISSFLFLGP TGTGKTELCK ALSGFLFDDE
HRGLININMT EYHDRYTMSR LLGAAPGLVG YEEGGQLTEA VRRRPYAVVM LDEIEKAHKD
VTQILLQILD EGTLTDSQGR KVDFKNTIIC LTSNLGSDVL ADPTSVDANG VVTSQGKERV
MARAAEFFAP ELLNRLDTIS VFNKLTRASI LQIVTLRLQD VTDRLKDRRI TIDVDEAAKQ
WLATEGYSDI YGARAIARIV RSKVLFPLAK QLLTGTIREG DVVSIRVAEG GKDLRIASIP
TPGAQEPTLV STEDTPLL
//