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Database: UniProt
Entry: A0A1E3PVW3_LIPST
LinkDB: A0A1E3PVW3_LIPST
Original site: A0A1E3PVW3_LIPST 
ID   A0A1E3PVW3_LIPST        Unreviewed;       482 AA.
AC   A0A1E3PVW3;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   13-SEP-2023, entry version 24.
DE   RecName: Full=AAA+ ATPase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=LIPSTDRAFT_100309 {ECO:0000313|EMBL:ODQ69563.1};
OS   Lipomyces starkeyi NRRL Y-11557.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Lipomycetaceae; Lipomyces.
OX   NCBI_TaxID=675824 {ECO:0000313|EMBL:ODQ69563.1, ECO:0000313|Proteomes:UP000094385};
RN   [1] {ECO:0000313|EMBL:ODQ69563.1, ECO:0000313|Proteomes:UP000094385}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-11557 {ECO:0000313|EMBL:ODQ69563.1,
RC   ECO:0000313|Proteomes:UP000094385};
RX   PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA   Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA   Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA   Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA   Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA   Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA   Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA   Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA   Jeffries T.W.;
RT   "Comparative genomics of biotechnologically important yeasts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
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DR   EMBL; KV454303; ODQ69563.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E3PVW3; -.
DR   STRING; 675824.A0A1E3PVW3; -.
DR   OrthoDB; 452393at2759; -.
DR   Proteomes; UP000094385; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR004487; Clp_protease_ATP-bd_su_ClpX.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00382; clpX; 1.
DR   PANTHER; PTHR48102:SF7; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR48102; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000094385}.
FT   DOMAIN          116..289
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          327..412
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   REGION          455..482
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   482 AA;  53312 MW;  FC1ABDB910038E81 CRC64;
     MTGARPSGPL FRRASTVPMF TYSNQQHLSP RAIKAYLDNY VIGQEHAKMV IAVAVYNHYL
     RAQNLEDRKR RMRKDFDSRL RSDAIIEDIP DESVQPTQPK AFFVAEAEED DTPVLEKTNV
     LLLGPTGSGK TLLMQTVAKV LGVPFAMVDC TSLTQAGYIG DDVDICIQRL LASADYDVEK
     AEFGIVVLDE CDKLAKPARV GFSSTKDISG EGVQQALLQM LEGSTVTVTR KSGTAGQTKE
     SYTVNTNNIL FVLSGAFVGL ENIIEERVSD KHAIGFKAVP GSAAMGKFFM PSNAHVLNYV
     EVQDLTKYGM IPELVGRIPH ISPLLPLSEA DMLRIITEPK NSIMKQYEHS FKMFGVELKF
     TTPALQALAK SALEQGTGAR GLKGIMARLL LNVNYELPES STKYVLVTEN VVKTFMNTNE
     SDRARPFYFS RGEQYKFLNE LASENQVAQA LLVESQTRDR NGESVSGQDE DEPTPQRVGF
     IE
//
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