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Database: UniProt
Entry: A0A1E3Q7I8_LIPST
LinkDB: A0A1E3Q7I8_LIPST
Original site: A0A1E3Q7I8_LIPST 
ID   A0A1E3Q7I8_LIPST        Unreviewed;       977 AA.
AC   A0A1E3Q7I8;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN   ORFNames=LIPSTDRAFT_266896 {ECO:0000313|EMBL:ODQ73663.1};
OS   Lipomyces starkeyi NRRL Y-11557.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Lipomycetaceae; Lipomyces.
OX   NCBI_TaxID=675824 {ECO:0000313|EMBL:ODQ73663.1, ECO:0000313|Proteomes:UP000094385};
RN   [1] {ECO:0000313|EMBL:ODQ73663.1, ECO:0000313|Proteomes:UP000094385}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-11557 {ECO:0000313|EMBL:ODQ73663.1,
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).
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
CC       {ECO:0000256|ARBA:ARBA00006914}.
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DR   EMBL; KV454293; ODQ73663.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E3Q7I8; -.
DR   STRING; 675824.A0A1E3Q7I8; -.
DR   OrthoDB; 276256at2759; -.
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   CDD; cd19509; RecA-like_VPS4-like; 1.
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; IPR041569; AAA_lid_3.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR015415; Spast_Vps4_C.
DR   PANTHER; PTHR23074; AAA DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR23074:SF17; FIDGETIN-LIKE PROTEIN 1; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   Pfam; PF09336; Vps4_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094385}.
FT   DOMAIN          725..872
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          119..203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          211..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          267..360
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          412..643
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        153..174
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        211..225
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        317..342
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        441..461
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        504..518
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        534..557
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        561..575
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        577..593
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        615..636
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   977 AA;  105562 MW;  2C409A73987C3585 CRC64;
     MPIKSKRASA SDNVLQRIYE EAYRTFVDAM FEDGRGNGAA ALDGWLNTLE LIENEHSKIV
     ACPQVSSLDI TLYARIVDIE RQSKDRVYSY AASFAGNTLT SAELKTIYEQ LRADRRKIQK
     EEPLQKQKQQ PPKQTARGKK QMMRPDGPLR SLSAGATVSN SADALRSQSP PKKSMLMTLR
     GPKSSKKDNH TMSSTTKNRL AVPATTAANL AWTSSSGASG NTSRRSSENK DNEEYLMHTA
     FKNFSSSSLP SIPSTSTAPV ATVTATSVNS VPDPRRNLST GSLLDDERQP PLISLSPAHT
     PPTLSSEFVP HRHQGVQGLS PPSSRSPSPT TSQPSTGING RTVPARQPPA VPTSSLPGLP
     QRIVKEQPKL TSAQATTTVV DADAMKTEPP PVLPPQQSSL FDPHLMTTIK PSKFVRRKIP
     SGSSAIRPPN EPLVSLPALP TALTAPPPPP LPPPSPPPPL SRANAEHARN PAPFGSPSAS
     SADMLSPSAP IHIPIPESLT LPPSTFPYPQ SAAKSSGRVS PKRTLRDPQP TKHRQGSART
     SPTPAGIAVT SNPLTAALAA TAKEERKDKE RKPHQPYGLT SSISSQSDIG NRIPRRMSPT
     HASTAKMKAP IVSPQPQRRQ RQTLVPAISS PNANVTTPGG PLPPLMPDTP NPEHQAWNNR
     VNAAVKNITG VEETAARQIL NEIIVKGDEV HWDDIAGLEQ AKTSLKETVV YPFLRPDLFK
     GLREPARGML LFGPPGTGKT MLARAVATES QSTFFAISAS SLTSKYLGES EKLVRALFAL
     ARALAPSIIF VDEIDSLLSS RSDTGEHEAS RRIKTEFLVK WSDLAHAAAG KEHKDGDDAQ
     RVLVLAATNL PWAIDEAARR RFVRRQYIPL PEPETRTKQI ETLLKYQVHD LSEAEIRNLV
     ALTDGFSGSD ITAVAKDAAM GPLRALGEAL LSTPRDQIRP VKFIDFEASL KNIRPSVSKE
     GLRAFEDWAL KYGSSGA
//
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