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Database: UniProt
Entry: A0A1E3NSS9_9ASCO
LinkDB: A0A1E3NSS9_9ASCO
Original site: A0A1E3NSS9_9ASCO 
ID   A0A1E3NSS9_9ASCO        Unreviewed;       899 AA.
AC   A0A1E3NSS9;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Clp R domain-containing protein {ECO:0000259|PROSITE:PS51903};
GN   ORFNames=PICMEDRAFT_14633 {ECO:0000313|EMBL:ODQ49159.1};
OS   Pichia membranifaciens NRRL Y-2026.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Pichia.
OX   NCBI_TaxID=763406 {ECO:0000313|EMBL:ODQ49159.1, ECO:0000313|Proteomes:UP000094455};
RN   [1] {ECO:0000313|EMBL:ODQ49159.1, ECO:0000313|Proteomes:UP000094455}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-2026 {ECO:0000313|EMBL:ODQ49159.1,
RC   ECO:0000313|Proteomes:UP000094455};
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 ClpA/ClpB family.
CC       {ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; KV454001; ODQ49159.1; -; Genomic_DNA.
DR   RefSeq; XP_019020272.1; XM_019160461.1.
DR   AlphaFoldDB; A0A1E3NSS9; -.
DR   STRING; 763406.A0A1E3NSS9; -.
DR   GeneID; 30177148; -.
DR   OrthoDB; 35211at2759; -.
DR   Proteomes; UP000094455; 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; 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:SF194; 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; 2.
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|RuleBase:RU004432};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094455};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..148
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          433..453
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          871..899
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        874..899
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   899 AA;  100390 MW;  BC01EB36CA1FC840 CRC64;
     MDSTQFTDRA LEIVTNAQKL CQQNSNPQLL PIHFLAAMIP DNESQAIYLK TIIEGSRYEW
     EPVKRSINQH LLKLPSNQGS NMEPGMSASA ASIITNAEKV KQIQKDSYIG QDHILTAMLD
     DDSIKRLFKD LSINTESLKK QIIQLRGSQR IDSRQADSSE EYEFLSKYAI DMTEQALQGK
     IDPVIGREEE IRRAIRVLSR RAKSNPCLIG DPGVGKTSIV EGVAQRIVDN DVPSVLQNCK
     LYGLDLGALK AGAKYQGEFE ERIKGVLNDI EKSKTMIILF IDEIHMLMGD GKSDAANLLK
     PALARGHFHC IGATTISEYR KYIEKDGAFE RRFQRIDVKE PTVRETVAIL RGLQPRYEIH
     HGVRILDSAL VTAAQLASRY LTYRKMPDSA VDLIDESAAG VAVARDSKPE ELDSKERQLE
     LLEVEINALE RDKDADASTK DRLKQAHKKK QELEEELQPL REQYSQEKAG HQELTAAKKK
     LDELDIKAQD AERRHDTATV ADIRMFAIPD VKKRIEELER EVEEEEHSAE FLVKNVVGPD
     QVAETAARLT GIPVSKLTQA ENAKLINMER ELSSAVVGQG EAVKAVSNAI RLSRSGLANP
     NQPASFLFLG LSGSGKTELA KKLAGFLFAD ERAMIRIDCS ELMEKHSVSK LIGTTAGYIG
     FEEGGLLTNQ LMRKPYSVIL FDEVEKAAPE VLNILLQLLD DGRITAANGT LVNCSNAILI
     LTSNLGAQFI NQSKVTKITP EVKEEVMTVV RQHFRPELLN RISATVVFNR LSRHAISKIV
     KIRLEEIEKR FEENGRHLKL KLDDLAMEYL CKHGYSMDLG ARPLNRLIQN GVLNPLAVMI
     LNGQVLDKED VKVSVNGKGL YVIPNHESSG EGMDVDAIED WTDDADEDDD YADNDVELD
//
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