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Database: UniProt
Entry: Q6CJJ3_KLULA
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Original site: Q6CJJ3_KLULA 
ID   Q6CJJ3_KLULA            Unreviewed;       899 AA.
AC   Q6CJJ3;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   27-MAR-2024, entry version 140.
DE   SubName: Full=KLLA0F18194p {ECO:0000313|EMBL:CAG98604.1};
GN   ORFNames=KLLA0_F18194g {ECO:0000313|EMBL:CAG98604.1};
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590 {ECO:0000313|EMBL:CAG98604.1, ECO:0000313|Proteomes:UP000000598};
RN   [1] {ECO:0000313|EMBL:CAG98604.1, ECO:0000313|Proteomes:UP000000598}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 /
RC   WM37 {ECO:0000313|Proteomes:UP000000598};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA   Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA   Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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DR   EMBL; CR382126; CAG98604.1; -; Genomic_DNA.
DR   RefSeq; XP_455896.1; XM_455896.1.
DR   AlphaFoldDB; Q6CJJ3; -.
DR   STRING; 284590.Q6CJJ3; -.
DR   PaxDb; 284590-Q6CJJ3; -.
DR   GeneID; 2895592; -.
DR   KEGG; kla:KLLA0_F18194g; -.
DR   eggNOG; KOG1051; Eukaryota.
DR   HOGENOM; CLU_005070_4_2_1; -.
DR   InParanoid; Q6CJJ3; -.
DR   OMA; MESEPAK; -.
DR   Proteomes; UP000000598; Chromosome F.
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; 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; PS00871; CLPAB_2; 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:UP000000598};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..150
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          868..899
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          466..533
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        883..899
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   899 AA;  100784 MW;  D9684D31A8A429DE CRC64;
     MNDETQFTNK ANEIIRLAQK LAQDHRHAQL QPIHLLAAFV EPNEDGSVGF LQNLVELAKY
     DYEPLKRAIN RNLVRTPSQT PAPLEIQPSY AFGQVLKDTS EIRKQQKDSF VGQDHILTAL
     FKDATTQSIF KECSIDIESV KQQMLELRGN QRIDSRDADT NEKWEYLKKY AIDMTEQARA
     GKLDPVIGRE EEIRTAITVL ARRIKSNPCL IGEPGIGKTA IVEGVAQRII DDDVPQILQG
     CKLFSLDLAA LTAGAKYKGD FEERLKGVLK EIEESKTLII LFIDEIHMLM GQGVDDSANA
     ANILKPALSR GGLKVIGATT TNEYRSLVEK DGAFERRFQK IDVPEPTTRQ TVAILRGLQP
     KYEIHHGVRI LDSALVSAAQ LAKRYLPYRR LPDSAIDLVD ISCAGVAVAR DSKPEELDNK
     ERELHLLQVE IKALERDEET DPTTKERLQQ ARQKEASLIE ELEPMRQRYQ QEVDSHEQLR
     QAKKKLDELE NKCMDAERRY DNATAADLKY FAIPDIKKRI EELEQKVAEE ESREGSETMV
     KNVVNSEVIA ETAARMTGIP VNKLTESENT KLIHMERELS QQVVGQMEAV KAVSNAVRLS
     RSGLSNPNQP ASFLFLGLSG SGKTELAKKV ASFLFNDEKA MVRIDCSELM EKHSVSKLLG
     TTAGYIGYQE GGFLTNQLQR RPYSVLLFDE VEKAHPDVLT VLLQMLDDGR ITSGQGKTID
     CSNCIVIMTS NLGAQFINAQ TGSKVTEGSK ELVMSAVKAH FRPEFLNRIS SIVVFNKLSH
     KAIHKIVDIR IKDLEKQFAD NDKNYKINVS PPARDFLTKN GYSEDMGARP LNRLIQTEIL
     NPMAIHILKG EIKDKEIVNV EVGADGSHLE VLPNHPASSE IGDEDMDLDL DDDDDLDLD
//
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