ID A5DJL9_PICGU Unreviewed; 900 AA.
AC A5DJL9;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 2.
DT 24-JAN-2024, entry version 95.
DE RecName: Full=Clp R domain-containing protein {ECO:0000259|PROSITE:PS51903};
GN ORFNames=PGUG_03470 {ECO:0000313|EMBL:EDK39372.2};
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746 {ECO:0000313|EMBL:EDK39372.2, ECO:0000313|Proteomes:UP000001997};
RN [1] {ECO:0000313|EMBL:EDK39372.2, ECO:0000313|Proteomes:UP000001997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL
RC Y-324 {ECO:0000313|Proteomes:UP000001997};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|RuleBase:RU004432}.
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DR EMBL; CH408158; EDK39372.2; -; Genomic_DNA.
DR RefSeq; XP_001484089.1; XM_001484039.1.
DR AlphaFoldDB; A5DJL9; -.
DR STRING; 294746.A5DJL9; -.
DR GeneID; 5126228; -.
DR KEGG; pgu:PGUG_03470; -.
DR VEuPathDB; FungiDB:PGUG_03470; -.
DR eggNOG; KOG1051; Eukaryota.
DR HOGENOM; CLU_005070_4_2_1; -.
DR InParanoid; A5DJL9; -.
DR OMA; ERMKAVM; -.
DR OrthoDB; 35211at2759; -.
DR Proteomes; UP000001997; 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:SF18; 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; 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; 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|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000001997};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..149
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 870..900
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 413..529
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 874..900
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 900 AA; 99784 MW; 76098D3DF0DBFD51 CRC64;
MEETQFTDNA LNIITNATQI AKEGSHAQLM PLHLLAAMVP SDNESSTPYL KTLITKARYE
WPDFERIVNR RVVRLPSQNP PPDTPAPSYA TGQVLQKAAK FKTQQKDNYI AQDHILLALL
EDASIKEIFK EAGINTETIS SEVMEMRKGQ RIDSRTADSS QTFEFLSKYC EDLTEKAREG
RIDPVIGREE EIRRVIRVLA RRTKSNSVLI GEAGVGKTSI VEGVAQRIVD GDVPNVLSQA
RLFALDLGAL TAGAKYKGEF EERIKGVLKD IENSKDMIIL FIDEIHMLMG DGKSDAANLL
KPMLARGSLH CIGATTFSEY QKFIAKDGAF ERRFQKIDVP AATVNETVAI LRGLQPRYEI
HHGVRILDSA LVTAAQLASR YLTYRSLPDS AVDLIDESAA TVAVARDSKP EELDNLEREL
HLVEVEINAL ERDVDADSAS KDRLEIAKRK QAELIEKLNP LREQFNQERA GHEELIAAKR
KLDELEIKAH DAERRHETAK AADLRYFAIP DVQKHIQELE IKVAEEEAQE GSEALLRNVV
GSEQVSETAA KLTGIPVTKL TRAENSKLIN MEKELASEVV GQPEAVKAVS NAIRLSRSGL
ANPNQPASFL FLGLSGSGKT ELAKKLAGFL FADERAMIRI DCSELGDKWS ASKLLGAAPG
YVGYEEGGIL TEALIRRPYS VVLFDEVEKA APEVLTVLLQ VLDDGRITSS QGKVVNCANA
IFIMTSNLGA QFINNSSHSK IDPQTKELVM TAVRNHFRPE FLNRISGMIV FNRLSRKAIA
KIVKIRLNEI QKRFAANGKA FTLSLDDAAL EYLCKNGYSS DLGARPLNRL IQNEILNKLA
ILLLKGQIKD KETARVTLGS KGLEVIPNHD VEDMDMGDAD DEGWWDVDDD DDDDVVETLD
//