ID G0V5V9_NAUCC Unreviewed; 909 AA.
AC G0V5V9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 63.
DE RecName: Full=Clp R domain-containing protein {ECO:0000259|PROSITE:PS51903};
GN Name=NCAS0A02890 {ECO:0000313|EMBL:CCC66847.1};
GN OrderedLocusNames=NCAS_0A02890 {ECO:0000313|EMBL:CCC66847.1};
OS Naumovozyma castellii (strain ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC
OS 1992 / NRRL Y-12630) (Yeast) (Saccharomyces castellii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1064592 {ECO:0000313|EMBL:CCC66847.1, ECO:0000313|Proteomes:UP000001640};
RN [1] {ECO:0000313|EMBL:CCC66847.1, ECO:0000313|Proteomes:UP000001640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC 1992 / NRRL Y-12630
RC {ECO:0000313|Proteomes:UP000001640};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Type strain:CBS 4309;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Genome sequence of Naumovozyma castellii.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|RuleBase:RU004432}.
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DR EMBL; HE576752; CCC66847.1; -; Genomic_DNA.
DR RefSeq; XP_003673238.1; XM_003673190.1.
DR AlphaFoldDB; G0V5V9; -.
DR STRING; 1064592.G0V5V9; -.
DR GeneID; 11526615; -.
DR KEGG; ncs:NCAS_0A02890; -.
DR eggNOG; KOG1051; Eukaryota.
DR HOGENOM; CLU_005070_4_2_1; -.
DR InParanoid; G0V5V9; -.
DR OMA; ERMKAVM; -.
DR OrthoDB; 35211at2759; -.
DR Proteomes; UP000001640; Chromosome 1.
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; 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|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000001640};
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 434..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 887..909
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 909 AA; 101342 MW; 3375FE2E4AFADDEC CRC64;
MNDETQFTER ALTIVTLAQK LAEDHQHPQL LPIHLLAAFI ETPEDGSISY LQNLIEKGRF
DFDLFKKVVN RTLVRVPQQH PAPSQITPSY SLGKVLQDAA KIQKQQKDSF VAQDHLLFAL
LDDSSIQTVF KEASIDIEAI KQQALVLRGN QKIDSRGADT NTPLEYLNKY AIDMTEQARE
GKLDPVIGRE EEIRNTIRVL ARRIKSNPCL IGEPGVGKSA IIEGVAQRII DDDVPTLLQG
AKLFSLDLAA LTAGAKYKGD FEERFKGVLK EIDQSKTLIV LFIDEIHMLM GNGKDDAANI
LKPALSRGQL KVIGATTNNE YRSIVEKDGA FERRFQKIEV SEPTLRETVA ILRGLQPKYE
IHHGVRILDS ALVTAAQLAK RYLPYRRLPD SALDLVDISC AGVAVARDSK PEELDSKERQ
LQLLQVEIKA LERDEDADST TQDRLKQAKQ KEASLQEELE PLRQRYNEER TGHEELTKAK
KKLDELESKA QDAERRYDNA TAADLRYFAI PDIQKQIAKL EEQVAEEEKR AGSHSMIQNV
VDSDTISETA ARLTGIPVKK LTESENEKLI HMERDLSSQV VGQMGAIKAV SNAVRLSRSG
LANPRQPASF LFLGLSGSGK TELAKKIAGF LFNDEDMMIR VDCSELSEKY SVSKLLGTTA
GYVGYDEGGF LTNQLQYKPY SVLLFDEVEK AHPDVLTVLL QMLDDGRITS GQGKTIDCSN
CIIIMTSNLG AQFINSQEGS KISDSTKDMV MGAVKNHFRP EFLNRISSIV VFNKLSRKAI
HKIVDIRIKE LEARFEANDK HYKLNVSPEA KDFLAKFGYS NDMGARPLNR LIQNEILNKL
AVRILRKEIL DKETVNIVLK ANGKGANDAT GEGESLEVLP NHEAAVDAKT ADGDAMDIDD
DLDDDLDLD
//