ID A0A0E9NS10_SAICN Unreviewed; 905 AA.
AC A0A0E9NS10;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Clp R domain-containing protein {ECO:0000259|PROSITE:PS51903};
GN ORFNames=G7K_6617-t1 {ECO:0000313|EMBL:GAO52543.1};
OS Saitoella complicata (strain BCRC 22490 / CBS 7301 / JCM 7358 / NBRC 10748
OS / NRRL Y-17804).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Taphrinomycotina incertae sedis; Saitoella.
OX NCBI_TaxID=698492 {ECO:0000313|EMBL:GAO52543.1, ECO:0000313|Proteomes:UP000033140};
RN [1] {ECO:0000313|EMBL:GAO52543.1, ECO:0000313|Proteomes:UP000033140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-17804 {ECO:0000313|EMBL:GAO52543.1,
RC ECO:0000313|Proteomes:UP000033140};
RX PubMed=21914972; DOI=10.2323/jgam.57.243;
RA Nishida H., Hamamoto M., Sugiyama J.;
RT "Draft genome sequencing of the enigmatic yeast Saitoella complicata.";
RL J. Gen. Appl. Microbiol. 57:243-246(2011).
RN [2] {ECO:0000313|EMBL:GAO52543.1, ECO:0000313|Proteomes:UP000033140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-17804 {ECO:0000313|EMBL:GAO52543.1,
RC ECO:0000313|Proteomes:UP000033140};
RX PubMed=24646756; DOI=10.2323/jgam.60.7;
RA Nishida H., Matsumoto T., Kondo S., Hamamoto M., Yoshikawa H.;
RT "The early diverging ascomycetous budding yeast Saitoella complicata has
RT three histone deacetylases belonging to the Clr6, Hos2, and Rpd3
RT lineages.";
RL J. Gen. Appl. Microbiol. 60:7-12(2014).
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|RuleBase:RU004432}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAO52543.1}.
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DR EMBL; BACD03000073; GAO52543.1; -; Genomic_DNA.
DR RefSeq; XP_019021694.1; XM_019169848.1.
DR AlphaFoldDB; A0A0E9NS10; -.
DR STRING; 698492.A0A0E9NS10; -.
DR GeneID; 30186695; -.
DR OMA; ERMKAVM; -.
DR OrthoDB; 35211at2759; -.
DR Proteomes; UP000033140; 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000033140};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 879..905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 413..527
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 883..905
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 905 AA; 100297 MW; 67B31F213EC6B45E CRC64;
MSLEFTEKAT QVLSLAQDLV RNYKHVHLEP VHIADALLSE DSPNPLLATI IDKAGGDVQA
FSRYIKRQLV RRPSQDPPPE TPSLSPGAAK VIRSAQDLAK KQKDSFVAID HMISALSEDA
SMKTAFSECG ISATAMEQAL LQARGNKRVE SKSFEEGFEA LSKYTADLTE QARDGSIDPV
IGREDEIRRV IRILSRRTKN NPVLIGEPGV GKTSIAEGLA QRIVNADVPA NLASCRLLSL
DVGSLVAGTK YRGEFEERMK SVLNEIEGAS EQIILFVDEM HLLMGAGGSG EGGMDAANLL
KPMLARGKLH CIGATTLAEY RKYIEKDAAF ERRFQQVLVK EPSVPDTLSI LRGLKEKYEV
HHGVTIADAA LVAAATLASR YLTSRKLPDS AIDLVDEAAA SVRVERESQP EVIDNLERRL
RRLQVEIHAL ERESDAASKE RLNVAKQEAA NVEEELRPLR EKYELERKRG DELQEARKKL
DQLKAKADDA ERRRDLQTAA DLRYYGIPDL QRHIENLEAK KAEMEAQAKP VPGSEPLLTD
VVGPDQINEI VARWTGIPVT RLKSTEKDKL LNMERLLAKQ VVGQREAITA VSNAIRLSRS
GLSNPNQPIA SFLFCGPSGT GKTLLTKSLA EFLFDDEKSM IRIDCTEYME KHSVSKLIGS
PPGYIGHDEG GQLTEQLRRK PYSVILFDEV EKADPSLLTV LLQLLDDGRI TDSKGTVVDA
RNALVILTSN LGAEFLTDAH ATPDGKVDAP TREAVMGAVR RFFRPEFINR LSAIVMFNRL
AKREIRKIVD IRLQDVQKRL ESNNKNVRIE VDDKAKAFLG EAGYSPAYGA RPLNRVIQNE
VLNKLAVMLL RGQIQDGEVA NVTCPDGHHI EILPNHQVGE EGVTGDEDDE MDYSDEDEME
MEPMD
//