ID A0A167CSG7_9ASCO Unreviewed; 890 AA.
AC A0A167CSG7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Chaperone ATPase HSP104 {ECO:0000313|EMBL:ANB12054.1};
GN Name=HSP104 {ECO:0000313|EMBL:ANB12054.1};
GN ORFNames=AWJ20_289 {ECO:0000313|EMBL:ANB12054.1};
OS Sugiyamaella lignohabitans.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Trichomonascaceae; Sugiyamaella.
OX NCBI_TaxID=796027 {ECO:0000313|EMBL:ANB12054.1, ECO:0000313|Proteomes:UP000189580};
RN [1] {ECO:0000313|EMBL:ANB12054.1, ECO:0000313|Proteomes:UP000189580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10342 {ECO:0000313|EMBL:ANB12054.1,
RC ECO:0000313|Proteomes:UP000189580};
RA Bellasio M., Peymann A., Valli M., Sipitzky M., Graf A., Sauer M., Marx H.,
RA Mattanovich D.;
RT "Complete genome sequence and transcriptome regulation of the pentose
RT utilising yeast Sugiyamaella lignohabitans.";
RL Submitted (FEB-2016) 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; CP014501; ANB12054.1; -; Genomic_DNA.
DR RefSeq; XP_018734531.1; XM_018879864.1.
DR AlphaFoldDB; A0A167CSG7; -.
DR GeneID; 30034850; -.
DR KEGG; slb:AWJ20_289; -.
DR OrthoDB; 35211at2759; -.
DR Proteomes; UP000189580; Chromosome a.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; 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 InterPro; IPR002078; Sigma_54_int.
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.
DR PROSITE; PS50045; SIGMA54_INTERACT_4; 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:UP000189580};
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 DOMAIN 575..766
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000259|PROSITE:PS50045"
FT REGION 863..890
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 413..502
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 873..890
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 890 AA; 98731 MW; EB699E4232BD2474 CRC64;
MDQSEFTDRA IKIITDAVQI ASDHGHAFVS PVHFLAAMTP DDQDGTPSYL RTVTEKARYD
WKPLERIINK HLVRIPSQSP APPKPELTSQ SANIIQSAAN IRAKQKDTFT AQDHILLALL
DDTSIQAIFK EVSIDIKALQ SQVQAIRGNR RIDSRMADSS EQFEFLSKYA LDLTTMAREG
KIDPVIGREE EIRRCIRVLA RRTKSNPCLI GDPGVGKTSI VEGVAQRIID GDVPNVLANT
RLFSLDLGAL KAGAKYQGDF EERVKGVLTE IEESKDMIVL FIDEIHMLMG DGKSDAANLL
KPMLARGALH CIGATTVEEY RKYIEKDGAF ERRFQKIDVP EPTIPETIAI LRGLQGKYEL
HHGVRILDSA LVTAAQLASR YLTYRKLPDS AVDLIDETAA SVAVARDSKP EELDTLERQL
QLLQVEIKAL ERDSGTDATT GDRLSAARQK AASLEEQLAP LRERFQEERK GHEELSSLKK
KLDELETKAQ DAERRRDTGA SADLRYFAIP DIKRRIDEIE RTIDDKSDST LLEDIVDSDK
VAETAARLSG IPVSKLTQAE NSKLINMEKT LSKQVVGQTE AVKAVSNAIR LSRSGLSNPN
APASFLFMGL SGSGKTELAK KVAGFLFADE KAMIRIDCSE LADKWSASKL LGAAPGYVGY
EEGGILTEAL ARKPYSVVLF DELEKAAPEV LTILLQILDD GRVRSSSGKV VNAANCIIIM
TSNLGAESIN RSSSSKIDPI TRDQVMEAVR AHFRPEFLNR ISSMIIFNRL SKKAIRKIVE
LRISEIEKRF VSSNKNIHLD LDDACYDYLV ENGYSKDLGA RPLNRLIQNE ILNKLALLML
RGQVQDNETV KITLGDRGLE LIPNHEPATT DEEYMEVDSD SDMDDIPALD
//