ID A0A1G4J0H7_9SACH Unreviewed; 905 AA.
AC A0A1G4J0H7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=LAMI_0C01596g1_1 {ECO:0000313|EMBL:SCU82987.1};
GN ORFNames=LAMI_0C01596G {ECO:0000313|EMBL:SCU82987.1};
OS Lachancea mirantina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=1230905 {ECO:0000313|EMBL:SCU82987.1, ECO:0000313|Proteomes:UP000191024};
RN [1] {ECO:0000313|Proteomes:UP000191024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Devillers H.;
RL Submitted (MAR-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; LT598466; SCU82987.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4J0H7; -.
DR STRING; 1230905.A0A1G4J0H7; -.
DR OrthoDB; 35211at2759; -.
DR Proteomes; UP000191024; Chromosome c.
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: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; 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|RuleBase:RU004432};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000191024};
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 432..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 878..905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..905
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 905 AA; 101821 MW; 73BAB0FE2C3EE875 CRC64;
MNDETQFTER ALTIVTLAQK LAQDHQHAQL QPIHFLAAFV ETPEDGSKPY LENLIEKARY
DYDTFRRVVN RHLVRIPQQN PAPAQVTPSY STGQVLQEAI KIQKQQKDSF IAQDHILFAL
FTDSSIQQIF KEAQVEIEAI KQQALEMRGN QKIDSRGADT STPLEYLSKY AIDMTEQARE
GKIDPVIGRE EEIRSTIRVL ARRIKSNPCL IGEPGIGKTA IIEGVAQRII DDDVPTILQG
SKLFSLDLAA LTAGAKYKGD FEERLKGVLK EIEDSKTLIV LFIDEIHMLM GNGKDDAANI
LKPALSRGQL KVIGATTNNE YRSIVEKDGA FERRFQKIDV QEPSVRQTVA ILRGLQQKYE
IHHGVRILDS SLVTAAQLAK RYLPYRRLPD SALDLVDISC AGVAVARDSK PEELDSKERQ
LHLLQVEIKA LERDEEADPT TKERLQQARQ KEASLKEELE PLRQRYNEER QGHEELTKAK
KKLDELENKA LDAERRYDTA TAADLRYFAI PDIKKQIEEL ENQVAEEERR AGAGAMVQNV
VDSDTIAETA ARLTGIPVNK LTESENEKLI HMERELSSEV VGQMEAIKAV SNAVRLSRSG
LANPRQPASF LFLGLSGSGK TELAKRIAAF LFNDADAMIR VDCSELSEKY SVSKLLGTTA
GYVGYEEGGF LTNQLQRKPY SVLLFDEVEK AHPDVLTVML QMLDDGRLTS GAGKTINCSN
CIVIMTSNLG ASFINAQPGA KIEESTKGLV MGAVKQHFRP EFLNRISSIV VFNKLSHKAI
HRIVDIRLKE IEERFEENDK HYKLDVSPEA KSFLSKYGYS EDMGARPLNR LIQNEILNRM
ALRILKGQIR DKETVHVILK KKKEHEGLDQ ELEVLPNHEN GDVDMDVDNG WDDIEDEIDD
ATPLD
//