ID A0A319FC90_ASPSB Unreviewed; 616 AA.
AC A0A319FC90;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 03-MAY-2023, entry version 16.
DE SubName: Full=ATP-dependent Clp protease {ECO:0000313|EMBL:PYI03813.1};
GN ORFNames=BO78DRAFT_321879 {ECO:0000313|EMBL:PYI03813.1};
OS Aspergillus sclerotiicarbonarius (strain CBS 121057 / IBT 28362).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448318 {ECO:0000313|EMBL:PYI03813.1, ECO:0000313|Proteomes:UP000248423};
RN [1] {ECO:0000313|EMBL:PYI03813.1, ECO:0000313|Proteomes:UP000248423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121057 {ECO:0000313|EMBL:PYI03813.1,
RC ECO:0000313|Proteomes:UP000248423};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KZ826376; PYI03813.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319FC90; -.
DR STRING; 1448318.A0A319FC90; -.
DR Proteomes; UP000248423; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR48102:SF7; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR48102; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:PYI03813.1};
KW Protease {ECO:0000313|EMBL:PYI03813.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000248423}.
FT DOMAIN 185..374
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 462..556
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT REGION 144..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..595
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 616 AA; 67501 MW; A29FF9AFE83754D8 CRC64;
MLRLPIQARG PFRAHRNSLV RYRHAPKPHI RPVRRGFTSS STTFPTLSQF DRSDFTNQPW
TGSYEPGLPT AGPLASAPAF GAPRVTPRTL KQYLDQFVVG QDRAKKILSV AVFNHYQRVQ
ELQRREEENA ELLAKRARKE AIEHHPVEDE FPGQQQTVQL SSEADALPPP PAQPELDDSS
ALQLEKSNIL LLGPSGVGKT LMAKTLARIL SVPFSISDCT PFTQAGYIGE DAEVCVHRLL
AAANYDVEQA ERGIIVLDEV DKIAAAKVSH GKDVSGEGVQ QALLKLIEGT TVQIQAKQER
SAPRAGSSPN TFPSNNPLGN SPYTPNGGNP PQKGEVYNVR TDNILFIFSG AFVGLHKVIM
DRISRGSIGF GQPVRGSAIT NDRSRESNPG SNQPIPILPG SEEEALYKKH LPFFTSASSG
SPDGEPTYFN ALDLLNPTDL QNYGFIPELV GRVPVTAALS TLTTPLLVRI LTEPRNSLLA
QYTTLFNLSG IELRFTTPAL HRIAANAFTM GTGARALRTE LETILSDAMF ETPGSSVKFV
LVTESVAERN EKPIYLARGQ GGRFHSMIAA EESKWEEKVR REKAEKGKDK TPRPPPSDEL
PPIASFREYR TQSAGF
//