ID A1D544_NEOFI Unreviewed; 591 AA.
AC A1D544;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 97.
DE SubName: Full=ATP-dependent Clp protease, putative {ECO:0000313|EMBL:EAW23537.1};
GN ORFNames=NFIA_022480 {ECO:0000313|EMBL:EAW23537.1};
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW23537.1, ECO:0000313|Proteomes:UP000006702};
RN [1] {ECO:0000313|Proteomes:UP000006702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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DR EMBL; DS027688; EAW23537.1; -; Genomic_DNA.
DR RefSeq; XP_001265434.1; XM_001265433.1.
DR AlphaFoldDB; A1D544; -.
DR STRING; 331117.A1D544; -.
DR EnsemblFungi; EAW23537; EAW23537; NFIA_022480.
DR GeneID; 4590689; -.
DR KEGG; nfi:NFIA_022480; -.
DR VEuPathDB; FungiDB:NFIA_022480; -.
DR eggNOG; KOG0745; Eukaryota.
DR HOGENOM; CLU_014218_1_2_1; -.
DR OMA; HRSDFTN; -.
DR OrthoDB; 452393at2759; -.
DR Proteomes; UP000006702; Unassembled WGS sequence.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:EnsemblFungi.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:EnsemblFungi.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:1904287; P:positive regulation of protein-pyridoxal-5-phosphate linkage; IEA:EnsemblFungi.
DR GO; GO:0030150; P:protein import into mitochondrial matrix; IEA:EnsemblFungi.
DR GO; GO:0042026; P:protein refolding; IEA:EnsemblFungi.
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:EAW23537.1};
KW Protease {ECO:0000313|EMBL:EAW23537.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006702}.
FT DOMAIN 160..350
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 439..533
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT REGION 119..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 591 AA; 64535 MW; 42656CC397C2B60A CRC64;
MCLKSTSQFP APLSACSYLP DLSGKSRSDF TNQPWSGIYE AGLPTAGPLG STPAFGAPRI
TPKTLKQYLD QFVVGQDRAK KILSVAVFNH YQRVQELQRR EEENAELLAR RARRQALEHH
PAEDEFPGQQ RTVHLPTSPK STTSNPDEAL LSDSSPLQLE KSNILLLGPS GVGKTLMAKT
LARVLSVPFS ISDCTPFTQA GYIGEDAEVC VHRLLAAANY DVEQAERGII VLDEVDKLAA
AKVNHGKDVS GEGVQQALLK IIEGTTVQVQ AKQERNAHRT SGTPSSYPSN NPLGNPPFSQ
SPTGNAPQKG EIYNVRTDNI LFIFSGAFVG LHKVIMDRIS HGSMGFGQPV RSQSSPTHRP
GDPLATTSNQ PVPILPGSEE EALYKKHLPF FTAASPTSPD GEPPYFNALD LLNPTDLQNY
GFIPELIGRI PVTAALSALS QPLLVRILTE PRNSLLAQYT TLFSLSGIEL RFTTPALHKV
AANAFAMGTG ARALRTEMEN ILSDAMFETP GSSVKFVLIT EAVADRKERP IYLSRGQGGR
FHSLIAAEES KWEEKVRREK SEKEKKIKGQ VSENQPSIAN FREYRTRAAG F
//