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Database: UniProt
Entry: A1D544_NEOFI
LinkDB: A1D544_NEOFI
Original site: A1D544_NEOFI 
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
//
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