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Database: UniProt
Entry: A0A0D2FJ44_9EURO
LinkDB: A0A0D2FJ44_9EURO
Original site: A0A0D2FJ44_9EURO 
ID   A0A0D2FJ44_9EURO        Unreviewed;       620 AA.
AC   A0A0D2FJ44;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=ATP-dependent Clp protease, ATP-binding subunit ClpX {ECO:0000313|EMBL:KIW68068.1};
GN   ORFNames=PV04_04037 {ECO:0000313|EMBL:KIW68068.1};
OS   Phialophora macrospora.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX   NCBI_TaxID=1851006 {ECO:0000313|EMBL:KIW68068.1, ECO:0000313|Proteomes:UP000054266};
RN   [1] {ECO:0000313|EMBL:KIW68068.1, ECO:0000313|Proteomes:UP000054266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 27337 {ECO:0000313|EMBL:KIW68068.1,
RC   ECO:0000313|Proteomes:UP000054266};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Capronia semiimmersa CBS27337.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KN846958; KIW68068.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D2FJ44; -.
DR   STRING; 5601.A0A0D2FJ44; -.
DR   HOGENOM; CLU_014218_1_2_1; -.
DR   OrthoDB; 452393at2759; -.
DR   Proteomes; UP000054266; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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   ATP-binding {ECO:0000313|EMBL:KIW68068.1};
KW   Hydrolase {ECO:0000313|EMBL:KIW68068.1};
KW   Nucleotide-binding {ECO:0000313|EMBL:KIW68068.1};
KW   Protease {ECO:0000313|EMBL:KIW68068.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054266}.
FT   DOMAIN          187..379
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          472..566
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   REGION          45..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          139..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          299..329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..69
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        151..170
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        306..325
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   620 AA;  66874 MW;  E4B8E85DBE248DB5 CRC64;
     MQPPTAIPSF LCPALDSAMA ASTSSIPLRL RPSYVALSKR SLSTSSHSRS SSQFHRSDFV
     NQPFTGTYEP GLPTSGPLGG ASSYGNPRLT PKMLKQHLDQ FVVGQERAKK VLSVAVFNHY
     QRIQELQRRE EEEEELLAQR ERRERHPVES EFPGQQTTIR MGGPSIPGFN PRTNTSPIID
     TSPLTLEKSN ILLLGPSGVG KTLMAKTLAR VLSVPFSMSD CTPFTQAGYI GEDAEVCVHR
     LLAAANYDVE RAERGIICLD EIDKIATAKV SHGKDVSGEG VQQALLKIVE GTTIQIQAKP
     ERNAPRAGGQ SQTYPTSSPL GAGFSSGPSS GAAAPAKGEV YNVRTDNILF ICSGAFIGLQ
     KHIMDRLAKG SIGFGANVRS SSNLISYGRD QKSTTTAPVP ILPGSQEEAL YKKHLPFFTP
     APAPQQSSLD GSPTEPNYFN PLDLVTPADL QSYGFIPELV GRIPTAAALA ALTHSMLLRI
     LTEPRNSLVA QYITLFSLSG IELRFTTPAL HVIASNALSM GTGARALRTE METILGDAMF
     EAPGSSVKYV LVTERVAKRE EGAIYFGRGQ GGKFHALIAQ EEGDWEDKQK RRDAERKIDT
     ASASFEDWRT KSTIAAGSGG
//
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