ID   A0A0G2GDP8_9EURO        Unreviewed;       616 AA.
AC   A0A0G2GDP8;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Putative atp-dependent clp protease {ECO:0000313|EMBL:KKY15190.1};
GN   ORFNames=UCRPC4_g06416 {ECO:0000313|EMBL:KKY15190.1};
OS   Phaeomoniella chlamydospora.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Phaeomoniellales; Phaeomoniellaceae; Phaeomoniella.
OX   NCBI_TaxID=158046 {ECO:0000313|EMBL:KKY15190.1, ECO:0000313|Proteomes:UP000053317};
RN   [1] {ECO:0000313|EMBL:KKY15190.1, ECO:0000313|Proteomes:UP000053317}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY15190.1};
RA   Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT   "Distinctive expansion of gene families associated with plant cell wall
RT   degradation and secondary metabolism in the genomes of grapevine trunk
RT   pathogens.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KKY15190.1, ECO:0000313|Proteomes:UP000053317}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY15190.1};
RA   Morales-Cruz A., Amrine K.C., Cantu D.;
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKY15190.1}.
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DR   EMBL; LCWF01000193; KKY15190.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G2GDP8; -.
DR   OrthoDB; 452393at2759; -.
DR   Proteomes; UP000053317; 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   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:KKY15190.1};
KW   Protease {ECO:0000313|EMBL:KKY15190.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053317}.
FT   DOMAIN          180..372
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          467..561
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   REGION          123..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          294..330
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          591..616
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        123..146
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        302..327
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        591..607
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   616 AA;  67654 MW;  D72D6B4CD942E5E4 CRC64;
     MQAASFLYPA VNASRSGRKA VRISQQLQLF YIAFARHFSS TPFLPSSSEF RRSDFGNQPF
     TGSYEANAPT TGPLAAAPIL GVPRLTPKML KQHLDQFVVG QERAKKILSV AVYNHYQRVQ
     ELQRREDEEE ERLARRERRE RHPVEDQWPG QQPTIRLGSP PGHREQIQTP LHDPTPLTLD
     KSNILLLGPS GVGKTLMAKT LARVLDVPFS MSDCTPFTQA GYIGEDAEVC VHRLLSAANY
     DVAKAERGII CLDEIDKIAT ARVSHGKDVS GEGVQQALLK IIEGTTIQVQ AKPERNAPRA
     GGQSNPFPTN GPLGGPSFTQ SPAGSSASPA KGEVYNVRTD NILFIFTGAF TGLPKVVMDR
     ISKGSLGFGQ TVRSKSSLQF SSSAVNSPQS SDPIPILPGS EEEALYKKHL PYFQPHTAHA
     SYSVSHTADE PQYFNALDLL TPTDLQSYGF IPELIGRIPT SAALSPLTHS LLLRILTEPR
     SSLVSQYITL FSLSGIELRF TTPALHVVAS NALTMGTGAR GLRTEMERIL GDAMFEGPGS
     SVKYVLITES VAKREEGAVY FSRGMGSRFH GMAAQEEANW EDRFRREMDE REREQLEKGR
     GSFEEWRERA TASGAG
//