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Database: UniProt
Entry: C0P081_AJECG
LinkDB: C0P081_AJECG
Original site: C0P081_AJECG 
ID   C0P081_AJECG            Unreviewed;       621 AA.
AC   C0P081;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit clpX {ECO:0000313|EMBL:EEH02897.1};
GN   ORFNames=HCBG_08800 {ECO:0000313|EMBL:EEH02897.1};
OS   Ajellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432)
OS   (Darling's disease fungus) (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=447093 {ECO:0000313|EMBL:EEH02897.1, ECO:0000313|Proteomes:UP000001631};
RN   [1] {ECO:0000313|Proteomes:UP000001631}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G186AR / H82 / ATCC MYA-2454 / RMSCC 2432
RC   {ECO:0000313|Proteomes:UP000001631};
RA   Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA   Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA   Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA   Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA   Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA   San-Blas G., Taylor J., Mendoza L., Galagan J.E., Nusbaum C., Birren B.W.;
RT   "The genome sequence of Ajellomyces capsulatus strain G186AR.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; GG663380; EEH02897.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0P081; -.
DR   STRING; 447093.C0P081; -.
DR   VEuPathDB; FungiDB:I7I50_08905; -.
DR   HOGENOM; CLU_014218_1_2_1; -.
DR   InParanoid; C0P081; -.
DR   OrthoDB; 452393at2759; -.
DR   Proteomes; UP000001631; 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:EEH02897.1};
KW   Hydrolase {ECO:0000313|EMBL:EEH02897.1};
KW   Nucleotide-binding {ECO:0000313|EMBL:EEH02897.1};
KW   Protease {ECO:0000313|EMBL:EEH02897.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001631}.
FT   DOMAIN          187..379
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          470..564
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   REGION          61..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          126..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          300..333
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          584..621
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..149
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        156..171
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        300..328
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        584..608
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   621 AA;  67765 MW;  18DCC64B45AFCF99 CRC64;
     MSFLRPFRSP LRPLDWTTTS SPVRRRVQLS YLALYSIRRH IFTSPRCSSP SQFHRSDFTN
     QPFTGSYEPG LPTSGPLGSA PSFGAPHLTP KILKQHLDQF VVGQDRAKKV LSVAVYNHYQ
     RVQELQRQEE EKEELKAQQA RRESVEGHPV ETEFPGQQRT IHTQRTTNDD IARSGPLPID
     SSPLTLEKSN ILLLGPSGVG KTLMAKTLAR VLSVPFSISD CTPFTQAGYI GEDADVCVHR
     LLAAANYDVA QAEWGIICLD EVDKLAAAKV SHGKDVSGEG VQQALLKIIE GTTVQIQAKP
     ERNASRSGGS HNSSPSTTGS NFGGSSFSSA PPGLPGKPEV YNVRTDNILF IFSGAFVGLN
     KMIMDRISRG SIGFGQPIRA SSNSFSSHNS SHAVSTAPIP ILPGSEEEAL YKKHLPFFTP
     APLPSGSGSP DEEPTYFNPL DLLTPVDLQT YGFIPELVGR IPVITALSQL THHLLLRILT
     EPRNSLLAQY TTLFSLSGIE LRFTTPALHK IASNAMSMAT GARGLRTEME MILGDAMFEA
     PGSSVKFVLI TEAVAARKEK AVYLARGQGG KFHAMIAAEE GEWEEKIRKQ KEGAGDNKNN
     DNSFEQWRLR ARTDTAVGGF S
//
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