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
//