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Database: UniProt
Entry: F0U7H9_AJEC8
LinkDB: F0U7H9_AJEC8
Original site: F0U7H9_AJEC8 
ID   F0U7H9_AJEC8            Unreviewed;       439 AA.
AC   F0U7H9;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=26S protease regulatory subunit 7 {ECO:0000313|EMBL:EGC40756.1};
GN   ORFNames=HCEG_00118 {ECO:0000313|EMBL:EGC40756.1}, I7I53_08554
GN   {ECO:0000313|EMBL:QSS52809.1};
OS   Ajellomyces capsulatus (strain H88) (Darling's disease fungus) (Histoplasma
OS   capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=544711 {ECO:0000313|Proteomes:UP000008142};
RN   [1] {ECO:0000313|EMBL:EGC40756.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H88 {ECO:0000313|EMBL:EGC40756.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Champion M., Cuomo C., Ma L.-J., Henn M.R., Sil A., Goldman B., Young S.K.,
RA   Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA   Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Klein B.,
RA   McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA   San-Blas G., Taylor J., Mendoza L., Galagan J., Nusbaum C., Birren B.;
RT   "Annotation of Ajellomyces capsulatus strain H88.";
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000008142}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H88 {ECO:0000313|Proteomes:UP000008142};
RA   Champion M., Cuomo C., Ma L.-J., Henn M.R., Sil A., Goldman B., Young S.K.,
RA   Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA   Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Klein B.,
RA   McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA   San-Blas G., Taylor J., Mendoza L., Galagan J., Nusbaum C., Birren B.;
RT   "Annotation of Ajellomyces capsulatus strain H88.";
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:QSS52809.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=H88 {ECO:0000313|EMBL:QSS52809.1};
RA   Voorhies M., Cohen S., Shea T.P., Petrus S., Munoz J.F., Poplawski S.,
RA   Goldman W.E., Michael T., Cuomo C.A., Sil A., Beyhan S.;
RT   "Chromosome-level genome assembly of a human fungal pathogen reveals
RT   clustering of transcriptionally co-regulated genes.";
RL   Submitted (JAN-2021) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
CC       {ECO:0000256|ARBA:ARBA00006914, ECO:0000256|RuleBase:RU003651}.
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DR   EMBL; DS990636; EGC40756.1; -; Genomic_DNA.
DR   EMBL; CP069103; QSS52809.1; -; Genomic_DNA.
DR   AlphaFoldDB; F0U7H9; -.
DR   STRING; 544711.F0U7H9; -.
DR   VEuPathDB; FungiDB:I7I53_08554; -.
DR   HOGENOM; CLU_000688_6_2_1; -.
DR   OMA; INGYKKF; -.
DR   Proteomes; UP000008142; Unassembled WGS sequence.
DR   Proteomes; UP000663419; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IEA:UniProt.
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   CDD; cd19502; RecA-like_PAN_like; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041569; AAA_lid_3.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR048723; PRS7-like_OB.
DR   PANTHER; PTHR23073; 26S PROTEASOME REGULATORY SUBUNIT; 1.
DR   PANTHER; PTHR23073:SF13; 26S PROTEASOME REGULATORY SUBUNIT 7; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   Pfam; PF21236; PRS7_OB; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU003651};
KW   Hydrolase {ECO:0000313|EMBL:EGC40756.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW   Protease {ECO:0000313|EMBL:EGC40756.1};
KW   Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008142}.
FT   DOMAIN          214..353
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..28
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   439 AA;  49129 MW;  9322FA3B93291851 CRC64;
     MPSATGQNWE KYKKNFADDE EPEKKITPLT DEDIQVLKTY GAAPYAAALK KLEKQIKEKQ
     TSVNDKIGVK ESDTGLAPPH LWDVAADRQR MQEEQPLQVA RCTKIIQDEK DPEKSKYVIN
     VKQIAKFVVN LGERISPTDI EEGMRVGVDR NKYQILLPLP PKIDPSVTMM TVEDKPDVTY
     GDVGGCKEQI EKLREVVEMP LLSPERFVSL GIDPPKGALL YGPPGTGKTL CARAVANRTD
     ATFIRVIGSE LVQKYVGEGA RMVRELFEMA RTKKACIIFF DEIDAIGGAR FDDGAGGDNE
     VQRTMLELIT QLDGFDSRGN IKVMFATNRP STLDPALMRP GRIDRKIEFS LPDLEGRANI
     LRIHARSMSM ERDIRWELIS RLCPNSTGAE LRSVATEAGM FAIRARRKVA TEKDFLAAVD
     KVIKGNLKFN STATYMQYN
//
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