ID C6HQL1_AJECH Unreviewed; 658 AA.
AC C6HQL1;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=26S proteasome non-ATPase regulatory subunit 3 {ECO:0000313|EMBL:EER37477.1};
GN ORFNames=HCDG_08929 {ECO:0000313|EMBL:EER37477.1};
OS Ajellomyces capsulatus (strain H143) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=544712 {ECO:0000313|EMBL:EER37477.1, ECO:0000313|Proteomes:UP000002624};
RN [1] {ECO:0000313|Proteomes:UP000002624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H143 {ECO:0000313|Proteomes:UP000002624};
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.M.,
RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S.,
RA Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA Yandava C., Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S.,
RA Nino-Vega G., San-Blas G., Taylor J.W., Mendoza L., Galagan J.E.,
RA Nusbaum C., Birren B.W.;
RT "The genome sequence of Ajellomyces capsulatus strain H143.";
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the proteasome subunit S3 family.
CC {ECO:0000256|ARBA:ARBA00007912}.
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DR EMBL; GG692435; EER37477.1; -; Genomic_DNA.
DR AlphaFoldDB; C6HQL1; -.
DR STRING; 544712.C6HQL1; -.
DR VEuPathDB; FungiDB:HCDG_08929; -.
DR eggNOG; KOG2581; Eukaryota.
DR HOGENOM; CLU_416741_0_0_1; -.
DR OMA; NQHDITM; -.
DR Proteomes; UP000002624; Unassembled WGS sequence.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR GO; GO:0042176; P:regulation of protein catabolic process; IEA:InterPro.
DR InterPro; IPR013586; 26S_Psome_reg_C.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10758:SF2; 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 3; 1.
DR PANTHER; PTHR10758; 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 3/COP9 SIGNALOSOME COMPLEX SUBUNIT 3; 1.
DR Pfam; PF01399; PCI; 1.
DR Pfam; PF08375; Rpn3_C; 1.
DR SMART; SM00753; PAM; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50250; PCI; 1.
PE 3: Inferred from homology;
KW Proteasome {ECO:0000313|EMBL:EER37477.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002624}.
FT DOMAIN 404..584
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 136..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 658 AA; 72335 MW; E00246895939CEFC CRC64;
MPPRQDQHVE GPNQAIRSTM RLVISNPLPA HRPPRLTQPG LPVLSPSSVD HLKHHLDTAL
SLLSALPIHA PQTLYVPASS LPPTALLSLY SVSHSPFFAL PSLPFQAASR QLHPPVPTFA
QATSSTPNKL LTFRVSNMPA ERRSLRSNKS DTSANGEKHR SNSTSQNSKD KRAPPSTRSS
VRGKTAAASG KKTSSSNTAS STSTPTSTSA STSAAKKMVA ENDQTAPHTN GGSDPVENGV
NNVNGTEDVE MAEDDADING SATQKNQREG GGESDDGMTV VVPPSKGSRL SGEPEQHQHD
ITMNEAEGGD EAEVEVQVDP REKALSDIKS NFTLLERAVI HFDPRFTLRA LRSISSFFER
TRTSRQPITT LLLRNYLSTS HISQADLFVS RSEFPPGAPN NQIARYLYYL GRIRAIQLQY
TEAHEHLIGA TRKSPSSHTA GGFYQASTKL LVVVELLMGD IPDRAIFRQA TLERAMHPYF
LLVQAVSIGD LDGFIGIVQK HSSTFRRDGT YTLILRLRQN VIKTGIRMMS LAYTRISLRD
ICLRLGLDSE ESAEYIVAKA IRDGVIEASL DHEHGYMKSK EVGDVYATGE PGEVFHERIR
FCLDLHDESV KAMRFPMNQH RLELKNAQEA RERERELAKE IVEGDLDDDD AGGDFDTI
//
