ID A0A0J8RQ73_COCIT Unreviewed; 437 AA.
AC A0A0J8RQ73;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 08-NOV-2023, entry version 38.
DE SubName: Full=Cathepsin E {ECO:0000313|EMBL:KMU87225.1};
GN ORFNames=CIHG_04669 {ECO:0000313|EMBL:KMU87225.1};
OS Coccidioides immitis H538.4.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=396776 {ECO:0000313|EMBL:KMU87225.1, ECO:0000313|Proteomes:UP000054563};
RN [1] {ECO:0000313|Proteomes:UP000054563}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H538.4 {ECO:0000313|Proteomes:UP000054563};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; DS016997; KMU87225.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J8RQ73; -.
DR STRING; 396776.A0A0J8RQ73; -.
DR VEuPathDB; FungiDB:CIHG_04669; -.
DR Proteomes; UP000054563; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05471; pepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR034164; Pepsin-like_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF75; ENDOPEPTIDASE (CTSD), PUTATIVE (AFU_ORTHOLOGUE AFUA_4G07040)-RELATED; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000054563}.
FT DOMAIN 52..347
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 350..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 277..308
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 437 AA; 47744 MW; 099A86357E319205 CRC64;
MPLQDEKKPL TLDLVKVPRK VRRENKYSAI MGSDPRMENS VAVNQDGQDY SYFSVARFGS
GAQEMWLLLD SGAFGVLACL QHNRFGIEHS KKLSVTDEEW EVSYRTEHVG GVHIGGTRLS
MAGFQLELDF GSALNVSQDF ANYPMDGILG LGPSKITKLK PILQVIADQK LFKKNIFGIS
LQRAADDTRD GQLTFGDIDK SKFTGDITYT DVIKSTNRWE IPVSDAIVGG KRVNFTKKSA
VIDTGTSFIL VPMKDAEAMH ALIPGSSKGD QYFTIPCDTN LSLEIEISGA RWTVSPKDYV
GSQNGDSCNS YILPRQALGP DQWLLGDTFL KNVYSVFDYD ESRIGFAARE YPGTPPSNKS
TPPNAVSSVK IVSEPTTSPV PPRDANANPT EGSSQPSDKN TPDKEGAAAF LSTPGWLSLA
VFLSTGYSWY LSSSGML
//