ID A0A167BJD2_9HYPO Unreviewed; 534 AA.
AC A0A167BJD2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 28-JUN-2023, entry version 32.
DE SubName: Full=Candidapepsin-4 {ECO:0000313|EMBL:OAA40103.1};
GN ORFNames=BBO_06161 {ECO:0000313|EMBL:OAA40103.1};
OS Beauveria brongniartii RCEF 3172.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria;
OC Beauveria brongniartii.
OX NCBI_TaxID=1081107 {ECO:0000313|EMBL:OAA40103.1, ECO:0000313|Proteomes:UP000076863};
RN [1] {ECO:0000313|EMBL:OAA40103.1, ECO:0000313|Proteomes:UP000076863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 3172 {ECO:0000313|EMBL:OAA40103.1,
RC ECO:0000313|Proteomes:UP000076863};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAA40103.1}.
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DR EMBL; AZHA01000020; OAA40103.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A167BJD2; -.
DR OrthoDB; 615305at2759; -.
DR Proteomes; UP000076863; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05474; SAP_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; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR033876; SAP-like.
DR PANTHER; PTHR47966:SF65; ASPARTIC-TYPE ENDOPEPTIDASE; 1.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-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 Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..534
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007884246"
FT TRANSMEM 513..533
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 70..394
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 478..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 88
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 290
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 324..359
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 534 AA; 56238 MW; F92086A7F1D95312 CRC64;
MRLSSANLAA GLVLAGRGVA TTAENVAHAD SNPGYLAVPV GIVPRTHRIE KRTKNADAIQ
TTLENMNFFY AAQIGIGTPP QNITLLIDTG SSELWVNPDC RTARPQDAQL CAEFGQYNHS
KSRTPPVGPF GKEEIRFGDT TDKSTLTSVK LTYFTDKMTF GSLSIENQTF GVVTESKRQS
QGILGLAPDL RAGFDGDEPY SLVLNSMAKQ GVIASRVFSL DLRHSDTKTG ALIYGGLDRS
KFVGTLEKVP IIKGLQGETR LAVSLDTLGI TMSREENYRL QGNDTNVMLD SGTTISRLQA
DVAMPILKAL RAESEDNGYF YIPCSARNQQ GSVDFGFGGT TVRVPFKDFI INVGDPYTCY
AGIALTGGQQ ILGETVLRAG YFVFDWDNEA VHIGQAADCG ESDIVKVGTG KDAVPSVTGN
CAASQILSAT SVSTSKLAQT ISVDGGAGAS AAATTYAVTA CPAFDPKCQT EMIKTVTAQA
NPTESGGEGE DGGSGKGSSN GDKKNSGGGR YGVVGWLFAV LCSVSTGSMI IALS
//