ID A0A167CUE9_9HYPO Unreviewed; 463 AA.
AC A0A167CUE9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Peptidase C14, caspase catalytic {ECO:0000313|EMBL:OAA41594.1};
GN ORFNames=BBO_05580 {ECO:0000313|EMBL:OAA41594.1};
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:OAA41594.1, ECO:0000313|Proteomes:UP000076863};
RN [1] {ECO:0000313|EMBL:OAA41594.1, ECO:0000313|Proteomes:UP000076863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 3172 {ECO:0000313|EMBL:OAA41594.1,
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 C14B family.
CC {ECO:0000256|ARBA:ARBA00009005}.
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:OAA41594.1}.
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DR EMBL; AZHA01000016; OAA41594.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A167CUE9; -.
DR OrthoDB; 1077459at2759; -.
DR Proteomes; UP000076863; Unassembled WGS sequence.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.12660; -; 1.
DR InterPro; IPR029030; Caspase-like_dom_sf.
DR InterPro; IPR011600; Pept_C14_caspase.
DR PANTHER; PTHR48104:SF30; METACASPASE-1; 1.
DR PANTHER; PTHR48104; METACASPASE-4; 1.
DR Pfam; PF00656; Peptidase_C14; 1.
DR SUPFAM; SSF52129; Caspase-like; 1.
PE 3: Inferred from homology;
KW Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022807};
KW Protease {ECO:0000256|ARBA:ARBA00022807};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 169..453
FT /note="Peptidase C14 caspase"
FT /evidence="ECO:0000259|Pfam:PF00656"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 463 AA; 51428 MW; 89D5AA13980EE281 CRC64;
MSSYQGHGRP QYGASPPMHH HQQQPPYQGA SYAYAPPISS PRFIRRILLL SADLQLLYFD
ASIRPPQQSP QPYPNQGHPS PQHAYYQQAQ LQQQQFAYPP NSSPHQYQQQ MPGQPPYGAR
PGAAPSPHHQ HGLQQGRQDT VQAPPSTPQH FGSGAPQSYS FKYSQCTGRR KALLIGINYF
GQRGQLRGCI NDVRNMTSYL AEHFGYRRED MVILTDDQQN PMSQPTKQNI LRAMHWLVKD
ARPNDSLFFH YSGHGGQTKD LDGDEPDGYD EVIYPVDFRQ HGHITDDEMH RIMVSPLCGG
VRLTAIFDSC HSGTALDLPY IYSTQGILKE PNLAKEAGQG LLGVISSYSQ GDLGGMSSQI
VSLFKKATSG EEAHSRALAT KTSPADVVMW SGSKDDQTSA DASIGLQATG AMSWAFITSL
KKNPQQSYVQ LLNSLRDELS TRYTQKPQLS CSHPLNTDLL FVM
//
