ID A0A1Y2VKC1_9PEZI Unreviewed; 472 AA.
AC A0A1Y2VKC1;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Peptidase C14 caspase domain-containing protein {ECO:0000259|Pfam:PF00656};
GN ORFNames=M434DRAFT_26280 {ECO:0000313|EMBL:OTA97883.1};
OS Hypoxylon sp. CO27-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX NCBI_TaxID=1001938 {ECO:0000313|EMBL:OTA97883.1, ECO:0000313|Proteomes:UP000194361};
RN [1] {ECO:0000313|EMBL:OTA97883.1, ECO:0000313|Proteomes:UP000194361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO27-5 {ECO:0000313|EMBL:OTA97883.1,
RC ECO:0000313|Proteomes:UP000194361};
RX PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA Henrissat B., Gladden J.M.;
RT "Characterization of four endophytic fungi as potential consolidated
RT bioprocessing hosts for conversion of lignocellulose into advanced
RT biofuels.";
RL Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
CC -!- SIMILARITY: Belongs to the peptidase C14B family.
CC {ECO:0000256|ARBA:ARBA00009005}.
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DR EMBL; KZ112422; OTA97883.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2VKC1; -.
DR STRING; 1001938.A0A1Y2VKC1; -.
DR Proteomes; UP000194361; 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 Reference proteome {ECO:0000313|Proteomes:UP000194361};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 178..463
FT /note="Peptidase C14 caspase"
FT /evidence="ECO:0000259|Pfam:PF00656"
FT REGION 1..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..84
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..129
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 472 AA; 50924 MW; F74A8F48C2ED8518 CRC64;
MSGWGNDQGY YGGGYSGGHQ PQHGAGGYSH QSPPPQGYNQ YGPPSGPPQG YNQYGAPPGP
PPQQPGYNQY PPPSGPPQGY NQYGAPPGAP PQQHGYNQYP PSGPPPSHHQ YPGRYPPPSG
PPPPGLDPYG YPVHSGGPPV QGYGGQHRAG PPPPTTPQQF GHGAPEGYTF QYSNCTGKRK
ALFIGINYFG QKGELRGCIN DTKNLSQFLM ERYGYKREDM IILTDDQHDP IMIPTKANIL
RALEWLVSGA RPNDALFLHY SGHGGQVEDE DGDEEDGYDE VIYPVDYETA GHIVDDQLHH
VVVKPLQAGV RLTAIFDSCH SGSVLDLPYI YSTKGVLKEP NLAAEAGQGL LKAISSYAQG
DTAGVASAIF NFAKTAYKGD DGYKKTIETK TSPADVIMWS GSKDDQTSAD ATIASQATGA
MSWAFITALK QDPKQSYVEL LNSIRDVLET KYTQKPQLSC SHPLDTNLLF VM
//
