ID A0A0J1ATT9_9TREE Unreviewed; 484 AA.
AC A0A0J1ATT9;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Peptidase C14 caspase domain-containing protein {ECO:0000259|Pfam:PF00656};
GN ORFNames=CC85DRAFT_252433 {ECO:0000313|EMBL:KLT38744.1};
OS Cutaneotrichosporon oleaginosum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Cutaneotrichosporon.
OX NCBI_TaxID=879819 {ECO:0000313|EMBL:KLT38744.1, ECO:0000313|Proteomes:UP000053611};
RN [1] {ECO:0000313|EMBL:KLT38744.1, ECO:0000313|Proteomes:UP000053611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBC0246 {ECO:0000313|EMBL:KLT38744.1,
RC ECO:0000313|Proteomes:UP000053611};
RG DOE Joint Genome Institute;
RA Kourist R., Kracht O., Bracharz F., Lipzen A., Nolan M., Ohm R.,
RA Grigoriev I., Sun S., Heitman J., Bruck T., Nowrousian M.;
RT "Genomics and transcriptomics of the oil-accumulating basidiomycete yeast
RT T. oleaginosus allow insights into substrate utilization and the diverse
RT evolutionary trajectories of mating systems in fungi.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase C14B family.
CC {ECO:0000256|ARBA:ARBA00009005}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KQ087286; KLT38744.1; -; Genomic_DNA.
DR RefSeq; XP_018275235.1; XM_018420572.1.
DR AlphaFoldDB; A0A0J1ATT9; -.
DR GeneID; 28981175; -.
DR OrthoDB; 1077459at2759; -.
DR Proteomes; UP000053611; 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; -; 2.
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:UP000053611};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 189..475
FT /note="Peptidase C14 caspase"
FT /evidence="ECO:0000259|Pfam:PF00656"
FT REGION 1..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..164
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 484 AA; 51962 MW; 2B09022BD0FA9784 CRC64;
MYGGGYNNNQ PPSGFQPQNG YQSNPPPPQF QDTRAFGGYP GAGGGYPGAG GGYPGAGAPP
PPQYGQPQYG GAGGGFQPQG GGYNQGGGFQ PQGGGYGQQS YGQQSYAPPP QQQQYGSYQP
PTGQPPPHHY HPNAQGYQPP QSSGQYGSYQ PPSGPPPPPP TGAQHYGPQF QGPGGKQQPY
FQYSNCTGKR KALLIGINYF GQQGQLRGCI NDVHNVQKFL MDRYHYRAED MVILTDDAKN
PRQIPTRQNI IQAMQWLVRD ARPNDALFFH YSGHGGQVKD QSGDEDDGYD ECIYPVDFKR
AGHLVDDDMH ALMVRPLPAG CRLTAIFDSC HSATALDLPY VYSTEGKIKE PNLLAEAGQG
LLGAAGSYLK GDLGGMVSGV FGVGKSLLGG NKDAAEKTRQ TRTSPADVIM WSGCKDSQTS
ADTSEAGKAT GAMSFAFIAA MTKNPQQSYV MLLRSIREEL RGRYDQKPQL SSSHPIDTNL
LFIC
//
