ID A0A0D7BPT6_9AGAR Unreviewed; 725 AA.
AC A0A0D7BPT6;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Peptidase C14 caspase domain-containing protein {ECO:0000259|Pfam:PF00656};
GN ORFNames=CYLTODRAFT_389056 {ECO:0000313|EMBL:KIY72174.1};
OS Cylindrobasidium torrendii FP15055 ss-10.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae;
OC Cylindrobasidium.
OX NCBI_TaxID=1314674 {ECO:0000313|EMBL:KIY72174.1, ECO:0000313|Proteomes:UP000054007};
RN [1] {ECO:0000313|EMBL:KIY72174.1, ECO:0000313|Proteomes:UP000054007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FP15055 ss-10 {ECO:0000313|EMBL:KIY72174.1,
RC ECO:0000313|Proteomes:UP000054007};
RX PubMed=25683379; DOI=10.1016/j.fgb.2015.02.002;
RA Floudas D., Held B.W., Riley R., Nagy L.G., Koehler G., Ransdell A.S.,
RA Younus H., Chow J., Chiniquy J., Lipzen A., Tritt A., Sun H., Haridas S.,
RA LaButti K., Ohm R.A., Kues U., Blanchette R.A., Grigoriev I.V., Minto R.E.,
RA Hibbett D.S.;
RT "Evolution of novel wood decay mechanisms in Agaricales revealed by the
RT genome sequences of Fistulina hepatica and Cylindrobasidium torrendii.";
RL Fungal Genet. Biol. 76:78-92(2015).
CC -!- SIMILARITY: Belongs to the peptidase C14B family.
CC {ECO:0000256|ARBA:ARBA00009005}.
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DR EMBL; KN880446; KIY72174.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D7BPT6; -.
DR OrthoDB; 1582860at2759; -.
DR Proteomes; UP000054007; 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; 3.40.50.1460; -; 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:UP000054007};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 67..324
FT /note="Peptidase C14 caspase"
FT /evidence="ECO:0000259|Pfam:PF00656"
FT REGION 24..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 725 AA; 81195 MW; C18CFE2C85787EDB CRC64;
MCVSTKQSHL KATRIVEQTV QHTAEGELSG ADPPPLAGHP SHADALDDVH TTFNNDRDQE
YLSRPLFALT IGINEYKHSC RELPNLKGCI PDADEVDAYL ERDLRVPKSN IVRLRNSDAT
RANIIKAIRS LSSNERIQEN DAIVIYYAGH GAETKRPPNW PGTNANIQMI LPHDFELSTT
QRKEGQGILD INLSRLLGKL ALKKGNNITV IMDCCHSGSG TRGAPACGVE SHGSDRRARL
PEDYEVLSSL YKPQRDDQNM LMASLNSHVL LAATSCTGLA REKDGRGAFT SALLGFLRNH
PGLRISWKEV IQRLPKLATQ NPQCEGNHSS RMPFRLQNAI DHPYFCVTKE GDHYRLHAGE
LQGIRAGVAV DLYERDDTDT FVFWSTTKVS CVTGASQSFL DEPVHLVSSE KPATQLWALK
TLTREITVAL RKKTFWRLVD EIAQPAKERP NVIKLVDIGQ PCDLSLCLYS KHHHTYAWFD
IADTKYRDLG ARRLVYAVPF YASVITQVLN SAADFFYNLR KENIHHPLAH IQPQHNSVLL
EAYALREAQR PRVEHSMITS GANININGVM KVNAGHHGTY GFRIVNKSNN ALYCWAFFFE
MSDLCIWPLF TPSCAEDSKS ADPSIQPGQD LTIGYGSGGA EPLRITPDRT HNPIPKAYLY
DDTKVDVSYL KIFLTTQYVD LAYMEQLTPF FTPPKTRRGR QVSAPKAMPI DVWDTLTLAV
ISSRE
//