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Database: UniProt
Entry: A0A068RXJ0_9FUNG
LinkDB: A0A068RXJ0_9FUNG
Original site: A0A068RXJ0_9FUNG 
ID   A0A068RXJ0_9FUNG        Unreviewed;       482 AA.
AC   A0A068RXJ0;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Peptidase c14 {ECO:0000313|EMBL:CDH53691.1};
GN   ORFNames=LCOR_05021.1 {ECO:0000313|EMBL:CDH53691.1};
OS   Lichtheimia corymbifera JMRC:FSU:9682.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Lichtheimiaceae; Lichtheimia.
OX   NCBI_TaxID=1263082 {ECO:0000313|EMBL:CDH53691.1, ECO:0000313|Proteomes:UP000027586};
RN   [1] {ECO:0000313|EMBL:CDH53691.1, ECO:0000313|Proteomes:UP000027586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMRC:FSU:9682 {ECO:0000313|Proteomes:UP000027586};
RA   Schwartze V.U., Winter S., Shelest E., Marcet-Houben M., Horn F.,
RA   Wehner S., Hoffmann K., Riege K., Sammeth M., Nowrousian M., Valiante V.,
RA   Linde J., Jacobsen I.D., Marz M., Brakhage A.A., Gabaldon T., Bocker S.,
RA   Voigt K.;
RT   "Gene expansion shapes genome architecture in the human pathogen
RT   Lichtheimia corymbifera: an evolutionary genomics analysis in the ancient
RT   terrestrial Mucorales (Mucoromycotina).";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
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:CDH53691.1}.
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DR   EMBL; CBTN010000019; CDH53691.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A068RXJ0; -.
DR   STRING; 1263082.A0A068RXJ0; -.
DR   VEuPathDB; FungiDB:LCOR_05021.1; -.
DR   OrthoDB; 1077459at2759; -.
DR   Proteomes; UP000027586; 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   Hydrolase {ECO:0000256|ARBA:ARBA00022807};
KW   Protease {ECO:0000256|ARBA:ARBA00022807};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027586};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT   DOMAIN          184..472
FT                   /note="Peptidase C14 caspase"
FT                   /evidence="ECO:0000259|Pfam:PF00656"
FT   REGION          1..156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..99
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   482 AA;  52487 MW;  522F03ACBBCF6ADC CRC64;
     MSYYPGQYGS YGGQPPPPQY PPPQQSYGGY PPPPPQGSYP PPPPQQHPGP YPPPPPQNYP
     PPPGGNYPPP PPPPTNTYPG AGPYPPPAGY APPTTQPPNY RPYGNGAIQP PPYTGEDPGF
     RPNDPSLAQA NYPQPPNSMH NSQPSPVPYG PPGGGNMGNF VMHVNPAMQN RPPPNFQLSN
     CQGRKRALLI GINYFGSPNE LKGCINDVHN LKEFLISLYH FRQEDMVVLT DDQSDPRFIP
     TKQNMIAAMQ WLVRDARPND SFFFHYSGHG GRVKDTNGDE DDGWDETIYP VDHQMYPGKN
     GQIVDDDMHE IMVRPLPPGC RLTAIFDSCH SGTALDLPYV YSTQGTLKEA NLFKDAGSGL
     LSAGMAYASG NIGGALSSVM SLGKNLLNGK SVDERVKQFK SSAADVIMFS GCKDQQTSAD
     AFEAGRSTGA MSHAFTTALR ANPHQSYLQL LNSVRAILRE KYSQRPQLSS SHPIDVNLQF
     IC
//
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