ID K1XJX8_MARBU Unreviewed; 422 AA.
AC K1XJX8;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Metacaspase CasA {ECO:0000313|EMBL:EKD12714.1};
GN ORFNames=MBM_08943 {ECO:0000313|EMBL:EKD12714.1};
OS Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Drepanopeziza.
OX NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD12714.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD12714.1, ECO:0000313|Proteomes:UP000006753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD12714.1,
RC ECO:0000313|Proteomes:UP000006753};
RX PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA Huang M.-R., Wu R., Zhou Y.;
RT "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT evolution.";
RL BMC Genomics 13:382-382(2012).
CC -!- SIMILARITY: Belongs to the peptidase C14B family.
CC {ECO:0000256|ARBA:ARBA00009005}.
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DR EMBL; JH921454; EKD12714.1; -; Genomic_DNA.
DR RefSeq; XP_007296832.1; XM_007296770.1.
DR AlphaFoldDB; K1XJX8; -.
DR GeneID; 18764878; -.
DR KEGG; mbe:MBM_08943; -.
DR eggNOG; KOG1546; Eukaryota.
DR HOGENOM; CLU_029389_0_2_1; -.
DR InParanoid; K1XJX8; -.
DR OMA; YLCRMER; -.
DR OrthoDB; 1077459at2759; -.
DR Proteomes; UP000006753; 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:UP000006753};
KW Signal {ECO:0000256|SAM:SignalP};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..422
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003855449"
FT DOMAIN 128..413
FT /note="Peptidase C14 caspase"
FT /evidence="ECO:0000259|Pfam:PF00656"
FT REGION 78..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 422 AA; 45874 MW; BEAC89CFBA01D09B CRC64;
MVVSLVVVGV SLVSIHVRSP DLKPCNDSHV NVNASDSSSR IAYNYTSHYN SPSSQQCQVI
QVKAMVGAIN SKQQQQQGYG YGYGSQQPQH DRGQQYGHAP PPPPQGMVSF GHGAPQEYAF
QYSNCAGRRK ALLIGINYFG QNGELRGCIN DVRNVSSYLT QSFGYRREDM VILTDDSQEP
MGQPTKENIL RAMNWLVQGS QPNDSLFFHY SGHGGQTEDT NGDEEDGSDE VIYPVDYQRH
GHIVDDEMHA IMVTPLQAGV RLTAIFDSCH SGSALDLPYL YSTQGVLKEP NLAKEAGMGL
LGVVSAASAG NYVAVAGHLI GFLKKASKTD GAYKKTITTK TSPADVIMWS GSKDDQTSAD
ATIASQATGA MSWAFITAMK ANPQQSYVQL LNSIRDVLAT KYSQKPQLSC SHPLDTNLLF
IM
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