ID V2XL71_MONRO Unreviewed; 521 AA.
AC V2XL71;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Metacaspase-1 {ECO:0000313|EMBL:ESK94487.1};
GN ORFNames=Moror_8145 {ECO:0000313|EMBL:ESK94487.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK94487.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK94487.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK94487.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(2014).
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:ESK94487.1}.
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DR EMBL; AWSO01000135; ESK94487.1; -; Genomic_DNA.
DR RefSeq; XP_007846304.1; XM_007848113.1.
DR AlphaFoldDB; V2XL71; -.
DR KEGG; mrr:Moror_8145; -.
DR HOGENOM; CLU_522827_0_0_1; -.
DR OrthoDB; 1077459at2759; -.
DR Proteomes; UP000017559; 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:UP000017559};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 352..499
FT /note="Peptidase C14 caspase"
FT /evidence="ECO:0000259|Pfam:PF00656"
FT REGION 1..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..206
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 521 AA; 58407 MW; 0F104FAAB7F3AF4C CRC64;
MSWDFTAGNN APPTQRSRTP APGIRMPTPF PSAAPSSAAP SITINPPSRN PSTYSLQYIV
PHTPMSAHPQ PPPSPMLAPS MHSSHSVTRS QTPAPVLANE VPSVQYHDQR RSGSRSRSRT
PVPVSLEAPP VQYGQHRSRS SSRSRTPAPV VTRETPIVQL HEPHHSRSRS RSQTPVAREG
RSVERHDHHH HQRSSSRPRR HSSPKRRPII VLQPPNTNII VVPQKLVSGK NRPNHRKSSS
HGAILIDGHT GKPYSHSNGD NSVGLPEKIL QQVQQAMNGR ANQQYSSSGP HRQNLAQQAQ
HIIGGILRPY LHHHSSSNQI DSYFPRPEHP AYNPVSFPNP QSTFEYSRCT GKKRALCIGI
NYTGQDRPLR GCVNDARHMR EFLIRRHGFK AEDIVLLTDD SSNPKQQPTK RNMLEAMRWL
VRDARPHDSL FFHYSGHGSR TEDLDGDELD GYDEIIMPVD YKKRGHILDD ELHSTMVKPL
PPGCRLTAIF DSCHSGTVLG KCLTFSLRLV ILIRFQICPT W
//
