MCA1_PICGU
ID MCA1_PICGU Reviewed; 410 AA.
AC A5D9W7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Metacaspase-1;
DE EC=3.4.22.-;
DE Flags: Precursor;
GN Name=MCA1; ORFNames=PGUG_00072;
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- FUNCTION: Involved in cell death (apoptosis). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase C14B family. {ECO:0000305}.
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DR EMBL; CH408155; EDK35974.2; -; Genomic_DNA.
DR RefSeq; XP_001486695.1; XM_001486645.1.
DR AlphaFoldDB; A5D9W7; -.
DR SMR; A5D9W7; -.
DR STRING; 4929.XP_001486695.1; -.
DR EnsemblFungi; EDK35974; EDK35974; PGUG_00072.
DR GeneID; 5128747; -.
DR KEGG; pgu:PGUG_00072; -.
DR VEuPathDB; FungiDB:PGUG_00072; -.
DR eggNOG; KOG1546; Eukaryota.
DR HOGENOM; CLU_029389_0_2_1; -.
DR InParanoid; A5D9W7; -.
DR OMA; PTKANMI; -.
DR OrthoDB; 821819at2759; -.
DR Proteomes; UP000001997; Unassembled WGS sequence.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR029030; Caspase-like_dom_sf.
DR SUPFAM; SSF52129; SSF52129; 1.
PE 3: Inferred from homology;
KW Apoptosis; Hydrolase; Protease; Reference proteome; Thiol protease;
KW Zymogen.
FT PROPEP 1..?
FT /evidence="ECO:0000255"
FT /id="PRO_0000333664"
FT CHAIN ?..410
FT /note="Metacaspase-1"
FT /id="PRO_0000333665"
FT REGION 1..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..36
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..58
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 200
FT /evidence="ECO:0000250"
FT ACT_SITE 256
FT /evidence="ECO:0000250"
SQ SEQUENCE 410 AA; 45081 MW; CFDD68AAE0D7E101 CRC64;
MFPGSGRQTY QQQGYPPPQG APQYNYGPPQ GPPQGYYNGP PQGYNGPPQG PPPQNYNYGH
YGPPQGQGQG YGQGGPAPQM YNNNRQSGAM NDVSTAPQRF GNTDMTYQLS NCSGRKKALL
VGINYFGSSN ELRGCVNDIK NMSNFLNRRF GYSYDDMVIL TDDQNQRNKI PTKENIIRAM
QWLVKDARPN DSLVFHYSGH GGITKDLDGD EDEGYDEVIY PVDFQQAGHI VDDDMHAIMV
RPLPPGCKLT ALFDSCHSGT ALDLPFVYST KGVVKEPNLW KDAGTDAFGA FMQYERGNIG
GAISSIGGLL KKVTNSSSSN RQQVINIKAS PADVISISGC KDDQTSADAS INNNATGAMS
WAFIKTMTDM PEQSYLSLLN NMRTLLKEKY SQKPQLSSSH PQDMNIRFIM