MCA1_LODEL
ID MCA1_LODEL Reviewed; 449 AA.
AC A5DZS4;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Metacaspase-1;
DE EC=3.4.22.-;
DE Flags: Precursor;
GN Name=MCA1; ORFNames=LELG_02861;
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC YB-4239;
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; CH981526; EDK44682.1; -; Genomic_DNA.
DR RefSeq; XP_001526303.1; XM_001526253.1.
DR AlphaFoldDB; A5DZS4; -.
DR SMR; A5DZS4; -.
DR STRING; 379508.A5DZS4; -.
DR EnsemblFungi; EDK44682; EDK44682; LELG_02861.
DR GeneID; 5233429; -.
DR KEGG; lel:LELG_02861; -.
DR VEuPathDB; FungiDB:LELG_02861; -.
DR eggNOG; KOG1546; Eukaryota.
DR HOGENOM; CLU_029389_0_1_1; -.
DR InParanoid; A5DZS4; -.
DR OMA; GMQQFGH; -.
DR OrthoDB; 821819at2759; -.
DR Proteomes; UP000001996; 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_0000333652"
FT CHAIN ?..449
FT /note="Metacaspase-1"
FT /id="PRO_0000333653"
FT REGION 1..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..57
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 232
FT /evidence="ECO:0000250"
FT ACT_SITE 293
FT /evidence="ECO:0000250"
SQ SEQUENCE 449 AA; 49227 MW; C3D013E3A2288702 CRC64;
MFPGQGRHTY GGQQQLLQLQ QYNYGPPQGP PPNGYGPPPG PPPNGYGPPP GPPPQNSWGY
GNPSGTQSSN QQRYQGQQSG QQNYNGGYQR PSQPPPQQSG NQRGQPGQNG EPDYGHQYGS
GQYSRPPTNQ QSFGVENYNY QYSACNGRKK ALLVGINYIG TANELRGPIN DVNNVEQFLL
THGFKSDDIV KLTDDQRVQR AIPTRQNILD AIQWLVKDAR PNDSLFFHYS GHGGQTEDQP
DQYGNYDEDD GYDEVIYPLD FQTNGFIVDD LLHDMMVKTL PPGCRMTALF DSCHSGSVLD
LPYMYSTKGV LKEPNVMKEA GQGLLQAAMS YATGNSAGIF KGLSSSVKSF MNQGRSSQAN
EYSKQTKTAA CDAISLSGCK DDQTSADSSI GGQATGAMSY AFLTVMNQNP NQSYLSLLQN
MRTILQSKYS QKPQLTASHP IDCNLQFIF
