MCA1B_ASPTN
ID MCA1B_ASPTN Reviewed; 378 AA.
AC Q0CQL9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Metacaspase-1B;
DE EC=3.4.22.-;
DE Flags: Precursor;
GN Name=casB; ORFNames=ATEG_04015;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476598; EAU35817.1; -; Genomic_DNA.
DR RefSeq; XP_001213193.1; XM_001213193.1.
DR AlphaFoldDB; Q0CQL9; -.
DR SMR; Q0CQL9; -.
DR STRING; 341663.Q0CQL9; -.
DR EnsemblFungi; EAU35817; EAU35817; ATEG_04015.
DR GeneID; 4318443; -.
DR VEuPathDB; FungiDB:ATEG_04015; -.
DR eggNOG; KOG1546; Eukaryota.
DR HOGENOM; CLU_029389_3_1_1; -.
DR OMA; PTKANMI; -.
DR OrthoDB; 821819at2759; -.
DR Proteomes; UP000007963; 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_0000333634"
FT CHAIN ?..378
FT /note="Metacaspase-1B"
FT /id="PRO_0000333635"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 169
FT /evidence="ECO:0000250"
FT ACT_SITE 225
FT /evidence="ECO:0000250"
SQ SEQUENCE 378 AA; 41709 MW; 144E8AD19A6DDC37 CRC64;
MCSPPPYPPQ GHHYPPSPHG SYYSPTPYGA APSPPQSSSP HPRGYHSPSP SWGQLPPRPP
QEAQSFGGGA PSNYRFQYSA CTGRRKALLI GINYIGQPNQ LRGCINDVAN VSRYLNERCR
YRREDMVILT DDQENPLSIP TKNNILRAMQ WLVKDAQPND SLFIHFSGHG GRTPDLDGDE
EDGYDDVIYP VDYRTAGHIV DDEMHAIMVR PLRPGVRLTA IFDSCHSGTA LDLPYVYSTQ
GVLKEPNLAK EAAMDLFSAI SSYGQGDLTG MAKTAIGFFK KAAIGDSARQ RTVMTKTSPA
DVVMFSGSKD TQTSADTFQD GEARGALSWA FVKTLQERPH QSYLQLLNSI RAELEGKYTQ
KPQLSCSHPL DVNLLFVM