ID M2R3M5_CERS8 Unreviewed; 475 AA.
AC M2R3M5;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Peptidase C14 caspase domain-containing protein {ECO:0000259|Pfam:PF00656};
GN ORFNames=CERSUDRAFT_118087 {ECO:0000313|EMBL:EMD33516.1};
OS Ceriporiopsis subvermispora (strain B) (White-rot fungus) (Gelatoporia
OS subvermispora).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Gelatoporiaceae; Gelatoporia.
OX NCBI_TaxID=914234 {ECO:0000313|EMBL:EMD33516.1, ECO:0000313|Proteomes:UP000016930};
RN [1] {ECO:0000313|EMBL:EMD33516.1, ECO:0000313|Proteomes:UP000016930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B {ECO:0000313|EMBL:EMD33516.1,
RC ECO:0000313|Proteomes:UP000016930};
RX PubMed=22434909; DOI=10.1073/pnas.1119912109;
RA Fernandez-Fueyo E., Ruiz-Duenas F.J., Ferreira P., Floudas D.,
RA Hibbett D.S., Canessa P., Larrondo L.F., James T.Y., Seelenfreund D.,
RA Lobos S., Polanco R., Tello M., Honda Y., Watanabe T., Watanabe T.,
RA Ryu J.S., Kubicek C.P., Schmoll M., Gaskell J., Hammel K.E., St John F.J.,
RA Vanden Wymelenberg A., Sabat G., Splinter BonDurant S., Syed K.,
RA Yadav J.S., Doddapaneni H., Subramanian V., Lavin J.L., Oguiza J.A.,
RA Perez G., Pisabarro A.G., Ramirez L., Santoyo F., Master E., Coutinho P.M.,
RA Henrissat B., Lombard V., Magnuson J.K., Kuees U., Hori C., Igarashi K.,
RA Samejima M., Held B.W., Barry K.W., LaButti K.M., Lapidus A.,
RA Lindquist E.A., Lucas S.M., Riley R., Salamov A.A., Hoffmeister D.,
RA Schwenk D., Hadar Y., Yarden O., de Vries R.P., Wiebenga A., Stenlid J.,
RA Eastwood D., Grigoriev I.V., Berka R.M., Blanchette R.A., Kersten P.,
RA Martinez A.T., Vicuna R., Cullen D.;
RT "Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete
RT chrysosporium provide insight into selective ligninolysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:5458-5463(2012).
CC -!- SIMILARITY: Belongs to the peptidase C14B family.
CC {ECO:0000256|ARBA:ARBA00009005}.
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DR EMBL; KB445806; EMD33516.1; -; Genomic_DNA.
DR AlphaFoldDB; M2R3M5; -.
DR HOGENOM; CLU_029389_0_2_1; -.
DR OrthoDB; 1077459at2759; -.
DR Proteomes; UP000016930; 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:UP000016930};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 179..465
FT /note="Peptidase C14 caspase"
FT /evidence="ECO:0000259|Pfam:PF00656"
FT REGION 1..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..30
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..78
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..153
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 475 AA; 51199 MW; 0EA6DE8A378B65AA CRC64;
MWNDPGSGYP GNSRYGPPSG PPPGGNAFGF PSPDVPPQGT RGFTPGYAPS YGPPPGAPPS
GYGGPPPFQP PAGPPPDAGY PGQGYEYHHH HHHHHHPEGG YAPPPGPPLS GYGGPPPIPT
RQYEFQPPPG PPGEYGTYAA PDGPPPPPPT SEQRYGPVFE GANHQQQQPF FQYSQCTGKR
KALCIGINYI GQSAELKGCI NDAHNVKRFL IDDYGYLEDD IVMLTDDAPH HRQIPTQQNM
LAAMEWLVRD AQPHDSLFFH YSGHGGQTKD LDGDEEDGYD EVIYPVDFQT SGQIIDDVLH
DVLVKPLPPG CRLTAIFDSC HSGSALDLPY LYSTEGKIKE PNLAREAGQG LLNAVSSYAR
GDMTGVFGSM KGLLQTVSSG GSSAARTRTQ QTKTSPADVI SWSGCKDSQT SADTFEDGQA
TGAMSYAFIS TLRQNRQQSY QQLLTSIRGI LQGKYSQIPQ LSSSHPMDTR LLFIC
//
