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Database: UniProt
Entry: M2R1X0_CERS8
LinkDB: M2R1X0_CERS8
Original site: M2R1X0_CERS8 
ID   M2R1X0_CERS8            Unreviewed;       465 AA.
AC   M2R1X0;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Peptidase C14 caspase domain-containing protein {ECO:0000259|Pfam:PF00656};
GN   ORFNames=CERSUDRAFT_88205 {ECO:0000313|EMBL:EMD32242.1};
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:EMD32242.1, ECO:0000313|Proteomes:UP000016930};
RN   [1] {ECO:0000313|EMBL:EMD32242.1, ECO:0000313|Proteomes:UP000016930}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B {ECO:0000313|EMBL:EMD32242.1,
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; KB445812; EMD32242.1; -; Genomic_DNA.
DR   AlphaFoldDB; M2R1X0; -.
DR   HOGENOM; CLU_029389_6_2_1; -.
DR   OrthoDB; 1610358at2759; -.
DR   Proteomes; UP000016930; Unassembled WGS sequence.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.50.12660; -; 1.
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.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000016930}.
FT   DOMAIN          20..412
FT                   /note="Peptidase C14 caspase"
FT                   /evidence="ECO:0000259|Pfam:PF00656"
FT   REGION          269..288
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   465 AA;  53759 MW;  26B7F3DE4A93B4DF CRC64;
     MAPLRHPRRR SSSVPTRPPR KKALIIGIQY SRTAPQYRED WQPLLGPHKD ADAFRRLLMN
     RYEYKEEDII LMVDDGKHKD LEPTRAHLLR EFRSLVRQAR SGDQFVLFYA GHSEQIPNRT
     HTEDDGRDEA ILPKDHHGLD EKHLIRDSSL RRILVDPLPA GARLTAIFDS CHSGTMLDLP
     HYNCNKVESR ENSFEGKWSR NFPQRKNALP HGTSPHESHS AHEAYARGTA TTMRMIEAER
     KLSGDIEMME RTYRSSVPAA RRAKSLMGIP GRRDWDSPGL PSQSPHTVKR HTESCVLIPE
     DEYISSPLKT SYVPMSFLED REERMEYAEP EEMRQCRSPT SSVRECDGSC HVHDTDADDS
     RKADVISLAA CRDWQLTYEN CKGDCSFTQG LVAYLDVNPH PTYQELVRYI SQERSRILRL
     VCEQFTRELE RTAASEKHSF REMLTFSRPI LGSERKLDME SRFDL
//
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