ID A0A165EHR5_9APHY Unreviewed; 590 AA.
AC A0A165EHR5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Peptidase C14 caspase domain-containing protein {ECO:0000259|Pfam:PF00656};
GN ORFNames=LAESUDRAFT_758880 {ECO:0000313|EMBL:KZT07073.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT07073.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT07073.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT07073.1,
RC ECO:0000313|Proteomes:UP000076871};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SIMILARITY: Belongs to the peptidase C14B family.
CC {ECO:0000256|ARBA:ARBA00009005}.
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DR EMBL; KV427621; KZT07073.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165EHR5; -.
DR InParanoid; A0A165EHR5; -.
DR OrthoDB; 555417at2759; -.
DR Proteomes; UP000076871; 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:UP000076871}.
FT DOMAIN 18..222
FT /note="Peptidase C14 caspase"
FT /evidence="ECO:0000259|Pfam:PF00656"
FT REGION 242..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 590 AA; 65611 MW; 1AFA5FC31CB4AB64 CRC64;
MTVGAPVAAV NAEVPSPRKK ALIVGNNGDD LQGPRRDAES FKGLLIHKYK FKAEDIMMMV
SNGDDPLMDP SRRENVIREL KALVRDARKD DSFVFFYAGH STQMTCRHGT EDDGLDEAIW
LKNGSGPVTE NDYILDNVLR EILVDTLLPL GAYMFSFFDA CTSGTLMDLD HDKCNQRQFE
KTYHPKRTIP PNTCWLEQPL CISTSHNLFS PDRSNVSSPV SMQSPQAQPL ARSIVATPLT
KTRVSSPLAR GAVQPSEPHS RRSNRVTTER SAQTTPAHFH HDTRTSVGRP TMNSDIPYTP
IATRLQHRST ANKENMQVED TCRHPKRRMS TSERLSMNTR KDPDRRRRAT SSATFMQSVI
PPPVPSTSLS RSSGSVGLHA GTPAKRRTAE DVWRDVTSSS PVPYCDSPPG SPLNASLSVR
REASAGVTFA EAASMVENQS RVKCTGFCHD QLLENNVGSG QGARIVSISA CADGQRTWEA
GSRSTTQFLV HYLRMDLDLP YTECKVANID VYVLVGTTPK PTWRQVWAHL STRGDTFIHT
GREKYREWHR EDSMPTYQDP LISSDSPLIL DSPFTLINPL SLEDAESTQP
//
