ID A0A178DWE6_9PLEO Unreviewed; 879 AA.
AC A0A178DWE6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Cysteine proteinase {ECO:0000313|EMBL:OAL47632.1};
GN ORFNames=IQ07DRAFT_572420 {ECO:0000313|EMBL:OAL47632.1};
OS Pyrenochaeta sp. DS3sAY3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC Pyrenochaeta.
OX NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL47632.1, ECO:0000313|Proteomes:UP000077535};
RN [1] {ECO:0000313|EMBL:OAL47632.1, ECO:0000313|Proteomes:UP000077535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL47632.1,
RC ECO:0000313|Proteomes:UP000077535};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KV441651; OAL47632.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178DWE6; -.
DR STRING; 765867.A0A178DWE6; -.
DR InParanoid; A0A178DWE6; -.
DR OrthoDB; 142935at2759; -.
DR Proteomes; UP000077535; Unassembled WGS sequence.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00044; CysPc; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR PANTHER; PTHR10183; CALPAIN; 1.
DR PANTHER; PTHR10183:SF425; CALPAIN-5; 1.
DR Pfam; PF00648; Peptidase_C2; 1.
DR SMART; SM00230; CysPc; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00239};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU00239};
KW Reference proteome {ECO:0000313|Proteomes:UP000077535};
KW Thiol protease {ECO:0000256|PROSITE-ProRule:PRU00239}.
FT DOMAIN 177..472
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT REGION 664..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..694
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..750
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..772
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..826
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 205
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 385
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 410
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00239"
SQ SEQUENCE 879 AA; 97347 MW; FDF99924685B8B14 CRC64;
MASVSSDDSD VGKPQEAINE FWENLITKKP TKVTKVFPPS LYAHLLPTPR KPGTVTGKNA
AESYLAAAAD CRARVKRIVR ECHRTNEKFT DPDFDIEDLR DKNCLEGLKH WLKDTAVPNA
SSTSASQLGN AISTLIQSDV LMQNAAPFDL IAAAKLLNPP SSDDDDEDSA DPGSVHRIDW
IFEKPQFEID GFSSSDLCQG SNGDCWFIAA VATICSNPEL INKVCVERDE ECGVYGFVFY
RDGEWIWTVV DDNLYLTFND FDAFGDRYDP TGIKEKKYKK NNQTGSEALY FASCADPNET
WLPLLEKAYA KVHGDYAAIA GGFSGEAVED LTGGVTTKIL TDRILSKERL WKELLQANKQ
FLFSASSPGS YGDDSSARRG LALSHAYSVI EAVDAEGEDG KNNRLVLIRN PWGKRANAAM
GEWTGPWADG SSEWTPYWMK KLNHKFGDDG LFWMSYEDLL KRFDLLDRTR LFDEEWTVVQ
HWTSVSVAWV TGYLNNKFRV EIKKSGPTVF VLCQLDDRYF RGLEGKYDFD LHFILQEENA
EAGDHIVRAR GAWFGNRSIS AEIDLEAGVY EVLPKIVASR DADALDVQEV VVKVAERNPQ
KLRQIGLNYD IANAKGAVEL TEEEKKKKEQ KKKEAAEKKK KEKEQEEKDK ADFDAWKKEE
KAEYEAWKKE KKENDEKEKP KEDAPKDSAS KKEETEAAAT AVVADFTKTL KEDAATKPDV
KPTDLPIRAK DSDPKEKESA AAPKIKVDEA SDSDDDDDDD EEEEEDGDDT PDDDGVTSQR
RGPPGPPSVA SGVSAVSGFR AGYGNRPDSV YGGEAPPPPP PPAAAGNADE IKPWNAVCVL
GLRVYSKDPD VSIKLVKPKD AEEAAILDVD GGTAAGATM
//