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Database: UniProt
Entry: A0A163ATA8_DIDRA
LinkDB: A0A163ATA8_DIDRA
Original site: A0A163ATA8_DIDRA 
ID   A0A163ATA8_DIDRA        Unreviewed;      1076 AA.
AC   A0A163ATA8;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Calcium-dependent cysteine-type endopeptidase {ECO:0000313|EMBL:KZM21373.1};
GN   ORFNames=EKO05_009894 {ECO:0000313|EMBL:KAF9703341.1}, ST47_g7483
GN   {ECO:0000313|EMBL:KZM21373.1};
OS   Didymella rabiei (Chickpea ascochyta blight fungus) (Mycosphaerella
OS   rabiei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Ascochyta.
OX   NCBI_TaxID=5454 {ECO:0000313|EMBL:KZM21373.1, ECO:0000313|Proteomes:UP000076837};
RN   [1] {ECO:0000313|EMBL:KZM21373.1, ECO:0000313|Proteomes:UP000076837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ArDII {ECO:0000313|EMBL:KZM21373.1,
RC   ECO:0000313|Proteomes:UP000076837};
RX   PubMed=27091329; DOI=10.1038/srep24638;
RA   Verma S., Gazara R.K., Nizam S., Parween S., Chattopadhyay D., Verma P.K.;
RT   "Draft genome sequencing and secretome analysis of fungal phytopathogen
RT   Ascochyta rabiei provides insight into the necrotrophic effector
RT   repertoire.";
RL   Sci. Rep. 6:24638-24638(2016).
RN   [2] {ECO:0000313|EMBL:KAF9703341.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Me14 {ECO:0000313|EMBL:KAF9703341.1};
RA   Syme R.A., Farfan-Caceres L., Lichtenzveig J.;
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:KAF9703341.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Me14 {ECO:0000313|EMBL:KAF9703341.1};
RX   PubMed=32345704; DOI=10.1534/g3.120.401265;
RA   Shah R.M., Williams A.H., Hane J.K., Lawrence J.A., Farfan-Caceres L.M.,
RA   Debler J.W., Oliver R.P., Lee R.C.;
RT   "Reference Genome Assembly for Australian Ascochyta rabiei Isolate
RT   ArME14.";
RL   G3 (Bethesda) 10:2131-2140(2020).
RN   [4] {ECO:0000313|EMBL:KAF9703341.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Me14 {ECO:0000313|EMBL:KAF9703341.1};
RA   Shah R.M., Williams A.H., Hane J.K., Lawrence J.A., Farfan-Caceres L.M.,
RA   Debler J.W., Oliver R.P., Lee R.C.;
RL   Submitted (MAY-2020) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase C2 family.
CC       {ECO:0000256|ARBA:ARBA00007623}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KZM21373.1}.
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DR   EMBL; RYYQ01000021; KAF9703341.1; -; Genomic_DNA.
DR   EMBL; JYNV01000246; KZM21373.1; -; Genomic_DNA.
DR   STRING; 5454.A0A163ATA8; -.
DR   OrthoDB; 142935at2759; -.
DR   Proteomes; UP000076837; Unassembled WGS sequence.
DR   GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IEA:InterPro.
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; IPR022684; Calpain_cysteine_protease.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR   PANTHER; PTHR10183; CALPAIN; 1.
DR   PANTHER; PTHR10183:SF379; CALPAIN-A-RELATED; 1.
DR   Pfam; PF00648; Peptidase_C2; 2.
DR   PRINTS; PR00704; CALPAIN.
DR   SMART; SM00230; CysPc; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS50203; CALPAIN_CAT; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00239};
KW   Protease {ECO:0000256|PROSITE-ProRule:PRU00239};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076837};
KW   Thiol protease {ECO:0000256|PROSITE-ProRule:PRU00239}.
FT   DOMAIN          161..450
FT                   /note="Calpain catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50203"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          589..655
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          670..721
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          770..940
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          993..1076
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        589..621
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        635..655
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        670..686
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        847..866
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        893..917
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1040..1055
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        190
FT                   /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00239"
FT   ACT_SITE        374
FT                   /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00239"
FT   ACT_SITE        394
FT                   /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00239"
SQ   SEQUENCE   1076 AA;  121927 MW;  FD10E6AFA216E287 CRC64;
     MTMASQVSPN DFINITRPQS RAPSMNGEAF AAASRPRLPV KKQAPQKSID DFWNTFTTKH
     PGKIFTILPD NLYAKRAAAH TPKGSIPGKN ALASYEEAVQ SCKTKVAKIV KECRRLNQKY
     RDPHFDIEAD FKRSQASPDT PPDCLTSLDK EQSEFQPMSV KRVEDIFENP QFFIEGATAN
     DVRQGNDGDC WFMSALATIS NKEELIQRVC VARDEQVGVY GFVFHRDGEW ISEVIDDKLY
     LIKEDFDEAK IERYHWLELQ NRKSPDEEYR TVMQTGSRAL YFAQCSDSNE TWLPLLEKAF
     AKAHGDYSAI DGGFVGEGIE DLTGGVTSEV FATDILDKDK FWHDELMNVN KTFLFGCGQM
     GGIYGARKGI QEKHAYSIME AREIDGQRLL KLRNPWGRTE WTGRWSDGSE EWTPEWMQKL
     NHKFGDDGVF WISYRDLLRN YQHFDRTRLF GPEWTVSQQW TSVNVPWSVD YLETKFKVHL
     EKPSPVVIVL SQLDDRYYQG LEGQYEFHLQ FRLHKDDEDE YIVRSNGTYY MKRSVSTELD
     LEAGNYTVLL KIKATRSPNP TPDEVIRATC TKRREKLLAT GLSYDLAHAK GQFREHEKEK
     DRQQREHKSD RKKADARRAH ERERKFRRRQ KLREQKKAAK ETRKLNRPGE MREIEKRLQD
     LTGLGIAVEE ENRTEGEEET KPGHPAVTRH RRAASASVVG ERSPSPGGGF QGRGGYNRGR
     DGYNAALPGA LQGRGGYNRN EQHGTAMAEA LALQGRGGYQ AANNGFQGRG GYNQNMPGEL
     QGRGGYNAEL PGSYQGRDGY NGRDGYNGRD GYNGRDGYNG RDGYNEGQTT ESPVPTPQPT
     PQSQPEEFRP GTPGQRTYSP QPDRRSRISP APSRRATLSP IPGVRPAIHI TRGRGTSVSS
     LRTRHGTYSP NEISDDSSWD SDLADSLDSE ASDNERDSPR LISQDQIRYY HQNGRSYYTI
     EDEDEFERDP WNAVCVIGLR VFSKDADVSI EVQNGGPEKR KDSDAESVAS VSTIRRRQKE
     LDVDDSAADA TSPMRTRNNM DEALKGEEKR AAEAELVSHV GTMPAGNELN RQDTLS
//
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