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Database: UniProt
Entry: W2KJ93_PHYPR
LinkDB: W2KJ93_PHYPR
Original site: W2KJ93_PHYPR 
ID   W2KJ93_PHYPR            Unreviewed;      1231 AA.
AC   W2KJ93;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=Calpain catalytic domain-containing protein {ECO:0000259|PROSITE:PS50203};
GN   ORFNames=L917_15152 {ECO:0000313|EMBL:ETL85238.1};
OS   Phytophthora parasitica (Potato buckeye rot agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=4792 {ECO:0000313|EMBL:ETL85238.1};
RN   [1] {ECO:0000313|EMBL:ETL85238.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CHvinca01 {ECO:0000313|EMBL:ETL85238.1};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica CHvinca01.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00239}.
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DR   EMBL; KI681630; ETL85238.1; -; Genomic_DNA.
DR   EMBL; KI681630; ETL85239.1; -; Genomic_DNA.
DR   EMBL; KI681630; ETL85240.1; -; Genomic_DNA.
DR   EnsemblProtists; ETL85238; ETL85238; L917_15152.
DR   EnsemblProtists; ETL85239; ETL85239; L917_15152.
DR   EnsemblProtists; ETL85240; ETL85240; L917_15152.
DR   VEuPathDB; FungiDB:PPTG_04889; -.
DR   Proteomes; UP000054423; Unassembled WGS sequence.
DR   GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR   PANTHER; PTHR46298; ANDROGLOBIN; 1.
DR   PANTHER; PTHR46298:SF1; ANDROGLOBIN; 1.
DR   Pfam; PF00648; Peptidase_C2; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS50203; CALPAIN_CAT; 1.
PE   4: Predicted;
FT   DOMAIN          338..405
FT                   /note="Calpain catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50203"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          115..186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          470..491
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1004..1050
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..35
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        138..152
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1007..1046
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1231 AA;  137591 MW;  F044476232851C67 CRC64;
     MPPKKPPSKL TAQGSTLNPP PTAHNYRQSV QAPNLPPSDS IPPLWKPNVV PNEVFPEWMD
     PAALPADHWG TVEQPFEDPL APENLVLPKE VIEFKDSIMW KRPSQFLPVI VETPVVHATP
     PPPTPEPKAT GKKGAAPAAK KGEPEPQKKP PPPKHAHVFV PKSEKAGTTT SSSSLPSTAE
     HHHDHTLRIP RDFQRRWSVE QLEALEAWTK EEERIELEQQ HRERMYMGFE DAIAYIVNDR
     PRDLLAEVDF DADDLIDDGQ DEDDALTTNM DVSNATSPWG VMPPPRIEIA PNAVYKPEIP
     HGDVIHADMA SYFRIVEQLY DSSKTSNNCM APFLWQAIYP QDNTGQPVYN PGGKYSVKLF
     VFGRWRRIDI DDKLPLDADG KVIYLASSMK NEIWPSLLVK ALYKVAYWLH PHRHETELER
     QSSTDGMCQN VIQTILALTS WKVSLWQPEA STKFSENVFH QLRQYILSSE KPDEASEQPT
     ESESVANSTT DVSPAVTETL ATVNALMPRA VICCTGINRA AGMVFGEIVL VTGVVGDTGS
     TTFKVVRQGS PATISEETND VNELVFLLVH QVLQYSDTFI REWMPNPEPP PEGVEDTRAP
     LVPFETPRVQ FVVITARDSI PEQPPGDNLS DISHMIQEPV NLVASLTPVQ SPEKYDQDLD
     NLSKPSVLMA THLVVDPNGS VILIEEIEKK ASTSSLPAIL PLNSTFAEYI SVPLVGKSKI
     VYRVYPQKSL RYGYSLVVES NQKVSFQDAP TYWRSLSNFH VIECDGAYPV MLPGTWNILF
     KQSFELVPPT HEDGDKEPSP ELRIDLYLSE EMLSSFTHIS IVNDATGEVK KASTLCTKVS
     LPSVSNLASN APIAYTMIID CAPGNFHVRE GKWKLTLASD WDFTKPTTHE MKITQFEGVY
     EPNKPLLCFR DVIMAPKTSI WTSFQLQLLS DGAVVNTLAA KLEVFDLGMN QTQRISEISS
     KGEVRLLQLP CVTAADGQSQ SDDKRGYIIQ GSIDRTTCIV PDELQSRRPF RNNSNRPSKE
     LTTTSVDENT SLEGNSGVSP PGSARSSRPS GIKWRLNCWS SEDVKLQADN AKELQFEAIR
     ASWAEKAVDR NTNGAVSRLL YLGKLEEAEA RMKQDNMTDE QIAKVRNRFE WIQAVRKAEG
     VCESYLEEVA GSEEKLLSKE ELDESKRLLL ERIGAVEADK EQRRVARATA KEERAKELKN
     MVRSVIDRRA ISLKKQQELK RQLAALQTQS A
//
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