ID A0A067BZM7_SAPPC Unreviewed; 423 AA.
AC A0A067BZM7;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Peptidase C1A papain C-terminal domain-containing protein {ECO:0000259|SMART:SM00645};
GN ORFNames=SPRG_15081 {ECO:0000313|EMBL:KDO19751.1};
OS Saprolegnia parasitica (strain CBS 223.65).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Saprolegnia.
OX NCBI_TaxID=695850 {ECO:0000313|EMBL:KDO19751.1, ECO:0000313|Proteomes:UP000030745};
RN [1] {ECO:0000313|EMBL:KDO19751.1, ECO:0000313|Proteomes:UP000030745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 223.65 {ECO:0000313|EMBL:KDO19751.1,
RC ECO:0000313|Proteomes:UP000030745};
RX PubMed=23785293;
RA Jiang R.H., de Bruijn I., Haas B.J., Belmonte R., Lobach L., Christie J.,
RA van den Ackerveken G., Bottin A., Bulone V., Diaz-Moreno S.M., Dumas B.,
RA Fan L., Gaulin E., Govers F., Grenville-Briggs L.J., Horner N.R.,
RA Levin J.Z., Mammella M., Meijer H.J., Morris P., Nusbaum C., Oome S.,
RA Phillips A.J., van Rooyen D., Rzeszutek E., Saraiva M., Secombes C.J.,
RA Seidl M.F., Snel B., Stassen J.H., Sykes S., Tripathy S., van den Berg H.,
RA Vega-Arreguin J.C., Wawra S., Young S.K., Zeng Q., Dieguez-Uribeondo J.,
RA Russ C., Tyler B.M., van West P.;
RT "Distinctive expansion of potential virulence genes in the genome of the
RT oomycete fish pathogen Saprolegnia parasitica.";
RL PLoS Genet. 9:E1003272-E1003272(2013).
CC -!- SIMILARITY: Belongs to the peptidase C1 family.
CC {ECO:0000256|ARBA:ARBA00008455}.
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DR EMBL; KK583336; KDO19751.1; -; Genomic_DNA.
DR RefSeq; XP_012209561.1; XM_012354171.1.
DR AlphaFoldDB; A0A067BZM7; -.
DR EnsemblProtists; KDO19751; KDO19751; SPRG_15081.
DR GeneID; 24136849; -.
DR KEGG; spar:SPRG_15081; -.
DR VEuPathDB; FungiDB:SPRG_15081; -.
DR OMA; QYMSGVY; -.
DR OrthoDB; 5472443at2759; -.
DR Proteomes; UP000030745; Unassembled WGS sequence.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd02248; Peptidase_C1A; 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; IPR025660; Pept_his_AS.
DR InterPro; IPR013128; Peptidase_C1A.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR039417; Peptidase_C1A_papain-like.
DR PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
DR PANTHER; PTHR12411:SF741; RE20049P; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000030745};
KW Signal {ECO:0000256|SAM:SignalP}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..423
FT /note="Peptidase C1A papain C-terminal domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018770868"
FT DOMAIN 138..351
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
FT REGION 346..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 423 AA; 46525 MW; DA28A24FD95845A6 CRC64;
MIHAATILVA ALATTAAAAD VFGQESLDLV REFEEWKASE VGQQAIESGF VPTVESNGRQ
EGAESEDAIQ LQRFQETKKI VDQLNKEHPE AEFSVHNPFA LLNETEFAAF VMKSFGNDDR
KLRAADHVAR ELTSAQREAS DVDWATHQCN GPVKHQGECG SCWTFSSTGQ AAFSHCLVTG
QRLDLSQQQL VSCARGAGNG CQGGWPWKAL DYIRETGVCM ESEYPYQSGN TKQDGQCYSC
NKQKLQIGRT VEIQGESALQ NALSSQPVQV VVEAGNNVWK NYKRGVIRQC PGARSDHAVL
AVGYGTKDGV QHFKIKNSWG TGWGEGGYMY LQRGVGRQGM CNVAEHPSYP EIGRRNDDNN
NNNDHNNNND NNNDDMNPTA APNDQCNGCD GCYYPYHGIC QQGYDAGNCQ MLAPYYGTVW
CGY
//