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Database: UniProt
Entry: H3GBY0_PHYRM
LinkDB: H3GBY0_PHYRM
Original site: H3GBY0_PHYRM 
ID   H3GBY0_PHYRM            Unreviewed;       574 AA.
AC   H3GBY0;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Peptidase C1A papain C-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
OS   Phytophthora ramorum (Sudden oak death agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=164328 {ECO:0000313|EnsemblProtists:Phyra72858, ECO:0000313|Proteomes:UP000005238};
RN   [1] {ECO:0000313|Proteomes:UP000005238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pr102 {ECO:0000313|Proteomes:UP000005238};
RX   PubMed=16946064; DOI=10.1126/science.1128796;
RA   Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H., Aerts A.,
RA   Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA   Damasceno C.M., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA   Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA   Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.K.,
RA   McDonald W.H., Medina M., Meijer H.J., Nordberg E.K., Maclean D.J.,
RA   Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA   Rose J.K., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA   Smith B.M., Sobral B.W., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA   Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT   "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT   of pathogenesis.";
RL   Science 313:1261-1266(2006).
RN   [2] {ECO:0000313|EnsemblProtists:Phyra72858}
RP   IDENTIFICATION.
RC   STRAIN=Pr102 {ECO:0000313|EnsemblProtists:Phyra72858};
RG   EnsemblProtists;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the peptidase C1 family.
CC       {ECO:0000256|ARBA:ARBA00008455}.
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DR   EMBL; DS565998; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; H3GBY0; -.
DR   STRING; 164328.H3GBY0; -.
DR   EnsemblProtists; Phyra72858; Phyra72858; Phyra72858.
DR   VEuPathDB; FungiDB:PSURA_42145; -.
DR   eggNOG; KOG1543; Eukaryota.
DR   HOGENOM; CLU_012184_11_0_1; -.
DR   InParanoid; H3GBY0; -.
DR   OMA; KAFHHFK; -.
DR   Proteomes; UP000005238; Unassembled WGS sequence.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR   CDD; cd02248; Peptidase_C1A; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR013128; Peptidase_C1A.
DR   InterPro; IPR000668; Peptidase_C1A_C.
DR   InterPro; IPR039417; Peptidase_C1A_papain-like.
DR   InterPro; IPR013201; Prot_inhib_I29.
DR   PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
DR   PANTHER; PTHR12411:SF642; PRO-CATHEPSIN H; 1.
DR   Pfam; PF08246; Inhibitor_I29; 1.
DR   Pfam; PF00112; Peptidase_C1; 1.
DR   SMART; SM00848; Inhibitor_I29; 1.
DR   SMART; SM00645; Pept_C1; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005238};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   TRANSMEM        52..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          296..352
FT                   /note="Cathepsin propeptide inhibitor"
FT                   /evidence="ECO:0000259|SMART:SM00848"
FT   DOMAIN          380..571
FT                   /note="Peptidase C1A papain C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00645"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..29
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   574 AA;  64709 MW;  B998B7230EDED138 CRC64;
     MGKKKTKATL PTEDLEASAS ESLLPESSSE YHRLEQQENA ILRRQRSKSR KIWCAIIALT
     TGILGFIAVL AILRAVEDAN HLAPTKRPVF PTQYEASVTF NMPYMDMVEP LYVHVDEKKG
     LQKLSYYGGT DVYIYNTSGT SYQIIPVIRE RKCFKSGSES LQRIFPNMTL FEPQHGVFLV
     EGRPCFSWKF VTKLHEPTED GLLGEYTLYV DQKTERPVRF HYVGRNGMLG GSHIDEYHLD
     YIYVREGPVD ENVFLSLPAS MNCTEMPGDD SGPSRNPKED IHLLMPEGTT RKKEIFDEFS
     TSHSKVYDDE AEAVQRMATF HHNRRFINAE NRKGLSYHLE LNQFADLNHE ERLTLHRSSR
     VKRAKDNGAM AVHELSSFED PGDMDWRTKG AVTPVKDQAR LEPWKQNLLD CSWDYGNNAC
     DGGLDYQAYE WIMANGGLET TATYGSYRNA PDYCHFNVDN AIGRMTGFVN VTSVVALNDA
     LATIGPLSVS IDATLPSFYF YGGGYYDDVE CKSDVDSLDH SVLAVGVTTH NGQKYTLVKN
     SWSTHWGEDG YVKISQKDNL CGVATAATYP VLAD
//
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