ID A0A0W8BVR8_PHYNI Unreviewed; 389 AA.
AC A0A0W8BVR8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Serine protease {ECO:0000256|RuleBase:RU004296};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU004296};
GN ORFNames=AM587_10001389 {ECO:0000313|EMBL:KUF79652.1}, AM587_10002409
GN {ECO:0000313|EMBL:KUF75928.1};
OS Phytophthora nicotianae (Buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4790 {ECO:0000313|EMBL:KUF75928.1, ECO:0000313|Proteomes:UP000052943};
RN [1] {ECO:0000313|EMBL:KUF75928.1, ECO:0000313|Proteomes:UP000052943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 0 {ECO:0000313|Proteomes:UP000052943}, and Race 0
RC {ECO:0000313|EMBL:KUF75928.1};
RA Liu H., Ma X., Yu H., Fang D., Li Y., Wang X., Wang W., Dong Y., Xiao B.;
RT "Genomes and virulence difference between two physiological races of
RT Phytophthora nicotianae.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S1B family.
CC {ECO:0000256|ARBA:ARBA00008764, ECO:0000256|RuleBase:RU004296}.
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:KUF75928.1}.
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DR EMBL; LNFO01005932; KUF75928.1; -; Genomic_DNA.
DR EMBL; LNFO01004753; KUF79652.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W8BVR8; -.
DR EnsemblProtists; KUF75928; KUF75928; AM587_10002409.
DR EnsemblProtists; KUF79652; KUF79652; AM587_10001389.
DR OMA; PEGAFFC; -.
DR Proteomes; UP000052943; Unassembled WGS sequence.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR008256; Peptidase_S1B.
DR PANTHER; PTHR36234; LYSYL ENDOPEPTIDASE; 1.
DR PANTHER; PTHR36234:SF5; LYSYL ENDOPEPTIDASE; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00839; V8PROTEASE.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU004296};
KW Protease {ECO:0000256|RuleBase:RU004296, ECO:0000313|EMBL:KUF75928.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000052943};
KW Serine protease {ECO:0000256|RuleBase:RU004296};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
SQ SEQUENCE 389 AA; 42381 MW; 95708F9B5EB32A4E CRC64;
MLSLTTAQEH FSRRNNATNT IAGIQAENFG VGCGGDMEYP STDEFTKQPR FAYLITNPLA
DFVAVHFKHF NLPENDYVQI RAADPASTEK QILRFQGNES SGDFYAPALS TVAVIVELFT
EIADFPQAVD ASECLGFSVD RYQYLARGSS LNGAKEEVCG FDNSREASCY KSFTEVFQAS
KAVARLLTKK PEGAFYCTGW LLGSEGHLMT NHHCISSQIH ADNTEFEFDA EGSVCSISCA
NARACSGSIR AKSATLIYAD DALDYALLKL PVDLSVEYGY LRLRTSGAEL SERVYMPEHP
AGWGKRIAMK TDSGWGTVKS LTMGGCATDQ VAYYLDTQGG SSGSPVLSWS DNTVIALHHC
GGCPNTAINS YKLVNDMKWR NILPANATV
//
