ID A0A1Z5KL94_FISSO Unreviewed; 444 AA.
AC A0A1Z5KL94;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Serine protease {ECO:0000256|RuleBase:RU004296};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU004296};
GN ORFNames=FisN_9Lh366 {ECO:0000313|EMBL:GAX27046.1};
OS Fistulifera solaris (Oleaginous diatom).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Bacillariophyceae; Bacillariophycidae; Naviculales; Naviculaceae;
OC Fistulifera.
OX NCBI_TaxID=1519565 {ECO:0000313|EMBL:GAX27046.1, ECO:0000313|Proteomes:UP000198406};
RN [1] {ECO:0000313|EMBL:GAX27046.1, ECO:0000313|Proteomes:UP000198406}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JPCC DA0580 {ECO:0000313|EMBL:GAX27046.1,
RC ECO:0000313|Proteomes:UP000198406};
RX PubMed=25634988; DOI=10.1105/tpc.114.135194;
RA Tanaka T., Maeda Y., Veluchamy A., Tanaka M., Abida H., Marechal E.,
RA Bowler C., Muto M., Sunaga Y., Tanaka M., Yoshino T., Taniguchi T.,
RA Fukuda Y., Nemoto M., Matsumoto M., Wong P.S., Aburatani S., Fujibuchi W.;
RT "Oil accumulation by the oleaginous diatom Fistulifera solaris as revealed
RT by the genome and transcriptome.";
RL Plant Cell 27:162-176(2015).
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC {ECO:0000256|ARBA:ARBA00007664}.
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:GAX27046.1}.
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DR EMBL; BDSP01000252; GAX27046.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z5KL94; -.
DR InParanoid; A0A1Z5KL94; -.
DR OrthoDB; 3606464at2759; -.
DR Proteomes; UP000198406; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00104; KAZAL_FS; 1.
DR Gene3D; 3.30.60.30; -; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR008256; Peptidase_S1B.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR PANTHER; PTHR15462; SERINE PROTEASE; 1.
DR PANTHER; PTHR15462:SF8; SERINE PROTEASE; 1.
DR Pfam; PF07648; Kazal_2; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00839; V8PROTEASE.
DR SMART; SM00280; KAZAL; 1.
DR SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS51465; KAZAL_2; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU004296};
KW Protease {ECO:0000256|RuleBase:RU004296};
KW Reference proteome {ECO:0000313|Proteomes:UP000198406};
KW Serine protease {ECO:0000256|RuleBase:RU004296};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU004296};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|RuleBase:RU004296"
FT CHAIN 29..444
FT /note="Serine protease"
FT /evidence="ECO:0000256|RuleBase:RU004296"
FT /id="PRO_5011825387"
FT DOMAIN 28..76
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
SQ SEQUENCE 444 AA; 49001 MW; FCC5666AF508BCDA CRC64;
MPSRTFLSLY SHSILLLILS LTLSSSQSSS SYDCENEGCS WETVPPVCGV NGVTYANECL
AYCQNIEIAF IGPCSESGSI ASTPYDDGIN ATISIMQRFQ KENFMLTERR NLADLVLPEY
NPTFHSEMRK DEIPLEQQPM LWSRFTSDGY VYTAVVTDES NKRFLQELPT NYESHNNRSL
IIIGADTRKI VTNNHNRLPY SPIVELDYGF GNSEGGCTGT LIGKSSVLTA AHCLYNFGRK
EYTNPLRMAP GRYRQGTSTI EPHGLFGFRY STIFSVYQTT GDGRYDLGVA TYNADSQGRF
PGQLAGTLCL TEAATQKLTA ETILAGYPMD FPDGNLVESR GCKWRLENGI ISHDCDTTGG
QSGSPIVSSM SEMLGLHIGY DPNAPTIINT ALGWNNATYS SVYAWAPDAR SCPDRRFCSN
CPVLERSLMR ALCSLVCRVF GNAE
//
