ID A0A1Z5K1Y3_FISSO Unreviewed; 373 AA.
AC A0A1Z5K1Y3;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Peptidase S1 domain-containing protein {ECO:0000259|PROSITE:PS50240};
GN ORFNames=FisN_9Hu005 {ECO:0000313|EMBL:GAX20300.1};
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:GAX20300.1, ECO:0000313|Proteomes:UP000198406};
RN [1] {ECO:0000313|EMBL:GAX20300.1, ECO:0000313|Proteomes:UP000198406}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JPCC DA0580 {ECO:0000313|EMBL:GAX20300.1,
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC {ECO:0000256|ARBA:ARBA00007664}.
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:GAX20300.1}.
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DR EMBL; BDSP01000147; GAX20300.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z5K1Y3; -.
DR InParanoid; A0A1Z5K1Y3; -.
DR OrthoDB; 4629979at2759; -.
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:InterPro.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR PANTHER; PTHR24276:SF91; AT26814P-RELATED; 1.
DR PANTHER; PTHR24276; POLYSERASE-RELATED; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000198406};
KW Signal {ECO:0000256|SAM:SignalP};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..373
FT /note="Peptidase S1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012938798"
FT DOMAIN 28..238
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 250..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..285
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..363
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 373 AA; 40674 MW; 6B810EE673D35AC7 CRC64;
MNVIAALMLP SLAVASNIFA HNEIQPRIVG GFPGGIGAYP YFCHAITNSS VCGGTLIAAD
VVLTVKSCEN VFDNNEVFIG SNDRLGRDFA PRISVSSLQM HPTEDLMLVL LNESSNNTLV
SLNLEGTLVA DLPLFTIGFG KSTEEESAYS DSLMEVDMFL LENGICRLQV GDLFNETTQY
CASFPFGGPC DGDEGGPLLD QITQEQSGVY SYNIGCTNQP SVYIRLSTYA DWITDFVCSN
STQAPEVLCG VMGGNKGKKS KKGKKSKSSS KSKKSASGKS SKKGKGGKGK GSEDVEMEDY
FYMNSTHHFL NETHFHNATV HDRGSSSKKS FKKGEQHGVV HSPATRTTHQ QRTRRKRRQI
QYPRIRGGRQ PLP
//
