ID A0A1Z5KLP4_FISSO Unreviewed; 484 AA.
AC A0A1Z5KLP4;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Serine protease {ECO:0000256|RuleBase:RU004296};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU004296};
GN ORFNames=FisN_9Lh364 {ECO:0000313|EMBL:GAX27045.1};
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:GAX27045.1, ECO:0000313|Proteomes:UP000198406};
RN [1] {ECO:0000313|EMBL:GAX27045.1, ECO:0000313|Proteomes:UP000198406}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JPCC DA0580 {ECO:0000313|EMBL:GAX27045.1,
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:GAX27045.1}.
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DR EMBL; BDSP01000252; GAX27045.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z5KLP4; -.
DR InParanoid; A0A1Z5KLP4; -.
DR OrthoDB; 5484374at2759; -.
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; PF00089; Trypsin; 1.
DR PRINTS; PR00839; V8PROTEASE.
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..30
FT /evidence="ECO:0000256|RuleBase:RU004296"
FT CHAIN 31..484
FT /note="Serine protease"
FT /evidence="ECO:0000256|RuleBase:RU004296"
FT /id="PRO_5011813512"
FT DOMAIN 34..84
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
SQ SEQUENCE 484 AA; 53164 MW; 91CFB084EFDFC9D2 CRC64;
MTCCSFISIS IAIISASLFA PSCLVVVVTA QEVQQPTYDC RTGCSLDANI NGPPVCGIDQ
LTYLNECLAV CQNVAIVHYG PCDQDGSLSE SELSTDSEVV TMELMTRFIS RGYRFVSKNT
RFLSQPENTE ESVVVNEAES ATVRVVEDIE PYFVLFTPDG YEYAYRTTDS LPSYPGPTPL
YMGMQQLRRR YLAIIGADTR TAISNTQAYP YRTIGEADFG TLEGGCTLTM ISRNAAITAG
HCVYNYQNKV PIQMKRIAPG RYRDSSGNTV EPFGTWEVET MQTFGQFKST GNMTFDMAVV
TFQPETRDNM QNCPYVYPGD VVGFLSLDRA QTSGGRISDS RLASSTITGY PADFPNGVMA
TSGTCSKAWH SNHEQFAYHY CDTFGGNSGS AVITSGNVVI GEHAYGFYDN NNVALNNGAV
MLTGQLYDSV YDWAGLGISQ EACGFIAGPE PSADCLCTQF EDRWFLQIVC FILNRDTCFR
RNAN
//
