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Database: UniProt
Entry: A0A2B4RCF4_STYPI
LinkDB: A0A2B4RCF4_STYPI
Original site: A0A2B4RCF4_STYPI 
ID   A0A2B4RCF4_STYPI        Unreviewed;       399 AA.
AC   A0A2B4RCF4;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Plasma kallikrein {ECO:0000313|EMBL:PFX14473.1};
GN   Name=Klkb1 {ECO:0000313|EMBL:PFX14473.1};
GN   ORFNames=AWC38_SpisGene21368 {ECO:0000313|EMBL:PFX14473.1};
OS   Stylophora pistillata (Smooth cauliflower coral).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC   Astrocoeniina; Pocilloporidae; Stylophora.
OX   NCBI_TaxID=50429 {ECO:0000313|EMBL:PFX14473.1, ECO:0000313|Proteomes:UP000225706};
RN   [1] {ECO:0000313|Proteomes:UP000225706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Voolstra C.R., Li Y., Liew Y.J., Baumgarten S., Zoccola D., Flot J.-F.,
RA   Tambutte S., Allemand D., Aranda M.;
RT   "Comparative analysis of the genomes of Stylophora pistillata and Acropora
RT   digitifera provides evidence for extensive differences between species of
RT   corals.";
RL   bioRxiv 0:0-0(2017).
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01005}.
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:PFX14473.1}.
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DR   EMBL; LSMT01000776; PFX14473.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2B4RCF4; -.
DR   STRING; 50429.A0A2B4RCF4; -.
DR   EnsemblMetazoa; XM_022951998.1; XP_022807733.1; LOC111344747.
DR   OrthoDB; 2909016at2759; -.
DR   Proteomes; UP000225706; Unassembled WGS sequence.
DR   GO; GO:0042151; C:nematocyst; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0007596; P:blood coagulation; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 1.10.10.1870; ShTK domain-like; 2.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR   InterPro; IPR012224; Pept_S1A_FX.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR003582; ShKT_dom.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR   PANTHER; PTHR24252:SF7; HYALIN; 1.
DR   Pfam; PF01549; ShK; 2.
DR   Pfam; PF00089; Trypsin; 1.
DR   PIRSF; PIRSF001143; Factor_X; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00254; ShKT; 2.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS51670; SHKT; 2.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU01005}; Hydrolase {ECO:0000256|RuleBase:RU363034};
KW   Protease {ECO:0000256|RuleBase:RU363034};
KW   Reference proteome {ECO:0000313|Proteomes:UP000225706};
KW   Serine protease {ECO:0000256|RuleBase:RU363034};
KW   Signal {ECO:0000256|SAM:SignalP}; Toxin {ECO:0000256|ARBA:ARBA00022656}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..399
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012451121"
FT   DOMAIN          49..83
FT                   /note="ShKT"
FT                   /evidence="ECO:0000259|PROSITE:PS51670"
FT   DOMAIN          87..121
FT                   /note="ShKT"
FT                   /evidence="ECO:0000259|PROSITE:PS51670"
FT   DOMAIN          156..392
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   ACT_SITE        199
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001143-1"
FT   ACT_SITE        249
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001143-1"
FT   ACT_SITE        344
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001143-1"
FT   DISULFID        49..83
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01005"
FT   DISULFID        87..121
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01005"
SQ   SEQUENCE   399 AA;  44362 MW;  CCCA5B9C165253FA CRC64;
     MLISFSSLIF LIYCAYFSQE REMSLQEGIT AGLETLSDEN NSSTKRAACE DLNSYCNIYK
     PYCKHIEYVD FVKVNCKKTC DLCPKACLDR VSYCHVIKNR CTDPVIGGSV RRFCAKTCGV
     CVVTPPTIPP TTIPRTEQPI DQGSVECGRK AVGSRIVGGT NARPGAWPWQ VTMDYKGHSG
     PHWCGGSIVT PHYILTAAHC FGSGDDPKDY SIVAGEHDLN TVDGFEQNTT IQEIIIHPKY
     NRIANHDYDV ALVKLKNPIR YNNHVRPVCL AKSDFDSGTN CYVTGWGYTS EDGSIAQILQ
     QAIVPLVSRE KCQEGYNDLG YKISTRMRCA GYSEGKIDAC QGDSGGPLVC VRNDKWYLMG
     VISWGQGCAR KGRYGVYADM MDLKFWVQQT INKGYQSKI
//
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