ID D7FK95_ECTSI Unreviewed; 397 AA.
AC D7FK95;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Serine type protease, similar to Protease Do-like 1, chloroplast {ECO:0000313|EMBL:CBJ29300.1};
GN ORFNames=Esi_0142_0050 {ECO:0000313|EMBL:CBJ29300.1};
OS Ectocarpus siliculosus (Brown alga) (Conferva siliculosa).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; PX clade; Phaeophyceae;
OC Ectocarpales; Ectocarpaceae; Ectocarpus.
OX NCBI_TaxID=2880 {ECO:0000313|EMBL:CBJ29300.1, ECO:0000313|Proteomes:UP000002630};
RN [1] {ECO:0000313|EMBL:CBJ29300.1, ECO:0000313|Proteomes:UP000002630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ec32 / CCAP1310/4 {ECO:0000313|Proteomes:UP000002630};
RX PubMed=20520714; DOI=10.1038/nature09016;
RA Cock J.M., Sterck L., Rouze P., Scornet D., Allen A.E., Amoutzias G.,
RA Anthouard V., Artiguenave F., Aury J.M., Badger J.H., Beszteri B.,
RA Billiau K., Bonnet E., Bothwell J.H., Bowler C., Boyen C., Brownlee C.,
RA Carrano C.J., Charrier B., Cho G.Y., Coelho S.M., Collen J., Corre E.,
RA Da Silva C., Delage L., Delaroque N., Dittami S.M., Doulbeau S., Elias M.,
RA Farnham G., Gachon C.M., Gschloessl B., Heesch S., Jabbari K., Jubin C.,
RA Kawai H., Kimura K., Kloareg B., Kupper F.C., Lang D., Le Bail A.,
RA Leblanc C., Lerouge P., Lohr M., Lopez P.J., Martens C., Maumus F.,
RA Michel G., Miranda-Saavedra D., Morales J., Moreau H., Motomura T.,
RA Nagasato C., Napoli C.A., Nelson D.R., Nyvall-Collen P., Peters A.F.,
RA Pommier C., Potin P., Poulain J., Quesneville H., Read B., Rensing S.A.,
RA Ritter A., Rousvoal S., Samanta M., Samson G., Schroeder D.C., Segurens B.,
RA Strittmatter M., Tonon T., Tregear J.W., Valentin K., von Dassow P.,
RA Yamagishi T., Van de Peer Y., Wincker P.;
RT "The Ectocarpus genome and the independent evolution of multicellularity in
RT brown algae.";
RL Nature 465:617-621(2010).
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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DR EMBL; FN648013; CBJ29300.1; -; Genomic_DNA.
DR AlphaFoldDB; D7FK95; -.
DR STRING; 2880.D7FK95; -.
DR EnsemblProtists; CBJ29300; CBJ29300; Esi_0142_0050.
DR eggNOG; KOG1320; Eukaryota.
DR InParanoid; D7FK95; -.
DR OMA; IMSPEGY; -.
DR OrthoDB; 2159919at2759; -.
DR Proteomes; UP000002630; Chromosome LG12.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00987; PDZ_serine_protease; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001940; Peptidase_S1C.
DR PANTHER; PTHR43343; PEPTIDASE S12; 1.
DR PANTHER; PTHR43343:SF3; PROTEASE DO-LIKE 8, CHLOROPLASTIC; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:CBJ29300.1};
KW Protease {ECO:0000313|EMBL:CBJ29300.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002630};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT DOMAIN 276..344
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 397 AA; 41284 MW; 90720EADEB30EB2F CRC64;
MALSDSGDGG DDGDGVGNGW LSGWKRGLVS AAVGLSVLSG GLTTSYLPGL TSSAAQAAMA
PSLMQDEKGY ISIFEKSTPG VVYINTFVNQ RDAFSMNVLE VPAGTGSGFV WDDQGNIVTN
FHVIREAQSA QVRLTLGDGT QRTFQAQVKG YDPDKDVAVL KIDAPSELLR PIALGVSNTL
KVGQLALAIG NPFGLDHTLT MGVVSGLGRE VKSPSGRPIS NVIQTDAAIN PGNSGGPLLD
SVGRIIGMNT AIYSPSGGSA GIGFAIPVDT LKTVVGTIIQ KGRVSRPIIG ITFLESARAN
TVGIKKGVLV LDVKEGTSAA NSGLRPTTRT QLGDIIVAID KQEINTEADL FKILESRKPG
DEISITAERV TEDGTETLFL KIQLAEAPQP IVQASSP
//
