ID D8LNG6_ECTSI Unreviewed; 969 AA.
AC D8LNG6;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=subtilisin {ECO:0000256|ARBA:ARBA00023619};
DE EC=3.4.21.62 {ECO:0000256|ARBA:ARBA00023619};
GN ORFNames=Esi_0044_0132 {ECO:0000313|EMBL:CBN77323.1};
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:CBN77323.1, ECO:0000313|Proteomes:UP000002630};
RN [1] {ECO:0000313|EMBL:CBN77323.1, 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 -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins with broad specificity for peptide
CC bonds, and a preference for a large uncharged residue in P1.
CC Hydrolyzes peptide amides.; EC=3.4.21.62;
CC Evidence={ECO:0000256|ARBA:ARBA00023529};
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240}.
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DR EMBL; FN648641; CBN77323.1; -; Genomic_DNA.
DR AlphaFoldDB; D8LNG6; -.
DR STRING; 2880.D8LNG6; -.
DR EnsemblProtists; CBN77323; CBN77323; Esi_0044_0132.
DR eggNOG; KOG1114; Eukaryota.
DR InParanoid; D8LNG6; -.
DR OrthoDB; 1220931at2759; -.
DR Proteomes; UP000002630; Chromosome LG22.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04842; Peptidases_S8_Kp43_protease; 1.
DR Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034058; TagA/B/C/D_pept_dom.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000002630};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..969
FT /note="subtilisin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003117379"
FT TRANSMEM 946..968
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 368..767
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT REGION 151..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 907..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 377
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 439
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 694
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 969 AA; 101391 MW; DB23786E5FB6D186 CRC64;
MSDKLHRLAL LVFLCSSAVA AGRLNSPALE LVENALLTTA KDDFKGHVGA FEAAATWNGE
RLRHSQEETR APHLACARYG DGHEASSRLK QFLSPEAVRV VSHSEDHGAC FFASASHAQA
AAIVEDQEQF GLENFSPFPS PLKLAPGLVD HTESHDEAEE EARSSGLDRL SARHGARMRK
PNVEGLSVEL TPGTLAARSS EAKSFINHML GDLMSASVDL HSTNFWSDPG MDGAGEHLSS
PAGAVRARDW RKAASVVHEL SEAASTGPGD ICSWNRIFVH HAGDDSLLVS GLDHLLFSGR
GAGGSHEEES TELHVACFMG LVSFLAGRPE VLRVSPRPTK RVLNAAARGV IQSASATDTP
LTDAGLDGTG EIIQVIDSGL DETSCYFIDD SGEEVDHGYY FDELGRAAVY SSSYSSDETA
TIFNGGDFSY YPERRKAGHG THTAGSAAGA TLNDPAETIT CNVTDTLSCV GACIDLLDAT
DDLVSISSQT DGTDLDRLCP MYGCDNSTDT TCLSDDVPET LSNNGGMAQG AKLAIFDVFY
GGYDASSSIG NNLWEVCTEA GCKLHSNSLG ADFECSIASW DILNDQFMYE NAENLLIFAA
GNEGGIERST CTINTPGIGK NSLAIGASTS GDTRVISTVG ATGIDTVAEF SSWGFTTDDR
IKPEVVAPGD SVYSAASDGT DTHSCRLWAY EGTSMSCPIV AGAAAMIRQY FVDETFYTAD
VTARGFCSDG FICEGFSPSA ATVKALLINS ANLMGGSSEP DGFRGFGRVH LEAGMPLEGE
GDLVLFVADA LDTSIAGGTL EEYLFDVDAD AGLDLRATLS WIDPPATATS AVQLVHNLDL
VVVSPDGTTY RMWGSDTTDN RNVNERVIVD ATDVVTGTWT VWVWANNLVT DSQSYSLVVN
GAISPGTGEG ASGSSSFEVS SSATSASSED GTGAGVTGGS LVAAPAAGFL AAVVGACVAA
MVAAGVFVA
//
