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Database: UniProt
Entry: F0Y2J4_AURAN
LinkDB: F0Y2J4_AURAN
Original site: F0Y2J4_AURAN 
ID   F0Y2J4_AURAN            Unreviewed;      1114 AA.
AC   F0Y2J4;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   03-MAY-2023, entry version 50.
DE   RecName: Full=subtilisin {ECO:0000256|ARBA:ARBA00023619};
DE            EC=3.4.21.62 {ECO:0000256|ARBA:ARBA00023619};
GN   ORFNames=AURANDRAFT_71024 {ECO:0000313|EMBL:EGB11061.1};
OS   Aureococcus anophagefferens (Harmful bloom alga).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Pelagophyceae; Pelagomonadales;
OC   Aureococcus.
OX   NCBI_TaxID=44056 {ECO:0000313|Proteomes:UP000002729};
RN   [1] {ECO:0000313|EMBL:EGB11061.1, ECO:0000313|Proteomes:UP000002729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP 1984 {ECO:0000313|Proteomes:UP000002729};
RX   PubMed=21368207; DOI=10.1073/pnas.1016106108;
RA   Gobler C.J., Berry D.L., Dyhrman S.T., Wilhelm S.W., Salamov A.,
RA   Lobanov A.V., Zhang Y., Collier J.L., Wurch L.L., Kustka A.B., Dill B.D.,
RA   Shah M., VerBerkmoes N.C., Kuo A., Terry A., Pangilinan J., Lindquist E.A.,
RA   Lucas S., Paulsen I.T., Hattenrath-Lehmann T.K., Talmage S.C., Walker E.A.,
RA   Koch F., Burson A.M., Marcoval M.A., Tang Y.Z., Lecleir G.R., Coyne K.J.,
RA   Berg G.M., Bertrand E.M., Saito M.A., Gladyshev V.N., Grigoriev I.V.;
RT   "Niche of harmful alga Aureococcus anophagefferens revealed through
RT   ecogenomics.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:4352-4357(2011).
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   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU01032};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PROSITE-
CC       ProRule:PRU01032};
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DR   EMBL; GL833123; EGB11061.1; -; Genomic_DNA.
DR   RefSeq; XP_009034615.1; XM_009036367.1.
DR   AlphaFoldDB; F0Y2J4; -.
DR   EnsemblProtists; EGB11061; EGB11061; AURANDRAFT_71024.
DR   GeneID; 20228038; -.
DR   KEGG; aaf:AURANDRAFT_71024; -.
DR   eggNOG; KOG1012; Eukaryota.
DR   InParanoid; F0Y2J4; -.
DR   OrthoDB; 1405251at2759; -.
DR   Proteomes; UP000002729; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00030; C2; 1.
DR   CDD; cd04056; Peptidases_S53; 1.
DR   CDD; cd11377; Pro-peptidase_S53; 1.
DR   CDD; cd06974; TerD_like; 2.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   Gene3D; 2.60.60.30; sav2460 like domains; 2.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015366; S53_propep.
DR   InterPro; IPR030400; Sedolisin_dom.
DR   InterPro; IPR003325; TerD.
DR   PANTHER; PTHR14218; PROTEASE S8 TRIPEPTIDYL PEPTIDASE I CLN2; 1.
DR   PANTHER; PTHR14218:SF15; TRIPEPTIDYL-PEPTIDASE 1; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   Pfam; PF09286; Pro-kuma_activ; 1.
DR   Pfam; PF02342; TerD; 2.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00944; Pro-kuma_activ; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS51695; SEDOLISIN; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW   ProRule:PRU01032}; Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU01032}; Protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002729};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   DOMAIN          19..147
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          740..1114
FT                   /note="Peptidase S53"
FT                   /evidence="ECO:0000259|PROSITE:PS51695"
FT   ACT_SITE        816
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   ACT_SITE        820
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   ACT_SITE        1031
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   BINDING         1073
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   BINDING         1074
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   BINDING         1092
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   BINDING         1094
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
SQ   SEQUENCE   1114 AA;  117794 MW;  9D4350A9DDBF8BB5 CRC64;
     MASLVDNMDG LAVADAVVVA GGVSGTVAGT SAEHMMNPGT LEIEVIQGRD LVIKDRGTFR
     SNKSDPFCVV AVDGAKVGKT KTVDRNLSPV WNFSTAAKVK RGAQKRLVVN CFDKDKLSSS
     DPMGTVVIEV LEALRGADVA TRVRRWYDVE NCEGCDNARG QIEIAFAWKP KTVIALEKGT
     PFRVEHPEQA LFVGLGWTGA CGAKVDLDAS CVFFDDQGAV VDALYFGNTQ CFDGAALHSG
     DALTGDEAAA EEDADERIEL RLAKLPRAVA SMLFVVTAYA EKSSFVDMKS AFVGLFDPVE
     GEMCRYAFDC RGDHTGLVMC RVARSGPAWV LNAIGDVAAG PRDYGTWVPE LKAYLSDLVS
     HVRVGDPNDR VAIMHKGSVV DLSYYQAGPL AEVRMGVAWD ITGGRSIDLD ASCLLLKAGC
     SEATTEIVSY QKLSSSDGRV RHSGDDTTGD GGGDDEVITV ELDKLAPDVR YVAFVVNSYS
     GQPFSQVDNV SCHLFLPPSR ARPKPQDLAI FNLSSKTYHT TALVMTILER STRPDGSPTW
     LMRAVGEGTE AKVAKQCLDE IQLVRGERVA ASALIELEFW LKHDAADLAA FHDDLVERST
     PGSAKYSDWL SKEEVRAMLA PSREALDAVL DYVVHDLGAA DVHVDDFKSV VSVAVPAGAV
     ERALDTKLYA HAHVDYAHVE VIRVGEAYSL PAAVAAHVSL VSELVRFPRL RRSDLVAAAV
     DAAPNATGAW AKCGAKNSAY TNPYVLAERY GFEFPLTDAA DGNSMAVAEF QGQYWDPKDL
     GAFSTACGLP SAISVSKTVG GNVPLLCEGL GQGCVESLLD IEYAGSIAGA IPLEVYYSGT
     YSLLAWANKL GDATPAPLVN SVSYGNDEAQ QTGSALCSAY MESVNAAFMK VSNAGGKRVV
     SNTGVSILFA AGDQGVWGRE GPGLKYHPDF PAASPYVTAV GGTDFATKSV IGDETTWNDG
     GSGFSNEFAQ PAWQADDVAA YLKSATGLPK ARMYNATGRA YPDVAALAGL VNPYLVALSG
     GKSFAGVGGT SAASPTVAAM IAQVNNNRLK AGKKSMGWLN PFLYKTGEAA FHDVTTGKTS
     GGFTGGFPAA PGWDAATGFG TVDFKKLNAA ALAA
//
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