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Database: UniProt
Entry: A0A0M0JP76_9EUKA
LinkDB: A0A0M0JP76_9EUKA
Original site: A0A0M0JP76_9EUKA 
ID   A0A0M0JP76_9EUKA        Unreviewed;       691 AA.
AC   A0A0M0JP76;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Subtilisin {ECO:0008006|Google:ProtNLM};
GN   ORFNames=Ctob_003037 {ECO:0000313|EMBL:KOO28092.1};
OS   Chrysochromulina tobinii.
OC   Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Prymnesiales;
OC   Chrysochromulinaceae; Chrysochromulina.
OX   NCBI_TaxID=1460289 {ECO:0000313|EMBL:KOO28092.1, ECO:0000313|Proteomes:UP000037460};
RN   [1] {ECO:0000313|Proteomes:UP000037460}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCMP291 {ECO:0000313|Proteomes:UP000037460};
RX   PubMed=26397803; DOI=10.1371/journal.pgen.1005469;
RA   Hovde B.T., Deodato C.R., Hunsperger H.M., Ryken S.A., Yost W., Jha R.K.,
RA   Patterson J., Monnat R.J. Jr., Barlow S.B., Starkenburg S.R.,
RA   Cattolico R.A.;
RT   "Genome Sequence and Transcriptome Analyses of Chrysochromulina tobin:
RT   Metabolic Tools for Enhanced Algal Fitness in the Prominent Order
RT   Prymnesiales (Haptophyceae).";
RL   PLoS Genet. 11:e1005469-e1005469(2015).
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01240}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01240}.
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:KOO28092.1}.
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DR   EMBL; JWZX01002622; KOO28092.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M0JP76; -.
DR   OrthoDB; 5474719at2759; -.
DR   Proteomes; UP000037460; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProt.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00992; PDZ_signaling; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR002884; P_dom.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   PANTHER; PTHR42884:SF14; NEUROENDOCRINE CONVERTASE 1; 1.
DR   PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1.
DR   Pfam; PF01483; P_proprotein; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51829; P_HOMO_B; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037460};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT   DOMAIN          284..432
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
FT   DOMAIN          568..623
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   REGION          512..535
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          661..691
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        512..526
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        661..679
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   691 AA;  74161 MW;  00CFCD3DEDC27E4B CRC64;
     MDRNHISSNS WGIDPCTALA SSGRRKLRQR LLQGCPFAAT AASGTSPCSD SQCAGASWTS
     PPSTCEAVIS TYCQDSYNYV ADGECALWTY LWMTCAYTHL HWDTVRVLQR GVLEGRSRRG
     IVYVFSSGNE YTHGEDVNME QYLHSRFTIT VGATDKLGLH AYYSTTGSSL FITAPGGDSH
     QHSNSWYMAA AGGGCAALVE GSYLQGTSFA CPVVSGVVAL MLEANPLLGW RDVQGILAAT
     TSRNDPTSPL WTTNAAGFIH NIKYGFGMVD ASAAVAAALS WTNWGIEQRI IASSTQHLLT
     VPHDGSTLST SVTVSAQSQT WAIEWIEIFL NLDHSSRGDL QLELTSPSGT HSILTPGPRP
     ETSNPPVEGC SAAADTCEFN NDGTCDNPEY CECDYVDCLA ANWVGENGQP SLYMPRFNWK
     MTSVRSWGES PATLLLALCA IQNVCVEIEY VDKLKAAGGM ERLQHIVGLA DPQLCQFAQG
     CFDNVRTVVA INAMQHMQQN FLRTRPKAEK AAAEAEAAEE SAAEKAAAEK AATGGAEPVL
     AKPTAYRRQR SLRQKIRSSV VVETCIQTCI IVKEDQGSIG LDLQQSSGHR ISIVRVKPDT
     PAARSVPPLV AGMAIVSVNG FPVLDAKVAA ECIAKAGRGQ MMLEVAPEAT RSWLSRLRRA
     SARQESVKGA DEARMSGDED SGHGAALAAE P
//
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