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Database: UniProt
Entry: K0TB77_THAOC
LinkDB: K0TB77_THAOC
Original site: K0TB77_THAOC 
ID   K0TB77_THAOC            Unreviewed;       399 AA.
AC   K0TB77;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Peptidase S1 domain-containing protein {ECO:0000259|PROSITE:PS50240};
DE   Flags: Fragment;
GN   ORFNames=THAOC_03571 {ECO:0000313|EMBL:EJK74735.1};
OS   Thalassiosira oceanica (Marine diatom).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC   Coscinodiscophyceae; Thalassiosirophycidae; Thalassiosirales;
OC   Thalassiosiraceae; Thalassiosira.
OX   NCBI_TaxID=159749 {ECO:0000313|EMBL:EJK74735.1, ECO:0000313|Proteomes:UP000266841};
RN   [1] {ECO:0000313|EMBL:EJK74735.1, ECO:0000313|Proteomes:UP000266841}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1005 {ECO:0000313|EMBL:EJK74735.1,
RC   ECO:0000313|Proteomes:UP000266841};
RX   PubMed=22835381; DOI=10.1186/gb-2012-13-7-r66;
RA   Lommer M., Specht M., Roy A.S., Kraemer L., Andreson R., Gutowska M.A.,
RA   Wolf J., Bergner S.V., Schilhabel M.B., Klostermeier U.C., Beiko R.G.,
RA   Rosenstiel P., Hippler M., Laroche J.;
RT   "Genome and low-iron response of an oceanic diatom adapted to chronic iron
RT   limitation.";
RL   Genome Biol. 13:R66-R66(2012).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000256|ARBA:ARBA00007664}.
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:EJK74735.1}.
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DR   EMBL; AGNL01003409; EJK74735.1; -; Genomic_DNA.
DR   AlphaFoldDB; K0TB77; -.
DR   MEROPS; S01.B79; -.
DR   EnsemblProtists; EJK74735; EJK74735; THAOC_03571.
DR   eggNOG; KOG3627; Eukaryota.
DR   Proteomes; UP000266841; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24276:SF91; AT26814P-RELATED; 1.
DR   PANTHER; PTHR24276; POLYSERASE-RELATED; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU363034};
KW   Protease {ECO:0000256|RuleBase:RU363034};
KW   Reference proteome {ECO:0000313|Proteomes:UP000266841};
KW   Serine protease {ECO:0000256|RuleBase:RU363034};
KW   Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT   DOMAIN          1..198
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EJK74735.1"
SQ   SEQUENCE   399 AA;  43673 MW;  6F7969A04867B0A4 CRC64;
     DVVLSAAHCG TDIPKVILGR HDLGKSSGGE VMTVKEAIKN PRYSTKNDNN DSMLIFLDRA
     SSMKQTELVR LGRDFVGEGQ HVTVRGWGDT NPSDYRENYP NELMEVEVKT LSNEDCEASK
     GRDFDYDGWI TGNMICAEHR LRKDACQGDS GGPLVVESGP EPVQVGIVSW GYGCAEDDYP
     GVYTRVSTQY KWIREQVCSR SSSPPDYFNC NTASTLQQSQ ASGNGEGIEE DANEEASIVV
     EEEPAGPAMF EKGSFRVEEF DNGDFGMFTE HSESARHYAE SHLQQGVVAV GDGLSIGTEY
     LSLGGFNSLA VSYRFLAEKL HPGDEFCLEY ILDEGESSSE CTSRQGPFAN GVWYIKTAKL
     DISNASSVKL KFVLRAKSSS GGQEDSDVLL DKVIFRGSS
//
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