ID K0R0B6_THAOC Unreviewed; 635 AA.
AC K0R0B6;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Peptidase S1 domain-containing protein {ECO:0000259|PROSITE:PS50240};
GN ORFNames=THAOC_37370 {ECO:0000313|EMBL:EJK44119.1};
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:EJK44119.1, ECO:0000313|Proteomes:UP000266841};
RN [1] {ECO:0000313|EMBL:EJK44119.1, ECO:0000313|Proteomes:UP000266841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1005 {ECO:0000313|EMBL:EJK44119.1,
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:EJK44119.1}.
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DR EMBL; AGNL01050148; EJK44119.1; -; Genomic_DNA.
DR AlphaFoldDB; K0R0B6; -.
DR MEROPS; S01.143; -.
DR EnsemblProtists; EJK44119; EJK44119; THAOC_37370.
DR eggNOG; KOG3627; Eukaryota.
DR OMA; CANDFAN; -.
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; IPR001314; Peptidase_S1A.
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 PRINTS; PR00722; CHYMOTRYPSIN.
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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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 Signal {ECO:0000256|SAM:SignalP};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..635
FT /note="Peptidase S1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003839817"
FT DOMAIN 116..346
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 21..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..66
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..558
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 635 AA; 67177 MW; E60365E86C5A551A CRC64;
MASSKLIAIS LLLSLAAANA QKGLRGSESA GQTDPAEPHH LKTHALGRSR PKKAKRTSKK
LTKRQNKARN QAREIDSSIA DSIAGRTQAQ QAETRENEED SHPAGGEHAD KMAPRVINGD
EAPRGKYTFA VSLQDYGHFC GGSLIARDYV LSAAHCKGGR YDAVVGKHDL RDWGGQVIEV
AEEIVHPYYN DWTTDNDFML LRLRYPADTQ YDIITPNSSN SKPSVGSKVD VMGWGDTHIS
DRVEQLSDVL MTVDVKVMSN SDCDDSEGYV DGTYGNYHGQ ITSNMLCAND FANREDSCQG
DSGGPLVQGD SLVGVVSWGI GCASNHFPGV YARVSKAYNW IENEVCKNSR YKPDWCGGSS
SANAPTEDKP STSAISDGSG SGGSGCKKHD RKSDCQDAGC QWDRDARGPV ASAPTCPSDS
TGLEVAGQAY APTTAQGNSA GKTQTKDASG IKTRRGARAG RPRRNPSHLR PPTYSPAEGA
SAAILRSLTA TPIGIASGRA DGVRSGSPST PGFGSTMIGG ADGTELEFHI SSGGPSCTVT
KSSTPATATV SGGDLNPQND CPRPQPAPIL PALELGTYLP RQRGYDQAVM PSHVHCHRCQ
HSVHPVTKQA VHMSTATSSK PSSLAGISTL KSQPV
//
