ID K0RM32_THAOC Unreviewed; 721 AA.
AC K0RM32;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Peptidase S1 domain-containing protein {ECO:0000259|PROSITE:PS50240};
DE Flags: Fragment;
GN ORFNames=THAOC_25591 {ECO:0000313|EMBL:EJK54753.1};
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:EJK54753.1, ECO:0000313|Proteomes:UP000266841};
RN [1] {ECO:0000313|EMBL:EJK54753.1, ECO:0000313|Proteomes:UP000266841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1005 {ECO:0000313|EMBL:EJK54753.1,
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:EJK54753.1}.
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DR EMBL; AGNL01035335; EJK54753.1; -; Genomic_DNA.
DR AlphaFoldDB; K0RM32; -.
DR EnsemblProtists; EJK54753; EJK54753; THAOC_25591.
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:InterPro.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR PANTHER; PTHR24276:SF91; AT26814P-RELATED; 1.
DR PANTHER; PTHR24276; POLYSERASE-RELATED; 1.
DR Pfam; PF00089; Trypsin; 2.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 2.
DR PROSITE; PS50240; TRYPSIN_DOM; 2.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000266841};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT DOMAIN 211..355
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 386..676
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 721
FT /evidence="ECO:0000313|EMBL:EJK54753.1"
SQ SEQUENCE 721 AA; 78532 MW; 7557FC672D00CFC7 CRC64;
MTTAAPAPAG DDRGHRGEEA TAKTRTDIIL ADRHSGNDRR EKEKGAWTTA WTRGSLGARV
ARARTMAAAA MPVVANARSV ASILTSTDGF HLSRAGMELH SPLNYKSLEH EFRRQRRLKV
KDDTATSRNV QAMNDLHASQ RRDEDAIFSE EEFCTPAGAS SLESNLQNEV YADRDVDVMC
GCLDGFAECS VTFNEEECEV LSCSDGRWNC LDPDASSVSV CTIERIITTW LLLDDIAPSL
FLIQSTTEYT SGVANIHKTS ALISVIEEEE PECLMFNVDR SQKKVTSKML CAKEDGKDSC
QGDSGGPLLI KGADSSQDLQ IGVVSWGVGC GEDGAYPSVY ARVSSAYDWI RAQVCKGSVD
PPASFECDES AADDTVRSGH AKQERIVGGE DAKVGRFQYA VGLAYPLFGQ FCGGSLIAPD
VVLSAAHCMN TADFVVPYNV IIGRHDLEEQ TEGESIAMSD EVKHPNYDLL SLENDFALVF
LASPTYNYEV VQLNQDDNIP QSGDPVTAIG YGDTDPDVTV MTPSMILQEV EKKALSNEEC
NEIPEWENFN GQACNSCEVC EQDGSSVKVK ADWWVMFRRP SSPPFPAESI CSSEDAFALK
MALSEVMPDG DIANIDCNCQ SDTGLVLCDV EFLEEICVDG FPLCWKSSQV QLWNVATFDL
KSVTYKSEYT QGALFVTSDS FTIENPQTND ATCSGYYVNG EQCSSCTLCS GVEEISTVGD
C
//