ID K0RT83_THAOC Unreviewed; 325 AA.
AC K0RT83;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Peptidase A2 domain-containing protein {ECO:0000259|PROSITE:PS50175};
GN ORFNames=THAOC_22935 {ECO:0000313|EMBL:EJK57063.1};
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:EJK57063.1, ECO:0000313|Proteomes:UP000266841};
RN [1] {ECO:0000313|EMBL:EJK57063.1, ECO:0000313|Proteomes:UP000266841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1005 {ECO:0000313|EMBL:EJK57063.1,
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 -!- SIMILARITY: Belongs to the DDI1 family.
CC {ECO:0000256|ARBA:ARBA00009136}.
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:EJK57063.1}.
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DR EMBL; AGNL01029629; EJK57063.1; -; Genomic_DNA.
DR AlphaFoldDB; K0RT83; -.
DR EnsemblProtists; EJK57063; EJK57063; THAOC_22935.
DR eggNOG; KOG0012; Eukaryota.
DR Proteomes; UP000266841; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.30.60.90; -; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR001995; Peptidase_A2_cat.
DR InterPro; IPR019103; Peptidase_aspartic_DDI1-type.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR12917; ASPARTYL PROTEASE DDI-RELATED; 1.
DR PANTHER; PTHR12917:SF1; AT13091P; 1.
DR Pfam; PF09668; Asp_protease; 1.
DR Pfam; PF00569; ZZ; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000266841};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 198..278
FT /note="Peptidase A2"
FT /evidence="ECO:0000259|PROSITE:PS50175"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 325 AA; 35073 MW; 8ADA2A13F3A5425B CRC64;
MAVAEDKRLP VLEGDAPPSV DGASRESPLK GTEILATIMH DCDYCDASPR CDAIPPPNSA
TADELFIALT TVGALYEPAY CTAHWIDYTE NDEAIARAIA EDRQSKTSNC PGRHGLEPFQ
ASNMQRVSCN GCSNTIANGR KVWSCVQCNF DLCEACHRRG VLSSSVPDHS SHSSPSSSPQ
IPSSHMCLVP CQIGSMTVEM LVDTGAQSSV LSSAVVRQLG LTGRVDRRYQ GVAAGVGRAR
ISGKLRDVVC AFGQHVEFPM DFIILSVDDP LCIMGLDQMR KYKCLVDLQR EKLVFGGTGG
VEVDFLPPER AHFDAQYLNS GCIVS
//
