ID A0A166B7X4_DAUCS Unreviewed; 465 AA.
AC A0A166B7X4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Protease Do-like PDZ domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=DCAR_011230 {ECO:0000313|EMBL:KZN02476.1};
OS Daucus carota subsp. sativus (Carrot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC Daucus; Daucus sect. Daucus.
OX NCBI_TaxID=79200 {ECO:0000313|EMBL:KZN02476.1, ECO:0000313|Proteomes:UP000077755};
RN [1] {ECO:0000313|EMBL:KZN02476.1, ECO:0000313|Proteomes:UP000077755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DH1 {ECO:0000313|Proteomes:UP000077755};
RC TISSUE=Leaf {ECO:0000313|EMBL:KZN02476.1};
RX PubMed=27158781; DOI=10.1038/ng.3565;
RA Iorizzo M., Ellison S., Senalik D., Zeng P., Satapoomin P., Huang J.,
RA Bowman M., Iovene M., Sanseverino W., Cavagnaro P., Yildiz M.,
RA Macko-Podgorni A., Moranska E., Grzebelus E., Grzebelus D., Ashrafi H.,
RA Zheng Z., Cheng S., Spooner D., Van Deynze A., Simon P.;
RT "A high-quality carrot genome assembly provides new insights into
RT carotenoid accumulation and asterid genome evolution.";
RL Nat. Genet. 48:657-666(2016).
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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:KZN02476.1}.
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DR EMBL; LNRQ01000003; KZN02476.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166B7X4; -.
DR STRING; 79200.A0A166B7X4; -.
DR EnsemblPlants; KZN02476; KZN02476; DCAR_011230.
DR Gramene; KZN02476; KZN02476; DCAR_011230.
DR OMA; HDKYTGF; -.
DR Proteomes; UP000077755; Chromosome 3.
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:InterPro.
DR CDD; cd00987; PDZ_serine_protease; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.20.190.20; -; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR041517; DEGP_PDZ.
DR InterPro; IPR046449; DEGP_PDZ_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001940; Peptidase_S1C.
DR PANTHER; PTHR45980; -; 1.
DR PANTHER; PTHR45980:SF18; PROTEASE DO-LIKE 9; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF17815; PDZ_3; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000077755}.
FT DOMAIN 210..312
FT /note="PDZ"
FT /evidence="ECO:0000259|Pfam:PF13180"
FT DOMAIN 319..462
FT /note="Protease Do-like PDZ"
FT /evidence="ECO:0000259|Pfam:PF17815"
SQ SEQUENCE 465 AA; 51338 MW; 7FBE6F140794DCB2 CRC64;
MSSMDAVVKV FCVHTEPNFS LPWQRKRQYS SSSSGFIIEG RRVLTNAHSV EHHTQVKLKK
RGSDTKYLAT VLAIGTECDI ALLTVSDDEF WEGVSPIEFG ELPVLQDAVT VVGYPIGGDT
ISVTSGVVSR IEILSYAHGS TELLGLQIDA AINAGNSGGP AFSDKDKCVG IAFQSLKHED
AENIGYVIPT PVILHFIQDY EENGNYTGFP VLGVEWQKME NPDLRMSMGM GLKQKGVRIR
RIEPTSPESL LLKPSDVILS FDGVDIANDG TVLFRDGERI GFSYLVSQKY TGDKALVKVL
RNSKTLEFNI TLATHTRLIP AHIKGKPPSY YIVAGFVFSA VSVPYLCSEY EKDYDAPVKL
LEKHLHGMAQ SVDEQLVVLS QVLVADINIG YEYIINTQVH AFNGKPVKNL KGLAYMVEKC
DEEFLKFHLE YEQIVVLQTE KAKAATPDIL TTHCIPSAMS DDLKA
//