ID A0A166E9L2_DAUCS Unreviewed; 313 AA.
AC A0A166E9L2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Peptidase M20 dimerisation domain-containing protein {ECO:0000259|Pfam:PF07687};
GN ORFNames=DCAR_007105 {ECO:0000313|EMBL:KZN06268.1};
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:KZN06268.1};
RN [1] {ECO:0000313|EMBL:KZN06268.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Leaf {ECO:0000313|EMBL:KZN06268.1};
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 -!- 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:KZN06268.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LNRQ01000002; KZN06268.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166E9L2; -.
DR EnsemblPlants; KZN06268; KZN06268; DCAR_007105.
DR Gramene; KZN06268; KZN06268; DCAR_007105.
DR OMA; THLWATE; -.
DR Proteomes; UP000077755; Chromosome 2.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR Gene3D; 3.40.630.10; Zn peptidases; 2.
DR InterPro; IPR017439; Amidohydrolase.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR NCBIfam; TIGR01891; amidohydrolases; 1.
DR PANTHER; PTHR11014:SF147; PEPTIDASE M20 DIMERISATION DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR11014; PEPTIDASE M20 FAMILY MEMBER; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Reference proteome {ECO:0000313|Proteomes:UP000077755}.
FT DOMAIN 97..195
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 313 AA; 34310 MW; 128FD2330E70494A CRC64;
MVEWEHKSKV DGKMHACGHD VHVSMLLGAA KVLQQIRKQL QGTVVLIFQP AEEIGEGAKH
MIREGVLDNV EAIFGMHAVL EYNTGVVAAR PGELLAGCGS FEATIRGRGG PAANPHQCVD
PILAASTAII SLQYIVSRET DPDDPKVVSV TIVDGGSTSF DLIPESAIIS GTYRAYSKQS
FYGLRRRIEE VIAAQVAVHR CSVEIDFDGK EHPTIPPTIN DERLYEHAFH VSSMVVGEEN
TRISRKYLGS EDFAFYQEKV PGFFLLLGIR NEKFGSIHTA HSPYYTVDED VLSVGAAMHA
TFAYTYLVNS TNS
//
