ID A0A1R3KCW9_COCAP Unreviewed; 292 AA.
AC A0A1R3KCW9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Lipoxygenase {ECO:0000313|EMBL:OMP04940.1};
DE Flags: Fragment;
GN ORFNames=CCACVL1_02091 {ECO:0000313|EMBL:OMP04940.1};
OS Corchorus capsularis (Jute).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX NCBI_TaxID=210143 {ECO:0000313|EMBL:OMP04940.1, ECO:0000313|Proteomes:UP000188268};
RN [1] {ECO:0000313|EMBL:OMP04940.1, ECO:0000313|Proteomes:UP000188268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. CVL-1 {ECO:0000313|Proteomes:UP000188268};
RC TISSUE=Whole seedling {ECO:0000313|EMBL:OMP04940.1};
RA Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA Rashid M.M., Khan S.A., Rahman M.S., Alam M.;
RT "Corchorus capsularis genome sequencing.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the lipoxygenase family.
CC {ECO:0000256|ARBA:ARBA00009419}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00152}.
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:OMP04940.1}.
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DR EMBL; AWWV01005542; OMP04940.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R3KCW9; -.
DR STRING; 210143.A0A1R3KCW9; -.
DR EnsemblPlants; OMP04940; OMP04940; CCACVL1_02091.
DR Gramene; OMP04940; OMP04940; CCACVL1_02091.
DR OrthoDB; 1121515at2759; -.
DR Proteomes; UP000188268; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0034440; P:lipid oxidation; IEA:InterPro.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd01751; PLAT_LH2; 1.
DR Gene3D; 2.60.60.20; PLAT/LH2 domain; 1.
DR InterPro; IPR000907; LipOase.
DR InterPro; IPR013819; LipOase_C.
DR InterPro; IPR036226; LipOase_C_sf.
DR InterPro; IPR001246; LipOase_plant.
DR InterPro; IPR042057; Lipoxy_PLAT/LH2.
DR InterPro; IPR001024; PLAT/LH2_dom.
DR InterPro; IPR036392; PLAT/LH2_dom_sf.
DR PANTHER; PTHR11771:SF126; LINOLEATE 9S-LIPOXYGENASE 1; 1.
DR PANTHER; PTHR11771; LIPOXYGENASE; 1.
DR Pfam; PF00305; Lipoxygenase; 1.
DR Pfam; PF01477; PLAT; 1.
DR PRINTS; PR00468; PLTLPOXGNASE.
DR SMART; SM00308; LH2; 1.
DR SUPFAM; SSF49723; Lipase/lipooxygenase domain (PLAT/LH2 domain); 1.
DR SUPFAM; SSF48484; Lipoxigenase; 1.
DR PROSITE; PS51393; LIPOXYGENASE_3; 1.
DR PROSITE; PS50095; PLAT; 1.
PE 3: Inferred from homology;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Oxylipin biosynthesis {ECO:0000256|ARBA:ARBA00022767};
KW Reference proteome {ECO:0000313|Proteomes:UP000188268};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..292
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012774349"
FT DOMAIN 79..210
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT DOMAIN 213..292
FT /note="Lipoxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51393"
FT REGION 255..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 292
FT /evidence="ECO:0000313|EMBL:OMP04940.1"
SQ SEQUENCE 292 AA; 31684 MW; CEB648682BB82BEC CRC64;
MASPNHNKLL CVLVLVVSCM LAVAPMATAA RCSGIVCDLH GIVDGVITTA GNVVNGIIGG
KNEPQKIKGT VVLTKKNFLD FNALASSAMD NVYELLGQKV TLQLISADTA DPANGNGGKL
GKAASLEKTW NPTSLLTSLL ASDSTYGVSF EWDEGFGTPG AIIVRNNQAS EFYLKTITLE
DVPGAGRIHF VCNSWIYPDN QYKKPRIFFS NKLYLPHEMP APLRKYRQEE LEVLRGDGKT
QLKTGDRVYD YATYNDLGNP DSNPGLARPI LGGSVEHPYP RRGRTSRPPS RS
//
