ID A0A3L8RTI7_CHLGU Unreviewed; 465 AA.
AC A0A3L8RTI7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 22-FEB-2023, entry version 11.
DE RecName: Full=Lipoxygenase domain-containing protein {ECO:0000259|PROSITE:PS51393};
GN ORFNames=DV515_00016003 {ECO:0000313|EMBL:RLV85399.1};
OS Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC Chloebia.
OX NCBI_TaxID=44316 {ECO:0000313|EMBL:RLV85399.1, ECO:0000313|Proteomes:UP000276834};
RN [1] {ECO:0000313|EMBL:RLV85399.1, ECO:0000313|Proteomes:UP000276834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red01 {ECO:0000313|EMBL:RLV85399.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:RLV85399.1};
RX PubMed=30282656;
RA Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT "A non-coding region near Follistatin controls head colour polymorphism in
RT the Gouldian finch.";
RL Proc. R. Soc. B 285:0-0(2018).
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:RLV85399.1}.
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DR EMBL; QUSF01000239; RLV85399.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L8RTI7; -.
DR Proteomes; UP000276834; 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:0034440; P:lipid oxidation; IEA:InterPro.
DR Gene3D; 3.10.450.60; -; 1.
DR InterPro; IPR000907; LipOase.
DR InterPro; IPR013819; LipOase_C.
DR InterPro; IPR036226; LipOase_C_sf.
DR PANTHER; PTHR11771; LIPOXYGENASE; 1.
DR PANTHER; PTHR11771:SF161; POLYUNSATURATED FATTY ACID LIPOXYGENASE ALOX15B; 1.
DR Pfam; PF00305; Lipoxygenase; 1.
DR PRINTS; PR00087; LIPOXYGENASE.
DR SUPFAM; SSF48484; Lipoxigenase; 1.
DR PROSITE; PS51393; LIPOXYGENASE_3; 1.
PE 4: Predicted;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000276834}.
FT DOMAIN 1..465
FT /note="Lipoxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51393"
SQ SEQUENCE 465 AA; 52525 MW; 806995DCAD25B589 CRC64;
MRTIFSRTQG RDIVPEYVAK HWQEDDFFGS QFLNGNNPII IRCCTTLPLK FPVTPEMVAG
SLGGGTDLGK ELQEGRIFIV DYKVLEDIPT DTIYGRQQYI AAPLCLLHQG TDGLLRPIAI
QLSQTPGPCS PIFLPSDDEW DWLLAKTWVR NADFYSHQLL THLLRTHLFG EVFAIATLRH
LPTCHPFFKL LIPHFHFTLH INTLARSVLI NQGGLIDKGS GVTYEGLLLV VQRGLEQVTY
TSLCLPDDIR HRGMSHVPNY HYRDDGMSLW EAIESFVTGI VTFYYGGDAA VSGDTELQAW
VMDIFTNGFL GRTSSGIPSS LQTVAELIKF LTMVMFTCSA QHAAVNNGQY DLGAFVPNAP
SSMRHPPPCE KGRAFLQHFL DTIPEVATTA NILVALILLS SQLKDRRLLG QYPEEWFTET
EPRRLIRAFQ GRLQEIRDRI EERNQVAELR YNYLNPLETE NSISI
//
