ID R7VW69_COLLI Unreviewed; 492 AA.
AC R7VW69;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=L-amino-acid oxidase {ECO:0000313|EMBL:EMC90054.1};
DE Flags: Fragment;
GN ORFNames=A306_00869 {ECO:0000313|EMBL:EMC90054.1};
OS Columba livia (Rock dove).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX NCBI_TaxID=8932 {ECO:0000313|EMBL:EMC90054.1};
RN [1] {ECO:0000313|EMBL:EMC90054.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Blood {ECO:0000313|EMBL:EMC90054.1};
RX PubMed=23371554; DOI=10.1126/science.1230422;
RA Shapiro M.D., Kronenberg Z., Li C., Domyan E.T., Pan H., Campbell M.,
RA Tan H., Huff C.D., Hu H., Vickrey A.I., Nielsen S.C., Stringham S.A.,
RA Hu H., Willerslev E., Gilbert M.T., Yandell M., Zhang G., Wang J.;
RT "Genomic diversity and evolution of the head crest in the rock pigeon.";
RL Science 339:1063-1067(2013).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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; KB376311; EMC90054.1; -; Genomic_DNA.
DR AlphaFoldDB; R7VW69; -.
DR eggNOG; KOG0029; Eukaryota.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.90.660.10; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 1.10.405.10; Guanine Nucleotide Dissociation Inhibitor, domain 1; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR10742:SF355; AMINE OXIDASE; 1.
DR PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..492
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012633076"
FT DOMAIN 53..492
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EMC90054.1"
FT NON_TER 492
FT /evidence="ECO:0000313|EMBL:EMC90054.1"
SQ SEQUENCE 492 AA; 56052 MW; 9B5EF2189133463D CRC64;
PVLFQILLLV GLLGADEFPC FPDKDYEELL EIAKHGLKHT THPVNVVIVG AGISGLTAAK
LLRDAGHNVT VLEMSDRVGG RIWTYRPKGH DWYAELGAMR LPPSHRIVHE FIRQFNLRVT
PFREDNNTWY AVNRVRKRTE EVNENPDVLN YPVDPSEEGK SATQLYREAL NKAFQKFHGM
DCKDFIKKYD SFSTKEYLIK EGNLSRGAVQ MIGDLLNEDA GFYLSFISSV WNFEIFSNDS
FSEIVGGFDQ LPNAFHKMLP GVVRLNSAVE KIVQDKEKDE VQVFYQSVDT WAPKSITADY
VLVTSSAKAT RHIRFVPKLS ISKTNALRSV HYASSTKIVL ACSERFWEKD GIHGGRSITD
RPSRFIYYPN HNFSSGVGVI LASYTWNDDS EFFLPLTDDE CLDVVFQDLA YIHQVNKDHL
LSICNQHVIQ KWQLDRHSLG AFASLTPYQF TDYSRVLFQN EGRLYFAGEH AAQPHAWIEA
SMKSAIRAAR NI
//