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Database: UniProt
Entry: A0A453M0N8_AEGTS
LinkDB: A0A453M0N8_AEGTS
Original site: A0A453M0N8_AEGTS 
ID   A0A453M0N8_AEGTS        Unreviewed;       686 AA.
AC   A0A453M0N8;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:AET5Gv20994800.27};
OS   Aegilops tauschii subsp. strangulata (Goatgrass).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX   NCBI_TaxID=200361 {ECO:0000313|EnsemblPlants:AET5Gv20994800.27, ECO:0000313|Proteomes:UP000015105};
RN   [1] {ECO:0000313|Proteomes:UP000015105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX   PubMed=25035499; DOI=10.1126/science.1250092;
RG   International Wheat Genome Sequencing Consortium,;
RA   Marcussen T., Sandve S.R., Heier L., Spannagl M., Pfeifer M.,
RA   Jakobsen K.S., Wulff B.B., Steuernagel B., Mayer K.F., Olsen O.A.;
RT   "Ancient hybridizations among the ancestral genomes of bread wheat.";
RL   Science 345:1250092-1250092(2014).
RN   [2] {ECO:0000313|Proteomes:UP000015105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX   PubMed=29158546; DOI=10.1038/s41477-017-0067-8;
RA   Zhao G., Zou C., Li K., Wang K., Li T., Gao L., Zhang X., Wang H., Yang Z.,
RA   Liu X., Jiang W., Mao L., Kong X., Jiao Y., Jia J.;
RT   "The Aegilops tauschii genome reveals multiple impacts of transposons.";
RL   Nat. Plants 3:946-955(2017).
RN   [3] {ECO:0000313|EnsemblPlants:AET5Gv20994800.27}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2019) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- COFACTOR:
CC       Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC         Evidence={ECO:0000256|ARBA:ARBA00001924};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|ARBA:ARBA00034078};
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DR   AlphaFoldDB; A0A453M0N8; -.
DR   EnsemblPlants; AET5Gv20994800.27; AET5Gv20994800.27; AET5Gv20994800.
DR   Gramene; AET5Gv20994800.27; AET5Gv20994800.27; AET5Gv20994800.
DR   Proteomes; UP000015105; Chromosome 5D.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 1.10.150.120; [2Fe-2S]-binding domain; 1.
DR   Gene3D; 3.90.1170.50; Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead; 1.
DR   Gene3D; 3.30.390.50; CO dehydrogenase flavoprotein, C-terminal domain; 1.
DR   InterPro; IPR002888; 2Fe-2S-bd.
DR   InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b.
DR   InterPro; IPR036856; Ald_Oxase/Xan_DH_a/b_sf.
DR   InterPro; IPR016208; Ald_Oxase/xanthine_DH-like.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR005107; CO_DH_flav_C.
DR   InterPro; IPR036683; CO_DH_flav_C_dom_sf.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR002346; Mopterin_DH_FAD-bd.
DR   PANTHER; PTHR11908:SF162; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR11908; XANTHINE DEHYDROGENASE; 1.
DR   Pfam; PF01315; Ald_Xan_dh_C; 1.
DR   Pfam; PF03450; CO_deh_flav_C; 1.
DR   Pfam; PF00941; FAD_binding_5; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   Pfam; PF01799; Fer2_2; 1.
DR   SMART; SM01008; Ald_Xan_dh_C; 1.
DR   SMART; SM01092; CO_deh_flav_C; 1.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF55447; CO dehydrogenase flavoprotein C-terminal domain-like; 1.
DR   SUPFAM; SSF47741; CO dehydrogenase ISP C-domain like; 1.
DR   SUPFAM; SSF54665; CO dehydrogenase molybdoprotein N-domain-like; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Iron {ECO:0000256|ARBA:ARBA00022714};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022714};
KW   Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015105}.
FT   DOMAIN          13..100
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          245..423
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   686 AA;  72649 MW;  5CD3C25A7771F9A8 CRC64;
     MGSLGKDAAA AAERVVLAVN SARHEAAGVD PSTTLLEFLR TRTPVRGPKL GCGEGGCGAC
     VVLISKYDPA TDEVTEFSAS SCLTLVGSLN HCSVTTSEGI GNTRDGYHPV QQRLAGFHAS
     QCGFCTPGMC MSIFSSLVKA DKPGTTTAGD HAPPPGFSKL TCAEAEHAVS GNLCRCTGYR
     PILDACKSFA ADVDLEDLGL NSFWKKGTDR ADVGKLPEYS SGSVCTFPEF LKSEIKGQMN
     DVPAAIAGED GWYHPRSIQE LHSLFDSNWF DENSVKIVAS NTGAGVYKDQ DLYDKYIDIK
     GIAELSVIDR NSKGLEIGAA VSISKAIEVF SDGTPVFRKI ASHLSKVASP FVRNTATVGG
     NVIMAQRLQF PSDIATVLLA AGSTVTIQTA SKMLCLTLDE FLEQPPCDAK TILLSIFVPD
     WGSDNVIFET SRVAPRPFGN AVSYVNSAFL ARTSGDGASG ELIIEDICLA FGAYGVDHTT
     RARKVEEFLK GQSVSAPVIL EAVRLLKDTI MPSEGTTHPE YRVSLAVSFL FSFLSSLGNN
     QIEPAKAIAP NGSCANGSMN GQVASEDLQI RSRQELVFND EYKPVGKPIT KSGAELQASG
     EAVYVDDIPA PKDCIYGAFI YSTHPHAHIK GVNFRPSLAS EKVIGVITAK DIPAGGKNVG
     AGINMLGTEA LFGDPVSEFA GQNIGI
//
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