ID D7FVT3_ECTSI Unreviewed; 651 AA.
AC D7FVT3;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE SubName: Full=Alternative oxidase, mitochondrial protein {ECO:0000313|EMBL:CBJ25453.1};
GN Name=quinol-to-oxygen {ECO:0000313|EMBL:CBJ25453.1};
GN ORFNames=Esi_0003_0013 {ECO:0000313|EMBL:CBJ25453.1};
OS Ectocarpus siliculosus (Brown alga) (Conferva siliculosa).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; PX clade; Phaeophyceae;
OC Ectocarpales; Ectocarpaceae; Ectocarpus.
OX NCBI_TaxID=2880 {ECO:0000313|EMBL:CBJ25453.1, ECO:0000313|Proteomes:UP000002630};
RN [1] {ECO:0000313|EMBL:CBJ25453.1, ECO:0000313|Proteomes:UP000002630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ec32 / CCAP1310/4 {ECO:0000313|Proteomes:UP000002630};
RX PubMed=20520714; DOI=10.1038/nature09016;
RA Cock J.M., Sterck L., Rouze P., Scornet D., Allen A.E., Amoutzias G.,
RA Anthouard V., Artiguenave F., Aury J.M., Badger J.H., Beszteri B.,
RA Billiau K., Bonnet E., Bothwell J.H., Bowler C., Boyen C., Brownlee C.,
RA Carrano C.J., Charrier B., Cho G.Y., Coelho S.M., Collen J., Corre E.,
RA Da Silva C., Delage L., Delaroque N., Dittami S.M., Doulbeau S., Elias M.,
RA Farnham G., Gachon C.M., Gschloessl B., Heesch S., Jabbari K., Jubin C.,
RA Kawai H., Kimura K., Kloareg B., Kupper F.C., Lang D., Le Bail A.,
RA Leblanc C., Lerouge P., Lohr M., Lopez P.J., Martens C., Maumus F.,
RA Michel G., Miranda-Saavedra D., Morales J., Moreau H., Motomura T.,
RA Nagasato C., Napoli C.A., Nelson D.R., Nyvall-Collen P., Peters A.F.,
RA Pommier C., Potin P., Poulain J., Quesneville H., Read B., Rensing S.A.,
RA Ritter A., Rousvoal S., Samanta M., Samson G., Schroeder D.C., Segurens B.,
RA Strittmatter M., Tonon T., Tregear J.W., Valentin K., von Dassow P.,
RA Yamagishi T., Van de Peer Y., Wincker P.;
RT "The Ectocarpus genome and the independent evolution of multicellularity in
RT brown algae.";
RL Nature 465:617-621(2010).
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|ARBA:ARBA00001962};
CC -!- SIMILARITY: Belongs to the alternative oxidase family.
CC {ECO:0000256|ARBA:ARBA00008388}.
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DR EMBL; FN648486; CBJ25453.1; -; Genomic_DNA.
DR AlphaFoldDB; D7FVT3; -.
DR STRING; 2880.D7FVT3; -.
DR EnsemblProtists; CBJ25453; CBJ25453; Esi_0003_0013.
DR eggNOG; ENOG502QRMM; Eukaryota.
DR InParanoid; D7FVT3; -.
DR OrthoDB; 36821at2759; -.
DR Proteomes; UP000002630; Chromosome LG02.
DR GO; GO:0043229; C:intracellular organelle; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0009916; F:alternative oxidase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 1.20.1260.140; Alternative oxidase; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR InterPro; IPR002680; AOX.
DR InterPro; IPR038659; AOX_sf.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR31803; ALTERNATIVE OXIDASE; 1.
DR PANTHER; PTHR31803:SF19; UBIQUINOL OXIDASE; 1.
DR Pfam; PF01786; AOX; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR SMART; SM00100; cNMP; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000002630};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 408..428
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 67..115
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT REGION 523..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..651
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 651 AA; 73193 MW; ECACDDE3BEFCA59D CRC64;
MAVWGRTGTI RDCPPLDSPA GAGLAKEGIT EREWAALLKV GEVISLKGSE LLISQGDTYD
EPGDRQLYLL SDGECRIEVK GKPVASIAPG DFVGEASFTS GRVQPRTATV RAKSDEIRVM
AWTWRDLQAF MDNPKNLRTK AALQAIWMEG LAGKLNDVMS ALGGQSVVEL AEEDKTRAGD
YGYRYLEDTR EVESIVPISA STLAWWTFTR EYRALRRTFR FGEFKDTGIA GPFSIIDRFL
ETSVFPVLRP SRVDLPQDPE VVDLQNRLNE LKLSNKAIED RETARIAATK AFLEDESRKG
LRAAGYILRS QTPWYVMAPY KALCWFLDVV FEDRPIQRFW FLETVARMPY FSYLSMLFLY
ETLGWWSGAA EVRKVHFAEE YNEMQHLRIM ESLGGDTRWS DRFLARHAAI IYFSVLILGY
LVSPFLAYNF SELIESHAVD TYTEFAEANE ELLKSLPPTP QALDYYHGGD MYLFDEFQTS
RPAFSRRPRI QNLYDVFSCI RDDELEHVKT MFACERGTGA LPSPNAAAAT PRWAQDATPT
MPNATAPNIR RNTVKRAETD DAGGGGRSGG SDKLRTDIAR KTPLEAFTAA FNPLRDLVKA
VEKRDVTEKL RRGRDNGGEQ GTDSAVGARG GEEEKIDVSA SRKEPEEKQD S
//
