ID E4WRG4_OIKDI Unreviewed; 770 AA.
AC E4WRG4;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=GSOID_T00000338001 {ECO:0000313|EMBL:CBY20345.1};
OS Oikopleura dioica (Tunicate).
OC Eukaryota; Metazoa; Chordata; Tunicata; Appendicularia; Copelata;
OC Oikopleuridae; Oikopleura.
OX NCBI_TaxID=34765 {ECO:0000313|EMBL:CBY20345.1};
RN [1] {ECO:0000313|EMBL:CBY20345.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21097902; DOI=10.1126/science.1194167;
RA Denoeud F., Henriet S., Mungpakdee S., Aury J.M., Da Silva C.,
RA Brinkmann H., Mikhaleva J., Olsen L.C., Jubin C., Canestro C.,
RA Bouquet J.M., Danks G., Poulain J., Campsteijn C., Adamski M., Cross I.,
RA Yadetie F., Muffato M., Louis A., Butcher S., Tsagkogeorga G., Konrad A.,
RA Singh S., Jensen M.F., Cong E.H., Eikeseth-Otteraa H., Noel B.,
RA Anthouard V., Porcel B.M., Kachouri-Lafond R., Nishino A., Ugolini M.,
RA Chourrout P., Nishida H., Aasland R., Huzurbazar S., Westhof E., Delsuc F.,
RA Lehrach H., Reinhardt R., Weissenbach J., Roy S.W., Artiguenave F.,
RA Postlethwait J.H., Manak J.R., Thompson E.M., Jaillon O., Du Pasquier L.,
RA Boudinot P., Liberles D.A., Volff J.N., Philippe H., Lenhard B.,
RA Roest Crollius H., Wincker P., Chourrout D.;
RT "Plasticity of animal genome architecture unmasked by rapid evolution of a
RT pelagic tunicate.";
RL Science 330:1381-1385(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + H(+) + NADH = AH2 + NAD(+); Xref=Rhea:RHEA:11356,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000256|ARBA:ARBA00000272};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00006442}.
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DR EMBL; FN653015; CBY20345.1; -; Genomic_DNA.
DR AlphaFoldDB; E4WRG4; -.
DR InParanoid; E4WRG4; -.
DR Proteomes; UP000001307; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR029324; AIF_C.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR PANTHER; PTHR43557; APOPTOSIS-INDUCING FACTOR 1; 1.
DR PANTHER; PTHR43557:SF4; APOPTOSIS-INDUCING FACTOR 1, MITOCHONDRIAL; 1.
DR Pfam; PF14721; AIF_C; 2.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SMART; SM01353; AIF_C; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 3: Inferred from homology;
KW Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001307};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 329..652
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 657..709
FT /note="Mitochondrial apoptosis-inducing factor C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14721"
FT DOMAIN 711..751
FT /note="Mitochondrial apoptosis-inducing factor C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14721"
FT REGION 84..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 770 AA; 83914 MW; 909989F50AB4003D CRC64;
MYRAFRNGSA AYKRFMPSVR NAAQSPYEKR GMGVNELAGI AGVSAFLFYA TSQQSSTPEK
SAKPQKVPPK GVAKEALQLE NPIDSLKEIS DIGSPNDPKP AKEEVAPVVQ ESVKEEVSTE
SEPIVEEPIV AESVVEVVQD TEVIVKAEPI VEAESVVEAE PIVVTEPVVE AEPVVEAEPI
AEPIVEAEQV VEAESEAEAE PIVVAEPVVE AEPVPEPVVE AEPIVVAESV VEPEPVVVAE
ESSEQAVESD PIPEPAEVAT QTEPEVESPK TIKSSDAATV SPYENVDPIV TEAGSAVEVD
PVTDEIIPLV EEQNSVKKIY PEVPPEVEYL IVGGGTAAYS AVRAIRKYDP TAKILIVSDE
PEMPYNRTPL SKELWFETEE NAALGKYKGW DDKERVIFHE KLENYCTGRD LQEREGYGGT
ALLLGAKVDR LDADRKKAIL YNGTEIGYGK VLLSIGGKPR NLPEFESVGD KVTLFRDLKD
FRQLSAISQK GGDVVVVGSG FLGTELSFAL AERAKKVENL KVSQICREQG VLGAVLPEHL
SNFSSEVLEK EGVNIVRNAE IAGVSEDSDK LLVNLKDGRS VPADHVVLAV GVDIDHGLAE
RSGLEVDSNR GGFIVNSELE SRKDIFVAGD AANFYDQRLG RRRVEHYDHA IVTGRLAGEN
MVGMRKAYTH QSMFWSDIGA DNGFEAIGLV DSKLKSVSVF AQPEEQNTEG GNFNERKFDK
GVVFYLRNES VVGVVTWNIF GKMGVARRLL AHKSEELDFA EMARLFNVHK
//
