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Database: UniProt
Entry: A0A3B4BSY2_PYGNA
LinkDB: A0A3B4BSY2_PYGNA
Original site: A0A3B4BSY2_PYGNA 
ID   A0A3B4BSY2_PYGNA        Unreviewed;       926 AA.
AC   A0A3B4BSY2;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Apoptosis inducing factor mitochondria associated 1 {ECO:0000313|Ensembl:ENSPNAP00000001625.1};
OS   Pygocentrus nattereri (Red-bellied piranha).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Pygocentrus.
OX   NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000001625.1, ECO:0000313|Proteomes:UP000261440};
RN   [1] {ECO:0000313|Ensembl:ENSPNAP00000001625.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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   RefSeq; XP_017577365.1; XM_017721876.1.
DR   AlphaFoldDB; A0A3B4BSY2; -.
DR   STRING; 42514.ENSPNAP00000001625; -.
DR   Ensembl; ENSPNAT00000011840.1; ENSPNAP00000001625.1; ENSPNAG00000008292.1.
DR   GeneID; 108442043; -.
DR   CTD; 9131; -.
DR   GeneTree; ENSGT00940000156455; -.
DR   OrthoDB; 74731at2759; -.
DR   Proteomes; UP000261440; Unplaced.
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   InterPro; IPR032773; MGARP_N.
DR   PANTHER; PTHR43557; APOPTOSIS-INDUCING FACTOR 1; 1.
DR   PANTHER; PTHR43557:SF4; APOPTOSIS-INDUCING FACTOR 1, MITOCHONDRIAL; 1.
DR   Pfam; PF14962; AIF-MLS; 1.
DR   Pfam; PF14721; AIF_C; 1.
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; 2.
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   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          49..182
FT                   /note="Protein MGARP N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14962"
FT   DOMAIN          447..773
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          777..907
FT                   /note="Mitochondrial apoptosis-inducing factor C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14721"
FT   REGION          97..157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          257..320
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          401..435
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..282
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        410..424
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   926 AA;  98573 MW;  14AA99D4FAFCD6FE CRC64;
     MFTCKAVWNK LAPLAPLARA SSTLCRQGGK RAAVFRHERR PPLVQQAHMS SGPTGGGGEN
     AIYLVLVGAA CLGGGVYVYR TVSGDKARYE ERVTQISSRL GSPAAQPDAP VKTQPEAAAE
     AASESTKELT DQGAGDVESA TQPVVEEPAP PSVTAEVAAE VPSEPVSEVI LEPPEAESVQ
     EAPVLDPVPE PIIGASAPAS VPEPPVSEPC ITEPVVEEVT AAPETALEVA TPDVVLEAHI
     PEAAPEVIVP EVVPEVPEPE VAPETPEPEV VPEAPEPEVA PEMPEPEVVS EAPEPEVVSE
     APEPEMAPEM PEPEVVSEAP KPEVVSEAPE PEMAPEMPEP EVVLEAPEPE LALEIPEPKV
     VLEVPEPEVV PEVISEAPEP EGVMKPVVLV AEAVSAEPPP AAMVESESVP ETPPVTNSAS
     EPAPASTAAP VEPTPAVSEV PAHAPYLLIG GGTASFAAAR SIRARDPGAR VLIVTDEADL
     PYMRPPLSKE LWFSDDPAVT ETLRFKQWNG KERSIYFQPS SFYVSPMELE SVENGGVAVL
     TGKKVVHMDV RGNKVKLSDG AEISYDKCLI ATGGIPRNLQ VIERASEEVA KRTTLFRKIE
     DFKALEKVSH ELKSITIIGG GFLGSELACA LGRRSADLGL EVVQMFPERG NMGKVLPEYL
     SNWTTEKVKK EGVKVLAEAV VKNVSYKDGQ LEIKLKDGRA VKTDHIVAAV GLEPSVELAK
     SAGLEIDSDF GGFRVNAELQ ARSNIWVAGD AACFYDIKLG RRRVEHHDHA VVSGRLAGEN
     MTGARKPYWH QSMFWSDLGP DVGYEAIGIV DSSLPTVGVF AKATAKDTPR AATEQSGTGI
     RSESETEAVA GPIAGPIAVG TAPAPPPQQK EDYGKGVIFY LRDKVVVGIV LWNVFNRMPI
     ARKIIKDGEE HADLNEVAKL FNIHED
//
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