ID   A0A2G5U9C5_9PELO        Unreviewed;       544 AA.
AC   A0A2G5U9C5;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 11.
DE   RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2 {ECO:0000256|ARBA:ARBA00040298};
GN   Name=Cni-F37C4.6 {ECO:0000313|EMBL:PIC36053.1};
GN   Synonyms=Cnig_chr_IV.g15194 {ECO:0000313|EMBL:PIC36053.1};
GN   ORFNames=B9Z55_015194 {ECO:0000313|EMBL:PIC36053.1};
OS   Caenorhabditis nigoni.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC36053.1, ECO:0000313|Proteomes:UP000230233};
RN   [1] {ECO:0000313|Proteomes:UP000230233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA   Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA   Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT   "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT   competition proteins.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probable oxidoreductase that may play a role as regulator of
CC       mitochondrial function. {ECO:0000256|ARBA:ARBA00037217}.
CC   -!- SUBUNIT: Interacts with COX5B; this interaction may contribute to
CC       localize PYROXD2 to the inner face of the inner mitochondrial membrane.
CC       {ECO:0000256|ARBA:ARBA00038825}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000256|ARBA:ARBA00004305}.
CC   -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00006046}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PIC36053.1}.
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DR   EMBL; PDUG01000004; PIC36053.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5U9C5; -.
DR   Proteomes; UP000230233; Chromosome iv.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR10668; PHYTOENE DEHYDROGENASE; 1.
DR   PANTHER; PTHR10668:SF103; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE DOMAIN-CONTAINING PROTEIN 2; 1.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   Pfam; PF13450; NAD_binding_8; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000230233}.
FT   DOMAIN          246..358
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   544 AA;  60393 MW;  691A6DC6A0375586 CRC64;
     MSFRICRRYF SKQSYDAIII GGGHNGLTAA AYLAKAGKKV CVLERRHVLG GAAVTEEIVP
     GFRFSRASYL LSLLRPVVMQ ELNLKKFGLR YHIRNPNSFT PIRDTHGSLT LGMDMAENQR
     EIAKFSKADA ENYPKYEHFI SEVTHAFEQL MDYEPLDLQK PIHKMLPHLY LLYKAVQPLG
     LRNAVDFYEL MTAPISKIMN KWFESDVLKA TLGTDGVIGL AASPMDPGTG YVLLHHVIGG
     LDEHKGAWGY VVGGMGAVSN AIAECAKSHG VEIFTEQEVD EVLLDGNVAK GVRLANGREI
     HSKIVMSNAT PHVTFNNLVK KEHLPADFYR SVSQIDYTSP VTKINVAVKE LPNFLAKPNL
     GSEPMPHHQT TIHMNCENMQ VVHDAVMDYK NGRYSRRPVI EMTIPSSVDR TIVDSEDGHV
     VLLFTQYTPF SPKDHEWTEE KKTEYAKHVF SEIDAYAPNF SSSVIGYDIL TPPDIQNTFG
     ITGGNIFHGS MSLDQLYTSR PVSKWANYST PIESLYLCGS GAHPGGGVTG APGRLSALHA
     LKHF
//