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Database: UniProt
Entry: A0A2K6DK31_MACNE
LinkDB: A0A2K6DK31_MACNE
Original site: A0A2K6DK31_MACNE 
ID   A0A2K6DK31_MACNE        Unreviewed;       500 AA.
AC   A0A2K6DK31;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 1 {ECO:0000256|ARBA:ARBA00018240};
GN   Name=PYROXD1 {ECO:0000313|Ensembl:ENSMNEP00000036253.1};
OS   Macaca nemestrina (Pig-tailed macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000036253.1, ECO:0000313|Proteomes:UP000233120};
RN   [1] {ECO:0000313|Ensembl:ENSMNEP00000036253.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere
CC       {ECO:0000256|ARBA:ARBA00004204}.
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. PYROXD1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008147}.
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DR   RefSeq; XP_011719710.1; XM_011721408.1.
DR   AlphaFoldDB; A0A2K6DK31; -.
DR   STRING; 9545.ENSMNEP00000036253; -.
DR   Ensembl; ENSMNET00000060716.1; ENSMNEP00000036253.1; ENSMNEG00000041260.1.
DR   GeneID; 105469867; -.
DR   KEGG; mni:105469867; -.
DR   CTD; 79912; -.
DR   GeneTree; ENSGT00390000014894; -.
DR   OMA; MCENLIL; -.
DR   OrthoDB; 5488855at2759; -.
DR   Proteomes; UP000233120; Unplaced.
DR   Bgee; ENSMNEG00000041260; Expressed in adult mammalian kidney and 12 other cell types or tissues.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0030017; C:sarcomere; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:Ensembl.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 3.
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; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR041575; Rubredoxin_C.
DR   PANTHER; PTHR43429; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR43429:SF2; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE DOMAIN-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF07992; Pyr_redox_2; 2.
DR   Pfam; PF18267; Rubredoxin_C; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000233120}.
FT   DOMAIN          12..218
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          286..383
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          413..478
FT                   /note="NADH-rubredoxin oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18267"
FT   REGION          209..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        209..227
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   500 AA;  55788 MW;  6B744F0AE93E5DFE CRC64;
     MEAARPPATA GKFVVVGGGI AGVTCAEQLA TQFPSEDILL ITASPVIKAV TNFKQISKIL
     EEFDVEEQSS TMLEKRFPNI KVIESGVKQL KSEEHCIVTE DGNQHVYKKL CLCAGAKPKL
     ICEGNPYVLG IRDTDSAQEF QKQLTKAKRI MIIGNGGIAL ELVYEIEGCE VIWAIKDKAI
     GNTFFDAGAA EFLTSKLIAE KPEAKIAQKR TRYTTEGRKK EARSKSKADN VGSALGPDWH
     EGLNLKGTKE FSHKIHLETM CEVKKIYLQD EFRILKKKSF TFPRDPKSVT TDTEMWPVYV
     ELTNEKIYGC DFIVSATGVT PNVEPFLHGN SFNLGEDGGL KVDDHMHTSL PDVYAAGDIC
     TASWQLSPVW QQMRLWTQAR QMGWYAAKCM AAASLGDSID MDFSFELFAH VTKFFNYKVV
     LLGKYNAQGL GSDHELMLRC TKGQEYIKVV MQNGRMMGAV LIGETDLEET FENLILNQMN
     LSSYGEDLLD PNIDIEDYFD
//
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