ID   PYRD1_BOVIN             Reviewed;         502 AA.
AC   A7YVH9;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 1;
DE            EC=1.8.1.-;
GN   Name=PYROXD1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal muscle;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probable FAD-dependent oxidoreductase; involved in the
CC       cellular oxidative stress response (By similarity). Required for normal
CC       sarcomere structure and muscle fiber integrity (By similarity).
CC       {ECO:0000250|UniProtKB:Q6PBT5, ECO:0000250|UniProtKB:Q8WU10}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:O52582};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:O52582};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8WU10}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q3TMV7}. Cytoplasm, myofibril, sarcomere
CC       {ECO:0000250|UniProtKB:Q8WU10}.
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. PYROXD1 subfamily. {ECO:0000305}.
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DR   EMBL; BC123726; AAI23727.1; -; mRNA.
DR   RefSeq; NP_001098804.1; NM_001105334.1.
DR   AlphaFoldDB; A7YVH9; -.
DR   SMR; A7YVH9; -.
DR   STRING; 9913.ENSBTAP00000050877; -.
DR   PaxDb; A7YVH9; -.
DR   PRIDE; A7YVH9; -.
DR   GeneID; 505859; -.
DR   KEGG; bta:505859; -.
DR   CTD; 79912; -.
DR   eggNOG; KOG2755; Eukaryota.
DR   HOGENOM; CLU_026335_0_0_1; -.
DR   InParanoid; A7YVH9; -.
DR   OrthoDB; 1463391at2759; -.
DR   TreeFam; TF105963; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0030017; C:sarcomere; ISS:UniProtKB.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0034599; P:cellular response to oxidative stress; ISS:UniProtKB.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; -; 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   Pfam; PF07992; Pyr_redox_2; 2.
DR   Pfam; PF18267; Rubredoxin_C; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; FAD; Flavoprotein; NADP; Nucleus; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..502
FT                   /note="Pyridine nucleotide-disulfide oxidoreductase domain-
FT                   containing protein 1"
FT                   /id="PRO_0000327418"
FT   REGION          208..231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..223
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WU10"
SQ   SEQUENCE   502 AA;  55876 MW;  7ACBBD4EB998A9D4 CRC64;
     MEAPCSPPTA GKFVVVGGGI AGVTCAEQLA INFPSEDILL ITASPVIKAV TNFKQVSKVL
     EEFDVEEQPS TMLENRFPNI KVIESGVKQL KSKEHCVLTE DGNQHIYKKL CLCAGAKPKL
     ICEGNPYVLG IRDTDSAQEF QKQLTKAKRI MIIGNGGIAL ELVYEIEGCE VIWVIKDKAI
     GNTFFDAGAA EFLTSKLIDE KPEAKIAQKR TRYTTEGRKK ETQARASAGN VGSALGPDWH
     EGLDLKGTKE FSHKIHIETM CEVKKIYLQE EFRISEKKSL TFPRDHHDQS VTTDKEIWPV
     YVELTNEKIY GCDFIVSATG VTPNTEPFLC GNNFDVGEDG GLKVDDHMHT SLPDIYAAGD
     ICTAAWHPSP VWQQMRLWTQ ARQMGWYAAK CMAAASVGES IDMDFSFELF AHVTKFFNYK
     VVLLGKYNAQ GLGSNHELLL RCTKGQEYIK AVLQNGRMMG AVLIGETDLE ETFENLILNQ
     MNLSAYGEDL LDPNIDIEDY FD