ID A0A3Q3F5R4_KRYMA Unreviewed; 488 AA.
AC A0A3Q3F5R4;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 1 {ECO:0000256|ARBA:ARBA00018240};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000008892.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000008892.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 AlphaFoldDB; A0A3Q3F5R4; -.
DR Ensembl; ENSKMAT00000009027.1; ENSKMAP00000008892.1; ENSKMAG00000006649.1.
DR GeneTree; ENSGT00390000014894; -.
DR OMA; MCENLIL; -.
DR Proteomes; UP000264800; Unplaced.
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 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; 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000264800}.
FT DOMAIN 12..167
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 288..371
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 401..465
FT /note="NADH-rubredoxin oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18267"
FT REGION 222..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 488 AA; 53313 MW; 7478C2AAEDF5B20D CRC64;
TAMAGKQVKK FEFVVVGGGI AGVTCVEQVA SRFPSADVAL ITAGLQIKAV TNYKQVSKTL
EEFDVEERPS GVLEERFPNL TVIHSAVKSL HTHSHCVETA DGRVFGYKKL CLCSGARPKL
LTQDDPRVLG IRDTDSAQEF QKRLSKAKRI VVVGNGGIGL ELVYEVEGCE VIWAVKDKAI
GNAFFDAGAA QFLIPALEAD KPQAAAPCRR LCYTTEEPGP GAAQTFTAGG TSRGRSSGSV
EPGSALGPDW HREPDLLISS YSPSPGLFFF DFHSFILKSS EGSWPVYIQL TNGKAVGCDF
VVSATGVVPN TEPFLRGNSF AVADDGGLQV DDHMRTSEPD VYAAGDVCTA CWEHSPLWQQ
MRLWTQARQM GWHAGRCVAA DVLSEPIELD FCFELFSHVT KFFNHKVVLL GRFNAQGLGS
DHELLVRCTK GREYVKVVLS RGRMVGAVLI GETDLEETFE NLMLNRMDLT AYGEELLNPD
VDIEDYFD
//