ID   A0A3B4F7H1_9CICH        Unreviewed;       465 AA.
AC   A0A3B4F7H1;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 1 {ECO:0000256|ARBA:ARBA00018240};
OS   Pundamilia nyererei.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX   NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000006472.1, ECO:0000313|Proteomes:UP000261460};
RN   [1] {ECO:0000313|Ensembl:ENSPNYP00000006472.1}
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   AlphaFoldDB; A0A3B4F7H1; -.
DR   Ensembl; ENSPNYT00000006635.1; ENSPNYP00000006472.1; ENSPNYG00000004948.1.
DR   GeneTree; ENSGT00390000014894; -.
DR   Proteomes; UP000261460; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          14..147
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          265..348
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          377..443
FT                   /note="NADH-rubredoxin oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18267"
SQ   SEQUENCE   465 AA;  52178 MW;  4D234674566C1A3E CRC64;
     RRMENKKEKT FQFVVVGGGI AGVTCVELSY HFSEWLLMLT LEEFDVEEQP SSVLEEKFPN
     LTIIHSAVKS LHTKSHCVET ADGRVFGYKK LCICSGARPK LLTQDNPYVL GIRDTDSAQE
     FQKRLSKAKR IVIVGNGGIA LELVYEVEGC EVIWAVKDKA IGNTFFDAGA AQFLIPSLEA
     DKPQAAAPCK RPRFTTEEAP ECSTQFILSY CPPVLMNPLT LLAFAQVSHR VSVEYQCEVE
     KIFTCEELHK SPEQTLRTEY WPVYVRLTNA QTFGCDFVVS ATGVVPNTEP FLQGNTFVVA
     DDGGLQVDDH MMTSEADVYA AGDVCTACWE QSPLWQQMRL WTQARQMGWY AGRCMAAHIL
     SEPVELDFCF ELFSHITKFF NYKVVLLGKF NGQGLGPDHE LLVRCTKGQE YVKVVLSGGR
     MVGAVLIGET DLEETFENLI LNQMDLTPYG EELLNPDIDI EDYFD
//