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Database: UniProt
Entry: D2V6C0_NAEGR
LinkDB: D2V6C0_NAEGR
Original site: D2V6C0_NAEGR 
ID   D2V6C0_NAEGR            Unreviewed;       530 AA.
AC   D2V6C0;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 62.
DE   SubName: Full=Predicted protein {ECO:0000313|EMBL:EFC47543.1};
GN   ORFNames=NAEGRDRAFT_31574 {ECO:0000313|EMBL:EFC47543.1};
OS   Naegleria gruberi (Amoeba).
OC   Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC   Vahlkampfiidae; Naegleria.
OX   NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN   [1] {ECO:0000313|EMBL:EFC47543.1, ECO:0000313|Proteomes:UP000006671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEG-M {ECO:0000313|EMBL:EFC47543.1,
RC   ECO:0000313|Proteomes:UP000006671};
RX   PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA   Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA   Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA   Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA   Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT   "The genome of Naegleria gruberi illuminates early eukaryotic
RT   versatility.";
RL   Cell 140:631-642(2010).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532,
CC       ECO:0000256|RuleBase:RU003691}.
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DR   EMBL; GG738854; EFC47543.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2V6C0; -.
DR   STRING; 5762.D2V6C0; -.
DR   EnsemblProtists; EFC47543; EFC47543; NAEGRDRAFT_31574.
DR   VEuPathDB; AmoebaDB:NAEGRDRAFT_31574; -.
DR   eggNOG; KOG4716; Eukaryota.
DR   InParanoid; D2V6C0; -.
DR   OMA; KWVNTEA; -.
DR   OrthoDB; 5473641at2759; -.
DR   Proteomes; UP000006671; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
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; IPR046952; GSHR/TRXR-like.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   InterPro; IPR006338; Thioredoxin/glutathione_Rdtase.
DR   NCBIfam; TIGR01438; TGR; 1.
DR   PANTHER; PTHR42737; GLUTATHIONE REDUCTASE; 1.
DR   PANTHER; PTHR42737:SF3; THIOREDOXIN-DISULFIDE REDUCTASE; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU003691};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003691};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003691};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW   ECO:0000256|RuleBase:RU003691};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006671}.
FT   DOMAIN          16..382
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          402..513
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
SQ   SEQUENCE   530 AA;  58732 MW;  B53D4D3A12719417 CRC64;
     MNLGGATNKQ EIPAHFDYIV IGGGSGGLSL SKQLSSLSSK ETRICLLDYR DPSSQWLRER
     NGKLNGWMWQ LGGTCVNVGC IPKKLMHNSA LIGEGINHDA EYFGWNDGKQ EGKLSGKHDW
     KTLVANVQQY IKSLNFGYRT SVTQTYAFDN EDPSLKKLYY LNMKGRFVDD HTLELTDPRK
     GITKTISGKV IILSVGGTPN IPQDVPGATE YAITSDDIFS LKEEPGKTLV IGASYIALET
     ASFLKGLGYE SSVMMRSIPL RGFDQECAWK VVDGMKERGV KFLEQCIPVK IEKSSDHETT
     GEYTVHYKDL STQQVYTENY KTIMFAVGRR AVTKELNIDL DMDESGKIIV SDNEQTSKKH
     IYAIGDCINK KTELTPVAIR AGKLLASRLT NKGTELMDYD NVPTSIFTHP YEYGCCGLSE
     EEAVQRYGED DIEVYISLYS PIEHQLSHRD TNKTFMKIIT LKSANEKVIG FHYVGANAGE
     ITQGIAVAIK AGATKEHFDN TIGIHPTAAE EMTLLSITKR SGNSAEKDGC
//
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