ID A0A151NHV1_ALLMI Unreviewed; 706 AA.
AC A0A151NHV1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=FAD-dependent oxidoreductase domain-containing protein 2 isoform B {ECO:0000313|EMBL:KYO36391.1};
GN Name=FOXRED2 {ECO:0000313|EMBL:KYO36391.1};
GN ORFNames=Y1Q_0024142 {ECO:0000313|EMBL:KYO36391.1};
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO36391.1};
RN [1] {ECO:0000313|EMBL:KYO36391.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO36391.1};
RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA Ray D.A.;
RT "Sequencing three crocodilian genomes to illuminate the evolution of
RT archosaurs and amniotes.";
RL Genome Biol. 13:415-415(2012).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYO36391.1}.
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DR EMBL; AKHW03002956; KYO36391.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151NHV1; -.
DR eggNOG; KOG1399; Eukaryota.
DR Proteomes; UP000050525; Unassembled WGS sequence.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR CDD; cd02947; TRX_family; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR005746; Thioredoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR NCBIfam; TIGR01068; thioredoxin; 1.
DR PANTHER; PTHR43601; THIOREDOXIN, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43601:SF3; THIOREDOXIN, MITOCHONDRIAL; 1.
DR Pfam; PF13738; Pyr_redox_3; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Reference proteome {ECO:0000313|Proteomes:UP000050525};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 589..705
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 706 AA; 79990 MW; 8BE0FDDCBDA7BB21 CRC64;
MAYFLQQASR DYVVFERSHT PGSFFALYPR HRKLISINKR LELQVQYNTA ITHVTLDRDP
QAWNGHYFIL TDQNSQTYRC SLLLVATGTW VPNVVSFTGS EYVEGYETVS INPEDFAGQT
VLILGRGNSA FETAENILGV TNFIHMVSRS RVRLSWATHY VGDLRAINNG LLDTYQLKSL
DGLLEGDLED LAIVKDKKGK LHITLRFYLE NSNSSAGAET ITLPQDELDN FATRAPYDRV
IRCLGWKFDF SIYNRSLRLV PGRGNKRKYP QIKPSYESRG TRGLFVLGTA SHSNDFRKSA
GGFIHGFRYT TRAVHRLLEN RHHGVPWPSP IYPITHLTNS IIKRVNEASG LYQMFSVLAD
IILLKENATA FEYLEEYPVG ILAQLELHTG RKAPGGLFAV IMEYGRNFSG ADKDVFYYNR
AVGEAQHAWQ SNFLHPVIYY YKRLPTEREM RLRPPDWPLP RPDAIHHIVE DFLTDWTAPN
AHILPLRRFL ENCLGTDLRN FFAESCFLFA LTRQKLPPSC QQGYLRMQGL VGSEGLRRHA
VEASLMENYT VVDTPNELLG GQKDIHDQLL KDHVIPTNEV AACPGSAREL RRPPGPGRST
FNVQDGEDFQ DRVINSAKPV VIDFHAQWCG PCKILGPRLE KMVAKQQGKV LMAKVDIDDH
TDLAIEYEVS AVPTVLAMKN GDVVDKFVGI KDEDQLEAFL KKLIGA
//
