ID M7BC47_CHEMY Unreviewed; 800 AA.
AC M7BC47;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=FAD-dependent oxidoreductase domain-containing protein 2 {ECO:0000313|EMBL:EMP33150.1};
GN ORFNames=UY3_09712 {ECO:0000313|EMBL:EMP33150.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP33150.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
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DR EMBL; KB537019; EMP33150.1; -; Genomic_DNA.
DR AlphaFoldDB; M7BC47; -.
DR STRING; 8469.M7BC47; -.
DR eggNOG; KOG1399; Eukaryota.
DR Proteomes; UP000031443; 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; PTHR43539:SF78; FAD-DEPENDENT OXIDOREDUCTASE DOMAIN-CONTAINING PROTEIN 2; 1.
DR PANTHER; PTHR43539; FLAVIN-BINDING MONOOXYGENASE-LIKE PROTEIN (AFU_ORTHOLOGUE AFUA_4G09220); 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..800
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004079973"
FT DOMAIN 667..799
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 800 AA; 90543 MW; 1A3F575DB921D212 CRC64;
MAPPAAQCPW GLLLIFAFYL GSSCTDSASA LPHHDYCIIG AGPSGLQMAY FLQRAGRDYV
VFERSHAPGS FFALYPRHRK LISINKRHTG KSNSEFNLRH DWNSLLSHDS RLLFQHYSHD
FFPEADTMVR YLEDFASMLE LRVQYNTAII HVRLERDSQA WNGHYFILTD HNSQDYRCSL
LLVATGTWVP NVVNFPGSEY VEGYESVSIN PENFAGQTVL ILGRGNSAFE TAENILGVTN
FIHMVSRSRV RLSWATHYVG DLRAINNGLL DTYQLKSLDG LLEGDLEDLA IVKDKKGKLH
ITLKFYLENS NSSAGAESIT LPQDELDNFA TRAPYDRVIR CLGWKFDFSI YNRSLRLMPG
KGNKKKYPLI KPSYESRGTL GLFVLGAASH SIDFRKSAGG FIHGFRYTTR AVHRLLEHRH
HGVPWPASIY PITQLTNSII KRVNEASGLY QMFSVLGDII LLRENATAFE YLEEYPVGIL
AELELHTGRK AHNGLFVVIM EYGKNFSGAD KDVFYYNRAV GEAQHAWQSN FLHPVIYYYK
RLPTEREMRL CPPDWPLPRP DAVHHIVEDF LTDWTAPNAH ILPLRRFLEN CLDTDLRSFF
AESCFLFALT HRKLPPFCQQ GYLRMQGLVG NKRLRHHAVE AGLLEDHTVM HSTDELLGGQ
RGSCDQLLKD HVIPGLNLKE GAGTFSTTPV CRATFNIQDG SDFQDRVVNS QKPVVVDFHA
QWCGPCKILG PRLEKMVAKQ QGKVLMAKVD IDDHTDLAIE YEVSAVPTVL AMKNGDVVDK
FVGIKDEDQL EAFLKKLIGA
//
