ID A0A061JDC3_TRYRA Unreviewed; 340 AA.
AC A0A061JDC3;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
GN ORFNames=TRSC58_00092 {ECO:0000313|EMBL:ESL12146.1};
OS Trypanosoma rangeli SC58.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Herpetosoma.
OX NCBI_TaxID=429131 {ECO:0000313|EMBL:ESL12146.1, ECO:0000313|Proteomes:UP000031737};
RN [1] {ECO:0000313|EMBL:ESL12146.1, ECO:0000313|Proteomes:UP000031737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC58 {ECO:0000313|EMBL:ESL12146.1,
RC ECO:0000313|Proteomes:UP000031737};
RA Stoco P.H., Wagner G., Gerber A., Zaha A., Thompson C., Bartholomeu D.C.,
RA Luckemeyer D.D., Bahia D., Loreto E., Prestes E.B., Lima F.M.,
RA Rodrigues-Luiz G., Vallejo G.A., Filho J.F., Monteiro K.M., Tyler K.M.,
RA de Almeida L.G., Ortiz M.F., Siervo M.A., de Moraes M.H., Cunha O.L.,
RA Mendonca-Neto R., Silva R., Teixeira S.M., Murta S.M., Sincero T.C.,
RA Mendes T.A., Urmenyi T.P., Silva V.G., da Rocha W.D., Andersson B.,
RA Romanha A.J., Steindel M., de Vasconcelos A.T., Grisard E.C.;
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR601834-1};
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:ESL12146.1}.
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DR EMBL; AUPL01000092; ESL12146.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061JDC3; -.
DR EnsemblProtists; ESL12146; ESL12146; TRSC58_00092.
DR VEuPathDB; TriTrypDB:TRSC58_00092; -.
DR OrthoDB; 169293at2759; -.
DR Proteomes; UP000031737; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd06183; cyt_b5_reduct_like; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR001834; CBR-like.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR19370; NADH-CYTOCHROME B5 REDUCTASE; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00406; CYTB5RDTASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|PIRSR:PIRSR601834-1};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|PIRSR:PIRSR601834-
KW 1}; Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000031737}.
FT DOMAIN 80..185
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT BINDING 137
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR601834-1"
FT BINDING 152
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR601834-1"
SQ SEQUENCE 340 AA; 37126 MW; 9C4EC81001E027AC CRC64;
MGGCLISPSA EIQMEGGQSS FFGRRRSILG LFGAGEVTGG VHGRNRLGGN SLLECVVFGR
IAGDRAATIL QKKSSPLSFT SWTSVILREV REGGKYGAGS RVLRFNLPGA LQRSGLHLGQ
FIAIRGEWDG QKLIGYYSPI TLPDDLGVIG ILARSDKGML REWISALQPG DAVEMKGCGG
LVIQRRFSER YLYFGNYQLR KLCLIAGGTG VAPMLQIIRA ALKKPFIDTI ESVRLIYAAE
DVSELTYREV LKQHQRLSNG KFRTTFVLNR PPSMWTDGVG FVDKTVLTSC VQPPADDLLV
AICGPPVMQR IVKACLKGLG YNMKLVRTVD EADPQTPSKM
//