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Database: UniProt
Entry: W6LB37_9TRYP
LinkDB: W6LB37_9TRYP
Original site: W6LB37_9TRYP 
ID   W6LB37_9TRYP            Unreviewed;       368 AA.
AC   W6LB37;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
DE   Flags: Fragment;
GN   ORFNames=GSHART1_T00002725001 {ECO:0000313|EMBL:CCW66786.1};
OS   Phytomonas sp. Hart1.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Phytomonas.
OX   NCBI_TaxID=223615 {ECO:0000313|EMBL:CCW66786.1, ECO:0000313|Proteomes:UP000053358};
RN   [1] {ECO:0000313|EMBL:CCW66786.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Hart1 {ECO:0000313|EMBL:CCW66786.1};
RA   Genoscope - CEA;
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CCW66786.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hart1 {ECO:0000313|EMBL:CCW66786.1};
RX   PubMed=24516393; DOI=10.1371/journal.pgen.1004007;
RA   Porcel B.M., Denoeud F., Opperdoes F., Noel B., Madoui M.A.,
RA   Hammarton T.C., Field M.C., Da Silva C., Couloux A., Poulain J.,
RA   Katinka M., Jabbari K., Aury J.M., Campbell D.A., Cintron R., Dickens N.J.,
RA   Docampo R., Sturm N.R., Koumandou V.L., Fabre S., Flegontov P., Lukes J.,
RA   Michaeli S., Mottram J.C., Szoor B., Zilberstein D., Bringaud F.,
RA   Wincker P., Dollet M.;
RT   "The Streamlined Genome of Phytomonas spp. Relative to Human Pathogenic
RT   Kinetoplastids Reveals a Parasite Tailored for Plants.";
RL   PLoS Genet. 10:e1004007-e1004007(2014).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|PIRSR:PIRSR601834-1};
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DR   EMBL; HF955200; CCW66786.1; -; Genomic_DNA.
DR   AlphaFoldDB; W6LB37; -.
DR   EnsemblProtists; CCW66786; CCW66786; GSHART1_T00002725001.
DR   OrthoDB; 979728at2759; -.
DR   Proteomes; UP000053358; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd06183; cyt_b5_reduct_like; 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; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
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   PANTHER; PTHR19370:SF185; NADH-CYTOCHROME B5 REDUCTASE 2; 1.
DR   Pfam; PF00970; FAD_binding_6; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00406; CYTB5RDTASE.
DR   PRINTS; PR00371; FPNCR.
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|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR601834-1};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|PIRSR:PIRSR601834-
KW   1}; Membrane {ECO:0000256|SAM:Phobius};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053358};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        349..367
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          44..163
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   REGION          288..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        289..306
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         105
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601834-1"
FT   BINDING         120
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601834-1"
FT   BINDING         122
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601834-1"
FT   BINDING         125
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601834-1"
FT   BINDING         195
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601834-1"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:CCW66786.1"
SQ   SEQUENCE   368 AA;  41800 MW;  B282D12CFBA4AA47 CRC64;
     MWDGGAWGRW GVALTLFSIL FAGWASARWI WRPRRSAEMV LNMSDFLPVR LLSRRQVSPD
     GFLFRFALEE PGMRLELPVG NHVVLRGPCG EKKEEGKRDM VQHSYTPISE KNAKGYVDFL
     IKVYFAGVNP KFPLGGRLTQ YLHSLCINDV IDMRGPIGRF EYLGNGRCKI GRRMAERTTV
     RVETLAMIGG GSGLTPLLQI IYAVRKDPSD TTKIILIYAN QTPEDILLRD ELDSIAQNSQ
     GMVKVWYTVD RNAPTDWPYD VGFINEEMLR AHLSIPQKLN DENLQTEKNE NGMKATGTNG
     ENSNKNGKDN NKWEEKTRSV LALVCGPHAM NQNAVVPNLE KMGYSKDDIF VLLITLYIYI
     YISFLPYR
//
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