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Database: UniProt
Entry: A0A0N0P5A2_LEPSE
LinkDB: A0A0N0P5A2_LEPSE
Original site: A0A0N0P5A2_LEPSE 
ID   A0A0N0P5A2_LEPSE        Unreviewed;       837 AA.
AC   A0A0N0P5A2;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   22-FEB-2023, entry version 18.
DE   RecName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0000259|Pfam:PF07992};
GN   ORFNames=ABL78_4699 {ECO:0000313|EMBL:KPI86226.1};
OS   Leptomonas seymouri.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leptomonas.
OX   NCBI_TaxID=5684 {ECO:0000313|EMBL:KPI86226.1, ECO:0000313|Proteomes:UP000038009};
RN   [1] {ECO:0000313|EMBL:KPI86226.1, ECO:0000313|Proteomes:UP000038009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 30220 {ECO:0000313|EMBL:KPI86226.1,
RC   ECO:0000313|Proteomes:UP000038009};
RX   PubMed=26317207;
RA   Kraeva N., Butenko A., Hlavacova J., Kostygov A., Myskova J., Grybchuk D.,
RA   Lestinova T., Votypka J., Volf P., Opperdoes F., Flegontov P., Lukes J.,
RA   Yurchenko V.;
RT   "Leptomonas seymouri: Adaptations to the Dixenous Life Cycle Analyzed by
RT   Genome Sequencing, Transcriptome Profiling and Co-infection with Leishmania
RT   donovani.";
RL   PLoS Pathog. 11:E1005127-E1005127(2015).
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:KPI86226.1}.
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DR   EMBL; LJSK01000141; KPI86226.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N0P5A2; -.
DR   EnsemblProtists; KPI86226; KPI86226; ABL78_4699.
DR   VEuPathDB; TriTrypDB:Lsey_0141_0040; -.
DR   OMA; RAMWPEM; -.
DR   OrthoDB; 121634at2759; -.
DR   Proteomes; UP000038009; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.50.50.100; -; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR015904; Sulphide_quinone_reductase.
DR   PANTHER; PTHR10632; SULFIDE:QUINONE OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR10632:SF2; SULFIDE:QUINONE OXIDOREDUCTASE, MITOCHONDRIAL; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
FT   DOMAIN          74..238
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   837 AA;  91868 MW;  55550A90EF72A4BE CRC64;
     MRRTRLRWMY IPRTPKKRER EHPMQVQNSE HFLRTAAAVA TLTCVVAAVM ALRKVQRRSR
     QSEQELTRKR GGQNVVIIGA GAGGCAAAAL IANASPDVRV TVIEKDRQQV FQGHVPLAHV
     GHRSYDLGTT SGVDSLRSPV TWNVTRDANL VIAEVLRVDP EAKQVYVQSS PGILASAKPL
     SAEETRAAAP AHPLVRWWRG VPTTPATVSA NEDGSLNLSD GTTVLSYDAL IIAAGAQRTV
     GHLRHQLLPQ QIDSYRIAVN PGTTRDSLAT IFSGNVMYIK MPPASFVWQM EAARALMGKG
     RMSQGDGCMS LDMGVQMETA AASSSAMPSA SATDSVPLGI LTSSVDTPVL STLWRAVRGF
     LVRKVNTSNA LSADDAIEKA SLPDEVALRL AAKAGKLTAP SSSSQPWPLF LLSQWCMHFS
     SRQHDSTFVS STNTIWKYLW HYNKLSLCHL FAVTADVQPI GPAPQQVNEV IERFWRERQL
     GSRCSSDVEG NRFHALYHSY VTSIDCHTNA VTLYDYKNNA EVRVPFQLVV LDLPLRAPGF
     VRQSGLHRTR YVEECVLPSL AEGARTAAEG IEQVGSATAA TAASAKALRK HPLLGKTKAD
     LEAIFADEAS FMDVDPTTLQ HRRYSDVFAL GDVAGLPCAK SYGAVFAQVP VVSHNVRQVL
     KAQQMQAPAS SSSDADLTQC KTKAAATPAQ ADVPAQALPC ANAHYTGYSS FHVIMTTWRS
     MWPEMRYPFD PHCKTEPLPP LTSNTAAPQK EETEMQKRVK WDVMSPLTYC DHHLWNNLAW
     RDLRGLMNGL YSQLALYELM YFFVFSRGQW HSPTWFSVPT FASEDGAPCV PSLLGFL
//
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