ID G0UMG4_TRYCI Unreviewed; 817 AA.
AC G0UMG4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 13-SEP-2023, entry version 31.
DE SubName: Full=Uncharacterized protein TCIL3000_5_640 {ECO:0000313|EMBL:CCC90370.1};
GN ORFNames=TCIL3000_5_640 {ECO:0000313|EMBL:CCC90370.1};
OS Trypanosoma congolense (strain IL3000).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Nannomonas.
OX NCBI_TaxID=1068625 {ECO:0000313|EMBL:CCC90370.1};
RN [1] {ECO:0000313|EMBL:CCC90370.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IL3000 {ECO:0000313|EMBL:CCC90370.1};
RX PubMed=22331916; DOI=10.1073/pnas.1117313109;
RA Jackson A.P., Berry A., Aslett M., Allison H.C., Burton P.,
RA Vavrova-Anderson J., Brown R., Browne H., Corton N., Hauser H., Gamble J.,
RA Gilderthorp R., Marcello L., McQuillan J., Otto T.D., Quail M.A.,
RA Sanders M.J., van Tonder A., Ginger M.L., Field M.C., Barry J.D.,
RA Hertz-Fowler C., Berriman M.;
RT "Antigenic diversity is generated by distinct evolutionary mechanisms in
RT African trypanosome species.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:3416-3421(2012).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; HE575318; CCC90370.1; -; Genomic_DNA.
DR AlphaFoldDB; G0UMG4; -.
DR VEuPathDB; TriTrypDB:TcIL3000_5_640; -.
DR OrthoDB; 169293at2759; -.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR InterPro; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR010960; Flavocytochrome_c.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR NCBIfam; TIGR01813; flavo_cyto_c; 1.
DR PANTHER; PTHR43400:SF7; FAD_BINDING_2 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43400; FUMARATE REDUCTASE; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
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 SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
PE 4: Predicted;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 84..554
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
SQ SEQUENCE 817 AA; 87131 MW; 4F3E40F4ED742DA0 CRC64;
MFFFTPVSRP TKLRTPKHRA SHYTWAPVNY FVGRLASKSF ASLVVILISA LITPAAASLA
GGTAGMSALK SPENLLGQPE KSRVIVVGGG LAGLSAAIEA ANSGAEVVLM EKQPRLGGNS
AKATSGINGW GTRAQAKASI VDGGKYFERD TYKSGIGGNT DPALVKTLSV KSADAINWLT
SLGVPLTVLS QLGGHSRKRT HRAPDKKDGT PLPIGFTIMK TLEDHVRGAL AGRVTIMESC
AVTSLLSETK ERPDGTTQVR VTGVEFVQAN NGKTSILADA VILATGGFSN DKTADSLLRE
YAPHLIGFPT TNGPWATGDG VKLAQRLGAE LVDMDKVQLH PTGLINPKDP ANSTKFLGPE
ALRGSGGILL NKQGKRFVNE LDLRSVVSKA IMEQKAEYPG SNGSMFAYCV LNEAARKLFG
VSSHEFYWKQ MGLFVKADTM KDLAALIGCP LESVQDTLGE YERLSSSQRS CPVTRKNVYP
CVLGTKGPFY VAFVTPSIHY TMGGCLISPS AEIQMKNTSS RSPLSHSNPI LGLFGAGEVT
GGVHGGNRLG GNSLLECVVF GRIAGASAAN SSYENATHLW HNKWSSVVLE TSLMDESGFV
WLYFRLPSTL QVSGVDALQS VVLRELQGRG EWDARIPFTT PDDVGIIGVA FPGGGGGDTT
NWLGRLEPGD VVEMRVGGPT DENYARLLNF PRQVIIATVN GVGPMFQIIR IALGKAKAKF
TVHIIYVVDD VKEIPQRTKL EALAQEQPNM FKCTFVVRQP PLLWSGAINA MDEIANATPP
DNEQGIFLAG SAGEAASFKA YLLDLGHSSD NIATIVQ
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