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Database: UniProt
Entry: K2MAW5_TRYCR
LinkDB: K2MAW5_TRYCR
Original site: K2MAW5_TRYCR 
ID   K2MAW5_TRYCR            Unreviewed;      1250 AA.
AC   K2MAW5;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   SubName: Full=NADH-dependent fumarate reductase, putative {ECO:0000313|EMBL:EKF32293.1};
DE   Flags: Fragment;
GN   ORFNames=MOQ_003860 {ECO:0000313|EMBL:EKF32293.1};
OS   Trypanosoma cruzi marinkellei.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX   NCBI_TaxID=85056 {ECO:0000313|EMBL:EKF32293.1, ECO:0000313|Proteomes:UP000007350};
RN   [1] {ECO:0000313|EMBL:EKF32293.1, ECO:0000313|Proteomes:UP000007350}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B7 {ECO:0000313|EMBL:EKF32293.1,
RC   ECO:0000313|Proteomes:UP000007350};
RX   PubMed=23035642; DOI=10.1186/1471-2164-13-531;
RA   Franzen O., Talavera-Lopez C., Ochaya S., Butler C.E., Messenger L.A.,
RA   Lewis M.D., Llewellyn M.S., Marinkelle C.J., Tyler K.M., Miles M.A.,
RA   Andersson B.;
RT   "Comparative genomic analysis of human infective Trypanosoma cruzi lineages
RT   with the bat-restricted subspecies T. cruzi marinkellei.";
RL   BMC Genomics 13:531-531(2012).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:EKF32293.1}.
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DR   EMBL; AHKC01009923; EKF32293.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2MAW5; -.
DR   EnsemblProtists; EKF32293; EKF32293; MOQ_003860.
DR   OrthoDB; 169293at2759; -.
DR   Proteomes; UP000007350; Unassembled WGS sequence.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   CDD; cd06183; cyt_b5_reduct_like; 1.
DR   Gene3D; 3.10.520.10; ApbE-like domains; 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; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   InterPro; IPR024932; ApbE.
DR   InterPro; IPR003374; ApbE-like_sf.
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; IPR010960; Flavocytochrome_c.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-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; PF02424; ApbE; 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; SSF143631; ApbE-like; 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.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   4: Predicted;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007350}.
FT   DOMAIN          993..1098
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   REGION          602..621
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EKF32293.1"
SQ   SEQUENCE   1250 AA;  136719 MW;  7C5D8C051773BC03 CRC64;
     FFCLLHFYFS VFSAAGRGGG KPKRRMFSRR RILLRSSFTI GVATGKMAIT KSLMFGAYPP
     AAPATAAVRW ASSSSSSTLD NSPTILSQRS FFSGSPDAHS SASVVVVDAE LAAKERDRIA
     REMLSQNMPS PHTEERLVVT LRGLEHTVPY TLRMVLNGAD EAKNGEIVAG NVLTEAFEVV
     NQHLNHYNPE SEVSAINQLP VGVKHTMSEH MRCVMECCVR VYASSGACFD PATGPLVEFL
     RSVMKDEKSD TESTLTEEEV EHFCLPQSFD VNITDGTIAR KHEGAKLDLG GVNKGYTVDR
     VVEKLNAAGM RDVMFEWGGD CRATGVNYQH QAWAIAIVRP PPVEVVEQHA KEGVDEKKET
     SQLLRLMYLD DEALCTSGDY ENVMYNPKYG VRSNIFDWKR RSLLEPVENE LAQVSIKCYS
     AMYADALATA SLIKRDITKV RHMLEDWRHS RNRVTNYVTY TRQGERVARM FEIATENAEI
     RKNRIAGSLP ARVIVVGGGL AGLSAAIEAT ACGAQVILLE KEPKVGGNSA KATSGINGWG
     TRAQALDDIQ DNCKTFERDT HKSGLGGSTD PSLVRTLSVK SGDAISWLSS LGVPLTVLSQ
     LGGHSRKRTH RAPDKADGTP VPIGFTIMRT LEQHIRTKLA DRVTILESTA VTSLLHEIKA
     TPDGGREVRV RGVTYKKSDE KEFISMKLTA DAVILATGGF SNDHMSQSLI GEFAPELSGF
     PTTNGPWATG DGVKLARRLG ATLVDMEKVQ LHPTGLIDPK DPANPTKYLG PEALRGSGGV
     LLNKKGERFV NELDLRSVVS NAIIEQGDEY PYSNGSKFAF CVLNDAAVKL FGVNLLNFYA
     NNLGLFKRVD DLQELAMLIG CDVLTLQNTL EAYESCSIST SACPFTGKVV YPCVLGPQGP
     FHVAFVTPSI HYTMGGCLIS PSAEIQREHH SLNLLENQRP ILGLFGAGEV TGGVHGGNRL
     GGNSLLECVV FGRIAGDRAA TILQKQVYAL SKDKWTSVVV RESRSGERFG TGSRVLRFNL
     PGALQRSGLY LGQFIAIRGE WDGQQLIGYY SPITLPDERG VISILARGDK GTLREWICAM
     RPGDSVEIKS CGGILIERNP AKKQFLFRGH VIRQFGLIAG GSGVAPMLQI IRAALERPYV
     DTTESIRLFY TAEEYEELTY RELLNHYCKE NPDKFSVEFS LNNPPEGWTG GVGFVDRPSL
     RKTLQPPSND LLIAICGPPA MQRAVKNDLL AMGYNPALVH TVDDDMQAAL
//
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