ID A0A161YCQ2_9PEZI Unreviewed; 1683 AA.
AC A0A161YCQ2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=indoleamine 2,3-dioxygenase {ECO:0000256|ARBA:ARBA00034333};
DE EC=1.13.11.52 {ECO:0000256|ARBA:ARBA00034333};
GN ORFNames=CT0861_05250 {ECO:0000313|EMBL:KZL70067.1};
OS Colletotrichum tofieldiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL70067.1, ECO:0000313|Proteomes:UP000076552};
RN [1] {ECO:0000313|EMBL:KZL70067.1, ECO:0000313|Proteomes:UP000076552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0861 {ECO:0000313|EMBL:KZL70067.1,
RC ECO:0000313|Proteomes:UP000076552};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the indoleamine 2,3-dioxygenase family.
CC {ECO:0000256|ARBA:ARBA00007119}.
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:KZL70067.1}.
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DR EMBL; LFIV01000096; KZL70067.1; -; Genomic_DNA.
DR STRING; 708197.A0A161YCQ2; -.
DR OrthoDB; 2723058at2759; -.
DR Proteomes; UP000076552; Unassembled WGS sequence.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0019441; P:tryptophan catabolic process to kynurenine; IEA:InterPro.
DR Gene3D; 1.20.58.480; -; 1.
DR Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid 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; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR000898; Indolamine_dOase.
DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR InterPro; IPR037217; Trp/Indoleamine_2_3_dOase-like.
DR PANTHER; PTHR19384:SF84; METHIONINE SYNTHASE REDUCTASE; 1.
DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF01231; IDO; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF140959; Indolic compounds 2,3-dioxygenase-like; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000076552}.
FT DOMAIN 559..822
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 1002..1083
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1503..1544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1558..1683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1515..1541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1588..1628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1683 AA; 184806 MW; 9427168FC55C3514 CRC64;
MPYSERSCPV SGTTGGVCPV GANNSGRQSR SSSRMGPRGC SFSGFSQPGD IHTAFDIPRG
VDAEEWLRMR ERKSINHVLY SKYPSTQQID TVKSQAEMDA FNVNEQDLLA VALGAPARQV
MLRAEEIGPQ TGWRDGYLST EHGFCPPDYD EAAGALARSP GRVWSDLCER MPGCVSRGRV
RESIAAAPVI EGSEDVIPDQ ALWAAIVALG MLCSIYRFEQ KYDGHDGVNA TTNPTKLKLN
CKMGDYLGEE LVGIPLSIAL PYFQVSRRMG RTLPHLTFVD QSSYNLKIKD ATSSYPYVAR
FDNIELRWPM FGERAEVAFL KGVAETSASF QHGPDAIAAC QEHVMNRNVE GLLHEMIRLK
EILERMPNAF HSISTNPNAG ENYVPVQQWV RWAKFSAPLS RRCPASSGLQ FPPYLVMDAF
LGRKKTLKSL TITHRYTSFL GAEGVHLRAW LPSNLRAFIA AIEYHYRIPE FVQQSGDPRL
MGVLDGIVEA YTGERGFMGV HRYKVFGILE VAAKTGRTET NGASGAADGE RPWEETHRQF
SEAMKERLEP YRGTLPVEPH QMRGTFEECR YVTRVLNRSF VDSDPKRSIA MVTLDIRETG
ITFAPGDRLA VMPLNGWEEC AKVIAALGLE EQIDAPVQVS GTWARFEMHL GSVRRTVAPK
LTVGDILRRG HLAPITKDMA LKIHSMLHAS SNTVLQVLST DEWPVRGSLG DLLQDAVTDT
PPQIWDRVFS LENLSWLAEL IPLEVPRTYS IASYTEELLP ETVDLAVSRS EYKLCSTFSR
GKEVSRAGVS SGFLNPPVEV GEIKSDDEIL IGVSRPAAFH LPLDPMAPCA FFAGGSGIAP
FRSFWQARLA QSGLSGGKNL LYLGVQSREK FCFEEELRQY INADFMEVHV AFSRDSRGLS
YEGRDLVEKH IPPRYIDTLV VEQGVAICDL VMSKKQGGLG GYLYVCGSVS VFDSVMNGIR
KAIYTYRTAT EKGVDVIINK AFAERRFMLD VFMTPKPLPC NLPTIPVSEL ALHTGHRPGS
RMWIGVHGSV YDVTDFCPMH PGGTLIIKSN AGVDCSKSFD NLAHTNNPEV SSLLTKYFVG
HLTPKPDYGN DEISALHDLW SAYLRSTVET LVAHQFEMFE IMGASIETSS SHDPAGSNNI
WLRESLPNII AVRTFYGYQS RLLQGGFAAL FGPKLQELVL KLSFGIASAN GPAADTKLPD
VLGTVARAKT SGDAATCTKE VALVGQFVCD ADASLRFQER GVFAYAARSV ELDIALLEDL
RQEACTGMDA FDSIANSIKE SSDPDVESSR LTALATFLLQ VLERMARHLE VFYTQLARCS
VYQPKLEQNP ARTRWALVRR RIRDGSLFVL ATKAELNSST PEQSAAAPYY MSRANPNQNI
DFDRVMAQVQ ASLRAGSQDA AFPNHSAHLQ PLTLNAVHQA RGRSTGDVSA VARRENAGAL
RAMNNFVEKN SRAIRRLSKL PAAAMNFEDI QRAALLEMSQ HSGPLSPPEM AGDMLGLGPE
HALRLGKHGY NSSDRILPTP PSSRGSSRSP TRFNHSLGIN QHHGRPTAEM LLANLNRPRG
ASLSRGPPSG PSSPASYPVI GSQSPPPSHP AVDAQTALSS MMGRLNTRPR SGSATMSASH
QHSSMNGGGL VRARSVMSMS SAGAVRERDG RPGHVPRTST SSLRALKLKS VMEQSEERVA
PTF
//
