ID A0A135UZL0_9PEZI Unreviewed; 1156 AA.
AC A0A135UZL0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 22-FEB-2023, entry version 23.
DE SubName: Full=FAD binding domain-containing protein {ECO:0000313|EMBL:KXH65782.1};
GN ORFNames=CSAL01_03370 {ECO:0000313|EMBL:KXH65782.1};
OS Colletotrichum salicis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1209931 {ECO:0000313|EMBL:KXH65782.1, ECO:0000313|Proteomes:UP000070121};
RN [1] {ECO:0000313|EMBL:KXH65782.1, ECO:0000313|Proteomes:UP000070121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 607.94 {ECO:0000313|EMBL:KXH65782.1,
RC ECO:0000313|Proteomes:UP000070121};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum salicis CBS 607.94.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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:KXH65782.1}.
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DR EMBL; JFFI01000819; KXH65782.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135UZL0; -.
DR STRING; 1209931.A0A135UZL0; -.
DR OrthoDB; 5488444at2759; -.
DR Proteomes; UP000070121; Unassembled WGS sequence.
DR GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IEA:InterPro.
DR CDD; cd06207; CyPoR_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR033412; PFOR_II.
DR InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR PANTHER; PTHR19384:SF109; SULFITE REDUCTASE [NADPH] FLAVOPROTEIN COMPONENT; 1.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR Pfam; PF17147; PFOR_II; 1.
DR Pfam; PF01558; POR; 1.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000070121}.
FT DOMAIN 769..1006
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1156 AA; 126262 MW; 66172BA5D2FFE2D5 CRC64;
MQFKQQESTG SAAVVDAKSP PSSAPQKKVS STLPFGQPVA LSSISGPTYV TAQLLVQQVA
FLLSDKIFSY SAPTFDLDVA AKAWSEAKEQ NIHGKTTDLI QLQTRTGAGA LALGYIFSPD
FDLAKRHLPQ TLLAPTLSLK NLRGALDQLS LLYGVASPFV AHVAALDYDA ANGLVSDYDT
ALRTAEDLGL GLVASSSAYE TQHMALFATL MAALMPTLHI YDGVRLARET SRVVDALSQS
GIADLYNNIT SESTGVSERA AISSKVAGLL DVFNKHLDPT EDHESQHTAL LATLMTALTP
NLGVEDGVKL AKQTLKASDA LNKKGVAETY KKISSEVQSL NKRLDDAGKV VELLRLFNNE
LGTAYKLFEY HGHDQAEAVL VVFGSAETQL AKQVVTRLAA DGAKVGAINV RVYRPFVEEA
FLASIPASAR TISVLGQVKD ELSVSDASLQ SALYTDVLTS VSFSGKWRQD PTVSDVKYSA
SEALTPQTVA DIFGKLLSAE AESKPFPALV QAHQYTFWDV DNSVAVDSPA VVSNLLSRES
TSNVYVHESF DNLLQGGIVR TDIRSSKKAI EAPYAVEEAD VVAVGEEKLL KDLDIIKSVK
AGGKLLLNLP TFKEEDLEKR LSPVVRKQIQ DKSIELYVLD ASAFAEKESQ AVKVLLEFAF
LQIARSDITV EEVAKLALPE GFSSTLVETQ EALSQALRKV ESQSAWAELP EDVVVSPLPA
TIKPNSFVGF DKEEAEETSQ LVDWQAAAKG LAFKEAYGTQ GVLRPELPVK THTITVKENR
RLTPGNYDRN IFHIEFDLGD SGLTYDIGEA LGIHAENDHE EVTAFIKWYG LDPEALVQVP
AREDNAAFET RTVYQSLKQN IDVLGKPPKR FYEALSEFAA DEREKAVLAS LGGAEGAADF
KKRSEVDFVT YVDILQEFPS ARPSFHDLVR IIAPLKRREY SIASAQAVTP TSVALMIVVV
DWVDPLGRNR FGHATRYLSA LPVGATVVAS VKPSVMKLPT SSKAPLIMAG LGTGLAPFRA
FVQYRALQKS RGEEIGSILL YLGSRHQREE YLYGEEWEAY VDAGVITHLG AAFSRDQPRK
IYIQDRMRES MRDVVQSYIR DEGSFYLCGP TWPVPDVTDV LMEAINVEAK MSGKKVNARN
EIEKLKEDGR YVLEVY
//
