ID A0A177C8N7_9PLEO Unreviewed; 647 AA.
AC A0A177C8N7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 28-JUN-2023, entry version 23.
DE RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
GN ORFNames=CC84DRAFT_1178604 {ECO:0000313|EMBL:OAG03070.1};
OS Paraphaeosphaeria sporulosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC Paraphaeosphaeria.
OX NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG03070.1, ECO:0000313|Proteomes:UP000077069};
RN [1] {ECO:0000313|EMBL:OAG03070.1, ECO:0000313|Proteomes:UP000077069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG03070.1,
RC ECO:0000313|Proteomes:UP000077069};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; KV441555; OAG03070.1; -; Genomic_DNA.
DR RefSeq; XP_018033435.1; XM_018180359.1.
DR AlphaFoldDB; A0A177C8N7; -.
DR STRING; 1460663.A0A177C8N7; -.
DR GeneID; 28763845; -.
DR InParanoid; A0A177C8N7; -.
DR OrthoDB; 9164at2759; -.
DR Proteomes; UP000077069; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; 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; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR19384:SF84; METHIONINE SYNTHASE REDUCTASE; 1.
DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase 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:UP000077069}.
FT DOMAIN 219..493
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 647 AA; 71471 MW; 98CD639C5331B2D6 CRC64;
MDTHSPIPTT ATSHPDDPIP CEPRNVPELT LKPSSPQQHI EHTSPQSLGE SMIWSNTSSD
DSEAPLTPNT EPERQMDEIV DKLQELPAAT VNFNEQPRPR RASTTLISEN PSDIRRILGD
GETATQLISQ CCGGGCCLLK TLAPDTASPN FLPVVIPDNK AFRSLNLKLG PLALDSELTD
TTPLPPVNMS FDKLPTAETK HVSRVHKEPP TYMKPHPPYD VYSAPLYHAR ELTKPGAEKR
TFHFDIDVTD YPDEGGVEFK VGGAIGVCPP NSQDIVDELF DVLCIPKFAR DKPVTLKTYT
GRWPTIWGDE KARELVTTRR ELLTWCVDLQ SFPPTKHLLR LMAEHADAPN EKKILMYLSS
AQGQAAFCDL RTTSHLTIAQ LLSAFPSSKP PLPALLSNLN QLMPRFYSLS NDPHVSAARP
GLPGNRRLIE VAVTIHESPD WHAENGTRTG VGSGFMERLA LQFIKAEKEG IDPGVLDLRV
PMFRGLMSNP LSRQFGGDGP MVLIGAGVGM APFRGFILNR LKNANCANKI WLIQGVRDSM
VDELYSGELG DHEREIKKVV QSRKVKVGAS DAKYVQDEVR LQADIVWFVV NALDGRIFVC
GSSKGMGEGV EQALVDVAMQ KGNLSEAEAH EFWNKKKEDG QYIAETW
//
