ID A0A0G4MMZ3_9PEZI Unreviewed; 424 AA.
AC A0A0G4MMZ3;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 03-MAY-2023, entry version 28.
DE RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
GN ORFNames=BN1708_001246 {ECO:0000313|EMBL:CRK35601.1};
OS Verticillium longisporum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=100787 {ECO:0000313|EMBL:CRK35601.1, ECO:0000313|Proteomes:UP000044602};
RN [1] {ECO:0000313|EMBL:CRK35601.1, ECO:0000313|Proteomes:UP000044602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VL1 {ECO:0000313|EMBL:CRK35601.1};
RA Wang D.B., Wang M.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR601834-1};
CC -!- SIMILARITY: Belongs to the flavoprotein pyridine nucleotide cytochrome
CC reductase family. {ECO:0000256|ARBA:ARBA00006105}.
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DR EMBL; CVQH01023638; CRK35601.1; -; Genomic_DNA.
DR STRING; 100787.A0A0G4MMZ3; -.
DR OrthoDB; 1387364at2759; -.
DR Proteomes; UP000044602; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd06183; cyt_b5_reduct_like; 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; IPR001834; CBR-like.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR19370:SF189; CYTOCHROME C MITOCHONDRIAL IMPORT FACTOR CYC2; 1.
DR PANTHER; PTHR19370; NADH-CYTOCHROME B5 REDUCTASE; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR PRINTS; PR00406; CYTB5RDTASE.
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 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR601834-1};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR601834-1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000044602}.
FT DOMAIN 84..194
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 54..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 144
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR601834-1"
FT BINDING 146
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR601834-1"
FT BINDING 160
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR601834-1"
FT BINDING 169
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR601834-1"
FT BINDING 170
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR601834-1"
SQ SEQUENCE 424 AA; 44849 MW; 403E2ED5DB2BA367 CRC64;
MARLHVDQDD LQQRLTMDFS LIIININDKT LQHKTQIKAN LPISRRTLLN HLSNTKPNAS
AVPPGNIQAP GFHPPSSAHI FNDHRFTPFT LVDREPVSAS SFVLTLHPST TLPPSEVAAQ
LAAPWTANDL WSLEVKQPQL QIAREYTPLP NAPPGALRFL VRAIDGGEVS TYLSRLPLGA
TIDLRGPHGS FDLQARLRPX GRLVFLAGGT GIASALQAAH SVLDRTDSPP PDVTILWAVR
ARDEIQATQP AAAAAASPRR PWWHPFHAAA PAPERLTPDM AAPTQTTRDL LALQARHPSL
QVHLFIDGAT APLSAAVLAA TLRAAPAAPH SDACALHAQT RHVAVADGGP NAGTRSRFPA
GACACACAGA APGKNLLVVS GPDGFVAALA GARPWRGGGQ VQGRVGGVLG EMGGLLRDWL
VLKL
//
