ID A0A0F4GUK3_9PEZI Unreviewed; 1125 AA.
AC A0A0F4GUK3;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=nitric-oxide synthase (NADPH) {ECO:0000256|ARBA:ARBA00012989};
DE EC=1.14.13.39 {ECO:0000256|ARBA:ARBA00012989};
GN ORFNames=TI39_contig314g00005 {ECO:0000313|EMBL:KJY00743.1};
OS Zymoseptoria brevis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=1047168 {ECO:0000313|EMBL:KJY00743.1, ECO:0000313|Proteomes:UP000033647};
RN [1] {ECO:0000313|EMBL:KJY00743.1, ECO:0000313|Proteomes:UP000033647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zb18110 {ECO:0000313|EMBL:KJY00743.1,
RC ECO:0000313|Proteomes:UP000033647};
RA Grandaubert J., Bhattacharyya A., Stukenbrock E.H.;
RT "RNA-seq based gene annotation and comparative genomics of four
RT Zymoseptoria species reveal species-specific pathogenicity related genes
RT and transposable element activity.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- SIMILARITY: Belongs to the NOS family. {ECO:0000256|ARBA:ARBA00006267}.
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:KJY00743.1}.
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DR EMBL; LAFY01000306; KJY00743.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F4GUK3; -.
DR STRING; 1047168.A0A0F4GUK3; -.
DR OrthoDB; 276396at2759; -.
DR Proteomes; UP000033647; 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:0004517; F:nitric-oxide synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006809; P:nitric oxide biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.90.440.10; Nitric Oxide Synthase;Heme Domain;Chain A domain 2; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR044943; NOS_dom_1.
DR InterPro; IPR044940; NOS_dom_2.
DR InterPro; IPR044944; NOS_dom_3.
DR InterPro; IPR004030; NOS_N.
DR InterPro; IPR036119; NOS_N_sf.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR43410; NITRIC OXIDE SYNTHASE OXYGENASE; 1.
DR PANTHER; PTHR43410:SF1; NITRIC OXIDE SYNTHASE OXYGENASE; 1.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF02898; NO_synthase; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF52218; Flavoproteins; 1.
DR SUPFAM; SSF56512; Nitric oxide (NO) synthase oxygenase domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022643};
KW FMN {ECO:0000256|ARBA:ARBA00022643}; Heme {ECO:0000256|ARBA:ARBA00022617};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000033647}.
FT DOMAIN 597..743
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 773..970
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 1..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1125 AA; 125489 MW; 76CECBCC5C7C55CD CRC64;
MPSQEQESTA VCSSPRHISK LAKPTPPRNH GDFTRHQQNE SNSSSSDAET EATDIASLST
PGTEDSEVLD EKERSNDEDS PFVESVSFHD PARAIRCPAA QLELGKIAAA YPKLRPTGCT
VDFCQSGRMI KTTEPRVGRD ASIQKIQSDA QDFLRQLRAE NVIDSDERLQ HRLNEVLVEI
ADTSCTSVQH TASKHNGHHA AITSSIGATW SQSLEELRHG LRLAWKHSSK CIMRSEYQTL
EVRDFRHINT SREMCTTVIA ALREAFNNGK IAPTVFAFPP RQPGTRGPMF WNQQLLSFAA
YEQDDGSVLG DPANLQLTKD ITELGWCPPN FRTRWDLLPI VAMAEGDEPY WLEVTEEDFP
LVPITHPQLR LQFEKLGLRW VPAPALSRLG FDIGGVQYTA APFIGWFMDA EIGVRNLADT
FRYNALPQVA VALDWIRSEH EIDRLPEYER LAVLSRAQTE LNFAVYHSFK TTGVAMSDTL
SASTMYCNYD DEHFRVKGFR LPSNPYWLAP PQGSIVPIWH RGGAPNYQPS PLICKHIQDP
VKAWRRETSK SPSEAAIKRI DKTASPLARS CSSASLQYHD VRHQQEACND GVNQRRIYIC
FCSAASTAKK LANDLHSRLR CVVDNQYALN LVTTLNDFKP RKGSKEDILL IIASTAGHGE
VPLNGQRFLE VSFGVEATSL LRYSVFGNGS TLYGDRYNAA ATAINEHLLT QKAKPLCDGL
YAGDTAQEEP PWSQFDDWYR HIVEALHVEP DLRNQVTDRK QASKAKAGME TASSYSLARI
VTCARSHAQG LQHVVLNIGE QRYEPLSHVA MIVPNDSSVV KQALRTVGLQ GNEPAQVLHR
QLSVEEYLVA FVDFDRPFLN LDWVQGWNFR RSQRHLFGRL PLRETLQAFR WPWRTSIDLQ
SLLAAMPLKT PRMFSVASSQ KVLKNGHHSG ELDLLIQHRE GGMVSNYLKT IGPGACVQLK
TNPSDDKTLL HSIDNPIICF ATGSGLAPVL SLLSHRLALQ KNSQRGSDGE NGRAFGAVTL
ILGFRKMDSS IIGQALRESI ERGIIDVLLM TPSNDEKMRA QDRVFDCNIC QTLEKKLKCE
GAAVFVCALP EAAADFAKNL SALLGCNVQE ALGERYVEQV YKPAC
//
