ID A0A135RMZ6_9PEZI Unreviewed; 1026 AA.
AC A0A135RMZ6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, 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=CSAL01_10507 {ECO:0000313|EMBL:KXH24995.1};
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:KXH24995.1, ECO:0000313|Proteomes:UP000070121};
RN [1] {ECO:0000313|EMBL:KXH24995.1, ECO:0000313|Proteomes:UP000070121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 607.94 {ECO:0000313|EMBL:KXH24995.1,
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 -!- 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:KXH24995.1}.
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DR EMBL; JFFI01002771; KXH24995.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135RMZ6; -.
DR STRING; 1209931.A0A135RMZ6; -.
DR OrthoDB; 276396at2759; -.
DR Proteomes; UP000070121; 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 Gene3D; 2.40.30.10; Translation factors; 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; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
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:UP000070121}.
FT DOMAIN 501..649
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 680..890
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 458..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1026 AA; 113479 MW; 3B8B9DC01ABB179C CRC64;
MDEERVGRNQ SYAQVREDAL DFLQQMYKDG LIDTEQLHHR AHEVLQEIQK NSTEGKFTTA
SECGAEAPPA ATVGLVGGLW TQTFEELEFG LRTAWKHARK CIMRSEYSNL RLCDLRHVRT
SKKMAETLIG NLRVAYNSGE INPTVFVFPP RDIDSRGPMI WNSQLLSFAG YQQSNGTILG
DPANVELTNA IIELGWTPPR FRSQWDLLPL VTMAEGEEPV ITELPKDAFP LVHIRHPKHP
ELETLGLRWV PAPALSRLGF SIGGVQYTAA PFIGWFMDAE IGVRNLADSF RYNALPQVAK
AIGLVDGDVD DLPDYERLAV LSRAQLELNY ATYWSFAQAG VRMSDSLGAA EQFAQFDDEH
LMNNGFRLPS DPYWLAPPQG SIIPIWHRGG SPNYQPKPLI CRHAQDPIKA WRRQRPTRRP
ARPSHHYASD TKLNISIPVV PSISLTRPVT PVSPFGTASS PSHFLPIPPP SQQQQQQQQQ
QVVRPTTPLT PLSPRGPGRR IYIGFCSSGN VAIKLCKRLC AQLQHACDIN PKLGSVVVPC
TLNALPISMV EPDDVLVIVA STTGRGEIPQ NGKAFADALA RNPKAISCQY AIFANGSLEY
ADTYNQAAMD IEELLSKGDA QRLIGMREAD TATENPPWSV LGQFLDQVLA GLQKSSPPQD
ESNTSDVQRT ARPVRPFDTR PWFQAKVVGQ PVLGTAADGM KRVTLDLGDR EYPTMGSVWI
LPPNSQNKVS RVLGALGVQA DERLSLPGEP TVGEFFQRFA DLDQPFKSTQ WAEWLSLPQP
ETLAKVPIEN VVHQIPANWR QIVTLDALCN AMPTIQPREY SIASDGSRTK QKNGNTMDLL
VQHHPNGKFS DKYLNCFETF GAATCKIRPS SHLQAMAENQ DKPMIIFTTG SGMAPVRGLL
QNRLQRLHSS DDKSAKGPAI SLFAGFKAAD ESLVREAVQE ASEAGILDIL RLTGSNKEKR
RAQDAMLEAG VRDKLVKSIE DGALVFACAR PRAVDDFLNN LSEVLGRDAR EVLGDRFVAD
VYQPAT
//
