ID A0A135SWH2_9PEZI Unreviewed; 1072 AA.
AC A0A135SWH2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Nitric oxide synthase {ECO:0000313|EMBL:KXH40187.1};
GN ORFNames=CSIM01_06365 {ECO:0000313|EMBL:KXH40187.1};
OS Colletotrichum simmondsii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=703756 {ECO:0000313|EMBL:KXH40187.1, ECO:0000313|Proteomes:UP000070328};
RN [1] {ECO:0000313|EMBL:KXH40187.1, ECO:0000313|Proteomes:UP000070328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS122122 {ECO:0000313|EMBL:KXH40187.1,
RC ECO:0000313|Proteomes:UP000070328};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum simmondsii CBS122122.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
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:KXH40187.1}.
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DR EMBL; JFBX01000374; KXH40187.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135SWH2; -.
DR OrthoDB; 276396at2759; -.
DR Proteomes; UP000070328; Unassembled WGS sequence.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
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 4: Predicted;
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}.
FT DOMAIN 547..695
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 726..936
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 699..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1072 AA; 118322 MW; CE0687E0D21B74C5 CRC64;
MACPFLQGTL AQPPRQISAE QEFANIRSQY PSLSSTGCTT KFCQSGRMTH MDEERVGRNQ
SYAQVREDAL DFLQQMYKDG LIDTEQLHRR AHEVLQEIQK NSTEGKFTTA SECGSEAPPA
ATVGLVGGLW TQTFEELEFG LRTAWKHARK CIMRSEYSNL RLCDLRHVRT SKKMAETLIE
SLRVAYNSGE 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 WRRQRQARPA ARPSHHYASD
TKLNISIPVV PSISLTRPVT PVSPFGTASS PSTFLPIPPP ASQQQQQAFR PTTPLTPLSP
RGPGRRIYIG FCSSGNVAIK LCKRLCAQLQ HACDINPKLG SVVVPCTLNA LPISMVEPDD
VLVIVASTTG RGEIPQNGKA FADALARNPK AISCQYAIFA NGSLEYADTY NQAAMDIEEL
LSKGDAQRLI GMREADTATE NPPWSVLGQF FDQVLAGLQK SSPPQDENKT SDVQRTARQA
RPFDTRPWFQ AKVVGQPVLG TAADGMKRVT LDLGDREYPT MGSVWILPPN SQNKVSRVLG
ALGVQADERL SLPGEPTVGE FFQRFADLDQ PFKSTQWAEW LSLPQPETLS KVPIENAVHQ
IPANWRQTVT LDALCNAMPT IQPREYSIAS DGSRTKQKNG NTLDLLVQHH PNGKFSDKYL
NCFETFGAAT CKIRPSSHLQ AMAENQDKPM IVFTTGSGMA PVRGLLQNRL QRLCSSGDKS
AKGPAISLFA GFKAADESLV REAVQEASEA GILDILRLTG SNKEKRRAQD AMLEAGVREK
LVKSIEDGAL VFACARPRAV DDFLNNLSEV LGRDAREVLG DRFVADVYQP AT
//