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Database: UniProt
Entry: A0A135SWH2_9PEZI
LinkDB: A0A135SWH2_9PEZI
Original site: A0A135SWH2_9PEZI 
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
//
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