UniProt: A0A3Q0JDR1

Database: UniProt
Entry: A0A3Q0JDR1_DIACI

LinkDB:  A0A3Q0JDR1_DIACI 
Original site:  A0A3Q0JDR1_DIACI

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
Protein domain (15)   
   InterPro (10)   
   Pfam (3)   
   PROSITE (2)   
All databases (22)   

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ID   A0A3Q0JDR1_DIACI        Unreviewed;       801 AA.
AC   A0A3Q0JDR1;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=nitric-oxide synthase (NADPH) {ECO:0000256|ARBA:ARBA00012989};
DE            EC=1.14.13.39 {ECO:0000256|ARBA:ARBA00012989};
GN   Name=LOC103519178 {ECO:0000313|RefSeq:XP_026686564.1};
OS   Diaphorina citri (Asian citrus psyllid).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Hemiptera; Sternorrhyncha; Psylloidea; Psyllidae;
OC   Diaphorininae; Diaphorina.
OX   NCBI_TaxID=121845 {ECO:0000313|Proteomes:UP000079169, ECO:0000313|RefSeq:XP_026686564.1};
RN   [1] {ECO:0000313|RefSeq:XP_026686564.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000256|ARBA:ARBA00001970};
CC   -!- SIMILARITY: Belongs to the NOS family. {ECO:0000256|ARBA:ARBA00006267}.
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DR   RefSeq; XP_026686564.1; XM_026830763.1.
DR   AlphaFoldDB; A0A3Q0JDR1; -.
DR   STRING; 121845.A0A3Q0JDR1; -.
DR   PaxDb; 121845-A0A3Q0JDR1; -.
DR   KEGG; dci:103519178; -.
DR   OrthoDB; 276396at2759; -.
DR   Proteomes; UP000079169; Unplaced.
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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.360; -; 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; 2.
DR   InterPro; IPR003097; CysJ-like_FAD-binding.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR001094; Flavdoxin-like.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR029039; Flavoprotein-like_sf.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
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; PF00667; FAD_binding_1; 3.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   PRINTS; PR00371; FPNCR.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF52218; Flavoproteins; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 3.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   3: Inferred from homology;
KW   Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
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   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000079169}.
FT   DOMAIN          1..107
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
FT   DOMAIN          160..481
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|RefSeq:XP_026686564.1"
SQ   SEQUENCE   801 AA;  90635 MW;  393156E29E9D5812 CRC64;
     VYTNNPTSTK ALRGEIEGCI NELQPDFLKF DIENVVRKER MYHLSRGVHR FAVFALGSSA
     YPNFAAFGSY VDTMLGELGG ERLLKLRAGD EMCGQEQAFR SWAPEVFNVA CETFCLDDDE
     TLSDATQVIS SVTLNASTVR FLPMTTADSL VTGLSKVHSR KVWQCPLIKK WNLYGSQPVA
     RTTLGIQMRK PHDCAYEPGD HVGIFASNKW DLVSGILARL NLGGIDPDEP MELQVLSETH
     TSTEVIKSWK PHERLPRASL RTLLSRYLDI TTPPPPALLQ FFATFATAPD DQEILTLLAT
     DSAAYEDWRH WRFPHLLEVL EQFPSIHLPP ALLVAQLTPL QPRFYSISSS PLAHPNEIHL
     TVAVVTYRTQ AYEDWRHWRF PHLLEVLEQF PSIHLPPALL VAQLTPLQPR FYSISSSPLA
     HPNEIHLTVA VVTYRTQGLS KVHSRKVWQC PLIKKWNLYG SQPVAFAPVT MRKPHDCAYE
     PGDHVGIFAS NKWDLVSGIL ARLNLGGIDP DEPMELQVLS ETHTSTEVIK SWKPHERLPR
     ASLRTLLSRY LDITTPPPPA LLQFFATFAT APDDQEILTL LATVSTPASC HILTARIAVR
     IPAETAPNFH LPKEEGRSII CVGPGTGVAP FRGFWEHRYA QKMQNSRVIK FGLQELGKMT
     LFFGCQLKTM DLYSDEKSKM LDQKVLTKSF LALSREPTIP KTYVQDLMKK EASMLYRELI
     KEGGHFYVCG DCTMAEHVYQ TLKYVFQHEG NLTEQNAEKL LLRLRDENRY HEDIFGITLR
     TAEVHKSSRE SARIRMYQSG P
//

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