ID A0A2G8KE15_STIJA Unreviewed; 492 AA.
AC A0A2G8KE15;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=nitric-oxide synthase (NADPH) {ECO:0000256|ARBA:ARBA00012989};
DE EC=1.14.13.39 {ECO:0000256|ARBA:ARBA00012989};
GN ORFNames=BSL78_16951 {ECO:0000313|EMBL:PIK46209.1};
OS Stichopus japonicus (Sea cucumber).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Holothuroidea;
OC Aspidochirotacea; Aspidochirotida; Stichopodidae; Apostichopus.
OX NCBI_TaxID=307972 {ECO:0000313|EMBL:PIK46209.1, ECO:0000313|Proteomes:UP000230750};
RN [1] {ECO:0000313|EMBL:PIK46209.1, ECO:0000313|Proteomes:UP000230750}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shaxun {ECO:0000313|EMBL:PIK46209.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PIK46209.1};
RX PubMed=29023486;
RA Zhang X., Sun L., Yuan J., Sun Y., Gao Y., Zhang L., Li S., Dai H.,
RA Hamel J.F., Liu C., Yu Y., Liu S., Lin W., Guo K., Jin S., Xu P.,
RA Storey K.B., Huan P., Zhang T., Zhou Y., Zhang J., Lin C., Li X., Xing L.,
RA Huo D., Sun M., Wang L., Mercier A., Li F., Yang H., Xiang J.;
RT "The sea cucumber genome provides insights into morphological evolution and
RT visceral regeneration.";
RL PLoS Biol. 15:E2003790-E2003790(2017).
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}.
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:PIK46209.1}.
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DR EMBL; MRZV01000660; PIK46209.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G8KE15; -.
DR STRING; 307972.A0A2G8KE15; -.
DR Proteomes; UP000230750; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
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; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000230750}.
FT DOMAIN 1..222
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 473..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 492 AA; 55863 MW; 7CF1344F28C9613F CRC64;
MSCQKDQELL YQPGDVISLF PANNSSQVDR ILRRLDYHKS PDAVFKLEKL VQKDTRLGRL
KVWTSITRLP VCSVRMALCR YLDITTPPSP DLLRLLAIRA GEPKERERLL VLGMGGDIYD
EWKLEEAPTI ADILERFESL RVPASLLITQ LPLLSPRLYS ISSSPDLYPS EIHITVTLST
FYTKGNLGEI QHNGVCSSWL QDISTDDVIP ACIVSNPSFH IPKDDSVPMI LVATGTGIAP
FRSFWQHREA DLTKYDSAPE VPESDRRVPT FGDMTLVYGC RKATVDEPYR SDLITAKEHG
VITSTMMTFS REESQQRQRY VQDVLRDHPW LVYSTICRRN GHVFVSGDVT MATEVRITVE
AILSQYGRMS MVDAQNYVTR MKEDCRYHEN IFGLVLHVAD VIKQKRQDKK QPRVLVSRDI
IKPIPLGIAG KKASISELAK KFDSDPRRPP SLHQRRATAT VLMPRYSKPL MIPQVERNDD
VNNNMKGHSG SK
//
