ID   NOS_RHOPR               Reviewed;        1174 AA.
AC   Q26240;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 73.
DE   RecName: Full=Nitric oxide synthase, salivary gland;
DE            Short=NOS;
DE            EC=1.14.13.39;
OS   Rhodnius prolixus (Triatomid bug).
OC   Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Hemiptera; Euhemiptera; Heteroptera;
OC   Panheteroptera; Cimicomorpha; Reduviidae; Triatominae; Rhodnius.
OX   NCBI_TaxID=13249;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Salivary gland;
RX   MEDLINE=97175053; PubMed=9022713;
RX   DOI=10.1111/j.1432-1033.1996.0807r.x;
RA   Yuda M., Hirai M., Miura K., Matsumura H., Ando K., Chinzei Y.;
RT   "cDNA cloning, expression and characterization of nitric-oxide
RT   synthase from the salivary glands of the blood-sucking insect Rhodnius
RT   prolixus.";
RL   Eur. J. Biochem. 242:807-812(1996).
CC   -!- FUNCTION: Produces nitric oxide (NO) which is a messenger molecule
CC       with diverse functions throughout the body. The production of NO
CC       in the salivary gland is used as a vasodilator for blood sucking.
CC   -!- CATALYTIC ACTIVITY: L-arginine + n NADPH + n H(+) + m O(2) =
CC       citrulline + nitric oxide + n NADP(+).
CC   -!- COFACTOR: Heme group (By similarity).
CC   -!- COFACTOR: Binds 1 FAD (By similarity).
CC   -!- COFACTOR: Binds 1 FMN (By similarity).
CC   -!- ENZYME REGULATION: Stimulated by calcium/calmodulin.
CC   -!- SIMILARITY: Belongs to the NOS family.
CC   -!- SIMILARITY: Contains 1 FAD-binding FR-type domain.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   EMBL; U59389; AAB03810.1; -; mRNA.
DR   HSSP; P29477; 1DD7.
DR   BRENDA; 1.14.13.39; 142456.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP or NADPH binding; IEA:InterPro.
DR   GO; GO:0004517; F:nitric-oxide synthase activity; IEA:EC.
DR   GO; GO:0006809; P:nitric oxide biosynthetic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR003097; FAD-binding_1.
DR   InterPro; IPR017927; Fd_Rdtase_FAD-bd.
DR   InterPro; IPR001094; Flavdoxin-like.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR012144; Nitric-oxide_synthase.
DR   InterPro; IPR004030; NO_synthase_oxygenase_reg.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD_bd.
DR   Gene3D; G3DSA:3.90.340.10; NO_synthase_oxygenase_reg; 1.
DR   Pfam; PF00667; FAD_binding_1; 1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   Pfam; PF02898; NO_synthase; 1.
DR   PIRSF; PIRSF000333; NOS; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   PRINTS; PR00371; FPNCR.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
DR   PROSITE; PS60001; NOS; 1.
PE   2: Evidence at transcript level;
KW   Calmodulin-binding; FAD; FMN; Heme; Iron; Metal-binding; NADP;
KW   Oxidoreductase.
FT   CHAIN         1   1174       Nitric oxide synthase, salivary gland.
FT                                /FTId=PRO_0000170952.
FT   DOMAIN      505    693       Flavodoxin-like.
FT   DOMAIN      745    990       FAD-binding FR-type.
FT   NP_BIND     639    670       FMN (By similarity).
FT   NP_BIND     780    791       FAD (By similarity).
FT   NP_BIND     923    933       FAD (By similarity).
FT   NP_BIND     998   1016       NADP (By similarity).
FT   NP_BIND    1095   1110       NADP (By similarity).
FT   REGION      475    495       Calmodulin-binding (Potential).
FT   COMPBIAS     35     45       Poly-Gln.
FT   METAL       162    162       Iron (heme axial ligand) (By similarity).
SQ   SEQUENCE   1174 AA;  132393 MW;  C32F664EE51409CF CRC64;
     MVHAECVWWL GIRILFVPPV SLEMHSVNVN NMSIQQQQQH QPQQQLLKPI RLANVSTQAQ
     SLDTLHYKCQ QEGPCMEQAC LASVIYAGVN LKPRVRPKEE LLAHAKDFLD QYFASIRRLQ
     SPAHEARWAQ VEKEVAATGT YELTETELVY GAKLAWRNAP RCIGRIQWAK LQVFDCRQVT
     TTSGMFEALC NHIKYSTNKG NIRSAITIFP HRTDGKHDFR IWNKQLISYA GHKSKDGTVI
     GDPACVEFTE ICIKLGWKGK GTMFDVLPLV LSANGEDPDY FDLPPELVFE VPLSHPKYKW
     FSELGLKWFA LPAVSGMMFD CGGLQFTAAP FNGWYMNSEI GSRNLGDTNR YNMLEKIAQK
     MELDTRTPVT LWKDLAMVEA NVAVLHSFQL HNVTIVDHHS AAESFMKHLE NEQRLRGGCP
     ADWVWIVPPI SGSATPVFFQ EMANYFLYPG YIYQEDAWKC HEWKEIDVKH GLKKEKRKFH
     FKQIARAVKF TSKLFGSALS KRIKATILFA TETGKSEMYA RKLGDIFSHA FHSQVLSMED
     YDMSKIEHEA LLLVVASTFG NGDPPENGQG FAQSLYTIKM DENGLPNGHT NNTLASSASF
     IKANSQTDRQ ASLERCDSFR GSTGDADVFG PLSNVRFAVF ALGSSAYPNF CAFGSYVDNL
     LGELGGERLV KLTTGDEMCG QAQACNKWAP EVFSVACDTF CLDSDETFLE ATQMLHSEAV
     TASTVRFVES ATQDLCKALS HLHNKKVWKC PLLGKRNLHG KGSTRATLLL EIERNENISY
     QPGDHVGVLA CNRKELVEGI ISHLESAIDP DKSVQLQILK ENTTPDGIVR NWIPHDRLPT
     CSLRTMLTRF LDITTPPSPN LLQFFASCAT NSEDQEKLTE LATDSAAYED WRYWKYPNLL
     EVLEEFPSVR VLPALLIAQL TPLQPRFYSI SSAPSLYANQ IHLTVAVVQY CTQDGKGPIH
     YGVASNYLYD VTIGDSIYLF TRSAPNFHLP KSDTAPIIMV GPGTGIAPFR GFWQHRLAQR
     SLNGPGKFGK MSLFFGCRLR NLDLYQEEKE SMLKEGILSK VFLALSREPS IPKTYVQDLL
     RVECKSVYIQ IVQEGGHFYV CGDCTMAEHV FRTLRQIIQD QGNMTDHQVD NFMLAMRDEN
     RYHEDIFGIT LRTAEVHNRS RESARIRMAS QSQP
//