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Conserved domains on  [gi|231571356|ref|NP_001153583|]
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nitric oxide synthase 3 isoform 4 [Homo sapiens]

Protein Classification

nitric oxide synthase oxygenase( domain architecture ID 10092403)

nitric oxide synthase oxygenase functions together with ferredoxins or flavodoxins to catalyze the production of nitric oxide

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NOS_oxygenase_euk cd00795
Nitric oxide synthase (NOS) eukaryotic oxygenase domain. NOS produces nitric oxide (NO) by ...
68-480 0e+00

Nitric oxide synthase (NOS) eukaryotic oxygenase domain. NOS produces nitric oxide (NO) by catalyzing a five-electron heme-based oxidation of a guanidine nitrogen of L-arginine to L-citrulline via two successive monooxygenation reactions producing N(omega)-hydroxy-L-arginine (NHA) as an intermediate. In mammals, there are three distinct NOS isozymes: neuronal (nNOS or NOS-1), cytokine-inducible (iNOS or NOS-2) and endothelial (eNOS or NOS-3) . Nitric oxide synthases are homodimers. In eukaryotes, each monomer has an N-terminal oxygenase domain, which binds to the substrate L-Arg, zinc, and to the cofactors heme and 5.6.7.8-(6R)-tetrahydrobiopterin (BH4) . Eukaryotic NOS's also have a C-terminal electron supplying reductase region, which is homologous to cytochrome P450 reductase and binds NADH, FAD and FMN.


:

Pssm-ID: 238410  Cd Length: 412  Bit Score: 863.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231571356  68 FPRVKNWEVGSITYDTLSAQAQQDGPCTPRRCLGSLVFPRKLQGRPSPGPPaPEQLLSQARDFINQYYSSIKRSGSQAHE 147
Cdd:cd00795    1 FVRVKNWETGSILYDTLHSKATQDGPCTERRCLGSIMDPKKLTRRPRDGRP-KEELLPQAKDFINQYYSSIKRSGSEAHL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231571356 148 QRLQEVEAEVAATGTYQLRESELVFGAKQAWRNAPRCVGRIQWGKLQVFDARDCRSAQEMFTYICNHIKYATNRGNLRSA 227
Cdd:cd00795   80 ARLEEVTKEIEATGTYQLTEDELIFGAKQAWRNAPRCIGRIQWSKLQVFDARDCTTAQEMFEAICNHIKYATNKGNLRSA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231571356 228 ITVFPQRCPGRGDFRIWNSQLVRYAGYRQQDGSVRGDPANVEITELCIQHGWTPGNGRFDVLPLLLQAPDDPPELFLLPP 307
Cdd:cd00795  160 ITVFPQRTDGKHDFRIWNSQLIRYAGYKQPDGSIIGDPANVEFTELCIKLGWKPKYGRFDVLPLVLQANGEDPELFEIPP 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231571356 308 ELVLEVPLEHPTLEWFAALGLRWYALPAVSNMLLEIGGLEFPAAPFSGWYMSTEIGTRNLCDPHRYNILEDVAVCMDLDT 387
Cdd:cd00795  240 ELVLEVPIEHPKYEWFKELGLKWYALPAVSNMLLEIGGLEFTACPFNGWYMGTEIGVRDLCDQQRYNILEEVAKKMGLDT 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231571356 388 RTTSSLWKDKAAVEINVAVLHSYQLAKVTIVDHHAATASFMKHLENEQKARGGCPADWAWIVPPISGSLTPVFHQEMVNY 467
Cdd:cd00795  320 RKTSSLWKDKALVEINVAVLHSFQKANVTIVDHHSASESFMKHMENEYRARGGCPADWVWIVPPMSGSITPVFHQEMLNY 399
                        410
                 ....*....|...
gi 231571356 468 FLSPAFRYQPDPW 480
Cdd:cd00795  400 VLSPSYEYQPDPW 412
CysJ super family cl43121
Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases ...
512-586 4.56e-20

Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases [Nucleotide transport and metabolism, Inorganic ion transport and metabolism]; Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases is part of the Pathway/BioSystem: Cysteine biosynthesis


The actual alignment was detected with superfamily member COG0369:

Pssm-ID: 440138 [Multi-domain]  Cd Length: 561  Bit Score: 94.06  E-value: 4.56e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 231571356 512 TVMAKRVKATILYGSETGRAQSYAQQLGRLFRKA-FDPRVLCMDEYDVVSLEHETLVLVVTSTFGNGDPPENGEGL 586
Cdd:COG0369   21 AAAAAGTPLTILYGSQTGNAEGLAEQLAERAKAAgLAVTLASLDDYKPKDLAKEGLLLIVTSTYGEGEPPDNARAF 96
 
Name Accession Description Interval E-value
NOS_oxygenase_euk cd00795
Nitric oxide synthase (NOS) eukaryotic oxygenase domain. NOS produces nitric oxide (NO) by ...
68-480 0e+00

Nitric oxide synthase (NOS) eukaryotic oxygenase domain. NOS produces nitric oxide (NO) by catalyzing a five-electron heme-based oxidation of a guanidine nitrogen of L-arginine to L-citrulline via two successive monooxygenation reactions producing N(omega)-hydroxy-L-arginine (NHA) as an intermediate. In mammals, there are three distinct NOS isozymes: neuronal (nNOS or NOS-1), cytokine-inducible (iNOS or NOS-2) and endothelial (eNOS or NOS-3) . Nitric oxide synthases are homodimers. In eukaryotes, each monomer has an N-terminal oxygenase domain, which binds to the substrate L-Arg, zinc, and to the cofactors heme and 5.6.7.8-(6R)-tetrahydrobiopterin (BH4) . Eukaryotic NOS's also have a C-terminal electron supplying reductase region, which is homologous to cytochrome P450 reductase and binds NADH, FAD and FMN.


Pssm-ID: 238410  Cd Length: 412  Bit Score: 863.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231571356  68 FPRVKNWEVGSITYDTLSAQAQQDGPCTPRRCLGSLVFPRKLQGRPSPGPPaPEQLLSQARDFINQYYSSIKRSGSQAHE 147
Cdd:cd00795    1 FVRVKNWETGSILYDTLHSKATQDGPCTERRCLGSIMDPKKLTRRPRDGRP-KEELLPQAKDFINQYYSSIKRSGSEAHL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231571356 148 QRLQEVEAEVAATGTYQLRESELVFGAKQAWRNAPRCVGRIQWGKLQVFDARDCRSAQEMFTYICNHIKYATNRGNLRSA 227
Cdd:cd00795   80 ARLEEVTKEIEATGTYQLTEDELIFGAKQAWRNAPRCIGRIQWSKLQVFDARDCTTAQEMFEAICNHIKYATNKGNLRSA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231571356 228 ITVFPQRCPGRGDFRIWNSQLVRYAGYRQQDGSVRGDPANVEITELCIQHGWTPGNGRFDVLPLLLQAPDDPPELFLLPP 307
Cdd:cd00795  160 ITVFPQRTDGKHDFRIWNSQLIRYAGYKQPDGSIIGDPANVEFTELCIKLGWKPKYGRFDVLPLVLQANGEDPELFEIPP 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231571356 308 ELVLEVPLEHPTLEWFAALGLRWYALPAVSNMLLEIGGLEFPAAPFSGWYMSTEIGTRNLCDPHRYNILEDVAVCMDLDT 387
Cdd:cd00795  240 ELVLEVPIEHPKYEWFKELGLKWYALPAVSNMLLEIGGLEFTACPFNGWYMGTEIGVRDLCDQQRYNILEEVAKKMGLDT 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231571356 388 RTTSSLWKDKAAVEINVAVLHSYQLAKVTIVDHHAATASFMKHLENEQKARGGCPADWAWIVPPISGSLTPVFHQEMVNY 467
Cdd:cd00795  320 RKTSSLWKDKALVEINVAVLHSFQKANVTIVDHHSASESFMKHMENEYRARGGCPADWVWIVPPMSGSITPVFHQEMLNY 399
                        410
                 ....*....|...
gi 231571356 468 FLSPAFRYQPDPW 480
Cdd:cd00795  400 VLSPSYEYQPDPW 412
NO_synthase pfam02898
Nitric oxide synthase, oxygenase domain;
120-481 0e+00

Nitric oxide synthase, oxygenase domain;


Pssm-ID: 460742  Cd Length: 362  Bit Score: 748.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231571356  120 PEQLLSQARDFINQYYSSIKRSgSQAHEQRLQEVEAEVAATGTYQLRESELVFGAKQAWRNAPRCVGRIQWGKLQVFDAR 199
Cdd:pfam02898   2 KEELLEEAKEFIEQYYTELKRS-SEEHEARWEEVRAEIEETGTYQHTYEELAYGAKLAWRNSNRCIGRIFWSKLQVFDAR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231571356  200 DCRSAQEMFTYICNHIKYATNRGNLRSAITVFPQRCPGRGDFRIWNSQLVRYAGYRQQDGSVRGDPANVEITELCIQHGW 279
Cdd:pfam02898  81 HVTTEEEMFEALCNHIKYATNGGNIRSAITIFPPRTDGKHDFRIWNHQLIRYAGYEQPDGSVIGDPANVEFTELCEKLGW 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231571356  280 TPGNGRFDVLPLLLQAPDDPPELFLLPPELVLEVPLEHPTLEWFAALGLRWYALPAVSNMLLEIGGLEFPAAPFSGWYMS 359
Cdd:pfam02898 161 KGKGTRFDVLPLVIQANGEDPKLFEIPPELVLEVPIEHPEYEWFAELGLKWYAVPAISNMRLEIGGIEYTAAPFNGWYMG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231571356  360 TEIGTRNLCDPHRYNILEDVAVCMDLDTRTTSSLWKDKAAVEINVAVLHSYQLAKVTIVDHHAATASFMKHLENEQKARG 439
Cdd:pfam02898 241 TEIGARNLADEYRYNLLEKVAKKMGLDTRSNSSLWKDRALVELNVAVLHSFQKAGVTIVDHHTAAEQFMKHEENEQRAGR 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 231571356  440 GCPADWAWIVPPISGSLTPVFHQEMVNYFLSPAFRYQPDPWK 481
Cdd:pfam02898 321 GCPGDWVWLVPPLSGSTTPVFHQEMDNYILKPNFFYQEDPWK 362
COG4362 COG4362
Nitric oxide synthase, oxygenase domain [Inorganic ion transport and metabolism];
119-478 0e+00

Nitric oxide synthase, oxygenase domain [Inorganic ion transport and metabolism];


Pssm-ID: 443495  Cd Length: 360  Bit Score: 590.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231571356 119 APEQLLSQARDFINQYYSSIKRSGsQAHEQRLQEVEAEVAATGTYQLRESELVFGAKQAWRNAPRCVGRIQWGKLQVFDA 198
Cdd:COG4362    2 EQEALLAEAEEFLRQCYKELGKSE-EEVERRLAEVRAEIAATGTYTHTYEELEYGARVAWRNSNRCIGRLFWRSLQVRDR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231571356 199 RDCRSAQEMFTYICNHIKYATNRGNLRSAITVFPQRCPGRGDFRIWNSQLVRYAGYRQQDGSVRGDPANVEITELCIQHG 278
Cdd:COG4362   81 RHVTTPEEVFEALVEHLRFATNGGKIRPTITVFAPDQPGRPGVRIWNHQLIRYAGYETEDGSVLGDPASVEFTDACQRLG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231571356 279 WTPGNGRFDVLPLLLQAPDDPPELFLLPPELVLEVPLEHPTLEWFAALGLRWYALPAVSNMLLEIGGLEFPAAPFSGWYM 358
Cdd:COG4362  161 WRGPRTAFDVLPLVIQVGGEPPRLFEIPRDLVLEVPITHPEYPWFAELGLRWYAVPAISNMRLEIGGIDYPAAPFNGWYM 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231571356 359 STEIGTRNLCDPHRYNILEDVAVCMDLDTRTTSSLWKDKAAVEINVAVLHSYQLAKVTIVDHHAATASFMKHLENEQKAR 438
Cdd:COG4362  241 GTEIGARNLADEDRYNLLPKVAERMGLDTSSNRTLWKDRALVELNIAVLHSFKKAGVTIVDHHTASQQFLTFEQREEKAG 320
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 231571356 439 GGCPADWAWIVPPISGSLTPVFHQEMVNYFLSPAFRYQPD 478
Cdd:COG4362  321 REVTGDWSWLIPPMSGATTHVFHRYYDNEILKPNFFYQDD 360
CysJ COG0369
Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases ...
512-586 4.56e-20

Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases [Nucleotide transport and metabolism, Inorganic ion transport and metabolism]; Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 440138 [Multi-domain]  Cd Length: 561  Bit Score: 94.06  E-value: 4.56e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 231571356 512 TVMAKRVKATILYGSETGRAQSYAQQLGRLFRKA-FDPRVLCMDEYDVVSLEHETLVLVVTSTFGNGDPPENGEGL 586
Cdd:COG0369   21 AAAAAGTPLTILYGSQTGNAEGLAEQLAERAKAAgLAVTLASLDDYKPKDLAKEGLLLIVTSTYGEGEPPDNARAF 96
Flavodoxin_1 pfam00258
Flavodoxin;
522-586 2.76e-16

Flavodoxin;


Pssm-ID: 425562 [Multi-domain]  Cd Length: 142  Bit Score: 75.87  E-value: 2.76e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 231571356  522 ILYGSETGRAQSYAQQLGRLFRKA-FDPRVLCMDEYDVVS--LEHETLVLVVTSTFGNGDPPENGEGL 586
Cdd:pfam00258   1 IFYGSQTGNTEKLAEAIAEGLGEAgFEVDVVDLDDVDETLseIEEEDLLLVVVSTWGEGEPPDNAKPF 68
PHA03247 PHA03247
large tegument protein UL36; Provisional
34-121 2.05e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 2.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231571356   34 PAPEPSRAPASLLPPAPEHSPPSSPLTQPPEGPKfPRVKnwevGSITYDTLSAQAQQDGPCTPRRCLGSLV-----FPRK 108
Cdd:PHA03247 2903 DQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPP-PRPQ----PPLAPTTDPAGAGEPSGAVPQPWLGALVpgrvaVPRF 2977
                          90
                  ....*....|...
gi 231571356  109 LQGRPSPGPPAPE 121
Cdd:PHA03247 2978 RVPQPAPSREAPA 2990
 
Name Accession Description Interval E-value
NOS_oxygenase_euk cd00795
Nitric oxide synthase (NOS) eukaryotic oxygenase domain. NOS produces nitric oxide (NO) by ...
68-480 0e+00

Nitric oxide synthase (NOS) eukaryotic oxygenase domain. NOS produces nitric oxide (NO) by catalyzing a five-electron heme-based oxidation of a guanidine nitrogen of L-arginine to L-citrulline via two successive monooxygenation reactions producing N(omega)-hydroxy-L-arginine (NHA) as an intermediate. In mammals, there are three distinct NOS isozymes: neuronal (nNOS or NOS-1), cytokine-inducible (iNOS or NOS-2) and endothelial (eNOS or NOS-3) . Nitric oxide synthases are homodimers. In eukaryotes, each monomer has an N-terminal oxygenase domain, which binds to the substrate L-Arg, zinc, and to the cofactors heme and 5.6.7.8-(6R)-tetrahydrobiopterin (BH4) . Eukaryotic NOS's also have a C-terminal electron supplying reductase region, which is homologous to cytochrome P450 reductase and binds NADH, FAD and FMN.


Pssm-ID: 238410  Cd Length: 412  Bit Score: 863.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231571356  68 FPRVKNWEVGSITYDTLSAQAQQDGPCTPRRCLGSLVFPRKLQGRPSPGPPaPEQLLSQARDFINQYYSSIKRSGSQAHE 147
Cdd:cd00795    1 FVRVKNWETGSILYDTLHSKATQDGPCTERRCLGSIMDPKKLTRRPRDGRP-KEELLPQAKDFINQYYSSIKRSGSEAHL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231571356 148 QRLQEVEAEVAATGTYQLRESELVFGAKQAWRNAPRCVGRIQWGKLQVFDARDCRSAQEMFTYICNHIKYATNRGNLRSA 227
Cdd:cd00795   80 ARLEEVTKEIEATGTYQLTEDELIFGAKQAWRNAPRCIGRIQWSKLQVFDARDCTTAQEMFEAICNHIKYATNKGNLRSA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231571356 228 ITVFPQRCPGRGDFRIWNSQLVRYAGYRQQDGSVRGDPANVEITELCIQHGWTPGNGRFDVLPLLLQAPDDPPELFLLPP 307
Cdd:cd00795  160 ITVFPQRTDGKHDFRIWNSQLIRYAGYKQPDGSIIGDPANVEFTELCIKLGWKPKYGRFDVLPLVLQANGEDPELFEIPP 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231571356 308 ELVLEVPLEHPTLEWFAALGLRWYALPAVSNMLLEIGGLEFPAAPFSGWYMSTEIGTRNLCDPHRYNILEDVAVCMDLDT 387
Cdd:cd00795  240 ELVLEVPIEHPKYEWFKELGLKWYALPAVSNMLLEIGGLEFTACPFNGWYMGTEIGVRDLCDQQRYNILEEVAKKMGLDT 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231571356 388 RTTSSLWKDKAAVEINVAVLHSYQLAKVTIVDHHAATASFMKHLENEQKARGGCPADWAWIVPPISGSLTPVFHQEMVNY 467
Cdd:cd00795  320 RKTSSLWKDKALVEINVAVLHSFQKANVTIVDHHSASESFMKHMENEYRARGGCPADWVWIVPPMSGSITPVFHQEMLNY 399
                        410
                 ....*....|...
gi 231571356 468 FLSPAFRYQPDPW 480
Cdd:cd00795  400 VLSPSYEYQPDPW 412
NO_synthase pfam02898
Nitric oxide synthase, oxygenase domain;
120-481 0e+00

Nitric oxide synthase, oxygenase domain;


Pssm-ID: 460742  Cd Length: 362  Bit Score: 748.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231571356  120 PEQLLSQARDFINQYYSSIKRSgSQAHEQRLQEVEAEVAATGTYQLRESELVFGAKQAWRNAPRCVGRIQWGKLQVFDAR 199
Cdd:pfam02898   2 KEELLEEAKEFIEQYYTELKRS-SEEHEARWEEVRAEIEETGTYQHTYEELAYGAKLAWRNSNRCIGRIFWSKLQVFDAR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231571356  200 DCRSAQEMFTYICNHIKYATNRGNLRSAITVFPQRCPGRGDFRIWNSQLVRYAGYRQQDGSVRGDPANVEITELCIQHGW 279
Cdd:pfam02898  81 HVTTEEEMFEALCNHIKYATNGGNIRSAITIFPPRTDGKHDFRIWNHQLIRYAGYEQPDGSVIGDPANVEFTELCEKLGW 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231571356  280 TPGNGRFDVLPLLLQAPDDPPELFLLPPELVLEVPLEHPTLEWFAALGLRWYALPAVSNMLLEIGGLEFPAAPFSGWYMS 359
Cdd:pfam02898 161 KGKGTRFDVLPLVIQANGEDPKLFEIPPELVLEVPIEHPEYEWFAELGLKWYAVPAISNMRLEIGGIEYTAAPFNGWYMG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231571356  360 TEIGTRNLCDPHRYNILEDVAVCMDLDTRTTSSLWKDKAAVEINVAVLHSYQLAKVTIVDHHAATASFMKHLENEQKARG 439
Cdd:pfam02898 241 TEIGARNLADEYRYNLLEKVAKKMGLDTRSNSSLWKDRALVELNVAVLHSFQKAGVTIVDHHTAAEQFMKHEENEQRAGR 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 231571356  440 GCPADWAWIVPPISGSLTPVFHQEMVNYFLSPAFRYQPDPWK 481
Cdd:pfam02898 321 GCPGDWVWLVPPLSGSTTPVFHQEMDNYILKPNFFYQEDPWK 362
NOS_oxygenase cd00575
Nitric oxide synthase (NOS) produces nitric oxide (NO) by catalyzing a five-electron ...
122-477 0e+00

Nitric oxide synthase (NOS) produces nitric oxide (NO) by catalyzing a five-electron heme-based oxidation of a guanidine nitrogen of L-arginine to L-citrulline via two successive monooxygenation reactions producing N(omega)-hydroxy-L-arginine (NHA) as an intermediate. In mammals, there are three distinct NOS isozymes: neuronal (nNOS or NOS-1), cytokine-inducible (iNOS or NOS-2) and endothelial (eNOS or NOS-3) . Nitric oxide synthases are homodimers. In eukaryotes, each monomer has an N-terminal oxygenase domain which binds to the substrate L-Arg, zinc, and to the cofactors heme and 5.6.7.8-(6R)-tetrahydrobiopterin (BH4) . Eukaryotic NOSs also have a C-terminal electron supplying reductase region, which is homologous to cytochrome P450 reductase and binds NADH, FAD and FMN. While prokaryotes can produce NO as a byproduct of denitrification, using a completely different set of enzymes than NOS, a few prokaryotes also have a NOS which consists solely of the NOS oxygenase domain. Prokaryotic NOS binds to the substrate L-Arg, zinc, and to the cofactors heme and tetrahydrofolate.


Pssm-ID: 238321  Cd Length: 356  Bit Score: 734.08  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231571356 122 QLLSQARDFINQYYSSIKRSGSQAHEQRLQEVEAEVAATGTYQLRESELVFGAKQAWRNAPRCVGRIQWGKLQVFDARDC 201
Cdd:cd00575    1 ELLPQAKDFINQYYSSIKRSGSEAHEARLEEVEKEIEATGTYQLTEEELIYGAKMAWRNAPRCIGRIQWSKLQVFDARDV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231571356 202 RSAQEMFTYICNHIKYATNRGNLRSAITVFPQRCPGRGDFRIWNSQLVRYAGYRQQDGSVRGDPANVEITELCIQHGWTP 281
Cdd:cd00575   81 TTAQEMFEAICNHIKYATNGGNIRSAITVFPQRTDGKHDFRIWNSQLIRYAGYKQPDGSIIGDPANVEFTELCIQLGWKP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231571356 282 GNGRFDVLPLLLQAPDDPPELFLLPPELVLEVPLEHPTLEWFAALGLRWYALPAVSNMLLEIGGLEFPAAPFSGWYMSTE 361
Cdd:cd00575  161 KGGRFDVLPLVLQANGEDPELFEIPPELVLEVPIEHPKYEWFAELGLKWYALPAVSNMLLEIGGLEFPAAPFNGWYMGTE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231571356 362 IGTRNLCDPHRYNILEDVAVCMDLDTRTTSSLWKDKAAVEINVAVLHSYQLAKVTIVDHHAATASFMKHLENEQKARGGC 441
Cdd:cd00575  241 IGVRNLCDTQRYNILEKVARKMGLDTRKNSSLWKDRALVELNVAVLHSFQKAGVTIVDHHTAAESFMKHLENEYRARGGC 320
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 231571356 442 PADWAWIVPPISGSLTPVFHQEMVNYFLSPAFRYQP 477
Cdd:cd00575  321 PADWVWLVPPMSGSLTPVFHQEMLNYVLSPSFFYQP 356
COG4362 COG4362
Nitric oxide synthase, oxygenase domain [Inorganic ion transport and metabolism];
119-478 0e+00

Nitric oxide synthase, oxygenase domain [Inorganic ion transport and metabolism];


Pssm-ID: 443495  Cd Length: 360  Bit Score: 590.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231571356 119 APEQLLSQARDFINQYYSSIKRSGsQAHEQRLQEVEAEVAATGTYQLRESELVFGAKQAWRNAPRCVGRIQWGKLQVFDA 198
Cdd:COG4362    2 EQEALLAEAEEFLRQCYKELGKSE-EEVERRLAEVRAEIAATGTYTHTYEELEYGARVAWRNSNRCIGRLFWRSLQVRDR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231571356 199 RDCRSAQEMFTYICNHIKYATNRGNLRSAITVFPQRCPGRGDFRIWNSQLVRYAGYRQQDGSVRGDPANVEITELCIQHG 278
Cdd:COG4362   81 RHVTTPEEVFEALVEHLRFATNGGKIRPTITVFAPDQPGRPGVRIWNHQLIRYAGYETEDGSVLGDPASVEFTDACQRLG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231571356 279 WTPGNGRFDVLPLLLQAPDDPPELFLLPPELVLEVPLEHPTLEWFAALGLRWYALPAVSNMLLEIGGLEFPAAPFSGWYM 358
Cdd:COG4362  161 WRGPRTAFDVLPLVIQVGGEPPRLFEIPRDLVLEVPITHPEYPWFAELGLRWYAVPAISNMRLEIGGIDYPAAPFNGWYM 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231571356 359 STEIGTRNLCDPHRYNILEDVAVCMDLDTRTTSSLWKDKAAVEINVAVLHSYQLAKVTIVDHHAATASFMKHLENEQKAR 438
Cdd:COG4362  241 GTEIGARNLADEDRYNLLPKVAERMGLDTSSNRTLWKDRALVELNIAVLHSFKKAGVTIVDHHTASQQFLTFEQREEKAG 320
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 231571356 439 GGCPADWAWIVPPISGSLTPVFHQEMVNYFLSPAFRYQPD 478
Cdd:COG4362  321 REVTGDWSWLIPPMSGATTHVFHRYYDNEILKPNFFYQDD 360
NOS_oxygenase_prok cd00794
Nitric oxide synthase (NOS) prokaryotic oxygenase domain. NOS produces nitric oxide (NO) by ...
123-477 1.02e-158

Nitric oxide synthase (NOS) prokaryotic oxygenase domain. NOS produces nitric oxide (NO) by catalyzing a five-electron heme-based oxidation of a guanidine nitrogen of L-arginine to L-citrulline via two successive monooxygenation reactions producing N(omega)-hydroxy-L-arginine (NHA) as an intermediate. Nitric oxide synthases are homodimers. Most prokaryotes produce NO as a byproduct of denitrification, using a completely different set of enzymes than NOS. However, a few prokaryotes also have a NOS, consisting solely of the NOS oxygenase domain. Prokaryotic NOS binds to the substrate L-Arg, zinc, and to the cofactors heme and tetrahydrofolate.


Pssm-ID: 238409  Cd Length: 353  Bit Score: 459.59  E-value: 1.02e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231571356 123 LLSQARDFINQYYSSIKRSGSQahEQRLQEVEAEVAATGTYQLRESELVFGAKQAWRNAPRCVGRIQWGKLQVFDARDCR 202
Cdd:cd00794    2 LFKEARAFLTNMYEELGETGEL--NKRLAAVESEIDETGTYTHTTEELVYGAKMAWRNSNRCIGRLFWESLNVRDARDVR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231571356 203 SAQEMFTYICNHIKYATNRGNLRSAITVFPQRCPGRGDFRIWNSQLVRYAGYrQQDGSVRGDPANVEITELCIQHGWTPG 282
Cdd:cd00794   80 TEEEVAEALLDHITEATNGGKIRPYITIFAPEAPGKDGPRIWNNQLIRYAGY-ERPGANIGDPASAKFTRLAERLGWKGK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231571356 283 NGRFDVLPLLLQAPDDPPELFLLPPELVLEVPLEHPTLEWFAALGLRWYALPAVSNMLLEIGGLEFPAAPFSGWYMSTEI 362
Cdd:cd00794  159 GTNFDVLPLIIQLPGDRPKWFELPNDAVKEVPITHPHYPKIRKLGLKWYAVPIISDMDLEIGGIHYPAAPFNGWYMGTEI 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231571356 363 GTRNLCDPHRYNILEDVAVCMDLDTRTTSSLWKDKAAVEINVAVLHSYQLAKVTIVDHHAATASFMKHLENEQKARGGCP 442
Cdd:cd00794  239 GARNLADEYRYNLLPKVAEALGLDTLKNRSLWKDRALVELNVAVLHSFKKAGVSIVDHHTAAKQFERFEEREARAGRKVT 318
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 231571356 443 ADWAWIVPPISGSLTPVFHQEMVNYFLSPAFRYQP 477
Cdd:cd00794  319 GKWSWLIPPLSPATTHIFHRGYDNTEVHPNFFYQK 353
CysJ COG0369
Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases ...
512-586 4.56e-20

Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases [Nucleotide transport and metabolism, Inorganic ion transport and metabolism]; Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 440138 [Multi-domain]  Cd Length: 561  Bit Score: 94.06  E-value: 4.56e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 231571356 512 TVMAKRVKATILYGSETGRAQSYAQQLGRLFRKA-FDPRVLCMDEYDVVSLEHETLVLVVTSTFGNGDPPENGEGL 586
Cdd:COG0369   21 AAAAAGTPLTILYGSQTGNAEGLAEQLAERAKAAgLAVTLASLDDYKPKDLAKEGLLLIVTSTYGEGEPPDNARAF 96
Flavodoxin_1 pfam00258
Flavodoxin;
522-586 2.76e-16

Flavodoxin;


Pssm-ID: 425562 [Multi-domain]  Cd Length: 142  Bit Score: 75.87  E-value: 2.76e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 231571356  522 ILYGSETGRAQSYAQQLGRLFRKA-FDPRVLCMDEYDVVS--LEHETLVLVVTSTFGNGDPPENGEGL 586
Cdd:pfam00258   1 IFYGSQTGNTEKLAEAIAEGLGEAgFEVDVVDLDDVDETLseIEEEDLLLVVVSTWGEGEPPDNAKPF 68
PHA03247 PHA03247
large tegument protein UL36; Provisional
34-121 2.05e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 2.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231571356   34 PAPEPSRAPASLLPPAPEHSPPSSPLTQPPEGPKfPRVKnwevGSITYDTLSAQAQQDGPCTPRRCLGSLV-----FPRK 108
Cdd:PHA03247 2903 DQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPP-PRPQ----PPLAPTTDPAGAGEPSGAVPQPWLGALVpgrvaVPRF 2977
                          90
                  ....*....|...
gi 231571356  109 LQGRPSPGPPAPE 121
Cdd:PHA03247 2978 RVPQPAPSREAPA 2990
PHA03247 PHA03247
large tegument protein UL36; Provisional
28-124 5.40e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.31  E-value: 5.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231571356   28 KQGPATPApEPSRAPASLLPpAPEHSPPSSPLTQPPEGPKFPRVKNWEVGSITYDTLSAQAQ-QDGPCTPRRCLGSLVFP 106
Cdd:PHA03247 2869 RSPAAKPA-APARPPVRRLA-RPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQpQPPPPPPPRPQPPLAPT 2946
                          90
                  ....*....|....*...
gi 231571356  107 RKLQGRPSPGPPAPEQLL 124
Cdd:PHA03247 2947 TDPAGAGEPSGAVPQPWL 2964
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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