NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|767993833|ref|XP_011522741|]
View 

N-acetylglutamate synthase, mitochondrial isoform X2 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
AAK super family cl00452
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ...
 1-205 1.92e-124

Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like N-acetylglutamate kinase (NAGK), carbamate kinase (CK), aspartokinase (AK), glutamate-5-kinase (G5K) and UMP kinase (UMPK). The AAK superfamily includes kinases that phosphorylate a variety of amino acid substrates. These kinases catalyze the formation of phosphoric anhydrides, generally with a carboxylate, and use ATP as the source of the phosphoryl group; are involved in amino acid biosynthesis. Some of these kinases control the process via allosteric feed-back inhibition.


The actual alignment was detected with superfamily member cd04236:

Pssm-ID: 444912 [Multi-domain]  Cd Length: 271  Bit Score: 359.16  E-value: 1.92e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833   1 MDMKPLVVLGLPAPTAPSG-CLSFWEAKAQLAKSCKVLVDALRHNAAAAVPFFGGGSVLRAAEPAPHASYGGIVSVETDL 79
Cdd:cd04236   66 MDMKLLVVMGLSAPDGTNMsDLELQAARSRLVKDCKTLVEALQANSAAAHPLFSGESVLQAEEPEPGASKGPSVSVDTEL 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833  80 LQWCLESGSIPILCPIGETAARRSVLLDSLEVTASLAKALRPTKIIFLNNTGGLRDSSHKVLSNVNLPADLDLVCNAEWV 159
Cdd:cd04236  146 LQWCLGSGHIPLVCPIGETSSGRSVSLDSSEVTTAIAKALQPIKVIFLNRSGGLRDQKHKVLPQVHLPADLPSLSDAEWL 225

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 767993833 160 STKERQQMRLIVDVLSRLPHHSSAVITAASTLLTELFSNKGSGTLF 205
Cdd:cd04236  226 SETEQNRIQDIATLLNALPSMSSAVITSAETLLTELFSHKGSGTLF 271
PRK04531 super family cl35266
acetylglutamate kinase; Provisional
 84-359 9.55e-87

acetylglutamate kinase; Provisional


The actual alignment was detected with superfamily member PRK04531:

Pssm-ID: 235306 [Multi-domain]  Cd Length: 398  Bit Score: 267.69  E-value: 9.55e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833  84 LESGSIPILCPIGETAARRSVLLDSLEVTASLAKALRPTKIIFLNNTGGLRDSSHKVLSNVNLPADLDLVCNAEWVSTKE 163
Cdd:PRK04531 126 LRAGSIPVIASLGETPSGQILNINADVAANELVSALQPYKIIFLTGTGGLLDADGKLISSINLSTEYDHLMQQPWINGGM 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833 164 RQQMRLIVDVLSRLPHHSSAVITAASTLLTELFSNKGSGTLFKNAERMLRVRSLDKLDQGRLVDLVNASFGKKLRDDYLA 243
Cdd:PRK04531 206 KLKLEQIKELLDRLPLESSVSITSPSDLAKELFTHKGSGTLVRRGERILRATDWDELDLERLNLLIESSFGRTLKPDYFD 285

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833 244 slRPRLHSIYVSEGYNAAAILTMEPvlgGTPYLDKFVVSSSRQGQGSGQMLWECLRRDLQTLFWRSRVTNPINPWYFKHS 323
Cdd:PRK04531 286 --TTQLLRAYVSENYRAAAILTETG---GGPYLDKFAVLDDARGEGLGRAVWNVMREETPQLFWRSRHNNTINKFYYAES 360

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 767993833 324 DGSFSNKQWIFFWFGLADIRDSYELVNHAKGLPDSF 359
Cdd:PRK04531 361 DGCIKQEKWKVFWYGLDDFEQIPKCVAHCANRPPTL 396
 
Name Accession Description Interval E-value
AAK_NAGS-Urea cd04236
AAK_NAGS-Urea: N-acetylglutamate (NAG) kinase-like domain of the NAG Synthase (NAGS) of the ...
 1-205 1.92e-124

AAK_NAGS-Urea: N-acetylglutamate (NAG) kinase-like domain of the NAG Synthase (NAGS) of the urea cycle found in animals. Ureogenic NAGS is a mitochondrial enzyme catalyzing the formation of NAG from acetylcoenzyme A and L-glutamate; NAG is an essential allosteric activator of carbamylphosphate synthase I, the first and rate limiting enzyme of the urea cycle. Ureogenic NAGS activity is dependent on the concentration of glutamate (substrate) and arginine (activator). Domain architecture of ureogenic NAGS consists of an N-terminal NAG kinase-like (ArgB) domain (this CD) and a C-terminal DUF619 domain. Members of this CD belong to the protein superfamily, the Amino Acid Kinase Family (AAKF).


Pssm-ID: 239769 [Multi-domain]  Cd Length: 271  Bit Score: 359.16  E-value: 1.92e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833   1 MDMKPLVVLGLPAPTAPSG-CLSFWEAKAQLAKSCKVLVDALRHNAAAAVPFFGGGSVLRAAEPAPHASYGGIVSVETDL 79
Cdd:cd04236   66 MDMKLLVVMGLSAPDGTNMsDLELQAARSRLVKDCKTLVEALQANSAAAHPLFSGESVLQAEEPEPGASKGPSVSVDTEL 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833  80 LQWCLESGSIPILCPIGETAARRSVLLDSLEVTASLAKALRPTKIIFLNNTGGLRDSSHKVLSNVNLPADLDLVCNAEWV 159
Cdd:cd04236  146 LQWCLGSGHIPLVCPIGETSSGRSVSLDSSEVTTAIAKALQPIKVIFLNRSGGLRDQKHKVLPQVHLPADLPSLSDAEWL 225

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 767993833 160 STKERQQMRLIVDVLSRLPHHSSAVITAASTLLTELFSNKGSGTLF 205
Cdd:cd04236  226 SETEQNRIQDIATLLNALPSMSSAVITSAETLLTELFSHKGSGTLF 271
ARG2 COG5630
N-acetylglutamate synthase (arginine biosynthesis) [Amino acid transport and metabolism];
37-361 1.88e-92

N-acetylglutamate synthase (arginine biosynthesis) [Amino acid transport and metabolism];


Pssm-ID: 444357 [Multi-domain]  Cd Length: 437  Bit Score: 283.52  E-value: 1.88e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833  37 LVDALRHNAAAAVPFFGGgsvLRAAEPAPHASYG---GIVSVETDLLQWCLESGSIPILCPIGETAARRSVLLDSLEVTA 113
Cdd:COG5630  118 LVEALEAMGTRARPIPSG---VFEAEYLDRDTLGlvgEVTGVHLAPIEASLRAGSIPIIASLGETPSGQILNINADVAAR 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833 114 SLAKALRPTKIIFLNNTGGLRDSSHKVLSNVNLPADLDLVCNAEWVSTKERQQMRLIVDVLSRLPHHSSAVITAASTLLT 193
Cdd:COG5630  195 ELVHALQPYKIVFLTGTGGLLDEDGKIISSINLATDFDHLMAQPWVNGGMRLKLEEIKDLLDDLPLTSSVSITRPSELAK 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833 194 ELFSNKGSGTLFKNAERMLRVRSLDKLDQGRLVDLVNASFGKKLRDDYLASLRPrlHSIYVSEGYNAAAILTMEPvlgGT 273
Cdd:COG5630  275 ELFTHKGSGTLVRRGERVLRHDSWDGLDLPRLRDLIESSFGRKLVEGYFDKTKF--YRAYVSESYRAAAILTLED---GV 349

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833 274 PYLDKFVVSSSRQGQGSGQMLWECLRRDLQTLFWRSRVTNPINPWYFKHSDGSFSNKQWIFFWFGLADIRDSYELVNHAK 353
Cdd:COG5630  350 PYLDKFAVLDDAQGEGLGRAVWQRMREENPQLFWRSRHDNPVNGFYFAEADGCYKQEKWTVFWYGLDGFDEIQACVEHAL 429


                 ....*...
gi 767993833 354 GLPDSFHK 361
Cdd:COG5630  430 ARPPTLKD 437
PRK04531 PRK04531
acetylglutamate kinase; Provisional
 84-359 9.55e-87

acetylglutamate kinase; Provisional


Pssm-ID: 235306 [Multi-domain]  Cd Length: 398  Bit Score: 267.69  E-value: 9.55e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833  84 LESGSIPILCPIGETAARRSVLLDSLEVTASLAKALRPTKIIFLNNTGGLRDSSHKVLSNVNLPADLDLVCNAEWVSTKE 163
Cdd:PRK04531 126 LRAGSIPVIASLGETPSGQILNINADVAANELVSALQPYKIIFLTGTGGLLDADGKLISSINLSTEYDHLMQQPWINGGM 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833 164 RQQMRLIVDVLSRLPHHSSAVITAASTLLTELFSNKGSGTLFKNAERMLRVRSLDKLDQGRLVDLVNASFGKKLRDDYLA 243
Cdd:PRK04531 206 KLKLEQIKELLDRLPLESSVSITSPSDLAKELFTHKGSGTLVRRGERILRATDWDELDLERLNLLIESSFGRTLKPDYFD 285

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833 244 slRPRLHSIYVSEGYNAAAILTMEPvlgGTPYLDKFVVSSSRQGQGSGQMLWECLRRDLQTLFWRSRVTNPINPWYFKHS 323
Cdd:PRK04531 286 --TTQLLRAYVSENYRAAAILTETG---GGPYLDKFAVLDDARGEGLGRAVWNVMREETPQLFWRSRHNNTINKFYYAES 360

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 767993833 324 DGSFSNKQWIFFWFGLADIRDSYELVNHAKGLPDSF 359
Cdd:PRK04531 361 DGCIKQEKWKVFWYGLDDFEQIPKCVAHCANRPPTL 396
NAT pfam04768
NAT, N-acetyltransferase, of N-acetylglutamate synthase; This is the C-terminal NAT or ...
 191-354 2.71e-65

NAT, N-acetyltransferase, of N-acetylglutamate synthase; This is the C-terminal NAT or N-acetyltransferase domain of bifunctional N-acetylglutamate synthase/kinases. It catalyzes the first two steps in arginine biosynthesis. This domain contains the putative NAGS - N-acetylglutamate synthase - active site. It is found at the C-terminus of Neurospora crassa acetylglutamate synthase - amino-acid acetyltransferase, EC: 2.3.1.1. It is also found C-terminal to the amino acid kinase region (pfam00696) in some fungal acetylglutamate kinase enzymes. it stabilizes the yeast NAGK, N-acetyl-L-glutamate kinase, slows catalysis and modulates feed-back inhibition by arginine. This domain is found to be the N-acetyltransferase (NAT) domain, and it has a typical GCN5-related NAT fold and a site that catalyzes NAG synthesis which is located >25 Angstrom away from the L-arginine binding site in the N-temrinal domain pfam00696.


Pssm-ID: 398437  Cd Length: 166  Bit Score: 204.41  E-value: 2.71e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833  191 LLTELFSNKGSGTLFKNAERMLRVRSLDKL-DQGRLVDLVNASF-GKKLRDDYLASLRPRLHSIYVSEGYNAAAILTMEp 268
Cdd:pfam04768   2 LQKELFTDSGAGTLIRRGYKVLRRTSLEELiDIERLRNLIERSFdGRLSVADYLDRLKGRLFKIYVDEPYEALAIVTKE- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833  269 vLGGTPYLDKFVVSSSRQGQGSGQMLWECLRRDLQTLFWRSRVTNPINPWYFKHSDGSFSNKQWIFFWFGLADIRDSYEL 348
Cdd:pfam04768  81 -DGGVPYLDKFAVSKSGWGNGVSDNVFNAIKKDFPKLVWRSREDNPNNKWYFERSDGSLLKNGWVLFWYGIKDLNEVSEL 159


                  ....*.
gi 767993833  349 VNHAKG 354
Cdd:pfam04768 160 VASFRD 165
DUF619-NAGS-U cd04265
DUF619 domain of various N-acetylglutamate Synthases (NAGS) of the urea (U) cycle of humans ...
 239-338 1.13e-59

DUF619 domain of various N-acetylglutamate Synthases (NAGS) of the urea (U) cycle of humans and fish; This family includes the DUF619 domain of various N-acetylglutamate synthases (NAGS) of the urea cycle found in humans and fish, the DUF619 domain of the NAGS of the fungal arginine-biosynthetic pathway (FABP), as well as the DUF619 domain present in C-terminal of a NAG kinase-like domain in a limited number of predicted NAGSs found in bacteria and Dictyostelium. Ureogenic NAGS is a mitochondrial enzyme catalyzing the formation of NAG from acetylcoenzyme A and L-glutamate. NAGS is an essential allosteric activator of carbamylphosphate synthase I, the first and rate limiting enzyme of the urea cycle. Domain architecture of ureogenic and fungal NAGS consists of an N-terminal NAG kinase-like domain and a C-terminal DUF619 domain. The DUF619 domain function has yet to be characterized.


Pssm-ID: 176267  Cd Length: 99  Bit Score: 187.58  E-value: 1.13e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833 239 DDYLASLRPRLHSIYVSEGYNAAAILTMEPVlGGTPYLDKFVVSSSRQGQGSGQMLWECLRRDLQTLFWRSRVTNPINPW 318
Cdd:cd04265    1 PDYFDSLQGRLHTIYLSEGYNAAAIVTNEEV-DGVPYLDKFAVSSSAQGEGTGEALWRRLRRDFPKLFWRSRSTNPINPW 79

                         90       100
                 ....*....|....*....|
gi 767993833 319 YFKHSDGSFSNKQWIFFWFG 338
Cdd:cd04265   80 YFKRCDGSFKNGHWTVFWYG 99
PRK05279 PRK05279
N-acetylglutamate synthase; Validated
 69-204 1.12e-05

N-acetylglutamate synthase; Validated


Pssm-ID: 235386 [Multi-domain]  Cd Length: 441  Bit Score: 47.07  E-value: 1.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833  69 YGGIV-SVETDLLQWCLESGSIPILCPIGETAARRSVLLDSLEVTASLAKALRPTKIIFLNNTGGLRDSSHKVLSNVnLP 147
Cdd:PRK05279 149 HTGEVrRIDAEAIRRQLDSGAIVLLSPLGYSPTGESFNLTMEEVATQVAIALKADKLIFFTESQGVLDEDGELIREL-SP 227

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767993833 148 ADLDlvcnaEWVSTKERQQmrLIVDVLSRLPHHSSAV---------ITAAS--TLLTELFSNKGSGTL 204
Cdd:PRK05279 228 NEAQ-----ALLEALEDGD--YNSGTARFLRAAVKACrggvrrshlISYAEdgALLQELFTRDGIGTM 288
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
 23-136 6.77e-04

Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino acid substrates, as well as uridylate kinase and carbamate kinase. This family includes: Aspartokinase EC:2.7.2.4. Acetylglutamate kinase EC:2.7.2.8. Glutamate 5-kinase EC:2.7.2.11. Uridylate kinase EC:2.7.4.-. Carbamate kinase EC:2.7.2.2.


Pssm-ID: 395565 [Multi-domain]  Cd Length: 232  Bit Score: 40.81  E-value: 6.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833   23 FWEAKAQLAKSCKVLVDALRHNAAAAVPFFGGGSVLRAAEPAPHAsyggIVSVETDLLQWCLESGSIPILCP-IGETAAR 101
Cdd:pfam00696  68 EVATMDALGSLGERLNAALLAAGLPAVGLPAAQLLATEAGFIDDV----VTRIDTEALEELLEAGVVPVITGfIGIDPEG 143

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 767993833  102 RSVLLDSLEVTASLAKALRPTKIIFLNNTGGLRDS 136
Cdd:pfam00696 144 ELGRGSSDTLAALLAEALGADKLIILTDVDGVYTA 178
 
Name Accession Description Interval E-value
AAK_NAGS-Urea cd04236
AAK_NAGS-Urea: N-acetylglutamate (NAG) kinase-like domain of the NAG Synthase (NAGS) of the ...
 1-205 1.92e-124

AAK_NAGS-Urea: N-acetylglutamate (NAG) kinase-like domain of the NAG Synthase (NAGS) of the urea cycle found in animals. Ureogenic NAGS is a mitochondrial enzyme catalyzing the formation of NAG from acetylcoenzyme A and L-glutamate; NAG is an essential allosteric activator of carbamylphosphate synthase I, the first and rate limiting enzyme of the urea cycle. Ureogenic NAGS activity is dependent on the concentration of glutamate (substrate) and arginine (activator). Domain architecture of ureogenic NAGS consists of an N-terminal NAG kinase-like (ArgB) domain (this CD) and a C-terminal DUF619 domain. Members of this CD belong to the protein superfamily, the Amino Acid Kinase Family (AAKF).


Pssm-ID: 239769 [Multi-domain]  Cd Length: 271  Bit Score: 359.16  E-value: 1.92e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833   1 MDMKPLVVLGLPAPTAPSG-CLSFWEAKAQLAKSCKVLVDALRHNAAAAVPFFGGGSVLRAAEPAPHASYGGIVSVETDL 79
Cdd:cd04236   66 MDMKLLVVMGLSAPDGTNMsDLELQAARSRLVKDCKTLVEALQANSAAAHPLFSGESVLQAEEPEPGASKGPSVSVDTEL 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833  80 LQWCLESGSIPILCPIGETAARRSVLLDSLEVTASLAKALRPTKIIFLNNTGGLRDSSHKVLSNVNLPADLDLVCNAEWV 159
Cdd:cd04236  146 LQWCLGSGHIPLVCPIGETSSGRSVSLDSSEVTTAIAKALQPIKVIFLNRSGGLRDQKHKVLPQVHLPADLPSLSDAEWL 225

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 767993833 160 STKERQQMRLIVDVLSRLPHHSSAVITAASTLLTELFSNKGSGTLF 205
Cdd:cd04236  226 SETEQNRIQDIATLLNALPSMSSAVITSAETLLTELFSHKGSGTLF 271
ARG2 COG5630
N-acetylglutamate synthase (arginine biosynthesis) [Amino acid transport and metabolism];
37-361 1.88e-92

N-acetylglutamate synthase (arginine biosynthesis) [Amino acid transport and metabolism];


Pssm-ID: 444357 [Multi-domain]  Cd Length: 437  Bit Score: 283.52  E-value: 1.88e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833  37 LVDALRHNAAAAVPFFGGgsvLRAAEPAPHASYG---GIVSVETDLLQWCLESGSIPILCPIGETAARRSVLLDSLEVTA 113
Cdd:COG5630  118 LVEALEAMGTRARPIPSG---VFEAEYLDRDTLGlvgEVTGVHLAPIEASLRAGSIPIIASLGETPSGQILNINADVAAR 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833 114 SLAKALRPTKIIFLNNTGGLRDSSHKVLSNVNLPADLDLVCNAEWVSTKERQQMRLIVDVLSRLPHHSSAVITAASTLLT 193
Cdd:COG5630  195 ELVHALQPYKIVFLTGTGGLLDEDGKIISSINLATDFDHLMAQPWVNGGMRLKLEEIKDLLDDLPLTSSVSITRPSELAK 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833 194 ELFSNKGSGTLFKNAERMLRVRSLDKLDQGRLVDLVNASFGKKLRDDYLASLRPrlHSIYVSEGYNAAAILTMEPvlgGT 273
Cdd:COG5630  275 ELFTHKGSGTLVRRGERVLRHDSWDGLDLPRLRDLIESSFGRKLVEGYFDKTKF--YRAYVSESYRAAAILTLED---GV 349

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833 274 PYLDKFVVSSSRQGQGSGQMLWECLRRDLQTLFWRSRVTNPINPWYFKHSDGSFSNKQWIFFWFGLADIRDSYELVNHAK 353
Cdd:COG5630  350 PYLDKFAVLDDAQGEGLGRAVWQRMREENPQLFWRSRHDNPVNGFYFAEADGCYKQEKWTVFWYGLDGFDEIQACVEHAL 429


                 ....*...
gi 767993833 354 GLPDSFHK 361
Cdd:COG5630  430 ARPPTLKD 437
PRK04531 PRK04531
acetylglutamate kinase; Provisional
 84-359 9.55e-87

acetylglutamate kinase; Provisional


Pssm-ID: 235306 [Multi-domain]  Cd Length: 398  Bit Score: 267.69  E-value: 9.55e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833  84 LESGSIPILCPIGETAARRSVLLDSLEVTASLAKALRPTKIIFLNNTGGLRDSSHKVLSNVNLPADLDLVCNAEWVSTKE 163
Cdd:PRK04531 126 LRAGSIPVIASLGETPSGQILNINADVAANELVSALQPYKIIFLTGTGGLLDADGKLISSINLSTEYDHLMQQPWINGGM 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833 164 RQQMRLIVDVLSRLPHHSSAVITAASTLLTELFSNKGSGTLFKNAERMLRVRSLDKLDQGRLVDLVNASFGKKLRDDYLA 243
Cdd:PRK04531 206 KLKLEQIKELLDRLPLESSVSITSPSDLAKELFTHKGSGTLVRRGERILRATDWDELDLERLNLLIESSFGRTLKPDYFD 285

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833 244 slRPRLHSIYVSEGYNAAAILTMEPvlgGTPYLDKFVVSSSRQGQGSGQMLWECLRRDLQTLFWRSRVTNPINPWYFKHS 323
Cdd:PRK04531 286 --TTQLLRAYVSENYRAAAILTETG---GGPYLDKFAVLDDARGEGLGRAVWNVMREETPQLFWRSRHNNTINKFYYAES 360

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 767993833 324 DGSFSNKQWIFFWFGLADIRDSYELVNHAKGLPDSF 359
Cdd:PRK04531 361 DGCIKQEKWKVFWYGLDDFEQIPKCVAHCANRPPTL 396
NAT pfam04768
NAT, N-acetyltransferase, of N-acetylglutamate synthase; This is the C-terminal NAT or ...
 191-354 2.71e-65

NAT, N-acetyltransferase, of N-acetylglutamate synthase; This is the C-terminal NAT or N-acetyltransferase domain of bifunctional N-acetylglutamate synthase/kinases. It catalyzes the first two steps in arginine biosynthesis. This domain contains the putative NAGS - N-acetylglutamate synthase - active site. It is found at the C-terminus of Neurospora crassa acetylglutamate synthase - amino-acid acetyltransferase, EC: 2.3.1.1. It is also found C-terminal to the amino acid kinase region (pfam00696) in some fungal acetylglutamate kinase enzymes. it stabilizes the yeast NAGK, N-acetyl-L-glutamate kinase, slows catalysis and modulates feed-back inhibition by arginine. This domain is found to be the N-acetyltransferase (NAT) domain, and it has a typical GCN5-related NAT fold and a site that catalyzes NAG synthesis which is located >25 Angstrom away from the L-arginine binding site in the N-temrinal domain pfam00696.


Pssm-ID: 398437  Cd Length: 166  Bit Score: 204.41  E-value: 2.71e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833  191 LLTELFSNKGSGTLFKNAERMLRVRSLDKL-DQGRLVDLVNASF-GKKLRDDYLASLRPRLHSIYVSEGYNAAAILTMEp 268
Cdd:pfam04768   2 LQKELFTDSGAGTLIRRGYKVLRRTSLEELiDIERLRNLIERSFdGRLSVADYLDRLKGRLFKIYVDEPYEALAIVTKE- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833  269 vLGGTPYLDKFVVSSSRQGQGSGQMLWECLRRDLQTLFWRSRVTNPINPWYFKHSDGSFSNKQWIFFWFGLADIRDSYEL 348
Cdd:pfam04768  81 -DGGVPYLDKFAVSKSGWGNGVSDNVFNAIKKDFPKLVWRSREDNPNNKWYFERSDGSLLKNGWVLFWYGIKDLNEVSEL 159


                  ....*.
gi 767993833  349 VNHAKG 354
Cdd:pfam04768 160 VASFRD 165
DUF619-NAGS-U cd04265
DUF619 domain of various N-acetylglutamate Synthases (NAGS) of the urea (U) cycle of humans ...
 239-338 1.13e-59

DUF619 domain of various N-acetylglutamate Synthases (NAGS) of the urea (U) cycle of humans and fish; This family includes the DUF619 domain of various N-acetylglutamate synthases (NAGS) of the urea cycle found in humans and fish, the DUF619 domain of the NAGS of the fungal arginine-biosynthetic pathway (FABP), as well as the DUF619 domain present in C-terminal of a NAG kinase-like domain in a limited number of predicted NAGSs found in bacteria and Dictyostelium. Ureogenic NAGS is a mitochondrial enzyme catalyzing the formation of NAG from acetylcoenzyme A and L-glutamate. NAGS is an essential allosteric activator of carbamylphosphate synthase I, the first and rate limiting enzyme of the urea cycle. Domain architecture of ureogenic and fungal NAGS consists of an N-terminal NAG kinase-like domain and a C-terminal DUF619 domain. The DUF619 domain function has yet to be characterized.


Pssm-ID: 176267  Cd Length: 99  Bit Score: 187.58  E-value: 1.13e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833 239 DDYLASLRPRLHSIYVSEGYNAAAILTMEPVlGGTPYLDKFVVSSSRQGQGSGQMLWECLRRDLQTLFWRSRVTNPINPW 318
Cdd:cd04265    1 PDYFDSLQGRLHTIYLSEGYNAAAIVTNEEV-DGVPYLDKFAVSSSAQGEGTGEALWRRLRRDFPKLFWRSRSTNPINPW 79

                         90       100
                 ....*....|....*....|
gi 767993833 319 YFKHSDGSFSNKQWIFFWFG 338
Cdd:cd04265   80 YFKRCDGSFKNGHWTVFWYG 99
DUF619-NAGS cd04264
DUF619 domain of various N-acetylglutamate Synthases of the fungal arginine-biosynthetic ...
 239-338 2.95e-59

DUF619 domain of various N-acetylglutamate Synthases of the fungal arginine-biosynthetic pathway and urea cycle found in humans and fish; DUF619-NAGS: This family includes the DUF619 domain of various N-acetylglutamate synthases (NAGS) of the urea cycle found in humans and fish, the DUF619 domain of the NAGS of the fungal arginine-biosynthetic pathway (FABP), as well as the DUF619 domain present in C-terminal of a NAG kinase-like domain in a limited number of predicted NAGSs found in bacteria and Dictyostelium. Ureogenic NAGS is a mitochondrial enzyme catalyzing the formation of NAG from acetylcoenzyme A and L-glutamate. NAGS is an essential allosteric activator of carbamylphosphate synthase I, the first and rate limiting enzyme of the urea cycle. Domain architecture of ureogenic and fungal NAGS consists of an N-terminal NAG kinase-like domain and a C-terminal DUF619 domain. The DUF619 domain function has yet to be characterized.


Pssm-ID: 176266  Cd Length: 99  Bit Score: 186.80  E-value: 2.95e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833 239 DDYLASLrPRLHSIYVSEGYNAAAILTMEPVLGGTPYLDKFVVSSSRQGQGSGQMLWECLRRDLQTLFWRSRVTNPINPW 318
Cdd:cd04264    1 PDYIDRL-QRLHAIYLSEGYNAAAIVTYEGVNNGVPYLDKFAVSSSAQGEGTSDALWRRLRRDFPKLFWRSRKTNPINPW 79

                         90       100
                 ....*....|....*....|
gi 767993833 319 YFKHSDGSFSNKQWIFFWFG 338
Cdd:cd04264   80 YFKRSDGSFKNGQWKVFWYG 99
AAK_NAGK-fArgBP cd04252
AAK_NAGK-fArgBP: N-Acetyl-L-glutamate kinase (NAGK) of the fungal arginine-biosynthetic ...
 37-204 5.98e-30

AAK_NAGK-fArgBP: N-Acetyl-L-glutamate kinase (NAGK) of the fungal arginine-biosynthetic pathway (fArgBP). The nuclear-encoded, mitochondrial polyprotein precursor with an N-terminal NAGK (ArgB) domain (this CD), a central DUF619 domain, and a C-terminal reductase domain (ArgC, N-Acetylglutamate Phosphate Reductase, NAGPR). The precursor is cleaved in the mitochondria into two distinct enzymes (NAGK-DUF619 and NAGPR). Native molecular weights of these proteins indicate that the kinase is an octamer whereas the reductase is a dimer. This CD also includes some gamma-proteobacteria (Xanthomonas and Xylella) NAG kinases with an N-terminal NAGK (ArgB) domain (this CD) and a C-terminal DUF619 domain. The DUF619 domain is described as a putative distant homolog of the acetyltransferase, ArgA, predicted to function in NAG synthase association in fungi. Eukaryotic sequences have an N-terminal mitochondrial transit peptide. Members of this NAG kinase domain CD belong to the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239785 [Multi-domain]  Cd Length: 248  Bit Score: 115.17  E-value: 5.98e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833  37 LVDALRHNAAAAVPFFGGgsvLRAAEPAPHASY---GGIVSVETDLLQWCLESGSIPILCPIGETAARRSVLLDSLEVTA 113
Cdd:cd04252   80 LVEALERNGARARPITSG---VFEAEYLDKDKYglvGKITGVNKAPIEAAIRAGYLPILTSLAETPSGQLLNVNADVAAG 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833 114 SLAKALRPTKIIFLNNTGGLRDSSHKVLSNVNLPADLDLVCNAEWVSTKERQQMRLIVDVLSRLPHHSSAVITAASTLLT 193
Cdd:cd04252  157 ELARVLEPLKIVFLNETGGLLDGTGKKISAINLDEEYDDLMKQPWVKYGTKLKIKEIKELLDTLPRSSSVSITSPDDLQK 236

                        170
                 ....*....|.
gi 767993833 194 ELFSNKGSGTL 204
Cdd:cd04252  237 ELFTHSGAGTL 247
AAK cd02115
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ...
 1-205 3.24e-24

Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like N-acetylglutamate kinase (NAGK), carbamate kinase (CK), aspartokinase (AK), glutamate-5-kinase (G5K) and UMP kinase (UMPK). The AAK superfamily includes kinases that phosphorylate a variety of amino acid substrates. These kinases catalyze the formation of phosphoric anhydrides, generally with a carboxylate, and use ATP as the source of the phosphoryl group; are involved in amino acid biosynthesis. Some of these kinases control the process via allosteric feed-back inhibition.


Pssm-ID: 239033 [Multi-domain]  Cd Length: 248  Bit Score: 99.82  E-value: 3.24e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833   1 MDMKPLVVLGLPAPTAPSGC-------------LSFWEAKAQLAKSCKVLVDALRHNAAAavpfFGGGSVLRAAEPAPHA 67
Cdd:cd02115   28 EGGRVVVVHGAGPQITDELLahgellgyarglrITDRETDALAAMGEGMSNLLIAAALEQ----HGIKAVPLDLTQAGFA 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833  68 S-----YGGIVSVETDLLQWCLESGSIPILCPIGETAA--RRSVLLDSLEVTAS-LAKALRPTKIIFLNNTGGLRDS--- 136
Cdd:cd02115  104 SpnqghVGKITKVSTDRLKSLLENGILPILSGFGGTDEkeTGTLGRGGSDSTAAlLAAALKADRLVILTDVDGVYTAdpr 183

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767993833 137 ---SHKVLSNVNlPADLDLVCNAEWvstkeRQQMRLIVDVLSRlpHHSSAVITAASTLLT-ELFSNKGSGTLF 205
Cdd:cd02115  184 kvpDAKLLSELT-YEEAAELAYAGA-----MVLKPKAADPAAR--AGIPVRIANTENPGAlALFTPDGGGTLI 248
DUF619-NAGS-FABP cd04266
DUF619 domain of N-acetylglutamate Synthase of the fungal arginine-biosynthetic pathway; ...
 239-338 2.54e-20

DUF619 domain of N-acetylglutamate Synthase of the fungal arginine-biosynthetic pathway; DUF619-NAGS-FABP: This family includes the DUF619 domain of N-acetylglutamate synthase (NAGS) of the fungal arginine-biosynthetic pathway (FABP). This NAGS (also known as arginine-requiring protein 2 or ARG2) consists of an N-terminal NAG kinase-like domain and a C-terminal DUF619 domain. NAGS catalyzes the formation of NAG from acetylcoenzyme A and L-glutamate. The DUF619 domain, yet to be characterized, is predicted to function in NAGS association in fungi.


Pssm-ID: 176268  Cd Length: 108  Bit Score: 84.82  E-value: 2.54e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833 239 DDYLASLRPRLHSIYVSEGYNAAAILTMEPVLGGTP----YLDKFVVSSSRQGQ-GSGQMLWECLRRDL-QTLFWRSRVT 312
Cdd:cd04266    1 EKYLDRLKNSLATVIIAGDYEGAAILTWEGPDGSTPekiaYLDKFAVLPKAQGSdGIADILFNAMLDGFpNELIWRSRKD 80

                         90       100
                 ....*....|....*....|....*...
gi 767993833 313 NPINPWYFKHSDGSFSNK--QWIFFWFG 338
Cdd:cd04266   81 NPVNKWYFERSVGVLKLSgsQWKLFWTG 108
DUF619-like cd03173
DUF619 domain of various N-acetylglutamate Kinases and N-acetylglutamate Synthases; ...
 240-338 3.59e-16

DUF619 domain of various N-acetylglutamate Kinases and N-acetylglutamate Synthases; DUF619-like: This family includes the DUF619 domain of various N-acetylglutamate synthases (NAGS) of the urea cycle found in humans and fish, the DUF619 domain of the NAGS of the fungal arginine-biosynthetic pathway (FABP), as well as the DUF619 domain present C-terminal of a NAG kinase-like domain in a limited number of predicted NAGSs found in bacteria and Dictyostelium. Ureogenic NAGS is a mitochondrial enzyme catalyzing the formation of NAG from acetylcoenzyme A and L-glutamate. NAGS is an essential allosteric activator of carbamylphosphate synthase I, the first and rate limiting enzyme of the urea cycle. Domain architecture of ureogenic and fungal NAGS consists of an N-terminal NAG kinase-like domain and a C-terminal DUF619 domain. This subgroup also includes the DUF619 domain of the FABP N-acetylglutamate kinase (NAGK), the enzyme that catalyzes the second reaction of arginine biosynthesis; the phosphorylation of the gamma-carboxyl group of NAG to produce N-acetylglutamylphosphate (NAGP) which is subsequently converted to ornithine in two more steps. The nuclear-encoded, mitochondrial polyprotein precursor (ARG5,6) consists of an N-terminal NAGK (ArgB) domain, a central DUF619 domain, and a C-terminal reductase domain (ArgC, N-acetylglutamate phosphate reductase). The DUF619 domain function has yet to be characterized.


Pssm-ID: 176264  Cd Length: 98  Bit Score: 73.29  E-value: 3.59e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833 240 DYLASLRPRLHSIYVSEGYNAAAILTMEPvlGGTPYLDKFVVSSSRQGQGSGQMLWECLRRDLQTLFWRSRVTNPINPWY 319
Cdd:cd03173    2 SYLKRLKNGKFASYADEPLEGVAIVTYEG--NSIPYLDKFAVSDHLWLNNVTDNIFNLIRKDFPSLLWRVRENDANLKWY 79

                         90
                 ....*....|....*....
gi 767993833 320 FKHSDGSFSNKQWIFFWFG 338
Cdd:cd03173   80 FSKSVGSLDKNGFILFWYG 98
DUF619-NAGK-FABP cd04263
DUF619 domain of N-acetylglutamate kinase (NAGK) of the fungal arginine-biosynthetic pathway; ...
 239-338 3.43e-11

DUF619 domain of N-acetylglutamate kinase (NAGK) of the fungal arginine-biosynthetic pathway; DUF619-NAGK-FABP: DUF619 domain of N-acetylglutamate kinase (NAGK) of the fungal arginine-biosynthetic pathway (FABP). The nuclear-encoded, mitochondrial polyprotein precursor (ARG5,6) consists of an N-terminal NAGK (ArgB) domain, a central DUF619 domain, and a C-terminal reductase domain (ArgC, N-Acetylglutamate Phosphate Reductase, NAGPR). The precursor is cleaved into two distinct enzymes (NAGK-DUF619 and NAGPR) in the mitochondria. Native molecular weights of these proteins indicate that the kinase is an octamer whereas the reductase is a dimer. Arg5,6 catalyzes the second reaction of arginine biosynthesis; the phosphorylation of the gamma-carboxyl group of NAG to produce N-acetylglutamylphosphate (NAGP) which is subsequently converted to ornithine in two more steps. It also binds and regulates the promoters of nuclear and mitochondrial genes, and may possibly regulate precursor mRNA metabolism. The DUF619 domain function has yet to be characterized.


Pssm-ID: 176265  Cd Length: 98  Bit Score: 59.26  E-value: 3.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833 239 DDYLASLRPRLHSIYVSEGYNAAAILTmePVLGGTPYLDKFVVSSSRQGQGSGQMLWECLRRDLQTLFWRSRVTNPINPW 318
Cdd:cd04263    1 ASYFDELKERPFKAYGDEPMEVLAIVL--PPSGEVATLATFTITKSGWLNNVADNIFTAIKKDHPKLVWTVREDDENLKW 78

                         90       100
                 ....*....|....*....|
gi 767993833 319 YFKHSDGSFSNKQWIFFWFG 338
Cdd:cd04263   79 HFEKADGSFTRNGKVLFWYG 98
ArgB COG0548
N-acetylglutamate kinase [Amino acid transport and metabolism]; N-acetylglutamate kinase is ...
 70-205 6.47e-11

N-acetylglutamate kinase [Amino acid transport and metabolism]; N-acetylglutamate kinase is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440314 [Multi-domain]  Cd Length: 283  Bit Score: 62.36  E-value: 6.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833  70 GGIVSVETDLLQWCLESGSIPILCPIGETAARRSVLLDSLEVTASLAKALRPTKIIFLNNTGGLRDSSHKVLSNVNlPAD 149
Cdd:COG0548  147 GEVRRVDPELIRALLDAGYIPVISPIGYSPTGEVYNINADTVAGAIAAALKAEKLILLTDVPGVLDDPGSLISELT-AAE 225

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767993833 150 LDLVCNAEWVSTKERQQMRLIVDVLS-----------RLPHhssavitaasTLLTELFSNKGSGTLF 205
Cdd:COG0548  226 AEELIADGVISGGMIPKLEAALDAVRggvkrvhiidgRVPH----------ALLLELFTDDGIGTMI 282
AAK_NAGK-like cd04238
AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the ...
 35-205 1.43e-08

AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the Escherichia coli and Pseudomonas aeruginosa type NAGKs which catalyze the phosphorylation of N-acetyl-L-glutamate (NAG) by ATP in the second step of arginine biosynthesis found in bacteria and photosynthetic organisms using either the acetylated, noncyclic (NC), or non-acetylated, cyclic (C) route of ornithine biosynthesis. Also included in this CD is a distinct group of uncharacterized (UC) bacterial and archeal NAGKs. Members of this CD belong to the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239771 [Multi-domain]  Cd Length: 256  Bit Score: 55.21  E-value: 1.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833  35 KVLVDALRHNAAAAVPFFGGGSVLRAAEPAPHASY-----GGIVSVETDLLQWCLESGSIPILCPIGETAARRSVLLDSL 109
Cdd:cd04238   81 KELVSLLNRAGGKAVGLSGKDGGLIKAEKKEEKDIdlgfvGEVTEVNPELLETLLEAGYIPVIAPIAVDEDGETYNVNAD 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833 110 EVTASLAKALRPTKIIFLNNTGGLRDSSHKVLSNVNlPADLDLVCNAEWVSTKERQQMRLIVDVLSRLPhhSSAVI---T 186
Cdd:cd04238  161 TAAGAIAAALKAEKLILLTDVPGVLDDPGSLISELT-PKEAEELIEDGVISGGMIPKVEAALEALEGGV--RKVHIidgR 237

                        170
                 ....*....|....*....
gi 767993833 187 AASTLLTELFSNKGSGTLF 205
Cdd:cd04238  238 VPHSLLLELFTDEGIGTMI 256
AAK_NAGK-C cd04250
AAK_NAGK-C: N-Acetyl-L-glutamate kinase - cyclic (NAGK-C) catalyzes the phosphorylation of the ...
 70-205 1.09e-06

AAK_NAGK-C: N-Acetyl-L-glutamate kinase - cyclic (NAGK-C) catalyzes the phosphorylation of the gamma-COOH group of N-acetyl-L-glutamate (NAG) by ATP in the second step of arginine biosynthesis found in some bacteria and photosynthetic organisms using the non-acetylated, cyclic route of ornithine biosynthesis. In this pathway, glutamate is first N-acetylated and then phosphorylated by NAGK to give phosphoryl NAG, which is converted to NAG-ornithine. There are two variants of this pathway. In one, typified by the pathway in Thermotoga maritima and Pseudomonas aeruginosa, the acetyl group is recycled by reversible transacetylation from acetylornithine to glutamate. The phosphorylation of NAG by NAGK is feedback inhibited by arginine. In photosynthetic organisms, NAGK is the target of the nitrogen-signaling protein PII. Hexameric formation of NAGK domains appears to be essential to both arginine inhibition and NAGK-PII complex formation. NAGK-C are members of the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239783 [Multi-domain]  Cd Length: 279  Bit Score: 49.43  E-value: 1.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833  70 GGIVSVETDLLQWCLESGSIPILCPIGETAARRSVLLDSLEVTASLAKALRPTKIIFLNNTGGLRDS---SHKVLSNVNl 146
Cdd:cd04250  141 GEVTEVNPELLETLLEAGYIPVIAPVGVGEDGETYNINADTAAGAIAAALKAEKLILLTDVAGVLDDpndPGSLISEIS- 219

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833 147 PADLDLVCNAEWVSTKERQQMRLIVDVLS-----------RLPHhssavitaasTLLTELFSNKGSGTLF 205
Cdd:cd04250  220 LKEAEELIADGIISGGMIPKVEACIEALEggvkaahiidgRVPH----------SLLLEIFTDEGIGTMI 279
AAK_NAGS-ABP cd04237
AAK_NAGS-ABP: N-acetylglutamate (NAG) kinase-like domain of the NAG Synthase (NAGS) of the ...
 69-204 5.39e-06

AAK_NAGS-ABP: N-acetylglutamate (NAG) kinase-like domain of the NAG Synthase (NAGS) of the arginine-biosynthesis pathway (ABP) found in gamma- and beta-proteobacteria and higher plant chloroplasts. Domain architecture of these NAGS consisted of an N-terminal NAG kinase-like (ArgB) domain (this CD) and a C-terminal NAG synthase, acetyltransferase (ArgA) domain. Both bacterial and plant sequences in this CD have a conserved N-terminal extension; a similar sequence in the NAG kinases of the cyclic arginine-biosynthesis pathway has been implicated in feedback inhibition sensing. Plant sequences also have an N-terminal chloroplast transit peptide and an insert (approx. 70 residues) in the C-terminal region of ArgB. Members of this CD belong to the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239770 [Multi-domain]  Cd Length: 280  Bit Score: 47.55  E-value: 5.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833  69 YGGIV-SVETDLLQWCLESGSIPILCPIGETAARRSVLLDSLEVTASLAKALRPTKIIFLNNTGGLRDSSHKVLSNVNLP 147
Cdd:cd04237  142 HTGEVrRIDADAIRRQLDQGSIVLLSPLGYSPTGEVFNLSMEDVATAVAIALKADKLIFLTDGPGLLDDDGELIRELTAQ 221

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767993833 148 ADLDLVCNAEWVSTKERQQMRLIVDVLSR-------LPHHSSavitaaSTLLTELFSNKGSGTL 204
Cdd:cd04237  222 EAEALLETGALLTNDTARLLQAAIEACRGgvprvhlISYAED------GALLLELFTRDGVGTL 279
PRK05279 PRK05279
N-acetylglutamate synthase; Validated
 69-204 1.12e-05

N-acetylglutamate synthase; Validated


Pssm-ID: 235386 [Multi-domain]  Cd Length: 441  Bit Score: 47.07  E-value: 1.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833  69 YGGIV-SVETDLLQWCLESGSIPILCPIGETAARRSVLLDSLEVTASLAKALRPTKIIFLNNTGGLRDSSHKVLSNVnLP 147
Cdd:PRK05279 149 HTGEVrRIDAEAIRRQLDSGAIVLLSPLGYSPTGESFNLTMEEVATQVAIALKADKLIFFTESQGVLDEDGELIREL-SP 227

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767993833 148 ADLDlvcnaEWVSTKERQQmrLIVDVLSRLPHHSSAV---------ITAAS--TLLTELFSNKGSGTL 204
Cdd:PRK05279 228 NEAQ-----ALLEALEDGD--YNSGTARFLRAAVKACrggvrrshlISYAEdgALLQELFTRDGIGTM 288
PRK00942 PRK00942
acetylglutamate kinase; Provisional
 70-207 2.19e-05

acetylglutamate kinase; Provisional


Pssm-ID: 234869 [Multi-domain]  Cd Length: 283  Bit Score: 45.48  E-value: 2.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833  70 GGIVSVETDLLQWCLESGSIPILCPIG------------ETAArrsvlldslevtASLAKALRPTKIIFLNNTGGLRDSS 137
Cdd:PRK00942 145 GEVTPVNPALLEALLEAGYIPVISPIGvgedgetyninaDTAA------------GAIAAALGAEKLILLTDVPGVLDDK 212

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833 138 HKVLSNVNlPADLD---------------LVCNAEWVSTKERQqmrliVDVLS-RLPHhssavitaasTLLTELFSNKGS 201
Cdd:PRK00942 213 GQLISELT-ASEAEeliedgvitggmipkVEAALDAARGGVRS-----VHIIDgRVPH----------ALLLELFTDEGI 276


                 ....*.
gi 767993833 202 GTLFKN 207
Cdd:PRK00942 277 GTMIVP 282
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
 23-136 6.77e-04

Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino acid substrates, as well as uridylate kinase and carbamate kinase. This family includes: Aspartokinase EC:2.7.2.4. Acetylglutamate kinase EC:2.7.2.8. Glutamate 5-kinase EC:2.7.2.11. Uridylate kinase EC:2.7.4.-. Carbamate kinase EC:2.7.2.2.


Pssm-ID: 395565 [Multi-domain]  Cd Length: 232  Bit Score: 40.81  E-value: 6.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833   23 FWEAKAQLAKSCKVLVDALRHNAAAAVPFFGGGSVLRAAEPAPHAsyggIVSVETDLLQWCLESGSIPILCP-IGETAAR 101
Cdd:pfam00696  68 EVATMDALGSLGERLNAALLAAGLPAVGLPAAQLLATEAGFIDDV----VTRIDTEALEELLEAGVVPVITGfIGIDPEG 143

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 767993833  102 RSVLLDSLEVTASLAKALRPTKIIFLNNTGGLRDS 136
Cdd:pfam00696 144 ELGRGSSDTLAALLAEALGADKLIILTDVDGVYTA 178
argB CHL00202
acetylglutamate kinase; Provisional
 35-150 1.80e-03

acetylglutamate kinase; Provisional


Pssm-ID: 133644 [Multi-domain]  Cd Length: 284  Bit Score: 39.78  E-value: 1.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993833  35 KVLVDALRHNAAAAVPFFGGGSVLRAAEPA--PHASY-GGIVSVETDLLQWCLESGSIPILCPIGETAARRSVLLDSLEV 111
Cdd:CHL00202 106 KDLVGSINANGGKAVGLCGKDANLIVARASdkKDLGLvGEIQQVDPQLIDMLLEKNYIPVIASVAADHDGQTYNINADVV 185

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 767993833 112 TASLAKALRPTKIIFLNNTGGlrdsshkVLSNVNLPADL 150
Cdd:CHL00202 186 AGEIAAKLNAEKLILLTDTPG-------ILADINDPNSL 217
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH