NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|490651794|ref|WP_004516788|]
View 

isopentenyl phosphate kinase [Haloarcula vallismortis]

Protein Classification

COG1608 family protein( domain architecture ID 10004056)

COG1608 family protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
COG1608 COG1608
Isopentenyl phosphate kinase [Lipid transport and metabolism];
2-244 1.57e-87

Isopentenyl phosphate kinase [Lipid transport and metabolism];


:

Pssm-ID: 441216 [Multi-domain]  Cd Length: 254  Bit Score: 260.15  E-value: 1.57e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651794   2 TVVLKLGGSVITEKDEPETVDRAALSAAVSAIAESAvGDDIVIVHGGGSFGHHHAADYGVSTTAGTHDVDGVQAIHGAMC 81
Cdd:COG1608    1 MIVLKLGGSVITDKDKPETVRRDALERIAREIAAAL-DLDLVIVHGGGSFGHPVAKKYGLHGTLGTEDAEGVSETHRAMR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651794  82 RLNAAVVDALTEHGVPAVPVHPFSVAVRDADGDLSLPTAQVTTLLDEGFVPVLHGDLVAHAGAGATVLSGDELVVELAPA 161
Cdd:COG1608   80 ELNRIVVDALLEAGVPAVSVPPSSFAVRDNGRILSFDTEPIKEMLEEGFVPVLHGDVVFDAERGFTILSGDEIVVYLAKE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651794 162 VDAERVGVCSTVPGVLDED--GAIIDRI--ETFEAVAPALGGSDATDVSGGMAGKVRAL---LALSAPALVFG---PDAL 231
Cdd:COG1608  160 LKPERVGLATDVDGVYDDDpkGKLIPEItrSNFDEVLDALGGSAGTDVTGGMAGKVEELlelAKPGVEVYIFNgnkPGNL 239
                        250
                 ....*....|....
gi 490651794 232 SAFLGGESP-GTTI 244
Cdd:COG1608  240 SAALRGEEVrGTRI 253
 
Name Accession Description Interval E-value
COG1608 COG1608
Isopentenyl phosphate kinase [Lipid transport and metabolism];
2-244 1.57e-87

Isopentenyl phosphate kinase [Lipid transport and metabolism];


Pssm-ID: 441216 [Multi-domain]  Cd Length: 254  Bit Score: 260.15  E-value: 1.57e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651794   2 TVVLKLGGSVITEKDEPETVDRAALSAAVSAIAESAvGDDIVIVHGGGSFGHHHAADYGVSTTAGTHDVDGVQAIHGAMC 81
Cdd:COG1608    1 MIVLKLGGSVITDKDKPETVRRDALERIAREIAAAL-DLDLVIVHGGGSFGHPVAKKYGLHGTLGTEDAEGVSETHRAMR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651794  82 RLNAAVVDALTEHGVPAVPVHPFSVAVRDADGDLSLPTAQVTTLLDEGFVPVLHGDLVAHAGAGATVLSGDELVVELAPA 161
Cdd:COG1608   80 ELNRIVVDALLEAGVPAVSVPPSSFAVRDNGRILSFDTEPIKEMLEEGFVPVLHGDVVFDAERGFTILSGDEIVVYLAKE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651794 162 VDAERVGVCSTVPGVLDED--GAIIDRI--ETFEAVAPALGGSDATDVSGGMAGKVRAL---LALSAPALVFG---PDAL 231
Cdd:COG1608  160 LKPERVGLATDVDGVYDDDpkGKLIPEItrSNFDEVLDALGGSAGTDVTGGMAGKVEELlelAKPGVEVYIFNgnkPGNL 239
                        250
                 ....*....|....
gi 490651794 232 SAFLGGESP-GTTI 244
Cdd:COG1608  240 SAALRGEEVrGTRI 253
AAK_FomA-like cd04241
AAK_FomA-like: This CD includes a fosfomycin biosynthetic gene product, FomA, and similar ...
2-244 6.34e-73

AAK_FomA-like: This CD includes a fosfomycin biosynthetic gene product, FomA, and similar proteins found in a wide range of organisms. Together, the fomA and fomB genes in the fosfomycin biosynthetic gene cluster of Streptomyces wedmorensis confer high-level fosfomycin resistance. FomA and FomB proteins converted fosfomycin to fosfomycin monophosphate and fosfomycin diphosphate in the presence of ATP and a magnesium ion, indicating that FomA and FomB catalyzed phosphorylations of fosfomycin and fosfomycin monophosphate, respectively. FomA and related sequences in this CD are members of the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239774 [Multi-domain]  Cd Length: 252  Bit Score: 222.91  E-value: 6.34e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651794   2 TVVLKLGGSVITEKDEPETVDRAALSAAVSAIAEsAVGDDIVIVHGGGSFGHHHAADYGVSTTAGTHDVDGVQAIHGAMC 81
Cdd:cd04241    1 MIILKLGGSVITDKDRPETIREENLERIARELAE-AIDEKLVLVHGGGSFGHPKAKEYGLPDGDGSFSAEGVAETHEAML 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651794  82 RLNAAVVDALTEHGVPAVPVHPFSVAVRDADGDLSLPTAQVTTLLDEGFVPVLHGDLVAHAGAGATVLSGDELVVELAPA 161
Cdd:cd04241   80 ELNSIVVDALLEAGVPAVSVPPSSFFVTENGRIVSFDLEVIKELLDRGFVPVLHGDVVLDEGGGITILSGDDIVVELAKA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651794 162 VDAERVGVCSTVPGVLDE---DGAIIDRIET--FEAVAPALgGSDATDVSGGMAGKVRALLALSAPAL---VFG---PDA 230
Cdd:cd04241  160 LKPERVIFLTDVDGVYDKpppDAKLIPEIDVgsLEDILAAL-GSAGTDVTGGMAGKIEELLELARRGIevyIFNgdkPEN 238
                        250
                 ....*....|....
gi 490651794 231 LSAFLGGESPGTTI 244
Cdd:cd04241  239 LYRALLGNFIGTRI 252
IPPK_Arch NF040647
isopentenyl phosphate kinase;
4-214 2.70e-37

isopentenyl phosphate kinase;


Pssm-ID: 468614 [Multi-domain]  Cd Length: 258  Bit Score: 131.57  E-value: 2.70e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651794   4 VLKLGGSVITEKDEPETVDRAALSAAVSAIAESAVGDDIVIVHGGGSFGHHHAADYGV-STTAGTHDVD---GVQAIHGA 79
Cdd:NF040647   2 ILKLGGSVITDKDIYPKIDWDNLERIAKEISNALDEDKLIIVHGGGSFGHPKAKKYGIgEGINGEEFERkrkGFWETQNA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651794  80 MCRLNAAVVDALTEHGVPAVPVHPFSVAVRDADGDLSLPTAQVTTLLDEGFVPVLHGDLVAHAGAGATVLSGDELVVELA 159
Cdd:NF040647  82 MRRLNNLVCDALIEYGIPAVSIQPSSFIRTGNKRILHFDLDLIKKYLELGFVPVLYGDVVLDNNIKYGILSGDQIIPYLA 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651794 160 PAVDAERVGVCSTVPGVLDEDGAIIDRIETFEAVA-----PALGGSDATDVSGGMAGKVR 214
Cdd:NF040647 162 KKLKPDRVILGSDVDGVYDKNPKKYPDAKLIDKVNslddlESLEGTNNVDVTGGMYGKVK 221
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
1-214 1.19e-24

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: 97.82  E-value: 1.19e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651794    1 MTVVLKLGGSVITEKDepetvdraALSAAVSAIAE-SAVGDDIVIVHGGGSFGHHHAADYGVSTT--AGTHDVDGVQAIH 77
Cdd:pfam00696   1 KRVVIKLGGSSLTDKE--------RLKRLADEIAAlLEEGRKLVVVHGGGAFADGLLALLGLSPRfaRLTDAETLEVATM 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651794   78 GAMCRLNAAVVDALTEHGVPAVPVHPFSVAVRDAD----GDLSLPTAQVTTLLDEGFVPVLHGDLVAHAGAGATVLSGDE 153
Cdd:pfam00696  73 DALGSLGERLNAALLAAGLPAVGLPAAQLLATEAGfiddVVTRIDTEALEELLEAGVVPVITGFIGIDPEGELGRGSSDT 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490651794  154 LVVELAPAVDAERVGVCSTVPGVLDEDGAIIDRIETFEAVAP--ALGGSDATDVSGGMAGKVR 214
Cdd:pfam00696 153 LAALLAEALGADKLIILTDVDGVYTADPRKVPDAKLIPEISYdeLLELLASGLATGGMKVKLP 215
argB TIGR00761
acetylglutamate kinase; This model describes N-acetylglutamate kinases (ArgB) of many ...
2-214 1.03e-03

acetylglutamate kinase; This model describes N-acetylglutamate kinases (ArgB) of many prokaryotes and the N-acetylglutamate kinase domains of multifunctional proteins from yeasts. This enzyme is the second step in the "acetylated" ornithine biosynthesis pathway. A related group of enzymes representing the first step of the pathway contain a homologous domain and are excluded from this model. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 273256 [Multi-domain]  Cd Length: 231  Bit Score: 39.19  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651794    2 TVVLKLGGSVITEKDEpetvdraalsAAVSAIAES-AVGDDIVIVHGGGSFGHHHAADYGVS---------TTAGTHDVd 71
Cdd:TIGR00761   1 TIVIKIGGAAISDLLE----------AFASDIAFLrAVGIKPVIVHGGGPEINELLEALGIPpefknglrvTDKETLEV- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651794   72 gvqaIHGAMC-RLNAAVVDALTEHGVPAVPV-----HPFSVAVRDADGD------LSLPTAQVTTLLDEGFVPVLHGDLV 139
Cdd:TIGR00761  70 ----VEMVLIgQVNKELVALLNKHGINAIGLtggdgQLFTARYLDKEDLgyvgeiKKVNKALIEALLKAGYIPVISSLAL 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490651794  140 AHAGAGATVlSGDELVVELAPAVDAERVGVCSTVPGVLDEDGA-IIDRIETFEAVAPALGGsdatDVSGGMAGKVR 214
Cdd:TIGR00761 146 TAEGQALNV-NADTAAGALAAALGAEKLVLLTDVPGILNGDGQsLISEIPLDEIEQLIKQG----IIKGGMIPKVN 216
PRK00942 PRK00942
acetylglutamate kinase; Provisional
119-214 9.79e-03

acetylglutamate kinase; Provisional


Pssm-ID: 234869 [Multi-domain]  Cd Length: 283  Bit Score: 36.62  E-value: 9.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651794 119 TAQVTTLLDEGFVPVlhgdlVAHAGAGATVLS----GDELVVELAPAVDAERVGVCSTVPGVLDEDGAIIDRIETFEAVA 194
Cdd:PRK00942 152 PALLEALLEAGYIPV-----ISPIGVGEDGETyninADTAAGAIAAALGAEKLILLTDVPGVLDDKGQLISELTASEAEE 226
                         90       100
                 ....*....|....*....|
gi 490651794 195 PALGGSdatdVSGGMAGKVR 214
Cdd:PRK00942 227 LIEDGV----ITGGMIPKVE 242
 
Name Accession Description Interval E-value
COG1608 COG1608
Isopentenyl phosphate kinase [Lipid transport and metabolism];
2-244 1.57e-87

Isopentenyl phosphate kinase [Lipid transport and metabolism];


Pssm-ID: 441216 [Multi-domain]  Cd Length: 254  Bit Score: 260.15  E-value: 1.57e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651794   2 TVVLKLGGSVITEKDEPETVDRAALSAAVSAIAESAvGDDIVIVHGGGSFGHHHAADYGVSTTAGTHDVDGVQAIHGAMC 81
Cdd:COG1608    1 MIVLKLGGSVITDKDKPETVRRDALERIAREIAAAL-DLDLVIVHGGGSFGHPVAKKYGLHGTLGTEDAEGVSETHRAMR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651794  82 RLNAAVVDALTEHGVPAVPVHPFSVAVRDADGDLSLPTAQVTTLLDEGFVPVLHGDLVAHAGAGATVLSGDELVVELAPA 161
Cdd:COG1608   80 ELNRIVVDALLEAGVPAVSVPPSSFAVRDNGRILSFDTEPIKEMLEEGFVPVLHGDVVFDAERGFTILSGDEIVVYLAKE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651794 162 VDAERVGVCSTVPGVLDED--GAIIDRI--ETFEAVAPALGGSDATDVSGGMAGKVRAL---LALSAPALVFG---PDAL 231
Cdd:COG1608  160 LKPERVGLATDVDGVYDDDpkGKLIPEItrSNFDEVLDALGGSAGTDVTGGMAGKVEELlelAKPGVEVYIFNgnkPGNL 239
                        250
                 ....*....|....
gi 490651794 232 SAFLGGESP-GTTI 244
Cdd:COG1608  240 SAALRGEEVrGTRI 253
AAK_FomA-like cd04241
AAK_FomA-like: This CD includes a fosfomycin biosynthetic gene product, FomA, and similar ...
2-244 6.34e-73

AAK_FomA-like: This CD includes a fosfomycin biosynthetic gene product, FomA, and similar proteins found in a wide range of organisms. Together, the fomA and fomB genes in the fosfomycin biosynthetic gene cluster of Streptomyces wedmorensis confer high-level fosfomycin resistance. FomA and FomB proteins converted fosfomycin to fosfomycin monophosphate and fosfomycin diphosphate in the presence of ATP and a magnesium ion, indicating that FomA and FomB catalyzed phosphorylations of fosfomycin and fosfomycin monophosphate, respectively. FomA and related sequences in this CD are members of the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239774 [Multi-domain]  Cd Length: 252  Bit Score: 222.91  E-value: 6.34e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651794   2 TVVLKLGGSVITEKDEPETVDRAALSAAVSAIAEsAVGDDIVIVHGGGSFGHHHAADYGVSTTAGTHDVDGVQAIHGAMC 81
Cdd:cd04241    1 MIILKLGGSVITDKDRPETIREENLERIARELAE-AIDEKLVLVHGGGSFGHPKAKEYGLPDGDGSFSAEGVAETHEAML 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651794  82 RLNAAVVDALTEHGVPAVPVHPFSVAVRDADGDLSLPTAQVTTLLDEGFVPVLHGDLVAHAGAGATVLSGDELVVELAPA 161
Cdd:cd04241   80 ELNSIVVDALLEAGVPAVSVPPSSFFVTENGRIVSFDLEVIKELLDRGFVPVLHGDVVLDEGGGITILSGDDIVVELAKA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651794 162 VDAERVGVCSTVPGVLDE---DGAIIDRIET--FEAVAPALgGSDATDVSGGMAGKVRALLALSAPAL---VFG---PDA 230
Cdd:cd04241  160 LKPERVIFLTDVDGVYDKpppDAKLIPEIDVgsLEDILAAL-GSAGTDVTGGMAGKIEELLELARRGIevyIFNgdkPEN 238
                        250
                 ....*....|....
gi 490651794 231 LSAFLGGESPGTTI 244
Cdd:cd04241  239 LYRALLGNFIGTRI 252
IPPK_Arch NF040647
isopentenyl phosphate kinase;
4-214 2.70e-37

isopentenyl phosphate kinase;


Pssm-ID: 468614 [Multi-domain]  Cd Length: 258  Bit Score: 131.57  E-value: 2.70e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651794   4 VLKLGGSVITEKDEPETVDRAALSAAVSAIAESAVGDDIVIVHGGGSFGHHHAADYGV-STTAGTHDVD---GVQAIHGA 79
Cdd:NF040647   2 ILKLGGSVITDKDIYPKIDWDNLERIAKEISNALDEDKLIIVHGGGSFGHPKAKKYGIgEGINGEEFERkrkGFWETQNA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651794  80 MCRLNAAVVDALTEHGVPAVPVHPFSVAVRDADGDLSLPTAQVTTLLDEGFVPVLHGDLVAHAGAGATVLSGDELVVELA 159
Cdd:NF040647  82 MRRLNNLVCDALIEYGIPAVSIQPSSFIRTGNKRILHFDLDLIKKYLELGFVPVLYGDVVLDNNIKYGILSGDQIIPYLA 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651794 160 PAVDAERVGVCSTVPGVLDEDGAIIDRIETFEAVA-----PALGGSDATDVSGGMAGKVR 214
Cdd:NF040647 162 KKLKPDRVILGSDVDGVYDKNPKKYPDAKLIDKVNslddlESLEGTNNVDVTGGMYGKVK 221
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
1-214 1.19e-24

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: 97.82  E-value: 1.19e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651794    1 MTVVLKLGGSVITEKDepetvdraALSAAVSAIAE-SAVGDDIVIVHGGGSFGHHHAADYGVSTT--AGTHDVDGVQAIH 77
Cdd:pfam00696   1 KRVVIKLGGSSLTDKE--------RLKRLADEIAAlLEEGRKLVVVHGGGAFADGLLALLGLSPRfaRLTDAETLEVATM 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651794   78 GAMCRLNAAVVDALTEHGVPAVPVHPFSVAVRDAD----GDLSLPTAQVTTLLDEGFVPVLHGDLVAHAGAGATVLSGDE 153
Cdd:pfam00696  73 DALGSLGERLNAALLAAGLPAVGLPAAQLLATEAGfiddVVTRIDTEALEELLEAGVVPVITGFIGIDPEGELGRGSSDT 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490651794  154 LVVELAPAVDAERVGVCSTVPGVLDEDGAIIDRIETFEAVAP--ALGGSDATDVSGGMAGKVR 214
Cdd:pfam00696 153 LAALLAEALGADKLIILTDVDGVYTADPRKVPDAKLIPEISYdeLLELLASGLATGGMKVKLP 215
AAK cd02115
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ...
4-186 6.02e-05

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: 43.20  E-value: 6.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651794   4 VLKLGGSVITEKDEPETVDRaalsaavsaIAESAVGDDIVIVHGGGSFGHHHAADYGVSTTAGTHDVDGVQAIHGAMC-- 81
Cdd:cd02115    1 VIKFGGSSVSSEERLRNLAR---------ILVKLASEGGRVVVVHGAGPQITDELLAHGELLGYARGLRITDRETDALaa 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651794  82 ----RLNAAVVDALTEHGVPAVPVHP-----FSVAVRDADGDLSLPTAQVTTLLDEGFVPVLHGDLVAHAGAGATVLSG- 151
Cdd:cd02115   72 mgegMSNLLIAAALEQHGIKAVPLDLtqagfASPNQGHVGKITKVSTDRLKSLLENGILPILSGFGGTDEKETGTLGRGg 151
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 490651794 152 -DELVVELAPAVDAERVGVCSTVPGVLDEDGAIIDR 186
Cdd:cd02115  152 sDSTAALLAAALKADRLVILTDVDGVYTADPRKVPD 187
AAK_NAGK-like cd04238
AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the ...
122-214 8.76e-05

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: 42.50  E-value: 8.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651794 122 VTTLLDEGFVPVlhgdlVAHAGAGATVLS----GDELVVELAPAVDAERVGVCSTVPGVLDEDGAIIDRIETFEAVAPAL 197
Cdd:cd04238  131 LETLLEAGYIPV-----IAPIAVDEDGETynvnADTAAGAIAAALKAEKLILLTDVPGVLDDPGSLISELTPKEAEELIE 205
                         90
                 ....*....|....*..
gi 490651794 198 GGSdatdVSGGMAGKVR 214
Cdd:cd04238  206 DGV----ISGGMIPKVE 218
ArgB COG0548
N-acetylglutamate kinase [Amino acid transport and metabolism]; N-acetylglutamate kinase is ...
119-214 4.51e-04

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: 40.79  E-value: 4.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651794 119 TAQVTTLLDEGFVPVlhgdlVAHAGAGATV----LSGDELVVELAPAVDAERVGVCSTVPGVLDEDGAIIDRIeTFEAVA 194
Cdd:COG0548  154 PELIRALLDAGYIPV-----ISPIGYSPTGevynINADTVAGAIAAALKAEKLILLTDVPGVLDDPGSLISEL-TAAEAE 227
                         90       100
                 ....*....|....*....|
gi 490651794 195 PALggsDATDVSGGMAGKVR 214
Cdd:COG0548  228 ELI---ADGVISGGMIPKLE 244
argB TIGR00761
acetylglutamate kinase; This model describes N-acetylglutamate kinases (ArgB) of many ...
2-214 1.03e-03

acetylglutamate kinase; This model describes N-acetylglutamate kinases (ArgB) of many prokaryotes and the N-acetylglutamate kinase domains of multifunctional proteins from yeasts. This enzyme is the second step in the "acetylated" ornithine biosynthesis pathway. A related group of enzymes representing the first step of the pathway contain a homologous domain and are excluded from this model. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 273256 [Multi-domain]  Cd Length: 231  Bit Score: 39.19  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651794    2 TVVLKLGGSVITEKDEpetvdraalsAAVSAIAES-AVGDDIVIVHGGGSFGHHHAADYGVS---------TTAGTHDVd 71
Cdd:TIGR00761   1 TIVIKIGGAAISDLLE----------AFASDIAFLrAVGIKPVIVHGGGPEINELLEALGIPpefknglrvTDKETLEV- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651794   72 gvqaIHGAMC-RLNAAVVDALTEHGVPAVPV-----HPFSVAVRDADGD------LSLPTAQVTTLLDEGFVPVLHGDLV 139
Cdd:TIGR00761  70 ----VEMVLIgQVNKELVALLNKHGINAIGLtggdgQLFTARYLDKEDLgyvgeiKKVNKALIEALLKAGYIPVISSLAL 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490651794  140 AHAGAGATVlSGDELVVELAPAVDAERVGVCSTVPGVLDEDGA-IIDRIETFEAVAPALGGsdatDVSGGMAGKVR 214
Cdd:TIGR00761 146 TAEGQALNV-NADTAAGALAAALGAEKLVLLTDVPGILNGDGQsLISEIPLDEIEQLIKQG----IIKGGMIPKVN 216
AAK_NAGK-UC cd04251
AAK_NAGK-UC: N-Acetyl-L-glutamate kinase - uncharacterized (NAGK-UC). This domain is similar ...
122-213 5.11e-03

AAK_NAGK-UC: N-Acetyl-L-glutamate kinase - uncharacterized (NAGK-UC). This domain is similar to Escherichia coli and Pseudomonas aeruginosa NAGKs which catalyze the phosphorylation of the gamma-COOH group of N-acetyl-L-glutamate (NAG) by ATP in the second step of microbial arginine biosynthesis. These uncharacterized domain sequences are found in some bacteria (Deinococci and Chloroflexi) and archea and belong to the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239784 [Multi-domain]  Cd Length: 257  Bit Score: 37.35  E-value: 5.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651794 122 VTTLLDEGFVPVLHGdlVAHAGAGATV-LSGDELVVELAPAVDAERVGVCSTVPGVLDeDGAIIDRIETFEAVapalggS 200
Cdd:cd04251  138 IEALLDAGYLPVVSP--VAYSEEGEPLnVDGDRAAAAIAAALKAERLILLTDVEGLYL-DGRVIERITVSDAE------S 208
                         90
                 ....*....|...
gi 490651794 201 DATDVSGGMAGKV 213
Cdd:cd04251  209 LLEKAGGGMKRKL 221
PRK00942 PRK00942
acetylglutamate kinase; Provisional
119-214 9.79e-03

acetylglutamate kinase; Provisional


Pssm-ID: 234869 [Multi-domain]  Cd Length: 283  Bit Score: 36.62  E-value: 9.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651794 119 TAQVTTLLDEGFVPVlhgdlVAHAGAGATVLS----GDELVVELAPAVDAERVGVCSTVPGVLDEDGAIIDRIETFEAVA 194
Cdd:PRK00942 152 PALLEALLEAGYIPV-----ISPIGVGEDGETyninADTAAGAIAAALGAEKLILLTDVPGVLDDKGQLISELTASEAEE 226
                         90       100
                 ....*....|....*....|
gi 490651794 195 PALGGSdatdVSGGMAGKVR 214
Cdd:PRK00942 227 LIEDGV----ITGGMIPKVE 242
 
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