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Conserved domains on  [gi|16128308|ref|NP_414857|]
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carbamate kinase-like protein YahI [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

carbamate kinase family protein( domain architecture ID 10793640)

carbamate kinase family protein similar to Escherichia coli carbamate kinase-like protein YahI

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PRK12352 PRK12352
putative carbamate kinase; Reviewed
 1-316 0e+00

putative carbamate kinase; Reviewed


:

Pssm-ID: 183464  Cd Length: 316  Bit Score: 627.98  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308    1 MKELVVVAIGGNSIIKDNASQSIEHQAEAVKAVADTVLEMLASDYDIVLTHGNGPQVGLDLRRAEIAHKREGLPLTPLAN 80
Cdd:PRK12352   1 MKELVVVAIGGNSIIKDNASQSIEHQAEAVKAVADTVLEMLASDYDIVLTHGNGPQVGLDLRRAEIAHEREGLPLTPLAN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308   81 CVADTQGGIGYLIQQALNNRLARHGEKKAVTVVTQVEVDKNDPGFAHPTKPIGAFFSDSQRDELQKANPDWCFVEDAGRG 160
Cdd:PRK12352  81 CVADTQGGIGYLIQQALNNRLARHGEKKAVTVVTQVEVDKNDPGFAHPTKPIGAFFSESQRDELQKANPDWRFVEDAGRG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308  161 YRRVVASPEPKRIVEAPAIKALIQQGFVVIGAGGGGIPVVRTDAGDYQSVDAVIDKDLSTALLAREIHADILVITTGVEK 240
Cdd:PRK12352 161 YRRVVASPEPKRIVEAPAIKALIQQGFVVIGAGGGGIPVVRTDAGDYQSVDAVIDKDLSTALLAREIHADILVITTGVEK 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128308  241 VCIHFGKPQQQALDRVDIATMTRYMQEGHFPPGSMLPKIIASLTFLEQGGKEVIITTPECLPAALRGETGTHIIKT 316
Cdd:PRK12352 241 VCIHFGKPQQQALDRVDIATMTRYMQEGHFPPGSMLPKIIASLTFLEQGGKEVIITTPECLPAALRGETGTHIIKT 316
 
Name Accession Description Interval E-value
PRK12352 PRK12352
putative carbamate kinase; Reviewed
 1-316 0e+00

putative carbamate kinase; Reviewed


Pssm-ID: 183464  Cd Length: 316  Bit Score: 627.98  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308    1 MKELVVVAIGGNSIIKDNASQSIEHQAEAVKAVADTVLEMLASDYDIVLTHGNGPQVGLDLRRAEIAHKREGLPLTPLAN 80
Cdd:PRK12352   1 MKELVVVAIGGNSIIKDNASQSIEHQAEAVKAVADTVLEMLASDYDIVLTHGNGPQVGLDLRRAEIAHEREGLPLTPLAN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308   81 CVADTQGGIGYLIQQALNNRLARHGEKKAVTVVTQVEVDKNDPGFAHPTKPIGAFFSDSQRDELQKANPDWCFVEDAGRG 160
Cdd:PRK12352  81 CVADTQGGIGYLIQQALNNRLARHGEKKAVTVVTQVEVDKNDPGFAHPTKPIGAFFSESQRDELQKANPDWRFVEDAGRG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308  161 YRRVVASPEPKRIVEAPAIKALIQQGFVVIGAGGGGIPVVRTDAGDYQSVDAVIDKDLSTALLAREIHADILVITTGVEK 240
Cdd:PRK12352 161 YRRVVASPEPKRIVEAPAIKALIQQGFVVIGAGGGGIPVVRTDAGDYQSVDAVIDKDLSTALLAREIHADILVITTGVEK 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128308  241 VCIHFGKPQQQALDRVDIATMTRYMQEGHFPPGSMLPKIIASLTFLEQGGKEVIITTPECLPAALRGETGTHIIKT 316
Cdd:PRK12352 241 VCIHFGKPQQQALDRVDIATMTRYMQEGHFPPGSMLPKIIASLTFLEQGGKEVIITTPECLPAALRGETGTHIIKT 316
ArcC COG0549
Carbamate kinase [Amino acid transport and metabolism];
1-315 5.11e-153

Carbamate kinase [Amino acid transport and metabolism];


Pssm-ID: 440315  Cd Length: 313  Bit Score: 431.04  E-value: 5.11e-153
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308   1 MKELVVVAIGGNSIIKDNASQSIEHQAEAVKAVADTVLEMLASDYDIVLTHGNGPQVGLDLRRAEIAHKreGLPLTPLAN 80
Cdd:COG0549   1 MKKRIVVALGGNALLRRGEPGTAEEQRENVREAAKALADLIEAGHEVVITHGNGPQVGLLLLQNEAAKK--KVPPMPLDV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308  81 CVADTQGGIGYLIQQALNNRLARHG-EKKAVTVVTQVEVDKNDPGFAHPTKPIGAFFSDSQRDELQKaNPDWCFVEDAGR 159
Cdd:COG0549  79 CGAMTQGMIGYMLQQALRNELPKRGiDKPVATLVTQVEVDPDDPAFQNPTKPIGPFYTEEEAEELAK-EKGWTFKEDAGR 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308 160 GYRRVVASPEPKRIVEAPAIKALIQQgfvvigaggggipvvRTDAGDYQSVDAVIDKDLSTALLAREIHADILVITTGVE 239
Cdd:COG0549 158 GYRRVVPSPKPKRIVEIDAIKALLEAgviviaaggggipvvRDEDGGLKGVEAVIDKDLASALLAEELDADLLLILTDVD 237

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128308 240 KVCIHFGKPQQQALDRVDIATMTRYMQEGHFPPGSMLPKIIASLTFLEQGGKEVIITTPECLPAALRGETGTHIIK 315
Cdd:COG0549 238 KVYINFGKPDQRALDEVTVAEAKKYIEEGHFAAGSMGPKVEAAIRFVEATGKRAIITSLEKAEEALAGKAGTRIVP 313
AAK_CK cd04235
AAK_CK: Carbamate kinase (CK) catalyzes both the ATP-phosphorylation of carbamate and ...
 4-314 9.14e-149

AAK_CK: Carbamate kinase (CK) catalyzes both the ATP-phosphorylation of carbamate and carbamoyl phosphate (CP) utilization with the production of ATP from ADP and CP. Both CK (this CD) and nonhomologous CP synthetase synthesize carbamoyl phosphate, an essential precursor of arginine and pyrimidine bases, in the presence of ATP, bicarbonate, and ammonia. CK is a homodimer of 33 kDa subunits and is a member of the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239768  Cd Length: 308  Bit Score: 419.99  E-value: 9.14e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308   4 LVVVAIGGNSIIKDNASQSIEHQAEAVKAVADTVLEMLASDYDIVLTHGNGPQVGLDLRRAEIAHkrEGLPLTPLANCVA 83
Cdd:cd04235   1 RIVVALGGNALLRRGEPGTAEEQRENVKIAAKALADLIKNGHEVVITHGNGPQVGNLLLQNEAAA--EKVPAYPLDVCGA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308  84 DTQGGIGYLIQQALNNRLARHG-EKKAVTVVTQVEVDKNDPGFAHPTKPIGAFFSDSQRDELQKANpDWCFVEDAGRGYR 162
Cdd:cd04235  79 MSQGMIGYMLQQALDNELPKRGiDKPVVTLVTQVVVDANDPAFKNPTKPIGPFYSEEEAEELAAEK-GWTFKEDAGRGYR 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308 163 RVVASPEPKRIVEAPAIKALIQQGFVVIGAGGGGIPVVRTDaGDYQSVDAVIDKDLSTALLAREIHADILVITTGVEKVC 242
Cdd:cd04235 158 RVVPSPKPKDIVEIEAIKTLVDNGVIVIAAGGGGIPVVREG-GGLKGVEAVIDKDLASALLAEEINADLLVILTDVDNVY 236

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128308 243 IHFGKPQQQALDRVDIATMTRYMQEGHFPPGSMLPKIIASLTFLEQGGKEVIITTPECLPAALRGETGTHII 314
Cdd:cd04235 237 INFGKPNQKALEQVTVEELEKYIEEGQFAPGSMGPKVEAAIRFVESGGKKAIITSLENAEAALEGKAGTVIV 308
arcC TIGR00746
carbamate kinase; In most species, carbamate kinase works in arginine catabolism and consumes ...
 5-315 1.61e-99

carbamate kinase; In most species, carbamate kinase works in arginine catabolism and consumes carbamoyl phosphate to convert ADP into ATP. In the pathway in Pyrococcus furiosus, the enzyme acts instead to generate carbamoyl phosphate.The seed alignment for this model includes experimentally confirmed examples from a set of phylogenetically distinct species. In a neighbor-joining tree constructed from an alignment of candidate carbamate kinases and several acetylglutamate kinases, the latter group forms a clear outgroup which roots the tree of carbamate kinase-like proteins. This analysis suggests that in E. coli, the ArcC paralog YqeA may be a second isozyme, while the paralog YahI branches as an outlier and is less likely to be an authentic carbamate kinase. The homolog from Mycoplasma pneumoniae likewise branches outside the set containing known carbamate kinases and also scores below the trusted cutoff. [Energy metabolism, Amino acids and amines]


Pssm-ID: 273248  Cd Length: 310  Bit Score: 295.13  E-value: 1.61e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308     5 VVVAIGGNSIIKDNASQSIEHQAEAVKAVADTVLEMLASDYDIVLTHGNGPQVGLDLRRAEIAhkREGLPLTPLANCVAD 84
Cdd:TIGR00746   3 VVVALGGNALLQRGEKGSAEAQRDNVRQTAPQIAKLIKRGYELVITHGNGPQVGNLLLQNQAA--DSEVPAMPLDVLGAM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308    85 TQGGIGYLIQQALNNRLARHG-EKKAVTVVTQVEVDKNDPGFAHPTKPIGAFFSDsQRDELQKANPDWCFVEDAGRGYRR 163
Cdd:TIGR00746  81 SQGMIGYMLQQALNNELPKRGmEKPVATVLTQTIVDPKDPAFQNPTKPIGPFYTE-EEAKRLAAEKGWIVKEDAGRGWRR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308   164 VVASPEPKRIVEAPAIKALIQQGFVVIGAGGGGIPVVRTDAGdYQSVDAVIDKDLSTALLAREIHADILVITTGVEKVCI 243
Cdd:TIGR00746 160 VVPSPRPKDIVEAETIKTLVENGVIVISSGGGGVPVVLEGAE-LKGVEAVIDKDLASEKLAEEVNADILVILTDVDAVYI 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128308   244 HFGKPQQQALDRVDIATMTRYMQEGHFPPGSMLPKIIASLTFLEQGGKEVIITTPECLPAALRGETGTHIIK 315
Cdd:TIGR00746 239 NYGKPDEKALREVTVEELEDYYKAGHFAAGSMGPKVEAAIEFVESGGKRAIITSLENAVEALEGKAGTRVTK 310
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
 3-296 3.04e-10

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: 59.30  E-value: 3.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308     3 ELVVVAIGGNSIikdnasqsieHQAEAVKAVADTVLEMLASDYDIVLTHGNGPQVGLDLRRAEIAHKREGLPLTPLANCV 82
Cdd:pfam00696   1 KRVVIKLGGSSL----------TDKERLKRLADEIAALLEEGRKLVVVHGGGAFADGLLALLGLSPRFARLTDAETLEVA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308    83 ADTQGGIgylIQQALNNRLARHGEKKavtvvtqvevdkndpgfahptKPIGAFFSDSQRDELQKAnpdwcfvedagrgyr 162
Cdd:pfam00696  71 TMDALGS---LGERLNAALLAAGLPA---------------------VGLPAAQLLATEAGFIDD--------------- 111

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308   163 rvvaspePKRIVEAPAIKALIQQGFVVIGAGGggipvvrtDAGDYQSVDAVIDKDLSTALLAREIHADILVITTGVEKVC 242
Cdd:pfam00696 112 -------VVTRIDTEALEELLEAGVVPVITGF--------IGIDPEGELGRGSSDTLAALLAEALGADKLIILTDVDGVY 176

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 16128308   243 IHFGKPQQQA--LDRVDIATMTRYmQEGHFPPGSMLPKIIASLTFLEQGGKEVIIT 296
Cdd:pfam00696 177 TADPRKVPDAklIPEISYDELLEL-LASGLATGGMKVKLPAALEAARRGGIPVVIV 231
 
Name Accession Description Interval E-value
PRK12352 PRK12352
putative carbamate kinase; Reviewed
 1-316 0e+00

putative carbamate kinase; Reviewed


Pssm-ID: 183464  Cd Length: 316  Bit Score: 627.98  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308    1 MKELVVVAIGGNSIIKDNASQSIEHQAEAVKAVADTVLEMLASDYDIVLTHGNGPQVGLDLRRAEIAHKREGLPLTPLAN 80
Cdd:PRK12352   1 MKELVVVAIGGNSIIKDNASQSIEHQAEAVKAVADTVLEMLASDYDIVLTHGNGPQVGLDLRRAEIAHEREGLPLTPLAN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308   81 CVADTQGGIGYLIQQALNNRLARHGEKKAVTVVTQVEVDKNDPGFAHPTKPIGAFFSDSQRDELQKANPDWCFVEDAGRG 160
Cdd:PRK12352  81 CVADTQGGIGYLIQQALNNRLARHGEKKAVTVVTQVEVDKNDPGFAHPTKPIGAFFSESQRDELQKANPDWRFVEDAGRG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308  161 YRRVVASPEPKRIVEAPAIKALIQQGFVVIGAGGGGIPVVRTDAGDYQSVDAVIDKDLSTALLAREIHADILVITTGVEK 240
Cdd:PRK12352 161 YRRVVASPEPKRIVEAPAIKALIQQGFVVIGAGGGGIPVVRTDAGDYQSVDAVIDKDLSTALLAREIHADILVITTGVEK 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128308  241 VCIHFGKPQQQALDRVDIATMTRYMQEGHFPPGSMLPKIIASLTFLEQGGKEVIITTPECLPAALRGETGTHIIKT 316
Cdd:PRK12352 241 VCIHFGKPQQQALDRVDIATMTRYMQEGHFPPGSMLPKIIASLTFLEQGGKEVIITTPECLPAALRGETGTHIIKT 316
ArcC COG0549
Carbamate kinase [Amino acid transport and metabolism];
1-315 5.11e-153

Carbamate kinase [Amino acid transport and metabolism];


Pssm-ID: 440315  Cd Length: 313  Bit Score: 431.04  E-value: 5.11e-153
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308   1 MKELVVVAIGGNSIIKDNASQSIEHQAEAVKAVADTVLEMLASDYDIVLTHGNGPQVGLDLRRAEIAHKreGLPLTPLAN 80
Cdd:COG0549   1 MKKRIVVALGGNALLRRGEPGTAEEQRENVREAAKALADLIEAGHEVVITHGNGPQVGLLLLQNEAAKK--KVPPMPLDV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308  81 CVADTQGGIGYLIQQALNNRLARHG-EKKAVTVVTQVEVDKNDPGFAHPTKPIGAFFSDSQRDELQKaNPDWCFVEDAGR 159
Cdd:COG0549  79 CGAMTQGMIGYMLQQALRNELPKRGiDKPVATLVTQVEVDPDDPAFQNPTKPIGPFYTEEEAEELAK-EKGWTFKEDAGR 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308 160 GYRRVVASPEPKRIVEAPAIKALIQQgfvvigaggggipvvRTDAGDYQSVDAVIDKDLSTALLAREIHADILVITTGVE 239
Cdd:COG0549 158 GYRRVVPSPKPKRIVEIDAIKALLEAgviviaaggggipvvRDEDGGLKGVEAVIDKDLASALLAEELDADLLLILTDVD 237

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128308 240 KVCIHFGKPQQQALDRVDIATMTRYMQEGHFPPGSMLPKIIASLTFLEQGGKEVIITTPECLPAALRGETGTHIIK 315
Cdd:COG0549 238 KVYINFGKPDQRALDEVTVAEAKKYIEEGHFAAGSMGPKVEAAIRFVEATGKRAIITSLEKAEEALAGKAGTRIVP 313
AAK_CK cd04235
AAK_CK: Carbamate kinase (CK) catalyzes both the ATP-phosphorylation of carbamate and ...
 4-314 9.14e-149

AAK_CK: Carbamate kinase (CK) catalyzes both the ATP-phosphorylation of carbamate and carbamoyl phosphate (CP) utilization with the production of ATP from ADP and CP. Both CK (this CD) and nonhomologous CP synthetase synthesize carbamoyl phosphate, an essential precursor of arginine and pyrimidine bases, in the presence of ATP, bicarbonate, and ammonia. CK is a homodimer of 33 kDa subunits and is a member of the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239768  Cd Length: 308  Bit Score: 419.99  E-value: 9.14e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308   4 LVVVAIGGNSIIKDNASQSIEHQAEAVKAVADTVLEMLASDYDIVLTHGNGPQVGLDLRRAEIAHkrEGLPLTPLANCVA 83
Cdd:cd04235   1 RIVVALGGNALLRRGEPGTAEEQRENVKIAAKALADLIKNGHEVVITHGNGPQVGNLLLQNEAAA--EKVPAYPLDVCGA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308  84 DTQGGIGYLIQQALNNRLARHG-EKKAVTVVTQVEVDKNDPGFAHPTKPIGAFFSDSQRDELQKANpDWCFVEDAGRGYR 162
Cdd:cd04235  79 MSQGMIGYMLQQALDNELPKRGiDKPVVTLVTQVVVDANDPAFKNPTKPIGPFYSEEEAEELAAEK-GWTFKEDAGRGYR 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308 163 RVVASPEPKRIVEAPAIKALIQQGFVVIGAGGGGIPVVRTDaGDYQSVDAVIDKDLSTALLAREIHADILVITTGVEKVC 242
Cdd:cd04235 158 RVVPSPKPKDIVEIEAIKTLVDNGVIVIAAGGGGIPVVREG-GGLKGVEAVIDKDLASALLAEEINADLLVILTDVDNVY 236

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128308 243 IHFGKPQQQALDRVDIATMTRYMQEGHFPPGSMLPKIIASLTFLEQGGKEVIITTPECLPAALRGETGTHII 314
Cdd:cd04235 237 INFGKPNQKALEQVTVEELEKYIEEGQFAPGSMGPKVEAAIRFVESGGKKAIITSLENAEAALEGKAGTVIV 308
PRK12353 PRK12353
putative amino acid kinase; Reviewed
 1-315 4.27e-139

putative amino acid kinase; Reviewed


Pssm-ID: 237071  Cd Length: 314  Bit Score: 395.68  E-value: 4.27e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308    1 MKELVVVAIGGNSIIKDNasQSIEHQAEAVKAVADTVLEMLASDYDIVLTHGNGPQVGLDLRRAEIAHK-REGLPLTPLA 79
Cdd:PRK12353   1 MMKKIVVALGGNALGSTP--EEATAQLEAVKKTAKSLVDLIEEGHEVVITHGNGPQVGNILLAQEAAASeKNKVPAMPLD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308   80 NCVADTQGGIGYLIQQALNNRLARHG-EKKAVTVVTQVEVDKNDPGFAHPTKPIGAFFSDSQRDELQKANpDWCFVEDAG 158
Cdd:PRK12353  79 VCGAMSQGYIGYHLQNALRNELLKRGiDKPVATVVTQVVVDANDPAFKNPTKPIGPFYTEEEAEKLAKEK-GYTFKEDAG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308  159 RGYRRVVASPEPKRIVEAPAIKALIqqgfvvigaggggipvvrtDAG------------------DYQSVDAVIDKDLST 220
Cdd:PRK12353 158 RGYRRVVPSPKPVDIVEIEAIKTLV-------------------DAGqvviaaggggipvireggGLKGVEAVIDKDFAS 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308  221 ALLAREIHADILVITTGVEKVCIHFGKPQQQALDRVDIATMTRYMQEGHFPPGSMLPKIIASLTFL-EQGGKEVIITTPE 299
Cdd:PRK12353 219 AKLAELVDADLLIILTAVDKVYINFGKPNQKKLDEVTVSEAEKYIEEGQFAPGSMLPKVEAAISFVeSRPGRKAIITSLE 298

                        330
                 ....*....|....*.
gi 16128308  300 CLPAALRGETGTHIIK 315
Cdd:PRK12353 299 KAKEALEGKAGTVIVK 314
PRK12454 PRK12454
carbamate kinase-like carbamoyl phosphate synthetase; Reviewed
 1-315 5.20e-121

carbamate kinase-like carbamoyl phosphate synthetase; Reviewed


Pssm-ID: 183535  Cd Length: 313  Bit Score: 350.07  E-value: 5.20e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308    1 MKELVVVAIGGNSIIKDNASQSIEHQAEAVKAVADTVLEMLASDYDIVLTHGNGPQVGLDLRRAEIAhKREGLPLTPLAN 80
Cdd:PRK12454   1 MKKRIVIALGGNALLQPGEKGTAENQMKNVRKTAKQIADLIEEGYEVVITHGNGPQVGNLLLQMDAA-KDVGIPPFPLDV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308   81 CVADTQGGIGYLIQQALNNRLARHG-EKKAVTVVTQVEVDKNDPGFAHPTKPIGAFFSDSQRDELQKANpDWCFVEDAGR 159
Cdd:PRK12454  80 AGAMTQGWIGYMIQQALRNELAKRGiEKQVATIVTQVIVDKNDPAFQNPTKPVGPFYDEEEAKKLAKEK-GWIVKEDAGR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308  160 GYRRVVASPEPKRIVEAPAIKALIQQGFVVIGAGGGGIPVVRTDaGDYQSVDAVIDKDLSTALLAREIHADILVITTGVE 239
Cdd:PRK12454 159 GWRRVVPSPDPLGIVEIEVIKALVENGFIVIASGGGGIPVIEED-GELKGVEAVIDKDLASELLAEELNADIFIILTDVE 237

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128308  240 KVCIHFGKPQQQALDRVDIATMTRYMQEGHFPPGSMLPKIIASLTFLEQGGKEVIITTPECLPAALRGETGTHIIK 315
Cdd:PRK12454 238 KVYLNYGKPDQKPLDKVTVEEAKKYYEEGHFKAGSMGPKILAAIRFVENGGKRAIIASLEKAVEALEGKTGTRIIP 313
PRK12686 PRK12686
carbamate kinase; Reviewed
 1-315 2.15e-120

carbamate kinase; Reviewed


Pssm-ID: 183683  Cd Length: 312  Bit Score: 348.18  E-value: 2.15e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308    1 MKELVVVAIGGNSIIKDNASqsIEHQAEAVKAVADTVLEMLASDYDIVLTHGNGPQVG-LDLRRAEIAhkREGLPLTPLA 79
Cdd:PRK12686   1 MKEKIVIALGGNAILQTEAT--AEAQQTAVREAAQHLVDLIEAGHDIVITHGNGPQVGnLLLQQAESN--SNKVPAMPLD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308   80 NCVADTQGGIGYLIQQALNNRLARHG-EKKAVTVVTQVEVDKNDPGFAHPTKPIGAFFSDSQRDELQKaNPDWCFVEDAG 158
Cdd:PRK12686  77 TCVAMSQGMIGYWLQNALNNELTERGiDKPVITLVTQVEVDKDDPAFANPTKPIGPFYTEEEAKQQAE-QPGSTFKEDAG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308  159 RGYRRVVASPEPKRIVEAPAIKALIQQGFVVIGAGGGGIPVVRTDAGdYQSVDAVIDKDLSTALLAREIHADILVITTGV 238
Cdd:PRK12686 156 RGYRRVVPSPKPQEIIEHDTIRTLVDGGNIVIACGGGGIPVIRDDNT-LKGVEAVIDKDFASEKLAEQIDADLLIILTGV 234

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128308  239 EKVCIHFGKPQQQALDRVDIATMTRYMQEGHFPPGSMLPKIIASLTFLEQG-GKEVIITTPECLPAALRGETGTHIIK 315
Cdd:PRK12686 235 ENVFINFNKPNQQKLDDITVAEAKQYIAEGQFAPGSMLPKVEAAIDFVESGeGKKAIITSLEQAKEALAGNAGTHITL 312
arcC TIGR00746
carbamate kinase; In most species, carbamate kinase works in arginine catabolism and consumes ...
 5-315 1.61e-99

carbamate kinase; In most species, carbamate kinase works in arginine catabolism and consumes carbamoyl phosphate to convert ADP into ATP. In the pathway in Pyrococcus furiosus, the enzyme acts instead to generate carbamoyl phosphate.The seed alignment for this model includes experimentally confirmed examples from a set of phylogenetically distinct species. In a neighbor-joining tree constructed from an alignment of candidate carbamate kinases and several acetylglutamate kinases, the latter group forms a clear outgroup which roots the tree of carbamate kinase-like proteins. This analysis suggests that in E. coli, the ArcC paralog YqeA may be a second isozyme, while the paralog YahI branches as an outlier and is less likely to be an authentic carbamate kinase. The homolog from Mycoplasma pneumoniae likewise branches outside the set containing known carbamate kinases and also scores below the trusted cutoff. [Energy metabolism, Amino acids and amines]


Pssm-ID: 273248  Cd Length: 310  Bit Score: 295.13  E-value: 1.61e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308     5 VVVAIGGNSIIKDNASQSIEHQAEAVKAVADTVLEMLASDYDIVLTHGNGPQVGLDLRRAEIAhkREGLPLTPLANCVAD 84
Cdd:TIGR00746   3 VVVALGGNALLQRGEKGSAEAQRDNVRQTAPQIAKLIKRGYELVITHGNGPQVGNLLLQNQAA--DSEVPAMPLDVLGAM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308    85 TQGGIGYLIQQALNNRLARHG-EKKAVTVVTQVEVDKNDPGFAHPTKPIGAFFSDsQRDELQKANPDWCFVEDAGRGYRR 163
Cdd:TIGR00746  81 SQGMIGYMLQQALNNELPKRGmEKPVATVLTQTIVDPKDPAFQNPTKPIGPFYTE-EEAKRLAAEKGWIVKEDAGRGWRR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308   164 VVASPEPKRIVEAPAIKALIQQGFVVIGAGGGGIPVVRTDAGdYQSVDAVIDKDLSTALLAREIHADILVITTGVEKVCI 243
Cdd:TIGR00746 160 VVPSPRPKDIVEAETIKTLVENGVIVISSGGGGVPVVLEGAE-LKGVEAVIDKDLASEKLAEEVNADILVILTDVDAVYI 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128308   244 HFGKPQQQALDRVDIATMTRYMQEGHFPPGSMLPKIIASLTFLEQGGKEVIITTPECLPAALRGETGTHIIK 315
Cdd:TIGR00746 239 NYGKPDEKALREVTVEELEDYYKAGHFAAGSMGPKVEAAIEFVESGGKRAIITSLENAVEALEGKAGTRVTK 310
PRK12354 PRK12354
carbamate kinase; Reviewed
 5-315 1.07e-87

carbamate kinase; Reviewed


Pssm-ID: 183466  Cd Length: 307  Bit Score: 264.77  E-value: 1.07e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308    5 VVVAIGGNSIIKDNASQSIEHQAEAVKAVADTVLEmLASDYDIVLTHGNGPQVGLDLRRAEIAHKREGLPLTPLancVAD 84
Cdd:PRK12354   3 IVVALGGNALLRRGEPLTAENQRANIRIAAEQIAK-IAREHELVIVHGNGPQVGLLALQNAAYKDVTPYPLDVL---GAE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308   85 TQGGIGYLIQQALNNRLarhGEKKAVTVVTQVEVDKNDPGFAHPTKPIGAFFSDSQRDELQKANpDWCFVEDaGRGYRRV 164
Cdd:PRK12354  79 TEGMIGYMLEQELGNLL---PERPVATLLTQVEVDANDPAFANPTKPIGPVYDEAEAERLAAEK-GWTIKPD-GDYFRRV 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308  165 VASPEPKRIVEAPAIKALIQQGFVVIGAGGGGIPVVRTDAGDYQSVDAVIDKDLSTALLAREIHADILVITTGVEKVCIH 244
Cdd:PRK12354 154 VPSPRPKRIVEIRPIRWLLEKGHLVICAGGGGIPVVYDADGKLHGVEAVIDKDLAAALLAEQLDADLLLILTDVDAVYLD 233

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128308  245 FGKPQQQALDRVDIATmtryMQEGHFPPGSMLPKIIASLTFLEQGGKEVIITTPECLPAALRGETGTHIIK 315
Cdd:PRK12354 234 WGKPTQRAIAQATPDE----LRELGFAAGSMGPKVEAACEFVRATGKIAGIGSLEDIQAILAGEAGTRISP 300
PRK09411 PRK09411
carbamate kinase; Reviewed
 1-315 1.44e-57

carbamate kinase; Reviewed


Pssm-ID: 181831  Cd Length: 297  Bit Score: 187.31  E-value: 1.44e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308    1 MKELVVvAIGGNSIIKDNASQSIEHQAEAVkAVADTVLEMLASDYDIVLTHGNGPQVGLdLRRAEIAHKreGLPLTPLAN 80
Cdd:PRK09411   1 MKTLVV-ALGGNALLQRGEALTAENQYRNI-ASAVPALARLARSYRLAIVHGNGPQVGL-LALQNLAWK--EVEPYPLDV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308   81 CVADTQGGIGYLIQQALNnrlARHGEKKAVTVVTQVEVDKNDPGFAHPTKPIGAFFSDSQRDELQKANpDWCFVEDaGRG 160
Cdd:PRK09411  76 LVAESQGMIGYMLAQSLS---AQPQMPPVTTVLTRIEVSPDDPAFLQPEKFIGPVYQPEEQEALEAAY-GWQMKRD-GKY 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308  161 YRRVVASPEPKRIVEAPAIKALIQQGFVVIGAGGGGIPVVRTDAGdyqsVDAVIDKDLSTALLAREIHADILVITTGVEK 240
Cdd:PRK09411 151 LRRVVASPQPRKILDSEAIELLLKEGHVVICSGGGGVPVTEDGAG----SEAVIDKDLAAALLAEQINADGLVILTDADA 226

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128308  241 VCIHFGKPQQQALDRV---DIATMTRymqeghfPPGSMLPKIIASLTFLEQGGKEVIITTPECLPAALRGETGTHIIK 315
Cdd:PRK09411 227 VYENWGTPQQRAIRHAtpdELAPFAK-------ADGAMGPKVTAVSGYVRSRGKPAWIGALSRIEETLAGEAGTCISL 297
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
 3-296 3.04e-10

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: 59.30  E-value: 3.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308     3 ELVVVAIGGNSIikdnasqsieHQAEAVKAVADTVLEMLASDYDIVLTHGNGPQVGLDLRRAEIAHKREGLPLTPLANCV 82
Cdd:pfam00696   1 KRVVIKLGGSSL----------TDKERLKRLADEIAALLEEGRKLVVVHGGGAFADGLLALLGLSPRFARLTDAETLEVA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308    83 ADTQGGIgylIQQALNNRLARHGEKKavtvvtqvevdkndpgfahptKPIGAFFSDSQRDELQKAnpdwcfvedagrgyr 162
Cdd:pfam00696  71 TMDALGS---LGERLNAALLAAGLPA---------------------VGLPAAQLLATEAGFIDD--------------- 111

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308   163 rvvaspePKRIVEAPAIKALIQQGFVVIGAGGggipvvrtDAGDYQSVDAVIDKDLSTALLAREIHADILVITTGVEKVC 242
Cdd:pfam00696 112 -------VVTRIDTEALEELLEAGVVPVITGF--------IGIDPEGELGRGSSDTLAALLAEALGADKLIILTDVDGVY 176

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 16128308   243 IHFGKPQQQA--LDRVDIATMTRYmQEGHFPPGSMLPKIIASLTFLEQGGKEVIIT 296
Cdd:pfam00696 177 TADPRKVPDAklIPEISYDELLEL-LASGLATGGMKVKLPAALEAARRGGIPVVIV 231
AAK cd02115
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ...
 6-313 2.60e-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: 44.74  E-value: 2.60e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308   6 VVAIGGNSIikdnasqsieHQAEAVKAVADTVLEMLASDYDIVLTHGNGPQVG-LDLRRAEIAHKREGLPLTPLAN--CV 82
Cdd:cd02115   1 VIKFGGSSV----------SSEERLRNLARILVKLASEGGRVVVVHGAGPQITdELLAHGELLGYARGLRITDRETdaLA 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308  83 ADTQGGIGYLIQQALNNRlarhgEKKAVTVVtqvevdkndpgfahptkPIGAFFSDSQRDELQKANPdwcfvEDAGRGYR 162
Cdd:cd02115  71 AMGEGMSNLLIAAALEQH-----GIKAVPLD-----------------LTQAGFASPNQGHVGKITK-----VSTDRLKS 123

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308 163 RVvaspEPKRIVEAPAIKALIQQGFvvigaggggipvvrtdagdyqSVDAVIDKDLSTALLAREIHADILVITTGVEKV- 241
Cdd:cd02115 124 LL----ENGILPILSGFGGTDEKET---------------------GTLGRGGSDSTAALLAAALKADRLVILTDVDGVy 178

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128308 242 -CIHFGKPQQQALDRVDIATMTRYMQEGHfppgsMLPKiIASLTFLEQGGKEVIITT---PECLPAALRGETGTHI 313
Cdd:cd02115 179 tADPRKVPDAKLLSELTYEEAAELAYAGA-----MVLK-PKAADPAARAGIPVRIANtenPGALALFTPDGGGTLI 248
AAK_NAGK-like cd04238
AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the ...
 5-313 1.79e-04

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: 42.11  E-value: 1.79e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308   5 VVVAIGGNSIIKDNASqsiehqaeavKAVADTVLEMLASDYDIVLTHGNGPQVGLDLRRAEI-AHKREGLPLTPlancvA 83
Cdd:cd04238   1 VVIKYGGSAMKDEELK----------EAFADDIVLLKQVGINPVIVHGGGPEINELLKRLGIeSEFVNGLRVTD-----K 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308  84 DT----QGGIGYLIQQALNNRLARHGeKKAV---------TVVTQVEVDKNDPGFahptkpIGaffsdsqrdELQKANPD 150
Cdd:cd04238  66 ETmeivEMVLAGKVNKELVSLLNRAG-GKAVglsgkdgglIKAEKKEEKDIDLGF------VG---------EVTEVNPE 129

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308 151 wcFVED-AGRGYRRVVASPepkriveapAIkaliqqgfvvigaggggipvvrTDAGDYQSVDAvidkDLSTALLAREIHA 229
Cdd:cd04238 130 --LLETlLEAGYIPVIAPI---------AV----------------------DEDGETYNVNA----DTAAGAIAAALKA 172

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308 230 DILVITTGVEKVCIHFGKPqqqaLDRVDIATMTRYMQEGHFPPGsMLPKIIASLTFLEQGGKEVII---TTPECLPAALR 306
Cdd:cd04238 173 EKLILLTDVPGVLDDPGSL----ISELTPKEAEELIEDGVISGG-MIPKVEAALEALEGGVRKVHIidgRVPHSLLLELF 247


                ....*....
gi 16128308 307 GE--TGTHI 313
Cdd:cd04238 248 TDegIGTMI 256
PRK14058 PRK14058
[LysW]-aminoadipate/[LysW]-glutamate kinase;
204-315 2.36e-04

[LysW]-aminoadipate/[LysW]-glutamate kinase;


Pssm-ID: 237599 [Multi-domain]  Cd Length: 268  Bit Score: 41.81  E-value: 2.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308  204 AGDYQSVDAVIDKDLSTALLAREIHADILVITTGVEKVCIHFGKPqQQALDRVDIATMTRYMQEGHfppGSMLPKIIASL 283
Cdd:PRK14058 158 ALSEEGEPLNVDGDRAAAAIAGALKAEALVLLSDVPGLLRDPPDE-GSLIERITPEEAEELSKAAG---GGMKKKVLMAA 233

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 16128308  284 TFLEQGGKEVIITT---PECLPAALRGEtGTHIIK 315
Cdd:PRK14058 234 EAVEGGVGRVIIADanvDDPISAALAGE-GTVIVN 267
AAK_NAGK-UC cd04251
AAK_NAGK-UC: N-Acetyl-L-glutamate kinase - uncharacterized (NAGK-UC). This domain is similar ...
 214-313 8.38e-04

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: 40.43  E-value: 8.38e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128308 214 IDKDLSTALLAREIHADILVITTGVEKVCIhfgkpQQQALDRVDIATMTRYMQEGHfppGSMLPKIIASLTFLEQGGKEV 293
Cdd:cd04251 164 VDGDRAAAAIAAALKAERLILLTDVEGLYL-----DGRVIERITVSDAESLLEKAG---GGMKRKLLAAAEAVEGGVREV 235

                        90       100
                ....*....|....*....|...
gi 16128308 294 II---TTPECLPAALRGeTGTHI 313
Cdd:cd04251 236 VIgdaRADSPISSALNG-GGTVI 257
PRK00942 PRK00942
acetylglutamate kinase; Provisional
 1-77 7.03e-03

acetylglutamate kinase; Provisional


Pssm-ID: 234869 [Multi-domain]  Cd Length: 283  Bit Score: 37.40  E-value: 7.03e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128308    1 MKELVVVAIGGNSIIKDNASqsiehqaeavKAVADTVLEMLASDYDIVLTHGNGPQVGLDLRRAEI-AHKREGLPLTP 77
Cdd:PRK00942  22 MGKTIVIKYGGNAMTDEELK----------EAFARDIVLLKQVGINPVVVHGGGPQIDELLKKLGIeSEFVNGLRVTD 89
 
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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