|
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: 628.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 1 MKELVVVAIGGNSIIKDNASQSIEHQAEAVKAVADTVLEMLASDYDIVLTHGNGPQVGLDLRRAEIAHEREGLPLTPLAN 80
Cdd:PRK12352 1 MKELVVVAIGGNSIIKDNASQSIEHQAEAVKAVADTVLEMLASDYDIVLTHGNGPQVGLDLRRAEIAHEREGLPLTPLAN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 81 CVADTQGGIGYLIQQALNNRLARHGEKKAVTVVTQVEVDKNDPGFAHPTKPIGAFFSESQRDKLQKANPDWCFVEDAGRG 160
Cdd:PRK12352 81 CVADTQGGIGYLIQQALNNRLARHGEKKAVTVVTQVEVDKNDPGFAHPTKPIGAFFSESQRDELQKANPDWRFVEDAGRG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 161 YRRVVASPEPKRIVEAPAIKALIQQGFVVIGAGGGGIPVVRTEAGDYQSVDAVIDKDLSTALLAREIHADILVITTGVEK 240
Cdd:PRK12352 161 YRRVVASPEPKRIVEAPAIKALIQQGFVVIGAGGGGIPVVRTDAGDYQSVDAVIDKDLSTALLAREIHADILVITTGVEK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446584303 241 VCIHFGKPQQQALDRVDIATMTRYMQEGHFPPGSMLPKIIASLTFLEQGGKEVIITTPECLPAALRGETGTHIIKT 316
Cdd:PRK12352 241 VCIHFGKPQQQALDRVDIATMTRYMQEGHFPPGSMLPKIIASLTFLEQGGKEVIITTPECLPAALRGETGTHIIKT 316
|
|
| ArcC |
COG0549 |
Carbamate kinase [Amino acid transport and metabolism]; |
1-315 |
3.35e-154 |
|
Carbamate kinase [Amino acid transport and metabolism];
Pssm-ID: 440315 Cd Length: 313 Bit Score: 434.12 E-value: 3.35e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 1 MKELVVVAIGGNSIIKDNASQSIEHQAEAVKAVADTVLEMLASDYDIVLTHGNGPQVGLDLRRAEIAHEreGLPLTPLAN 80
Cdd:COG0549 1 MKKRIVVALGGNALLRRGEPGTAEEQRENVREAAKALADLIEAGHEVVITHGNGPQVGLLLLQNEAAKK--KVPPMPLDV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 81 CVADTQGGIGYLIQQALNNRLARHG-EKKAVTVVTQVEVDKNDPGFAHPTKPIGAFFSESQRDKLQKaNPDWCFVEDAGR 159
Cdd:COG0549 79 CGAMTQGMIGYMLQQALRNELPKRGiDKPVATLVTQVEVDPDDPAFQNPTKPIGPFYTEEEAEELAK-EKGWTFKEDAGR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 160 GYRRVVASPEPKRIVEAPAIKALIQQgfvvigaggggipvvRTEAGDYQSVDAVIDKDLSTALLAREIHADILVITTGVE 239
Cdd:COG0549 158 GYRRVVPSPKPKRIVEIDAIKALLEAgviviaaggggipvvRDEDGGLKGVEAVIDKDLASALLAEELDADLLLILTDVD 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446584303 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 |
3.93e-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: 421.15 E-value: 3.93e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 4 LVVVAIGGNSIIKDNASQSIEHQAEAVKAVADTVLEMLASDYDIVLTHGNGPQVGLDLRRAEIAHEreGLPLTPLANCVA 83
Cdd:cd04235 1 RIVVALGGNALLRRGEPGTAEEQRENVKIAAKALADLIKNGHEVVITHGNGPQVGNLLLQNEAAAE--KVPAYPLDVCGA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 84 DTQGGIGYLIQQALNNRLARHG-EKKAVTVVTQVEVDKNDPGFAHPTKPIGAFFSESQRDKLQKANpDWCFVEDAGRGYR 162
Cdd:cd04235 79 MSQGMIGYMLQQALDNELPKRGiDKPVVTLVTQVVVDANDPAFKNPTKPIGPFYSEEEAEELAAEK-GWTFKEDAGRGYR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 163 RVVASPEPKRIVEAPAIKALIQQGFVVIGAGGGGIPVVRTEaGDYQSVDAVIDKDLSTALLAREIHADILVITTGVEKVC 242
Cdd:cd04235 158 RVVPSPKPKDIVEIEAIKTLVDNGVIVIAAGGGGIPVVREG-GGLKGVEAVIDKDLASALLAEEINADLLVILTDVDNVY 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446584303 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 |
2.51e-100 |
|
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: 297.45 E-value: 2.51e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 5 VVVAIGGNSIIKDNASQSIEHQAEAVKAVADTVLEMLASDYDIVLTHGNGPQVGLDLRRAEIAheREGLPLTPLANCVAD 84
Cdd:TIGR00746 3 VVVALGGNALLQRGEKGSAEAQRDNVRQTAPQIAKLIKRGYELVITHGNGPQVGNLLLQNQAA--DSEVPAMPLDVLGAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 85 TQGGIGYLIQQALNNRLARHG-EKKAVTVVTQVEVDKNDPGFAHPTKPIGAFFSEsQRDKLQKANPDWCFVEDAGRGYRR 163
Cdd:TIGR00746 81 SQGMIGYMLQQALNNELPKRGmEKPVATVLTQTIVDPKDPAFQNPTKPIGPFYTE-EEAKRLAAEKGWIVKEDAGRGWRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 164 VVASPEPKRIVEAPAIKALIQQGFVVIGAGGGGIPVVRTEAGdYQSVDAVIDKDLSTALLAREIHADILVITTGVEKVCI 243
Cdd:TIGR00746 160 VVPSPRPKDIVEAETIKTLVENGVIVISSGGGGVPVVLEGAE-LKGVEAVIDKDLASEKLAEEVNADILVILTDVDAVYI 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446584303 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 |
1.09e-09 |
|
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: 57.76 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 3 ELVVVAIGGNSIikdnasqsieHQAEAVKAVADTVLEMLASDYDIVLTHGNGPQVGLDLRRAEIAHEREGLPLTPLANCV 82
Cdd:pfam00696 1 KRVVIKLGGSSL----------TDKERLKRLADEIAALLEEGRKLVVVHGGGAFADGLLALLGLSPRFARLTDAETLEVA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 83 ADTQGGIgylIQQALNNRLARHGEKKavtvvtqvevdkndpgFAHPTKPIGAFFSESQRDKLQKANPDwcFVEDAGRGYR 162
Cdd:pfam00696 71 TMDALGS---LGERLNAALLAAGLPA----------------VGLPAAQLLATEAGFIDDVVTRIDTE--ALEELLEAGV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 163 RVVASPepkriveapaikaliqqgfvvigaggggiPVVRTEAGDYqsvdAVIDKDLSTALLAREIHADILVITTGVEKVC 242
Cdd:pfam00696 130 VPVITG-----------------------------FIGIDPEGEL----GRGSSDTLAALLAEALGADKLIILTDVDGVY 176
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 446584303 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: 628.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 1 MKELVVVAIGGNSIIKDNASQSIEHQAEAVKAVADTVLEMLASDYDIVLTHGNGPQVGLDLRRAEIAHEREGLPLTPLAN 80
Cdd:PRK12352 1 MKELVVVAIGGNSIIKDNASQSIEHQAEAVKAVADTVLEMLASDYDIVLTHGNGPQVGLDLRRAEIAHEREGLPLTPLAN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 81 CVADTQGGIGYLIQQALNNRLARHGEKKAVTVVTQVEVDKNDPGFAHPTKPIGAFFSESQRDKLQKANPDWCFVEDAGRG 160
Cdd:PRK12352 81 CVADTQGGIGYLIQQALNNRLARHGEKKAVTVVTQVEVDKNDPGFAHPTKPIGAFFSESQRDELQKANPDWRFVEDAGRG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 161 YRRVVASPEPKRIVEAPAIKALIQQGFVVIGAGGGGIPVVRTEAGDYQSVDAVIDKDLSTALLAREIHADILVITTGVEK 240
Cdd:PRK12352 161 YRRVVASPEPKRIVEAPAIKALIQQGFVVIGAGGGGIPVVRTDAGDYQSVDAVIDKDLSTALLAREIHADILVITTGVEK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446584303 241 VCIHFGKPQQQALDRVDIATMTRYMQEGHFPPGSMLPKIIASLTFLEQGGKEVIITTPECLPAALRGETGTHIIKT 316
Cdd:PRK12352 241 VCIHFGKPQQQALDRVDIATMTRYMQEGHFPPGSMLPKIIASLTFLEQGGKEVIITTPECLPAALRGETGTHIIKT 316
|
|
| ArcC |
COG0549 |
Carbamate kinase [Amino acid transport and metabolism]; |
1-315 |
3.35e-154 |
|
Carbamate kinase [Amino acid transport and metabolism];
Pssm-ID: 440315 Cd Length: 313 Bit Score: 434.12 E-value: 3.35e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 1 MKELVVVAIGGNSIIKDNASQSIEHQAEAVKAVADTVLEMLASDYDIVLTHGNGPQVGLDLRRAEIAHEreGLPLTPLAN 80
Cdd:COG0549 1 MKKRIVVALGGNALLRRGEPGTAEEQRENVREAAKALADLIEAGHEVVITHGNGPQVGLLLLQNEAAKK--KVPPMPLDV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 81 CVADTQGGIGYLIQQALNNRLARHG-EKKAVTVVTQVEVDKNDPGFAHPTKPIGAFFSESQRDKLQKaNPDWCFVEDAGR 159
Cdd:COG0549 79 CGAMTQGMIGYMLQQALRNELPKRGiDKPVATLVTQVEVDPDDPAFQNPTKPIGPFYTEEEAEELAK-EKGWTFKEDAGR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 160 GYRRVVASPEPKRIVEAPAIKALIQQgfvvigaggggipvvRTEAGDYQSVDAVIDKDLSTALLAREIHADILVITTGVE 239
Cdd:COG0549 158 GYRRVVPSPKPKRIVEIDAIKALLEAgviviaaggggipvvRDEDGGLKGVEAVIDKDLASALLAEELDADLLLILTDVD 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446584303 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 |
3.93e-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: 421.15 E-value: 3.93e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 4 LVVVAIGGNSIIKDNASQSIEHQAEAVKAVADTVLEMLASDYDIVLTHGNGPQVGLDLRRAEIAHEreGLPLTPLANCVA 83
Cdd:cd04235 1 RIVVALGGNALLRRGEPGTAEEQRENVKIAAKALADLIKNGHEVVITHGNGPQVGNLLLQNEAAAE--KVPAYPLDVCGA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 84 DTQGGIGYLIQQALNNRLARHG-EKKAVTVVTQVEVDKNDPGFAHPTKPIGAFFSESQRDKLQKANpDWCFVEDAGRGYR 162
Cdd:cd04235 79 MSQGMIGYMLQQALDNELPKRGiDKPVVTLVTQVVVDANDPAFKNPTKPIGPFYSEEEAEELAAEK-GWTFKEDAGRGYR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 163 RVVASPEPKRIVEAPAIKALIQQGFVVIGAGGGGIPVVRTEaGDYQSVDAVIDKDLSTALLAREIHADILVITTGVEKVC 242
Cdd:cd04235 158 RVVPSPKPKDIVEIEAIKTLVDNGVIVIAAGGGGIPVVREG-GGLKGVEAVIDKDLASALLAEEINADLLVILTDVDNVY 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446584303 243 IHFGKPQQQALDRVDIATMTRYMQEGHFPPGSMLPKIIASLTFLEQGGKEVIITTPECLPAALRGETGTHII 314
Cdd:cd04235 237 INFGKPNQKALEQVTVEELEKYIEEGQFAPGSMGPKVEAAIRFVESGGKKAIITSLENAEAALEGKAGTVIV 308
|
|
| PRK12353 |
PRK12353 |
putative amino acid kinase; Reviewed |
1-315 |
9.55e-140 |
|
putative amino acid kinase; Reviewed
Pssm-ID: 237071 Cd Length: 314 Bit Score: 397.22 E-value: 9.55e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 1 MKELVVVAIGGNSIIKDNasQSIEHQAEAVKAVADTVLEMLASDYDIVLTHGNGPQVGLDLRRAEIAHE-REGLPLTPLA 79
Cdd:PRK12353 1 MMKKIVVALGGNALGSTP--EEATAQLEAVKKTAKSLVDLIEEGHEVVITHGNGPQVGNILLAQEAAASeKNKVPAMPLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 80 NCVADTQGGIGYLIQQALNNRLARHG-EKKAVTVVTQVEVDKNDPGFAHPTKPIGAFFSESQRDKLQKANpDWCFVEDAG 158
Cdd:PRK12353 79 VCGAMSQGYIGYHLQNALRNELLKRGiDKPVATVVTQVVVDANDPAFKNPTKPIGPFYTEEEAEKLAKEK-GYTFKEDAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 159 RGYRRVVASPEPKRIVEAPAIKALIqqgfvvigaggggipvvrtEAG------------------DYQSVDAVIDKDLST 220
Cdd:PRK12353 158 RGYRRVVPSPKPVDIVEIEAIKTLV-------------------DAGqvviaaggggipvireggGLKGVEAVIDKDFAS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 221 ALLAREIHADILVITTGVEKVCIHFGKPQQQALDRVDIATMTRYMQEGHFPPGSMLPKIIASLTFL-EQGGKEVIITTPE 299
Cdd:PRK12353 219 AKLAELVDADLLIILTAVDKVYINFGKPNQKKLDEVTVSEAEKYIEEGQFAPGSMLPKVEAAISFVeSRPGRKAIITSLE 298
|
330
....*....|....*.
gi 446584303 300 CLPAALRGETGTHIIK 315
Cdd:PRK12353 299 KAKEALEGKAGTVIVK 314
|
|
| PRK12454 |
PRK12454 |
carbamate kinase-like carbamoyl phosphate synthetase; Reviewed |
1-315 |
5.91e-122 |
|
carbamate kinase-like carbamoyl phosphate synthetase; Reviewed
Pssm-ID: 183535 Cd Length: 313 Bit Score: 352.38 E-value: 5.91e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 1 MKELVVVAIGGNSIIKDNASQSIEHQAEAVKAVADTVLEMLASDYDIVLTHGNGPQVGLDLRRAEIAHErEGLPLTPLAN 80
Cdd:PRK12454 1 MKKRIVIALGGNALLQPGEKGTAENQMKNVRKTAKQIADLIEEGYEVVITHGNGPQVGNLLLQMDAAKD-VGIPPFPLDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 81 CVADTQGGIGYLIQQALNNRLARHG-EKKAVTVVTQVEVDKNDPGFAHPTKPIGAFFSESQRDKLQKANpDWCFVEDAGR 159
Cdd:PRK12454 80 AGAMTQGWIGYMIQQALRNELAKRGiEKQVATIVTQVIVDKNDPAFQNPTKPVGPFYDEEEAKKLAKEK-GWIVKEDAGR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 160 GYRRVVASPEPKRIVEAPAIKALIQQGFVVIGAGGGGIPVVRtEAGDYQSVDAVIDKDLSTALLAREIHADILVITTGVE 239
Cdd:PRK12454 159 GWRRVVPSPDPLGIVEIEVIKALVENGFIVIASGGGGIPVIE-EDGELKGVEAVIDKDLASELLAEELNADIFIILTDVE 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446584303 240 KVCIHFGKPQQQALDRVDIATMTRYMQEGHFPPGSMLPKIIASLTFLEQGGKEVIITTPECLPAALRGETGTHIIK 315
Cdd:PRK12454 238 KVYLNYGKPDQKPLDKVTVEEAKKYYEEGHFKAGSMGPKILAAIRFVENGGKRAIIASLEKAVEALEGKTGTRIIP 313
|
|
| PRK12686 |
PRK12686 |
carbamate kinase; Reviewed |
1-315 |
1.64e-121 |
|
carbamate kinase; Reviewed
Pssm-ID: 183683 Cd Length: 312 Bit Score: 351.26 E-value: 1.64e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 1 MKELVVVAIGGNSIIKDNASqsIEHQAEAVKAVADTVLEMLASDYDIVLTHGNGPQVG-LDLRRAEIAHERegLPLTPLA 79
Cdd:PRK12686 1 MKEKIVIALGGNAILQTEAT--AEAQQTAVREAAQHLVDLIEAGHDIVITHGNGPQVGnLLLQQAESNSNK--VPAMPLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 80 NCVADTQGGIGYLIQQALNNRLARHG-EKKAVTVVTQVEVDKNDPGFAHPTKPIGAFFSESQRDKLQKaNPDWCFVEDAG 158
Cdd:PRK12686 77 TCVAMSQGMIGYWLQNALNNELTERGiDKPVITLVTQVEVDKDDPAFANPTKPIGPFYTEEEAKQQAE-QPGSTFKEDAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 159 RGYRRVVASPEPKRIVEAPAIKALIQQGFVVIGAGGGGIPVVRtEAGDYQSVDAVIDKDLSTALLAREIHADILVITTGV 238
Cdd:PRK12686 156 RGYRRVVPSPKPQEIIEHDTIRTLVDGGNIVIACGGGGIPVIR-DDNTLKGVEAVIDKDFASEKLAEQIDADLLIILTGV 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446584303 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 |
2.51e-100 |
|
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: 297.45 E-value: 2.51e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 5 VVVAIGGNSIIKDNASQSIEHQAEAVKAVADTVLEMLASDYDIVLTHGNGPQVGLDLRRAEIAheREGLPLTPLANCVAD 84
Cdd:TIGR00746 3 VVVALGGNALLQRGEKGSAEAQRDNVRQTAPQIAKLIKRGYELVITHGNGPQVGNLLLQNQAA--DSEVPAMPLDVLGAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 85 TQGGIGYLIQQALNNRLARHG-EKKAVTVVTQVEVDKNDPGFAHPTKPIGAFFSEsQRDKLQKANPDWCFVEDAGRGYRR 163
Cdd:TIGR00746 81 SQGMIGYMLQQALNNELPKRGmEKPVATVLTQTIVDPKDPAFQNPTKPIGPFYTE-EEAKRLAAEKGWIVKEDAGRGWRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 164 VVASPEPKRIVEAPAIKALIQQGFVVIGAGGGGIPVVRTEAGdYQSVDAVIDKDLSTALLAREIHADILVITTGVEKVCI 243
Cdd:TIGR00746 160 VVPSPRPKDIVEAETIKTLVENGVIVISSGGGGVPVVLEGAE-LKGVEAVIDKDLASEKLAEEVNADILVILTDVDAVYI 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446584303 244 HFGKPQQQALDRVDIATMTRYMQEGHFPPGSMLPKIIASLTFLEQGGKEVIITTPECLPAALRGETGTHIIK 315
Cdd:TIGR00746 239 NYGKPDEKALREVTVEELEDYYKAGHFAAGSMGPKVEAAIEFVESGGKRAIITSLENAVEALEGKAGTRVTK 310
|
|
| PRK12354 |
PRK12354 |
carbamate kinase; Reviewed |
5-315 |
1.81e-88 |
|
carbamate kinase; Reviewed
Pssm-ID: 183466 Cd Length: 307 Bit Score: 266.70 E-value: 1.81e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 5 VVVAIGGNSIIKDNASQSIEHQAEAVKAVADTVLEmLASDYDIVLTHGNGPQVGLDLRRAEIAHEREGLPLTPLancVAD 84
Cdd:PRK12354 3 IVVALGGNALLRRGEPLTAENQRANIRIAAEQIAK-IAREHELVIVHGNGPQVGLLALQNAAYKDVTPYPLDVL---GAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 85 TQGGIGYLIQQALNNRLarhGEKKAVTVVTQVEVDKNDPGFAHPTKPIGAFFSESQRDKLQKANpDWCFVEDaGRGYRRV 164
Cdd:PRK12354 79 TEGMIGYMLEQELGNLL---PERPVATLLTQVEVDANDPAFANPTKPIGPVYDEAEAERLAAEK-GWTIKPD-GDYFRRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 165 VASPEPKRIVEAPAIKALIQQGFVVIGAGGGGIPVVRTEAGDYQSVDAVIDKDLSTALLAREIHADILVITTGVEKVCIH 244
Cdd:PRK12354 154 VPSPRPKRIVEIRPIRWLLEKGHLVICAGGGGIPVVYDADGKLHGVEAVIDKDLAAALLAEQLDADLLLILTDVDAVYLD 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446584303 245 FGKPQQQALDRVDIATmtryMQEGHFPPGSMLPKIIASLTFLEQGGKEVIITTPECLPAALRGETGTHIIK 315
Cdd:PRK12354 234 WGKPTQRAIAQATPDE----LRELGFAAGSMGPKVEAACEFVRATGKIAGIGSLEDIQAILAGEAGTRISP 300
|
|
| PRK09411 |
PRK09411 |
carbamate kinase; Reviewed |
1-315 |
3.91e-56 |
|
carbamate kinase; Reviewed
Pssm-ID: 181831 Cd Length: 297 Bit Score: 183.85 E-value: 3.91e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 1 MKELVVvAIGGNSIIKDNASQSIEHQAEAVkAVADTVLEMLASDYDIVLTHGNGPQVGLdLRRAEIAHEreGLPLTPLAN 80
Cdd:PRK09411 1 MKTLVV-ALGGNALLQRGEALTAENQYRNI-ASAVPALARLARSYRLAIVHGNGPQVGL-LALQNLAWK--EVEPYPLDV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 81 CVADTQGGIGYLIQQALNnrlARHGEKKAVTVVTQVEVDKNDPGFAHPTKPIGAFFSESQRDKLQKANpDWCFVEDaGRG 160
Cdd:PRK09411 76 LVAESQGMIGYMLAQSLS---AQPQMPPVTTVLTRIEVSPDDPAFLQPEKFIGPVYQPEEQEALEAAY-GWQMKRD-GKY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 161 YRRVVASPEPKRIVEAPAIKALIQQGFVVIGAGGGGIPVVRTEAGdyqsVDAVIDKDLSTALLAREIHADILVITTGVEK 240
Cdd:PRK09411 151 LRRVVASPQPRKILDSEAIELLLKEGHVVICSGGGGVPVTEDGAG----SEAVIDKDLAAALLAEQINADGLVILTDADA 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446584303 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 |
1.09e-09 |
|
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: 57.76 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 3 ELVVVAIGGNSIikdnasqsieHQAEAVKAVADTVLEMLASDYDIVLTHGNGPQVGLDLRRAEIAHEREGLPLTPLANCV 82
Cdd:pfam00696 1 KRVVIKLGGSSL----------TDKERLKRLADEIAALLEEGRKLVVVHGGGAFADGLLALLGLSPRFARLTDAETLEVA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 83 ADTQGGIgylIQQALNNRLARHGEKKavtvvtqvevdkndpgFAHPTKPIGAFFSESQRDKLQKANPDwcFVEDAGRGYR 162
Cdd:pfam00696 71 TMDALGS---LGERLNAALLAAGLPA----------------VGLPAAQLLATEAGFIDDVVTRIDTE--ALEELLEAGV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 163 RVVASPepkriveapaikaliqqgfvvigaggggiPVVRTEAGDYqsvdAVIDKDLSTALLAREIHADILVITTGVEKVC 242
Cdd:pfam00696 130 VPVITG-----------------------------FIGIDPEGEL----GRGSSDTLAALLAEALGADKLIILTDVDGVY 176
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 446584303 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 |
4.26e-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: 43.97 E-value: 4.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 6 VVAIGGNSIikdnasqsieHQAEAVKAVADTVLEMLASDYDIVLTHGNGPQVG-LDLRRAEIAHEREGLPLTPLAN--CV 82
Cdd:cd02115 1 VIKFGGSSV----------SSEERLRNLARILVKLASEGGRVVVVHGAGPQITdELLAHGELLGYARGLRITDRETdaLA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 83 ADTQGGIGYLIQQALNNRlarhgEKKAVTV-VTQVEVDKNDPGFAHPTKPIgaffsesqrdklqkanpdwcfveDAGRGY 161
Cdd:cd02115 71 AMGEGMSNLLIAAALEQH-----GIKAVPLdLTQAGFASPNQGHVGKITKV-----------------------STDRLK 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 162 RRVvaspEPKRIVEAPAIKALIQQGFvvigaggggipvvrteagdyqSVDAVIDKDLSTALLAREIHADILVITTGVEKV 241
Cdd:cd02115 123 SLL----ENGILPILSGFGGTDEKET---------------------GTLGRGGSDSTAALLAAALKADRLVILTDVDGV 177
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446584303 242 --CIHFGKPQQQALDRVDIATMTRYMQEGHfppgsMLPKiIASLTFLEQGGKEVIITT---PECLPAALRGETGTHI 313
Cdd:cd02115 178 ytADPRKVPDAKLLSELTYEEAAELAYAGA-----MVLK-PKAADPAARAGIPVRIANtenPGALALFTPDGGGTLI 248
|
|
| PRK14058 |
PRK14058 |
[LysW]-aminoadipate/[LysW]-glutamate kinase; |
204-315 |
2.41e-04 |
|
[LysW]-aminoadipate/[LysW]-glutamate kinase;
Pssm-ID: 237599 [Multi-domain] Cd Length: 268 Bit Score: 41.81 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 204 AGDYQSVDAVIDKDLSTALLAREIHADILVITTGVEKVCIHFGKPqQQALDRVDIATMTRYMQEGHfppGSMLPKIIASL 283
Cdd:PRK14058 158 ALSEEGEPLNVDGDRAAAAIAGALKAEALVLLSDVPGLLRDPPDE-GSLIERITPEEAEELSKAAG---GGMKKKVLMAA 233
|
90 100 110
....*....|....*....|....*....|....*
gi 446584303 284 TFLEQGGKEVIITT---PECLPAALRGEtGTHIIK 315
Cdd:PRK14058 234 EAVEGGVGRVIIADanvDDPISAALAGE-GTVIVN 267
|
|
| AAK_NAGK-like |
cd04238 |
AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the ... |
214-313 |
5.49e-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: 40.96 E-value: 5.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584303 214 IDKDLSTALLAREIHADILVITTGVEKVCIHFGKPqqqaLDRVDIATMTRYMQEGHFPPGsMLPKIIASLTFLEQGGKEV 293
Cdd:cd04238 157 VNADTAAGAIAAALKAEKLILLTDVPGVLDDPGSL----ISELTPKEAEELIEDGVISGG-MIPKVEAALEALEGGVRKV 231
|
90 100
....*....|....*....|....*
gi 446584303 294 II---TTPECLPAALRGE--TGTHI 313
Cdd:cd04238 232 HIidgRVPHSLLLELFTDegIGTMI 256
|
|
| 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 446584303 214 IDKDLSTALLAREIHADILVITTGVEKVCIhfgkpQQQALDRVDIATMTRYMQEGHfppGSMLPKIIASLTFLEQGGKEV 293
Cdd:cd04251 164 VDGDRAAAAIAAALKAERLILLTDVEGLYL-----DGRVIERITVSDAESLLEKAG---GGMKRKLLAAAEAVEGGVREV 235
|
90 100
....*....|....*....|...
gi 446584303 294 II---TTPECLPAALRGeTGTHI 313
Cdd:cd04251 236 VIgdaRADSPISSALNG-GGTVI 257
|
|
| |
