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Conserved domains on  [gi|972905635|gb|ALW83425|]
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arginine kinase, partial [Bembidion (Eupetedromus) sp. 'Inuvik']

Protein Classification

ATP--guanido phosphotransferase( domain architecture ID 3111)

ATP--guanido phosphotransferase reversibly catalyzes the transfer of phosphate between ATP and various phosphogens; similar to Arenicola marina taurocyamine kinase that catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate)

EC:  2.7.3.-
Gene Ontology:  GO:0046314|GO:0005524

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
phosphagen_kinases super family cl02823
Phosphagen (guanidino) kinases; Phosphagen (guanidino) kinases are enzymes that ...
1-195 9.96e-148

Phosphagen (guanidino) kinases; Phosphagen (guanidino) kinases are enzymes that transphosphorylate a high energy phosphoguanidino compound, like phosphocreatine (PCr) in the case of creatine kinase (CK) or phosphoarginine in the case of arginine kinase, which is used as an energy-storage and -transport metabolite, to ADP, thereby creating ATP. The substrate binding site is located in the cleft between the N and C-terminal domains, but most of the catalytic residues are found in the larger C-terminal domain. In higher eukaryotes, CK exists in tissue-specific (muscle, brain), as well as compartment-specific (mitochondrial and cytosolic) isoforms. They are either coupled to glycolysis (cytosolic form) or oxidative phosphorylation (mitochondrial form). Besides CK and AK, the most studied members of this family are also other phosphagen kinases with different substrate specificities, like glycocyamine kinase (GK), lombricine kinase (LK), taurocyamine kinase (TK) and hypotaurocyamine kinase (HTK). The majority of bacterial phosphagen kinases appear to lack the N-terminal domain and have not been functionally characterized.


The actual alignment was detected with superfamily member cd07932:

Pssm-ID: 470681 [Multi-domain]  Cd Length: 350  Bit Score: 413.63  E-value: 9.96e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972905635   1 GNVDPTGEYVVSTRVRCGRSMEGYPFNPCLTEEQYKEMEQKVSTTLNGLEGELKGTFFPLTGMSKDVQQKLIDDHFLFKE 80
Cdd:cd07932  105 GNLDPEGKYVISTRVRCGRSVEGYPFNPCLTKEQYIEMEEKVKSALETLTGELAGTYYPLTGMDKETQQQLIDDHFLFKE 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972905635  81 GDRFLQAANACRFWPSGRGIFHNDTKTFLVWCNEEDHLRLISMQMGGDLGQVYRRLVTAVNDIEKRVPFSHHDRLGFLTF 160
Cdd:cd07932  185 GDRFLQAAGGYRFWPTGRGIFHNDDKTFLVWVNEEDHLRIISMQKGGDLGAVYKRLVTALKELEKKLPFARDDRLGYLTF 264
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 972905635 161 CPTNLGTTVRASVHIKVPKLAANKAKLEEVAAKYN 195
Cdd:cd07932  265 CPTNLGTTLRASVHIKLPKLSKDPPRLKEICEKYN 299
 
Name Accession Description Interval E-value
arginine_kinase_like cd07932
Phosphagen (guanidino) kinases such as arginine kinase and similar enzymes; Eukaryotic ...
1-195 9.96e-148

Phosphagen (guanidino) kinases such as arginine kinase and similar enzymes; Eukaryotic arginine kinase-like phosphagen (guanidino) kinases are enzymes that transphosphorylate a high energy phosphoguanidino compound, like phosphoarginine in the case of arginine kinase (AK), which is used as an energy-storage and -transport metabolite, to ADP, thereby creating ATP. The substrate binding site is located in the cleft between the N and C-terminal domains, but most of the catalytic residues are found in the larger C-terminal domain. Besides AK, one of the most studied members of this family, this model also represents a phosphagen kinase with different substrate specificity, hypotaurocyamine kinase (HTK).


Pssm-ID: 153079 [Multi-domain]  Cd Length: 350  Bit Score: 413.63  E-value: 9.96e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972905635   1 GNVDPTGEYVVSTRVRCGRSMEGYPFNPCLTEEQYKEMEQKVSTTLNGLEGELKGTFFPLTGMSKDVQQKLIDDHFLFKE 80
Cdd:cd07932  105 GNLDPEGKYVISTRVRCGRSVEGYPFNPCLTKEQYIEMEEKVKSALETLTGELAGTYYPLTGMDKETQQQLIDDHFLFKE 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972905635  81 GDRFLQAANACRFWPSGRGIFHNDTKTFLVWCNEEDHLRLISMQMGGDLGQVYRRLVTAVNDIEKRVPFSHHDRLGFLTF 160
Cdd:cd07932  185 GDRFLQAAGGYRFWPTGRGIFHNDDKTFLVWVNEEDHLRIISMQKGGDLGAVYKRLVTALKELEKKLPFARDDRLGYLTF 264
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 972905635 161 CPTNLGTTVRASVHIKVPKLAANKAKLEEVAAKYN 195
Cdd:cd07932  265 CPTNLGTTLRASVHIKLPKLSKDPPRLKEICEKYN 299
ATP-gua_Ptrans pfam00217
ATP:guanido phosphotransferase, C-terminal catalytic domain; The substrate binding site is ...
37-195 4.06e-76

ATP:guanido phosphotransferase, C-terminal catalytic domain; The substrate binding site is located in the cleft between N and C-terminal domains, but most of the catalytic residues are found in the larger C-terminal domain.


Pssm-ID: 459716  Cd Length: 203  Bit Score: 227.04  E-value: 4.06e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972905635   37 EMEQKVSTTLNGLEGELKGTFFPLTGMSKDVQQKLIDDHFLFkegdrflqaANACRFWPSGRGIFHNDTKTFLVWCNEED 116
Cdd:pfam00217   1 EVEELVVDALESLSGDLKGKYYPLTEMDPEERQQLVEKHLIS---------PGLARDWPDGRGIFINEDETFSIWVNEED 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972905635  117 HLRLISMQMGGDLGQVYRRLVTAVNDIEKRVPFSHHDRLGFLTFCPTNLGTTVRASVHIKVPKLAANK--AKLEEVAAKY 194
Cdd:pfam00217  72 HLRIISMEPGGDLGEVYERANRGDDLLEEKLDFAFDERLGYLTSCPTNLGTGLRASVMIHLPALSKTNqiNRLLEALKKL 151

                  .
gi 972905635  195 N 195
Cdd:pfam00217 152 G 152
McsB COG3869
Protein-arginine kinase McsB [Posttranslational modification, protein turnover, chaperones];
5-184 1.55e-32

Protein-arginine kinase McsB [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443078  Cd Length: 353  Bit Score: 119.51  E-value: 1.55e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972905635   5 PTGEYVVSTRVRCGRSMEGYPFNPCLTEEQYKEMEQKVSTTLNGLEGELKG--TFFPLTGMSKDVQQKLIDDHFLFKEgd 82
Cdd:COG3869   19 PESDIVLSSRIRLARNLAGFPFPHRASEEEAEQVLSLVREALLSLSFQELGkfELIKLEDLSPLERQVLVEKHLISPE-- 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972905635  83 rFLQAanacrfwPSGRGIFHNDTKTFLVWCNEEDHLRLISMQMGGDLGQVYRRLVTAVNDIEKRVPFSHHDRLGFLTFCP 162
Cdd:COG3869   97 -LAEN-------PGGRAVLLSEDESVSIMVNEEDHLRIQCLLPGLQLEEAWELANKIDDALEEKLDYAFDEKFGYLTSCP 168
                        170       180
                 ....*....|....*....|..
gi 972905635 163 TNLGTTVRASVHIKVPKLAANK 184
Cdd:COG3869  169 TNVGTGLRASVMLHLPALVLTG 190
PRK01059 PRK01059
ATP:guanido phosphotransferase; Provisional
10-184 2.03e-31

ATP:guanido phosphotransferase; Provisional


Pssm-ID: 234894 [Multi-domain]  Cd Length: 346  Bit Score: 116.46  E-value: 2.03e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972905635  10 VVSTRVRCGRSMEGYPFNPCLTEEQYKEMEQKVSTTLNGLEGELKGTFF--PLTGMSKDVQQKLIDDHFLFKEgdrFLQA 87
Cdd:PRK01059  22 VLSSRIRLARNLKDIPFPNKLSEEEARDIIELVEKAFLNNEIEGFGEFEllKLKDLDPLEKEVLVEKHLISPD---LAEN 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972905635  88 anacrfwPSGRGIFHNDTKTFLVWCNEEDHLRLISMQMGGDLGQVYRRLVTAVNDIEKRVPFSHHDRLGFLTFCPTNLGT 167
Cdd:PRK01059  99 -------PEGGAVLLNEDETISIMINEEDHLRIQCIDPGLQLEEALEKANQIDDLLEEKLDYAFDEKLGYLTSCPTNVGT 171
                        170
                 ....*....|....*..
gi 972905635 168 TVRASVHIKVPKLAANK 184
Cdd:PRK01059 172 GLRASVMLHLPALVLTK 188
 
Name Accession Description Interval E-value
arginine_kinase_like cd07932
Phosphagen (guanidino) kinases such as arginine kinase and similar enzymes; Eukaryotic ...
1-195 9.96e-148

Phosphagen (guanidino) kinases such as arginine kinase and similar enzymes; Eukaryotic arginine kinase-like phosphagen (guanidino) kinases are enzymes that transphosphorylate a high energy phosphoguanidino compound, like phosphoarginine in the case of arginine kinase (AK), which is used as an energy-storage and -transport metabolite, to ADP, thereby creating ATP. The substrate binding site is located in the cleft between the N and C-terminal domains, but most of the catalytic residues are found in the larger C-terminal domain. Besides AK, one of the most studied members of this family, this model also represents a phosphagen kinase with different substrate specificity, hypotaurocyamine kinase (HTK).


Pssm-ID: 153079 [Multi-domain]  Cd Length: 350  Bit Score: 413.63  E-value: 9.96e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972905635   1 GNVDPTGEYVVSTRVRCGRSMEGYPFNPCLTEEQYKEMEQKVSTTLNGLEGELKGTFFPLTGMSKDVQQKLIDDHFLFKE 80
Cdd:cd07932  105 GNLDPEGKYVISTRVRCGRSVEGYPFNPCLTKEQYIEMEEKVKSALETLTGELAGTYYPLTGMDKETQQQLIDDHFLFKE 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972905635  81 GDRFLQAANACRFWPSGRGIFHNDTKTFLVWCNEEDHLRLISMQMGGDLGQVYRRLVTAVNDIEKRVPFSHHDRLGFLTF 160
Cdd:cd07932  185 GDRFLQAAGGYRFWPTGRGIFHNDDKTFLVWVNEEDHLRIISMQKGGDLGAVYKRLVTALKELEKKLPFARDDRLGYLTF 264
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 972905635 161 CPTNLGTTVRASVHIKVPKLAANKAKLEEVAAKYN 195
Cdd:cd07932  265 CPTNLGTTLRASVHIKLPKLSKDPPRLKEICEKYN 299
eukaryotic_phosphagen_kinases cd07931
Phosphagen (guanidino) kinases mostly found in eukaryotes; Phosphagen (guanidino) kinases are ...
1-195 3.74e-105

Phosphagen (guanidino) kinases mostly found in eukaryotes; Phosphagen (guanidino) kinases are enzymes that transphosphorylate a high energy phosphoguanidino compound, like phosphocreatine (PCr) in the case of creatine kinase (CK) or phosphoarginine in the case of arginine kinase, which is used as an energy-storage and -transport metabolite, to ADP, thereby creating ATP. The substrate binding site is located in the cleft between the N and C-terminal domains, but most of the catalytic residues are found in the larger C-terminal domain. In higher eukaryotes, CK exists in tissue-specific (muscle, brain), as well as compartment-specific (mitochondrial and cytosolic) isoforms. They are either coupled to glycolysis (cytosolic form) or oxidative phosphorylation (mitochondrial form). Besides CK and AK, the most studied members of this family are also other phosphagen kinases with different substrate specificities, like glycocyamine kinase (GK), lombricine kinase (LK), taurocyamine kinase (TK) and hypotaurocyamine kinase (HTK).


Pssm-ID: 153078 [Multi-domain]  Cd Length: 338  Bit Score: 305.35  E-value: 3.74e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972905635   1 GNVDPTGEYVVSTRVRCGRSMEGYPFNPCLTEEQYKEMEQKVSTTLNGLEGELKGTFFPLTGMSKDVQQKLIDDHFLFKE 80
Cdd:cd07931   92 EDLDPRKKYIISTRIRVARNLDGFPLPPGMTKEQRRQIERLMVSALSSLEGDLKGTYYSLTEMTEEQQQQLIDDHFLFKD 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972905635  81 GDRFLQAANACRFWPSGRGIFHNDTKTFLVWCNEEDHLRLISMQMGGDLGQVYRRLVTAVNDIEKRVP--FSHHDRLGFL 158
Cdd:cd07931  172 GDRFLEAAGENRDWPDGRGIFHNSDKTFLVWVNEEDHLRIISMQKGGDLKAVFTRLSRALTEIEKSLKeeFAHDPHLGYI 251
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 972905635 159 TFCPTNLGTTVRASVHIKVPKLAANKAKLEEVAAKYN 195
Cdd:cd07931  252 TSCPTNLGTGMRASVHVKLPNLIKDMDKLKAIARKLG 288
phosphagen_kinases cd00330
Phosphagen (guanidino) kinases; Phosphagen (guanidino) kinases are enzymes that ...
10-195 1.79e-99

Phosphagen (guanidino) kinases; Phosphagen (guanidino) kinases are enzymes that transphosphorylate a high energy phosphoguanidino compound, like phosphocreatine (PCr) in the case of creatine kinase (CK) or phosphoarginine in the case of arginine kinase, which is used as an energy-storage and -transport metabolite, to ADP, thereby creating ATP. The substrate binding site is located in the cleft between the N and C-terminal domains, but most of the catalytic residues are found in the larger C-terminal domain. In higher eukaryotes, CK exists in tissue-specific (muscle, brain), as well as compartment-specific (mitochondrial and cytosolic) isoforms. They are either coupled to glycolysis (cytosolic form) or oxidative phosphorylation (mitochondrial form). Besides CK and AK, the most studied members of this family are also other phosphagen kinases with different substrate specificities, like glycocyamine kinase (GK), lombricine kinase (LK), taurocyamine kinase (TK) and hypotaurocyamine kinase (HTK). The majority of bacterial phosphagen kinases appear to lack the N-terminal domain and have not been functionally characterized.


Pssm-ID: 153075  Cd Length: 236  Bit Score: 287.56  E-value: 1.79e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972905635  10 VVSTRVRCGRSMEGYPFNPCLTEEQYKEMEQKVSTTLNGLEGELKGTFFPLTGMSKDVQQKLIDDHFLFKEGDRFLQAAN 89
Cdd:cd00330    1 VLSSRVRLGRSFEGIRFPPRYSNEEASSIEQQFEDQLSSQEIPLIGKYYLLRMMDPAEQQQLIDDHFLFPNLTRFLQTAN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972905635  90 ACRFWPSGRGIFHNDTKTFLVWCNEEDHLRLISMQMGGDLGQVYRRLVTAVNDIEKRVPFSHHDRLGFLTFCPTNLGTTV 169
Cdd:cd00330   81 ACREWPFGRGILHNDEKTFLVWVNEEDHLRIISMQKGGQLKEVMKRANTVDDWIEEKVDFAFNEQRGYLTSCPTNLGTGL 160
                        170       180
                 ....*....|....*....|....*.
gi 972905635 170 RASVHIKVPKLAANKAKLEEVAAKYN 195
Cdd:cd00330  161 RASVHIHLPALVKTINRIIPAINQLG 186
creatine_kinase_like cd00716
Phosphagen (guanidino) kinases such as creatine kinase and similar enzymes; Eukaryotic ...
1-193 5.97e-79

Phosphagen (guanidino) kinases such as creatine kinase and similar enzymes; Eukaryotic creatine kinase-like phosphagen (guanidino) kinases are enzymes that transphosphorylate a high energy phosphoguanidino compound, like phosphocreatine (PCr) in the case of creatine kinase (CK), which is used as an energy-storage and -transport metabolite, to ADP, thereby creating ATP. The substrate binding site is located in the cleft between the N and C-terminal domains, but most of the catalytic residues are found in the larger C-terminal domain. In higher eukaryotes, CKs are found as tissue-specific (muscle, brain), as well as compartment-specific (mitochondrial, cytosolic, and flagellar) isoforms. Mitochondrial and cytoplasmic CKs are dimeric or octameric, while the flagellar isoforms are trimers with three CD domains fused as a single protein chain. CKs are either coupled to glycolysis (cytosolic form) or oxidative phosphorylation (mitochondrial form). Besides CK, one of the most studied members of this family, this model also represents other phosphagen kinases with different substrate specificities, like glycocyamine kinase (GK), lombricine kinase (LK), taurocyamine kinase (TK), and echinoderm arginine kinase (AK).


Pssm-ID: 153076 [Multi-domain]  Cd Length: 357  Bit Score: 239.55  E-value: 5.97e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972905635   1 GNVDPTgeYVVSTRVRCGRSMEGYPFNPCLTEEQYKEMEQKVSTTLNGLEGELKGTFFPLTGMSKDVQQKLIDDHFLFKE 80
Cdd:cd00716  103 GQFDPK--YVLSSRVRTGRSIRGFCLPPHCSRAERREVEKIAVEALASLDGDLKGKYYPLSGMTEEEQQQLIEDHFLFDK 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972905635  81 GD-RFLQAANACRFWPSGRGIFHNDTKTFLVWCNEEDHLRLISMQMGGDLGQVYRRLVTAVNDIEKRVP-----FSHHDR 154
Cdd:cd00716  181 PVsPLLLSSGMARDWPDARGIWHNDDKTFLVWVNEEDHLRVISMQKGGDMKAVFARFCRGLTEVEKLMKkkgyeFMWNEH 260
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 972905635 155 LGFLTFCPTNLGTTVRASVHIKVPKLAANKaKLEEVAAK 193
Cdd:cd00716  261 LGYVLTCPSNLGTGLRASVHVKLPNLSKDP-RFDEILRK 298
ATP-gua_Ptrans pfam00217
ATP:guanido phosphotransferase, C-terminal catalytic domain; The substrate binding site is ...
37-195 4.06e-76

ATP:guanido phosphotransferase, C-terminal catalytic domain; The substrate binding site is located in the cleft between N and C-terminal domains, but most of the catalytic residues are found in the larger C-terminal domain.


Pssm-ID: 459716  Cd Length: 203  Bit Score: 227.04  E-value: 4.06e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972905635   37 EMEQKVSTTLNGLEGELKGTFFPLTGMSKDVQQKLIDDHFLFkegdrflqaANACRFWPSGRGIFHNDTKTFLVWCNEED 116
Cdd:pfam00217   1 EVEELVVDALESLSGDLKGKYYPLTEMDPEERQQLVEKHLIS---------PGLARDWPDGRGIFINEDETFSIWVNEED 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972905635  117 HLRLISMQMGGDLGQVYRRLVTAVNDIEKRVPFSHHDRLGFLTFCPTNLGTTVRASVHIKVPKLAANK--AKLEEVAAKY 194
Cdd:pfam00217  72 HLRIISMEPGGDLGEVYERANRGDDLLEEKLDFAFDERLGYLTSCPTNLGTGLRASVMIHLPALSKTNqiNRLLEALKKL 151

                  .
gi 972905635  195 N 195
Cdd:pfam00217 152 G 152
bacterial_phosphagen_kinase cd07930
Phosphagen (guanidino) kinases found in bacteria; Phosphagen (guanidino) kinases are enzymes ...
10-184 2.06e-34

Phosphagen (guanidino) kinases found in bacteria; Phosphagen (guanidino) kinases are enzymes that transphosphorylate a high energy phosphoguanidino compound, such as phosphocreatine (PCr) or phosphoarginine, which is used as an energy-storage and -transport metabolite, to ADP, thereby creating ATP. This subfamily is specific to bacteria and lacks an N-terminal domain, which otherwise forms part of the substrate binding site. Most of the catalytic residues are found in the larger C-terminal domain, however, which appears conserved in these bacterial proteins. Their functions have not been characterized.


Pssm-ID: 153077  Cd Length: 232  Bit Score: 121.46  E-value: 2.06e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972905635  10 VVSTRVRCGRSMEGYPFNPCLTEEQYKEMEQKVSTTLNGLEGELKGTFFPLTGMSKDVQQKLIDDHFLFKEgdrflQAAN 89
Cdd:cd07930    4 VISSRIRLARNLKGYPFPNKLSEEQAADVLEKVEKALSNIEDKDEFELLKLKDLDPLERQVLVEKHLISPE-----LAEN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972905635  90 acrfwPSGRGIFHNDTKTFLVWCNEEDHLRLISMQMGGDLGQVYRRLVTAVNDIEKRVPFSHHDRLGFLTFCPTNLGTTV 169
Cdd:cd07930   79 -----KEGGAVIVNEDETVSIMINEEDHLRIQCLLPGLQLEEAYERADKIDDLLEEKLDYAFDEKLGYLTACPTNVGTGL 153
                        170
                 ....*....|....*
gi 972905635 170 RASVHIKVPKLAANK 184
Cdd:cd07930  154 RASVMLHLPALVLTG 168
McsB COG3869
Protein-arginine kinase McsB [Posttranslational modification, protein turnover, chaperones];
5-184 1.55e-32

Protein-arginine kinase McsB [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443078  Cd Length: 353  Bit Score: 119.51  E-value: 1.55e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972905635   5 PTGEYVVSTRVRCGRSMEGYPFNPCLTEEQYKEMEQKVSTTLNGLEGELKG--TFFPLTGMSKDVQQKLIDDHFLFKEgd 82
Cdd:COG3869   19 PESDIVLSSRIRLARNLAGFPFPHRASEEEAEQVLSLVREALLSLSFQELGkfELIKLEDLSPLERQVLVEKHLISPE-- 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972905635  83 rFLQAanacrfwPSGRGIFHNDTKTFLVWCNEEDHLRLISMQMGGDLGQVYRRLVTAVNDIEKRVPFSHHDRLGFLTFCP 162
Cdd:COG3869   97 -LAEN-------PGGRAVLLSEDESVSIMVNEEDHLRIQCLLPGLQLEEAWELANKIDDALEEKLDYAFDEKFGYLTSCP 168
                        170       180
                 ....*....|....*....|..
gi 972905635 163 TNLGTTVRASVHIKVPKLAANK 184
Cdd:COG3869  169 TNVGTGLRASVMLHLPALVLTG 190
PRK01059 PRK01059
ATP:guanido phosphotransferase; Provisional
10-184 2.03e-31

ATP:guanido phosphotransferase; Provisional


Pssm-ID: 234894 [Multi-domain]  Cd Length: 346  Bit Score: 116.46  E-value: 2.03e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972905635  10 VVSTRVRCGRSMEGYPFNPCLTEEQYKEMEQKVSTTLNGLEGELKGTFF--PLTGMSKDVQQKLIDDHFLFKEgdrFLQA 87
Cdd:PRK01059  22 VLSSRIRLARNLKDIPFPNKLSEEEARDIIELVEKAFLNNEIEGFGEFEllKLKDLDPLEKEVLVEKHLISPD---LAEN 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972905635  88 anacrfwPSGRGIFHNDTKTFLVWCNEEDHLRLISMQMGGDLGQVYRRLVTAVNDIEKRVPFSHHDRLGFLTFCPTNLGT 167
Cdd:PRK01059  99 -------PEGGAVLLNEDETISIMINEEDHLRIQCIDPGLQLEEALEKANQIDDLLEEKLDYAFDEKLGYLTSCPTNVGT 171
                        170
                 ....*....|....*..
gi 972905635 168 TVRASVHIKVPKLAANK 184
Cdd:PRK01059 172 GLRASVMLHLPALVLTK 188
 
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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