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Conserved domains on  [gi|972905631|gb|ALW83423|]
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arginine kinase, partial [Bembidion sp. 'Desert Spotted']

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 ...
 1-121 1.11e-44

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: 148.23  E-value: 1.11e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972905631   1 FLFKEGDRFLQAANACRFWPSGRGIFHNDTKTFLVW*NEEDHJRIISMQ******************************* 80
Cdd:cd07932  180 FLFKEGDRFLQAAGGYRFWPTGRGIFHNDDKTFLVWVNEEDHLRIISMQKGGDLGAVYKRLVTALKELEKKLPFARDDRL 259

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 972905631  81 **********GTTVRASVHIKVPKLAANKAKLEEVA*KYNL 121
Cdd:cd07932  260 GYLTFCPTNLGTTLRASVHIKLPKLSKDPPRLKEICEKYNL 300
 
Name Accession Description Interval E-value
arginine_kinase_like cd07932
Phosphagen (guanidino) kinases such as arginine kinase and similar enzymes; Eukaryotic ...
 1-121 1.11e-44

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: 148.23  E-value: 1.11e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972905631   1 FLFKEGDRFLQAANACRFWPSGRGIFHNDTKTFLVW*NEEDHJRIISMQ******************************* 80
Cdd:cd07932  180 FLFKEGDRFLQAAGGYRFWPTGRGIFHNDDKTFLVWVNEEDHLRIISMQKGGDLGAVYKRLVTALKELEKKLPFARDDRL 259

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 972905631  81 **********GTTVRASVHIKVPKLAANKAKLEEVA*KYNL 121
Cdd:cd07932  260 GYLTFCPTNLGTTLRASVHIKLPKLSKDPPRLKEICEKYNL 300
ATP-gua_Ptrans pfam00217
ATP:guanido phosphotransferase, C-terminal catalytic domain; The substrate binding site is ...
 7-121 1.74e-19

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: 79.12  E-value: 1.74e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972905631    7 DRFLQAANACRFWPSGRGIFHNDTKTFLVW*NEEDHJRIISMQ************************************* 86
Cdd:pfam00217  37 EKHLISPGLARDWPDGRGIFINEDETFSIWVNEEDHLRIISMEPGGDLGEVYERANRGDDLLEEKLDFAFDERLGYLTSC 116

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 972905631   87 ****GTTVRASVHIKVPKLAANK--AKLEEVA*KYNL 121
Cdd:pfam00217 117 PTNLGTGLRASVMIHLPALSKTNqiNRLLEALKKLGL 153
 
Name Accession Description Interval E-value
arginine_kinase_like cd07932
Phosphagen (guanidino) kinases such as arginine kinase and similar enzymes; Eukaryotic ...
 1-121 1.11e-44

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: 148.23  E-value: 1.11e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972905631   1 FLFKEGDRFLQAANACRFWPSGRGIFHNDTKTFLVW*NEEDHJRIISMQ******************************* 80
Cdd:cd07932  180 FLFKEGDRFLQAAGGYRFWPTGRGIFHNDDKTFLVWVNEEDHLRIISMQKGGDLGAVYKRLVTALKELEKKLPFARDDRL 259

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 972905631  81 **********GTTVRASVHIKVPKLAANKAKLEEVA*KYNL 121
Cdd:cd07932  260 GYLTFCPTNLGTTLRASVHIKLPKLSKDPPRLKEICEKYNL 300
eukaryotic_phosphagen_kinases cd07931
Phosphagen (guanidino) kinases mostly found in eukaryotes; Phosphagen (guanidino) kinases are ...
 1-121 4.83e-33

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: 117.76  E-value: 4.83e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972905631   1 FLFKEGDRFLQAANACRFWPSGRGIFHNDTKTFLVW*NEEDHJRIISMQ******************************* 80
Cdd:cd07931  167 FLFKDGDRFLEAAGENRDWPDGRGIFHNSDKTFLVWVNEEDHLRIISMQKGGDLKAVFTRLSRALTEIEKSLKEEFAHDP 246

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 972905631  81 *******--***GTTVRASVHIKVPKLAANKAKLEEVA*KYNL 121
Cdd:cd07931  247 HLGYITScpTNLGTGMRASVHVKLPNLIKDMDKLKAIARKLGL 289
phosphagen_kinases cd00330
Phosphagen (guanidino) kinases; Phosphagen (guanidino) kinases are enzymes that ...
 1-121 1.21e-32

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: 114.22  E-value: 1.21e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972905631   1 FLFKEGDRFLQAANACRFWPSGRGIFHNDTKTFLVW*NEEDHJRIISMQ******************************* 80
Cdd:cd00330   67 FLFPNLTRFLQTANACREWPFGRGILHNDEKTFLVWVNEEDHLRIISMQKGGQLKEVMKRANTVDDWIEEKVDFAFNEQR 146

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 972905631  81 **********GTTVRASVHIKVPKLAANKAKLEEVA*KYNL 121
Cdd:cd00330  147 GYLTSCPTNLGTGLRASVHIHLPALVKTINRIIPAINQLGL 187
creatine_kinase_like cd00716
Phosphagen (guanidino) kinases such as creatine kinase and similar enzymes; Eukaryotic ...
 1-49 3.72e-22

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: 88.93  E-value: 3.72e-22
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 972905631   1 FLFKEGD-RFLQAANACRFWPSGRGIFHNDTKTFLVW*NEEDHJRIISMQ 49
Cdd:cd00716  176 FLFDKPVsPLLLSSGMARDWPDARGIWHNDDKTFLVWVNEEDHLRVISMQ 225
ATP-gua_Ptrans pfam00217
ATP:guanido phosphotransferase, C-terminal catalytic domain; The substrate binding site is ...
 7-121 1.74e-19

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: 79.12  E-value: 1.74e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972905631    7 DRFLQAANACRFWPSGRGIFHNDTKTFLVW*NEEDHJRIISMQ************************************* 86
Cdd:pfam00217  37 EKHLISPGLARDWPDGRGIFINEDETFSIWVNEEDHLRIISMEPGGDLGEVYERANRGDDLLEEKLDFAFDERLGYLTSC 116

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 972905631   87 ****GTTVRASVHIKVPKLAANK--AKLEEVA*KYNL 121
Cdd:pfam00217 117 PTNLGTGLRASVMIHLPALSKTNqiNRLLEALKKLGL 153
 
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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