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Conserved domains on  [gi|992007714|gb|AMH39761|]
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arginine kinase, partial [Aglaothorax ovata gigantea]

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 ...
 1-149 4.48e-100

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: 290.75  E-value: 4.48e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992007714   1 AESYLTFADLFDPIIEDYHGGFKKTDKHPRKDWGDVD--TLGNLDPDGDYIISTRVRCGRSMQGYPFNPCLTEAQYKEME 78
Cdd:cd07932   64 PEAYTVFADLFDPVIEDYHGGFKPEDKHPAPDFGDLKnlELGNLDPEGKYVISTRVRCGRSVEGYPFNPCLTKEQYIEME 143

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 992007714  79 DKVSSTLSFLEGKLKGKFYPLTGMTKDTQQKLIDDHFLFKEGDRFLQAANACRFWPTGRGIYHNDTKTFLV 149
Cdd:cd07932  144 EKVKSALETLTGELAGTYYPLTGMDKETQQQLIDDHFLFKEGDRFLQAAGGYRFWPTGRGIFHNDDKTFLV 214
 
Name Accession Description Interval E-value
arginine_kinase_like cd07932
Phosphagen (guanidino) kinases such as arginine kinase and similar enzymes; Eukaryotic ...
 1-149 4.48e-100

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: 290.75  E-value: 4.48e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992007714   1 AESYLTFADLFDPIIEDYHGGFKKTDKHPRKDWGDVD--TLGNLDPDGDYIISTRVRCGRSMQGYPFNPCLTEAQYKEME 78
Cdd:cd07932   64 PEAYTVFADLFDPVIEDYHGGFKPEDKHPAPDFGDLKnlELGNLDPEGKYVISTRVRCGRSVEGYPFNPCLTKEQYIEME 143

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 992007714  79 DKVSSTLSFLEGKLKGKFYPLTGMTKDTQQKLIDDHFLFKEGDRFLQAANACRFWPTGRGIYHNDTKTFLV 149
Cdd:cd07932  144 EKVKSALETLTGELAGTYYPLTGMDKETQQQLIDDHFLFKEGDRFLQAAGGYRFWPTGRGIFHNDDKTFLV 214
ATP-gua_Ptrans pfam00217
ATP:guanido phosphotransferase, C-terminal catalytic domain; The substrate binding site is ...
 76-149 6.42e-24

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: 91.83  E-value: 6.42e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 992007714   76 EMEDKVSSTLSFLEGKLKGKFYPLTGMTKDTQQKLIDDHFLFkegdrflqaANACRFWPTGRGIYHNDTKTFLV 149
Cdd:pfam00217   1 EVEELVVDALESLSGDLKGKYYPLTEMDPEERQQLVEKHLIS---------PGLARDWPDGRGIFINEDETFSI 65
PRK01059 PRK01059
ATP:guanido phosphotransferase; Provisional
 44-117 1.26e-08

ATP:guanido phosphotransferase; Provisional


Pssm-ID: 234894 [Multi-domain]  Cd Length: 346  Bit Score: 52.13  E-value: 1.26e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 992007714  44 PDGDYIISTRVRCGRSMQGYPFNPCLTEAQYKEMEDKVSSTLSFLEGKLKGKF--YPLTGMTKDTQQKLIdDHFLF 117
Cdd:PRK01059  17 PDSDIVLSSRIRLARNLKDIPFPNKLSEEEARDIIELVEKAFLNNEIEGFGEFelLKLKDLDPLEKEVLV-EKHLI 91
McsB COG3869
Protein-arginine kinase McsB [Posttranslational modification, protein turnover, chaperones];
44-116 3.00e-08

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


Pssm-ID: 443078  Cd Length: 353  Bit Score: 50.95  E-value: 3.00e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 992007714  44 PDGDYIISTRVRCGRSMQGYPFNPCLTEAQYKEMEDKVSSTLSFLEGKLKGKF--YPLTGMTKDTQQKLIDDHFL 116
Cdd:COG3869   19 PESDIVLSSRIRLARNLAGFPFPHRASEEEAEQVLSLVREALLSLSFQELGKFelIKLEDLSPLERQVLVEKHLI 93
 
Name Accession Description Interval E-value
arginine_kinase_like cd07932
Phosphagen (guanidino) kinases such as arginine kinase and similar enzymes; Eukaryotic ...
 1-149 4.48e-100

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: 290.75  E-value: 4.48e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992007714   1 AESYLTFADLFDPIIEDYHGGFKKTDKHPRKDWGDVD--TLGNLDPDGDYIISTRVRCGRSMQGYPFNPCLTEAQYKEME 78
Cdd:cd07932   64 PEAYTVFADLFDPVIEDYHGGFKPEDKHPAPDFGDLKnlELGNLDPEGKYVISTRVRCGRSVEGYPFNPCLTKEQYIEME 143

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 992007714  79 DKVSSTLSFLEGKLKGKFYPLTGMTKDTQQKLIDDHFLFKEGDRFLQAANACRFWPTGRGIYHNDTKTFLV 149
Cdd:cd07932  144 EKVKSALETLTGELAGTYYPLTGMDKETQQQLIDDHFLFKEGDRFLQAAGGYRFWPTGRGIFHNDDKTFLV 214
eukaryotic_phosphagen_kinases cd07931
Phosphagen (guanidino) kinases mostly found in eukaryotes; Phosphagen (guanidino) kinases are ...
 1-149 2.25e-72

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: 220.23  E-value: 2.25e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992007714   1 AESYLTFADLFDPIIEDYHGGFKKTDKHPRkDWGDVD-TLGNLDPDGDYIISTRVRCGRSMQGYPFNPCLTEAQYKEMED 79
Cdd:cd07931   53 EESYDVFAPLFDPVIEDYHGGYKPEDKHTS-DLDPEKpGLEDLDPRKKYIISTRIRVARNLDGFPLPPGMTKEQRRQIER 131

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992007714  80 KVSSTLSFLEGKLKGKFYPLTGMTKDTQQKLIDDHFLFKEGDRFLQAANACRFWPTGRGIYHNDTKTFLV 149
Cdd:cd07931  132 LMVSALSSLEGDLKGTYYSLTEMTEEQQQQLIDDHFLFKDGDRFLEAAGENRDWPDGRGIFHNSDKTFLV 201
creatine_kinase_like cd00716
Phosphagen (guanidino) kinases such as creatine kinase and similar enzymes; Eukaryotic ...
 2-149 1.59e-57

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: 182.54  E-value: 1.59e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992007714   2 ESYLTFADLFDPIIEDYHGGFKKTDKHPRkdwgDVD----TLGNLDPDgdYIISTRVRCGRSMQGYPFNPCLTEAQYKEM 77
Cdd:cd00716   65 ESYEVFKDLFDPVIDERHGGYKPTAKHPT----DLDptklKGGQFDPK--YVLSSRVRTGRSIRGFCLPPHCSRAERREV 138

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 992007714  78 EDKVSSTLSFLEGKLKGKFYPLTGMTKDTQQKLIDDHFLFKEGD-RFLQAANACRFWPTGRGIYHNDTKTFLV 149
Cdd:cd00716  139 EKIAVEALASLDGDLKGKYYPLSGMTEEEQQQLIEDHFLFDKPVsPLLLSSGMARDWPDARGIWHNDDKTFLV 211
phosphagen_kinases cd00330
Phosphagen (guanidino) kinases; Phosphagen (guanidino) kinases are enzymes that ...
 49-149 4.51e-52

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: 165.07  E-value: 4.51e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992007714  49 IISTRVRCGRSMQGYPFNPCLTEAQYKEMEDKVSSTLSFLEGKLKGKFYPLTGMTKDTQQKLIDDHFLFKEGDRFLQAAN 128
Cdd:cd00330    1 VLSSRVRLGRSFEGIRFPPRYSNEEASSIEQQFEDQLSSQEIPLIGKYYLLRMMDPAEQQQLIDDHFLFPNLTRFLQTAN 80

                         90       100
                 ....*....|....*....|.
gi 992007714 129 ACRFWPTGRGIYHNDTKTFLV 149
Cdd:cd00330   81 ACREWPFGRGILHNDEKTFLV 101
ATP-gua_Ptrans pfam00217
ATP:guanido phosphotransferase, C-terminal catalytic domain; The substrate binding site is ...
 76-149 6.42e-24

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: 91.83  E-value: 6.42e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 992007714   76 EMEDKVSSTLSFLEGKLKGKFYPLTGMTKDTQQKLIDDHFLFkegdrflqaANACRFWPTGRGIYHNDTKTFLV 149
Cdd:pfam00217   1 EVEELVVDALESLSGDLKGKYYPLTEMDPEERQQLVEKHLIS---------PGLARDWPDGRGIFINEDETFSI 65
PRK01059 PRK01059
ATP:guanido phosphotransferase; Provisional
 44-117 1.26e-08

ATP:guanido phosphotransferase; Provisional


Pssm-ID: 234894 [Multi-domain]  Cd Length: 346  Bit Score: 52.13  E-value: 1.26e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 992007714  44 PDGDYIISTRVRCGRSMQGYPFNPCLTEAQYKEMEDKVSSTLSFLEGKLKGKF--YPLTGMTKDTQQKLIdDHFLF 117
Cdd:PRK01059  17 PDSDIVLSSRIRLARNLKDIPFPNKLSEEEARDIIELVEKAFLNNEIEGFGEFelLKLKDLDPLEKEVLV-EKHLI 91
McsB COG3869
Protein-arginine kinase McsB [Posttranslational modification, protein turnover, chaperones];
44-116 3.00e-08

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


Pssm-ID: 443078  Cd Length: 353  Bit Score: 50.95  E-value: 3.00e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 992007714  44 PDGDYIISTRVRCGRSMQGYPFNPCLTEAQYKEMEDKVSSTLSFLEGKLKGKF--YPLTGMTKDTQQKLIDDHFL 116
Cdd:COG3869   19 PESDIVLSSRIRLARNLAGFPFPHRASEEEAEQVLSLVREALLSLSFQELGKFelIKLEDLSPLERQVLVEKHLI 93
bacterial_phosphagen_kinase cd07930
Phosphagen (guanidino) kinases found in bacteria; Phosphagen (guanidino) kinases are enzymes ...
 46-114 1.37e-07

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: 48.66  E-value: 1.37e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 992007714  46 GDYIISTRVRCGRSMQGYPFNPCLTEAQYKEMEDKVSSTLSFLEGKLKGKFYPLTGMTKDTQQKLIDDH 114
Cdd:cd07930    1 SDIVISSRIRLARNLKGYPFPNKLSEEQAADVLEKVEKALSNIEDKDEFELLKLKDLDPLERQVLVEKH 69
ATP-gua_PtransN pfam02807
ATP:guanido phosphotransferase, N-terminal domain; The N-terminal domain has an all-alpha fold.
 1-16 9.87e-05

ATP:guanido phosphotransferase, N-terminal domain; The N-terminal domain has an all-alpha fold.


Pssm-ID: 460702 [Multi-domain]  Cd Length: 67  Bit Score: 38.25  E-value: 9.87e-05
                          10
                  ....*....|....*.
gi 992007714    1 AESYLTFADLFDPIIE 16
Cdd:pfam02807  52 EESYEVFADLFDPIIE 67
 
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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