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Conserved domains on  [gi|76446019|gb|ABA42880|]
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arginine kinase, partial [Cnidaria environmental sample]

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 ...
 1-136 3.28e-71

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 cd07931:

Pssm-ID: 470681 [Multi-domain]  Cd Length: 338  Bit Score: 221.38  E-value: 3.28e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76446019   1 INEEDQLRIISMEMGSDILSVFKRLCDAVNEIDKQLG--FQYTQQHGYLSSCPTNLGTGMRASVHVKIPHAAEH-PDFKK 77
Cdd:cd07931 203 VNEEDHLRIISMQKGGDLKAVFTRLSRALTEIEKSLKeeFAHDPHLGYITSCPTNLGTGMRASVHVKLPNLIKDmDKLKA 282

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 76446019  78 ICDEYHIQPRGIHGEHSESTGadvGVFDISNRRRLGLSEVQCVQDMYNGVKKLLEIEKE 136
Cdd:cd07931 283 IARKLGLQIRGIGGEHSESEG---GVVDISNKRRLGFSEVQLVQDMYDGVKKLIEEEKK 338
phosphagen_kinases super family cl02823
Phosphagen (guanidino) kinases; Phosphagen (guanidino) kinases are enzymes that ...
 154-245 1.47e-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.


The actual alignment was detected with superfamily member cd07931:

Pssm-ID: 470681 [Multi-domain]  Cd Length: 338  Bit Score: 121.23  E-value: 1.47e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76446019 154 VKSLLKKFLTEDVFDELKVKKTTRGCTLWDQIVSGVEQLDSSNGIYATDEEAYTVFAKIFDPIIEAYHAPYKLADKHSSD 233
Cdd:cd07931   4 NKSLLAKYLTPEVYEKLKNRKTASGFTLADVIQSGVDNPDSGVGVYAGDEESYDVFAPLFDPVIEDYHGGYKPEDKHTSD 83

                        90
                ....*....|..
gi 76446019 234 MNPEKVDAPNLD 245
Cdd:cd07931  84 LDPEKPGLEDLD 95
 
Name Accession Description Interval E-value
eukaryotic_phosphagen_kinases cd07931
Phosphagen (guanidino) kinases mostly found in eukaryotes; Phosphagen (guanidino) kinases are ...
 1-136 3.28e-71

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: 221.38  E-value: 3.28e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76446019   1 INEEDQLRIISMEMGSDILSVFKRLCDAVNEIDKQLG--FQYTQQHGYLSSCPTNLGTGMRASVHVKIPHAAEH-PDFKK 77
Cdd:cd07931 203 VNEEDHLRIISMQKGGDLKAVFTRLSRALTEIEKSLKeeFAHDPHLGYITSCPTNLGTGMRASVHVKLPNLIKDmDKLKA 282

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 76446019  78 ICDEYHIQPRGIHGEHSESTGadvGVFDISNRRRLGLSEVQCVQDMYNGVKKLLEIEKE 136
Cdd:cd07931 283 IARKLGLQIRGIGGEHSESEG---GVVDISNKRRLGFSEVQLVQDMYDGVKKLIEEEKK 338
ATP-gua_Ptrans pfam00217
ATP:guanido phosphotransferase, C-terminal catalytic domain; The substrate binding site is ...
 1-137 3.90e-66

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: 203.54  E-value: 3.90e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76446019     1 INEEDQLRIISMEMGSDILSVFKRLCDAVNEIDKQLGFQYTQQHGYLSSCPTNLGTGMRASVHVKIPHAA---EHPDFKK 77
Cdd:pfam00217  67 VNEEDHLRIISMEPGGDLGEVYERANRGDDLLEEKLDFAFDERLGYLTSCPTNLGTGLRASVMIHLPALSktnQINRLLE 146

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 76446019    78 ICDEYHIQPRGIHGEHSESTGadvGVFDISNRRRLGLSEVQCVQDMYNGVKKLLEIEKEA 137
Cdd:pfam00217 147 ALKKLGLQVRGIYGEGSEAVG---GIYDISNQITLGLSEEEIVQDLIDGVKQLIEQEKKA 203
eukaryotic_phosphagen_kinases cd07931
Phosphagen (guanidino) kinases mostly found in eukaryotes; Phosphagen (guanidino) kinases are ...
 154-245 1.47e-32

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: 121.23  E-value: 1.47e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76446019 154 VKSLLKKFLTEDVFDELKVKKTTRGCTLWDQIVSGVEQLDSSNGIYATDEEAYTVFAKIFDPIIEAYHAPYKLADKHSSD 233
Cdd:cd07931   4 NKSLLAKYLTPEVYEKLKNRKTASGFTLADVIQSGVDNPDSGVGVYAGDEESYDVFAPLFDPVIEDYHGGYKPEDKHTSD 83

                        90
                ....*....|..
gi 76446019 234 MNPEKVDAPNLD 245
Cdd:cd07931  84 LDPEKPGLEDLD 95
ATP-gua_PtransN pfam02807
ATP:guanido phosphotransferase, N-terminal domain; The N-terminal domain has an all-alpha fold.
 155-218 7.30e-28

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: 101.04  E-value: 7.30e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 76446019   155 KSLLKKFLTEDVFDELKVKKTTRGCTLWDQIVSGVEQLDSSNGIYATDEEAYTVFAKIFDPIIE 218
Cdd:pfam02807   4 NSLLKKYLTPEVYDKLKDKKTPSGFTLDDCIQSGVDNPDSGVGVYAGDEESYEVFADLFDPIIE 67
McsB COG3869
Protein-arginine kinase McsB [Posttranslational modification, protein turnover, chaperones];
1-150 3.52e-26

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


Pssm-ID: 443078  Cd Length: 353  Bit Score: 104.10  E-value: 3.52e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76446019   1 INEEDQLRIISMEMGSDILSVFKRLcdavNEID----KQLGFQYTQQHGYLSSCPTNLGTGMRASVHVKIP---HAAEHP 73
Cdd:COG3869 118 VNEEDHLRIQCLLPGLQLEEAWELA----NKIDdaleEKLDYAFDEKFGYLTSCPTNVGTGLRASVMLHLPalvLTGQIN 193

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 76446019  74 DFKKICDEYHIQPRGIHGEHSESTGAdvgVFDISNRRRLGLSEVQCVQDMYNGVKKLLEIEKEALAKELEKFPEALK 150
Cdd:COG3869 194 RVLQALNQLGLTVRGLYGEGSEALGN---IFQISNQITLGKSEEEIIENLESVVRQIIEQERNAREALLKENRLELE 267
PRK01059 PRK01059
ATP:guanido phosphotransferase; Provisional
 1-150 2.18e-22

ATP:guanido phosphotransferase; Provisional


Pssm-ID: 234894 [Multi-domain]  Cd Length: 346  Bit Score: 93.73  E-value: 2.18e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76446019    1 INEEDQLRIISMEMGSDILSVFKRLCDAVNEIDKQLGFQYTQQHGYLSSCPTNLGTGMRASVHVKIP---HAAEHPDFKK 77
Cdd:PRK01059 116 INEEDHLRIQCIDPGLQLEEALEKANQIDDLLEEKLDYAFDEKLGYLTSCPTNVGTGLRASVMLHLPalvLTKRINRILQ 195

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 76446019   78 ICDEYHIQPRGIHGEHSESTGadvGVFDISNRRRLGLSEVQCVQDMYNGVKKLLEIEKEALAKELEKFPEALK 150
Cdd:PRK01059 196 AINQLGLTVRGIYGEGSEALG---NIYQISNQITLGKSEEEIISNLRSVVNQIISQERAAREKLVKENKIELE 265
 
Name Accession Description Interval E-value
eukaryotic_phosphagen_kinases cd07931
Phosphagen (guanidino) kinases mostly found in eukaryotes; Phosphagen (guanidino) kinases are ...
 1-136 3.28e-71

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: 221.38  E-value: 3.28e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76446019   1 INEEDQLRIISMEMGSDILSVFKRLCDAVNEIDKQLG--FQYTQQHGYLSSCPTNLGTGMRASVHVKIPHAAEH-PDFKK 77
Cdd:cd07931 203 VNEEDHLRIISMQKGGDLKAVFTRLSRALTEIEKSLKeeFAHDPHLGYITSCPTNLGTGMRASVHVKLPNLIKDmDKLKA 282

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 76446019  78 ICDEYHIQPRGIHGEHSESTGadvGVFDISNRRRLGLSEVQCVQDMYNGVKKLLEIEKE 136
Cdd:cd07931 283 IARKLGLQIRGIGGEHSESEG---GVVDISNKRRLGFSEVQLVQDMYDGVKKLIEEEKK 338
ATP-gua_Ptrans pfam00217
ATP:guanido phosphotransferase, C-terminal catalytic domain; The substrate binding site is ...
 1-137 3.90e-66

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: 203.54  E-value: 3.90e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76446019     1 INEEDQLRIISMEMGSDILSVFKRLCDAVNEIDKQLGFQYTQQHGYLSSCPTNLGTGMRASVHVKIPHAA---EHPDFKK 77
Cdd:pfam00217  67 VNEEDHLRIISMEPGGDLGEVYERANRGDDLLEEKLDFAFDERLGYLTSCPTNLGTGLRASVMIHLPALSktnQINRLLE 146

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 76446019    78 ICDEYHIQPRGIHGEHSESTGadvGVFDISNRRRLGLSEVQCVQDMYNGVKKLLEIEKEA 137
Cdd:pfam00217 147 ALKKLGLQVRGIYGEGSEAVG---GIYDISNQITLGLSEEEIVQDLIDGVKQLIEQEKKA 203
arginine_kinase_like cd07932
Phosphagen (guanidino) kinases such as arginine kinase and similar enzymes; Eukaryotic ...
 1-137 1.10e-64

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: 204.86  E-value: 1.10e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76446019   1 INEEDQLRIISMEMGSDILSVFKRLCDAVNEIDKQLGFQYTQQHGYLSSCPTNLGTGMRASVHVKIPH-AAEHPDFKKIC 79
Cdd:cd07932 216 VNEEDHLRIISMQKGGDLGAVYKRLVTALKELEKKLPFARDDRLGYLTFCPTNLGTTLRASVHIKLPKlSKDPPRLKEIC 295

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 76446019  80 DEYHIQPRGIHGEHSESTGadvGVFDISNRRRLGLSEVQCVQDMYNGVKKLLEIEKEA 137
Cdd:cd07932 296 EKYNLQVRGTHGEHTESVG---GVYDISNKRRLGLTEFEAVKEMQDGVLELIKLEKEL 350
creatine_kinase_like cd00716
Phosphagen (guanidino) kinases such as creatine kinase and similar enzymes; Eukaryotic ...
 1-144 1.55e-53

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: 176.38  E-value: 1.55e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76446019   1 INEEDQLRIISMEMGSDILSVFKRLCDAVNEIDKQL-----GFQYTQQHGYLSSCPTNLGTGMRASVHVKIPHAAEHPDF 75
Cdd:cd00716 213 VNEEDHLRVISMQKGGDMKAVFARFCRGLTEVEKLMkkkgyEFMWNEHLGYVLTCPSNLGTGLRASVHVKLPNLSKDPRF 292

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 76446019  76 KKICDEYHIQPRGIHGEHSESTGadvGVFDISNRRRLGLSEVQCVQDMYNGVKKLLEIEkealaKELEK 144
Cdd:cd00716 293 DEILRKLRLQKRGTGGVDTAAVG---GTYDISNADRLGKSEVELVQFVIDGVNLLIEME-----KRLEK 353
phosphagen_kinases cd00330
Phosphagen (guanidino) kinases; Phosphagen (guanidino) kinases are enzymes that ...
 1-135 1.22e-48

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: 160.06  E-value: 1.22e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76446019   1 INEEDQLRIISMEMGSDILSVFKRLCDAVNEIDKQLGFQYTQQHGYLSSCPTNLGTGMRASVHVKIPHAAEHPD-FKKIC 79
Cdd:cd00330 103 VNEEDHLRIISMQKGGQLKEVMKRANTVDDWIEEKVDFAFNEQRGYLTSCPTNLGTGLRASVHIHLPALVKTINrIIPAI 182

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 76446019  80 DEYHIQPRGIHGEHSESTGadvGVFDISNRRRLGLSEVQCVQDMYNGVKKLLEIEK 135
Cdd:cd00330 183 NQLGLQVRGTYGEGTEAVG---GVFDISNQIRLGKSEQDIVEDLNDGAAQLIEMER 235
eukaryotic_phosphagen_kinases cd07931
Phosphagen (guanidino) kinases mostly found in eukaryotes; Phosphagen (guanidino) kinases are ...
 154-245 1.47e-32

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: 121.23  E-value: 1.47e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76446019 154 VKSLLKKFLTEDVFDELKVKKTTRGCTLWDQIVSGVEQLDSSNGIYATDEEAYTVFAKIFDPIIEAYHAPYKLADKHSSD 233
Cdd:cd07931   4 NKSLLAKYLTPEVYEKLKNRKTASGFTLADVIQSGVDNPDSGVGVYAGDEESYDVFAPLFDPVIEDYHGGYKPEDKHTSD 83

                        90
                ....*....|..
gi 76446019 234 MNPEKVDAPNLD 245
Cdd:cd07931  84 LDPEKPGLEDLD 95
arginine_kinase_like cd07932
Phosphagen (guanidino) kinases such as arginine kinase and similar enzymes; Eukaryotic ...
 140-230 5.26e-31

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: 117.03  E-value: 5.26e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76446019 140 KELEKFPEALKGAEVKSLLKKFLTEDVFDELKVKKTTRGCTLWDQIVSGVEQLDSSNGIYATDEEAYTVFAKIFDPIIEA 219
Cdd:cd07932   1 KLEEELAKLQDAEDCKSLLKKYLTPEVLKKLKDKKTKLGGTLADCIQSGAENLDSGVGIYACDPEAYTVFADLFDPVIED 80

                        90
                ....*....|.
gi 76446019 220 YHAPYKLADKH 230
Cdd:cd07932  81 YHGGFKPEDKH 91
bacterial_phosphagen_kinase cd07930
Phosphagen (guanidino) kinases found in bacteria; Phosphagen (guanidino) kinases are enzymes ...
 1-137 6.50e-29

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: 108.75  E-value: 6.50e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76446019   1 INEEDQLRIISMEMGSDILSVFKRLCDAVNEIDKQLGFQYTQQHGYLSSCPTNLGTGMRASVHVKIP---HAAEHPDFKK 77
Cdd:cd07930  96 INEEDHLRIQCLLPGLQLEEAYERADKIDDLLEEKLDYAFDEKLGYLTACPTNVGTGLRASVMLHLPalvLTGQINRILN 175

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 76446019  78 ICDEYHIQPRGIHGEHSESTGadvGVFDISNRRRLGLSEVQCVQDMYNGVKKLLEIEKEA 137
Cdd:cd07930 176 ALSQLGLAVRGLYGEGSEALG---NIYQISNQVTLGLSEEEIIENLESVVRQIIEQEREA 232
ATP-gua_PtransN pfam02807
ATP:guanido phosphotransferase, N-terminal domain; The N-terminal domain has an all-alpha fold.
 155-218 7.30e-28

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: 101.04  E-value: 7.30e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 76446019   155 KSLLKKFLTEDVFDELKVKKTTRGCTLWDQIVSGVEQLDSSNGIYATDEEAYTVFAKIFDPIIE 218
Cdd:pfam02807   4 NSLLKKYLTPEVYDKLKDKKTPSGFTLDDCIQSGVDNPDSGVGVYAGDEESYEVFADLFDPIIE 67
McsB COG3869
Protein-arginine kinase McsB [Posttranslational modification, protein turnover, chaperones];
1-150 3.52e-26

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


Pssm-ID: 443078  Cd Length: 353  Bit Score: 104.10  E-value: 3.52e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76446019   1 INEEDQLRIISMEMGSDILSVFKRLcdavNEID----KQLGFQYTQQHGYLSSCPTNLGTGMRASVHVKIP---HAAEHP 73
Cdd:COG3869 118 VNEEDHLRIQCLLPGLQLEEAWELA----NKIDdaleEKLDYAFDEKFGYLTSCPTNVGTGLRASVMLHLPalvLTGQIN 193

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 76446019  74 DFKKICDEYHIQPRGIHGEHSESTGAdvgVFDISNRRRLGLSEVQCVQDMYNGVKKLLEIEKEALAKELEKFPEALK 150
Cdd:COG3869 194 RVLQALNQLGLTVRGLYGEGSEALGN---IFQISNQITLGKSEEEIIENLESVVRQIIEQERNAREALLKENRLELE 267
PRK01059 PRK01059
ATP:guanido phosphotransferase; Provisional
 1-150 2.18e-22

ATP:guanido phosphotransferase; Provisional


Pssm-ID: 234894 [Multi-domain]  Cd Length: 346  Bit Score: 93.73  E-value: 2.18e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76446019    1 INEEDQLRIISMEMGSDILSVFKRLCDAVNEIDKQLGFQYTQQHGYLSSCPTNLGTGMRASVHVKIP---HAAEHPDFKK 77
Cdd:PRK01059 116 INEEDHLRIQCIDPGLQLEEALEKANQIDDLLEEKLDYAFDEKLGYLTSCPTNVGTGLRASVMLHLPalvLTKRINRILQ 195

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 76446019   78 ICDEYHIQPRGIHGEHSESTGadvGVFDISNRRRLGLSEVQCVQDMYNGVKKLLEIEKEALAKELEKFPEALK 150
Cdd:PRK01059 196 AINQLGLTVRGIYGEGSEALG---NIYQISNQITLGKSEEEIISNLRSVVNQIISQERAAREKLVKENKIELE 265
creatine_kinase_like cd00716
Phosphagen (guanidino) kinases such as creatine kinase and similar enzymes; Eukaryotic ...
 143-245 2.36e-19

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: 85.47  E-value: 2.36e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76446019 143 EKFPEALKGaevKSLLKKFLTEDVFDELKVKKTTRGCTLWDQIVSGVEQLDSSN----GIYATDEEAYTVFAKIFDPIIE 218
Cdd:cd00716   3 ENFPDLSKH---NNHMAKVLTPEMYAKLRDKVTPNGVTLDKCIQTGVDNPGHPFiktvGCVAGDEESYEVFKDLFDPVID 79

                        90       100
                ....*....|....*....|....*..
gi 76446019 219 AYHAPYKLADKHSSDMNPEKVDAPNLD 245
Cdd:cd00716  80 ERHGGYKPTAKHPTDLDPTKLKGGQFD 106
 
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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