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Conserved domains on  [gi|189083744|ref|NP_001121124|]
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creatine kinase S-type, mitochondrial precursor [Rattus norvegicus]

Protein Classification

creatine kinase family protein( domain architecture ID 10091282)

creatine kinase family protein similar to creatine kinase that reversibly catalyzes the transfer of phosphate between ATP and various phosphogens

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
creatine_kinase_like cd00716
Phosphagen (guanidino) kinases such as creatine kinase and similar enzymes; Eukaryotic ...
50-407 0e+00

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: 731.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083744  50 PSADYPDLRKHNNCMAECLTPTIYAKLRNKMTPSGYTLDQCIQTGVDNPGHPFIKTVGMVAGDEESYEVFADLFDPVIKL 129
Cdd:cd00716    1 APENFPDLSKHNNHMAKVLTPEMYAKLRDKVTPNGVTLDKCIQTGVDNPGHPFIKTVGCVAGDEESYEVFKDLFDPVIDE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083744 130 RHNGYDPRVmKHPTDLDASKITHGQFDERYVLSSRVRTGRSIRGLSLPPACSRAERREVENVAITALEGLKGDLAGRYYK 209
Cdd:cd00716   81 RHGGYKPTA-KHPTDLDPTKLKGGQFDPKYVLSSRVRTGRSIRGFCLPPHCSRAERREVEKIAVEALASLDGDLKGKYYP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083744 210 LSEMTEQDQQRLIDDHFLFDKPVSPLLTCAGMARDWPDARGIWHNYDKTFLIWINEEDHTRVISMEKGGNMKRVFERFCR 289
Cdd:cd00716  160 LSGMTEEEQQQLIEDHFLFDKPVSPLLLSSGMARDWPDARGIWHNDDKTFLVWVNEEDHLRVISMQKGGDMKAVFARFCR 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083744 290 GLKEVERLIQERGWEFMWNERLGYILTCPSNLGTGLRAGVHVRIPKLSKDPRFSKILENLRLQKRGTGGVDTAAVADVYD 369
Cdd:cd00716  240 GLTEVEKLMKKKGYEFMWNEHLGYVLTCPSNLGTGLRASVHVKLPNLSKDPRFDEILRKLRLQKRGTGGVDTAAVGGTYD 319
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 189083744 370 ISNIDRIGRSEVELVQIVIDGVNYLVDCEKKLERGQDI 407
Cdd:cd00716  320 ISNADRLGKSEVELVQFVIDGVNLLIEMEKRLEKGKSI 357
 
Name Accession Description Interval E-value
creatine_kinase_like cd00716
Phosphagen (guanidino) kinases such as creatine kinase and similar enzymes; Eukaryotic ...
50-407 0e+00

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: 731.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083744  50 PSADYPDLRKHNNCMAECLTPTIYAKLRNKMTPSGYTLDQCIQTGVDNPGHPFIKTVGMVAGDEESYEVFADLFDPVIKL 129
Cdd:cd00716    1 APENFPDLSKHNNHMAKVLTPEMYAKLRDKVTPNGVTLDKCIQTGVDNPGHPFIKTVGCVAGDEESYEVFKDLFDPVIDE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083744 130 RHNGYDPRVmKHPTDLDASKITHGQFDERYVLSSRVRTGRSIRGLSLPPACSRAERREVENVAITALEGLKGDLAGRYYK 209
Cdd:cd00716   81 RHGGYKPTA-KHPTDLDPTKLKGGQFDPKYVLSSRVRTGRSIRGFCLPPHCSRAERREVEKIAVEALASLDGDLKGKYYP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083744 210 LSEMTEQDQQRLIDDHFLFDKPVSPLLTCAGMARDWPDARGIWHNYDKTFLIWINEEDHTRVISMEKGGNMKRVFERFCR 289
Cdd:cd00716  160 LSGMTEEEQQQLIEDHFLFDKPVSPLLLSSGMARDWPDARGIWHNDDKTFLVWVNEEDHLRVISMQKGGDMKAVFARFCR 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083744 290 GLKEVERLIQERGWEFMWNERLGYILTCPSNLGTGLRAGVHVRIPKLSKDPRFSKILENLRLQKRGTGGVDTAAVADVYD 369
Cdd:cd00716  240 GLTEVEKLMKKKGYEFMWNEHLGYVLTCPSNLGTGLRASVHVKLPNLSKDPRFDEILRKLRLQKRGTGGVDTAAVGGTYD 319
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 189083744 370 ISNIDRIGRSEVELVQIVIDGVNYLVDCEKKLERGQDI 407
Cdd:cd00716  320 ISNADRLGKSEVELVQFVIDGVNLLIEMEKRLEKGKSI 357
ATP-gua_Ptrans pfam00217
ATP:guanido phosphotransferase, C-terminal catalytic domain; The substrate binding site is ...
187-401 6.08e-110

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: 321.41  E-value: 6.08e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083744  187 EVENVAITALEGLKGDLAGRYYKLSEMTEQDQQRLIDDHFLFdkpvsplltcAGMARDWPDARGIWHNYDKTFLIWINEE 266
Cdd:pfam00217   1 EVEELVVDALESLSGDLKGKYYPLTEMDPEERQQLVEKHLIS----------PGLARDWPDGRGIFINEDETFSIWVNEE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083744  267 DHTRVISMEKGGNMKRVFERFCRGLKEVERLIqergwEFMWNERLGYILTCPSNLGTGLRAGVHVRIPKLSKD---PRFS 343
Cdd:pfam00217  71 DHLRIISMEPGGDLGEVYERANRGDDLLEEKL-----DFAFDERLGYLTSCPTNLGTGLRASVMIHLPALSKTnqiNRLL 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 189083744  344 KILENLRLQKRGTGGVDTAAVADVYDISNIDRIGRSEVELVQIVIDGVNYLVDCEKKL 401
Cdd:pfam00217 146 EALKKLGLQVRGIYGEGSEAVGGIYDISNQITLGLSEEEIVQDLIDGVKQLIEQEKKA 203
McsB COG3869
Protein-arginine kinase McsB [Posttranslational modification, protein turnover, chaperones];
160-400 7.12e-35

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


Pssm-ID: 443078  Cd Length: 353  Bit Score: 132.22  E-value: 7.12e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083744 160 VLSSRVRTGRSIRGLSLPPACSRAERREVENVAITALEGLKGDLAGR--YYKLSEMTEQDQQRLIDDHFlfdkpVSPLLt 237
Cdd:COG3869   24 VLSSRIRLARNLAGFPFPHRASEEEAEQVLSLVREALLSLSFQELGKfeLIKLEDLSPLERQVLVEKHL-----ISPEL- 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083744 238 cagmARDwPDARGIWHNYDKTFLIWINEEDHTRVISMEKGGNMKRVFERfcrgLKEVERLIQERgWEFMWNERLGYILTC 317
Cdd:COG3869   98 ----AEN-PGGRAVLLSEDESVSIMVNEEDHLRIQCLLPGLQLEEAWEL----ANKIDDALEEK-LDYAFDEKFGYLTSC 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083744 318 PSNLGTGLRAGVHVRIPKLSKDPRFSKILENLR---LQKRGTGGVDTAAVADVYDISNIDRIGRSEVELVQIVIDGVNYL 394
Cdd:COG3869  168 PTNVGTGLRASVMLHLPALVLTGQINRVLQALNqlgLTVRGLYGEGSEALGNIFQISNQITLGKSEEEIIENLESVVRQI 247

                 ....*.
gi 189083744 395 VDCEKK 400
Cdd:COG3869  248 IEQERN 253
PRK01059 PRK01059
ATP:guanido phosphotransferase; Provisional
139-400 1.13e-32

ATP:guanido phosphotransferase; Provisional


Pssm-ID: 234894 [Multi-domain]  Cd Length: 346  Bit Score: 126.09  E-value: 1.13e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083744 139 MKHPTDLDASKITHGQFDERYVLSSRVRTGRSIRGLSLPPACSRAERREVENVAITALEGLKGDLAGR--YYKLSEMTEQ 216
Cdd:PRK01059   1 MKLPNDALSNWMKGDGPDSDIVLSSRIRLARNLKDIPFPNKLSEEEARDIIELVEKAFLNNEIEGFGEfeLLKLKDLDPL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083744 217 DQQRLIDdHFLFdkpvSPLLTcagmarDWPDARGIWHNYDKTFLIWINEEDHTRVISMEKGGNMKRVFERfcrgLKEVER 296
Cdd:PRK01059  81 EKEVLVE-KHLI----SPDLA------ENPEGGAVLLNEDETISIMINEEDHLRIQCIDPGLQLEEALEK----ANQIDD 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083744 297 LIQERgWEFMWNERLGYILTCPSNLGTGLRAGVHVRIPKLSKDPRFSKILENLR---LQKRGTGGVDTAAVADVYDISNI 373
Cdd:PRK01059 146 LLEEK-LDYAFDEKLGYLTSCPTNVGTGLRASVMLHLPALVLTKRINRILQAINqlgLTVRGIYGEGSEALGNIYQISNQ 224
                        250       260
                 ....*....|....*....|....*..
gi 189083744 374 DRIGRSEVELVQIVIDGVNYLVDCEKK 400
Cdd:PRK01059 225 ITLGKSEEEIISNLRSVVNQIISQERA 251
 
Name Accession Description Interval E-value
creatine_kinase_like cd00716
Phosphagen (guanidino) kinases such as creatine kinase and similar enzymes; Eukaryotic ...
50-407 0e+00

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: 731.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083744  50 PSADYPDLRKHNNCMAECLTPTIYAKLRNKMTPSGYTLDQCIQTGVDNPGHPFIKTVGMVAGDEESYEVFADLFDPVIKL 129
Cdd:cd00716    1 APENFPDLSKHNNHMAKVLTPEMYAKLRDKVTPNGVTLDKCIQTGVDNPGHPFIKTVGCVAGDEESYEVFKDLFDPVIDE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083744 130 RHNGYDPRVmKHPTDLDASKITHGQFDERYVLSSRVRTGRSIRGLSLPPACSRAERREVENVAITALEGLKGDLAGRYYK 209
Cdd:cd00716   81 RHGGYKPTA-KHPTDLDPTKLKGGQFDPKYVLSSRVRTGRSIRGFCLPPHCSRAERREVEKIAVEALASLDGDLKGKYYP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083744 210 LSEMTEQDQQRLIDDHFLFDKPVSPLLTCAGMARDWPDARGIWHNYDKTFLIWINEEDHTRVISMEKGGNMKRVFERFCR 289
Cdd:cd00716  160 LSGMTEEEQQQLIEDHFLFDKPVSPLLLSSGMARDWPDARGIWHNDDKTFLVWVNEEDHLRVISMQKGGDMKAVFARFCR 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083744 290 GLKEVERLIQERGWEFMWNERLGYILTCPSNLGTGLRAGVHVRIPKLSKDPRFSKILENLRLQKRGTGGVDTAAVADVYD 369
Cdd:cd00716  240 GLTEVEKLMKKKGYEFMWNEHLGYVLTCPSNLGTGLRASVHVKLPNLSKDPRFDEILRKLRLQKRGTGGVDTAAVGGTYD 319
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 189083744 370 ISNIDRIGRSEVELVQIVIDGVNYLVDCEKKLERGQDI 407
Cdd:cd00716  320 ISNADRLGKSEVELVQFVIDGVNLLIEMEKRLEKGKSI 357
eukaryotic_phosphagen_kinases cd07931
Phosphagen (guanidino) kinases mostly found in eukaryotes; Phosphagen (guanidino) kinases are ...
57-400 8.04e-167

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: 471.38  E-value: 8.04e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083744  57 LRKHNNCMAECLTPTIYAKLRNKMTPSGYTLDQCIQTGVDNPGhpfiKTVGMVAGDEESYEVFADLFDPVIKLRHNGYDP 136
Cdd:cd07931    1 LESNKSLLAKYLTPEVYEKLKNRKTASGFTLADVIQSGVDNPD----SGVGVYAGDEESYDVFAPLFDPVIEDYHGGYKP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083744 137 RvMKHPTDLDASKITHGQFDER--YVLSSRVRTGRSIRGLSLPPACSRAERREVENVAITALEGLKGDLAGRYYKLSEMT 214
Cdd:cd07931   77 E-DKHTSDLDPEKPGLEDLDPRkkYIISTRIRVARNLDGFPLPPGMTKEQRRQIERLMVSALSSLEGDLKGTYYSLTEMT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083744 215 EQDQQRLIDDHFLFDKPvSPLLTCAGMARDWPDARGIWHNYDKTFLIWINEEDHTRVISMEKGGNMKRVFERFCRGLKEV 294
Cdd:cd07931  156 EEQQQQLIDDHFLFKDG-DRFLEAAGENRDWPDGRGIFHNSDKTFLVWVNEEDHLRIISMQKGGDLKAVFTRLSRALTEI 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083744 295 ERLIQErgwEFMWNERLGYILTCPSNLGTGLRAGVHVRIPKLSKD-PRFSKILENLRLQKRGTGGVDTAAVADVYDISNI 373
Cdd:cd07931  235 EKSLKE---EFAHDPHLGYITSCPTNLGTGMRASVHVKLPNLIKDmDKLKAIARKLGLQIRGIGGEHSESEGGVVDISNK 311
                        330       340
                 ....*....|....*....|....*..
gi 189083744 374 DRIGRSEVELVQIVIDGVNYLVDCEKK 400
Cdd:cd07931  312 RRLGFSEVQLVQDMYDGVKKLIEEEKK 338
arginine_kinase_like cd07932
Phosphagen (guanidino) kinases such as arginine kinase and similar enzymes; Eukaryotic ...
39-401 1.05e-125

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: 367.41  E-value: 1.05e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083744  39 ADAREQHKLfppsadypdLRKHnncmaecLTPTIYAKLRNKMTPSGYTLDQCIQTGVDNPGHPfiktVGMVAGDEESYEV 118
Cdd:cd07932   10 QDAEDCKSL---------LKKY-------LTPEVLKKLKDKKTKLGGTLADCIQSGAENLDSG----VGIYACDPEAYTV 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083744 119 FADLFDPVIKLRHNGYDPRVmKHPT----DLDASKITHGQFDERYVLSSRVRTGRSIRGLSLPPACSRAERREVENVAIT 194
Cdd:cd07932   70 FADLFDPVIEDYHGGFKPED-KHPApdfgDLKNLELGNLDPEGKYVISTRVRCGRSVEGYPFNPCLTKEQYIEMEEKVKS 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083744 195 ALEGLKGDLAGRYYKLSEMTEQDQQRLIDDHFLFDKPvSPLLTCAGMARDWPDARGIWHNYDKTFLIWINEEDHTRVISM 274
Cdd:cd07932  149 ALETLTGELAGTYYPLTGMDKETQQQLIDDHFLFKEG-DRFLQAAGGYRFWPTGRGIFHNDDKTFLVWVNEEDHLRIISM 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083744 275 EKGGNMKRVFERFCRGLKEVERLIQergweFMWNERLGYILTCPSNLGTGLRAGVHVRIPKLSKD-PRFSKILENLRLQK 353
Cdd:cd07932  228 QKGGDLGAVYKRLVTALKELEKKLP-----FARDDRLGYLTFCPTNLGTTLRASVHIKLPKLSKDpPRLKEICEKYNLQV 302
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 189083744 354 RGTGGVDTAAVADVYDISNIDRIGRSEVELVQIVIDGVNYLVDCEKKL 401
Cdd:cd07932  303 RGTHGEHTESVGGVYDISNKRRLGLTEFEAVKEMQDGVLELIKLEKEL 350
ATP-gua_Ptrans pfam00217
ATP:guanido phosphotransferase, C-terminal catalytic domain; The substrate binding site is ...
187-401 6.08e-110

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: 321.41  E-value: 6.08e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083744  187 EVENVAITALEGLKGDLAGRYYKLSEMTEQDQQRLIDDHFLFdkpvsplltcAGMARDWPDARGIWHNYDKTFLIWINEE 266
Cdd:pfam00217   1 EVEELVVDALESLSGDLKGKYYPLTEMDPEERQQLVEKHLIS----------PGLARDWPDGRGIFINEDETFSIWVNEE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083744  267 DHTRVISMEKGGNMKRVFERFCRGLKEVERLIqergwEFMWNERLGYILTCPSNLGTGLRAGVHVRIPKLSKD---PRFS 343
Cdd:pfam00217  71 DHLRIISMEPGGDLGEVYERANRGDDLLEEKL-----DFAFDERLGYLTSCPTNLGTGLRASVMIHLPALSKTnqiNRLL 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 189083744  344 KILENLRLQKRGTGGVDTAAVADVYDISNIDRIGRSEVELVQIVIDGVNYLVDCEKKL 401
Cdd:pfam00217 146 EALKKLGLQVRGIYGEGSEAVGGIYDISNQITLGLSEEEIVQDLIDGVKQLIEQEKKA 203
phosphagen_kinases cd00330
Phosphagen (guanidino) kinases; Phosphagen (guanidino) kinases are enzymes that ...
160-400 1.54e-109

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: 321.85  E-value: 1.54e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083744 160 VLSSRVRTGRSIRGLSLPPACSRAERREVENVAITALEGLKGDLAGRYYKLSEMTEQDQQRLIDDHFLFDKPVSPLLTcA 239
Cdd:cd00330    1 VLSSRVRLGRSFEGIRFPPRYSNEEASSIEQQFEDQLSSQEIPLIGKYYLLRMMDPAEQQQLIDDHFLFPNLTRFLQT-A 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083744 240 GMARDWPDARGIWHNYDKTFLIWINEEDHTRVISMEKGGNMKRVFERFCRGLKEVERLIqergwEFMWNERLGYILTCPS 319
Cdd:cd00330   80 NACREWPFGRGILHNDEKTFLVWVNEEDHLRIISMQKGGQLKEVMKRANTVDDWIEEKV-----DFAFNEQRGYLTSCPT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083744 320 NLGTGLRAGVHVRIPKLSKDP-RFSKILENLRLQKRGTGGVDTAAVADVYDISNIDRIGRSEVELVQIVIDGVNYLVDCE 398
Cdd:cd00330  155 NLGTGLRASVHIHLPALVKTInRIIPAINQLGLQVRGTYGEGTEAVGGVFDISNQIRLGKSEQDIVEDLNDGAAQLIEME 234

                 ..
gi 189083744 399 KK 400
Cdd:cd00330  235 RS 236
bacterial_phosphagen_kinase cd07930
Phosphagen (guanidino) kinases found in bacteria; Phosphagen (guanidino) kinases are enzymes ...
160-400 1.42e-36

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: 133.40  E-value: 1.42e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083744 160 VLSSRVRTGRSIRGLSLPPACSRAERREVENVAITALEGL--KGDLagRYYKLSEMTEQDQQRLIDDHFLfdkpvSPLLt 237
Cdd:cd07930    4 VISSRIRLARNLKGYPFPNKLSEEQAADVLEKVEKALSNIedKDEF--ELLKLKDLDPLERQVLVEKHLI-----SPEL- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083744 238 cagmARDwPDARGIWHNYDKTFLIWINEEDHTRVISMEKGGNMKRVFERfcrgLKEVERLIQERGwEFMWNERLGYILTC 317
Cdd:cd07930   76 ----AEN-KEGGAVIVNEDETVSIMINEEDHLRIQCLLPGLQLEEAYER----ADKIDDLLEEKL-DYAFDEKLGYLTAC 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083744 318 PSNLGTGLRAGVHVRIPKLSKDPRFSKILENLR---LQKRGTGGVDTAAVADVYDISNIDRIGRSEVELVQIVIDGVNYL 394
Cdd:cd07930  146 PTNVGTGLRASVMLHLPALVLTGQINRILNALSqlgLAVRGLYGEGSEALGNIYQISNQVTLGLSEEEIIENLESVVRQI 225

                 ....*.
gi 189083744 395 VDCEKK 400
Cdd:cd07930  226 IEQERE 231
ATP-gua_PtransN pfam02807
ATP:guanido phosphotransferase, N-terminal domain; The N-terminal domain has an all-alpha fold.
59-128 3.34e-36

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: 126.85  E-value: 3.34e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083744   59 KHNNCMAECLTPTIYAKLRNKMTPSGYTLDQCIQTGVDNPGHPfiktVGMVAGDEESYEVFADLFDPVIK 128
Cdd:pfam02807   2 NHNSLLKKYLTPEVYDKLKDKKTPSGFTLDDCIQSGVDNPDSG----VGVYAGDEESYEVFADLFDPIIE 67
McsB COG3869
Protein-arginine kinase McsB [Posttranslational modification, protein turnover, chaperones];
160-400 7.12e-35

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


Pssm-ID: 443078  Cd Length: 353  Bit Score: 132.22  E-value: 7.12e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083744 160 VLSSRVRTGRSIRGLSLPPACSRAERREVENVAITALEGLKGDLAGR--YYKLSEMTEQDQQRLIDDHFlfdkpVSPLLt 237
Cdd:COG3869   24 VLSSRIRLARNLAGFPFPHRASEEEAEQVLSLVREALLSLSFQELGKfeLIKLEDLSPLERQVLVEKHL-----ISPEL- 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083744 238 cagmARDwPDARGIWHNYDKTFLIWINEEDHTRVISMEKGGNMKRVFERfcrgLKEVERLIQERgWEFMWNERLGYILTC 317
Cdd:COG3869   98 ----AEN-PGGRAVLLSEDESVSIMVNEEDHLRIQCLLPGLQLEEAWEL----ANKIDDALEEK-LDYAFDEKFGYLTSC 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083744 318 PSNLGTGLRAGVHVRIPKLSKDPRFSKILENLR---LQKRGTGGVDTAAVADVYDISNIDRIGRSEVELVQIVIDGVNYL 394
Cdd:COG3869  168 PTNVGTGLRASVMLHLPALVLTGQINRVLQALNqlgLTVRGLYGEGSEALGNIFQISNQITLGKSEEEIIENLESVVRQI 247

                 ....*.
gi 189083744 395 VDCEKK 400
Cdd:COG3869  248 IEQERN 253
PRK01059 PRK01059
ATP:guanido phosphotransferase; Provisional
139-400 1.13e-32

ATP:guanido phosphotransferase; Provisional


Pssm-ID: 234894 [Multi-domain]  Cd Length: 346  Bit Score: 126.09  E-value: 1.13e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083744 139 MKHPTDLDASKITHGQFDERYVLSSRVRTGRSIRGLSLPPACSRAERREVENVAITALEGLKGDLAGR--YYKLSEMTEQ 216
Cdd:PRK01059   1 MKLPNDALSNWMKGDGPDSDIVLSSRIRLARNLKDIPFPNKLSEEEARDIIELVEKAFLNNEIEGFGEfeLLKLKDLDPL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083744 217 DQQRLIDdHFLFdkpvSPLLTcagmarDWPDARGIWHNYDKTFLIWINEEDHTRVISMEKGGNMKRVFERfcrgLKEVER 296
Cdd:PRK01059  81 EKEVLVE-KHLI----SPDLA------ENPEGGAVLLNEDETISIMINEEDHLRIQCIDPGLQLEEALEK----ANQIDD 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083744 297 LIQERgWEFMWNERLGYILTCPSNLGTGLRAGVHVRIPKLSKDPRFSKILENLR---LQKRGTGGVDTAAVADVYDISNI 373
Cdd:PRK01059 146 LLEEK-LDYAFDEKLGYLTSCPTNVGTGLRASVMLHLPALVLTKRINRILQAINqlgLTVRGIYGEGSEALGNIYQISNQ 224
                        250       260
                 ....*....|....*....|....*..
gi 189083744 374 DRIGRSEVELVQIVIDGVNYLVDCEKK 400
Cdd:PRK01059 225 ITLGKSEEEIISNLRSVVNQIISQERA 251
 
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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