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Conserved domains on  [gi|1013371617|ref|NP_001308856|]
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creatine kinase U-type, mitochondrial isoform 2 [Homo sapiens]

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 ...
80-437 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: 700.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013371617  80 PSAEYPDLRKHNNCMASHLTPAVYARLCDKTTPTGWTLDQCIQTGVDNPGHPFIKTVGMVAGDEETYEVFADLFDPVIQE 159
Cdd:cd00716     1 APENFPDLSKHNNHMAKVLTPEMYAKLRDKVTPNGVTLDKCIQTGVDNPGHPFIKTVGCVAGDEESYEVFKDLFDPVIDE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013371617 160 RHNGYdPRTMKHTTDLDASKIRSGYFDERYVLSSRVRTGRSIRGLSLPPACTRAERREVERVVVDALSGLKGDLAGRYYR 239
Cdd:cd00716    81 RHGGY-KPTAKHPTDLDPTKLKGGQFDPKYVLSSRVRTGRSIRGFCLPPHCSRAERREVEKIAVEALASLDGDLKGKYYP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013371617 240 LSEMTEAEQQQLIDDHFLFDKPVSPLLTAAGMARDWPDARGIWHNNEKSFLIWVNEEDHTRVISMEKGGNMKRVFERFCR 319
Cdd:cd00716   160 LSGMTEEEQQQLIEDHFLFDKPVSPLLLSSGMARDWPDARGIWHNDDKTFLVWVNEEDHLRVISMQKGGDMKAVFARFCR 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013371617 320 GLKEVERLIQERGWEFMWNERLGYILTCPSNLGTGLRAGVHIKLPLLSKDSRFPKILENLRLQKRGTGGVDTAATGGVFD 399
Cdd:cd00716   240 GLTEVEKLMKKKGYEFMWNEHLGYVLTCPSNLGTGLRASVHVKLPNLSKDPRFDEILRKLRLQKRGTGGVDTAAVGGTYD 319
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1013371617 400 ISNLDRLGKSEVELVQLVIDGVNYLIDCERRLERGQDI 437
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 ...
80-437 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: 700.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013371617  80 PSAEYPDLRKHNNCMASHLTPAVYARLCDKTTPTGWTLDQCIQTGVDNPGHPFIKTVGMVAGDEETYEVFADLFDPVIQE 159
Cdd:cd00716     1 APENFPDLSKHNNHMAKVLTPEMYAKLRDKVTPNGVTLDKCIQTGVDNPGHPFIKTVGCVAGDEESYEVFKDLFDPVIDE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013371617 160 RHNGYdPRTMKHTTDLDASKIRSGYFDERYVLSSRVRTGRSIRGLSLPPACTRAERREVERVVVDALSGLKGDLAGRYYR 239
Cdd:cd00716    81 RHGGY-KPTAKHPTDLDPTKLKGGQFDPKYVLSSRVRTGRSIRGFCLPPHCSRAERREVEKIAVEALASLDGDLKGKYYP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013371617 240 LSEMTEAEQQQLIDDHFLFDKPVSPLLTAAGMARDWPDARGIWHNNEKSFLIWVNEEDHTRVISMEKGGNMKRVFERFCR 319
Cdd:cd00716   160 LSGMTEEEQQQLIEDHFLFDKPVSPLLLSSGMARDWPDARGIWHNDDKTFLVWVNEEDHLRVISMQKGGDMKAVFARFCR 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013371617 320 GLKEVERLIQERGWEFMWNERLGYILTCPSNLGTGLRAGVHIKLPLLSKDSRFPKILENLRLQKRGTGGVDTAATGGVFD 399
Cdd:cd00716   240 GLTEVEKLMKKKGYEFMWNEHLGYVLTCPSNLGTGLRASVHVKLPNLSKDPRFDEILRKLRLQKRGTGGVDTAAVGGTYD 319
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1013371617 400 ISNLDRLGKSEVELVQLVIDGVNYLIDCERRLERGQDI 437
Cdd:cd00716   320 ISNADRLGKSEVELVQFVIDGVNLLIEMEKRLEKGKSI 357
ATP-gua_Ptrans pfam00217
ATP:guanido phosphotransferase, C-terminal catalytic domain; The substrate binding site is ...
224-431 7.98e-111

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: 324.88  E-value: 7.98e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013371617 224 DALSGLKGDLAGRYYRLSEMTEAEQQQLIDDHFLFdkpvsplltaAGMARDWPDARGIWHNNEKSFLIWVNEEDHTRVIS 303
Cdd:pfam00217   8 DALESLSGDLKGKYYPLTEMDPEERQQLVEKHLIS----------PGLARDWPDGRGIFINEDETFSIWVNEEDHLRIIS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013371617 304 MEKGGNMKRVFERFCRGLKEVERLIqergwEFMWNERLGYILTCPSNLGTGLRAGVHIKLPLLSKDSRFPKILEN---LR 380
Cdd:pfam00217  78 MEPGGDLGEVYERANRGDDLLEEKL-----DFAFDERLGYLTSCPTNLGTGLRASVMIHLPALSKTNQINRLLEAlkkLG 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1013371617 381 LQKRGTGGVDTAATGGVFDISNLDRLGKSEVELVQLVIDGVNYLIDCERRL 431
Cdd:pfam00217 153 LQVRGIYGEGSEAVGGIYDISNQITLGLSEEEIVQDLIDGVKQLIEQEKKA 203
McsB COG3869
Protein-arginine kinase McsB [Posttranslational modification, protein turnover, chaperones];
190-430 5.93e-33

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


Pssm-ID: 443078  Cd Length: 353  Bit Score: 127.60  E-value: 5.93e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013371617 190 VLSSRVRTGRSIRGLSLPPACTRAERREVERVVVDALSGLKGDLAGR--YYRLSEMTEAEQQQLIDDHFlfdkpVSPLLT 267
Cdd:COG3869    24 VLSSRIRLARNLAGFPFPHRASEEEAEQVLSLVREALLSLSFQELGKfeLIKLEDLSPLERQVLVEKHL-----ISPELA 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013371617 268 AAgmardwPDARGIWHNNEKSFLIWVNEEDHTRVISMEKGGNMKRVFERfcrgLKEVERLIQERgWEFMWNERLGYILTC 347
Cdd:COG3869    99 EN------PGGRAVLLSEDESVSIMVNEEDHLRIQCLLPGLQLEEAWEL----ANKIDDALEEK-LDYAFDEKFGYLTSC 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013371617 348 PSNLGTGLRAGVHIKLPLLSKDSRFPKILENLR---LQKRGTGGVDTAATGGVFDISNLDRLGKSEVELVQLVIDGVNYL 424
Cdd:COG3869   168 PTNVGTGLRASVMLHLPALVLTGQINRVLQALNqlgLTVRGLYGEGSEALGNIFQISNQITLGKSEEEIIENLESVVRQI 247

                  ....*.
gi 1013371617 425 IDCERR 430
Cdd:COG3869   248 IEQERN 253
PRK01059 PRK01059
ATP:guanido phosphotransferase; Provisional
190-429 1.57e-30

ATP:guanido phosphotransferase; Provisional


Pssm-ID: 234894 [Multi-domain]  Cd Length: 346  Bit Score: 120.70  E-value: 1.57e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013371617 190 VLSSRVRTGRSIRGLSLPPACTRAERREVERVVVDALSGLKGDLAGR--YYRLSEMTEAEQQQLIDdHFLFdkpvSPLLT 267
Cdd:PRK01059   22 VLSSRIRLARNLKDIPFPNKLSEEEARDIIELVEKAFLNNEIEGFGEfeLLKLKDLDPLEKEVLVE-KHLI----SPDLA 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013371617 268 AAgmardwPDARGIWHNNEKSFLIWVNEEDHTRVISMEKGGNMKRVFERfcrgLKEVERLIQERgWEFMWNERLGYILTC 347
Cdd:PRK01059   97 EN------PEGGAVLLNEDETISIMINEEDHLRIQCIDPGLQLEEALEK----ANQIDDLLEEK-LDYAFDEKLGYLTSC 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013371617 348 PSNLGTGLRAGVHIKLPLLSKDSRFPKILENLR---LQKRGTGGVDTAATGGVFDISNLDRLGKSEVELVQLVIDGVNYL 424
Cdd:PRK01059  166 PTNVGTGLRASVMLHLPALVLTKRINRILQAINqlgLTVRGIYGEGSEALGNIYQISNQITLGKSEEEIISNLRSVVNQI 245

                  ....*
gi 1013371617 425 IDCER 429
Cdd:PRK01059  246 ISQER 250
 
Name Accession Description Interval E-value
creatine_kinase_like cd00716
Phosphagen (guanidino) kinases such as creatine kinase and similar enzymes; Eukaryotic ...
80-437 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: 700.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013371617  80 PSAEYPDLRKHNNCMASHLTPAVYARLCDKTTPTGWTLDQCIQTGVDNPGHPFIKTVGMVAGDEETYEVFADLFDPVIQE 159
Cdd:cd00716     1 APENFPDLSKHNNHMAKVLTPEMYAKLRDKVTPNGVTLDKCIQTGVDNPGHPFIKTVGCVAGDEESYEVFKDLFDPVIDE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013371617 160 RHNGYdPRTMKHTTDLDASKIRSGYFDERYVLSSRVRTGRSIRGLSLPPACTRAERREVERVVVDALSGLKGDLAGRYYR 239
Cdd:cd00716    81 RHGGY-KPTAKHPTDLDPTKLKGGQFDPKYVLSSRVRTGRSIRGFCLPPHCSRAERREVEKIAVEALASLDGDLKGKYYP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013371617 240 LSEMTEAEQQQLIDDHFLFDKPVSPLLTAAGMARDWPDARGIWHNNEKSFLIWVNEEDHTRVISMEKGGNMKRVFERFCR 319
Cdd:cd00716   160 LSGMTEEEQQQLIEDHFLFDKPVSPLLLSSGMARDWPDARGIWHNDDKTFLVWVNEEDHLRVISMQKGGDMKAVFARFCR 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013371617 320 GLKEVERLIQERGWEFMWNERLGYILTCPSNLGTGLRAGVHIKLPLLSKDSRFPKILENLRLQKRGTGGVDTAATGGVFD 399
Cdd:cd00716   240 GLTEVEKLMKKKGYEFMWNEHLGYVLTCPSNLGTGLRASVHVKLPNLSKDPRFDEILRKLRLQKRGTGGVDTAAVGGTYD 319
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1013371617 400 ISNLDRLGKSEVELVQLVIDGVNYLIDCERRLERGQDI 437
Cdd:cd00716   320 ISNADRLGKSEVELVQFVIDGVNLLIEMEKRLEKGKSI 357
eukaryotic_phosphagen_kinases cd07931
Phosphagen (guanidino) kinases mostly found in eukaryotes; Phosphagen (guanidino) kinases are ...
87-430 1.59e-164

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: 466.75  E-value: 1.59e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013371617  87 LRKHNNCMASHLTPAVYARLCDKTTPTGWTLDQCIQTGVDNPGhpfiKTVGMVAGDEETYEVFADLFDPVIQERHNGYDP 166
Cdd:cd07931     1 LESNKSLLAKYLTPEVYEKLKNRKTASGFTLADVIQSGVDNPD----SGVGVYAGDEESYDVFAPLFDPVIEDYHGGYKP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013371617 167 rTMKHTTDLDASKIRSGYFDER--YVLSSRVRTGRSIRGLSLPPACTRAERREVERVVVDALSGLKGDLAGRYYRLSEMT 244
Cdd:cd07931    77 -EDKHTSDLDPEKPGLEDLDPRkkYIISTRIRVARNLDGFPLPPGMTKEQRRQIERLMVSALSSLEGDLKGTYYSLTEMT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013371617 245 EAEQQQLIDDHFLFDKPvSPLLTAAGMARDWPDARGIWHNNEKSFLIWVNEEDHTRVISMEKGGNMKRVFERFCRGLKEV 324
Cdd:cd07931   156 EEQQQQLIDDHFLFKDG-DRFLEAAGENRDWPDGRGIFHNSDKTFLVWVNEEDHLRIISMQKGGDLKAVFTRLSRALTEI 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013371617 325 ERLIQErgwEFMWNERLGYILTCPSNLGTGLRAGVHIKLPLLSKDS-RFPKILENLRLQKRGTGGVDTAATGGVFDISNL 403
Cdd:cd07931   235 EKSLKE---EFAHDPHLGYITSCPTNLGTGMRASVHVKLPNLIKDMdKLKAIARKLGLQIRGIGGEHSESEGGVVDISNK 311
                         330       340
                  ....*....|....*....|....*..
gi 1013371617 404 DRLGKSEVELVQLVIDGVNYLIDCERR 430
Cdd:cd07931   312 RRLGFSEVQLVQDMYDGVKKLIEEEKK 338
arginine_kinase_like cd07932
Phosphagen (guanidino) kinases such as arginine kinase and similar enzymes; Eukaryotic ...
80-431 3.44e-123

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: 362.02  E-value: 3.44e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013371617  80 PSAEYPDLRKHNNC---MASHLTPAVYARLCDKTTPTGWTLDQCIQTGVDNPGHPfiktVGMVAGDEETYEVFADLFDPV 156
Cdd:cd07932     2 LEEELAKLQDAEDCkslLKKYLTPEVLKKLKDKKTKLGGTLADCIQSGAENLDSG----VGIYACDPEAYTVFADLFDPV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013371617 157 IQERHNGYDPrTMKHTtDLDASKIRSGYF-----DERYVLSSRVRTGRSIRGLSLPPACTRAERREVERVVVDALSGLKG 231
Cdd:cd07932    78 IEDYHGGFKP-EDKHP-APDFGDLKNLELgnldpEGKYVISTRVRCGRSVEGYPFNPCLTKEQYIEMEEKVKSALETLTG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013371617 232 DLAGRYYRLSEMTEAEQQQLIDDHFLFDKPvSPLLTAAGMARDWPDARGIWHNNEKSFLIWVNEEDHTRVISMEKGGNMK 311
Cdd:cd07932   156 ELAGTYYPLTGMDKETQQQLIDDHFLFKEG-DRFLQAAGGYRFWPTGRGIFHNDDKTFLVWVNEEDHLRIISMQKGGDLG 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013371617 312 RVFERFCRGLKEVERLIQergweFMWNERLGYILTCPSNLGTGLRAGVHIKLPLLSKD-SRFPKILENLRLQKRGTGGVD 390
Cdd:cd07932   235 AVYKRLVTALKELEKKLP-----FARDDRLGYLTFCPTNLGTTLRASVHIKLPKLSKDpPRLKEICEKYNLQVRGTHGEH 309
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1013371617 391 TAATGGVFDISNLDRLGKSEVELVQLVIDGVNYLIDCERRL 431
Cdd:cd07932   310 TESVGGVYDISNKRRLGLTEFEAVKEMQDGVLELIKLEKEL 350
phosphagen_kinases cd00330
Phosphagen (guanidino) kinases; Phosphagen (guanidino) kinases are enzymes that ...
190-430 1.60e-113

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: 333.02  E-value: 1.60e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013371617 190 VLSSRVRTGRSIRGLSLPPACTRAERREVERVVVDALSGLKGDLAGRYYRLSEMTEAEQQQLIDDHFLFDKPVSPLLTaA 269
Cdd:cd00330     1 VLSSRVRLGRSFEGIRFPPRYSNEEASSIEQQFEDQLSSQEIPLIGKYYLLRMMDPAEQQQLIDDHFLFPNLTRFLQT-A 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013371617 270 GMARDWPDARGIWHNNEKSFLIWVNEEDHTRVISMEKGGNMKRVFERFCRGLKEVERLIqergwEFMWNERLGYILTCPS 349
Cdd:cd00330    80 NACREWPFGRGILHNDEKTFLVWVNEEDHLRIISMQKGGQLKEVMKRANTVDDWIEEKV-----DFAFNEQRGYLTSCPT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013371617 350 NLGTGLRAGVHIKLPLLSKD-SRFPKILENLRLQKRGTGGVDTAATGGVFDISNLDRLGKSEVELVQLVIDGVNYLIDCE 428
Cdd:cd00330   155 NLGTGLRASVHIHLPALVKTiNRIIPAINQLGLQVRGTYGEGTEAVGGVFDISNQIRLGKSEQDIVEDLNDGAAQLIEME 234

                  ..
gi 1013371617 429 RR 430
Cdd:cd00330   235 RS 236
ATP-gua_Ptrans pfam00217
ATP:guanido phosphotransferase, C-terminal catalytic domain; The substrate binding site is ...
224-431 7.98e-111

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: 324.88  E-value: 7.98e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013371617 224 DALSGLKGDLAGRYYRLSEMTEAEQQQLIDDHFLFdkpvsplltaAGMARDWPDARGIWHNNEKSFLIWVNEEDHTRVIS 303
Cdd:pfam00217   8 DALESLSGDLKGKYYPLTEMDPEERQQLVEKHLIS----------PGLARDWPDGRGIFINEDETFSIWVNEEDHLRIIS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013371617 304 MEKGGNMKRVFERFCRGLKEVERLIqergwEFMWNERLGYILTCPSNLGTGLRAGVHIKLPLLSKDSRFPKILEN---LR 380
Cdd:pfam00217  78 MEPGGDLGEVYERANRGDDLLEEKL-----DFAFDERLGYLTSCPTNLGTGLRASVMIHLPALSKTNQINRLLEAlkkLG 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1013371617 381 LQKRGTGGVDTAATGGVFDISNLDRLGKSEVELVQLVIDGVNYLIDCERRL 431
Cdd:pfam00217 153 LQVRGIYGEGSEAVGGIYDISNQITLGLSEEEIVQDLIDGVKQLIEQEKKA 203
ATP-gua_PtransN pfam02807
ATP:guanido phosphotransferase, N-terminal domain; The N-terminal domain has an all-alpha fold.
89-158 3.19e-35

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: 124.92  E-value: 3.19e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013371617  89 KHNNCMASHLTPAVYARLCDKTTPTGWTLDQCIQTGVDNPGHPfiktVGMVAGDEETYEVFADLFDPVIQ 158
Cdd:pfam02807   2 NHNSLLKKYLTPEVYDKLKDKKTPSGFTLDDCIQSGVDNPDSG----VGVYAGDEESYEVFADLFDPIIE 67
bacterial_phosphagen_kinase cd07930
Phosphagen (guanidino) kinases found in bacteria; Phosphagen (guanidino) kinases are enzymes ...
190-430 1.78e-34

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


Pssm-ID: 153077  Cd Length: 232  Bit Score: 128.40  E-value: 1.78e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013371617 190 VLSSRVRTGRSIRGLSLPPACTRAERREVERVVVDALSGL--KGDLagRYYRLSEMTEAEQQQLIDDHFLfdkpvSPLLT 267
Cdd:cd07930     4 VISSRIRLARNLKGYPFPNKLSEEQAADVLEKVEKALSNIedKDEF--ELLKLKDLDPLERQVLVEKHLI-----SPELA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013371617 268 AAgmardwPDARGIWHNNEKSFLIWVNEEDHTRVISMEKGGNMKRVFERfcrgLKEVERLIQERGwEFMWNERLGYILTC 347
Cdd:cd07930    77 EN------KEGGAVIVNEDETVSIMINEEDHLRIQCLLPGLQLEEAYER----ADKIDDLLEEKL-DYAFDEKLGYLTAC 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013371617 348 PSNLGTGLRAGVHIKLPLLSKDSRFPKILENLR---LQKRGTGGVDTAATGGVFDISNLDRLGKSEVELVQLVIDGVNYL 424
Cdd:cd07930   146 PTNVGTGLRASVMLHLPALVLTGQINRILNALSqlgLAVRGLYGEGSEALGNIYQISNQVTLGLSEEEIIENLESVVRQI 225

                  ....*.
gi 1013371617 425 IDCERR 430
Cdd:cd07930   226 IEQERE 231
McsB COG3869
Protein-arginine kinase McsB [Posttranslational modification, protein turnover, chaperones];
190-430 5.93e-33

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


Pssm-ID: 443078  Cd Length: 353  Bit Score: 127.60  E-value: 5.93e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013371617 190 VLSSRVRTGRSIRGLSLPPACTRAERREVERVVVDALSGLKGDLAGR--YYRLSEMTEAEQQQLIDDHFlfdkpVSPLLT 267
Cdd:COG3869    24 VLSSRIRLARNLAGFPFPHRASEEEAEQVLSLVREALLSLSFQELGKfeLIKLEDLSPLERQVLVEKHL-----ISPELA 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013371617 268 AAgmardwPDARGIWHNNEKSFLIWVNEEDHTRVISMEKGGNMKRVFERfcrgLKEVERLIQERgWEFMWNERLGYILTC 347
Cdd:COG3869    99 EN------PGGRAVLLSEDESVSIMVNEEDHLRIQCLLPGLQLEEAWEL----ANKIDDALEEK-LDYAFDEKFGYLTSC 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013371617 348 PSNLGTGLRAGVHIKLPLLSKDSRFPKILENLR---LQKRGTGGVDTAATGGVFDISNLDRLGKSEVELVQLVIDGVNYL 424
Cdd:COG3869   168 PTNVGTGLRASVMLHLPALVLTGQINRVLQALNqlgLTVRGLYGEGSEALGNIFQISNQITLGKSEEEIIENLESVVRQI 247

                  ....*.
gi 1013371617 425 IDCERR 430
Cdd:COG3869   248 IEQERN 253
PRK01059 PRK01059
ATP:guanido phosphotransferase; Provisional
190-429 1.57e-30

ATP:guanido phosphotransferase; Provisional


Pssm-ID: 234894 [Multi-domain]  Cd Length: 346  Bit Score: 120.70  E-value: 1.57e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013371617 190 VLSSRVRTGRSIRGLSLPPACTRAERREVERVVVDALSGLKGDLAGR--YYRLSEMTEAEQQQLIDdHFLFdkpvSPLLT 267
Cdd:PRK01059   22 VLSSRIRLARNLKDIPFPNKLSEEEARDIIELVEKAFLNNEIEGFGEfeLLKLKDLDPLEKEVLVE-KHLI----SPDLA 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013371617 268 AAgmardwPDARGIWHNNEKSFLIWVNEEDHTRVISMEKGGNMKRVFERfcrgLKEVERLIQERgWEFMWNERLGYILTC 347
Cdd:PRK01059   97 EN------PEGGAVLLNEDETISIMINEEDHLRIQCIDPGLQLEEALEK----ANQIDDLLEEK-LDYAFDEKLGYLTSC 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013371617 348 PSNLGTGLRAGVHIKLPLLSKDSRFPKILENLR---LQKRGTGGVDTAATGGVFDISNLDRLGKSEVELVQLVIDGVNYL 424
Cdd:PRK01059  166 PTNVGTGLRASVMLHLPALVLTKRINRILQAINqlgLTVRGIYGEGSEALGNIYQISNQITLGKSEEEIISNLRSVVNQI 245

                  ....*
gi 1013371617 425 IDCER 429
Cdd:PRK01059  246 ISQER 250
 
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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