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Conserved domains on  [gi|401461784|ref|NP_036661|]
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creatine kinase B-type [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 ...
16-373 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: 748.01  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461784  16 AEDEFPDLSSHNNHMAKVLTPELYAELRAKCTPSGFTLDDAIQTGVDNPGHPYIMTVGAVAGDEESYDVFKDLFDPIIED 95
Cdd:cd00716    1 APENFPDLSKHNNHMAKVLTPEMYAKLRDKVTPNGVTLDKCIQTGVDNPGHPFIKTVGCVAGDEESYEVFKDLFDPVIDE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461784  96 RHGGYQPSDEHKTDLNPDNLQGGDdLDPNYVLSSRVRTGRSIRGFCLPPHCSRGERRAIEKLAVEALSSLDGDLSGRYYA 175
Cdd:cd00716   81 RHGGYKPTAKHPTDLDPTKLKGGQ-FDPKYVLSSRVRTGRSIRGFCLPPHCSRAERREVEKIAVEALASLDGDLKGKYYP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461784 176 LKSMTEAEQQQLIDDHFLFDKPVSPLLLASGMARDWPDARGIWHNDNKTFLVWINEEDHLRVISMQKGGNMKEVFTRFCT 255
Cdd:cd00716  160 LSGMTEEEQQQLIEDHFLFDKPVSPLLLSSGMARDWPDARGIWHNDDKTFLVWVNEEDHLRVISMQKGGDMKAVFARFCR 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461784 256 GLTQIETLFKSKNYEFMWNPHLGYILTCPSNLGTGLRAGVHIKLPHLGKHEKFSEVLKRLRLQKRGTGGVDTAAVGGVFD 335
Cdd:cd00716  240 GLTEVEKLMKKKGYEFMWNEHLGYVLTCPSNLGTGLRASVHVKLPNLSKDPRFDEILRKLRLQKRGTGGVDTAAVGGTYD 319
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 401461784 336 VSNADRLGFSEVELVQMVVDGVKLLIEMEQRLEQGQPI 373
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 ...
16-373 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: 748.01  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461784  16 AEDEFPDLSSHNNHMAKVLTPELYAELRAKCTPSGFTLDDAIQTGVDNPGHPYIMTVGAVAGDEESYDVFKDLFDPIIED 95
Cdd:cd00716    1 APENFPDLSKHNNHMAKVLTPEMYAKLRDKVTPNGVTLDKCIQTGVDNPGHPFIKTVGCVAGDEESYEVFKDLFDPVIDE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461784  96 RHGGYQPSDEHKTDLNPDNLQGGDdLDPNYVLSSRVRTGRSIRGFCLPPHCSRGERRAIEKLAVEALSSLDGDLSGRYYA 175
Cdd:cd00716   81 RHGGYKPTAKHPTDLDPTKLKGGQ-FDPKYVLSSRVRTGRSIRGFCLPPHCSRAERREVEKIAVEALASLDGDLKGKYYP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461784 176 LKSMTEAEQQQLIDDHFLFDKPVSPLLLASGMARDWPDARGIWHNDNKTFLVWINEEDHLRVISMQKGGNMKEVFTRFCT 255
Cdd:cd00716  160 LSGMTEEEQQQLIEDHFLFDKPVSPLLLSSGMARDWPDARGIWHNDDKTFLVWVNEEDHLRVISMQKGGDMKAVFARFCR 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461784 256 GLTQIETLFKSKNYEFMWNPHLGYILTCPSNLGTGLRAGVHIKLPHLGKHEKFSEVLKRLRLQKRGTGGVDTAAVGGVFD 335
Cdd:cd00716  240 GLTEVEKLMKKKGYEFMWNEHLGYVLTCPSNLGTGLRASVHVKLPNLSKDPRFDEILRKLRLQKRGTGGVDTAAVGGTYD 319
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 401461784 336 VSNADRLGFSEVELVQMVVDGVKLLIEMEQRLEQGQPI 373
Cdd:cd00716  320 ISNADRLGKSEVELVQFVIDGVNLLIEMEKRLEKGKSI 357
ATP-gua_Ptrans pfam00217
ATP:guanido phosphotransferase, C-terminal catalytic domain; The substrate binding site is ...
154-367 1.25e-115

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: 334.51  E-value: 1.25e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461784  154 IEKLAVEALSSLDGDLSGRYYALKSMTEAEQQQLIDDHFLFdkpvsplllaSGMARDWPDARGIWHNDNKTFLVWINEED 233
Cdd:pfam00217   2 VEELVVDALESLSGDLKGKYYPLTEMDPEERQQLVEKHLIS----------PGLARDWPDGRGIFINEDETFSIWVNEED 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461784  234 HLRVISMQKGGNMKEVFTRFCTGLTQIEtlfksKNYEFMWNPHLGYILTCPSNLGTGLRAGVHIKLPHLGKH---EKFSE 310
Cdd:pfam00217  72 HLRIISMEPGGDLGEVYERANRGDDLLE-----EKLDFAFDERLGYLTSCPTNLGTGLRASVMIHLPALSKTnqiNRLLE 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 401461784  311 VLKRLRLQKRGTGGVDTAAVGGVFDVSNADRLGFSEVELVQMVVDGVKLLIEMEQRL 367
Cdd:pfam00217 147 ALKKLGLQVRGIYGEGSEAVGGIYDISNQITLGLSEEEIVQDLIDGVKQLIEQEKKA 203
McsB COG3869
Protein-arginine kinase McsB [Posttranslational modification, protein turnover, chaperones];
118-366 7.54e-39

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


Pssm-ID: 443078  Cd Length: 353  Bit Score: 141.85  E-value: 7.54e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461784 118 GDDLDPNYVLSSRVRTGRSIRGFCLPPHCSRGERRAIEKLAVEALSSLDGDLSGR--YYALKSMTEAEQQQLIDDHFlfd 195
Cdd:COG3869   16 GSGPESDIVLSSRIRLARNLAGFPFPHRASEEEAEQVLSLVREALLSLSFQELGKfeLIKLEDLSPLERQVLVEKHL--- 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461784 196 kpVSPLLLASgmardwPDARGIWHNDNKTFLVWINEEDHLRVISMQKGGNMKEVFTRfctgLTQIETLFKSK-NYEFmwN 274
Cdd:COG3869   93 --ISPELAEN------PGGRAVLLSEDESVSIMVNEEDHLRIQCLLPGLQLEEAWEL----ANKIDDALEEKlDYAF--D 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461784 275 PHLGYILTCPSNLGTGLRAGVHIKLPHLGKHEKFSEVL---KRLRLQKRGTGGVDTAAVGGVFDVSNADRLGFSEVELVQ 351
Cdd:COG3869  159 EKFGYLTSCPTNVGTGLRASVMLHLPALVLTGQINRVLqalNQLGLTVRGLYGEGSEALGNIFQISNQITLGKSEEEIIE 238
                        250
                 ....*....|....*
gi 401461784 352 MVVDGVKLLIEMEQR 366
Cdd:COG3869  239 NLESVVRQIIEQERN 253
PRK01059 PRK01059
ATP:guanido phosphotransferase; Provisional
118-364 1.30e-33

ATP:guanido phosphotransferase; Provisional


Pssm-ID: 234894 [Multi-domain]  Cd Length: 346  Bit Score: 127.63  E-value: 1.30e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461784 118 GDDLDPNYVLSSRVRTGRSIRGFCLPPHCSRGERRAIEKLAVEALSSLDGDLSGR--YYALKSMTEAEQQQLIDdHFLFd 195
Cdd:PRK01059  14 GDGPDSDIVLSSRIRLARNLKDIPFPNKLSEEEARDIIELVEKAFLNNEIEGFGEfeLLKLKDLDPLEKEVLVE-KHLI- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461784 196 kpvSPLLLASgmardwPDARGIWHNDNKTFLVWINEEDHLRVISMQKGGNMKEVFTRfctgLTQIETLFKSK-NYEFmwN 274
Cdd:PRK01059  92 ---SPDLAEN------PEGGAVLLNEDETISIMINEEDHLRIQCIDPGLQLEEALEK----ANQIDDLLEEKlDYAF--D 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461784 275 PHLGYILTCPSNLGTGLRAGVHIKLPHL---GKHEKFSEVLKRLRLQKRGTGGVDTAAVGGVFDVSNADRLGFSEVELVQ 351
Cdd:PRK01059 157 EKLGYLTSCPTNVGTGLRASVMLHLPALvltKRINRILQAINQLGLTVRGIYGEGSEALGNIYQISNQITLGKSEEEIIS 236
                        250
                 ....*....|...
gi 401461784 352 MVVDGVKLLIEME 364
Cdd:PRK01059 237 NLRSVVNQIISQE 249
 
Name Accession Description Interval E-value
creatine_kinase_like cd00716
Phosphagen (guanidino) kinases such as creatine kinase and similar enzymes; Eukaryotic ...
16-373 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: 748.01  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461784  16 AEDEFPDLSSHNNHMAKVLTPELYAELRAKCTPSGFTLDDAIQTGVDNPGHPYIMTVGAVAGDEESYDVFKDLFDPIIED 95
Cdd:cd00716    1 APENFPDLSKHNNHMAKVLTPEMYAKLRDKVTPNGVTLDKCIQTGVDNPGHPFIKTVGCVAGDEESYEVFKDLFDPVIDE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461784  96 RHGGYQPSDEHKTDLNPDNLQGGDdLDPNYVLSSRVRTGRSIRGFCLPPHCSRGERRAIEKLAVEALSSLDGDLSGRYYA 175
Cdd:cd00716   81 RHGGYKPTAKHPTDLDPTKLKGGQ-FDPKYVLSSRVRTGRSIRGFCLPPHCSRAERREVEKIAVEALASLDGDLKGKYYP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461784 176 LKSMTEAEQQQLIDDHFLFDKPVSPLLLASGMARDWPDARGIWHNDNKTFLVWINEEDHLRVISMQKGGNMKEVFTRFCT 255
Cdd:cd00716  160 LSGMTEEEQQQLIEDHFLFDKPVSPLLLSSGMARDWPDARGIWHNDDKTFLVWVNEEDHLRVISMQKGGDMKAVFARFCR 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461784 256 GLTQIETLFKSKNYEFMWNPHLGYILTCPSNLGTGLRAGVHIKLPHLGKHEKFSEVLKRLRLQKRGTGGVDTAAVGGVFD 335
Cdd:cd00716  240 GLTEVEKLMKKKGYEFMWNEHLGYVLTCPSNLGTGLRASVHVKLPNLSKDPRFDEILRKLRLQKRGTGGVDTAAVGGTYD 319
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 401461784 336 VSNADRLGFSEVELVQMVVDGVKLLIEMEQRLEQGQPI 373
Cdd:cd00716  320 ISNADRLGKSEVELVQFVIDGVNLLIEMEKRLEKGKSI 357
eukaryotic_phosphagen_kinases cd07931
Phosphagen (guanidino) kinases mostly found in eukaryotes; Phosphagen (guanidino) kinases are ...
23-366 0e+00

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: 527.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461784  23 LSSHNNHMAKVLTPELYAELRAKCTPSGFTLDDAIQTGVDNPGhpyiMTVGAVAGDEESYDVFKDLFDPIIEDRHGGYQP 102
Cdd:cd07931    1 LESNKSLLAKYLTPEVYEKLKNRKTASGFTLADVIQSGVDNPD----SGVGVYAGDEESYDVFAPLFDPVIEDYHGGYKP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461784 103 SDEHKTDLNPDNlQGGDDLDPN--YVLSSRVRTGRSIRGFCLPPHCSRGERRAIEKLAVEALSSLDGDLSGRYYALKSMT 180
Cdd:cd07931   77 EDKHTSDLDPEK-PGLEDLDPRkkYIISTRIRVARNLDGFPLPPGMTKEQRRQIERLMVSALSSLEGDLKGTYYSLTEMT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461784 181 EAEQQQLIDDHFLFDKPvSPLLLASGMARDWPDARGIWHNDNKTFLVWINEEDHLRVISMQKGGNMKEVFTRFCTGLTQI 260
Cdd:cd07931  156 EEQQQQLIDDHFLFKDG-DRFLEAAGENRDWPDGRGIFHNSDKTFLVWVNEEDHLRIISMQKGGDLKAVFTRLSRALTEI 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461784 261 ETLFKSknyEFMWNPHLGYILTCPSNLGTGLRAGVHIKLPHLGKH-EKFSEVLKRLRLQKRGTGGVDTAAVGGVFDVSNA 339
Cdd:cd07931  235 EKSLKE---EFAHDPHLGYITSCPTNLGTGMRASVHVKLPNLIKDmDKLKAIARKLGLQIRGIGGEHSESEGGVVDISNK 311
                        330       340
                 ....*....|....*....|....*..
gi 401461784 340 DRLGFSEVELVQMVVDGVKLLIEMEQR 366
Cdd:cd07931  312 RRLGFSEVQLVQDMYDGVKKLIEEEKK 338
phosphagen_kinases cd00330
Phosphagen (guanidino) kinases; Phosphagen (guanidino) kinases are enzymes that ...
126-366 6.49e-147

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: 415.45  E-value: 6.49e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461784 126 VLSSRVRTGRSIRGFCLPPHCSRGERRAIEKLAVEALSSLDGDLSGRYYALKSMTEAEQQQLIDDHFLFDKPVSPLLLaS 205
Cdd:cd00330    1 VLSSRVRLGRSFEGIRFPPRYSNEEASSIEQQFEDQLSSQEIPLIGKYYLLRMMDPAEQQQLIDDHFLFPNLTRFLQT-A 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461784 206 GMARDWPDARGIWHNDNKTFLVWINEEDHLRVISMQKGGNMKEVFTRFCTGLTQIETLFKsknyeFMWNPHLGYILTCPS 285
Cdd:cd00330   80 NACREWPFGRGILHNDEKTFLVWVNEEDHLRIISMQKGGQLKEVMKRANTVDDWIEEKVD-----FAFNEQRGYLTSCPT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461784 286 NLGTGLRAGVHIKLPHLGKH-EKFSEVLKRLRLQKRGTGGVDTAAVGGVFDVSNADRLGFSEVELVQMVVDGVKLLIEME 364
Cdd:cd00330  155 NLGTGLRASVHIHLPALVKTiNRIIPAINQLGLQVRGTYGEGTEAVGGVFDISNQIRLGKSEQDIVEDLNDGAAQLIEME 234

                 ..
gi 401461784 365 QR 366
Cdd:cd00330  235 RS 236
arginine_kinase_like cd07932
Phosphagen (guanidino) kinases such as arginine kinase and similar enzymes; Eukaryotic ...
17-367 3.50e-133

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: 384.74  E-value: 3.50e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461784  17 EDEFPDLSS-HNNH--MAKVLTPELYAELRAKCTPSGFTLDDAIQTGVDNPGHPyimtVGAVAGDEESYDVFKDLFDPII 93
Cdd:cd07932    3 EEELAKLQDaEDCKslLKKYLTPEVLKKLKDKKTKLGGTLADCIQSGAENLDSG----VGIYACDPEAYTVFADLFDPVI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461784  94 EDRHGGYQPSDEH-KTDLNPDNLQGGDDLDP--NYVLSSRVRTGRSIRGFCLPPHCSRGERRAIEKLAVEALSSLDGDLS 170
Cdd:cd07932   79 EDYHGGFKPEDKHpAPDFGDLKNLELGNLDPegKYVISTRVRCGRSVEGYPFNPCLTKEQYIEMEEKVKSALETLTGELA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461784 171 GRYYALKSMTEAEQQQLIDDHFLFDKPvSPLLLASGMARDWPDARGIWHNDNKTFLVWINEEDHLRVISMQKGGNMKEVF 250
Cdd:cd07932  159 GTYYPLTGMDKETQQQLIDDHFLFKEG-DRFLQAAGGYRFWPTGRGIFHNDDKTFLVWVNEEDHLRIISMQKGGDLGAVY 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461784 251 TRFCTGLTQIEtlfksKNYEFMWNPHLGYILTCPSNLGTGLRAGVHIKLPHLGK-HEKFSEVLKRLRLQKRGTGGVDTAA 329
Cdd:cd07932  238 KRLVTALKELE-----KKLPFARDDRLGYLTFCPTNLGTTLRASVHIKLPKLSKdPPRLKEICEKYNLQVRGTHGEHTES 312
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 401461784 330 VGGVFDVSNADRLGFSEVELVQMVVDGVKLLIEMEQRL 367
Cdd:cd07932  313 VGGVYDISNKRRLGLTEFEAVKEMQDGVLELIKLEKEL 350
ATP-gua_Ptrans pfam00217
ATP:guanido phosphotransferase, C-terminal catalytic domain; The substrate binding site is ...
154-367 1.25e-115

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: 334.51  E-value: 1.25e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461784  154 IEKLAVEALSSLDGDLSGRYYALKSMTEAEQQQLIDDHFLFdkpvsplllaSGMARDWPDARGIWHNDNKTFLVWINEED 233
Cdd:pfam00217   2 VEELVVDALESLSGDLKGKYYPLTEMDPEERQQLVEKHLIS----------PGLARDWPDGRGIFINEDETFSIWVNEED 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461784  234 HLRVISMQKGGNMKEVFTRFCTGLTQIEtlfksKNYEFMWNPHLGYILTCPSNLGTGLRAGVHIKLPHLGKH---EKFSE 310
Cdd:pfam00217  72 HLRIISMEPGGDLGEVYERANRGDDLLE-----EKLDFAFDERLGYLTSCPTNLGTGLRASVMIHLPALSKTnqiNRLLE 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 401461784  311 VLKRLRLQKRGTGGVDTAAVGGVFDVSNADRLGFSEVELVQMVVDGVKLLIEMEQRL 367
Cdd:pfam00217 147 ALKKLGLQVRGIYGEGSEAVGGIYDISNQITLGLSEEEIVQDLIDGVKQLIEQEKKA 203
McsB COG3869
Protein-arginine kinase McsB [Posttranslational modification, protein turnover, chaperones];
118-366 7.54e-39

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


Pssm-ID: 443078  Cd Length: 353  Bit Score: 141.85  E-value: 7.54e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461784 118 GDDLDPNYVLSSRVRTGRSIRGFCLPPHCSRGERRAIEKLAVEALSSLDGDLSGR--YYALKSMTEAEQQQLIDDHFlfd 195
Cdd:COG3869   16 GSGPESDIVLSSRIRLARNLAGFPFPHRASEEEAEQVLSLVREALLSLSFQELGKfeLIKLEDLSPLERQVLVEKHL--- 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461784 196 kpVSPLLLASgmardwPDARGIWHNDNKTFLVWINEEDHLRVISMQKGGNMKEVFTRfctgLTQIETLFKSK-NYEFmwN 274
Cdd:COG3869   93 --ISPELAEN------PGGRAVLLSEDESVSIMVNEEDHLRIQCLLPGLQLEEAWEL----ANKIDDALEEKlDYAF--D 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461784 275 PHLGYILTCPSNLGTGLRAGVHIKLPHLGKHEKFSEVL---KRLRLQKRGTGGVDTAAVGGVFDVSNADRLGFSEVELVQ 351
Cdd:COG3869  159 EKFGYLTSCPTNVGTGLRASVMLHLPALVLTGQINRVLqalNQLGLTVRGLYGEGSEALGNIFQISNQITLGKSEEEIIE 238
                        250
                 ....*....|....*
gi 401461784 352 MVVDGVKLLIEMEQR 366
Cdd:COG3869  239 NLESVVRQIIEQERN 253
bacterial_phosphagen_kinase cd07930
Phosphagen (guanidino) kinases found in bacteria; Phosphagen (guanidino) kinases are enzymes ...
126-366 1.56e-38

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: 137.64  E-value: 1.56e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461784 126 VLSSRVRTGRSIRGFCLPPHCSRGERRAIEKLAVEALSSLDGDLSGRYYALKSMTEAEQQQLIDDHFLfdkpvSPLLLAS 205
Cdd:cd07930    4 VISSRIRLARNLKGYPFPNKLSEEQAADVLEKVEKALSNIEDKDEFELLKLKDLDPLERQVLVEKHLI-----SPELAEN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461784 206 gmardwPDARGIWHNDNKTFLVWINEEDHLRVISMQKGGNMKEVFTRfctgLTQIETLFKSK-NYEFmwNPHLGYILTCP 284
Cdd:cd07930   79 ------KEGGAVIVNEDETVSIMINEEDHLRIQCLLPGLQLEEAYER----ADKIDDLLEEKlDYAF--DEKLGYLTACP 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461784 285 SNLGTGLRAGVHIKLPHL---GKHEKFSEVLKRLRLQKRGTGGVDTAAVGGVFDVSNADRLGFSEVELVQMVVDGVKLLI 361
Cdd:cd07930  147 TNVGTGLRASVMLHLPALvltGQINRILNALSQLGLAVRGLYGEGSEALGNIYQISNQVTLGLSEEEIIENLESVVRQII 226

                 ....*
gi 401461784 362 EMEQR 366
Cdd:cd07930  227 EQERE 231
ATP-gua_PtransN pfam02807
ATP:guanido phosphotransferase, N-terminal domain; The N-terminal domain has an all-alpha fold.
24-94 4.48e-38

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: 131.09  E-value: 4.48e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 401461784   24 SSHNNHMAKVLTPELYAELRAKCTPSGFTLDDAIQTGVDNPGHPyimtVGAVAGDEESYDVFKDLFDPIIE 94
Cdd:pfam02807   1 SNHNSLLKKYLTPEVYDKLKDKKTPSGFTLDDCIQSGVDNPDSG----VGVYAGDEESYEVFADLFDPIIE 67
PRK01059 PRK01059
ATP:guanido phosphotransferase; Provisional
118-364 1.30e-33

ATP:guanido phosphotransferase; Provisional


Pssm-ID: 234894 [Multi-domain]  Cd Length: 346  Bit Score: 127.63  E-value: 1.30e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461784 118 GDDLDPNYVLSSRVRTGRSIRGFCLPPHCSRGERRAIEKLAVEALSSLDGDLSGR--YYALKSMTEAEQQQLIDdHFLFd 195
Cdd:PRK01059  14 GDGPDSDIVLSSRIRLARNLKDIPFPNKLSEEEARDIIELVEKAFLNNEIEGFGEfeLLKLKDLDPLEKEVLVE-KHLI- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461784 196 kpvSPLLLASgmardwPDARGIWHNDNKTFLVWINEEDHLRVISMQKGGNMKEVFTRfctgLTQIETLFKSK-NYEFmwN 274
Cdd:PRK01059  92 ---SPDLAEN------PEGGAVLLNEDETISIMINEEDHLRIQCIDPGLQLEEALEK----ANQIDDLLEEKlDYAF--D 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401461784 275 PHLGYILTCPSNLGTGLRAGVHIKLPHL---GKHEKFSEVLKRLRLQKRGTGGVDTAAVGGVFDVSNADRLGFSEVELVQ 351
Cdd:PRK01059 157 EKLGYLTSCPTNVGTGLRASVMLHLPALvltKRINRILQAINQLGLTVRGIYGEGSEALGNIYQISNQITLGKSEEEIIS 236
                        250
                 ....*....|...
gi 401461784 352 MVVDGVKLLIEME 364
Cdd:PRK01059 237 NLRSVVNQIISQE 249
 
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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