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Conserved domains on  [gi|2462507847|ref|XP_054191937|]
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adenylate kinase isoenzyme 5 isoform X3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ADK cd01428
Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine ...
 134-307 6.07e-55

Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine triphosphates (ATP) to adenosine monophosphates (AMP) and to yield adenosine diphosphates (ADP). This enzyme is required for the biosynthesis of ADP and is essential for homeostasis of adenosine phosphates.


:

Pssm-ID: 238713 [Multi-domain]  Cd Length: 194  Bit Score: 179.35  E-value: 6.07e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 134 IILVIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIHSTSSNrkWSLIAKIITTGELAPQETTITEIKQKLMQIPDEE 213
Cdd:cd01428     1 RILLLGPPGSGKGTQAERLAKKYGLPHISTGDLLREEIASGTEL--GKKAKEYIDSGKLVPDEIVIKLLKERLKKPDCKK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 214 GIVIDGFPRDVAQALSFEDQIC---TPDLVVFLACANQRLKERLLKR-------------------AEQQGRPDDNVKAT 271
Cdd:cd01428    79 GFILDGFPRTVDQAEALDELLDegiKPDKVIELDVPDEVLIERILGRricpvsgrvyhlgkddvtgEPLSQRSDDNEETI 158

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2462507847 272 QRRLMNFKQNAAPLVKYFQEKGLIMTFDADRDEDEV 307
Cdd:cd01428   159 KKRLEVYKEQTAPLIDYYKKKGKLVEIDGSGDIDEV 194
DD_AK5 cd22978
dimerization/docking (D/D) domain found in adenylate kinase isoenzyme 5 (AK5) and similar ...
 3-46 7.07e-21

dimerization/docking (D/D) domain found in adenylate kinase isoenzyme 5 (AK5) and similar proteins; AK5 (EC 2.7.4.3/EC 2.7.4.6), also called ATP-AMP transphosphorylase 5, acts as a nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. It is active on AMP and dAMP with ATP as a donor. When GTP is used as phosphate donor, the enzyme phosphorylates AMP, CMP, and to a small extent dCMP. It also displays broad nucleoside diphosphate kinase activity. AK5 contains an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.


:

Pssm-ID: 438547  Cd Length: 44  Bit Score: 84.89  E-value: 7.07e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2462507847   3 TNDAKEYLARREIPQLFESLLNGLMCSKPEDPVEYLESCLQKVK 46
Cdd:cd22978     1 SEDAKDYLSRKEIPQLFESLMTGLMYNRPDDPIEFLEDCLEKIR 44
 
Name Accession Description Interval E-value
ADK cd01428
Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine ...
 134-307 6.07e-55

Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine triphosphates (ATP) to adenosine monophosphates (AMP) and to yield adenosine diphosphates (ADP). This enzyme is required for the biosynthesis of ADP and is essential for homeostasis of adenosine phosphates.


Pssm-ID: 238713 [Multi-domain]  Cd Length: 194  Bit Score: 179.35  E-value: 6.07e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 134 IILVIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIHSTSSNrkWSLIAKIITTGELAPQETTITEIKQKLMQIPDEE 213
Cdd:cd01428     1 RILLLGPPGSGKGTQAERLAKKYGLPHISTGDLLREEIASGTEL--GKKAKEYIDSGKLVPDEIVIKLLKERLKKPDCKK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 214 GIVIDGFPRDVAQALSFEDQIC---TPDLVVFLACANQRLKERLLKR-------------------AEQQGRPDDNVKAT 271
Cdd:cd01428    79 GFILDGFPRTVDQAEALDELLDegiKPDKVIELDVPDEVLIERILGRricpvsgrvyhlgkddvtgEPLSQRSDDNEETI 158

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2462507847 272 QRRLMNFKQNAAPLVKYFQEKGLIMTFDADRDEDEV 307
Cdd:cd01428   159 KKRLEVYKEQTAPLIDYYKKKGKLVEIDGSGDIDEV 194
aden_kin_iso1 TIGR01360
adenylate kinase, isozyme 1 subfamily; Members of this family are adenylate kinase, EC 2.7.4.3. ...
 133-316 7.62e-52

adenylate kinase, isozyme 1 subfamily; Members of this family are adenylate kinase, EC 2.7.4.3. This clade is found only in eukaryotes and includes human adenylate kinase isozyme 1 (myokinase). Within the adenylate kinase superfamily, this set appears specifically closely related to a subfamily of eukaryotic UMP-CMP kinases (TIGR01359), rather than to the large clade of bacterial, archaeal, and eukaryotic adenylate kinase family members in TIGR01351.


Pssm-ID: 130427 [Multi-domain]  Cd Length: 188  Bit Score: 171.54  E-value: 7.62e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 133 KIILVIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIHSTSSNRKwsLIAKIITTGELAPQETTITEIKQKLMQ-IPD 211
Cdd:TIGR01360   4 KIIFIVGGPGSGKGTQCEKIVEKYGFTHLSTGDLLRAEVASGSERGK--QLQAIMESGDLVPLDTVLDLLKDAMVAaLGT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 212 EEGIVIDGFPRDVAQALSFEDQICTPDLVVFLACANQRLKERLLKRAEQQGRPDDNVKATQRRLMNFKQNAAPLVKYFQE 291
Cdd:TIGR01360  82 SKGFLIDGYPREVKQGEEFERRIGPPTLVLYFDCSEDTMVKRLLKRAETSGRVDDNEKTIKKRLETYYKATEPVIAYYET 161

                         170       180
                  ....*....|....*....|....*
gi 2462507847 292 KGLIMTFDADRDEDEVFYDISMAVD 316
Cdd:TIGR01360 162 KGKLRKINAEGTVDDVFLQVCTAID 186
PLN02200 PLN02200
adenylate kinase family protein
 113-308 1.18e-39

adenylate kinase family protein


Pssm-ID: 215125 [Multi-domain]  Cd Length: 234  Bit Score: 141.18  E-value: 1.18e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 113 SETAELIEEYEVFDPTRPR-PKIILVIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIHSTSSNrkWSLIAKIITTGE 191
Cdd:PLN02200   23 SFSTEIITLEERGSSSKEKtPFITFVLGGPGSGKGTQCEKIVETFGFKHLSAGDLLRREIASNSEH--GAMILNTIKEGK 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 192 LAPQETTITEIKQKlMQIPDEEGIVIDGFPRDVAQALSFEDQI-CTPDLVVFLACANQRLKERLLKRaeQQGRPDDNVKA 270
Cdd:PLN02200  101 IVPSEVTVKLIQKE-MESSDNNKFLIDGFPRTEENRIAFERIIgAEPNVVLFFDCPEEEMVKRVLNR--NQGRVDDNIDT 177

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2462507847 271 TQRRLMNFKQNAAPLVKYFQEKGLIMTFDADRDEDEVF 308
Cdd:PLN02200  178 IKKRLKVFNALNLPVIDYYSKKGKLYTINAVGTVDEIF 215
Adk COG0563
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ...
 133-311 5.68e-39

Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or related kinase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440329 [Multi-domain]  Cd Length: 212  Bit Score: 138.34  E-value: 5.68e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 133 KIILvIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIhstSSNRKWSLIAK-IITTGELAPQETTITEIKQKLMQIPD 211
Cdd:COG0563     2 RIIL-LGPPGAGKGTQAKRLAEKYGIPHISTGDMLRAAV---KAGTELGKKAKeYMDAGELVPDEIVIGLVKERLAQPDC 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 212 EEGIVIDGFPRDVAQALSFEDQIC----TPDLVVFLACANQRLKERLLKRA---------------------------EQ 260
Cdd:COG0563    78 ANGFILDGFPRTVAQAEALDELLAelgiKLDAVIELDVDDEELVERLSGRRvcpncgatyhvkfnppkvegvcdkcggEL 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462507847 261 QGRPDDNVKATQRRLMNFKQNAAPLVKYFQEKGLIMTFDADRDEDEVFYDI 311
Cdd:COG0563   158 VQRADDNEETVRKRLEVYHEQTAPLIDYYRKKGKLVEIDGEGSIEEVTADI 208
ADK pfam00406
Adenylate kinase;
137-292 7.69e-37

Adenylate kinase;


Pssm-ID: 395329 [Multi-domain]  Cd Length: 184  Bit Score: 132.05  E-value: 7.69e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 137 VIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIHSTSSNRKwsLIAKIITTGELAPQETTITEIKQKLMQIPDEEGIV 216
Cdd:pfam00406   1 LLGPPGAGKGTQAEKIVQKYGLPHLSTGDLLRAEIKSGTELGK--EAKEYMDKGELVPDEVVVGLVKERLEQNDCKNGFL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 217 IDGFPRDVAQALSFED---QICTPDLVVFLACANQRLKERLLKRAEQQ---------------------------GRPDD 266
Cdd:pfam00406  79 LDGFPRTVPQAEALEElleRGIKLDYVIEFDVPDEVLVERLTGRRIHPnsgrsyhlefnppkvpgkddvtgeplvQRSDD 158

                         170       180
                  ....*....|....*....|....*.
gi 2462507847 267 NVKATQRRLMNFKQNAAPLVKYFQEK 292
Cdd:pfam00406 159 NEETVKKRLETYHKQTKPLIDYYKKK 184
DD_AK5 cd22978
dimerization/docking (D/D) domain found in adenylate kinase isoenzyme 5 (AK5) and similar ...
 3-46 7.07e-21

dimerization/docking (D/D) domain found in adenylate kinase isoenzyme 5 (AK5) and similar proteins; AK5 (EC 2.7.4.3/EC 2.7.4.6), also called ATP-AMP transphosphorylase 5, acts as a nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. It is active on AMP and dAMP with ATP as a donor. When GTP is used as phosphate donor, the enzyme phosphorylates AMP, CMP, and to a small extent dCMP. It also displays broad nucleoside diphosphate kinase activity. AK5 contains an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.


Pssm-ID: 438547  Cd Length: 44  Bit Score: 84.89  E-value: 7.07e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2462507847   3 TNDAKEYLARREIPQLFESLLNGLMCSKPEDPVEYLESCLQKVK 46
Cdd:cd22978     1 SEDAKDYLSRKEIPQLFESLMTGLMYNRPDDPIEFLEDCLEKIR 44
BREX_3_BrxF NF033453
BREX-3 system P-loop-containing protein BrxF; This family of proteins that are about 150 amino ...
 133-187 3.14e-03

BREX-3 system P-loop-containing protein BrxF; This family of proteins that are about 150 amino acids in length includes BrxF from type 3 BREX (bacteriophage exclusion) systems. Most members have the P-loop motif GxxGxGKT, but the region is surprisingly poorly conserved in a sizable fraction of otherwise strongly similar proteins.


Pssm-ID: 468038  Cd Length: 149  Bit Score: 37.86  E-value: 3.14e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462507847 133 KIILVIGGPGSGKgTQSLK-IAERYGFQYISVGELLRKKIHSTSSNRKWSLIAKII 187
Cdd:NF033453   17 KLILLVGPPGSGK-TALLReLAAKRGAPVINVNLELSRRLLELPEKQRALRAPRLL 71
 
Name Accession Description Interval E-value
ADK cd01428
Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine ...
 134-307 6.07e-55

Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine triphosphates (ATP) to adenosine monophosphates (AMP) and to yield adenosine diphosphates (ADP). This enzyme is required for the biosynthesis of ADP and is essential for homeostasis of adenosine phosphates.


Pssm-ID: 238713 [Multi-domain]  Cd Length: 194  Bit Score: 179.35  E-value: 6.07e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 134 IILVIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIHSTSSNrkWSLIAKIITTGELAPQETTITEIKQKLMQIPDEE 213
Cdd:cd01428     1 RILLLGPPGSGKGTQAERLAKKYGLPHISTGDLLREEIASGTEL--GKKAKEYIDSGKLVPDEIVIKLLKERLKKPDCKK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 214 GIVIDGFPRDVAQALSFEDQIC---TPDLVVFLACANQRLKERLLKR-------------------AEQQGRPDDNVKAT 271
Cdd:cd01428    79 GFILDGFPRTVDQAEALDELLDegiKPDKVIELDVPDEVLIERILGRricpvsgrvyhlgkddvtgEPLSQRSDDNEETI 158

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2462507847 272 QRRLMNFKQNAAPLVKYFQEKGLIMTFDADRDEDEV 307
Cdd:cd01428   159 KKRLEVYKEQTAPLIDYYKKKGKLVEIDGSGDIDEV 194
aden_kin_iso1 TIGR01360
adenylate kinase, isozyme 1 subfamily; Members of this family are adenylate kinase, EC 2.7.4.3. ...
 133-316 7.62e-52

adenylate kinase, isozyme 1 subfamily; Members of this family are adenylate kinase, EC 2.7.4.3. This clade is found only in eukaryotes and includes human adenylate kinase isozyme 1 (myokinase). Within the adenylate kinase superfamily, this set appears specifically closely related to a subfamily of eukaryotic UMP-CMP kinases (TIGR01359), rather than to the large clade of bacterial, archaeal, and eukaryotic adenylate kinase family members in TIGR01351.


Pssm-ID: 130427 [Multi-domain]  Cd Length: 188  Bit Score: 171.54  E-value: 7.62e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 133 KIILVIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIHSTSSNRKwsLIAKIITTGELAPQETTITEIKQKLMQ-IPD 211
Cdd:TIGR01360   4 KIIFIVGGPGSGKGTQCEKIVEKYGFTHLSTGDLLRAEVASGSERGK--QLQAIMESGDLVPLDTVLDLLKDAMVAaLGT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 212 EEGIVIDGFPRDVAQALSFEDQICTPDLVVFLACANQRLKERLLKRAEQQGRPDDNVKATQRRLMNFKQNAAPLVKYFQE 291
Cdd:TIGR01360  82 SKGFLIDGYPREVKQGEEFERRIGPPTLVLYFDCSEDTMVKRLLKRAETSGRVDDNEKTIKKRLETYYKATEPVIAYYET 161

                         170       180
                  ....*....|....*....|....*
gi 2462507847 292 KGLIMTFDADRDEDEVFYDISMAVD 316
Cdd:TIGR01360 162 KGKLRKINAEGTVDDVFLQVCTAID 186
UMP_CMP_kin_fam TIGR01359
UMP-CMP kinase family; This subfamily of the adenylate kinase superfamily contains examples of ...
 134-311 1.14e-39

UMP-CMP kinase family; This subfamily of the adenylate kinase superfamily contains examples of UMP-CMP kinase, as well as others proteins with unknown specificity, some currently designated adenylate kinase. All known members are eukaryotic.


Pssm-ID: 273576 [Multi-domain]  Cd Length: 185  Bit Score: 139.43  E-value: 1.14e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 134 IILVIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIHSTSSNRKwSLIAKIITTGELAPQETTITEIKQKLMQIPDEE 213
Cdd:TIGR01359   1 VVFVLGGPGSGKGTQCAKIVENFGFTHLSAGDLLRAEIKREGSENG-SLIESYIKEGKIVPSEVTVELLKKAIQEDGSSK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 214 GIVIDGFPRDVAQALSFEDQICT---PDLVVFLACANQRLKERLLKRAEQQGRPDDNVKATQRRLMNFKQNAAPLVKYFQ 290
Cdd:TIGR01359  80 KFLIDGFPRNEENLEAWEKLMDNkvnFKFVLFFDCPEETMIKRLLKRGQTSGRVDDNIETLKKRFRTYNEETLPIIEHFE 159

                         170       180
                  ....*....|....*....|.
gi 2462507847 291 EKGLIMTFDADRDEDEVFYDI 311
Cdd:TIGR01359 160 NKGKVKEINAEGSVEEVFEDV 180
PLN02200 PLN02200
adenylate kinase family protein
 113-308 1.18e-39

adenylate kinase family protein


Pssm-ID: 215125 [Multi-domain]  Cd Length: 234  Bit Score: 141.18  E-value: 1.18e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 113 SETAELIEEYEVFDPTRPR-PKIILVIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIHSTSSNrkWSLIAKIITTGE 191
Cdd:PLN02200   23 SFSTEIITLEERGSSSKEKtPFITFVLGGPGSGKGTQCEKIVETFGFKHLSAGDLLRREIASNSEH--GAMILNTIKEGK 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 192 LAPQETTITEIKQKlMQIPDEEGIVIDGFPRDVAQALSFEDQI-CTPDLVVFLACANQRLKERLLKRaeQQGRPDDNVKA 270
Cdd:PLN02200  101 IVPSEVTVKLIQKE-MESSDNNKFLIDGFPRTEENRIAFERIIgAEPNVVLFFDCPEEEMVKRVLNR--NQGRVDDNIDT 177

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2462507847 271 TQRRLMNFKQNAAPLVKYFQEKGLIMTFDADRDEDEVF 308
Cdd:PLN02200  178 IKKRLKVFNALNLPVIDYYSKKGKLYTINAVGTVDEIF 215
Adk COG0563
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ...
 133-311 5.68e-39

Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or related kinase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440329 [Multi-domain]  Cd Length: 212  Bit Score: 138.34  E-value: 5.68e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 133 KIILvIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIhstSSNRKWSLIAK-IITTGELAPQETTITEIKQKLMQIPD 211
Cdd:COG0563     2 RIIL-LGPPGAGKGTQAKRLAEKYGIPHISTGDMLRAAV---KAGTELGKKAKeYMDAGELVPDEIVIGLVKERLAQPDC 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 212 EEGIVIDGFPRDVAQALSFEDQIC----TPDLVVFLACANQRLKERLLKRA---------------------------EQ 260
Cdd:COG0563    78 ANGFILDGFPRTVAQAEALDELLAelgiKLDAVIELDVDDEELVERLSGRRvcpncgatyhvkfnppkvegvcdkcggEL 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462507847 261 QGRPDDNVKATQRRLMNFKQNAAPLVKYFQEKGLIMTFDADRDEDEVFYDI 311
Cdd:COG0563   158 VQRADDNEETVRKRLEVYHEQTAPLIDYYRKKGKLVEIDGEGSIEEVTADI 208
adk TIGR01351
adenylate kinase; Adenylate kinase (EC 2.7.4.3) converts ATP + AMP to ADP + ADP, that is, uses ...
 135-316 1.70e-37

adenylate kinase; Adenylate kinase (EC 2.7.4.3) converts ATP + AMP to ADP + ADP, that is, uses ATP as a phosphate donor for AMP. Most members of this family are known or believed to be adenylate kinase. However, some members accept other nucleotide triphosphates as donors, may be unable to use ATP, and may fail to complement adenylate kinase mutants. An example of a nucleoside-triphosphate--adenylate kinase (EC 2.7.4.10) is SP|Q9UIJ7, a GTP:AMP phosphotransferase. This family is designated subfamily rather than equivalog for this reason. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]


Pssm-ID: 273569 [Multi-domain]  Cd Length: 210  Bit Score: 134.67  E-value: 1.70e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 135 ILVIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIHSTSSNRKwsLIAKIITTGELAPQETTITEIKQKLMQIPDEE- 213
Cdd:TIGR01351   2 LVLLGPPGSGKGTQAKRIAEKYGLPHISTGDLLRAEIKAGTPLGK--KAKEYMEKGELVPDEIVNQLVKERLTQNDDNEn 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 214 GIVIDGFPRDVAQALSFEDQIC-TPDLVVFLACANQRLKERLLKR---------------------------AEQQGRPD 265
Cdd:TIGR01351  80 GFILDGFPRTLSQAEALDALLEePIDAVIELDVPDEELVERLSGRricpscgrvyhlkfnppkvpgcddctgELLVQRED 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462507847 266 DNVKATQRRLMNFKQNAAPLVKYFQEKGLIMTFDADRDEDEVFYDISMAVD 316
Cdd:TIGR01351 160 DTEEVVKKRLEVYKEQTEPLIDYYKKRGILVQIDGNGPIDEVWKRILEALK 210
ADK pfam00406
Adenylate kinase;
137-292 7.69e-37

Adenylate kinase;


Pssm-ID: 395329 [Multi-domain]  Cd Length: 184  Bit Score: 132.05  E-value: 7.69e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 137 VIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIHSTSSNRKwsLIAKIITTGELAPQETTITEIKQKLMQIPDEEGIV 216
Cdd:pfam00406   1 LLGPPGAGKGTQAEKIVQKYGLPHLSTGDLLRAEIKSGTELGK--EAKEYMDKGELVPDEVVVGLVKERLEQNDCKNGFL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 217 IDGFPRDVAQALSFED---QICTPDLVVFLACANQRLKERLLKRAEQQ---------------------------GRPDD 266
Cdd:pfam00406  79 LDGFPRTVPQAEALEElleRGIKLDYVIEFDVPDEVLVERLTGRRIHPnsgrsyhlefnppkvpgkddvtgeplvQRSDD 158

                         170       180
                  ....*....|....*....|....*.
gi 2462507847 267 NVKATQRRLMNFKQNAAPLVKYFQEK 292
Cdd:pfam00406 159 NEETVKKRLETYHKQTKPLIDYYKKK 184
adk PRK00279
adenylate kinase; Reviewed
 133-318 4.68e-36

adenylate kinase; Reviewed


Pssm-ID: 234711 [Multi-domain]  Cd Length: 215  Bit Score: 131.04  E-value: 4.68e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 133 KIILvIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIHSTSSNRKwsLIAKIITTGELAPQETTITEIKQKLMQIPDE 212
Cdd:PRK00279    2 RLIL-LGPPGAGKGTQAKFIAEKYGIPHISTGDMLRAAVKAGTELGK--EAKSYMDAGELVPDEIVIGLVKERLAQPDCK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 213 EGIVIDGFPRDVAQALSFEDQIC----TPDLVVFLACANQRLKERLLKRA---------------------------EQQ 261
Cdd:PRK00279   79 NGFLLDGFPRTIPQAEALDEMLKelgiKLDAVIEIDVPDEELVERLSGRRicpacgrtyhvkfnppkvegkcdvcgeELI 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462507847 262 GRPDDNVKATQRRLMNFKQNAAPLVKYFQEKGLIMTFDADRDEDEVFYDISMAVDNK 318
Cdd:PRK00279  159 QRADDNEETVRKRLEVYHKQTAPLIDYYKKKGKLKKIDGTGSIDEVFADILKALGKL 215
PRK14532 PRK14532
adenylate kinase; Provisional
 135-315 6.80e-32

adenylate kinase; Provisional


Pssm-ID: 184729 [Multi-domain]  Cd Length: 188  Bit Score: 119.16  E-value: 6.80e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 135 ILVIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIHSTSS-NRKwslIAKIITTGELAPQETTITEIKQKLMQIPDEE 213
Cdd:PRK14532    3 LILFGPPAAGKGTQAKRLVEERGMVQLSTGDMLRAAIASGSElGQR---VKGIMDRGELVSDEIVIALIEERLPEAEAAG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 214 GIVIDGFPRDVAQA-------LSFEDQIctpDLVVFLACANQRLKERLLKRAEQQGRPDDNVKATQRRLMNFKQNAAPLV 286
Cdd:PRK14532   80 GAIFDGFPRTVAQAealdkmlASRGQKI---DVVIRLKVDDEALIERIVKRFEEQGRPDDNPEVFVTRLDAYNAQTAPLL 156

                         170       180
                  ....*....|....*....|....*....
gi 2462507847 287 KYFQEKGLIMTFDADRDEDEVFYDISMAV 315
Cdd:PRK14532  157 PYYAGQGKLTEVDGMGSIEAVAASIDAAL 185
PRK14527 PRK14527
adenylate kinase; Provisional
 128-315 1.37e-29

adenylate kinase; Provisional


Pssm-ID: 237745 [Multi-domain]  Cd Length: 191  Bit Score: 112.96  E-value: 1.37e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 128 TRPRPKIILVIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIhstSSNRKWSLIAK-IITTGELAPQETTITEIKQKL 206
Cdd:PRK14527    2 TQTKNKVVIFLGPPGAGKGTQAERLAQELGLKKLSTGDILRDHV---ARGTELGQRAKpIMEAGDLVPDELILALIRDEL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 207 MQIPDEEgIVIDGFPRDVAQA----LSFEDQICTPDLVVFLACANQRLKERLLKRAEQQGRPDDNVKATQRRLMNFKQNA 282
Cdd:PRK14527   79 AGMEPVR-VIFDGFPRTLAQAealdRLLEELGARLLAVVLLEVPDEELIRRIVERARQEGRSDDNEETVRRRQQVYREQT 157

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2462507847 283 APLVKYFQEKGLIMTFDADRDEDEVFYDISMAV 315
Cdd:PRK14527  158 QPLVDYYEARGHLKRVDGLGTPDEVYARILKAL 190
adk PRK02496
adenylate kinase; Provisional
 135-307 4.25e-28

adenylate kinase; Provisional


Pssm-ID: 179433 [Multi-domain]  Cd Length: 184  Bit Score: 108.68  E-value: 4.25e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 135 ILVIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIhstSSNRKWSLIAKI-ITTGELAPQETTITEIKQKLMQIPDEE 213
Cdd:PRK02496    4 LIFLGPPGAGKGTQAVVLAEHLHIPHISTGDILRQAI---KEQTPLGIKAQGyMDKGELVPDQLVLDLVQERLQQPDAAN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 214 GIVIDGFPRDVAQAlSFEDQICTP-----DLVVFLACANQRLKERLLKRaeqqGRPDDNVKATQRRLMNFKQNAAPLVKY 288
Cdd:PRK02496   81 GWILDGFPRKVTQA-AFLDELLQEigqsgERVVNLDVPDDVVVERLLAR----GRKDDTEEVIRRRLEVYREQTAPLIDY 155

                         170
                  ....*....|....*....
gi 2462507847 289 FQEKGLIMTFDADRDEDEV 307
Cdd:PRK02496  156 YRDRQKLLTIDGNQSVEAV 174
AAA_17 pfam13207
AAA domain;
139-268 3.46e-27

AAA domain;


Pssm-ID: 463810 [Multi-domain]  Cd Length: 136  Bit Score: 104.63  E-value: 3.46e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 139 GGPGSGKGTQSLKIAERYGFQYISVGELLRKKIhstsSNRKWSLIAKIITTGELAPQETTITEIKQKLMQIPDEEGIVID 218
Cdd:pfam13207   2 GVPGSGKTTQLKKLAEKLGFPHISAGDLLREEA----KERGLVEDRDEMRKLPLEPQKELQKLAAERIAEEAGEGGVIVD 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462507847 219 GFPRDVAQALSFED------QICTPDLVVFLACANQRLKERLLKRAEqQGRPDDNV 268
Cdd:pfam13207  78 GHPRIKTPAGYLPGlpvevlRELKPDAIILLEADPEEILERRLKDRT-RGRDDDSE 132
PRK14530 PRK14530
adenylate kinase; Provisional
 135-319 1.75e-25

adenylate kinase; Provisional


Pssm-ID: 237747 [Multi-domain]  Cd Length: 215  Bit Score: 102.56  E-value: 1.75e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 135 ILVIGGPGSGKGTQSLKIAERYGFQYISVGELLR--KKIHSTSSNRKWSLIAKIITTGELAPQEtTITEIKQKlmQIPDE 212
Cdd:PRK14530    6 ILLLGAPGAGKGTQSSNLAEEFGVEHVTTGDALRanKQMDISDMDTEYDTPGEYMDAGELVPDA-VVNEIVEE--ALSDA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 213 EGIVIDGFPRDVAQALSFEDqICTPDLVVFLACANQRLKERLLKR----------------AEQQG-----------RPD 265
Cdd:PRK14530   83 DGFVLDGYPRNLEQAEYLES-ITDLDVVLYLDVSEEELVDRLTGRrvcpdcganyhvefnqPEEEGvcdecggeliqRDD 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462507847 266 DNVKATQRRLMNFKQNAAPLVKYFQEKGLIMTFDADRDEDEVFYDISMAVDNKL 319
Cdd:PRK14530  162 DTEETVRERLDVFEENTEPVIEHYRDQGVLVEVDGEQTPDEVWADIQDAIDDAT 215
PRK14531 PRK14531
adenylate kinase; Provisional
 135-300 8.45e-25

adenylate kinase; Provisional


Pssm-ID: 172997 [Multi-domain]  Cd Length: 183  Bit Score: 99.89  E-value: 8.45e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 135 ILVIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIHSTSSNRKWSliAKIITTGELAPQETTITEIKQKlMQIPDEEG 214
Cdd:PRK14531    5 LLFLGPPGAGKGTQAARLCAAHGLRHLSTGDLLRSEVAAGSALGQEA--EAVMNRGELVSDALVLAIVESQ-LKALNSGG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 215 IVIDGFPRDVAQALSFE---DQICTP-DLVVFLACANQRLKERLLKRaeqqGRPDDNVKATQRRLMNFKQNAAPLVKYFQ 290
Cdd:PRK14531   82 WLLDGFPRTVAQAEALEpllEELKQPiEAVVLLELDDAVLIERLLAR----GRADDNEAVIRNRLEVYREKTAPLIDHYR 157

                         170
                  ....*....|
gi 2462507847 291 EKGLIMTFDA 300
Cdd:PRK14531  158 QRGLLQSVEA 167
PRK13808 PRK13808
adenylate kinase; Provisional
 133-311 1.01e-23

adenylate kinase; Provisional


Pssm-ID: 172341 [Multi-domain]  Cd Length: 333  Bit Score: 100.35  E-value: 1.01e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 133 KIILvIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIhstSSNRKWSLIAK-IITTGELAPQETTITEIKQKLMQIPD 211
Cdd:PRK13808    2 RLIL-LGPPGAGKGTQAQRLVQQYGIVQLSTGDMLRAAV---AAGTPVGLKAKdIMASGGLVPDEVVVGIISDRIEQPDA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 212 EEGIVIDGFPRDVAQALSFE----DQICTPDLVVFLACANQRLKERLLKR-AEQQG-----RPDDNVKATQRRLMNFKQN 281
Cdd:PRK13808   78 ANGFILDGFPRTVPQAEALDallkDKQLKLDAVVELRVNEGALLARVETRvAEMRArgeevRADDTPEVLAKRLASYRAQ 157

                         170       180       190
                  ....*....|....*....|....*....|
gi 2462507847 282 AAPLVKYFQEKGLIMTFDADRDEDEVFYDI 311
Cdd:PRK13808  158 TEPLVHYYSEKRKLLTVDGMMTIDEVTREI 187
PRK14528 PRK14528
adenylate kinase; Provisional
 133-295 1.05e-22

adenylate kinase; Provisional


Pssm-ID: 172994 [Multi-domain]  Cd Length: 186  Bit Score: 94.31  E-value: 1.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 133 KIILVIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIHSTSSNRKWSliAKIITTGELAPQETTITEIKQKLMQIPDE 212
Cdd:PRK14528    2 KNIIFMGPPGAGKGTQAKILCERLSIPQISTGDILREAVKNQTAMGIEA--KRYMDAGDLVPDSVVIGIIKDRIREADCK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 213 EGIVIDGFPRDVAQALSFEDQI----CTPDLVVFLACANQRLKERLLKRAEQQGRPDDNVKATQRRLMNFKQNAAPLVKY 288
Cdd:PRK14528   80 NGFLLDGFPRTVEQADALDALLknegKSIDKAINLEVPDGELLKRLLGRAEIEGRADDNEATIKNRLDNYNKKTLPLLDF 159


                  ....*..
gi 2462507847 289 FQEKGLI 295
Cdd:PRK14528  160 YAAQKKL 166
DD_AK5 cd22978
dimerization/docking (D/D) domain found in adenylate kinase isoenzyme 5 (AK5) and similar ...
 3-46 7.07e-21

dimerization/docking (D/D) domain found in adenylate kinase isoenzyme 5 (AK5) and similar proteins; AK5 (EC 2.7.4.3/EC 2.7.4.6), also called ATP-AMP transphosphorylase 5, acts as a nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. It is active on AMP and dAMP with ATP as a donor. When GTP is used as phosphate donor, the enzyme phosphorylates AMP, CMP, and to a small extent dCMP. It also displays broad nucleoside diphosphate kinase activity. AK5 contains an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.


Pssm-ID: 438547  Cd Length: 44  Bit Score: 84.89  E-value: 7.07e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2462507847   3 TNDAKEYLARREIPQLFESLLNGLMCSKPEDPVEYLESCLQKVK 46
Cdd:cd22978     1 SEDAKDYLSRKEIPQLFESLMTGLMYNRPDDPIEFLEDCLEKIR 44
PLN02842 PLN02842
nucleotide kinase
 136-312 8.81e-21

nucleotide kinase


Pssm-ID: 178435 [Multi-domain]  Cd Length: 505  Bit Score: 93.77  E-value: 8.81e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 136 LVIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIHSTSSNRKWSliAKIITTGELAPQETTITEIKQKLmQIPD--EE 213
Cdd:PLN02842    1 MISGAPASGKGTQCELIVHKFGLVHISTGDLLRAEVSAGTDIGKRA--KEFMNSGRLVPDEIVIAMVTGRL-SREDakEK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 214 GIVIDGFPRDVAQALSFEDQICTPDLVVFLACANQRLKERLLKR-----------------------AEQQGRPDDNVKA 270
Cdd:PLN02842   78 GWLLDGYPRSFAQAQSLEKLKIRPDIFILLDVPDEILIDRCVGRrldpvtgkiyhiknfppeseeikARLITRPDDTEEK 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2462507847 271 TQRRLMNFKQNAAPLVKYFQEkgLIMTFDADRDEDEVFYDIS 312
Cdd:PLN02842  158 VKARLQIYKKNAEAILSTYSD--IMVKIDGNRPKEVVFEEIS 197
PTZ00088 PTZ00088
adenylate kinase 1; Provisional
 131-293 1.19e-14

adenylate kinase 1; Provisional


Pssm-ID: 240262 [Multi-domain]  Cd Length: 229  Bit Score: 72.52  E-value: 1.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 131 RPKIILVIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIHSTSSNRKwsLIAKIITTGELAPQETTITEIKQKLMQIP 210
Cdd:PTZ00088    5 GPLKIVLFGAPGVGKGTFAEILSKKENLKHINMGNILREEIKAKTTIGK--EIQKVVTSGNLVPDNLVIAIVKDEIAKVT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 211 DE--EGIVIDGFPRDVAQALSFEdQICTPDLVVFLACANQRLKERLLKR------------------------------- 257
Cdd:PTZ00088   83 DDcfKGFILDGFPRNLKQCKELG-KITNIDLFVNIYLPRNILIKKLLGRricntcnrnfniahirsdpydmppilppadc 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2462507847 258 ------AEQQGRPDDNVKATQRRLMNFKQNAAPLVKYFQEKG 293
Cdd:PTZ00088  162 egckgnPKLQKRSDDTEEIVAHRLNTYESTNSPIIQFFKNEN 203
PRK14526 PRK14526
adenylate kinase; Provisional
 135-307 6.00e-14

adenylate kinase; Provisional


Pssm-ID: 172992 [Multi-domain]  Cd Length: 211  Bit Score: 70.27  E-value: 6.00e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 135 ILVIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIHSTSSNRKWslIAKIITTGELAPQETTITEIKQKLMQIPDEEG 214
Cdd:PRK14526    3 LVFLGPPGSGKGTIAKILSNELNYYHISTGDLFRENILNSTPLGKE--IKQIVENGQLVPDSITIKIVEDKINTIKNNDN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 215 IVIDGFPRDVAQALSFEDQICTPDLVVFL---ACANQRLKERLLKRA------------EQQG-----------RPDDNV 268
Cdd:PRK14526   81 FILDGFPRNINQAKALDKFLPNIKIINFLideELLIKRLSGRRICKScnnifniytlptKEKGicdvckgdlyqRKDDKE 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2462507847 269 KATQRRLMNFKQNAAPLVKYFQEKGLIMTFDADRDEDEV 307
Cdd:PRK14526  161 ESLKTRLQEYKLQTKPLIEFYSKCNRLNNIDASKDIDEV 199
PLN02674 PLN02674
adenylate kinase
 128-315 7.13e-14

adenylate kinase


Pssm-ID: 178279 [Multi-domain]  Cd Length: 244  Bit Score: 70.68  E-value: 7.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 128 TRPRPKIILvIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIhstSSNRKWSLIAK-IITTGELAPQETTITEIKQKL 206
Cdd:PLN02674   28 SKPDKRLIL-IGPPGSGKGTQSPIIKDEYCLCHLATGDMLRAAV---AAKTPLGIKAKeAMDKGELVSDDLVVGIIDEAM 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 207 MQIPDEEGIVIDGFPRDVAQALSFED----QICTPDLVVFLACANQRLKERLLKR----------------------AEQ 260
Cdd:PLN02674  104 KKPSCQKGFILDGFPRTVVQAQKLDEmlakQGAKIDKVLNFAIDDAILEERITGRwihpssgrtyhtkfappkvpgvDDV 183

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 261 QGRP-----DDNVKATQRRLMNFKQNAAPLVKYFQEKGLIMTFDADRDEDEVFYDISMAV 315
Cdd:PLN02674  184 TGEPliqrkDDTAAVLKSRLEAFHKQTEPVIDYYAKKGVVANLHAEKPPKEVTAEVQKAL 243
PLN02459 PLN02459
probable adenylate kinase
 108-299 2.63e-13

probable adenylate kinase


Pssm-ID: 215253 [Multi-domain]  Cd Length: 261  Bit Score: 69.49  E-value: 2.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 108 SDTDLSETAELIEEYEVF-DPTRPRPKII--LVIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIHSTSSnrKWSLIA 184
Cdd:PLN02459    2 SERDAKSTSALADDLASAcDRSLAKGRNVnwVFLGCPGVGKGTYASRLSKLLGVPHIATGDLVREEIKSSGP--LGAQLK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 185 KIITTGELAPQETTITEIKQKLMQIPD--EEGIVIDGFPRDVAQALSFEDqICTPDLVVFLACANQRLKERLLKR----- 257
Cdd:PLN02459   80 EIVNQGKLVPDEIIFSLLSKRLEAGEEegESGFILDGFPRTVRQAEILEG-VTDIDLVVNLKLREEVLVEKCLGRricse 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462507847 258 ------------AEQQGRP---------------------DDNVKATQRRLMNFKQNAAPLVKYFQEKGLIMTFD 299
Cdd:PLN02459  159 cgknfnvadidlKGEDGRPgivmppllpppecasklitraDDTEEVVKARLRVYKEESQPVEDFYRKRGKLLEFE 233
DD_TEX55-like cd22961
dimerization/docking (D/D) domain found in the testis-specific expressed protein 55 (TEX55) ...
 5-44 4.50e-12

dimerization/docking (D/D) domain found in the testis-specific expressed protein 55 (TEX55)-like family; The TEX55-like family includes TEX55, F-box/LRR-repeat protein 13 (FBXL13), adenylate kinase isoenzymes AK5 and AK8, as well as uncharacterized EF-hand calcium-binding domain-containing protein 10 (EFCAB10), and protein VEST-1. TEX55, also called testis-specific conserved cAMP-dependent type II PK-anchoring protein (TSCPA), is a putative A-kinase anchoring protein (AKAP) that is dispensable for male fertility. FBXL13, also called F-box and leucine-rich repeat protein 13, or dynein regulatory complex subunit 6 (DRC6), is a component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. It may also function as a substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. AK5 and AK8 act as nucleoside monophosphate (NMP) kinases that catalyze the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. Members of this family contain a conserved helical bundle domain that shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.


Pssm-ID: 438530  Cd Length: 43  Bit Score: 60.12  E-value: 4.50e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2462507847   5 DAKEYLARREIPQLFESLLNGLMCSKPEDPVEYLESCLQK 44
Cdd:cd22961     3 DAEEYLEKHKIPELFESLLTALLIEKPEDPIEFLIDKLQQ 42
PRK14529 PRK14529
adenylate kinase; Provisional
 135-227 3.26e-10

adenylate kinase; Provisional


Pssm-ID: 237746 [Multi-domain]  Cd Length: 223  Bit Score: 59.73  E-value: 3.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 135 ILVIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIhstSSNRKWSLIAK-IITTGELAPQETTITEIKQKLmQIPDEE 213
Cdd:PRK14529    3 ILIFGPNGSGKGTQGALVKKKYDLAHIESGAIFREHI---GGGTELGKKAKeYIDRGDLVPDDITIPMILETL-KQDGKN 78

                          90
                  ....*....|....
gi 2462507847 214 GIVIDGFPRDVAQA 227
Cdd:PRK14529   79 GWLLDGFPRNKVQA 92
DD_FBXL13 cd22977
dimerization/docking (D/D) domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar ...
 7-45 2.47e-07

dimerization/docking (D/D) domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar proteins; FBXL13, also called F-box and leucine-rich repeat protein 13, or dynein regulatory complex subunit 6 (DRC6), is a component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. It may also function as a substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It contains an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.


Pssm-ID: 438546  Cd Length: 43  Bit Score: 46.78  E-value: 2.47e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2462507847   7 KEYLARREIPQLFESLLNGLMCSKPEDPVEYLESCLQKV 45
Cdd:cd22977     5 RKYLRKHKLPDVYEALLTGLAVMCPEDPLRFIEEKLKEL 43
DD_EFCAB10 cd22976
dimerization/docking (D/D) domain found in EF-hand calcium-binding domain-containing protein ...
 5-47 9.43e-07

dimerization/docking (D/D) domain found in EF-hand calcium-binding domain-containing protein 10 (EFCAB10) and similar proteins; The subfamily includes uncharacterized EF-hand calcium-binding domain-containing protein 10 (EFCAB10), which contains an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.


Pssm-ID: 438545  Cd Length: 47  Bit Score: 45.17  E-value: 9.43e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2462507847   5 DAKEYLARREIPQLFESLLNGLMCSKPEDPVEYLESCLQKVKE 47
Cdd:cd22976     3 EAEEYLEKHKIPELFENLTSLLLYHRPEDPKAFLIEQLEKLKE 45
DD_AK8 cd22979
dimerization/docking (D/D) domain found in adenylate kinase isoenzyme 8 (AK8) and similar ...
 8-44 6.45e-06

dimerization/docking (D/D) domain found in adenylate kinase isoenzyme 8 (AK8) and similar proteins; AK8 (EC 2.7.4.3/EC 2.7.4.6), also called ATP-AMP transphosphorylase 8, acts as a nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. It has highest activity toward AMP, and weaker activity toward dAMP, CMP and dCMP. It also displays broad nucleoside diphosphate kinase activity. AK8 contains an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.


Pssm-ID: 438548  Cd Length: 45  Bit Score: 42.84  E-value: 6.45e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2462507847   8 EYLARREIPQLFESLLNGLMCSKPEDPVEYLESCLQK 44
Cdd:cd22979     8 AYAEKHRIFELFQDLLKQLLIHKPEDPLQFLIDYLQK 44
CMPK cd02020
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ...
 135-166 9.41e-06

Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.


Pssm-ID: 238978 [Multi-domain]  Cd Length: 147  Bit Score: 45.17  E-value: 9.41e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2462507847 135 ILVIGGP-GSGKGTQSLKIAERYGFQYISVGEL 166
Cdd:cd02020     1 IIAIDGPaGSGKSTVAKLLAKKLGLPYLDTGGI 33
DD_TbAK-like cd22981
dimerization/docking (D/D) domain found in Trypanosoma brucei adenylate kinase (AK) and ...
 5-44 1.02e-05

dimerization/docking (D/D) domain found in Trypanosoma brucei adenylate kinase (AK) and similar proteins; AK (EC 2.7.4.3), also called ATP-AMP transphosphorylase, ATP:AMP phosphotransferase, or adenylate monophosphate kinase, catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. It plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Members of this subfamily contain an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.


Pssm-ID: 438550  Cd Length: 44  Bit Score: 42.02  E-value: 1.02e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2462507847   5 DAKEYLARREIPQLFESLLNGLMCSKPEDPVEYLESCLQK 44
Cdd:cd22981     4 DAQKYLKEKNIPQLFEFLLRHLLLDKPENPLEYLHDLLER 43
PRK04182 PRK04182
cytidylate kinase; Provisional
 135-169 1.51e-05

cytidylate kinase; Provisional


Pssm-ID: 235244 [Multi-domain]  Cd Length: 180  Bit Score: 45.18  E-value: 1.51e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2462507847 135 ILVIGG-PGSGKGTQSLKIAERYGFQYISVGELLRK 169
Cdd:PRK04182    2 IITISGpPGSGKTTVARLLAEKLGLKHVSAGEIFRE 37
PRK01184 PRK01184
flagellar hook-basal body complex protein FliE;
132-266 1.58e-05

flagellar hook-basal body complex protein FliE;


Pssm-ID: 234914 [Multi-domain]  Cd Length: 184  Bit Score: 44.94  E-value: 1.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 132 PKIILVIGGPGSGKGTQSlKIAERYGFQYISVGELLRKK-----IHSTSSNrkwslIAKIITT-----GELAPQETTITE 201
Cdd:PRK01184    1 MKIIGVVGMPGSGKGEFS-KIAREMGIPVVVMGDVIREEvkkrgLEPTDEN-----IGKVAIDlrkelGMDAVAKRTVPK 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462507847 202 IKQKLMQIpdeegIVIDGFpRDVAQALSFEDQI-CTPDLVVFLACANQRLkERLLKRaeqqGRPDD 266
Cdd:PRK01184   75 IREKGDEV-----VVIDGV-RGDAEVEYFRKEFpEDFILIAIHAPPEVRF-ERLKKR----GRSDD 129
Pgk2 COG2074
2-phosphoglycerate kinase/Mevalonate-3-phosphate 5-kinase [Carbohydrate transport and ...
 129-279 2.27e-05

2-phosphoglycerate kinase/Mevalonate-3-phosphate 5-kinase [Carbohydrate transport and metabolism, Lipid transport and metabolism];


Pssm-ID: 441677  Cd Length: 207  Bit Score: 44.94  E-value: 2.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 129 RPRPKIILVIGGPGSGKGTQSLKIAERYGFQYI----SVGELLRK--------KIHsTSSNRKW-SLIAKIITTGELAPQ 195
Cdd:COG2074     3 MKRPRIILIGGASGVGKSTIAAELARRLGIPRVistdSIREVMRPiiskelvpTLH-TSSYEAYkSLSEEEIIAGFLDQA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 196 ETTITEIKQklMQ---IPDEEGIVIDG---FPRDVAQALSFEDQICtpdLVVFLACANQRLKERLLKRAEQQGRpddnvK 269
Cdd:COG2074    82 EAVSPGIEA--VIeraLKEGESLVIEGvhlVPGFLAELKFNGGNVV---MLVLLVSDEELHRERFYSRARYTHA-----N 151

                         170
                  ....*....|.
gi 2462507847 270 ATQRRLM-NFK 279
Cdd:COG2074   152 RPGERYLdHFE 162
DD_CrRSP_unchar cd22964
dimerization/docking (D/D) domain of an uncharacterized subunit found in Chlamydomonas ...
 4-47 5.87e-05

dimerization/docking (D/D) domain of an uncharacterized subunit found in Chlamydomonas reinhardtii radial spoke 1; Flagellar radial spokes contribute to the regulation of dynein arm activity and thus the pattern of flagellar bending. They consist of a thin stalk, which is attached to a subfiber of the outer doublet microtubule, and a bulbous head, which is attached to the stalk and appears to interact with the projections from the central pair of microtubules. This subfamily includes an uncharacterized protein found in Chlamydomonas reinhardtii radial spoke 1. It contains a conserved domain that shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.


Pssm-ID: 438533  Cd Length: 46  Bit Score: 40.29  E-value: 5.87e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2462507847   4 NDAKEYLARREIPQLFESLLNGLMCSKPEDPVEYLESCLQKVKE 47
Cdd:cd22964     3 EEKKEYLQQKVINPILEQLVTDLLQEKPEDPVPFMIQWLRKKRS 46
AAA_18 pfam13238
AAA domain;
135-272 6.16e-05

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 42.42  E-value: 6.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 135 ILVIGGPGSGKGTQSLKIAERYGFqYISVGELLRKKIHSTSSNRKWSLiAKIITTGELApqettitEIKQKLMQIPDEEG 214
Cdd:pfam13238   1 ILITGTPGVGKTTLAKELSKRLGF-GDNVRDLALENGLVLGDDPETRE-SKRLDEDKLD-------RLLDLLEENAALEE 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462507847 215 ---IVIDGFPrdvAQALSFEDqicTPDLVVFLACANQRLKERLLKRAEQQGRPDDNVKATQ 272
Cdd:pfam13238  72 ggnLIIDGHL---AELEPERA---KDLVGIVLRASPEELLERLEKRGYEEAKIKENEEAEI 126
PRK03839 PRK03839
putative kinase; Provisional
 134-356 1.20e-04

putative kinase; Provisional


Pssm-ID: 179660  Cd Length: 180  Bit Score: 42.40  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 134 IILVIGGPGSGKGTQSLKIAERYGFQYISVGEL-LRKKIHSTSSNrkwsliakiittgELapqETTITEIKQKLMQIPDE 212
Cdd:PRK03839    2 IIAITGTPGVGKTTVSKLLAEKLGYEYVDLTEFaLKKGIGEEKDD-------------EM---EIDFDKLAYFIEEEFKE 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 213 EGIVIDGFprdvaqaLSfedQICTPDLVVFLACANQRLKERLLKRAEQQGRPDDNVKAtqrRLMNfkqnaAPLVKYFQEK 292
Cdd:PRK03839   66 KNVVLDGH-------LS---HLLPVDYVIVLRAHPKIIKERLKERGYSKKKILENVEA---ELVD-----VCLCEALEEK 127

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462507847 293 GLIMTFD-ADRDEDEVFYDISMAVDNKlfpnKEAAAGssdldpsmILDTGEIIDTGSDYEDQGDD 356
Cdd:PRK03839  128 EKVIEVDtTGKTPEEVVEEILELIKSG----KKRKVG--------IVDWSEVYDEIFPYLRLGID 180
DD_VEST1 cd22980
dimerization/docking (D/D) domain found in protein VEST-1 and similar proteins; VEST-1 (also ...
 9-47 8.94e-04

dimerization/docking (D/D) domain found in protein VEST-1 and similar proteins; VEST-1 (also called protein C8orf34) is an uncharacterized protein which contains an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.


Pssm-ID: 438549  Cd Length: 45  Bit Score: 36.85  E-value: 8.94e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2462507847   9 YLARREIPQLFESLLNGLMCSKPEDPVEYLESCLQKVKE 47
Cdd:cd22980     7 YLEKHKIGALFEDLMAKLIRDTPDEPIPYLIKVLQKKAG 45
CmkB COG1102
Cytidylate kinase [Nucleotide transport and metabolism];
134-219 2.53e-03

Cytidylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 440719 [Multi-domain]  Cd Length: 188  Bit Score: 38.65  E-value: 2.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507847 134 IILVIGG-PGSGKGTQSLKIAERYGFQYISvGELLRKkihsTSSNRKWSLI--------AKIITTGELAPQETTITEIKQ 204
Cdd:COG1102     1 MVITISRePGSGGTTIAKRLAEKLGLPLYD-GEILRE----AAKERGLSEEefekldekAPSLLYRDTAEEDEIDRALDK 75

                          90
                  ....*....|....*
gi 2462507847 205 KLMQIPDEEGIVIDG 219
Cdd:COG1102    76 VIRELARKGNCVIVG 90
BREX_3_BrxF NF033453
BREX-3 system P-loop-containing protein BrxF; This family of proteins that are about 150 amino ...
 133-187 3.14e-03

BREX-3 system P-loop-containing protein BrxF; This family of proteins that are about 150 amino acids in length includes BrxF from type 3 BREX (bacteriophage exclusion) systems. Most members have the P-loop motif GxxGxGKT, but the region is surprisingly poorly conserved in a sizable fraction of otherwise strongly similar proteins.


Pssm-ID: 468038  Cd Length: 149  Bit Score: 37.86  E-value: 3.14e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462507847 133 KIILVIGGPGSGKgTQSLK-IAERYGFQYISVGELLRKKIHSTSSNRKWSLIAKII 187
Cdd:NF033453   17 KLILLVGPPGSGK-TALLReLAAKRGAPVINVNLELSRRLLELPEKQRALRAPRLL 71
DD_TEX55 cd22975
dimerization/docking (D/D) domain found in testis-specific expressed protein 55 (TEX55) and ...
 6-47 8.39e-03

dimerization/docking (D/D) domain found in testis-specific expressed protein 55 (TEX55) and similar proteins; TEX55, also called testis-specific conserved cAMP-dependent type II PK-anchoring protein (TSCPA), is a putative A-kinase anchoring protein (AKAP) that is dispensable for male fertility. It contains a C-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.


Pssm-ID: 438544  Cd Length: 50  Bit Score: 34.08  E-value: 8.39e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2462507847   6 AKEYLARREIPQLFESLLNGLMCSKPEDPVEYLESCLQKVKE 47
Cdd:cd22975     7 AVKYLEKHNILQLFQELTAGLVYERPDDPIQFMIDEIEKIIK 48
 
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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