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Conserved domains on  [gi|767956394|ref|XP_011516579|]
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adenylate kinase 8 isoform X4 [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 ...
 71-261 9.09e-36

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: 129.28  E-value: 9.09e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394  71 RIVILGPPASGKTTIAMWLCKHLNSSLLT----LENLILNEFSYTAtEARRLYLQRKTVPSALLVQLIQERLAEEDCiKQ 146
Cdd:cd01428    1 RILLLGPPGSGKGTQAERLAKKYGLPHIStgdlLREEIASGTELGK-KAKEYIDSGKLVPDEIVIKLLKERLKKPDC-KK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394 147 GWILDGIPETREQALRIQTL---GITPRHVIVLSAPDTVLIERNLGKRIDPQTGEIYHTTFDWPPESEIQNRlmvPEDis 223
Cdd:cd01428   79 GFILDGFPRTVDQAEALDELldeGIKPDKVIELDVPDEVLIERILGRRICPVSGRVYHLGKDDVTGEPLSQR---SDD-- 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 767956394 224 ELETAQKLLE-YHRNIVRVIPSYPK--ILKVISADQPCVDV 261
Cdd:cd01428  154 NEETIKKRLEvYKEQTAPLIDYYKKkgKLVEIDGSGDIDEV 194
DD_AK8 cd22979
dimerization/docking (D/D) domain found in adenylate kinase isoenzyme 8 (AK8) and similar ...
 9-65 3.98e-15

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: 68.65  E-value: 3.98e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767956394   9 RIPPEMPQYGEENHIFELMQvlttwvsalhpqNMLEQLLIHQPEDPIPFMIQHLHRD 65
Cdd:cd22979    1 EIPPEFAAYAEKHRIFELFQ------------DLLKQLLIHKPEDPLQFLIDYLQKP 45
NK super family cl17190
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ...
 282-335 9.33e-15

Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of enzymes that share structural similarity and are functionally related to the catalysis of the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars. Members of this family play a wide variety of essential roles in nucleotide metabolism, the biosynthesis of coenzymes and aromatic compounds, as well as the metabolism of sugar and sulfate.


The actual alignment was detected with superfamily member cd01428:

Pssm-ID: 450170 [Multi-domain]  Cd Length: 194  Bit Score: 71.88  E-value: 9.33e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767956394 282 RVLLLGPVGSGKSLQAALLAQKYRLVNVCCGQLLKEAVADRTTFGELIQPFFEK 335
Cdd:cd01428    1 RILLLGPPGSGKGTQAERLAKKYGLPHISTGDLLREEIASGTELGKKAKEYIDS 54
 
Name Accession Description Interval E-value
ADK cd01428
Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine ...
 71-261 9.09e-36

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: 129.28  E-value: 9.09e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394  71 RIVILGPPASGKTTIAMWLCKHLNSSLLT----LENLILNEFSYTAtEARRLYLQRKTVPSALLVQLIQERLAEEDCiKQ 146
Cdd:cd01428    1 RILLLGPPGSGKGTQAERLAKKYGLPHIStgdlLREEIASGTELGK-KAKEYIDSGKLVPDEIVIKLLKERLKKPDC-KK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394 147 GWILDGIPETREQALRIQTL---GITPRHVIVLSAPDTVLIERNLGKRIDPQTGEIYHTTFDWPPESEIQNRlmvPEDis 223
Cdd:cd01428   79 GFILDGFPRTVDQAEALDELldeGIKPDKVIELDVPDEVLIERILGRRICPVSGRVYHLGKDDVTGEPLSQR---SDD-- 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 767956394 224 ELETAQKLLE-YHRNIVRVIPSYPK--ILKVISADQPCVDV 261
Cdd:cd01428  154 NEETIKKRLEvYKEQTAPLIDYYKKkgKLVEIDGSGDIDEV 194
PLN02842 PLN02842
nucleotide kinase
 73-262 2.14e-30

nucleotide kinase


Pssm-ID: 178435 [Multi-domain]  Cd Length: 505  Bit Score: 121.51  E-value: 2.14e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394  73 VILGPPASGKTTIAMWLCKHLNSSLLTLENLILNEFSyTATE----ARRLYLQRKTVPSALLVQLIQERLAEEDCIKQGW 148
Cdd:PLN02842   1 MISGAPASGKGTQCELIVHKFGLVHISTGDLLRAEVS-AGTDigkrAKEFMNSGRLVPDEIVIAMVTGRLSREDAKEKGW 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394 149 ILDGIPETREQALRIQTLGITPRHVIVLSAPDTVLIERNLGKRIDPQTGEIYHTTFdWPPES-EIQNRLMVPEDISELET 227
Cdd:PLN02842  80 LLDGYPRSFAQAQSLEKLKIRPDIFILLDVPDEILIDRCVGRRLDPVTGKIYHIKN-FPPESeEIKARLITRPDDTEEKV 158

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 767956394 228 AQKLLEYHRNIVRVIPSYPKILKVISADQPCVDVF 262
Cdd:PLN02842 159 KARLQIYKKNAEAILSTYSDIMVKIDGNRPKEVVF 193
adk TIGR01351
adenylate kinase; Adenylate kinase (EC 2.7.4.3) converts ATP + AMP to ADP + ADP, that is, uses ...
 71-270 2.68e-30

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: 115.02  E-value: 2.68e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394   71 RIVILGPPASGKTTIAMWLCK-----HLNSSLLTLENLILNefSYTATEARRlYLQR-KTVPSALLVQLIQERLAEEDCI 144
Cdd:TIGR01351   1 RLVLLGPPGSGKGTQAKRIAEkyglpHISTGDLLRAEIKAG--TPLGKKAKE-YMEKgELVPDEIVNQLVKERLTQNDDN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394  145 KQGWILDGIPETREQALRI-QTLGITPRHVIVLSAPDTVLIERNLGKRIDPQTGEIYHTTFDWPPESEIQN----RLMVP 219
Cdd:TIGR01351  78 ENGFILDGFPRTLSQAEALdALLEEPIDAVIELDVPDEELVERLSGRRICPSCGRVYHLKFNPPKVPGCDDctgeLLVQR 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767956394  220 EDISElETAQKLLE-YHRNIVRVIPSYPK--ILKVISADQPCVDVFYQALTYVQ 270
Cdd:TIGR01351 158 EDDTE-EVVKKRLEvYKEQTEPLIDYYKKrgILVQIDGNGPIDEVWKRILEALK 210
Adk COG0563
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ...
 71-262 6.25e-28

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: 108.68  E-value: 6.25e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394  71 RIVILGPPASGKTTIAMWLCKHLNSSLLT----LENLILNEfsytaTEarrLYLQRKT-------VPSALLVQLIQERLA 139
Cdd:COG0563    2 RIILLGPPGAGKGTQAKRLAEKYGIPHIStgdmLRAAVKAG-----TE---LGKKAKEymdagelVPDEIVIGLVKERLA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394 140 EEDCiKQGWILDGIPETREQALRIQTL----GITPRHVIVLSAPDTVLIERNLGKRIDPQTGEIYHTTFDWPPESEI--- 212
Cdd:COG0563   74 QPDC-ANGFILDGFPRTVAQAEALDELlaelGIKLDAVIELDVDDEELVERLSGRRVCPNCGATYHVKFNPPKVEGVcdk 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767956394 213 -QNRLMVPEDISElETAQKLLE-YHRNIVRVIPSYPK--ILKVISADQPCVDVF 262
Cdd:COG0563  153 cGGELVQRADDNE-ETVRKRLEvYHEQTAPLIDYYRKkgKLVEIDGEGSIEEVT 205
ADK pfam00406
Adenylate kinase;
74-247 4.99e-21

Adenylate kinase;


Pssm-ID: 395329 [Multi-domain]  Cd Length: 184  Bit Score: 89.29  E-value: 4.99e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394   74 ILGPPASGKTTIAMWLCKHLNSSLLTLENLILNEFSyTATE----ARRLYLQRKTVPSALLVQLIQERLAEEDCiKQGWI 149
Cdd:pfam00406   1 LLGPPGAGKGTQAEKIVQKYGLPHLSTGDLLRAEIK-SGTElgkeAKEYMDKGELVPDEVVVGLVKERLEQNDC-KNGFL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394  150 LDGIPETREQAL---RIQTLGITPRHVIVLSAPDTVLIERNLGKRIDPQTGEIYHTTFDwPPESEIQN-----RLMVPED 221
Cdd:pfam00406  79 LDGFPRTVPQAEaleELLERGIKLDYVIEFDVPDEVLVERLTGRRIHPNSGRSYHLEFN-PPKVPGKDdvtgePLVQRSD 157

                         170       180
                  ....*....|....*....|....*..
gi 767956394  222 ISElETAQKLLE-YHRNIVRVIPSYPK 247
Cdd:pfam00406 158 DNE-ETVKKRLEtYHKQTKPLIDYYKK 183
DD_AK8 cd22979
dimerization/docking (D/D) domain found in adenylate kinase isoenzyme 8 (AK8) and similar ...
 9-65 3.98e-15

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: 68.65  E-value: 3.98e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767956394   9 RIPPEMPQYGEENHIFELMQvlttwvsalhpqNMLEQLLIHQPEDPIPFMIQHLHRD 65
Cdd:cd22979    1 EIPPEFAAYAEKHRIFELFQ------------DLLKQLLIHKPEDPLQFLIDYLQKP 45
ADK cd01428
Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine ...
 282-335 9.33e-15

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: 71.88  E-value: 9.33e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767956394 282 RVLLLGPVGSGKSLQAALLAQKYRLVNVCCGQLLKEAVADRTTFGELIQPFFEK 335
Cdd:cd01428    1 RILLLGPPGSGKGTQAERLAKKYGLPHISTGDLLREEIASGTELGKKAKEYIDS 54
Adk COG0563
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ...
 282-335 6.14e-07

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: 49.74  E-value: 6.14e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767956394 282 RVLLLGPVGSGKSLQAALLAQKYRLVNVCCGQLLKEAVADRTTFGELIQPFFEK 335
Cdd:COG0563    2 RIILLGPPGAGKGTQAKRLAEKYGIPHISTGDMLRAAVKAGTELGKKAKEYMDA 55
PRK13808 PRK13808
adenylate kinase; Provisional
 282-326 6.46e-07

adenylate kinase; Provisional


Pssm-ID: 172341 [Multi-domain]  Cd Length: 333  Bit Score: 50.66  E-value: 6.46e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 767956394 282 RVLLLGPVGSGKSLQAALLAQKYRLVNVCCGQLLKEAVADRTTFG 326
Cdd:PRK13808   2 RLILLGPPGAGKGTQAQRLVQQYGIVQLSTGDMLRAAVAAGTPVG 46
ADK pfam00406
Adenylate kinase;
285-335 8.41e-07

Adenylate kinase;


Pssm-ID: 395329 [Multi-domain]  Cd Length: 184  Bit Score: 48.84  E-value: 8.41e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767956394  285 LLGPVGSGKSLQAALLAQKYRLVNVCCGQLLKEAVADRTTFGELIQPFFEK 335
Cdd:pfam00406   1 LLGPPGAGKGTQAEKIVQKYGLPHLSTGDLLRAEIKSGTELGKEAKEYMDK 51
UMP_CMP_kin_fam TIGR01359
UMP-CMP kinase family; This subfamily of the adenylate kinase superfamily contains examples of ...
 283-330 2.31e-04

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: 41.59  E-value: 2.31e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 767956394  283 VLLLGPVGSGKSLQAALLAQKYRLVNVCCGQLLKEAVADR-TTFGELIQ 330
Cdd:TIGR01359   2 VFVLGGPGSGKGTQCAKIVENFGFTHLSAGDLLRAEIKREgSENGSLIE 50
 
Name Accession Description Interval E-value
ADK cd01428
Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine ...
 71-261 9.09e-36

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: 129.28  E-value: 9.09e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394  71 RIVILGPPASGKTTIAMWLCKHLNSSLLT----LENLILNEFSYTAtEARRLYLQRKTVPSALLVQLIQERLAEEDCiKQ 146
Cdd:cd01428    1 RILLLGPPGSGKGTQAERLAKKYGLPHIStgdlLREEIASGTELGK-KAKEYIDSGKLVPDEIVIKLLKERLKKPDC-KK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394 147 GWILDGIPETREQALRIQTL---GITPRHVIVLSAPDTVLIERNLGKRIDPQTGEIYHTTFDWPPESEIQNRlmvPEDis 223
Cdd:cd01428   79 GFILDGFPRTVDQAEALDELldeGIKPDKVIELDVPDEVLIERILGRRICPVSGRVYHLGKDDVTGEPLSQR---SDD-- 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 767956394 224 ELETAQKLLE-YHRNIVRVIPSYPK--ILKVISADQPCVDV 261
Cdd:cd01428  154 NEETIKKRLEvYKEQTAPLIDYYKKkgKLVEIDGSGDIDEV 194
PLN02842 PLN02842
nucleotide kinase
 73-262 2.14e-30

nucleotide kinase


Pssm-ID: 178435 [Multi-domain]  Cd Length: 505  Bit Score: 121.51  E-value: 2.14e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394  73 VILGPPASGKTTIAMWLCKHLNSSLLTLENLILNEFSyTATE----ARRLYLQRKTVPSALLVQLIQERLAEEDCIKQGW 148
Cdd:PLN02842   1 MISGAPASGKGTQCELIVHKFGLVHISTGDLLRAEVS-AGTDigkrAKEFMNSGRLVPDEIVIAMVTGRLSREDAKEKGW 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394 149 ILDGIPETREQALRIQTLGITPRHVIVLSAPDTVLIERNLGKRIDPQTGEIYHTTFdWPPES-EIQNRLMVPEDISELET 227
Cdd:PLN02842  80 LLDGYPRSFAQAQSLEKLKIRPDIFILLDVPDEILIDRCVGRRLDPVTGKIYHIKN-FPPESeEIKARLITRPDDTEEKV 158

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 767956394 228 AQKLLEYHRNIVRVIPSYPKILKVISADQPCVDVF 262
Cdd:PLN02842 159 KARLQIYKKNAEAILSTYSDIMVKIDGNRPKEVVF 193
adk TIGR01351
adenylate kinase; Adenylate kinase (EC 2.7.4.3) converts ATP + AMP to ADP + ADP, that is, uses ...
 71-270 2.68e-30

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: 115.02  E-value: 2.68e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394   71 RIVILGPPASGKTTIAMWLCK-----HLNSSLLTLENLILNefSYTATEARRlYLQR-KTVPSALLVQLIQERLAEEDCI 144
Cdd:TIGR01351   1 RLVLLGPPGSGKGTQAKRIAEkyglpHISTGDLLRAEIKAG--TPLGKKAKE-YMEKgELVPDEIVNQLVKERLTQNDDN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394  145 KQGWILDGIPETREQALRI-QTLGITPRHVIVLSAPDTVLIERNLGKRIDPQTGEIYHTTFDWPPESEIQN----RLMVP 219
Cdd:TIGR01351  78 ENGFILDGFPRTLSQAEALdALLEEPIDAVIELDVPDEELVERLSGRRICPSCGRVYHLKFNPPKVPGCDDctgeLLVQR 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767956394  220 EDISElETAQKLLE-YHRNIVRVIPSYPK--ILKVISADQPCVDVFYQALTYVQ 270
Cdd:TIGR01351 158 EDDTE-EVVKKRLEvYKEQTEPLIDYYKKrgILVQIDGNGPIDEVWKRILEALK 210
Adk COG0563
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ...
 71-262 6.25e-28

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: 108.68  E-value: 6.25e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394  71 RIVILGPPASGKTTIAMWLCKHLNSSLLT----LENLILNEfsytaTEarrLYLQRKT-------VPSALLVQLIQERLA 139
Cdd:COG0563    2 RIILLGPPGAGKGTQAKRLAEKYGIPHIStgdmLRAAVKAG-----TE---LGKKAKEymdagelVPDEIVIGLVKERLA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394 140 EEDCiKQGWILDGIPETREQALRIQTL----GITPRHVIVLSAPDTVLIERNLGKRIDPQTGEIYHTTFDWPPESEI--- 212
Cdd:COG0563   74 QPDC-ANGFILDGFPRTVAQAEALDELlaelGIKLDAVIELDVDDEELVERLSGRRVCPNCGATYHVKFNPPKVEGVcdk 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767956394 213 -QNRLMVPEDISElETAQKLLE-YHRNIVRVIPSYPK--ILKVISADQPCVDVF 262
Cdd:COG0563  153 cGGELVQRADDNE-ETVRKRLEvYHEQTAPLIDYYRKkgKLVEIDGEGSIEEVT 205
adk PRK00279
adenylate kinase; Reviewed
 71-262 3.16e-22

adenylate kinase; Reviewed


Pssm-ID: 234711 [Multi-domain]  Cd Length: 215  Bit Score: 93.29  E-value: 3.16e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394  71 RIVILGPPASGKTTIAMWLCKHLNsslltlenliLNEFSyT----------ATEarrLYLQRKT-------VPSALLVQL 133
Cdd:PRK00279   2 RLILLGPPGAGKGTQAKFIAEKYG----------IPHIS-TgdmlraavkaGTE---LGKEAKSymdagelVPDEIVIGL 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394 134 IQERLAEEDCiKQGWILDGIPETREQAL----RIQTLGITPRHVIVLSAPDTVLIERNLGKRIDPQTGEIYHTTFDWPPE 209
Cdd:PRK00279  68 VKERLAQPDC-KNGFLLDGFPRTIPQAEaldeMLKELGIKLDAVIEIDVPDEELVERLSGRRICPACGRTYHVKFNPPKV 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394 210 SEIQNR----LMVPEDISElETAQKLLE-YHRNIVRVIPSYPK--ILKVISADQPCVDVF 262
Cdd:PRK00279 147 EGKCDVcgeeLIQRADDNE-ETVRKRLEvYHKQTAPLIDYYKKkgKLKKIDGTGSIDEVF 205
ADK pfam00406
Adenylate kinase;
74-247 4.99e-21

Adenylate kinase;


Pssm-ID: 395329 [Multi-domain]  Cd Length: 184  Bit Score: 89.29  E-value: 4.99e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394   74 ILGPPASGKTTIAMWLCKHLNSSLLTLENLILNEFSyTATE----ARRLYLQRKTVPSALLVQLIQERLAEEDCiKQGWI 149
Cdd:pfam00406   1 LLGPPGAGKGTQAEKIVQKYGLPHLSTGDLLRAEIK-SGTElgkeAKEYMDKGELVPDEVVVGLVKERLEQNDC-KNGFL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394  150 LDGIPETREQAL---RIQTLGITPRHVIVLSAPDTVLIERNLGKRIDPQTGEIYHTTFDwPPESEIQN-----RLMVPED 221
Cdd:pfam00406  79 LDGFPRTVPQAEaleELLERGIKLDYVIEFDVPDEVLVERLTGRRIHPNSGRSYHLEFN-PPKVPGKDdvtgePLVQRSD 157

                         170       180
                  ....*....|....*....|....*..
gi 767956394  222 ISElETAQKLLE-YHRNIVRVIPSYPK 247
Cdd:pfam00406 158 DNE-ETVKKRLEtYHKQTKPLIDYYKK 183
adk PRK02496
adenylate kinase; Provisional
 71-236 8.27e-18

adenylate kinase; Provisional


Pssm-ID: 179433 [Multi-domain]  Cd Length: 184  Bit Score: 80.56  E-value: 8.27e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394  71 RIVILGPPASGKTTIAMWLCKHLNSSLLTLENLI---LNEFSYTATEARRLYLQRKTVPSALLVQLIQERLAEEDCiKQG 147
Cdd:PRK02496   3 RLIFLGPPGAGKGTQAVVLAEHLHIPHISTGDILrqaIKEQTPLGIKAQGYMDKGELVPDQLVLDLVQERLQQPDA-ANG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394 148 WILDGIPETREQA----LRIQTLGITPRHVIVLSAPDTVLIERNLGK-RIDPQtgeiyhttfdwppESEIQNRLMVPEDi 222
Cdd:PRK02496  82 WILDGFPRKVTQAafldELLQEIGQSGERVVNLDVPDDVVVERLLARgRKDDT-------------EEVIRRRLEVYRE- 147

                        170
                 ....*....|....
gi 767956394 223 selETAqKLLEYHR 236
Cdd:PRK02496 148 ---QTA-PLIDYYR 157
PRK14530 PRK14530
adenylate kinase; Provisional
 70-245 2.65e-16

adenylate kinase; Provisional


Pssm-ID: 237747 [Multi-domain]  Cd Length: 215  Bit Score: 76.75  E-value: 2.65e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394  70 PRIVILGPPASGKTTIAMWLCKHLNSSLLT----LENLILNEFSYTATE--ARRLYLQR-KTVPSALLVQLIQERLAEED 142
Cdd:PRK14530   4 PRILLLGAPGAGKGTQSSNLAEEFGVEHVTtgdaLRANKQMDISDMDTEydTPGEYMDAgELVPDAVVNEIVEEALSDAD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394 143 cikqGWILDGIPETREQALRIQtlGITPRHVIV-LSAPDTVLIERNLGKRIDPQTGEIYHTTFDWPPESEIQN----RLM 217
Cdd:PRK14530  84 ----GFVLDGYPRNLEQAEYLE--SITDLDVVLyLDVSEEELVDRLTGRRVCPDCGANYHVEFNQPEEEGVCDecggELI 157

                        170       180
                 ....*....|....*....|....*....
gi 767956394 218 VPEDISElETAQKLLE-YHRNIVRVIPSY 245
Cdd:PRK14530 158 QRDDDTE-ETVRERLDvFEENTEPVIEHY 185
DD_AK8 cd22979
dimerization/docking (D/D) domain found in adenylate kinase isoenzyme 8 (AK8) and similar ...
 9-65 3.98e-15

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: 68.65  E-value: 3.98e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767956394   9 RIPPEMPQYGEENHIFELMQvlttwvsalhpqNMLEQLLIHQPEDPIPFMIQHLHRD 65
Cdd:cd22979    1 EIPPEFAAYAEKHRIFELFQ------------DLLKQLLIHKPEDPLQFLIDYLQKP 45
PRK14528 PRK14528
adenylate kinase; Provisional
 71-192 5.08e-15

adenylate kinase; Provisional


Pssm-ID: 172994 [Multi-domain]  Cd Length: 186  Bit Score: 72.74  E-value: 5.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394  71 RIVILGPPASGKTTIAMWLCKHLNSSLLTLENlILNEFSYTAT----EARRLYLQRKTVPSALLVQLIQERLAEEDCiKQ 146
Cdd:PRK14528   3 NIIFMGPPGAGKGTQAKILCERLSIPQISTGD-ILREAVKNQTamgiEAKRYMDAGDLVPDSVVIGIIKDRIREADC-KN 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 767956394 147 GWILDGIPETREQALR----IQTLGITPRHVIVLSAPDTVLIERNLGKRI 192
Cdd:PRK14528  81 GFLLDGFPRTVEQADAldalLKNEGKSIDKAINLEVPDGELLKRLLGRAE 130
ADK cd01428
Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine ...
 282-335 9.33e-15

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: 71.88  E-value: 9.33e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767956394 282 RVLLLGPVGSGKSLQAALLAQKYRLVNVCCGQLLKEAVADRTTFGELIQPFFEK 335
Cdd:cd01428    1 RILLLGPPGSGKGTQAERLAKKYGLPHISTGDLLREEIASGTELGKKAKEYIDS 54
PLN02674 PLN02674
adenylate kinase
 71-261 2.56e-11

adenylate kinase


Pssm-ID: 178279 [Multi-domain]  Cd Length: 244  Bit Score: 62.98  E-value: 2.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394  71 RIVILGPPASGKTTIA------MWLCKHLNSSLLTLENLILNEFSYTATEARRlylQRKTVPSALLVQLIQERLAEEDCI 144
Cdd:PLN02674  33 RLILIGPPGSGKGTQSpiikdeYCLCHLATGDMLRAAVAAKTPLGIKAKEAMD---KGELVSDDLVVGIIDEAMKKPSCQ 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394 145 KqGWILDGIPETREQALRIQTL----GITPRHVIVLSAPDTVLIERNLGKRIDPQTGEIYHTTFDwPP----------ES 210
Cdd:PLN02674 110 K-GFILDGFPRTVVQAQKLDEMlakqGAKIDKVLNFAIDDAILEERITGRWIHPSSGRTYHTKFA-PPkvpgvddvtgEP 187

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767956394 211 EIQNRlmvpEDISELeTAQKLLEYHRNIVRVIPSYPK--ILKVISADQPCVDV 261
Cdd:PLN02674 188 LIQRK----DDTAAV-LKSRLEAFHKQTEPVIDYYAKkgVVANLHAEKPPKEV 235
PTZ00088 PTZ00088
adenylate kinase 1; Provisional
 71-208 4.64e-10

adenylate kinase 1; Provisional


Pssm-ID: 240262 [Multi-domain]  Cd Length: 229  Bit Score: 59.04  E-value: 4.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394  71 RIVILGPPASGKTTIAMWLCKHLNSSLLTLENLILNEFSYTAT---EARRLYLQRKTVPSALLVQLIQERLAE-EDCIKQ 146
Cdd:PTZ00088   8 KIVLFGAPGVGKGTFAEILSKKENLKHINMGNILREEIKAKTTigkEIQKVVTSGNLVPDNLVIAIVKDEIAKvTDDCFK 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767956394 147 GWILDGIPETREQALRIQTLgITPRHVIVLSAPDTVLIERNLGKRIDPQTGEIYH------TTFDWPP 208
Cdd:PTZ00088  88 GFILDGFPRNLKQCKELGKI-TNIDLFVNIYLPRNILIKKLLGRRICNTCNRNFNiahirsDPYDMPP 154
AAA_17 pfam13207
AAA domain;
75-191 7.03e-10

AAA domain;


Pssm-ID: 463810 [Multi-domain]  Cd Length: 136  Bit Score: 56.48  E-value: 7.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394   75 LGPPASGKTTIAMWLCKHLN------SSLLtLENLILNEFSYTATEARRLYLQRKTVpsalLVQLIQERLAEEdCIKQGW 148
Cdd:pfam13207   1 TGVPGSGKTTQLKKLAEKLGfphisaGDLL-REEAKERGLVEDRDEMRKLPLEPQKE----LQKLAAERIAEE-AGEGGV 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 767956394  149 ILDGIPETREQALRIQTL------GITPRHVIVLSAPDTVLIERNLGKR 191
Cdd:pfam13207  75 IVDGHPRIKTPAGYLPGLpvevlrELKPDAIILLEADPEEILERRLKDR 123
DD_TEX55-like cd22961
dimerization/docking (D/D) domain found in the testis-specific expressed protein 55 (TEX55) ...
 12-64 1.44e-09

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: 52.80  E-value: 1.44e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767956394  12 PEMPQYGEENHIFELMQvlttwvsalhpqNMLEQLLIHQPEDPIPFMIQHLHR 64
Cdd:cd22961    2 EDAEEYLEKHKIPELFE------------SLLTALLIEKPEDPIEFLIDKLQQ 42
PRK14527 PRK14527
adenylate kinase; Provisional
 68-190 1.51e-09

adenylate kinase; Provisional


Pssm-ID: 237745 [Multi-domain]  Cd Length: 191  Bit Score: 57.11  E-value: 1.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394  68 NVPRIVI-LGPPASGKTTIAMWLCKHLNSSLLTLENlILNEFSYTATE----ARRLYLQRKTVPSALLVQLIQERLAEED 142
Cdd:PRK14527   4 TKNKVVIfLGPPGAGKGTQAERLAQELGLKKLSTGD-ILRDHVARGTElgqrAKPIMEAGDLVPDELILALIRDELAGME 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767956394 143 CIKQgwILDGIPETREQA----LRIQTLGITPRHVIVLSAPDTVLIERNLGK 190
Cdd:PRK14527  83 PVRV--IFDGFPRTLAQAealdRLLEELGARLLAVVLLEVPDEELIRRIVER 132
PRK14531 PRK14531
adenylate kinase; Provisional
 71-237 1.29e-08

adenylate kinase; Provisional


Pssm-ID: 172997 [Multi-domain]  Cd Length: 183  Bit Score: 54.05  E-value: 1.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394  71 RIVILGPPASGKTTIAMWLCKHLNSSLLTLENLILNEF---SYTATEARRLYLQRKTVPSALLVQLIQERLAEEDciKQG 147
Cdd:PRK14531   4 RLLFLGPPGAGKGTQAARLCAAHGLRHLSTGDLLRSEVaagSALGQEAEAVMNRGELVSDALVLAIVESQLKALN--SGG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394 148 WILDGIPETREQALR----IQTLGITPRHVIVLSAPDTVLIERNLGK-RIDPQtgeiyhttfdwppESEIQNRLMVPEDi 222
Cdd:PRK14531  82 WLLDGFPRTVAQAEAleplLEELKQPIEAVVLLELDDAVLIERLLARgRADDN-------------EAVIRNRLEVYRE- 147

                        170
                 ....*....|....*
gi 767956394 223 selETAqKLLEYHRN 237
Cdd:PRK14531 148 ---KTA-PLIDHYRQ 158
Kti12 COG4088
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ...
 70-237 6.24e-08

tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) [Translation, ribosomal structure and biogenesis, Defense mechanisms];


Pssm-ID: 443264 [Multi-domain]  Cd Length: 179  Bit Score: 52.04  E-value: 6.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394  70 PRIVIL-GPPASGKTTIAmwlcKHLnSSLLTLENlilNEFSYTATEARRLYLQRKTVPSALLVQLIQErlAEEDCIKQG- 147
Cdd:COG4088    4 PMLLILtGPPGSGKTTFA----KAL-AQRLYAEG---IAVALLHSDDFRRFLVNESFPKETYEEVVED--VRTTTADNAl 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394 148 -----WILDGIPETREQALRIQTLGI--TPRHVIVLSAPDTVLIERNL--GKRIDPQTGEIYHTTFDWPPESEIQNRLMV 218
Cdd:COG4088   74 dngysVIVDGTFYYRSWQRDFRNLAKhkAPIHIIYLKAPLETALRRNRerGEPIPERVIARMYRKFDKPGTKDRPDLVID 153

                        170
                 ....*....|....*....
gi 767956394 219 PEDISELETAQKLLEYHRN 237
Cdd:COG4088  154 TTEDSVSETLDAILKAIET 172
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
72-211 9.51e-08

Predicted kinase, contains AAA domain [General function prediction only];


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 51.07  E-value: 9.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394  72 IVILGPPASGKTTIAMWLCKHLNSSLL-------TLENLILNEFSYTATEARRLYlqrktvpsALLVQLIqerlaeEDCI 144
Cdd:COG0645    2 ILVCGLPGSGKSTLARALAERLGAVRLrsdvvrkRLFGAGLAPLERSPEATARTY--------ARLLALA------RELL 67

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767956394 145 KQGW--ILDG---IPETREQALRI-QTLGITPrHVIVLSAPDTVLIE----RNLGKRIDPQTGEIY-HTTFDWPPESE 211
Cdd:COG0645   68 AAGRsvILDAtflRRAQREAFRALaEEAGAPF-VLIWLDAPEEVLRErleaRNAEGGDSDATWEVLeRQLAFEEPLTE 144
UMP_CMP_kin_fam TIGR01359
UMP-CMP kinase family; This subfamily of the adenylate kinase superfamily contains examples of ...
 72-190 3.49e-07

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: 50.06  E-value: 3.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394   72 IVILGPPASGKTTIAMWLCKHLNSSLLTLENLILNEFSYTATEARRLYL----QRKTVPSALLVQLIQERLaEEDCIKQG 147
Cdd:TIGR01359   2 VFVLGGPGSGKGTQCAKIVENFGFTHLSAGDLLRAEIKREGSENGSLIEsyikEGKIVPSEVTVELLKKAI-QEDGSSKK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 767956394  148 WILDGIP---ETREQALRIQTLGITPRHVIVLSAPDTVLIERNLGK 190
Cdd:TIGR01359  81 FLIDGFPrneENLEAWEKLMDNKVNFKFVLFFDCPEETMIKRLLKR 126
Adk COG0563
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ...
 282-335 6.14e-07

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: 49.74  E-value: 6.14e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767956394 282 RVLLLGPVGSGKSLQAALLAQKYRLVNVCCGQLLKEAVADRTTFGELIQPFFEK 335
Cdd:COG0563    2 RIILLGPPGAGKGTQAKRLAEKYGIPHISTGDMLRAAVKAGTELGKKAKEYMDA 55
PRK13808 PRK13808
adenylate kinase; Provisional
 282-326 6.46e-07

adenylate kinase; Provisional


Pssm-ID: 172341 [Multi-domain]  Cd Length: 333  Bit Score: 50.66  E-value: 6.46e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 767956394 282 RVLLLGPVGSGKSLQAALLAQKYRLVNVCCGQLLKEAVADRTTFG 326
Cdd:PRK13808   2 RLILLGPPGAGKGTQAQRLVQQYGIVQLSTGDMLRAAVAAGTPVG 46
ADK pfam00406
Adenylate kinase;
285-335 8.41e-07

Adenylate kinase;


Pssm-ID: 395329 [Multi-domain]  Cd Length: 184  Bit Score: 48.84  E-value: 8.41e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767956394  285 LLGPVGSGKSLQAALLAQKYRLVNVCCGQLLKEAVADRTTFGELIQPFFEK 335
Cdd:pfam00406   1 LLGPPGAGKGTQAEKIVQKYGLPHLSTGDLLRAEIKSGTELGKEAKEYMDK 51
PRK14527 PRK14527
adenylate kinase; Provisional
 283-334 1.10e-06

adenylate kinase; Provisional


Pssm-ID: 237745 [Multi-domain]  Cd Length: 191  Bit Score: 48.63  E-value: 1.10e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767956394 283 VLLLGPVGSGKSLQAALLAQKYRLVNVCCGQLLKEAVADRTTFGELIQPFFE 334
Cdd:PRK14527   9 VIFLGPPGAGKGTQAERLAQELGLKKLSTGDILRDHVARGTELGQRAKPIME 60
DD_EFCAB10 cd22976
dimerization/docking (D/D) domain found in EF-hand calcium-binding domain-containing protein ...
 16-62 1.26e-06

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: 44.78  E-value: 1.26e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 767956394  16 QYGEENHIFELMQvlttwvsalhpqNMLEQLLIHQPEDPIPFMIQHL 62
Cdd:cd22976    6 EYLEKHKIPELFE------------NLTSLLLYHRPEDPKAFLIEQL 40
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 72-187 2.37e-06

AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.


Pssm-ID: 463952 [Multi-domain]  Cd Length: 143  Bit Score: 46.53  E-value: 2.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394   72 IVILGPPASGKTTIAMWLCKHLNSSLLTLENLIlnefsytateaRRLY-LQRKTVP-SALLVQLIQERLAE--EDCIKQG 147
Cdd:pfam13671   2 ILLVGLPGSGKSTLARRLLEELGAVRLSSDDER-----------KRLFgEGRPSISyYTDATDRTYERLHElaRIALRAG 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 767956394  148 W--ILDGI---PETREQALRI-QTLGItPRHVIVLSAPDTVLIERN 187
Cdd:pfam13671  71 RpvILDATnlrRDERARLLALaREYGV-PVRIVVFEAPEEVLRERL 115
AAA_18 pfam13238
AAA domain;
72-186 4.05e-06

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 45.50  E-value: 4.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394   72 IVILGPPASGKTTIAMWLCKHLNSSLLTLENLILNEFSYTATEARRLYL-QRKTVPSALLVQLIQERLAEEDcikQGWIL 150
Cdd:pfam13238   1 ILITGTPGVGKTTLAKELSKRLGFGDNVRDLALENGLVLGDDPETRESKrLDEDKLDRLLDLLEENAALEEG---GNLII 77

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 767956394  151 DGIPETREQALRIQtlgitpRHVIVLSAPDTVLIER 186
Cdd:pfam13238  78 DGHLAELEPERAKD------LVGIVLRASPEELLER 107
PRK14526 PRK14526
adenylate kinase; Provisional
 71-247 5.59e-06

adenylate kinase; Provisional


Pssm-ID: 172992 [Multi-domain]  Cd Length: 211  Bit Score: 46.77  E-value: 5.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394  71 RIVILGPPASGKTTIAMWLCKHLNSSLLTLENL----ILNEfSYTATEARRLYLQRKTVPSALLVQLIQERLAEEDCiKQ 146
Cdd:PRK14526   2 KLVFLGPPGSGKGTIAKILSNELNYYHISTGDLfrenILNS-TPLGKEIKQIVENGQLVPDSITIKIVEDKINTIKN-ND 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394 147 GWILDGIPETREQALRIQTLgITPRHVIVLSAPDTVLIERNLGKRIDPQTGEIYHTTFDWPPESEI----QNRLMVPEDI 222
Cdd:PRK14526  80 NFILDGFPRNINQAKALDKF-LPNIKIINFLIDEELLIKRLSGRRICKSCNNIFNIYTLPTKEKGIcdvcKGDLYQRKDD 158

                        170       180
                 ....*....|....*....|....*
gi 767956394 223 SELETAQKLLEYHRNIVRVIPSYPK 247
Cdd:PRK14526 159 KEESLKTRLQEYKLQTKPLIEFYSK 183
adk PRK02496
adenylate kinase; Provisional
 282-335 6.10e-06

adenylate kinase; Provisional


Pssm-ID: 179433 [Multi-domain]  Cd Length: 184  Bit Score: 46.28  E-value: 6.10e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767956394 282 RVLLLGPVGSGKSLQAALLAQKYRLVNVCCGQLLKEAVADRTTFGELIQPFFEK 335
Cdd:PRK02496   3 RLIFLGPPGAGKGTQAVVLAEHLHIPHISTGDILRQAIKEQTPLGIKAQGYMDK 56
adk PRK00279
adenylate kinase; Reviewed
 282-330 9.97e-06

adenylate kinase; Reviewed


Pssm-ID: 234711 [Multi-domain]  Cd Length: 215  Bit Score: 45.91  E-value: 9.97e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 767956394 282 RVLLLGPVGSGKSLQAALLAQKYRLVNVCCGQLLKEAVADRTTFGELIQ 330
Cdd:PRK00279   2 RLILLGPPGAGKGTQAKFIAEKYGIPHISTGDMLRAAVKAGTELGKEAK 50
PLN02674 PLN02674
adenylate kinase
 255-326 2.43e-05

adenylate kinase


Pssm-ID: 178279 [Multi-domain]  Cd Length: 244  Bit Score: 45.26  E-value: 2.43e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767956394 255 DQPCVDVFYQALTYVQSNHRTNApftpRVLLLGPVGSGKSLQAALLAQKYRLVNVCCGQLLKEAVADRTTFG 326
Cdd:PLN02674  10 DVPSVDLMTELLRRMKCSSKPDK----RLILIGPPGSGKGTQSPIIKDEYCLCHLATGDMLRAAVAAKTPLG 77
PRK14529 PRK14529
adenylate kinase; Provisional
 71-192 3.20e-05

adenylate kinase; Provisional


Pssm-ID: 237746 [Multi-domain]  Cd Length: 223  Bit Score: 44.71  E-value: 3.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394  71 RIVILGPPASGKTTIAMWLCK-----HLNSSLLTLENLIL-NEFSYTATEarrlYLQR-KTVPSALLVQLIQERLAEEDc 143
Cdd:PRK14529   2 NILIFGPNGSGKGTQGALVKKkydlaHIESGAIFREHIGGgTELGKKAKE----YIDRgDLVPDDITIPMILETLKQDG- 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767956394 144 iKQGWILDGIPETREQALR----IQTLGITPRHVIVLSAPDTVLIERNLGKRI 192
Cdd:PRK14529  77 -KNGWLLDGFPRNKVQAEKlweaLQKEGMKLDYVIEILLPREVAKNRIMGRRL 128
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
 71-186 5.15e-05

Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic pathway which converts erythrose-4-phosphate to chorismic acid, found in bacteria, fungi and plants. Chorismic acid is a important intermediate in the synthesis of aromatic compounds, such as aromatic amino acids, p-aminobenzoic acid, folate and ubiquinone. Shikimate kinase catalyses the phosphorylation of the 3-hydroxyl group of shikimic acid using ATP.


Pssm-ID: 238260 [Multi-domain]  Cd Length: 154  Bit Score: 42.93  E-value: 5.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394  71 RIVILGPPASGKTTIAMWLCKHLNSSLLTLENLIlnefsytatEARrlylQRKTVPsallvQLIQE------RLAEEDCI 144
Cdd:cd00464    1 NIVLIGMMGAGKTTVGRLLAKALGLPFVDLDELI---------EQR----AGMSIP-----EIFAEegeegfRELEREVL 62

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 767956394 145 KQ-----GWIL---DGIPETREQALRIQTLGItprhVIVLSAPDTVLIER 186
Cdd:cd00464   63 LLlltkeNAVIatgGGAVLREENRRLLLENGI----VVWLDASPEELLER 108
PRK14532 PRK14532
adenylate kinase; Provisional
 72-195 9.85e-05

adenylate kinase; Provisional


Pssm-ID: 184729 [Multi-domain]  Cd Length: 188  Bit Score: 42.89  E-value: 9.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394  72 IVILGPPASGKTTIAMWLCKHLNSSLLTLENLILNEFSYTATEARRL--YLQR-KTVPSALLVQLIQERLAEEDCiKQGW 148
Cdd:PRK14532   3 LILFGPPAAGKGTQAKRLVEERGMVQLSTGDMLRAAIASGSELGQRVkgIMDRgELVSDEIVIALIEERLPEAEA-AGGA 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767956394 149 ILDGIPETREQA----LRIQTLGITPRHVIVLSAPDTVLIERnLGKRIDPQ 195
Cdd:PRK14532  82 IFDGFPRTVAQAealdKMLASRGQKIDVVIRLKVDDEALIER-IVKRFEEQ 131
PRK14528 PRK14528
adenylate kinase; Provisional
 282-326 1.02e-04

adenylate kinase; Provisional


Pssm-ID: 172994 [Multi-domain]  Cd Length: 186  Bit Score: 42.69  E-value: 1.02e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 767956394 282 RVLLLGPVGSGKSLQAALLAQKYRLVNVCCGQLLKEAVADRTTFG 326
Cdd:PRK14528   3 NIIFMGPPGAGKGTQAKILCERLSIPQISTGDILREAVKNQTAMG 47
DD_TEX55 cd22975
dimerization/docking (D/D) domain found in testis-specific expressed protein 55 (TEX55) and ...
 16-64 1.37e-04

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: 39.08  E-value: 1.37e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 767956394  16 QYGEENHIFELMQVLTtwvsalhpqnmlEQLLIHQPEDPIPFMIQHLHR 64
Cdd:cd22975    9 KYLEKHNILQLFQELT------------AGLVYERPDDPIQFMIDEIEK 45
UMP_CMP_kin_fam TIGR01359
UMP-CMP kinase family; This subfamily of the adenylate kinase superfamily contains examples of ...
 283-330 2.31e-04

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: 41.59  E-value: 2.31e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 767956394  283 VLLLGPVGSGKSLQAALLAQKYRLVNVCCGQLLKEAVADR-TTFGELIQ 330
Cdd:TIGR01359   2 VFVLGGPGSGKGTQCAKIVENFGFTHLSAGDLLRAEIKREgSENGSLIE 50
DD_CrRSP_unchar cd22964
dimerization/docking (D/D) domain of an uncharacterized subunit found in Chlamydomonas ...
 40-62 8.17e-04

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: 36.82  E-value: 8.17e-04
                         10        20
                 ....*....|....*....|...
gi 767956394  40 QNMLEQLLIHQPEDPIPFMIQHL 62
Cdd:cd22964   19 EQLVTDLLQEKPEDPVPFMIQWL 41
PLN02200 PLN02200
adenylate kinase family protein
 74-193 8.33e-04

adenylate kinase family protein


Pssm-ID: 215125 [Multi-domain]  Cd Length: 234  Bit Score: 40.65  E-value: 8.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394  74 ILGPPASGKTTIAMWLCKHLNSSLLTLENLILNEF-SYTATEARRLYLQR--KTVPSALLVQLIQERLAEEDCIKqgWIL 150
Cdd:PLN02200  48 VLGGPGSGKGTQCEKIVETFGFKHLSAGDLLRREIaSNSEHGAMILNTIKegKIVPSEVTVKLIQKEMESSDNNK--FLI 125

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 767956394 151 DGIPETREQALRI-QTLGITPRHVIVLSAPDTVLIERNLGK---RID 193
Cdd:PLN02200 126 DGFPRTEENRIAFeRIIGAEPNVVLFFDCPEEEMVKRVLNRnqgRVD 172
PRK14531 PRK14531
adenylate kinase; Provisional
 282-327 8.61e-04

adenylate kinase; Provisional


Pssm-ID: 172997 [Multi-domain]  Cd Length: 183  Bit Score: 39.79  E-value: 8.61e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 767956394 282 RVLLLGPVGSGKSLQAALLAQKYRLVNVCCGQLLKEAVADRTTFGE 327
Cdd:PRK14531   4 RLLFLGPPGAGKGTQAARLCAAHGLRHLSTGDLLRSEVAAGSALGQ 49
NadR3 COG3172
Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase ...
 67-95 8.64e-04

Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 442405 [Multi-domain]  Cd Length: 178  Bit Score: 39.80  E-value: 8.64e-04
                         10        20
                 ....*....|....*....|....*....
gi 767956394  67 DNVPRIVILGPPASGKTTIAMWLCKHLNS 95
Cdd:COG3172    6 SFVKKIVLLGAESTGKTTLARALAAHYNT 34
DD_TbAK-like cd22981
dimerization/docking (D/D) domain found in Trypanosoma brucei adenylate kinase (AK) and ...
 16-64 1.07e-03

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: 36.62  E-value: 1.07e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 767956394  16 QYGEENHIFELMQVLttwvsalhpqnmLEQLLIHQPEDPIPFMIQHLHR 64
Cdd:cd22981    7 KYLKEKNIPQLFEFL------------LRHLLLDKPENPLEYLHDLLER 43
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 62-130 1.55e-03

proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 38.80  E-value: 1.55e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767956394  62 LHRDNDNVPRIVIL-GPPASGKTTIAMWLCKHLNSSLL--TLENLILNEFSYTATEARRLY-LQRKTVPSALL 130
Cdd:cd19481   18 LRRYGLGLPKGILLyGPPGTGKTLLAKALAGELGLPLIvvKLSSLLSKYVGESEKNLRKIFeRARRLAPCILF 90
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
43-166 1.97e-03

Predicted NTPase, NACHT family domain [Signal transduction mechanisms];


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 40.17  E-value: 1.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394  43 LEQLLIHQPEDPIPFMIQHLHRDNDNVPRIVILGPPASGKTTIAMWLCKHLNSSLLTLENLI-----LNEFSYTATearr 117
Cdd:COG5635  154 LDDLYVPLNLLERIESLKRLELLEAKKKRLLILGEPGSGKTTLLRYLALELAERYLDAEDPIpilieLRDLAEEAS---- 229

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767956394 118 lylqrktvpsalLVQLIQERLAEEDCIKQGW------------ILDGIPETREQALRIQTL 166
Cdd:COG5635  230 ------------LEDLLAEALEKRGGEPEDAlerllrngrlllLLDGLDEVPDEADRDEVL 278
DD_AK5 cd22978
dimerization/docking (D/D) domain found in adenylate kinase isoenzyme 5 (AK5) and similar ...
 16-64 2.44e-03

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: 35.59  E-value: 2.44e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 767956394  16 QYGEENHIFELMQVLTTwvsalhpqnmleQLLIHQPEDPIPFMIQHLHR 64
Cdd:cd22978    6 DYLSRKEIPQLFESLMT------------GLMYNRPDDPIEFLEDCLEK 42
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
57-130 2.50e-03

Predicted ATPase, AAA+ superfamily [General function prediction only];


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 39.10  E-value: 2.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956394  57 FMIQHLHRDN----DNVPRIVIL--GPPASGKTTIAMWLCKHLNSSLLT--LENLI---LNEfsyTATEARRLYLQRKTV 125
Cdd:COG1223   17 IIKELRRRENlrkfGLWPPRKILfyGPPGTGKTMLAEALAGELKLPLLTvrLDSLIgsyLGE---TARNLRKLFDFARRA 93


                 ....*
gi 767956394 126 PSALL 130
Cdd:COG1223   94 PCVIF 98
Hydin_ADK pfam17213
Hydin Adenylate kinase-like domain; This domain found in the Hydin protein is homologous to ...
 72-109 2.64e-03

Hydin Adenylate kinase-like domain; This domain found in the Hydin protein is homologous to adenylate kinases.


Pssm-ID: 465383  Cd Length: 199  Bit Score: 38.58  E-value: 2.64e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 767956394   72 IVILGPPASGKTTIAMWLCKHLNSSLLTLENLILNEFS 109
Cdd:pfam17213   2 IIVHGAPLSGKTATAVTLAKHYGAACLTIDSIVLEAIS 39
aden_kin_iso1 TIGR01360
adenylate kinase, isozyme 1 subfamily; Members of this family are adenylate kinase, EC 2.7.4.3. ...
 281-335 3.34e-03

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: 38.26  E-value: 3.34e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767956394  281 PRVLLLGPVGSGKSLQAALLAQKYRLVNVCCGQLLKEAVADRTTFGELIQPFFEK 335
Cdd:TIGR01360   4 KIIFIVGGPGSGKGTQCEKIVEKYGFTHLSTGDLLRAEVASGSERGKQLQAIMES 58
AAA_17 pfam13207
AAA domain;
286-323 3.86e-03

AAA domain;


Pssm-ID: 463810 [Multi-domain]  Cd Length: 136  Bit Score: 37.22  E-value: 3.86e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 767956394  286 LGPVGSGKSLQAALLAQKYRLVNVCCGQLLKEAVADRT 323
Cdd:pfam13207   1 TGVPGSGKTTQLKKLAEKLGFPHISAGDLLREEAKERG 38
 
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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