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Conserved domains on  [gi|1958762442|ref|XP_038961149|]
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adenylate kinase 8 isoform X2 [Rattus norvegicus]

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 ...
 270-369 2.38e-34

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: 125.81  E-value: 2.38e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442 270 KVLLCGPMGCGKKLQAALLSQKYGLVNISCGQLLKEAMAAESSLGDLIEPFFEKRMTVPDSIITRVLTERLKQQDCiQKG 349
Cdd:cd01428     1 RILLLGPPGSGKGTQAERLAKKYGLPHISTGDLLREEIASGTELGKKAKEYIDSGKLVPDEIVIKLLKERLKKPDC-KKG 79

                          90       100
                  ....*....|....*....|
gi 1958762442 350 WVLHGFPRDLDQARLLNSMG 369
Cdd:cd01428    80 FILDGFPRTVDQAEALDELL 99
ADK cd01428
Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine ...
 59-249 2.70e-33

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: 123.12  E-value: 2.70e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442  59 RVVILGPPASGKTTIAMWLCKHLNSNLITKENLLEREFSL---LSLEAKKHYQVYKRVPNSTLVSLVQERLNEDDClRRG 135
Cdd:cd01428     1 RILLLGPPGSGKGTQAERLAKKYGLPHISTGDLLREEIASgteLGKKAKEYIDSGKLVPDEIVIKLLKERLKKPDC-KKG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442 136 WILDGIPERREQALMIQTL---GLAPKHVIVLSAPDSVLIERNVGKRIDPVTGEIYHTTFDWPPELEIQNRLIQpegisE 212
Cdd:cd01428    80 FILDGFPRTVDQAEALDELldeGIKPDKVIELDVPDEVLIERILGRRICPVSGRVYHLGKDDVTGEPLSQRSDD-----N 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1958762442 213 IDTAKKLLE-YHRHIIRILPSYPK--ILKTISSDQPCVDV 249
Cdd:cd01428   155 EETIKKRLEvYKEQTAPLIDYYKKkgKLVEIDGSGDIDEV 194
DD_AK8 cd22979
dimerization/docking (D/D) domain found in adenylate kinase isoenzyme 8 (AK8) and similar ...
 9-52 9.05e-18

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: 76.35  E-value: 9.05e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1958762442   9 RIPPEMPQYGEDYHIFEMMQSMLEQLLIHQPEDPISFMISHLRR 52
Cdd:cd22979     1 EIPPEFAAYAEKHRIFELFQDLLKQLLIHKPEDPLQFLIDYLQK 44
 
Name Accession Description Interval E-value
ADK cd01428
Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine ...
 270-369 2.38e-34

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: 125.81  E-value: 2.38e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442 270 KVLLCGPMGCGKKLQAALLSQKYGLVNISCGQLLKEAMAAESSLGDLIEPFFEKRMTVPDSIITRVLTERLKQQDCiQKG 349
Cdd:cd01428     1 RILLLGPPGSGKGTQAERLAKKYGLPHISTGDLLREEIASGTELGKKAKEYIDSGKLVPDEIVIKLLKERLKKPDC-KKG 79

                          90       100
                  ....*....|....*....|
gi 1958762442 350 WVLHGFPRDLDQARLLNSMG 369
Cdd:cd01428    80 FILDGFPRTVDQAEALDELL 99
ADK cd01428
Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine ...
 59-249 2.70e-33

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: 123.12  E-value: 2.70e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442  59 RVVILGPPASGKTTIAMWLCKHLNSNLITKENLLEREFSL---LSLEAKKHYQVYKRVPNSTLVSLVQERLNEDDClRRG 135
Cdd:cd01428     1 RILLLGPPGSGKGTQAERLAKKYGLPHISTGDLLREEIASgteLGKKAKEYIDSGKLVPDEIVIKLLKERLKKPDC-KKG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442 136 WILDGIPERREQALMIQTL---GLAPKHVIVLSAPDSVLIERNVGKRIDPVTGEIYHTTFDWPPELEIQNRLIQpegisE 212
Cdd:cd01428    80 FILDGFPRTVDQAEALDELldeGIKPDKVIELDVPDEVLIERILGRRICPVSGRVYHLGKDDVTGEPLSQRSDD-----N 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1958762442 213 IDTAKKLLE-YHRHIIRILPSYPK--ILKTISSDQPCVDV 249
Cdd:cd01428   155 EETIKKRLEvYKEQTAPLIDYYKKkgKLVEIDGSGDIDEV 194
PLN02842 PLN02842
nucleotide kinase
 61-250 1.27e-30

nucleotide kinase


Pssm-ID: 178435 [Multi-domain]  Cd Length: 505  Bit Score: 122.66  E-value: 1.27e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442  61 VILGPPASGKTTIAMWLCKHLNSNLITKENLLEREFSL---LSLEAKKHYQVYKRVPNSTLVSLVQERLNEDDCLRRGWI 137
Cdd:PLN02842    1 MISGAPASGKGTQCELIVHKFGLVHISTGDLLRAEVSAgtdIGKRAKEFMNSGRLVPDEIVIAMVTGRLSREDAKEKGWL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442 138 LDGIPERREQALMIQTLGLAPKHVIVLSAPDSVLIERNVGKRIDPVTGEIYHTTFdWPPEL-EIQNRLIQPEGISEIDTA 216
Cdd:PLN02842   81 LDGYPRSFAQAQSLEKLKIRPDIFILLDVPDEILIDRCVGRRLDPVTGKIYHIKN-FPPESeEIKARLITRPDDTEEKVK 159

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1958762442 217 KKLLEYHRHIIRILPSYPKILKTISSDQPCVDVF 250
Cdd:PLN02842  160 ARLQIYKKNAEAILSTYSDIMVKIDGNRPKEVVF 193
adk TIGR01351
adenylate kinase; Adenylate kinase (EC 2.7.4.3) converts ATP + AMP to ADP + ADP, that is, uses ...
 59-258 1.76e-28

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: 110.79  E-value: 1.76e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442  59 RVVILGPPASGKTTIAMWLCKHLNSNLITKENLLEREFSL---LSLEAKKHYQVYKRVPNSTLVSLVQERLNEDDCLRRG 135
Cdd:TIGR01351   1 RLVLLGPPGSGKGTQAKRIAEKYGLPHISTGDLLRAEIKAgtpLGKKAKEYMEKGELVPDEIVNQLVKERLTQNDDNENG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442 136 WILDGIPERREQALMI-QTLGLAPKHVIVLSAPDSVLIERNVGKRIDPVTGEIYHTTFDWPPELEIQNRLIQPEGISEID 214
Cdd:TIGR01351  81 FILDGFPRTLSQAEALdALLEEPIDAVIELDVPDEELVERLSGRRICPSCGRVYHLKFNPPKVPGCDDCTGELLVQREDD 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958762442 215 TA----KKLLEYHRHIIRILPSYPK--ILKTISSDQPCVDVFYQALTYVQ 258
Cdd:TIGR01351 161 TEevvkKRLEVYKEQTEPLIDYYKKrgILVQIDGNGPIDEVWKRILEALK 210
Adk COG0563
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ...
 59-250 8.25e-27

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: 105.98  E-value: 8.25e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442  59 RVVILGPPASGKTTIAMWLCKHLNSNLITKENLLEREFSL---LSLEAKKhyqVYKR---VPNSTLVSLVQERLNEDDCl 132
Cdd:COG0563     2 RIILLGPPGAGKGTQAKRLAEKYGIPHISTGDMLRAAVKAgteLGKKAKE---YMDAgelVPDEIVIGLVKERLAQPDC- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442 133 RRGWILDGIPERREQAL----MIQTLGLAPKHVIVLSAPDSVLIERNVGKRIDPVTGEIYHTTFDWPPELEI----QNRL 204
Cdd:COG0563    78 ANGFILDGFPRTVAQAEaldeLLAELGIKLDAVIELDVDDEELVERLSGRRVCPNCGATYHVKFNPPKVEGVcdkcGGEL 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958762442 205 IQ-----PEGIseidtAKKLLEYHRHIIRILPSYPK--ILKTISSDQPCVDVF 250
Cdd:COG0563   158 VQraddnEETV-----RKRLEVYHEQTAPLIDYYRKkgKLVEIDGEGSIEEVT 205
adk TIGR01351
adenylate kinase; Adenylate kinase (EC 2.7.4.3) converts ATP + AMP to ADP + ADP, that is, uses ...
 270-373 5.77e-26

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: 103.85  E-value: 5.77e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442 270 KVLLCGPMGCGKKLQAALLSQKYGLVNISCGQLLKEAMAAESSLGDLIEPFFEKRMTVPDSIITRVLTERLKQQDCIQKG 349
Cdd:TIGR01351   1 RLVLLGPPGSGKGTQAKRIAEKYGLPHISTGDLLRAEIKAGTPLGKKAKEYMEKGELVPDEIVNQLVKERLTQNDDNENG 80

                          90       100
                  ....*....|....*....|....
gi 1958762442 350 WVLHGFPRDLDQARLLNSMGYSPN 373
Cdd:TIGR01351  81 FILDGFPRTLSQAEALDALLEEPI 104
Adk COG0563
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ...
 270-368 4.84e-24

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: 98.66  E-value: 4.84e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442 270 KVLLCGPMGCGKKLQAALLSQKYGLVNISCGQLLKEAMAAESSLGDLIEPFFEKRMTVPDSIITRVLTERLKQQDCiQKG 349
Cdd:COG0563     2 RIILLGPPGAGKGTQAKRLAEKYGIPHISTGDMLRAAVKAGTELGKKAKEYMDAGELVPDEIVIGLVKERLAQPDC-ANG 80

                          90
                  ....*....|....*....
gi 1958762442 350 WVLHGFPRDLDQARLLNSM 368
Cdd:COG0563    81 FILDGFPRTVAQAEALDEL 99
ADK pfam00406
Adenylate kinase;
273-368 1.02e-23

Adenylate kinase;


Pssm-ID: 395329 [Multi-domain]  Cd Length: 184  Bit Score: 96.99  E-value: 1.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442 273 LCGPMGCGKKLQAALLSQKYGLVNISCGQLLKEAMAAESSLGDLIEPFFEKRMTVPDSIITRVLTERLKQQDCiQKGWVL 352
Cdd:pfam00406   1 LLGPPGAGKGTQAEKIVQKYGLPHLSTGDLLRAEIKSGTELGKEAKEYMDKGELVPDEVVVGLVKERLEQNDC-KNGFLL 79

                          90
                  ....*....|....*.
gi 1958762442 353 HGFPRDLDQARLLNSM 368
Cdd:pfam00406  80 DGFPRTVPQAEALEEL 95
ADK pfam00406
Adenylate kinase;
62-223 2.52e-22

Adenylate kinase;


Pssm-ID: 395329 [Multi-domain]  Cd Length: 184  Bit Score: 93.14  E-value: 2.52e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442  62 ILGPPASGKTTIAMWLCKHLNSNLITKENLLEREFSL---LSLEAKKHYQVYKRVPNSTLVSLVQERLNEDDClRRGWIL 138
Cdd:pfam00406   1 LLGPPGAGKGTQAEKIVQKYGLPHLSTGDLLRAEIKSgteLGKEAKEYMDKGELVPDEVVVGLVKERLEQNDC-KNGFLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442 139 DGIPERREQALMIQTL---GLAPKHVIVLSAPDSVLIERNVGKRIDPVTGEIYHTTFDwPPELEIQN-----RLIQPEGI 210
Cdd:pfam00406  80 DGFPRTVPQAEALEELlerGIKLDYVIEFDVPDEVLVERLTGRRIHPNSGRSYHLEFN-PPKVPGKDdvtgePLVQRSDD 158

                         170
                  ....*....|...
gi 1958762442 211 SEIDTAKKLLEYH 223
Cdd:pfam00406 159 NEETVKKRLETYH 171
adk PRK00279
adenylate kinase; Reviewed
 270-368 5.02e-21

adenylate kinase; Reviewed


Pssm-ID: 234711 [Multi-domain]  Cd Length: 215  Bit Score: 90.21  E-value: 5.02e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442 270 KVLLCGPMGCGKKLQAALLSQKYGLVNISCGQLLKEAMAAESSLGDLIEPFFEKRMTVPDSIITRVLTERLKQQDCiQKG 349
Cdd:PRK00279    2 RLILLGPPGAGKGTQAKFIAEKYGIPHISTGDMLRAAVKAGTELGKEAKSYMDAGELVPDEIVIGLVKERLAQPDC-KNG 80

                          90
                  ....*....|....*....
gi 1958762442 350 WVLHGFPRDLDQARLLNSM 368
Cdd:PRK00279   81 FLLDGFPRTIPQAEALDEM 99
DD_AK8 cd22979
dimerization/docking (D/D) domain found in adenylate kinase isoenzyme 8 (AK8) and similar ...
 9-52 9.05e-18

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: 76.35  E-value: 9.05e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1958762442   9 RIPPEMPQYGEDYHIFEMMQSMLEQLLIHQPEDPISFMISHLRR 52
Cdd:cd22979     1 EIPPEFAAYAEKHRIFELFQDLLKQLLIHKPEDPLQFLIDYLQK 44
DUF5582 pfam17819
Family of unknown function (DUF5582); This is a family of unknown function found in chordata.
 9-48 8.13e-04

Family of unknown function (DUF5582); This is a family of unknown function found in chordata.


Pssm-ID: 465519  Cd Length: 146  Bit Score: 39.42  E-value: 8.13e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1958762442   9 RIPP---EMP-----QYGEDYHIFEMMQSMLEQLLIHQPEDPISFMIS 48
Cdd:pfam17819  97 RFPPivyEDPyqvslRYMEKHHILQIFQQITENLVYEKPEDPLHFMLC 144
 
Name Accession Description Interval E-value
ADK cd01428
Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine ...
 270-369 2.38e-34

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: 125.81  E-value: 2.38e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442 270 KVLLCGPMGCGKKLQAALLSQKYGLVNISCGQLLKEAMAAESSLGDLIEPFFEKRMTVPDSIITRVLTERLKQQDCiQKG 349
Cdd:cd01428     1 RILLLGPPGSGKGTQAERLAKKYGLPHISTGDLLREEIASGTELGKKAKEYIDSGKLVPDEIVIKLLKERLKKPDC-KKG 79

                          90       100
                  ....*....|....*....|
gi 1958762442 350 WVLHGFPRDLDQARLLNSMG 369
Cdd:cd01428    80 FILDGFPRTVDQAEALDELL 99
ADK cd01428
Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine ...
 59-249 2.70e-33

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: 123.12  E-value: 2.70e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442  59 RVVILGPPASGKTTIAMWLCKHLNSNLITKENLLEREFSL---LSLEAKKHYQVYKRVPNSTLVSLVQERLNEDDClRRG 135
Cdd:cd01428     1 RILLLGPPGSGKGTQAERLAKKYGLPHISTGDLLREEIASgteLGKKAKEYIDSGKLVPDEIVIKLLKERLKKPDC-KKG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442 136 WILDGIPERREQALMIQTL---GLAPKHVIVLSAPDSVLIERNVGKRIDPVTGEIYHTTFDWPPELEIQNRLIQpegisE 212
Cdd:cd01428    80 FILDGFPRTVDQAEALDELldeGIKPDKVIELDVPDEVLIERILGRRICPVSGRVYHLGKDDVTGEPLSQRSDD-----N 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1958762442 213 IDTAKKLLE-YHRHIIRILPSYPK--ILKTISSDQPCVDV 249
Cdd:cd01428   155 EETIKKRLEvYKEQTAPLIDYYKKkgKLVEIDGSGDIDEV 194
PLN02842 PLN02842
nucleotide kinase
 61-250 1.27e-30

nucleotide kinase


Pssm-ID: 178435 [Multi-domain]  Cd Length: 505  Bit Score: 122.66  E-value: 1.27e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442  61 VILGPPASGKTTIAMWLCKHLNSNLITKENLLEREFSL---LSLEAKKHYQVYKRVPNSTLVSLVQERLNEDDCLRRGWI 137
Cdd:PLN02842    1 MISGAPASGKGTQCELIVHKFGLVHISTGDLLRAEVSAgtdIGKRAKEFMNSGRLVPDEIVIAMVTGRLSREDAKEKGWL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442 138 LDGIPERREQALMIQTLGLAPKHVIVLSAPDSVLIERNVGKRIDPVTGEIYHTTFdWPPEL-EIQNRLIQPEGISEIDTA 216
Cdd:PLN02842   81 LDGYPRSFAQAQSLEKLKIRPDIFILLDVPDEILIDRCVGRRLDPVTGKIYHIKN-FPPESeEIKARLITRPDDTEEKVK 159

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1958762442 217 KKLLEYHRHIIRILPSYPKILKTISSDQPCVDVF 250
Cdd:PLN02842  160 ARLQIYKKNAEAILSTYSDIMVKIDGNRPKEVVF 193
adk TIGR01351
adenylate kinase; Adenylate kinase (EC 2.7.4.3) converts ATP + AMP to ADP + ADP, that is, uses ...
 59-258 1.76e-28

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: 110.79  E-value: 1.76e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442  59 RVVILGPPASGKTTIAMWLCKHLNSNLITKENLLEREFSL---LSLEAKKHYQVYKRVPNSTLVSLVQERLNEDDCLRRG 135
Cdd:TIGR01351   1 RLVLLGPPGSGKGTQAKRIAEKYGLPHISTGDLLRAEIKAgtpLGKKAKEYMEKGELVPDEIVNQLVKERLTQNDDNENG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442 136 WILDGIPERREQALMI-QTLGLAPKHVIVLSAPDSVLIERNVGKRIDPVTGEIYHTTFDWPPELEIQNRLIQPEGISEID 214
Cdd:TIGR01351  81 FILDGFPRTLSQAEALdALLEEPIDAVIELDVPDEELVERLSGRRICPSCGRVYHLKFNPPKVPGCDDCTGELLVQREDD 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958762442 215 TA----KKLLEYHRHIIRILPSYPK--ILKTISSDQPCVDVFYQALTYVQ 258
Cdd:TIGR01351 161 TEevvkKRLEVYKEQTEPLIDYYKKrgILVQIDGNGPIDEVWKRILEALK 210
Adk COG0563
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ...
 59-250 8.25e-27

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: 105.98  E-value: 8.25e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442  59 RVVILGPPASGKTTIAMWLCKHLNSNLITKENLLEREFSL---LSLEAKKhyqVYKR---VPNSTLVSLVQERLNEDDCl 132
Cdd:COG0563     2 RIILLGPPGAGKGTQAKRLAEKYGIPHISTGDMLRAAVKAgteLGKKAKE---YMDAgelVPDEIVIGLVKERLAQPDC- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442 133 RRGWILDGIPERREQAL----MIQTLGLAPKHVIVLSAPDSVLIERNVGKRIDPVTGEIYHTTFDWPPELEI----QNRL 204
Cdd:COG0563    78 ANGFILDGFPRTVAQAEaldeLLAELGIKLDAVIELDVDDEELVERLSGRRVCPNCGATYHVKFNPPKVEGVcdkcGGEL 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958762442 205 IQ-----PEGIseidtAKKLLEYHRHIIRILPSYPK--ILKTISSDQPCVDVF 250
Cdd:COG0563   158 VQraddnEETV-----RKRLEVYHEQTAPLIDYYRKkgKLVEIDGEGSIEEVT 205
adk TIGR01351
adenylate kinase; Adenylate kinase (EC 2.7.4.3) converts ATP + AMP to ADP + ADP, that is, uses ...
 270-373 5.77e-26

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: 103.85  E-value: 5.77e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442 270 KVLLCGPMGCGKKLQAALLSQKYGLVNISCGQLLKEAMAAESSLGDLIEPFFEKRMTVPDSIITRVLTERLKQQDCIQKG 349
Cdd:TIGR01351   1 RLVLLGPPGSGKGTQAKRIAEKYGLPHISTGDLLRAEIKAGTPLGKKAKEYMEKGELVPDEIVNQLVKERLTQNDDNENG 80

                          90       100
                  ....*....|....*....|....
gi 1958762442 350 WVLHGFPRDLDQARLLNSMGYSPN 373
Cdd:TIGR01351  81 FILDGFPRTLSQAEALDALLEEPI 104
Adk COG0563
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ...
 270-368 4.84e-24

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: 98.66  E-value: 4.84e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442 270 KVLLCGPMGCGKKLQAALLSQKYGLVNISCGQLLKEAMAAESSLGDLIEPFFEKRMTVPDSIITRVLTERLKQQDCiQKG 349
Cdd:COG0563     2 RIILLGPPGAGKGTQAKRLAEKYGIPHISTGDMLRAAVKAGTELGKKAKEYMDAGELVPDEIVIGLVKERLAQPDC-ANG 80

                          90
                  ....*....|....*....
gi 1958762442 350 WVLHGFPRDLDQARLLNSM 368
Cdd:COG0563    81 FILDGFPRTVAQAEALDEL 99
ADK pfam00406
Adenylate kinase;
273-368 1.02e-23

Adenylate kinase;


Pssm-ID: 395329 [Multi-domain]  Cd Length: 184  Bit Score: 96.99  E-value: 1.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442 273 LCGPMGCGKKLQAALLSQKYGLVNISCGQLLKEAMAAESSLGDLIEPFFEKRMTVPDSIITRVLTERLKQQDCiQKGWVL 352
Cdd:pfam00406   1 LLGPPGAGKGTQAEKIVQKYGLPHLSTGDLLRAEIKSGTELGKEAKEYMDKGELVPDEVVVGLVKERLEQNDC-KNGFLL 79

                          90
                  ....*....|....*.
gi 1958762442 353 HGFPRDLDQARLLNSM 368
Cdd:pfam00406  80 DGFPRTVPQAEALEEL 95
ADK pfam00406
Adenylate kinase;
62-223 2.52e-22

Adenylate kinase;


Pssm-ID: 395329 [Multi-domain]  Cd Length: 184  Bit Score: 93.14  E-value: 2.52e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442  62 ILGPPASGKTTIAMWLCKHLNSNLITKENLLEREFSL---LSLEAKKHYQVYKRVPNSTLVSLVQERLNEDDClRRGWIL 138
Cdd:pfam00406   1 LLGPPGAGKGTQAEKIVQKYGLPHLSTGDLLRAEIKSgteLGKEAKEYMDKGELVPDEVVVGLVKERLEQNDC-KNGFLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442 139 DGIPERREQALMIQTL---GLAPKHVIVLSAPDSVLIERNVGKRIDPVTGEIYHTTFDwPPELEIQN-----RLIQPEGI 210
Cdd:pfam00406  80 DGFPRTVPQAEALEELlerGIKLDYVIEFDVPDEVLVERLTGRRIHPNSGRSYHLEFN-PPKVPGKDdvtgePLVQRSDD 158

                         170
                  ....*....|...
gi 1958762442 211 SEIDTAKKLLEYH 223
Cdd:pfam00406 159 NEETVKKRLETYH 171
adk PRK00279
adenylate kinase; Reviewed
 59-250 8.99e-22

adenylate kinase; Reviewed


Pssm-ID: 234711 [Multi-domain]  Cd Length: 215  Bit Score: 92.52  E-value: 8.99e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442  59 RVVILGPPASGKTTIAMWLCKHLNSNLITKENLLEREFSL---LSLEAKKhyqvY----KRVPNSTLVSLVQERLNEDDC 131
Cdd:PRK00279    2 RLILLGPPGAGKGTQAKFIAEKYGIPHISTGDMLRAAVKAgteLGKEAKS----YmdagELVPDEIVIGLVKERLAQPDC 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442 132 lRRGWILDGIPERREQAL----MIQTLGLAPKHVIVLSAPDSVLIERNVGKRIDPVTGEIYHTTFDwPPELE-----IQN 202
Cdd:PRK00279   78 -KNGFLLDGFPRTIPQAEaldeMLKELGIKLDAVIEIDVPDEELVERLSGRRICPACGRTYHVKFN-PPKVEgkcdvCGE 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958762442 203 RLIQ-----PEGIseidtAKKLLEYHRHIIRILPSYPK--ILKTISSDQPCVDVF 250
Cdd:PRK00279  156 ELIQraddnEETV-----RKRLEVYHKQTAPLIDYYKKkgKLKKIDGTGSIDEVF 205
adk PRK00279
adenylate kinase; Reviewed
 270-368 5.02e-21

adenylate kinase; Reviewed


Pssm-ID: 234711 [Multi-domain]  Cd Length: 215  Bit Score: 90.21  E-value: 5.02e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442 270 KVLLCGPMGCGKKLQAALLSQKYGLVNISCGQLLKEAMAAESSLGDLIEPFFEKRMTVPDSIITRVLTERLKQQDCiQKG 349
Cdd:PRK00279    2 RLILLGPPGAGKGTQAKFIAEKYGIPHISTGDMLRAAVKAGTELGKEAKSYMDAGELVPDEIVIGLVKERLAQPDC-KNG 80

                          90
                  ....*....|....*....
gi 1958762442 350 WVLHGFPRDLDQARLLNSM 368
Cdd:PRK00279   81 FLLDGFPRTIPQAEALDEM 99
adk PRK02496
adenylate kinase; Provisional
 59-174 1.52e-18

adenylate kinase; Provisional


Pssm-ID: 179433 [Multi-domain]  Cd Length: 184  Bit Score: 82.49  E-value: 1.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442  59 RVVILGPPASGKTTIAMWLCKHLNSNLITKENLLE---REFSLLSLEAKKHYQVYKRVPNSTLVSLVQERLNEDDClRRG 135
Cdd:PRK02496    3 RLIFLGPPGAGKGTQAVVLAEHLHIPHISTGDILRqaiKEQTPLGIKAQGYMDKGELVPDQLVLDLVQERLQQPDA-ANG 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1958762442 136 WILDGIPERREQA----LMIQTLGLAPKHVIVLSAPDSVLIER 174
Cdd:PRK02496   82 WILDGFPRKVTQAafldELLQEIGQSGERVVNLDVPDDVVVER 124
adk PRK02496
adenylate kinase; Provisional
 270-376 1.98e-18

adenylate kinase; Provisional


Pssm-ID: 179433 [Multi-domain]  Cd Length: 184  Bit Score: 82.49  E-value: 1.98e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442 270 KVLLCGPMGCGKKLQAALLSQKYGLVNISCGQLLKEAMAAESSLGDLIEPFFEKRMTVPDSIITRVLTERLKQQDCiQKG 349
Cdd:PRK02496    3 RLIFLGPPGAGKGTQAVVLAEHLHIPHISTGDILRQAIKEQTPLGIKAQGYMDKGELVPDQLVLDLVQERLQQPDA-ANG 81

                          90       100
                  ....*....|....*....|....*..
gi 1958762442 350 WVLHGFPRDLDQARLLNSMGYSPNRSG 376
Cdd:PRK02496   82 WILDGFPRKVTQAAFLDELLQEIGQSG 108
DD_AK8 cd22979
dimerization/docking (D/D) domain found in adenylate kinase isoenzyme 8 (AK8) and similar ...
 9-52 9.05e-18

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: 76.35  E-value: 9.05e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1958762442   9 RIPPEMPQYGEDYHIFEMMQSMLEQLLIHQPEDPISFMISHLRR 52
Cdd:cd22979     1 EIPPEFAAYAEKHRIFELFQDLLKQLLIHKPEDPLQFLIDYLQK 44
PLN02842 PLN02842
nucleotide kinase
 272-373 2.02e-17

nucleotide kinase


Pssm-ID: 178435 [Multi-domain]  Cd Length: 505  Bit Score: 83.76  E-value: 2.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442 272 LLCGPMGCGKKLQAALLSQKYGLVNISCGQLLKEAMAAESSLGDLIEPFFEKRMTVPDSIITRVLTERLKQQDCIQKGWV 351
Cdd:PLN02842    1 MISGAPASGKGTQCELIVHKFGLVHISTGDLLRAEVSAGTDIGKRAKEFMNSGRLVPDEIVIAMVTGRLSREDAKEKGWL 80

                          90       100
                  ....*....|....*....|..
gi 1958762442 352 LHGFPRDLDQARLLNSMGYSPN 373
Cdd:PLN02842   81 LDGYPRSFAQAQSLEKLKIRPD 102
PRK14528 PRK14528
adenylate kinase; Provisional
 59-180 5.29e-16

adenylate kinase; Provisional


Pssm-ID: 172994 [Multi-domain]  Cd Length: 186  Bit Score: 75.43  E-value: 5.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442  59 RVVILGPPASGKTTIAMWLCKHLNSNLITKENLLE---REFSLLSLEAKKHYQVYKRVPNSTLVSLVQERLNEDDClRRG 135
Cdd:PRK14528    3 NIIFMGPPGAGKGTQAKILCERLSIPQISTGDILReavKNQTAMGIEAKRYMDAGDLVPDSVVIGIIKDRIREADC-KNG 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1958762442 136 WILDGIPERREQA----LMIQTLGLAPKHVIVLSAPDSVLIERNVGKRI 180
Cdd:PRK14528   82 FLLDGFPRTVEQAdaldALLKNEGKSIDKAINLEVPDGELLKRLLGRAE 130
PLN02674 PLN02674
adenylate kinase
 243-368 1.37e-15

adenylate kinase


Pssm-ID: 178279 [Multi-domain]  Cd Length: 244  Bit Score: 75.69  E-value: 1.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442 243 DQPCVDVFYQALTYVQsghrCNAPFTPKVLLCGPMGCGKKLQAALLSQKYGLVNISCGQLLKEAMAAESSLGDLIEPFFE 322
Cdd:PLN02674   10 DVPSVDLMTELLRRMK----CSSKPDKRLILIGPPGSGKGTQSPIIKDEYCLCHLATGDMLRAAVAAKTPLGIKAKEAMD 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1958762442 323 KRMTVPDSIITRVLTERLKQQDCiQKGWVLHGFPRDLDQARLLNSM 368
Cdd:PLN02674   86 KGELVSDDLVVGIIDEAMKKPSC-QKGFILDGFPRTVVQAQKLDEM 130
PRK14528 PRK14528
adenylate kinase; Provisional
 270-368 2.81e-15

adenylate kinase; Provisional


Pssm-ID: 172994 [Multi-domain]  Cd Length: 186  Bit Score: 73.51  E-value: 2.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442 270 KVLLCGPMGCGKKLQAALLSQKYGLVNISCGQLLKEAMAAESSLGDLIEPFFEKRMTVPDSIITRVLTERLKQQDCiQKG 349
Cdd:PRK14528    3 NIIFMGPPGAGKGTQAKILCERLSIPQISTGDILREAVKNQTAMGIEAKRYMDAGDLVPDSVVIGIIKDRIREADC-KNG 81

                          90
                  ....*....|....*....
gi 1958762442 350 WVLHGFPRDLDQARLLNSM 368
Cdd:PRK14528   82 FLLDGFPRTVEQADALDAL 100
PRK13808 PRK13808
adenylate kinase; Provisional
 270-368 1.03e-14

adenylate kinase; Provisional


Pssm-ID: 172341 [Multi-domain]  Cd Length: 333  Bit Score: 74.54  E-value: 1.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442 270 KVLLCGPMGCGKKLQAALLSQKYGLVNISCGQLLKEAMAAESSLGDLIEPFFEKRMTVPDSIITRVLTERLKQQDCIQkG 349
Cdd:PRK13808    2 RLILLGPPGAGKGTQAQRLVQQYGIVQLSTGDMLRAAVAAGTPVGLKAKDIMASGGLVPDEVVVGIISDRIEQPDAAN-G 80

                          90
                  ....*....|....*....
gi 1958762442 350 WVLHGFPRDLDQARLLNSM 368
Cdd:PRK13808   81 FILDGFPRTVPQAEALDAL 99
PRK14529 PRK14529
adenylate kinase; Provisional
 271-365 2.37e-14

adenylate kinase; Provisional


Pssm-ID: 237746 [Multi-domain]  Cd Length: 223  Bit Score: 71.67  E-value: 2.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442 271 VLLCGPMGCGKKLQAALLSQKYGLVNISCGQLLKEAMAAESSLGDLIEPFFEKRMTVPDSIITRVLTERLKQQDciQKGW 350
Cdd:PRK14529    3 ILIFGPNGSGKGTQGALVKKKYDLAHIESGAIFREHIGGGTELGKKAKEYIDRGDLVPDDITIPMILETLKQDG--KNGW 80

                          90
                  ....*....|....*
gi 1958762442 351 VLHGFPRDLDQARLL 365
Cdd:PRK14529   81 LLDGFPRNKVQAEKL 95
PTZ00088 PTZ00088
adenylate kinase 1; Provisional
 270-368 4.61e-14

adenylate kinase 1; Provisional


Pssm-ID: 240262 [Multi-domain]  Cd Length: 229  Bit Score: 70.98  E-value: 4.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442 270 KVLLCGPMGCGKKLQAALLSQKYGLVNISCGQLLKEAMAAESSLGDLIEPFFEKRMTVPDSIITRVLTERLKQ-QDCIQK 348
Cdd:PTZ00088    8 KIVLFGAPGVGKGTFAEILSKKENLKHINMGNILREEIKAKTTIGKEIQKVVTSGNLVPDNLVIAIVKDEIAKvTDDCFK 87

                          90       100
                  ....*....|....*....|
gi 1958762442 349 GWVLHGFPRDLDQARLLNSM 368
Cdd:PTZ00088   88 GFILDGFPRNLKQCKELGKI 107
PRK14530 PRK14530
adenylate kinase; Provisional
 58-221 3.05e-13

adenylate kinase; Provisional


Pssm-ID: 237747 [Multi-domain]  Cd Length: 215  Bit Score: 68.28  E-value: 3.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442  58 PRVVILGPPASGKTTIAMWLCKHLNSNLITKENLL----EREFSLLSLE---AKKHYQVYKRVPNSTLVSLVQERLNEDD 130
Cdd:PRK14530    4 PRILLLGAPGAGKGTQSSNLAEEFGVEHVTTGDALrankQMDISDMDTEydtPGEYMDAGELVPDAVVNEIVEEALSDAD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442 131 clrrGWILDGIPERREQALMIQTLgLAPKHVIVLSAPDSVLIERNVGKRIDPVTGEIYHTTFDWPPELEIQN----RLIQ 206
Cdd:PRK14530   84 ----GFVLDGYPRNLEQAEYLESI-TDLDVVLYLDVSEEELVDRLTGRRVCPDCGANYHVEFNQPEEEGVCDecggELIQ 158

                         170
                  ....*....|....*
gi 1958762442 207 PEGISEiDTAKKLLE 221
Cdd:PRK14530  159 RDDDTE-ETVRERLD 172
PRK14531 PRK14531
adenylate kinase; Provisional
 270-368 1.04e-12

adenylate kinase; Provisional


Pssm-ID: 172997 [Multi-domain]  Cd Length: 183  Bit Score: 65.99  E-value: 1.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442 270 KVLLCGPMGCGKKLQAALLSQKYGLVNISCGQLLKEAMAAESSLGDLIEPFFEKRMTVPDSIITRVLTERLKQQDciQKG 349
Cdd:PRK14531    4 RLLFLGPPGAGKGTQAARLCAAHGLRHLSTGDLLRSEVAAGSALGQEAEAVMNRGELVSDALVLAIVESQLKALN--SGG 81

                          90
                  ....*....|....*....
gi 1958762442 350 WVLHGFPRDLDQARLLNSM 368
Cdd:PRK14531   82 WLLDGFPRTVAQAEALEPL 100
PRK14532 PRK14532
adenylate kinase; Provisional
 271-368 1.55e-12

adenylate kinase; Provisional


Pssm-ID: 184729 [Multi-domain]  Cd Length: 188  Bit Score: 65.61  E-value: 1.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442 271 VLLCGPMGCGKKLQAALLSQKYGLVNISCGQLLKEAMAAESSLGDLIEPFFEKRMTVPDSIITRVLTERLKQQDCiQKGW 350
Cdd:PRK14532    3 LILFGPPAAGKGTQAKRLVEERGMVQLSTGDMLRAAIASGSELGQRVKGIMDRGELVSDEIVIALIEERLPEAEA-AGGA 81

                          90
                  ....*....|....*...
gi 1958762442 351 VLHGFPRDLDQARLLNSM 368
Cdd:PRK14532   82 IFDGFPRTVAQAEALDKM 99
PRK14527 PRK14527
adenylate kinase; Provisional
 271-368 1.71e-12

adenylate kinase; Provisional


Pssm-ID: 237745 [Multi-domain]  Cd Length: 191  Bit Score: 65.58  E-value: 1.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442 271 VLLCGPMGCGKKLQAALLSQKYGLVNISCGQLLKEAMAAESSLGDLIEPFFEKRMTVPDSIITRVLTERLKQQDCIQKgw 350
Cdd:PRK14527    9 VIFLGPPGAGKGTQAERLAQELGLKKLSTGDILRDHVARGTELGQRAKPIMEAGDLVPDELILALIRDELAGMEPVRV-- 86

                          90
                  ....*....|....*...
gi 1958762442 351 VLHGFPRDLDQARLLNSM 368
Cdd:PRK14527   87 IFDGFPRTLAQAEALDRL 104
DD_TEX55-like cd22961
dimerization/docking (D/D) domain found in the testis-specific expressed protein 55 (TEX55) ...
 12-52 3.13e-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: 60.51  E-value: 3.13e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1958762442  12 PEMPQYGEDYHIFEMMQSMLEQLLIHQPEDPISFMISHLRR 52
Cdd:cd22961     2 EDAEEYLEKHKIPELFESLLTALLIEKPEDPIEFLIDKLQQ 42
PLN02674 PLN02674
adenylate kinase
 59-249 1.62e-11

adenylate kinase


Pssm-ID: 178279 [Multi-domain]  Cd Length: 244  Bit Score: 63.75  E-value: 1.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442  59 RVVILGPPASGKTTIA------MWLCkHLNSNLITKENLLERefSLLSLEAKKHYQVYKRVPNSTLVSLVQERLNEDDCl 132
Cdd:PLN02674   33 RLILIGPPGSGKGTQSpiikdeYCLC-HLATGDMLRAAVAAK--TPLGIKAKEAMDKGELVSDDLVVGIIDEAMKKPSC- 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442 133 RRGWILDGIPERREQAL----MIQTLGLAPKHVIVLSAPDSVLIERNVGKRIDPVTGEIYHTTFDWPPELEIQNRLIQPE 208
Cdd:PLN02674  109 QKGFILDGFPRTVVQAQkldeMLAKQGAKIDKVLNFAIDDAILEERITGRWIHPSSGRTYHTKFAPPKVPGVDDVTGEPL 188

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1958762442 209 GISEIDTA---KKLLE-YHRHIIRILPSYPK--ILKTISSDQPCVDV 249
Cdd:PLN02674  189 IQRKDDTAavlKSRLEaFHKQTEPVIDYYAKkgVVANLHAEKPPKEV 235
Kti12 COG4088
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ...
 58-222 5.04e-11

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: 61.28  E-value: 5.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442  58 PRVVIL-GPPASGKTTIAMWLCKHLNSNLITKENLLEREFSLLSLEAKKHYQVYKRVPNSTLVSLVQERLNeddcLRRGW 136
Cdd:COG4088     4 PMLLILtGPPGSGKTTFAKALAQRLYAEGIAVALLHSDDFRRFLVNESFPKETYEEVVEDVRTTTADNALD----NGYSV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442 137 ILDGIPERREQALMIQTLGL--APKHVIVLSAPDSVLIERNV--GKRIDPVTGEIYHTTFDWPPELEIQNRLIQPEGISE 212
Cdd:COG4088    80 IVDGTFYYRSWQRDFRNLAKhkAPIHIIYLKAPLETALRRNRerGEPIPERVIARMYRKFDKPGTKDRPDLVIDTTEDSV 159

                         170
                  ....*....|
gi 1958762442 213 IDTAKKLLEY 222
Cdd:COG4088   160 SETLDAILKA 169
PRK14530 PRK14530
adenylate kinase; Provisional
 269-368 7.24e-11

adenylate kinase; Provisional


Pssm-ID: 237747 [Multi-domain]  Cd Length: 215  Bit Score: 61.34  E-value: 7.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442 269 PKVLLCGPMGCGKKLQAALLSQKYGLVNISCGQLLKEAMAAESSLGDL----IEPFFEKRMTVPDSIITRVLTERLKQQD 344
Cdd:PRK14530    4 PRILLLGAPGAGKGTQSSNLAEEFGVEHVTTGDALRANKQMDISDMDTeydtPGEYMDAGELVPDAVVNEIVEEALSDAD 83

                          90       100
                  ....*....|....*....|....
gi 1958762442 345 ciqkGWVLHGFPRDLDQARLLNSM 368
Cdd:PRK14530   84 ----GFVLDGYPRNLEQAEYLESI 103
aden_kin_iso1 TIGR01360
adenylate kinase, isozyme 1 subfamily; Members of this family are adenylate kinase, EC 2.7.4.3. ...
 275-361 2.07e-10

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: 59.44  E-value: 2.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442 275 GPmGCGKKLQAALLSQKYGLVNISCGQLLKEAMAAESSLGDLIEPFFEKRMTVPDSIITRVLTERLKQQDCIQKGWVLHG 354
Cdd:TIGR01360  11 GP-GSGKGTQCEKIVEKYGFTHLSTGDLLRAEVASGSERGKQLQAIMESGDLVPLDTVLDLLKDAMVAALGTSKGFLIDG 89


                  ....*..
gi 1958762442 355 FPRDLDQ 361
Cdd:TIGR01360  90 YPREVKQ 96
PRK14526 PRK14526
adenylate kinase; Provisional
 270-366 2.46e-10

adenylate kinase; Provisional


Pssm-ID: 172992 [Multi-domain]  Cd Length: 211  Bit Score: 59.86  E-value: 2.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442 270 KVLLCGPMGCGKKLQAALLSQKYGLVNISCGQLLKEAMAAESSLGDLIEPFFEKRMTVPDSIITRVLTERLKQQDCiQKG 349
Cdd:PRK14526    2 KLVFLGPPGSGKGTIAKILSNELNYYHISTGDLFRENILNSTPLGKEIKQIVENGQLVPDSITIKIVEDKINTIKN-NDN 80

                          90
                  ....*....|....*..
gi 1958762442 350 WVLHGFPRDLDQARLLN 366
Cdd:PRK14526   81 FILDGFPRNINQAKALD 97
PTZ00088 PTZ00088
adenylate kinase 1; Provisional
 59-198 1.07e-09

adenylate kinase 1; Provisional


Pssm-ID: 240262 [Multi-domain]  Cd Length: 229  Bit Score: 58.27  E-value: 1.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442  59 RVVILGPPASGKTTIAMWLCKHLNSNLITKENLLEREF---SLLSLEAKKHYQVYKRVPNSTLVSLVQERL-NEDDCLRR 134
Cdd:PTZ00088    8 KIVLFGAPGVGKGTFAEILSKKENLKHINMGNILREEIkakTTIGKEIQKVVTSGNLVPDNLVIAIVKDEIaKVTDDCFK 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442 135 GWILDGIPERREQALMIQTLGlAPKHVIVLSAPDSVLIERNVGKRIDPVTGEIYH------TTFDWPPEL 198
Cdd:PTZ00088   88 GFILDGFPRNLKQCKELGKIT-NIDLFVNIYLPRNILIKKLLGRRICNTCNRNFNiahirsDPYDMPPIL 156
AAA_17 pfam13207
AAA domain;
275-365 5.20e-09

AAA domain;


Pssm-ID: 463810 [Multi-domain]  Cd Length: 136  Bit Score: 54.17  E-value: 5.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442 275 GPMGCGKKLQAALLSQKYGLVNISCGQLLKEaMAAESSLGDLIEpFFEKRMTVPDSIITRVLTERLKqQDCIQKGWVLHG 354
Cdd:pfam13207   2 GVPGSGKTTQLKKLAEKLGFPHISAGDLLRE-EAKERGLVEDRD-EMRKLPLEPQKELQKLAAERIA-EEAGEGGVIVDG 78

                          90
                  ....*....|.
gi 1958762442 355 FPRDLDQARLL 365
Cdd:pfam13207  79 HPRIKTPAGYL 89
AAA_17 pfam13207
AAA domain;
63-174 6.89e-09

AAA domain;


Pssm-ID: 463810 [Multi-domain]  Cd Length: 136  Bit Score: 53.78  E-value: 6.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442  63 LGPPASGKTTIAMWLCKHLNSNLIT-----KENLLEREfsllSLEAKKHYQVYKRVPNSTLVSLVQERLNEdDCLRRGWI 137
Cdd:pfam13207   1 TGVPGSGKTTQLKKLAEKLGFPHISagdllREEAKERG----LVEDRDEMRKLPLEPQKELQKLAAERIAE-EAGEGGVI 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1958762442 138 LDGIPERREQA-----LMIQTL-GLAPKHVIVLSAPDSVLIER 174
Cdd:pfam13207  76 VDGHPRIKTPAgylpgLPVEVLrELKPDAIILLEADPEEILER 118
DD_EFCAB10 cd22976
dimerization/docking (D/D) domain found in EF-hand calcium-binding domain-containing protein ...
 16-52 1.74e-08

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: 50.18  E-value: 1.74e-08
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1958762442  16 QYGEDYHIFEMMQSMLEQLLIHQPEDPISFMISHLRR 52
Cdd:cd22976     6 EYLEKHKIPELFENLTSLLLYHRPEDPKAFLIEQLEK 42
PRK14526 PRK14526
adenylate kinase; Provisional
 59-223 7.64e-08

adenylate kinase; Provisional


Pssm-ID: 172992 [Multi-domain]  Cd Length: 211  Bit Score: 52.55  E-value: 7.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442  59 RVVILGPPASGKTTIAMWLCKHLNSNLITKENLLEREFS---LLSLEAKKHYQVYKRVPNSTLVSLVQERLNEDDClRRG 135
Cdd:PRK14526    2 KLVFLGPPGSGKGTIAKILSNELNYYHISTGDLFRENILnstPLGKEIKQIVENGQLVPDSITIKIVEDKINTIKN-NDN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442 136 WILDGIPERREQALMIQTLgLAPKHVIVLSAPDSVLIERNVGKRIDPVTGEIYHTTFDWPPELEI----QNRLIQPEGIS 211
Cdd:PRK14526   81 FILDGFPRNINQAKALDKF-LPNIKIINFLIDEELLIKRLSGRRICKSCNNIFNIYTLPTKEKGIcdvcKGDLYQRKDDK 159

                         170
                  ....*....|..
gi 1958762442 212 EIDTAKKLLEYH 223
Cdd:PRK14526  160 EESLKTRLQEYK 171
PLN02459 PLN02459
probable adenylate kinase
 275-368 7.65e-08

probable adenylate kinase


Pssm-ID: 215253 [Multi-domain]  Cd Length: 261  Bit Score: 52.93  E-value: 7.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442 275 GPMGCGKKLQAALLSQKYGLVNISCGQLLKEAMAAESSLGDLIEPFFEKRMTVPDSIITRVLTERLKQ-QDCIQKGWVLH 353
Cdd:PLN02459   36 GCPGVGKGTYASRLSKLLGVPHIATGDLVREEIKSSGPLGAQLKEIVNQGKLVPDEIIFSLLSKRLEAgEEEGESGFILD 115

                          90
                  ....*....|....*
gi 1958762442 354 GFPRDLDQARLLNSM 368
Cdd:PLN02459  116 GFPRTVRQAEILEGV 130
AAA_18 pfam13238
AAA domain;
60-174 1.14e-07

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 50.12  E-value: 1.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442  60 VVILGPPASGKTTIAMWLCKHLNSNLITKENLLEREfslLSLEAKKHYQVYKRVPNSTLVSLVQErLNEDDCLRRG--WI 137
Cdd:pfam13238   1 ILITGTPGVGKTTLAKELSKRLGFGDNVRDLALENG---LVLGDDPETRESKRLDEDKLDRLLDL-LEENAALEEGgnLI 76

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1958762442 138 LDGIPERREQALMIQtlglapKHVIVLSAPDSVLIER 174
Cdd:pfam13238  77 IDGHLAELEPERAKD------LVGIVLRASPEELLER 107
PRK14527 PRK14527
adenylate kinase; Provisional
 56-178 1.31e-07

adenylate kinase; Provisional


Pssm-ID: 237745 [Multi-domain]  Cd Length: 191  Bit Score: 51.33  E-value: 1.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442  56 NVPRVVI-LGPPASGKTTIAMWLCKHLNSNLITKENLLEREFSL---LSLEAKKHYQVYKRVPNSTLVSLVQERLNEDDC 131
Cdd:PRK14527    4 TKNKVVIfLGPPGAGKGTQAERLAQELGLKKLSTGDILRDHVARgteLGQRAKPIMEAGDLVPDELILALIRDELAGMEP 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958762442 132 LRRgwILDGIPERREQA----LMIQTLGLAPKHVIVLSAPDSVLIERNVGK 178
Cdd:PRK14527   84 VRV--IFDGFPRTLAQAealdRLLEELGARLLAVVLLEVPDEELIRRIVER 132
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 60-178 3.59e-07

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: 49.23  E-value: 3.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442  60 VVIL-GPPASGKTTIAMWLCKHLNSNLITKENLLERefslLSLEAKKHYQVYKRVPnstlvSLVQERLNE--DDCLRRGW 136
Cdd:pfam13671   1 LILLvGLPGSGKSTLARRLLEELGAVRLSSDDERKR----LFGEGRPSISYYTDAT-----DRTYERLHElaRIALRAGR 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958762442 137 --ILD-GIPERREQALMIQ---TLGlAPKHVIVLSAPDSVLIERNVGK 178
Cdd:pfam13671  72 pvILDaTNLRRDERARLLAlarEYG-VPVRIVVFEAPEEVLRERLAAR 118
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
60-212 3.98e-07

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 49.53  E-value: 3.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442  60 VVILGPPASGKTTIAMWLCKHLNSNLITK----ENLLEREFSLLSLEAKKHYQVYKRvpnstLVSLVQerlnedDCLRRG 135
Cdd:COG0645     2 ILVCGLPGSGKSTLARALAERLGAVRLRSdvvrKRLFGAGLAPLERSPEATARTYAR-----LLALAR------ELLAAG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442 136 W--ILDG---IPERREQALMI-QTLGlAPKHVIVLSAPDSVLIE----RNVGKRIDPVTGEIY-HTTFDWPP--ELEIQN 202
Cdd:COG0645    71 RsvILDAtflRRAQREAFRALaEEAG-APFVLIWLDAPEEVLRErleaRNAEGGDSDATWEVLeRQLAFEEPltEDEGFL 149

                         170
                  ....*....|
gi 1958762442 203 RLIQPEGISE 212
Cdd:COG0645   150 LVVDTSGLEE 159
PRK14531 PRK14531
adenylate kinase; Provisional
 59-174 5.32e-07

adenylate kinase; Provisional


Pssm-ID: 172997 [Multi-domain]  Cd Length: 183  Bit Score: 49.42  E-value: 5.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442  59 RVVILGPPASGKTTIAMWLC-----KHLNSNlitkeNLLEREFSLLSLEAKKHYQVYKR---VPNSTLVSLVQERLNEDD 130
Cdd:PRK14531    4 RLLFLGPPGAGKGTQAARLCaahglRHLSTG-----DLLRSEVAAGSALGQEAEAVMNRgelVSDALVLAIVESQLKALN 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958762442 131 clRRGWILDGIPERREQA----LMIQTLGLAPKHVIVLSAPDSVLIER 174
Cdd:PRK14531   79 --SGGWLLDGFPRTVAQAealePLLEELKQPIEAVVLLELDDAVLIER 124
PRK14529 PRK14529
adenylate kinase; Provisional
 59-180 1.43e-06

adenylate kinase; Provisional


Pssm-ID: 237746 [Multi-domain]  Cd Length: 223  Bit Score: 48.95  E-value: 1.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442  59 RVVILGPPASGKTTIAMWLCK-----HLNSNLITKENLleREFSLLSLEAKKHYQVYKRVPNSTLVSLVQERLNEDDclR 133
Cdd:PRK14529    2 NILIFGPNGSGKGTQGALVKKkydlaHIESGAIFREHI--GGGTELGKKAKEYIDRGDLVPDDITIPMILETLKQDG--K 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958762442 134 RGWILDGIPERREQAL----MIQTLGLAPKHVIVLSAPDSVLIERNVGKRI 180
Cdd:PRK14529   78 NGWLLDGFPRNKVQAEklweALQKEGMKLDYVIEILLPREVAKNRIMGRRL 128
DD_TEX55 cd22975
dimerization/docking (D/D) domain found in testis-specific expressed protein 55 (TEX55) and ...
 16-50 1.67e-06

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: 44.48  E-value: 1.67e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1958762442  16 QYGEDYHIFEMMQSMLEQLLIHQPEDPISFMISHL 50
Cdd:cd22975     9 KYLEKHNILQLFQELTAGLVYERPDDPIQFMIDEI 43
UMP_CMP_kin_fam TIGR01359
UMP-CMP kinase family; This subfamily of the adenylate kinase superfamily contains examples of ...
 60-174 2.98e-05

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: 44.28  E-value: 2.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442  60 VVILGPPASGKTTIAMWLCKHLNSNLITKENLLEREFSLLSLEAKKHYQVYKR----VPNSTLVSLVQERLNEDDClRRG 135
Cdd:TIGR01359   2 VFVLGGPGSGKGTQCAKIVENFGFTHLSAGDLLRAEIKREGSENGSLIESYIKegkiVPSEVTVELLKKAIQEDGS-SKK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1958762442 136 WILDGIP---ERREQALMIQTLGLAPKHVIVLSAPDSVLIER 174
Cdd:TIGR01359  81 FLIDGFPrneENLEAWEKLMDNKVNFKFVLFFDCPEETMIKR 122
DD_TbAK-like cd22981
dimerization/docking (D/D) domain found in Trypanosoma brucei adenylate kinase (AK) and ...
 16-53 6.75e-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: 39.71  E-value: 6.75e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1958762442  16 QYGEDYHIFEMMQSMLEQLLIHQPEDPISFMISHLRRN 53
Cdd:cd22981     7 KYLKEKNIPQLFEFLLRHLLLDKPENPLEYLHDLLERP 44
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
31-154 1.76e-04

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 43.64  E-value: 1.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442  31 LEQLLIHQPEDPISFMISHLRRNNDNVPRVVILGPPASGKTTiamwLCKHLNSNLITKENLLEREFSLL-SLeakKHYQv 109
Cdd:COG5635   154 LDDLYVPLNLLERIESLKRLELLEAKKKRLLILGEPGSGKTT----LLRYLALELAERYLDAEDPIPILiEL---RDLA- 225

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442 110 ykrvPNSTLVSLVQERLNEDDCLRRGW------------ILDG---IPERREQALMIQTL 154
Cdd:COG5635   226 ----EEASLEDLLAEALEKRGGEPEDAlerllrngrlllLLDGldeVPDEADRDEVLNQL 281
DD_R_PKA_DPY30-like cd22957
dimerization/docking (D/D) domains found in the cAMP-dependent protein kinase regulatory ...
 25-50 2.98e-04

dimerization/docking (D/D) domains found in the cAMP-dependent protein kinase regulatory subunit (PRKAR) and the DPY30/SDC1-like family; This hierarchy includes the dimerization/docking (D/D) domains of type I and type II cAMP-dependent protein kinase (PKA) regulatory (R) subunits, DPY30 from animals and its homologs, SDC1 from yeasts, and similar domains. PKA is a serine/threonine kinase (STK), catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of R subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. There are two classes of R subunits, RI and RII; each exists as two isoforms (alpha and beta) from distinct genes. These functionally non-redundant R isoforms allow for specificity in PKA signaling. The R subunit contains an N-terminal D/D domain, a linker with an inhibitory sequence (IS), and two c-AMP binding domains. The D/D domain dimerizes to form a four-helix bundle that serves as a docking site for A-kinase-anchoring proteins (AKAPs), which facilitates the localization of PKA to specific sites in the cell. DPY30, also called dumpy-30, was initially discovered in Caenorhabditis elegans as a key player in X chromosome dosage compensation. Human DPY30 plays a dual function in moderately regulating the methyltransferase activity of SET1/COMPASS (COMplex of Proteins ASsociated with Set1) enzymes and contributing to the recruitment of the complex to chromatin. Yeast SDC1 (suppressor of CDC25 protein 1) is the smallest subunit of COMPASS (COMplex of Proteins ASsociated with Set1) and interacts exclusively with Bre2 at the distal end of the catalytic module. It positively regulates the COMPASS catalytic module by stabilizing the non-canonical Bre2 SPRY domain. DPY30/SDC1 contains a C-terminal helical bundle domain that directly interacts with Ash2L (in human)/Bre2 (in yeast) COMPASS through the DPY30-binding motif (DBM). The DPY30/SDC1 helical bundle domain, also called D/D domain, is formed of two alpha-helices that may be analogous to the D/D domain found in regulatory subunit of PKA.


Pssm-ID: 438526  Cd Length: 29  Bit Score: 37.87  E-value: 2.98e-04
                          10        20
                  ....*....|....*....|....*.
gi 1958762442  25 EMMQSMLEQLLIHQPEDPISFMISHL 50
Cdd:cd22957     1 ELLQDAVAKLLEERPEDPVEFLAEYF 26
DD_CrRSP_unchar cd22964
dimerization/docking (D/D) domain of an uncharacterized subunit found in Chlamydomonas ...
 10-52 3.34e-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: 37.98  E-value: 3.34e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1958762442  10 IPPEMPQYGEDYHIFEMMQSMLEQLLIHQPEDPISFMISHLRR 52
Cdd:cd22964     1 KAEEKKEYLQQKVINPILEQLVTDLLQEKPEDPVPFMIQWLRK 43
DD_AK5 cd22978
dimerization/docking (D/D) domain found in adenylate kinase isoenzyme 5 (AK5) and similar ...
 16-52 3.47e-04

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: 37.90  E-value: 3.47e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1958762442  16 QYGEDYHIFEMMQSMLEQLLIHQPEDPISFMISHLRR 52
Cdd:cd22978     6 DYLSRKEIPQLFESLMTGLMYNRPDDPIEFLEDCLEK 42
NadR3 COG3172
Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase ...
 55-86 5.89e-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: 40.57  E-value: 5.89e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1958762442  55 DNVPRVVILGPPASGKTTIAMWLCKHLNSNLI 86
Cdd:COG3172     6 SFVKKIVLLGAESTGKTTLARALAAHYNTPWV 37
DUF5582 pfam17819
Family of unknown function (DUF5582); This is a family of unknown function found in chordata.
 9-48 8.13e-04

Family of unknown function (DUF5582); This is a family of unknown function found in chordata.


Pssm-ID: 465519  Cd Length: 146  Bit Score: 39.42  E-value: 8.13e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1958762442   9 RIPP---EMP-----QYGEDYHIFEMMQSMLEQLLIHQPEDPISFMIS 48
Cdd:pfam17819  97 RFPPivyEDPyqvslRYMEKHHILQIFQQITENLVYEKPEDPLHFMLC 144
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
 59-174 7.90e-03

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: 36.76  E-value: 7.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762442  59 RVVILGPPASGKTTIAMWLCKHLNSNLITKENLLEREF--SLLSLEAKKHYQVYKRvpnstlvslvQERLNEDD-CLRRG 135
Cdd:cd00464     1 NIVLIGMMGAGKTTVGRLLAKALGLPFVDLDELIEQRAgmSIPEIFAEEGEEGFRE----------LEREVLLLlLTKEN 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1958762442 136 WIL---DGIPERREQALMIQTLGLapkhVIVLSAPDSVLIER 174
Cdd:cd00464    71 AVIatgGGAVLREENRRLLLENGI----VVWLDASPEELLER 108
PRK04182 PRK04182
cytidylate kinase; Provisional
 275-318 8.12e-03

cytidylate kinase; Provisional


Pssm-ID: 235244 [Multi-domain]  Cd Length: 180  Bit Score: 37.09  E-value: 8.12e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1958762442 275 GPMGCGKKLQAALLSQKYGLVNISCGQLLKEaMAAESSLgDLIE 318
Cdd:PRK04182    7 GPPGSGKTTVARLLAEKLGLKHVSAGEIFRE-LAKERGM-SLEE 48
cyt_kin_arch TIGR02173
cytidylate kinase, putative; Proteins in this family are believed to be cytidylate kinase. ...
 60-87 9.22e-03

cytidylate kinase, putative; Proteins in this family are believed to be cytidylate kinase. Members of this family are found in the archaea and in spirochaetes, and differ considerably from the common bacterial form of cytidylate kinase described by TIGR00017.


Pssm-ID: 274012 [Multi-domain]  Cd Length: 171  Bit Score: 36.63  E-value: 9.22e-03
                          10        20
                  ....*....|....*....|....*...
gi 1958762442  60 VVILGPPASGKTTIAMWLCKHLNSNLIT 87
Cdd:TIGR02173   3 ITISGPPGSGKTTVAKILAEKLSLKLIS 30
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
49-87 9.48e-03

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 37.56  E-value: 9.48e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1958762442  49 HLRRNNDNVPRVVIL-GPPASGKTTIAMWLCKHLNSNLIT 87
Cdd:COG1223    26 NLRKFGLWPPRKILFyGPPGTGKTMLAEALAGELKLPLLT 65
 
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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