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Conserved domains on  [gi|568914211|ref|XP_006498352|]
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adenylate kinase 8 isoform X2 [Mus musculus]

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 ...
 298-490 2.44e-53

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: 178.58  E-value: 2.44e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211 298 KVLLCGPLGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSSFGELIQPFFEKRMTVPDSIITKVLADRMEQQDCiQKG 377
Cdd:cd01428    1 RILLLGPPGSGKGTQAERLAKKYGLPHISTGDLLREEIASGTELGKKAKEYIDSGKLVPDEIVIKLLKERLKKPDC-KKG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211 378 WVLHGFPRDLDQARMLNSM---GYNPNRVFFLSVPLDSILERLTLRRTDPVTGERFHLMYKPpptiEVQVRLLQNPKDSE 454
Cdd:cd01428   80 FILDGFPRTVDQAEALDELldeGIKPDKVIELDVPDEVLIERILGRRICPVSGRVYHLGKDD----VTGEPLSQRSDDNE 155

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 568914211 455 EYIKLQTDLFYRNSGDLEQYYDRA---IIVNGDQDPYTV 490
Cdd:cd01428  156 ETIKKRLEVYKEQTAPLIDYYKKKgklVEIDGSGDIDEV 194
ADK cd01428
Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine ...
 88-277 2.88e-32

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: 122.35  E-value: 2.88e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211  88 KVVILGPPASGKTTIAMWLCKHLNSNLITKESLLEREF---SRLSVEAKSYYQVYK-IPNSILVSLVQERLNEDDClRKG 163
Cdd:cd01428    1 RILLLGPPGSGKGTQAERLAKKYGLPHISTGDLLREEIasgTELGKKAKEYIDSGKlVPDEIVIKLLKERLKKPDC-KKG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211 164 WILDGIPERREQALMIQTL---GLAPKHVIVLNAPDTVLIERNVGKRIDPVTGEIYHTTFDWPPEPEIQNRLRQpegisE 240
Cdd:cd01428   80 FILDGFPRTVDQAEALDELldeGIKPDKVIELDVPDEVLIERILGRRICPVSGRVYHLGKDDVTGEPLSQRSDD-----N 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 568914211 241 IETAKKLLE-YHRHIIRILPSYPK--ILKTISSDQPCVDV 277
Cdd:cd01428  155 EETIKKRLEvYKEQTAPLIDYYKKkgKLVEIDGSGDIDEV 194
DD_AK8 cd22979
dimerization/docking (D/D) domain found in adenylate kinase isoenzyme 8 (AK8) and similar ...
 9-52 1.48e-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: 70.57  E-value: 1.48e-15
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 568914211   9 RIPPEMPQYGEDYYIFEMMQNMLEQLLIHQPEDPISFMITHLRR 52
Cdd:cd22979    1 EIPPEFAAYAEKHRIFELFQDLLKQLLIHKPEDPLQFLIDYLQK 44
 
Name Accession Description Interval E-value
ADK cd01428
Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine ...
 298-490 2.44e-53

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: 178.58  E-value: 2.44e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211 298 KVLLCGPLGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSSFGELIQPFFEKRMTVPDSIITKVLADRMEQQDCiQKG 377
Cdd:cd01428    1 RILLLGPPGSGKGTQAERLAKKYGLPHISTGDLLREEIASGTELGKKAKEYIDSGKLVPDEIVIKLLKERLKKPDC-KKG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211 378 WVLHGFPRDLDQARMLNSM---GYNPNRVFFLSVPLDSILERLTLRRTDPVTGERFHLMYKPpptiEVQVRLLQNPKDSE 454
Cdd:cd01428   80 FILDGFPRTVDQAEALDELldeGIKPDKVIELDVPDEVLIERILGRRICPVSGRVYHLGKDD----VTGEPLSQRSDDNE 155

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 568914211 455 EYIKLQTDLFYRNSGDLEQYYDRA---IIVNGDQDPYTV 490
Cdd:cd01428  156 ETIKKRLEVYKEQTAPLIDYYKKKgklVEIDGSGDIDEV 194
adk TIGR01351
adenylate kinase; Adenylate kinase (EC 2.7.4.3) converts ATP + AMP to ADP + ADP, that is, uses ...
 298-496 3.19e-42

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: 149.69  E-value: 3.19e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211  298 KVLLCGPLGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSSFGELIQPFFEKRMTVPDSIITKVLADRMEQQDCIQKG 377
Cdd:TIGR01351   1 RLVLLGPPGSGKGTQAKRIAEKYGLPHISTGDLLRAEIKAGTPLGKKAKEYMEKGELVPDEIVNQLVKERLTQNDDNENG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211  378 WVLHGFPRDLDQARMLNSMGYNPNR-VFFLSVPLDSILERLTLRRTDPVTGERFHLMYKPPPTIEVQV----RLLQNPKD 452
Cdd:TIGR01351  81 FILDGFPRTLSQAEALDALLEEPIDaVIELDVPDEELVERLSGRRICPSCGRVYHLKFNPPKVPGCDDctgeLLVQREDD 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 568914211  453 SEEYIKLQTDLFYRNSGDLEQYYDRAII---VNGDQDPYTVFEYIES 496
Cdd:TIGR01351 161 TEEVVKKRLEVYKEQTEPLIDYYKKRGIlvqIDGNGPIDEVWKRILE 207
Adk COG0563
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ...
 298-498 4.38e-41

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: 146.43  E-value: 4.38e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211 298 KVLLCGPLGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSSFGELIQPFFEKRMTVPDSIITKVLADRMEQQDCiQKG 377
Cdd:COG0563    2 RIILLGPPGAGKGTQAKRLAEKYGIPHISTGDMLRAAVKAGTELGKKAKEYMDAGELVPDEIVIGLVKERLAQPDC-ANG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211 378 WVLHGFPRDLDQA----RMLNSMGYNPNRVFFLSVPLDSILERLTLRRTDPVTGERFHLMYKPPPTIEV----QVRLLQN 449
Cdd:COG0563   81 FILDGFPRTVAQAealdELLAELGIKLDAVIELDVDDEELVERLSGRRVCPNCGATYHVKFNPPKVEGVcdkcGGELVQR 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568914211 450 PKDSEEYIKLQTDLFYRNSGDLEQYYDRA---IIVNGDQDPYTVFEYIESGI 498
Cdd:COG0563  161 ADDNEETVRKRLEVYHEQTAPLIDYYRKKgklVEIDGEGSIEEVTADILAIL 212
ADK pfam00406
Adenylate kinase;
301-475 1.17e-39

Adenylate kinase;


Pssm-ID: 395329 [Multi-domain]  Cd Length: 184  Bit Score: 141.68  E-value: 1.17e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211  301 LCGPLGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSSFGELIQPFFEKRMTVPDSIITKVLADRMEQQDCiQKGWVL 380
Cdd:pfam00406   1 LLGPPGAGKGTQAEKIVQKYGLPHLSTGDLLRAEIKSGTELGKEAKEYMDKGELVPDEVVVGLVKERLEQNDC-KNGFLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211  381 HGFPRDLDQARMLNSM---GYNPNRVFFLSVPLDSILERLTLRRTDPVTGERFHLMYKPPPTIEVQV----RLLQNPKDS 453
Cdd:pfam00406  80 DGFPRTVPQAEALEELlerGIKLDYVIEFDVPDEVLVERLTGRRIHPNSGRSYHLEFNPPKVPGKDDvtgePLVQRSDDN 159

                         170       180
                  ....*....|....*....|..
gi 568914211  454 EEYIKLQTDLFYRNSGDLEQYY 475
Cdd:pfam00406 160 EETVKKRLETYHKQTKPLIDYY 181
PLN02842 PLN02842
nucleotide kinase
 300-496 6.03e-38

nucleotide kinase


Pssm-ID: 178435 [Multi-domain]  Cd Length: 505  Bit Score: 145.39  E-value: 6.03e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211 300 LLCGPLGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSSFGELIQPFFEKRMTVPDSIITKVLADRMEQQDCIQKGWV 379
Cdd:PLN02842   1 MISGAPASGKGTQCELIVHKFGLVHISTGDLLRAEVSAGTDIGKRAKEFMNSGRLVPDEIVIAMVTGRLSREDAKEKGWL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211 380 LHGFPRDLDQARMLNSMGYNPNRVFFLSVPLDSILERLTLRRTDPVTGERFHLMYKPPPTIEVQVRLLQNPKDSEEYIKL 459
Cdd:PLN02842  81 LDGYPRSFAQAQSLEKLKIRPDIFILLDVPDEILIDRCVGRRLDPVTGKIYHIKNFPPESEEIKARLITRPDDTEEKVKA 160

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 568914211 460 QTDLFYRNSGD-LEQYYDRAIIVNGDQDPYTVFEYIES 496
Cdd:PLN02842 161 RLQIYKKNAEAiLSTYSDIMVKIDGNRPKEVVFEEISS 198
ADK cd01428
Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine ...
 88-277 2.88e-32

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: 122.35  E-value: 2.88e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211  88 KVVILGPPASGKTTIAMWLCKHLNSNLITKESLLEREF---SRLSVEAKSYYQVYK-IPNSILVSLVQERLNEDDClRKG 163
Cdd:cd01428    1 RILLLGPPGSGKGTQAERLAKKYGLPHISTGDLLREEIasgTELGKKAKEYIDSGKlVPDEIVIKLLKERLKKPDC-KKG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211 164 WILDGIPERREQALMIQTL---GLAPKHVIVLNAPDTVLIERNVGKRIDPVTGEIYHTTFDWPPEPEIQNRLRQpegisE 240
Cdd:cd01428   80 FILDGFPRTVDQAEALDELldeGIKPDKVIELDVPDEVLIERILGRRICPVSGRVYHLGKDDVTGEPLSQRSDD-----N 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 568914211 241 IETAKKLLE-YHRHIIRILPSYPK--ILKTISSDQPCVDV 277
Cdd:cd01428  155 EETIKKRLEvYKEQTAPLIDYYKKkgKLVEIDGSGDIDEV 194
PLN02842 PLN02842
nucleotide kinase
 90-278 1.09e-29

nucleotide kinase


Pssm-ID: 178435 [Multi-domain]  Cd Length: 505  Bit Score: 121.89  E-value: 1.09e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211  90 VILGPPASGKTTIAMWLCKHLNSNLITKESLLEREFS---RLSVEAKSYYQVYK-IPNSILVSLVQERLNEDDCLRKGWI 165
Cdd:PLN02842   1 MISGAPASGKGTQCELIVHKFGLVHISTGDLLRAEVSagtDIGKRAKEFMNSGRlVPDEIVIAMVTGRLSREDAKEKGWL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211 166 LDGIPERREQALMIQTLGLAPKHVIVLNAPDTVLIERNVGKRIDPVTGEIYHTTFdWPPE-PEIQNRLRQPEGISEIETA 244
Cdd:PLN02842  81 LDGYPRSFAQAQSLEKLKIRPDIFILLDVPDEILIDRCVGRRLDPVTGKIYHIKN-FPPEsEEIKARLITRPDDTEEKVK 159

                        170       180       190
                 ....*....|....*....|....*....|....
gi 568914211 245 KKLLEYHRHIIRILPSYPKILKTISSDQPCVDVF 278
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 ...
 88-286 7.10e-27

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: 107.71  E-value: 7.10e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211   88 KVVILGPPASGKTTIAMWLCKHLNSNLITKESLLEREFSR---LSVEAKSYYQVYK-IPNSILVSLVQERLNEDDCLRKG 163
Cdd:TIGR01351   1 RLVLLGPPGSGKGTQAKRIAEKYGLPHISTGDLLRAEIKAgtpLGKKAKEYMEKGElVPDEIVNQLVKERLTQNDDNENG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211  164 WILDGIPERREQALMI-QTLGLAPKHVIVLNAPDTVLIERNVGKRIDPVTGEIYHTTFDWPPEPEIQN----RLRQ---- 234
Cdd:TIGR01351  81 FILDGFPRTLSQAEALdALLEEPIDAVIELDVPDEELVERLSGRRICPSCGRVYHLKFNPPKVPGCDDctgeLLVQredd 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568914211  235 -PEGISE-----IETAKKLLEYHRHIIrilpsypkILKTISSDQPCVDVFYQALTYVQ 286
Cdd:TIGR01351 161 tEEVVKKrlevyKEQTEPLIDYYKKRG--------ILVQIDGNGPIDEVWKRILEALK 210
Adk COG0563
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ...
 88-278 3.82e-26

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: 105.59  E-value: 3.82e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211  88 KVVILGPPASGKTTIAMWLCKHLNSNLITKESLLEREFSR---LSVEAKSYY----QVykiPNSILVSLVQERLNEDDCl 160
Cdd:COG0563    2 RIILLGPPGAGKGTQAKRLAEKYGIPHISTGDMLRAAVKAgteLGKKAKEYMdageLV---PDEIVIGLVKERLAQPDC- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211 161 RKGWILDGIPERREQAL----MIQTLGLAPKHVIVLNAPDTVLIERNVGKRIDPVTGEIYHTTFDWPPEPEI----QNRL 232
Cdd:COG0563   78 ANGFILDGFPRTVAQAEaldeLLAELGIKLDAVIELDVDDEELVERLSGRRVCPNCGATYHVKFNPPKVEGVcdkcGGEL 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568914211 233 RQ-----PEGIseietAKKLLEYHRHIIRILPSYPK--ILKTISSDQPCVDVF 278
Cdd:COG0563  158 VQraddnEETV-----RKRLEVYHEQTAPLIDYYRKkgKLVEIDGEGSIEEVT 205
ADK pfam00406
Adenylate kinase;
91-251 1.25e-22

Adenylate kinase;


Pssm-ID: 395329 [Multi-domain]  Cd Length: 184  Bit Score: 95.07  E-value: 1.25e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211   91 ILGPPASGKTTIAMWLCKHLNSNLITKESLLEREF---SRLSVEAKSYYQVYKI-PNSILVSLVQERLNEDDClRKGWIL 166
Cdd:pfam00406   1 LLGPPGAGKGTQAEKIVQKYGLPHLSTGDLLRAEIksgTELGKEAKEYMDKGELvPDEVVVGLVKERLEQNDC-KNGFLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211  167 DGIPERREQALMIQTL---GLAPKHVIVLNAPDTVLIERNVGKRIDPVTGEIYHTTFDWPPEPEIQN----RLRQPEGIS 239
Cdd:pfam00406  80 DGFPRTVPQAEALEELlerGIKLDYVIEFDVPDEVLVERLTGRRIHPNSGRSYHLEFNPPKVPGKDDvtgePLVQRSDDN 159

                         170
                  ....*....|...
gi 568914211  240 EiETAKKLLE-YH 251
Cdd:pfam00406 160 E-ETVKKRLEtYH 171
DD_AK8 cd22979
dimerization/docking (D/D) domain found in adenylate kinase isoenzyme 8 (AK8) and similar ...
 9-52 1.48e-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: 70.57  E-value: 1.48e-15
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 568914211   9 RIPPEMPQYGEDYYIFEMMQNMLEQLLIHQPEDPISFMITHLRR 52
Cdd:cd22979    1 EIPPEFAAYAEKHRIFELFQDLLKQLLIHKPEDPLQFLIDYLQK 44
 
Name Accession Description Interval E-value
ADK cd01428
Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine ...
 298-490 2.44e-53

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: 178.58  E-value: 2.44e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211 298 KVLLCGPLGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSSFGELIQPFFEKRMTVPDSIITKVLADRMEQQDCiQKG 377
Cdd:cd01428    1 RILLLGPPGSGKGTQAERLAKKYGLPHISTGDLLREEIASGTELGKKAKEYIDSGKLVPDEIVIKLLKERLKKPDC-KKG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211 378 WVLHGFPRDLDQARMLNSM---GYNPNRVFFLSVPLDSILERLTLRRTDPVTGERFHLMYKPpptiEVQVRLLQNPKDSE 454
Cdd:cd01428   80 FILDGFPRTVDQAEALDELldeGIKPDKVIELDVPDEVLIERILGRRICPVSGRVYHLGKDD----VTGEPLSQRSDDNE 155

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 568914211 455 EYIKLQTDLFYRNSGDLEQYYDRA---IIVNGDQDPYTV 490
Cdd:cd01428  156 ETIKKRLEVYKEQTAPLIDYYKKKgklVEIDGSGDIDEV 194
adk TIGR01351
adenylate kinase; Adenylate kinase (EC 2.7.4.3) converts ATP + AMP to ADP + ADP, that is, uses ...
 298-496 3.19e-42

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: 149.69  E-value: 3.19e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211  298 KVLLCGPLGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSSFGELIQPFFEKRMTVPDSIITKVLADRMEQQDCIQKG 377
Cdd:TIGR01351   1 RLVLLGPPGSGKGTQAKRIAEKYGLPHISTGDLLRAEIKAGTPLGKKAKEYMEKGELVPDEIVNQLVKERLTQNDDNENG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211  378 WVLHGFPRDLDQARMLNSMGYNPNR-VFFLSVPLDSILERLTLRRTDPVTGERFHLMYKPPPTIEVQV----RLLQNPKD 452
Cdd:TIGR01351  81 FILDGFPRTLSQAEALDALLEEPIDaVIELDVPDEELVERLSGRRICPSCGRVYHLKFNPPKVPGCDDctgeLLVQREDD 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 568914211  453 SEEYIKLQTDLFYRNSGDLEQYYDRAII---VNGDQDPYTVFEYIES 496
Cdd:TIGR01351 161 TEEVVKKRLEVYKEQTEPLIDYYKKRGIlvqIDGNGPIDEVWKRILE 207
Adk COG0563
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ...
 298-498 4.38e-41

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: 146.43  E-value: 4.38e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211 298 KVLLCGPLGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSSFGELIQPFFEKRMTVPDSIITKVLADRMEQQDCiQKG 377
Cdd:COG0563    2 RIILLGPPGAGKGTQAKRLAEKYGIPHISTGDMLRAAVKAGTELGKKAKEYMDAGELVPDEIVIGLVKERLAQPDC-ANG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211 378 WVLHGFPRDLDQA----RMLNSMGYNPNRVFFLSVPLDSILERLTLRRTDPVTGERFHLMYKPPPTIEV----QVRLLQN 449
Cdd:COG0563   81 FILDGFPRTVAQAealdELLAELGIKLDAVIELDVDDEELVERLSGRRVCPNCGATYHVKFNPPKVEGVcdkcGGELVQR 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568914211 450 PKDSEEYIKLQTDLFYRNSGDLEQYYDRA---IIVNGDQDPYTVFEYIESGI 498
Cdd:COG0563  161 ADDNEETVRKRLEVYHEQTAPLIDYYRKKgklVEIDGEGSIEEVTADILAIL 212
ADK pfam00406
Adenylate kinase;
301-475 1.17e-39

Adenylate kinase;


Pssm-ID: 395329 [Multi-domain]  Cd Length: 184  Bit Score: 141.68  E-value: 1.17e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211  301 LCGPLGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSSFGELIQPFFEKRMTVPDSIITKVLADRMEQQDCiQKGWVL 380
Cdd:pfam00406   1 LLGPPGAGKGTQAEKIVQKYGLPHLSTGDLLRAEIKSGTELGKEAKEYMDKGELVPDEVVVGLVKERLEQNDC-KNGFLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211  381 HGFPRDLDQARMLNSM---GYNPNRVFFLSVPLDSILERLTLRRTDPVTGERFHLMYKPPPTIEVQV----RLLQNPKDS 453
Cdd:pfam00406  80 DGFPRTVPQAEALEELlerGIKLDYVIEFDVPDEVLVERLTGRRIHPNSGRSYHLEFNPPKVPGKDDvtgePLVQRSDDN 159

                         170       180
                  ....*....|....*....|..
gi 568914211  454 EEYIKLQTDLFYRNSGDLEQYY 475
Cdd:pfam00406 160 EETVKKRLETYHKQTKPLIDYY 181
PLN02842 PLN02842
nucleotide kinase
 300-496 6.03e-38

nucleotide kinase


Pssm-ID: 178435 [Multi-domain]  Cd Length: 505  Bit Score: 145.39  E-value: 6.03e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211 300 LLCGPLGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSSFGELIQPFFEKRMTVPDSIITKVLADRMEQQDCIQKGWV 379
Cdd:PLN02842   1 MISGAPASGKGTQCELIVHKFGLVHISTGDLLRAEVSAGTDIGKRAKEFMNSGRLVPDEIVIAMVTGRLSREDAKEKGWL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211 380 LHGFPRDLDQARMLNSMGYNPNRVFFLSVPLDSILERLTLRRTDPVTGERFHLMYKPPPTIEVQVRLLQNPKDSEEYIKL 459
Cdd:PLN02842  81 LDGYPRSFAQAQSLEKLKIRPDIFILLDVPDEILIDRCVGRRLDPVTGKIYHIKNFPPESEEIKARLITRPDDTEEKVKA 160

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 568914211 460 QTDLFYRNSGD-LEQYYDRAIIVNGDQDPYTVFEYIES 496
Cdd:PLN02842 161 RLQIYKKNAEAiLSTYSDIMVKIDGNRPKEVVFEEISS 198
adk PRK00279
adenylate kinase; Reviewed
 298-496 3.14e-33

adenylate kinase; Reviewed


Pssm-ID: 234711 [Multi-domain]  Cd Length: 215  Bit Score: 125.26  E-value: 3.14e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211 298 KVLLCGPLGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSSFGELIQPFFEKRMTVPDSIITKVLADRMEQQDCiQKG 377
Cdd:PRK00279   2 RLILLGPPGAGKGTQAKFIAEKYGIPHISTGDMLRAAVKAGTELGKEAKSYMDAGELVPDEIVIGLVKERLAQPDC-KNG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211 378 WVLHGFPRDLDQA----RMLNSMGYNPNRVFFLSVPLDSILERLTLRRTDPVTGERFHLMYKPPPTIEV----QVRLLQN 449
Cdd:PRK00279  81 FLLDGFPRTIPQAealdEMLKELGIKLDAVIEIDVPDEELVERLSGRRICPACGRTYHVKFNPPKVEGKcdvcGEELIQR 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 568914211 450 PKDSEEYIKLQTDLFYRNSGDLEQYYDRA---IIVNGDQDPYTVFEYIES 496
Cdd:PRK00279 161 ADDNEETVRKRLEVYHKQTAPLIDYYKKKgklKKIDGTGSIDEVFADILK 210
ADK cd01428
Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine ...
 88-277 2.88e-32

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: 122.35  E-value: 2.88e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211  88 KVVILGPPASGKTTIAMWLCKHLNSNLITKESLLEREF---SRLSVEAKSYYQVYK-IPNSILVSLVQERLNEDDClRKG 163
Cdd:cd01428    1 RILLLGPPGSGKGTQAERLAKKYGLPHISTGDLLREEIasgTELGKKAKEYIDSGKlVPDEIVIKLLKERLKKPDC-KKG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211 164 WILDGIPERREQALMIQTL---GLAPKHVIVLNAPDTVLIERNVGKRIDPVTGEIYHTTFDWPPEPEIQNRLRQpegisE 240
Cdd:cd01428   80 FILDGFPRTVDQAEALDELldeGIKPDKVIELDVPDEVLIERILGRRICPVSGRVYHLGKDDVTGEPLSQRSDD-----N 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 568914211 241 IETAKKLLE-YHRHIIRILPSYPK--ILKTISSDQPCVDV 277
Cdd:cd01428  155 EETIKKRLEvYKEQTAPLIDYYKKkgKLVEIDGSGDIDEV 194
PLN02842 PLN02842
nucleotide kinase
 90-278 1.09e-29

nucleotide kinase


Pssm-ID: 178435 [Multi-domain]  Cd Length: 505  Bit Score: 121.89  E-value: 1.09e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211  90 VILGPPASGKTTIAMWLCKHLNSNLITKESLLEREFS---RLSVEAKSYYQVYK-IPNSILVSLVQERLNEDDCLRKGWI 165
Cdd:PLN02842   1 MISGAPASGKGTQCELIVHKFGLVHISTGDLLRAEVSagtDIGKRAKEFMNSGRlVPDEIVIAMVTGRLSREDAKEKGWL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211 166 LDGIPERREQALMIQTLGLAPKHVIVLNAPDTVLIERNVGKRIDPVTGEIYHTTFdWPPE-PEIQNRLRQPEGISEIETA 244
Cdd:PLN02842  81 LDGYPRSFAQAQSLEKLKIRPDIFILLDVPDEILIDRCVGRRLDPVTGKIYHIKN-FPPEsEEIKARLITRPDDTEEKVK 159

                        170       180       190
                 ....*....|....*....|....*....|....
gi 568914211 245 KKLLEYHRHIIRILPSYPKILKTISSDQPCVDVF 278
Cdd:PLN02842 160 ARLQIYKKNAEAILSTYSDIMVKIDGNRPKEVVF 193
PRK14530 PRK14530
adenylate kinase; Provisional
 297-498 1.23e-27

adenylate kinase; Provisional


Pssm-ID: 237747 [Multi-domain]  Cd Length: 215  Bit Score: 109.88  E-value: 1.23e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211 297 PKVLLCGPLGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSSFGEL----IQPFFEKRMTVPDSIITKVLADRMEQQD 372
Cdd:PRK14530   4 PRILLLGAPGAGKGTQSSNLAEEFGVEHVTTGDALRANKQMDISDMDTeydtPGEYMDAGELVPDAVVNEIVEEALSDAD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211 373 ciqkGWVLHGFPRDLDQARMLNSMGyNPNRVFFLSVPLDSILERLTLRRTDPVTGERFHLMYKPPPTIEV----QVRLLQ 448
Cdd:PRK14530  84 ----GFVLDGYPRNLEQAEYLESIT-DLDVVLYLDVSEEELVDRLTGRRVCPDCGANYHVEFNQPEEEGVcdecGGELIQ 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568914211 449 NPKDSEEYIKLQTDLFYRNSGDLEQYY-DRAIIV--NGDQDPYTVFEYIESGI 498
Cdd:PRK14530 159 RDDDTEETVRERLDVFEENTEPVIEHYrDQGVLVevDGEQTPDEVWADIQDAI 211
adk TIGR01351
adenylate kinase; Adenylate kinase (EC 2.7.4.3) converts ATP + AMP to ADP + ADP, that is, uses ...
 88-286 7.10e-27

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: 107.71  E-value: 7.10e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211   88 KVVILGPPASGKTTIAMWLCKHLNSNLITKESLLEREFSR---LSVEAKSYYQVYK-IPNSILVSLVQERLNEDDCLRKG 163
Cdd:TIGR01351   1 RLVLLGPPGSGKGTQAKRIAEKYGLPHISTGDLLRAEIKAgtpLGKKAKEYMEKGElVPDEIVNQLVKERLTQNDDNENG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211  164 WILDGIPERREQALMI-QTLGLAPKHVIVLNAPDTVLIERNVGKRIDPVTGEIYHTTFDWPPEPEIQN----RLRQ---- 234
Cdd:TIGR01351  81 FILDGFPRTLSQAEALdALLEEPIDAVIELDVPDEELVERLSGRRICPSCGRVYHLKFNPPKVPGCDDctgeLLVQredd 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568914211  235 -PEGISE-----IETAKKLLEYHRHIIrilpsypkILKTISSDQPCVDVFYQALTYVQ 286
Cdd:TIGR01351 161 tEEVVKKrlevyKEQTEPLIDYYKKRG--------ILVQIDGNGPIDEVWKRILEALK 210
Adk COG0563
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ...
 88-278 3.82e-26

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: 105.59  E-value: 3.82e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211  88 KVVILGPPASGKTTIAMWLCKHLNSNLITKESLLEREFSR---LSVEAKSYY----QVykiPNSILVSLVQERLNEDDCl 160
Cdd:COG0563    2 RIILLGPPGAGKGTQAKRLAEKYGIPHISTGDMLRAAVKAgteLGKKAKEYMdageLV---PDEIVIGLVKERLAQPDC- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211 161 RKGWILDGIPERREQAL----MIQTLGLAPKHVIVLNAPDTVLIERNVGKRIDPVTGEIYHTTFDWPPEPEI----QNRL 232
Cdd:COG0563   78 ANGFILDGFPRTVAQAEaldeLLAELGIKLDAVIELDVDDEELVERLSGRRVCPNCGATYHVKFNPPKVEGVcdkcGGEL 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568914211 233 RQ-----PEGIseietAKKLLEYHRHIIRILPSYPK--ILKTISSDQPCVDVF 278
Cdd:COG0563  158 VQraddnEETV-----RKRLEVYHEQTAPLIDYYRKkgKLVEIDGEGSIEEVT 205
PLN02674 PLN02674
adenylate kinase
 271-481 3.53e-24

adenylate kinase


Pssm-ID: 178279 [Multi-domain]  Cd Length: 244  Bit Score: 101.12  E-value: 3.53e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211 271 DQPCVDVFYQALTYVQsghrCNAPFTPKVLLCGPLGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSSFGELIQPFFE 350
Cdd:PLN02674  10 DVPSVDLMTELLRRMK----CSSKPDKRLILIGPPGSGKGTQSPIIKDEYCLCHLATGDMLRAAVAAKTPLGIKAKEAMD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211 351 KRMTVPDSIITKVLADRMEQQDCiQKGWVLHGFPRDLDQAR----MLNSMGYNPNRVFFLSVPlDSIL-ERLTLRRTDPV 425
Cdd:PLN02674  86 KGELVSDDLVVGIIDEAMKKPSC-QKGFILDGFPRTVVQAQkldeMLAKQGAKIDKVLNFAID-DAILeERITGRWIHPS 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211 426 TGERFHLMYKPPPTIEVQ----VRLLQNPKDSEEYIKLQTDLFYRNSGDLEQYYDRAIIV 481
Cdd:PLN02674 164 SGRTYHTKFAPPKVPGVDdvtgEPLIQRKDDTAAVLKSRLEAFHKQTEPVIDYYAKKGVV 223
ADK pfam00406
Adenylate kinase;
91-251 1.25e-22

Adenylate kinase;


Pssm-ID: 395329 [Multi-domain]  Cd Length: 184  Bit Score: 95.07  E-value: 1.25e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211   91 ILGPPASGKTTIAMWLCKHLNSNLITKESLLEREF---SRLSVEAKSYYQVYKI-PNSILVSLVQERLNEDDClRKGWIL 166
Cdd:pfam00406   1 LLGPPGAGKGTQAEKIVQKYGLPHLSTGDLLRAEIksgTELGKEAKEYMDKGELvPDEVVVGLVKERLEQNDC-KNGFLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211  167 DGIPERREQALMIQTL---GLAPKHVIVLNAPDTVLIERNVGKRIDPVTGEIYHTTFDWPPEPEIQN----RLRQPEGIS 239
Cdd:pfam00406  80 DGFPRTVPQAEALEELlerGIKLDYVIEFDVPDEVLVERLTGRRIHPNSGRSYHLEFNPPKVPGKDDvtgePLVQRSDDN 159

                         170
                  ....*....|...
gi 568914211  240 EiETAKKLLE-YH 251
Cdd:pfam00406 160 E-ETVKKRLEtYH 171
adk PRK02496
adenylate kinase; Provisional
 298-498 1.88e-22

adenylate kinase; Provisional


Pssm-ID: 179433 [Multi-domain]  Cd Length: 184  Bit Score: 94.43  E-value: 1.88e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211 298 KVLLCGPLGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSSFGELIQPFFEKRMTVPDSIITKVLADRMEQQDCiQKG 377
Cdd:PRK02496   3 RLIFLGPPGAGKGTQAVVLAEHLHIPHISTGDILRQAIKEQTPLGIKAQGYMDKGELVPDQLVLDLVQERLQQPDA-ANG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211 378 WVLHGFPRDLDQARMLN----SMGYNPNRVFFLSVPLDSILERLTLR-RTDpvtgerfhlmykppptievqvrllqnpkD 452
Cdd:PRK02496  82 WILDGFPRKVTQAAFLDellqEIGQSGERVVNLDVPDDVVVERLLARgRKD----------------------------D 133

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 568914211 453 SEEYIKLQTDLFYRNSGDLEQYY-DRAII--VNGDQDPYTVFEYIESGI 498
Cdd:PRK02496 134 TEEVIRRRLEVYREQTAPLIDYYrDRQKLltIDGNQSVEAVTTELKAAL 182
adk PRK00279
adenylate kinase; Reviewed
 88-278 8.38e-22

adenylate kinase; Reviewed


Pssm-ID: 234711 [Multi-domain]  Cd Length: 215  Bit Score: 93.68  E-value: 8.38e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211  88 KVVILGPPASGKTTIAMWLCKHLNsnlITKES---LLEREFSR---LSVEAKSYyqVYK---IPNSILVSLVQERLNEDD 158
Cdd:PRK00279   2 RLILLGPPGAGKGTQAKFIAEKYG---IPHIStgdMLRAAVKAgteLGKEAKSY--MDAgelVPDEIVIGLVKERLAQPD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211 159 ClRKGWILDGIPERREQAL----MIQTLGLAPKHVIVLNAPDTVLIERNVGKRIDPVTGEIYHTTFDWPPEPEIQNRLRQ 234
Cdd:PRK00279  77 C-KNGFLLDGFPRTIPQAEaldeMLKELGIKLDAVIEIDVPDEELVERLSGRRICPACGRTYHVKFNPPKVEGKCDVCGE 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 568914211 235 PEGISE---IETAKKLLE-YHRHIIRILPSYPK--ILKTISSDQPCVDVF 278
Cdd:PRK00279 156 ELIQRAddnEETVRKRLEvYHKQTAPLIDYYKKkgKLKKIDGTGSIDEVF 205
adk PRK02496
adenylate kinase; Provisional
 88-202 4.38e-18

adenylate kinase; Provisional


Pssm-ID: 179433 [Multi-domain]  Cd Length: 184  Bit Score: 82.10  E-value: 4.38e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211  88 KVVILGPPASGKTTIAMWLCKHLNSNLITKESLLE---REFSRLSVEAKSYY-QVYKIPNSILVSLVQERLNEDDClRKG 163
Cdd:PRK02496   3 RLIFLGPPGAGKGTQAVVLAEHLHIPHISTGDILRqaiKEQTPLGIKAQGYMdKGELVPDQLVLDLVQERLQQPDA-ANG 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 568914211 164 WILDGIPERREQA----LMIQTLGLAPKHVIVLNAPDTVLIER 202
Cdd:PRK02496  82 WILDGFPRKVTQAafldELLQEIGQSGERVVNLDVPDDVVVER 124
PRK14528 PRK14528
adenylate kinase; Provisional
 298-420 6.43e-18

adenylate kinase; Provisional


Pssm-ID: 172994 [Multi-domain]  Cd Length: 186  Bit Score: 81.60  E-value: 6.43e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211 298 KVLLCGPLGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSSFGELIQPFFEKRMTVPDSIITKVLADRMEQQDCiQKG 377
Cdd:PRK14528   3 NIIFMGPPGAGKGTQAKILCERLSIPQISTGDILREAVKNQTAMGIEAKRYMDAGDLVPDSVVIGIIKDRIREADC-KNG 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 568914211 378 WVLHGFPRDLDQAR----MLNSMGYNPNRVFFLSVPLDSILERLTLR 420
Cdd:PRK14528  82 FLLDGFPRTVEQADaldaLLKNEGKSIDKAINLEVPDGELLKRLLGR 128
PRK13808 PRK13808
adenylate kinase; Provisional
 298-420 2.44e-17

adenylate kinase; Provisional


Pssm-ID: 172341 [Multi-domain]  Cd Length: 333  Bit Score: 83.01  E-value: 2.44e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211 298 KVLLCGPLGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSSFGELIQPFFEKRMTVPDSIITKVLADRMEQQDCIQkG 377
Cdd:PRK13808   2 RLILLGPPGAGKGTQAQRLVQQYGIVQLSTGDMLRAAVAAGTPVGLKAKDIMASGGLVPDEVVVGIISDRIEQPDAAN-G 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 568914211 378 WVLHGFPRDLDQA----RMLNSMGYNPNRVFFLSVPLDSILERLTLR 420
Cdd:PRK13808  81 FILDGFPRTVPQAealdALLKDKQLKLDAVVELRVNEGALLARVETR 127
PTZ00088 PTZ00088
adenylate kinase 1; Provisional
 298-475 3.83e-17

adenylate kinase 1; Provisional


Pssm-ID: 240262 [Multi-domain]  Cd Length: 229  Bit Score: 80.61  E-value: 3.83e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211 298 KVLLCGPLGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSSFGELIQPFFEKRMTVPDSIITKVLADRMEQ-QDCIQK 376
Cdd:PTZ00088   8 KIVLFGAPGVGKGTFAEILSKKENLKHINMGNILREEIKAKTTIGKEIQKVVTSGNLVPDNLVIAIVKDEIAKvTDDCFK 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211 377 GWVLHGFPRDLDQARMLNSMGyNPNRVFFLSVPLDSILERLTLRRTDPVTGERFHLM------YKPPPTIEVQ------- 443
Cdd:PTZ00088  88 GFILDGFPRNLKQCKELGKIT-NIDLFVNIYLPRNILIKKLLGRRICNTCNRNFNIAhirsdpYDMPPILPPAdcegckg 166

                        170       180       190
                 ....*....|....*....|....*....|...
gi 568914211 444 -VRLLQNPKDSEEYIKLQTDLFYRNSGDLEQYY 475
Cdd:PTZ00088 167 nPKLQKRSDDTEEIVAHRLNTYESTNSPIIQFF 199
DD_AK8 cd22979
dimerization/docking (D/D) domain found in adenylate kinase isoenzyme 8 (AK8) and similar ...
 9-52 1.48e-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: 70.57  E-value: 1.48e-15
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 568914211   9 RIPPEMPQYGEDYYIFEMMQNMLEQLLIHQPEDPISFMITHLRR 52
Cdd:cd22979    1 EIPPEFAAYAEKHRIFELFQDLLKQLLIHKPEDPLQFLIDYLQK 44
aden_kin_iso1 TIGR01360
adenylate kinase, isozyme 1 subfamily; Members of this family are adenylate kinase, EC 2.7.4.3. ...
 303-491 6.31e-15

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: 72.93  E-value: 6.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211  303 GPlGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSSFGELIQPFFEKRMTVPDSIITKVLADRMEQQDCIQKGWVLHG 382
Cdd:TIGR01360  11 GP-GSGKGTQCEKIVEKYGFTHLSTGDLLRAEVASGSERGKQLQAIMESGDLVPLDTVLDLLKDAMVAALGTSKGFLIDG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211  383 FPRDLDQARMLNSMGYNPNRVFFLSVPLDSILERLTLR-----RTDpvtgerfhlmykppptievqvrllqnpkDSEEYI 457
Cdd:TIGR01360  90 YPREVKQGEEFERRIGPPTLVLYFDCSEDTMVKRLLKRaetsgRVD----------------------------DNEKTI 141

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 568914211  458 KLQTDLFYRNSGDLEQYYDRAIIV---NGDQDPYTVF 491
Cdd:TIGR01360 142 KKRLETYYKATEPVIAYYETKGKLrkiNAEGTVDDVF 178
PRK14527 PRK14527
adenylate kinase; Provisional
 299-423 8.60e-15

adenylate kinase; Provisional


Pssm-ID: 237745 [Multi-domain]  Cd Length: 191  Bit Score: 72.90  E-value: 8.60e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211 299 VLLCGPLGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSSFGELIQPFFEKRMTVPDSIITKVLADRMEQQDCIQKgw 378
Cdd:PRK14527   9 VIFLGPPGAGKGTQAERLAQELGLKKLSTGDILRDHVARGTELGQRAKPIMEAGDLVPDELILALIRDELAGMEPVRV-- 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568914211 379 VLHGFPRDLDQA----RMLNSMGYNPNRVFFLSVPLDSILERLTLR-----RTD 423
Cdd:PRK14527  87 IFDGFPRTLAQAealdRLLEELGARLLAVVLLEVPDEELIRRIVERarqegRSD 140
PRK14532 PRK14532
adenylate kinase; Provisional
 299-475 2.20e-14

adenylate kinase; Provisional


Pssm-ID: 184729 [Multi-domain]  Cd Length: 188  Bit Score: 71.39  E-value: 2.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211 299 VLLCGPLGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSSFGELIQPFFEKRMTVPDSIITKVLADRMEQQDCiQKGW 378
Cdd:PRK14532   3 LILFGPPAAGKGTQAKRLVEERGMVQLSTGDMLRAAIASGSELGQRVKGIMDRGELVSDEIVIALIEERLPEAEA-AGGA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211 379 VLHGFPRDLDQARMLNSM----GYNPNRVFFLSVPLDSILERLTlrrtdpvtgERFhlmykppptiEVQVRllqnPKDSE 454
Cdd:PRK14532  82 IFDGFPRTVAQAEALDKMlasrGQKIDVVIRLKVDDEALIERIV---------KRF----------EEQGR----PDDNP 138

                        170       180
                 ....*....|....*....|.
gi 568914211 455 EYIKLQTDLFYRNSGDLEQYY 475
Cdd:PRK14532 139 EVFVTRLDAYNAQTAPLLPYY 159
PRK14528 PRK14528
adenylate kinase; Provisional
 88-208 2.64e-14

adenylate kinase; Provisional


Pssm-ID: 172994 [Multi-domain]  Cd Length: 186  Bit Score: 71.20  E-value: 2.64e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211  88 KVVILGPPASGKTTIAMWLCKHLNSNLITKESLLE---REFSRLSVEAKSYYQVYK-IPNSILVSLVQERLNEDDClRKG 163
Cdd:PRK14528   3 NIIFMGPPGAGKGTQAKILCERLSIPQISTGDILReavKNQTAMGIEAKRYMDAGDlVPDSVVIGIIKDRIREADC-KNG 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 568914211 164 WILDGIPERREQA----LMIQTLGLAPKHVIVLNAPDTVLIERNVGKRI 208
Cdd:PRK14528  82 FLLDGFPRTVEQAdaldALLKNEGKSIDKAINLEVPDGELLKRLLGRAE 130
PRK14526 PRK14526
adenylate kinase; Provisional
 298-482 2.92e-14

adenylate kinase; Provisional


Pssm-ID: 172992 [Multi-domain]  Cd Length: 211  Bit Score: 71.81  E-value: 2.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211 298 KVLLCGPLGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSSFGELIQPFFEKRMTVPDSIITKVLADRMEQQDCiQKG 377
Cdd:PRK14526   2 KLVFLGPPGSGKGTIAKILSNELNYYHISTGDLFRENILNSTPLGKEIKQIVENGQLVPDSITIKIVEDKINTIKN-NDN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211 378 WVLHGFPRDLDQARMLNSMGYNPNRVFFLsVPLDSILERLTLRRTDPVTGERFHLMYKPPPTIEV----QVRLLQNPKDS 453
Cdd:PRK14526  81 FILDGFPRNINQAKALDKFLPNIKIINFL-IDEELLIKRLSGRRICKSCNNIFNIYTLPTKEKGIcdvcKGDLYQRKDDK 159

                        170       180
                 ....*....|....*....|....*....
gi 568914211 454 EEYIKLQTDLFYRNSGDLEQYYDRAIIVN 482
Cdd:PRK14526 160 EESLKTRLQEYKLQTKPLIEFYSKCNRLN 188
UMP_CMP_kin_fam TIGR01359
UMP-CMP kinase family; This subfamily of the adenylate kinase superfamily contains examples of ...
 299-496 1.64e-13

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: 68.94  E-value: 1.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211  299 VLLC-GPLGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSS-FGELIQPFFEKRMTVPdSIITKVLADRMEQQDCIQK 376
Cdd:TIGR01359   1 VVFVlGGPGSGKGTQCAKIVENFGFTHLSAGDLLRAEIKREGSeNGSLIESYIKEGKIVP-SEVTVELLKKAIQEDGSSK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211  377 GWVLHGFPR---DLDQARMLNSMGYNPNRVFFLSVPLDSILERLTLR-----RTDpvtgerfhlmyKPPPTIEVQVRLLQ 448
Cdd:TIGR01359  80 KFLIDGFPRneeNLEAWEKLMDNKVNFKFVLFFDCPEETMIKRLLKRgqtsgRVD-----------DNIETLKKRFRTYN 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 568914211  449 NpkDSEEYIKlqtdlFYRNSGDLeqyydraIIVNGDQDPYTVFEYIES 496
Cdd:TIGR01359 149 E--ETLPIIE-----HFENKGKV-------KEINAEGSVEEVFEDVEK 182
PRK14529 PRK14529
adenylate kinase; Provisional
 299-393 3.67e-13

adenylate kinase; Provisional


Pssm-ID: 237746 [Multi-domain]  Cd Length: 223  Bit Score: 68.59  E-value: 3.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211 299 VLLCGPLGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSSFGELIQPFFEKRMTVPDSIITKVLADRMEQQDciQKGW 378
Cdd:PRK14529   3 ILIFGPNGSGKGTQGALVKKKYDLAHIESGAIFREHIGGGTELGKKAKEYIDRGDLVPDDITIPMILETLKQDG--KNGW 80

                         90
                 ....*....|....*
gi 568914211 379 VLHGFPRDLDQARML 393
Cdd:PRK14529  81 LLDGFPRNKVQAEKL 95
PRK14531 PRK14531
adenylate kinase; Provisional
 298-423 1.07e-12

adenylate kinase; Provisional


Pssm-ID: 172997 [Multi-domain]  Cd Length: 183  Bit Score: 66.37  E-value: 1.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211 298 KVLLCGPLGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSSFGELIQPFFEKRMTVPDSIITKVLADRMeqQDCIQKG 377
Cdd:PRK14531   4 RLLFLGPPGAGKGTQAARLCAAHGLRHLSTGDLLRSEVAAGSALGQEAEAVMNRGELVSDALVLAIVESQL--KALNSGG 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568914211 378 WVLHGFPRDLDQAR----MLNSMGYNPNRVFFLSVPLDSILERLTLR-RTD 423
Cdd:PRK14531  82 WLLDGFPRTVAQAEalepLLEELKQPIEAVVLLELDDAVLIERLLARgRAD 132
PRK14530 PRK14530
adenylate kinase; Provisional
 87-249 1.16e-12

adenylate kinase; Provisional


Pssm-ID: 237747 [Multi-domain]  Cd Length: 215  Bit Score: 67.12  E-value: 1.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211  87 PKVVILGPPASGKTTIAMWLCKHLNSNLITKESLL----EREFSRLSVE---AKSYYQVYK-IPNSILVSLVQERLNEDD 158
Cdd:PRK14530   4 PRILLLGAPGAGKGTQSSNLAEEFGVEHVTTGDALrankQMDISDMDTEydtPGEYMDAGElVPDAVVNEIVEEALSDAD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211 159 clrkGWILDGIPERREQALMIQTLgLAPKHVIVLNAPDTVLIERNVGKRIDPVTGEIYHTTFDWPPEPEIQN----RLRQ 234
Cdd:PRK14530  84 ----GFVLDGYPRNLEQAEYLESI-TDLDVVLYLDVSEEELVDRLTGRRVCPDCGANYHVEFNQPEEEGVCDecggELIQ 158

                        170
                 ....*....|....*
gi 568914211 235 PEGISEiETAKKLLE 249
Cdd:PRK14530 159 RDDDTE-ETVRERLD 172
AAA_17 pfam13207
AAA domain;
303-422 1.21e-12

AAA domain;


Pssm-ID: 463810 [Multi-domain]  Cd Length: 136  Bit Score: 64.95  E-value: 1.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211  303 GPLGSGKRLQATLLAQKYGLVNISCGQLLKEavAAKSSFGELIQPFFEKRMTVPDSIITKVLADRMEqQDCIQKGWVLHG 382
Cdd:pfam13207   2 GVPGSGKTTQLKKLAEKLGFPHISAGDLLRE--EAKERGLVEDRDEMRKLPLEPQKELQKLAAERIA-EEAGEGGVIVDG 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 568914211  383 FPRDLDQARMLNSM------GYNPNRVFFLSVPLDSILERLTLRRT 422
Cdd:pfam13207  79 HPRIKTPAGYLPGLpvevlrELKPDAIILLEADPEEILERRLKDRT 124
PLN02674 PLN02674
adenylate kinase
 88-277 1.11e-10

adenylate kinase


Pssm-ID: 178279 [Multi-domain]  Cd Length: 244  Bit Score: 61.82  E-value: 1.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211  88 KVVILGPPASGKTTIA------MWLCkHLNSNLITKESLLERefSRLSVEAKSYYQVYK-IPNSILVSLVQERLNEDDCl 160
Cdd:PLN02674  33 RLILIGPPGSGKGTQSpiikdeYCLC-HLATGDMLRAAVAAK--TPLGIKAKEAMDKGElVSDDLVVGIIDEAMKKPSC- 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211 161 RKGWILDGIPERREQAL----MIQTLGLAPKHVIVLNAPDTVLIERNVGKRIDPVTGEIYHTTFDWPPEPEIQNRLRQPE 236
Cdd:PLN02674 109 QKGFILDGFPRTVVQAQkldeMLAKQGAKIDKVLNFAIDDAILEERITGRWIHPSSGRTYHTKFAPPKVPGVDDVTGEPL 188

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 568914211 237 GISEIETA----KKLLEYHRHIIRILPSYPK--ILKTISSDQPCVDV 277
Cdd:PLN02674 189 IQRKDDTAavlkSRLEAFHKQTEPVIDYYAKkgVVANLHAEKPPKEV 235
DD_TEX55-like cd22961
dimerization/docking (D/D) domain found in the testis-specific expressed protein 55 (TEX55) ...
 12-52 1.81e-10

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: 55.89  E-value: 1.81e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 568914211  12 PEMPQYGEDYYIFEMMQNMLEQLLIHQPEDPISFMITHLRR 52
Cdd:cd22961    2 EDAEEYLEKHKIPELFESLLTALLIEKPEDPIEFLIDKLQQ 42
PTZ00088 PTZ00088
adenylate kinase 1; Provisional
 88-224 1.60e-08

adenylate kinase 1; Provisional


Pssm-ID: 240262 [Multi-domain]  Cd Length: 229  Bit Score: 55.19  E-value: 1.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211  88 KVVILGPPASGKTTIAMWLCKHLNSNLITKESLLEREFSRLSVEAKSYYQVYK----IPNSILVSLVQERL-NEDDCLRK 162
Cdd:PTZ00088   8 KIVLFGAPGVGKGTFAEILSKKENLKHINMGNILREEIKAKTTIGKEIQKVVTsgnlVPDNLVIAIVKDEIaKVTDDCFK 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568914211 163 GWILDGIPERREQALMIQTLGlAPKHVIVLNAPDTVLIERNVGKRIDPVTGEIYH------TTFDWPP 224
Cdd:PTZ00088  88 GFILDGFPRNLKQCKELGKIT-NIDLFVNIYLPRNILIKKLLGRRICNTCNRNFNiahirsDPYDMPP 154
Kti12 COG4088
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ...
 89-250 2.04e-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: 53.96  E-value: 2.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211  89 VVILGPPASGKTTIAMWLCKHLNSNLITKESLLEREFSRLSVEA----KSYYQVYKipnSILVSLVQERLNeddcLRKGW 164
Cdd:COG4088    7 LILTGPPGSGKTTFAKALAQRLYAEGIAVALLHSDDFRRFLVNEsfpkETYEEVVE---DVRTTTADNALD----NGYSV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211 165 ILDGIPERREQALMIQTLGL--APKHVIVLNAPDTVLIERNV--GKRIDPVTGEIYHTTFDWPPEPEIQNRLRQPEGISE 240
Cdd:COG4088   80 IVDGTFYYRSWQRDFRNLAKhkAPIHIIYLKAPLETALRRNRerGEPIPERVIARMYRKFDKPGTKDRPDLVIDTTEDSV 159

                        170
                 ....*....|
gi 568914211 241 IETAKKLLEY 250
Cdd:COG4088  160 SETLDAILKA 169
PRK14527 PRK14527
adenylate kinase; Provisional
 82-206 2.13e-08

adenylate kinase; Provisional


Pssm-ID: 237745 [Multi-domain]  Cd Length: 191  Bit Score: 54.03  E-value: 2.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211  82 IRIDVPKVVI-LGPPASGKTTIAMWLCKHLNSNLITKESLLEREFSR---LSVEAKSYYQVYK-IPNSILVSLVQERLNE 156
Cdd:PRK14527   1 MTQTKNKVVIfLGPPGAGKGTQAERLAQELGLKKLSTGDILRDHVARgteLGQRAKPIMEAGDlVPDELILALIRDELAG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568914211 157 DDCLRKgwILDGIPERREQA----LMIQTLGLAPKHVIVLNAPDTVLIERNVGK 206
Cdd:PRK14527  81 MEPVRV--IFDGFPRTLAQAealdRLLEELGARLLAVVLLEVPDEELIRRIVER 132
AAA_17 pfam13207
AAA domain;
92-202 3.20e-08

AAA domain;


Pssm-ID: 463810 [Multi-domain]  Cd Length: 136  Bit Score: 52.24  E-value: 3.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211   92 LGPPASGKTTIAMWLCKHLNSNLITKESLLEREFSRLS-VEAKSYYQ-VYKIPNSILVSLVQERLNEdDCLRKGWILDGI 169
Cdd:pfam13207   1 TGVPGSGKTTQLKKLAEKLGFPHISAGDLLREEAKERGlVEDRDEMRkLPLEPQKELQKLAAERIAE-EAGEGGVIVDGH 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 568914211  170 PERREQA-----LMIQTL-GLAPKHVIVLNAPDTVLIER 202
Cdd:pfam13207  80 PRIKTPAgylpgLPVEVLrELKPDAIILLEADPEEILER 118
PRK14526 PRK14526
adenylate kinase; Provisional
 88-251 4.51e-08

adenylate kinase; Provisional


Pssm-ID: 172992 [Multi-domain]  Cd Length: 211  Bit Score: 53.70  E-value: 4.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211  88 KVVILGPPASGKTTIAMWLCKHLNSNLITKESLLEREFSRLSVEAKSYYQVYK----IPNSILVSLVQERLNEDDClRKG 163
Cdd:PRK14526   2 KLVFLGPPGSGKGTIAKILSNELNYYHISTGDLFRENILNSTPLGKEIKQIVEngqlVPDSITIKIVEDKINTIKN-NDN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211 164 WILDGIPERREQALMIQTLgLAPKHVIVLNAPDTVLIERNVGKRIDPVTGEIYHTTFDWPPEPEI----QNRLRQPEGIS 239
Cdd:PRK14526  81 FILDGFPRNINQAKALDKF-LPNIKIINFLIDEELLIKRLSGRRICKSCNNIFNIYTLPTKEKGIcdvcKGDLYQRKDDK 159

                        170
                 ....*....|..
gi 568914211 240 EIETAKKLLEYH 251
Cdd:PRK14526 160 EESLKTRLQEYK 171
DD_EFCAB10 cd22976
dimerization/docking (D/D) domain found in EF-hand calcium-binding domain-containing protein ...
 16-52 1.02e-07

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


Pssm-ID: 438545  Cd Length: 47  Bit Score: 48.25  E-value: 1.02e-07
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 568914211  16 QYGEDYYIFEMMQNMLEQLLIHQPEDPISFMITHLRR 52
Cdd:cd22976    6 EYLEKHKIPELFENLTSLLLYHRPEDPKAFLIEQLEK 42
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 89-206 3.54e-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: 49.62  E-value: 3.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211   89 VVIL-GPPASGKTTIAMWLCKHLNSNLITKESLLEREFSRLsVEAKSYYQvykipnsILVSLVQERLNE--DDCLRKGW- 164
Cdd:pfam13671   1 LILLvGLPGSGKSTLARRLLEELGAVRLSSDDERKRLFGEG-RPSISYYT-------DATDRTYERLHElaRIALRAGRp 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 568914211  165 -ILD-GIPERREQALMIQ---TLGlAPKHVIVLNAPDTVLIERNVGK 206
Cdd:pfam13671  73 vILDaTNLRRDERARLLAlarEYG-VPVRIVVFEAPEEVLRERLAAR 118
AAA_18 pfam13238
AAA domain;
89-202 3.98e-07

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 48.96  E-value: 3.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211   89 VVILGPPASGKTTIAMWLCKHLNSNLITKESLLEREfsrLSVEAKSYYQVYKIPNSILVSLVQERLNEDDCLRKG--WIL 166
Cdd:pfam13238   1 ILITGTPGVGKTTLAKELSKRLGFGDNVRDLALENG---LVLGDDPETRESKRLDEDKLDRLLDLLEENAALEEGgnLII 77

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 568914211  167 DGIPERREQALMIQtlglapKHVIVLNAPDTVLIER 202
Cdd:pfam13238  78 DGHLAELEPERAKD------LVGIVLRASPEELLER 107
UMP_CMP_kin_fam TIGR01359
UMP-CMP kinase family; This subfamily of the adenylate kinase superfamily contains examples of ...
 89-278 5.11e-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: 5.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211   89 VVILGPPASGKTTIAMWLCKHLNSNLITKESLLEREFSRLSVEAKSYYQVY----KI-PNSILVSLVQERLNEDDClRKG 163
Cdd:TIGR01359   2 VFVLGGPGSGKGTQCAKIVENFGFTHLSAGDLLRAEIKREGSENGSLIESYikegKIvPSEVTVELLKKAIQEDGS-SKK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211  164 WILDGIP---ERREQALMIQTLGLAPKHVIVLNAPDTVLIERnvgkridpvtgeiyhttfdwppepeIQNRlRQPEGISE 240
Cdd:TIGR01359  81 FLIDGFPrneENLEAWEKLMDNKVNFKFVLFFDCPEETMIKR-------------------------LLKR-GQTSGRVD 134

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 568914211  241 --IETAKKLLE-YHRHIIRILPSYPK--ILKTISSDQPCVDVF 278
Cdd:TIGR01359 135 dnIETLKKRFRtYNEETLPIIEHFENkgKVKEINAEGSVEEVF 177
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
89-233 5.85e-07

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 49.53  E-value: 5.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211  89 VVILGPPASGKTTIAMWLCKHLNSNLITKESLLEREFSRLSVEAKSYYQVykipnsilVSLVQERLNE--DDCLRKGW-- 164
Cdd:COG0645    2 ILVCGLPGSGKSTLARALAERLGAVRLRSDVVRKRLFGAGLAPLERSPEA--------TARTYARLLAlaRELLAAGRsv 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568914211 165 ILDG---IPERREQALMI-QTLGlAPKHVIVLNAPDTVLIE----RNVGKRIDPVTGEIYH--TTFDWPPEPEIQNRLR 233
Cdd:COG0645   74 ILDAtflRRAQREAFRALaEEAG-APFVLIWLDAPEEVLRErleaRNAEGGDSDATWEVLErqLAFEEPLTEDEGFLLV 151
PRK14529 PRK14529
adenylate kinase; Provisional
 89-208 2.72e-06

adenylate kinase; Provisional


Pssm-ID: 237746 [Multi-domain]  Cd Length: 223  Bit Score: 48.56  E-value: 2.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211  89 VVILGPPASGKTTIAMWLCK-----HLNSNLITKESLleREFSRLSVEAKSYYQVYK-IPNSILVSLVQERLNEDDclRK 162
Cdd:PRK14529   3 ILIFGPNGSGKGTQGALVKKkydlaHIESGAIFREHI--GGGTELGKKAKEYIDRGDlVPDDITIPMILETLKQDG--KN 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 568914211 163 GWILDGIPERREQAL----MIQTLGLAPKHVIVLNAPDTVLIERNVGKRI 208
Cdd:PRK14529  79 GWLLDGFPRNKVQAEklweALQKEGMKLDYVIEILLPREVAKNRIMGRRL 128
DD_TEX55 cd22975
dimerization/docking (D/D) domain found in testis-specific expressed protein 55 (TEX55) and ...
 16-47 2.71e-05

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: 41.40  E-value: 2.71e-05
                         10        20        30
                 ....*....|....*....|....*....|..
gi 568914211  16 QYGEDYYIFEMMQNMLEQLLIHQPEDPISFMI 47
Cdd:cd22975    9 KYLEKHNILQLFQELTAGLVYERPDDPIQFMI 40
PRK14531 PRK14531
adenylate kinase; Provisional
 88-202 4.07e-05

adenylate kinase; Provisional


Pssm-ID: 172997 [Multi-domain]  Cd Length: 183  Bit Score: 44.42  E-value: 4.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211  88 KVVILGPPASGKTTIAMWLC-----KHLNSNlitkeSLLEREF---SRLSVEAKSYYQVYKIPNSILV-SLVQERLNEDD 158
Cdd:PRK14531   4 RLLFLGPPGAGKGTQAARLCaahglRHLSTG-----DLLRSEVaagSALGQEAEAVMNRGELVSDALVlAIVESQLKALN 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 568914211 159 clRKGWILDGIPERREQA----LMIQTLGLAPKHVIVLNAPDTVLIER 202
Cdd:PRK14531  79 --SGGWLLDGFPRTVAQAealePLLEELKQPIEAVVLLELDDAVLIER 124
DD_CrRSP_unchar cd22964
dimerization/docking (D/D) domain of an uncharacterized subunit found in Chlamydomonas ...
 10-52 3.10e-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: 38.36  E-value: 3.10e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 568914211  10 IPPEMPQYGEDYYIFEMMQNMLEQLLIHQPEDPISFMITHLRR 52
Cdd:cd22964    1 KAEEKKEYLQQKVINPILEQLVTDLLQEKPEDPVPFMIQWLRK 43
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
66-182 3.86e-04

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 43.25  E-value: 3.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211  66 PHGVLPAPRAQESLKSIRIDVPKVVILGPPASGKTTiamwLCKHLNSNLITKESLLEREFSrLSVEAKSyyqvYKIPNSI 145
Cdd:COG5635  160 PLNLLERIESLKRLELLEAKKKRLLILGEPGSGKTT----LLRYLALELAERYLDAEDPIP-ILIELRD----LAEEASL 230

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568914211 146 LvSLVQERLNEDDCLRKGW------------ILDG---IPERREQALMIQTL 182
Cdd:COG5635  231 E-DLLAEALEKRGGEPEDAlerllrngrlllLLDGldeVPDEADRDEVLNQL 281
DD_R_PKA_DPY30-like cd22957
dimerization/docking (D/D) domains found in the cAMP-dependent protein kinase regulatory ...
 25-50 5.62e-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: 37.10  E-value: 5.62e-04
                         10        20
                 ....*....|....*....|....*.
gi 568914211  25 EMMQNMLEQLLIHQPEDPISFMITHL 50
Cdd:cd22957    1 ELLQDAVAKLLEERPEDPVEFLAEYF 26
NadR3 COG3172
Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase ...
 85-133 1.38e-03

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: 1.38e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 568914211  85 DVPKVVILGPPASGKTTIAMWLCKHLNSNLItkeslleREFSRLSVEAK 133
Cdd:COG3172    7 FVKKIVLLGAESTGKTTLARALAAHYNTPWV-------PEYGREYLEEK 48
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 77-116 5.49e-03

ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 38.83  E-value: 5.49e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 568914211  77 ESLKSIRIDVPKVVIL-GPPASGKTTIAMWLCKHLNSNLIT 116
Cdd:COG1222  102 ELFRKYGIEPPKGVLLyGPPGTGKTLLAKAVAGELGAPFIR 142
rho TIGR00767
transcription termination factor Rho; This RNA helicase, the transcription termination factor ...
 188-260 5.91e-03

transcription termination factor Rho; This RNA helicase, the transcription termination factor Rho, occurs in nearly all bacteria but is missing from the Cyanobacteria, the Mollicutes (Mycoplasmas), and various Lactobacillales including Streptococcus. It is also missing, of course, from the Archaea, which also lack Nus factors. Members of this family from Micrococcus luteus, Mycobacterium tuberculosis, and related species have a related but highly variable long, highly charged insert near the amino end. Members of this family differ in the specificity of RNA binding. [Transcription, Transcription factors]


Pssm-ID: 162030 [Multi-domain]  Cd Length: 415  Bit Score: 38.90  E-value: 5.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914211  188 HVIVLNAPDTVLIERNVGKRIDPVT-------GEIYHTTFDWPPEPEIQnrlrqpegISE--IETAKKLLEYHRHIIRIL 258
Cdd:TIGR00767 190 QAITRNHPEVELIVLLIDERPEEVTdmqrsvkGEVVASTFDEPASRHVQ--------VAEmvIEKAKRLVEHKKDVVILL 261


                  ..
gi 568914211  259 PS 260
Cdd:TIGR00767 262 DS 263
DD_TbAK-like cd22981
dimerization/docking (D/D) domain found in Trypanosoma brucei adenylate kinase (AK) and ...
 16-53 7.06e-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: 34.70  E-value: 7.06e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 568914211  16 QYGEDYYIFEMMQNMLEQLLIHQPEDPISFMITHLRRN 53
Cdd:cd22981    7 KYLKEKNIPQLFEFLLRHLLLDKPENPLEYLHDLLERP 44
cyt_kin_arch TIGR02173
cytidylate kinase, putative; Proteins in this family are believed to be cytidylate kinase. ...
 88-116 7.82e-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: 37.40  E-value: 7.82e-03
                          10        20
                  ....*....|....*....|....*....
gi 568914211   88 KVVILGPPASGKTTIAMWLCKHLNSNLIT 116
Cdd:TIGR02173   2 IITISGPPGSGKTTVAKILAEKLSLKLIS 30
 
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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