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Conserved domains on  [gi|1720400556|ref|XP_030107902|]
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adenylate kinase 8 isoform X5 [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 ...
 269-461 1.67e-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: 178.20  E-value: 1.67e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 269 KVLLCGPLGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSSFGELIQPFFEKRMTVPDSIITKVLADRMEQQDCiQKG 348
Cdd:cd01428     1 RILLLGPPGSGKGTQAERLAKKYGLPHISTGDLLREEIASGTELGKKAKEYIDSGKLVPDEIVIKLLKERLKKPDC-KKG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 349 WVLHGFPRDLDQARMLNSM---GYNPNRVFFLSVPLDSILERLTLRRTDPVTGERFHLMYKPpptiEVQVRLLQNPKDSE 425
Cdd:cd01428    80 FILDGFPRTVDQAEALDELldeGIKPDKVIELDVPDEVLIERILGRRICPVSGRVYHLGKDD----VTGEPLSQRSDDNE 155

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1720400556 426 EYIKLQTDLFYRNSGDLEQYYDRA---IIVNGDQDPYTV 461
Cdd:cd01428   156 ETIKKRLEVYKEQTAPLIDYYKKKgklVEIDGSGDIDEV 194
ADK cd01428
Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine ...
 59-248 2.51e-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: 121.96  E-value: 2.51e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556  59 KVVILGPPASGKTTIAMWLCKHLNSNLITKESLLEREF---SRLSVEAKSYYQVYK-IPNSILVSLVQERLNEDDClRKG 134
Cdd:cd01428     1 RILLLGPPGSGKGTQAERLAKKYGLPHISTGDLLREEIasgTELGKKAKEYIDSGKlVPDEIVIKLLKERLKKPDC-KKG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 135 WILDGIPERREQALMIQTL---GLAPKHVIVLNAPDTVLIERNVGKRIDPVTGEIYHTTFDWPPEPEIQNRLRQpegisE 211
Cdd:cd01428    80 FILDGFPRTVDQAEALDELldeGIKPDKVIELDVPDEVLIERILGRRICPVSGRVYHLGKDDVTGEPLSQRSDD-----N 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1720400556 212 IETAKKLLE-YHRHIIRILPSYPK--ILKTISSDQPCVDV 248
Cdd:cd01428   155 EETIKKRLEvYKEQTAPLIDYYKKkgKLVEIDGSGDIDEV 194
DD_AK8 cd22979
dimerization/docking (D/D) domain found in adenylate kinase isoenzyme 8 (AK8) and similar ...
 9-52 1.33e-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: 1.33e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1720400556   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 ...
 269-461 1.67e-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: 178.20  E-value: 1.67e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 269 KVLLCGPLGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSSFGELIQPFFEKRMTVPDSIITKVLADRMEQQDCiQKG 348
Cdd:cd01428     1 RILLLGPPGSGKGTQAERLAKKYGLPHISTGDLLREEIASGTELGKKAKEYIDSGKLVPDEIVIKLLKERLKKPDC-KKG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 349 WVLHGFPRDLDQARMLNSM---GYNPNRVFFLSVPLDSILERLTLRRTDPVTGERFHLMYKPpptiEVQVRLLQNPKDSE 425
Cdd:cd01428    80 FILDGFPRTVDQAEALDELldeGIKPDKVIELDVPDEVLIERILGRRICPVSGRVYHLGKDD----VTGEPLSQRSDDNE 155

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1720400556 426 EYIKLQTDLFYRNSGDLEQYYDRA---IIVNGDQDPYTV 461
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 ...
 269-467 1.84e-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: 1.84e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 269 KVLLCGPLGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSSFGELIQPFFEKRMTVPDSIITKVLADRMEQQDCIQKG 348
Cdd:TIGR01351   1 RLVLLGPPGSGKGTQAKRIAEKYGLPHISTGDLLRAEIKAGTPLGKKAKEYMEKGELVPDEIVNQLVKERLTQNDDNENG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 349 WVLHGFPRDLDQARMLNSMGYNPNR-VFFLSVPLDSILERLTLRRTDPVTGERFHLMYKPPPTIEVQV----RLLQNPKD 423
Cdd:TIGR01351  81 FILDGFPRTLSQAEALDALLEEPIDaVIELDVPDEELVERLSGRRICPSCGRVYHLKFNPPKVPGCDDctgeLLVQREDD 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1720400556 424 SEEYIKLQTDLFYRNSGDLEQYYDRAII---VNGDQDPYTVFEYIES 467
Cdd:TIGR01351 161 TEEVVKKRLEVYKEQTEPLIDYYKKRGIlvqIDGNGPIDEVWKRILE 207
Adk COG0563
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ...
 269-469 2.67e-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: 2.67e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 269 KVLLCGPLGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSSFGELIQPFFEKRMTVPDSIITKVLADRMEQQDCiQKG 348
Cdd:COG0563     2 RIILLGPPGAGKGTQAKRLAEKYGIPHISTGDMLRAAVKAGTELGKKAKEYMDAGELVPDEIVIGLVKERLAQPDC-ANG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 349 WVLHGFPRDLDQA----RMLNSMGYNPNRVFFLSVPLDSILERLTLRRTDPVTGERFHLMYKPPPTIEV----QVRLLQN 420
Cdd:COG0563    81 FILDGFPRTVAQAealdELLAELGIKLDAVIELDVDDEELVERLSGRRVCPNCGATYHVKFNPPKVEGVcdkcGGELVQR 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720400556 421 PKDSEEYIKLQTDLFYRNSGDLEQYYDRA---IIVNGDQDPYTVFEYIESGI 469
Cdd:COG0563   161 ADDNEETVRKRLEVYHEQTAPLIDYYRKKgklVEIDGEGSIEEVTADILAIL 212
ADK pfam00406
Adenylate kinase;
272-446 8.67e-40

Adenylate kinase;


Pssm-ID: 395329 [Multi-domain]  Cd Length: 184  Bit Score: 141.68  E-value: 8.67e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 272 LCGPLGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSSFGELIQPFFEKRMTVPDSIITKVLADRMEQQDCiQKGWVL 351
Cdd:pfam00406   1 LLGPPGAGKGTQAEKIVQKYGLPHLSTGDLLRAEIKSGTELGKEAKEYMDKGELVPDEVVVGLVKERLEQNDC-KNGFLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 352 HGFPRDLDQARMLNSM---GYNPNRVFFLSVPLDSILERLTLRRTDPVTGERFHLMYKPPPTIEVQV----RLLQNPKDS 424
Cdd:pfam00406  80 DGFPRTVPQAEALEELlerGIKLDYVIEFDVPDEVLVERLTGRRIHPNSGRSYHLEFNPPKVPGKDDvtgePLVQRSDDN 159

                         170       180
                  ....*....|....*....|..
gi 1720400556 425 EEYIKLQTDLFYRNSGDLEQYY 446
Cdd:pfam00406 160 EETVKKRLETYHKQTKPLIDYY 181
PLN02842 PLN02842
nucleotide kinase
 271-467 3.73e-38

nucleotide kinase


Pssm-ID: 178435 [Multi-domain]  Cd Length: 505  Bit Score: 145.39  E-value: 3.73e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 271 LLCGPLGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSSFGELIQPFFEKRMTVPDSIITKVLADRMEQQDCIQKGWV 350
Cdd:PLN02842    1 MISGAPASGKGTQCELIVHKFGLVHISTGDLLRAEVSAGTDIGKRAKEFMNSGRLVPDEIVIAMVTGRLSREDAKEKGWL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 351 LHGFPRDLDQARMLNSMGYNPNRVFFLSVPLDSILERLTLRRTDPVTGERFHLMYKPPPTIEVQVRLLQNPKDSEEYIKL 430
Cdd:PLN02842   81 LDGYPRSFAQAQSLEKLKIRPDIFILLDVPDEILIDRCVGRRLDPVTGKIYHIKNFPPESEEIKARLITRPDDTEEKVKA 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1720400556 431 QTDLFYRNSGD-LEQYYDRAIIVNGDQDPYTVFEYIES 467
Cdd:PLN02842  161 RLQIYKKNAEAiLSTYSDIMVKIDGNRPKEVVFEEISS 198
ADK cd01428
Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine ...
 59-248 2.51e-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: 121.96  E-value: 2.51e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556  59 KVVILGPPASGKTTIAMWLCKHLNSNLITKESLLEREF---SRLSVEAKSYYQVYK-IPNSILVSLVQERLNEDDClRKG 134
Cdd:cd01428     1 RILLLGPPGSGKGTQAERLAKKYGLPHISTGDLLREEIasgTELGKKAKEYIDSGKlVPDEIVIKLLKERLKKPDC-KKG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 135 WILDGIPERREQALMIQTL---GLAPKHVIVLNAPDTVLIERNVGKRIDPVTGEIYHTTFDWPPEPEIQNRLRQpegisE 211
Cdd:cd01428    80 FILDGFPRTVDQAEALDELldeGIKPDKVIELDVPDEVLIERILGRRICPVSGRVYHLGKDDVTGEPLSQRSDD-----N 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1720400556 212 IETAKKLLE-YHRHIIRILPSYPK--ILKTISSDQPCVDV 248
Cdd:cd01428   155 EETIKKRLEvYKEQTAPLIDYYKKkgKLVEIDGSGDIDEV 194
PLN02842 PLN02842
nucleotide kinase
 61-249 7.59e-30

nucleotide kinase


Pssm-ID: 178435 [Multi-domain]  Cd Length: 505  Bit Score: 121.89  E-value: 7.59e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556  61 VILGPPASGKTTIAMWLCKHLNSNLITKESLLEREFS---RLSVEAKSYYQVYK-IPNSILVSLVQERLNEDDCLRKGWI 136
Cdd:PLN02842    1 MISGAPASGKGTQCELIVHKFGLVHISTGDLLRAEVSagtDIGKRAKEFMNSGRlVPDEIVIAMVTGRLSREDAKEKGWL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 137 LDGIPERREQALMIQTLGLAPKHVIVLNAPDTVLIERNVGKRIDPVTGEIYHTTFdWPPE-PEIQNRLRQPEGISEIETA 215
Cdd:PLN02842   81 LDGYPRSFAQAQSLEKLKIRPDIFILLDVPDEILIDRCVGRRLDPVTGKIYHIKN-FPPEsEEIKARLITRPDDTEEKVK 159

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1720400556 216 KKLLEYHRHIIRILPSYPKILKTISSDQPCVDVF 249
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 ...
 59-257 5.53e-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: 5.53e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556  59 KVVILGPPASGKTTIAMWLCKHLNSNLITKESLLEREFSR---LSVEAKSYYQVYK-IPNSILVSLVQERLNEDDCLRKG 134
Cdd:TIGR01351   1 RLVLLGPPGSGKGTQAKRIAEKYGLPHISTGDLLRAEIKAgtpLGKKAKEYMEKGElVPDEIVNQLVKERLTQNDDNENG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 135 WILDGIPERREQALMI-QTLGLAPKHVIVLNAPDTVLIERNVGKRIDPVTGEIYHTTFDWPPEPEIQN----RLRQ---- 205
Cdd:TIGR01351  81 FILDGFPRTLSQAEALdALLEEPIDAVIELDVPDEELVERLSGRRICPSCGRVYHLKFNPPKVPGCDDctgeLLVQredd 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720400556 206 -PEGISE-----IETAKKLLEYHRHIIrilpsypkILKTISSDQPCVDVFYQALTYVQ 257
Cdd:TIGR01351 161 tEEVVKKrlevyKEQTEPLIDYYKKRG--------ILVQIDGNGPIDEVWKRILEALK 210
Adk COG0563
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ...
 59-249 3.04e-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: 3.04e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556  59 KVVILGPPASGKTTIAMWLCKHLNSNLITKESLLEREFSR---LSVEAKSYY----QVykiPNSILVSLVQERLNEDDCl 131
Cdd:COG0563     2 RIILLGPPGAGKGTQAKRLAEKYGIPHISTGDMLRAAVKAgteLGKKAKEYMdageLV---PDEIVIGLVKERLAQPDC- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 132 RKGWILDGIPERREQAL----MIQTLGLAPKHVIVLNAPDTVLIERNVGKRIDPVTGEIYHTTFDWPPEPEI----QNRL 203
Cdd:COG0563    78 ANGFILDGFPRTVAQAEaldeLLAELGIKLDAVIELDVDDEELVERLSGRRVCPNCGATYHVKFNPPKVEGVcdkcGGEL 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720400556 204 RQ-----PEGIseietAKKLLEYHRHIIRILPSYPK--ILKTISSDQPCVDVF 249
Cdd:COG0563   158 VQraddnEETV-----RKRLEVYHEQTAPLIDYYRKkgKLVEIDGEGSIEEVT 205
ADK pfam00406
Adenylate kinase;
62-222 1.22e-22

Adenylate kinase;


Pssm-ID: 395329 [Multi-domain]  Cd Length: 184  Bit Score: 94.68  E-value: 1.22e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556  62 ILGPPASGKTTIAMWLCKHLNSNLITKESLLEREF---SRLSVEAKSYYQVYKI-PNSILVSLVQERLNEDDClRKGWIL 137
Cdd:pfam00406   1 LLGPPGAGKGTQAEKIVQKYGLPHLSTGDLLRAEIksgTELGKEAKEYMDKGELvPDEVVVGLVKERLEQNDC-KNGFLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 138 DGIPERREQALMIQTL---GLAPKHVIVLNAPDTVLIERNVGKRIDPVTGEIYHTTFDWPPEPEIQN----RLRQPEGIS 210
Cdd:pfam00406  80 DGFPRTVPQAEALEELlerGIKLDYVIEFDVPDEVLVERLTGRRIHPNSGRSYHLEFNPPKVPGKDDvtgePLVQRSDDN 159

                         170
                  ....*....|...
gi 1720400556 211 EiETAKKLLE-YH 222
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 1.33e-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: 1.33e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1720400556   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 ...
 269-461 1.67e-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: 178.20  E-value: 1.67e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 269 KVLLCGPLGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSSFGELIQPFFEKRMTVPDSIITKVLADRMEQQDCiQKG 348
Cdd:cd01428     1 RILLLGPPGSGKGTQAERLAKKYGLPHISTGDLLREEIASGTELGKKAKEYIDSGKLVPDEIVIKLLKERLKKPDC-KKG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 349 WVLHGFPRDLDQARMLNSM---GYNPNRVFFLSVPLDSILERLTLRRTDPVTGERFHLMYKPpptiEVQVRLLQNPKDSE 425
Cdd:cd01428    80 FILDGFPRTVDQAEALDELldeGIKPDKVIELDVPDEVLIERILGRRICPVSGRVYHLGKDD----VTGEPLSQRSDDNE 155

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1720400556 426 EYIKLQTDLFYRNSGDLEQYYDRA---IIVNGDQDPYTV 461
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 ...
 269-467 1.84e-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: 1.84e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 269 KVLLCGPLGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSSFGELIQPFFEKRMTVPDSIITKVLADRMEQQDCIQKG 348
Cdd:TIGR01351   1 RLVLLGPPGSGKGTQAKRIAEKYGLPHISTGDLLRAEIKAGTPLGKKAKEYMEKGELVPDEIVNQLVKERLTQNDDNENG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 349 WVLHGFPRDLDQARMLNSMGYNPNR-VFFLSVPLDSILERLTLRRTDPVTGERFHLMYKPPPTIEVQV----RLLQNPKD 423
Cdd:TIGR01351  81 FILDGFPRTLSQAEALDALLEEPIDaVIELDVPDEELVERLSGRRICPSCGRVYHLKFNPPKVPGCDDctgeLLVQREDD 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1720400556 424 SEEYIKLQTDLFYRNSGDLEQYYDRAII---VNGDQDPYTVFEYIES 467
Cdd:TIGR01351 161 TEEVVKKRLEVYKEQTEPLIDYYKKRGIlvqIDGNGPIDEVWKRILE 207
Adk COG0563
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ...
 269-469 2.67e-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: 2.67e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 269 KVLLCGPLGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSSFGELIQPFFEKRMTVPDSIITKVLADRMEQQDCiQKG 348
Cdd:COG0563     2 RIILLGPPGAGKGTQAKRLAEKYGIPHISTGDMLRAAVKAGTELGKKAKEYMDAGELVPDEIVIGLVKERLAQPDC-ANG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 349 WVLHGFPRDLDQA----RMLNSMGYNPNRVFFLSVPLDSILERLTLRRTDPVTGERFHLMYKPPPTIEV----QVRLLQN 420
Cdd:COG0563    81 FILDGFPRTVAQAealdELLAELGIKLDAVIELDVDDEELVERLSGRRVCPNCGATYHVKFNPPKVEGVcdkcGGELVQR 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720400556 421 PKDSEEYIKLQTDLFYRNSGDLEQYYDRA---IIVNGDQDPYTVFEYIESGI 469
Cdd:COG0563   161 ADDNEETVRKRLEVYHEQTAPLIDYYRKKgklVEIDGEGSIEEVTADILAIL 212
ADK pfam00406
Adenylate kinase;
272-446 8.67e-40

Adenylate kinase;


Pssm-ID: 395329 [Multi-domain]  Cd Length: 184  Bit Score: 141.68  E-value: 8.67e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 272 LCGPLGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSSFGELIQPFFEKRMTVPDSIITKVLADRMEQQDCiQKGWVL 351
Cdd:pfam00406   1 LLGPPGAGKGTQAEKIVQKYGLPHLSTGDLLRAEIKSGTELGKEAKEYMDKGELVPDEVVVGLVKERLEQNDC-KNGFLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 352 HGFPRDLDQARMLNSM---GYNPNRVFFLSVPLDSILERLTLRRTDPVTGERFHLMYKPPPTIEVQV----RLLQNPKDS 424
Cdd:pfam00406  80 DGFPRTVPQAEALEELlerGIKLDYVIEFDVPDEVLVERLTGRRIHPNSGRSYHLEFNPPKVPGKDDvtgePLVQRSDDN 159

                         170       180
                  ....*....|....*....|..
gi 1720400556 425 EEYIKLQTDLFYRNSGDLEQYY 446
Cdd:pfam00406 160 EETVKKRLETYHKQTKPLIDYY 181
PLN02842 PLN02842
nucleotide kinase
 271-467 3.73e-38

nucleotide kinase


Pssm-ID: 178435 [Multi-domain]  Cd Length: 505  Bit Score: 145.39  E-value: 3.73e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 271 LLCGPLGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSSFGELIQPFFEKRMTVPDSIITKVLADRMEQQDCIQKGWV 350
Cdd:PLN02842    1 MISGAPASGKGTQCELIVHKFGLVHISTGDLLRAEVSAGTDIGKRAKEFMNSGRLVPDEIVIAMVTGRLSREDAKEKGWL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 351 LHGFPRDLDQARMLNSMGYNPNRVFFLSVPLDSILERLTLRRTDPVTGERFHLMYKPPPTIEVQVRLLQNPKDSEEYIKL 430
Cdd:PLN02842   81 LDGYPRSFAQAQSLEKLKIRPDIFILLDVPDEILIDRCVGRRLDPVTGKIYHIKNFPPESEEIKARLITRPDDTEEKVKA 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1720400556 431 QTDLFYRNSGD-LEQYYDRAIIVNGDQDPYTVFEYIES 467
Cdd:PLN02842  161 RLQIYKKNAEAiLSTYSDIMVKIDGNRPKEVVFEEISS 198
adk PRK00279
adenylate kinase; Reviewed
 269-467 2.25e-33

adenylate kinase; Reviewed


Pssm-ID: 234711 [Multi-domain]  Cd Length: 215  Bit Score: 125.26  E-value: 2.25e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 269 KVLLCGPLGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSSFGELIQPFFEKRMTVPDSIITKVLADRMEQQDCiQKG 348
Cdd:PRK00279    2 RLILLGPPGAGKGTQAKFIAEKYGIPHISTGDMLRAAVKAGTELGKEAKSYMDAGELVPDEIVIGLVKERLAQPDC-KNG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 349 WVLHGFPRDLDQA----RMLNSMGYNPNRVFFLSVPLDSILERLTLRRTDPVTGERFHLMYKPPPTIEV----QVRLLQN 420
Cdd:PRK00279   81 FLLDGFPRTIPQAealdEMLKELGIKLDAVIEIDVPDEELVERLSGRRICPACGRTYHVKFNPPKVEGKcdvcGEELIQR 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720400556 421 PKDSEEYIKLQTDLFYRNSGDLEQYYDRA---IIVNGDQDPYTVFEYIES 467
Cdd:PRK00279  161 ADDNEETVRKRLEVYHKQTAPLIDYYKKKgklKKIDGTGSIDEVFADILK 210
ADK cd01428
Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine ...
 59-248 2.51e-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: 121.96  E-value: 2.51e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556  59 KVVILGPPASGKTTIAMWLCKHLNSNLITKESLLEREF---SRLSVEAKSYYQVYK-IPNSILVSLVQERLNEDDClRKG 134
Cdd:cd01428     1 RILLLGPPGSGKGTQAERLAKKYGLPHISTGDLLREEIasgTELGKKAKEYIDSGKlVPDEIVIKLLKERLKKPDC-KKG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 135 WILDGIPERREQALMIQTL---GLAPKHVIVLNAPDTVLIERNVGKRIDPVTGEIYHTTFDWPPEPEIQNRLRQpegisE 211
Cdd:cd01428    80 FILDGFPRTVDQAEALDELldeGIKPDKVIELDVPDEVLIERILGRRICPVSGRVYHLGKDDVTGEPLSQRSDD-----N 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1720400556 212 IETAKKLLE-YHRHIIRILPSYPK--ILKTISSDQPCVDV 248
Cdd:cd01428   155 EETIKKRLEvYKEQTAPLIDYYKKkgKLVEIDGSGDIDEV 194
PLN02842 PLN02842
nucleotide kinase
 61-249 7.59e-30

nucleotide kinase


Pssm-ID: 178435 [Multi-domain]  Cd Length: 505  Bit Score: 121.89  E-value: 7.59e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556  61 VILGPPASGKTTIAMWLCKHLNSNLITKESLLEREFS---RLSVEAKSYYQVYK-IPNSILVSLVQERLNEDDCLRKGWI 136
Cdd:PLN02842    1 MISGAPASGKGTQCELIVHKFGLVHISTGDLLRAEVSagtDIGKRAKEFMNSGRlVPDEIVIAMVTGRLSREDAKEKGWL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 137 LDGIPERREQALMIQTLGLAPKHVIVLNAPDTVLIERNVGKRIDPVTGEIYHTTFdWPPE-PEIQNRLRQPEGISEIETA 215
Cdd:PLN02842   81 LDGYPRSFAQAQSLEKLKIRPDIFILLDVPDEILIDRCVGRRLDPVTGKIYHIKN-FPPEsEEIKARLITRPDDTEEKVK 159

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1720400556 216 KKLLEYHRHIIRILPSYPKILKTISSDQPCVDVF 249
Cdd:PLN02842  160 ARLQIYKKNAEAILSTYSDIMVKIDGNRPKEVVF 193
PRK14530 PRK14530
adenylate kinase; Provisional
 268-469 9.34e-28

adenylate kinase; Provisional


Pssm-ID: 237747 [Multi-domain]  Cd Length: 215  Bit Score: 110.26  E-value: 9.34e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 268 PKVLLCGPLGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSSFGEL----IQPFFEKRMTVPDSIITKVLADRMEQQD 343
Cdd:PRK14530    4 PRILLLGAPGAGKGTQSSNLAEEFGVEHVTTGDALRANKQMDISDMDTeydtPGEYMDAGELVPDAVVNEIVEEALSDAD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 344 ciqkGWVLHGFPRDLDQARMLNSMGyNPNRVFFLSVPLDSILERLTLRRTDPVTGERFHLMYKPPPTIEV----QVRLLQ 419
Cdd:PRK14530   84 ----GFVLDGYPRNLEQAEYLESIT-DLDVVLYLDVSEEELVDRLTGRRVCPDCGANYHVEFNQPEEEGVcdecGGELIQ 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720400556 420 NPKDSEEYIKLQTDLFYRNSGDLEQYY-DRAII--VNGDQDPYTVFEYIESGI 469
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 ...
 59-257 5.53e-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: 5.53e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556  59 KVVILGPPASGKTTIAMWLCKHLNSNLITKESLLEREFSR---LSVEAKSYYQVYK-IPNSILVSLVQERLNEDDCLRKG 134
Cdd:TIGR01351   1 RLVLLGPPGSGKGTQAKRIAEKYGLPHISTGDLLRAEIKAgtpLGKKAKEYMEKGElVPDEIVNQLVKERLTQNDDNENG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 135 WILDGIPERREQALMI-QTLGLAPKHVIVLNAPDTVLIERNVGKRIDPVTGEIYHTTFDWPPEPEIQN----RLRQ---- 205
Cdd:TIGR01351  81 FILDGFPRTLSQAEALdALLEEPIDAVIELDVPDEELVERLSGRRICPSCGRVYHLKFNPPKVPGCDDctgeLLVQredd 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720400556 206 -PEGISE-----IETAKKLLEYHRHIIrilpsypkILKTISSDQPCVDVFYQALTYVQ 257
Cdd:TIGR01351 161 tEEVVKKrlevyKEQTEPLIDYYKKRG--------ILVQIDGNGPIDEVWKRILEALK 210
Adk COG0563
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ...
 59-249 3.04e-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: 3.04e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556  59 KVVILGPPASGKTTIAMWLCKHLNSNLITKESLLEREFSR---LSVEAKSYY----QVykiPNSILVSLVQERLNEDDCl 131
Cdd:COG0563     2 RIILLGPPGAGKGTQAKRLAEKYGIPHISTGDMLRAAVKAgteLGKKAKEYMdageLV---PDEIVIGLVKERLAQPDC- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 132 RKGWILDGIPERREQAL----MIQTLGLAPKHVIVLNAPDTVLIERNVGKRIDPVTGEIYHTTFDWPPEPEI----QNRL 203
Cdd:COG0563    78 ANGFILDGFPRTVAQAEaldeLLAELGIKLDAVIELDVDDEELVERLSGRRVCPNCGATYHVKFNPPKVEGVcdkcGGEL 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720400556 204 RQ-----PEGIseietAKKLLEYHRHIIRILPSYPK--ILKTISSDQPCVDVF 249
Cdd:COG0563   158 VQraddnEETV-----RKRLEVYHEQTAPLIDYYRKkgKLVEIDGEGSIEEVT 205
PLN02674 PLN02674
adenylate kinase
 242-452 2.22e-24

adenylate kinase


Pssm-ID: 178279 [Multi-domain]  Cd Length: 244  Bit Score: 101.50  E-value: 2.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 242 DQPCVDVFYQALTYVQsghrCNAPFTPKVLLCGPLGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSSFGELIQPFFE 321
Cdd:PLN02674   10 DVPSVDLMTELLRRMK----CSSKPDKRLILIGPPGSGKGTQSPIIKDEYCLCHLATGDMLRAAVAAKTPLGIKAKEAMD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 322 KRMTVPDSIITKVLADRMEQQDCiQKGWVLHGFPRDLDQAR----MLNSMGYNPNRVFFLSVPlDSIL-ERLTLRRTDPV 396
Cdd:PLN02674   86 KGELVSDDLVVGIIDEAMKKPSC-QKGFILDGFPRTVVQAQkldeMLAKQGAKIDKVLNFAID-DAILeERITGRWIHPS 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 397 TGERFHLMYKPPPTIEVQ----VRLLQNPKDSEEYIKLQTDLFYRNSGDLEQYYDRAIIV 452
Cdd:PLN02674  164 SGRTYHTKFAPPKVPGVDdvtgEPLIQRKDDTAAVLKSRLEAFHKQTEPVIDYYAKKGVV 223
ADK pfam00406
Adenylate kinase;
62-222 1.22e-22

Adenylate kinase;


Pssm-ID: 395329 [Multi-domain]  Cd Length: 184  Bit Score: 94.68  E-value: 1.22e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556  62 ILGPPASGKTTIAMWLCKHLNSNLITKESLLEREF---SRLSVEAKSYYQVYKI-PNSILVSLVQERLNEDDClRKGWIL 137
Cdd:pfam00406   1 LLGPPGAGKGTQAEKIVQKYGLPHLSTGDLLRAEIksgTELGKEAKEYMDKGELvPDEVVVGLVKERLEQNDC-KNGFLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 138 DGIPERREQALMIQTL---GLAPKHVIVLNAPDTVLIERNVGKRIDPVTGEIYHTTFDWPPEPEIQN----RLRQPEGIS 210
Cdd:pfam00406  80 DGFPRTVPQAEALEELlerGIKLDYVIEFDVPDEVLVERLTGRRIHPNSGRSYHLEFNPPKVPGKDDvtgePLVQRSDDN 159

                         170
                  ....*....|...
gi 1720400556 211 EiETAKKLLE-YH 222
Cdd:pfam00406 160 E-ETVKKRLEtYH 171
adk PRK02496
adenylate kinase; Provisional
 269-469 1.59e-22

adenylate kinase; Provisional


Pssm-ID: 179433 [Multi-domain]  Cd Length: 184  Bit Score: 94.43  E-value: 1.59e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 269 KVLLCGPLGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSSFGELIQPFFEKRMTVPDSIITKVLADRMEQQDCiQKG 348
Cdd:PRK02496    3 RLIFLGPPGAGKGTQAVVLAEHLHIPHISTGDILRQAIKEQTPLGIKAQGYMDKGELVPDQLVLDLVQERLQQPDA-ANG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 349 WVLHGFPRDLDQARMLN----SMGYNPNRVFFLSVPLDSILERLTLR-RTDpvtgerfhlmykppptievqvrllqnpkD 423
Cdd:PRK02496   82 WILDGFPRKVTQAAFLDellqEIGQSGERVVNLDVPDDVVVERLLARgRKD----------------------------D 133

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1720400556 424 SEEYIKLQTDLFYRNSGDLEQYY-DRAII--VNGDQDPYTVFEYIESGI 469
Cdd:PRK02496  134 TEEVIRRRLEVYREQTAPLIDYYrDRQKLltIDGNQSVEAVTTELKAAL 182
adk PRK00279
adenylate kinase; Reviewed
 59-249 7.30e-22

adenylate kinase; Reviewed


Pssm-ID: 234711 [Multi-domain]  Cd Length: 215  Bit Score: 93.68  E-value: 7.30e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556  59 KVVILGPPASGKTTIAMWLCKHLNsnlITKES---LLEREFSR---LSVEAKSYyqVYK---IPNSILVSLVQERLNEDD 129
Cdd:PRK00279    2 RLILLGPPGAGKGTQAKFIAEKYG---IPHIStgdMLRAAVKAgteLGKEAKSY--MDAgelVPDEIVIGLVKERLAQPD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 130 ClRKGWILDGIPERREQAL----MIQTLGLAPKHVIVLNAPDTVLIERNVGKRIDPVTGEIYHTTFDWPPEPEIQNRLRQ 205
Cdd:PRK00279   77 C-KNGFLLDGFPRTIPQAEaldeMLKELGIKLDAVIEIDVPDEELVERLSGRRICPACGRTYHVKFNPPKVEGKCDVCGE 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720400556 206 PEGISE---IETAKKLLE-YHRHIIRILPSYPK--ILKTISSDQPCVDVF 249
Cdd:PRK00279  156 ELIQRAddnEETVRKRLEvYHKQTAPLIDYYKKkgKLKKIDGTGSIDEVF 205
adk PRK02496
adenylate kinase; Provisional
 59-173 3.80e-18

adenylate kinase; Provisional


Pssm-ID: 179433 [Multi-domain]  Cd Length: 184  Bit Score: 82.10  E-value: 3.80e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556  59 KVVILGPPASGKTTIAMWLCKHLNSNLITKESLLE---REFSRLSVEAKSYY-QVYKIPNSILVSLVQERLNEDDClRKG 134
Cdd:PRK02496    3 RLIFLGPPGAGKGTQAVVLAEHLHIPHISTGDILRqaiKEQTPLGIKAQGYMdKGELVPDQLVLDLVQERLQQPDA-ANG 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1720400556 135 WILDGIPERREQA----LMIQTLGLAPKHVIVLNAPDTVLIER 173
Cdd:PRK02496   82 WILDGFPRKVTQAafldELLQEIGQSGERVVNLDVPDDVVVER 124
PRK14528 PRK14528
adenylate kinase; Provisional
 269-391 5.64e-18

adenylate kinase; Provisional


Pssm-ID: 172994 [Multi-domain]  Cd Length: 186  Bit Score: 81.60  E-value: 5.64e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 269 KVLLCGPLGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSSFGELIQPFFEKRMTVPDSIITKVLADRMEQQDCiQKG 348
Cdd:PRK14528    3 NIIFMGPPGAGKGTQAKILCERLSIPQISTGDILREAVKNQTAMGIEAKRYMDAGDLVPDSVVIGIIKDRIREADC-KNG 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1720400556 349 WVLHGFPRDLDQAR----MLNSMGYNPNRVFFLSVPLDSILERLTLR 391
Cdd:PRK14528   82 FLLDGFPRTVEQADaldaLLKNEGKSIDKAINLEVPDGELLKRLLGR 128
PRK13808 PRK13808
adenylate kinase; Provisional
 269-391 2.14e-17

adenylate kinase; Provisional


Pssm-ID: 172341 [Multi-domain]  Cd Length: 333  Bit Score: 83.01  E-value: 2.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 269 KVLLCGPLGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSSFGELIQPFFEKRMTVPDSIITKVLADRMEQQDCIQkG 348
Cdd:PRK13808    2 RLILLGPPGAGKGTQAQRLVQQYGIVQLSTGDMLRAAVAAGTPVGLKAKDIMASGGLVPDEVVVGIISDRIEQPDAAN-G 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1720400556 349 WVLHGFPRDLDQA----RMLNSMGYNPNRVFFLSVPLDSILERLTLR 391
Cdd:PRK13808   81 FILDGFPRTVPQAealdALLKDKQLKLDAVVELRVNEGALLARVETR 127
PTZ00088 PTZ00088
adenylate kinase 1; Provisional
 269-446 3.69e-17

adenylate kinase 1; Provisional


Pssm-ID: 240262 [Multi-domain]  Cd Length: 229  Bit Score: 80.61  E-value: 3.69e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 269 KVLLCGPLGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSSFGELIQPFFEKRMTVPDSIITKVLADRMEQ-QDCIQK 347
Cdd:PTZ00088    8 KIVLFGAPGVGKGTFAEILSKKENLKHINMGNILREEIKAKTTIGKEIQKVVTSGNLVPDNLVIAIVKDEIAKvTDDCFK 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 348 GWVLHGFPRDLDQARMLNSMGyNPNRVFFLSVPLDSILERLTLRRTDPVTGERFHLM------YKPPPTIEVQ------- 414
Cdd:PTZ00088   88 GFILDGFPRNLKQCKELGKIT-NIDLFVNIYLPRNILIKKLLGRRICNTCNRNFNIAhirsdpYDMPPILPPAdcegckg 166

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1720400556 415 -VRLLQNPKDSEEYIKLQTDLFYRNSGDLEQYY 446
Cdd:PTZ00088  167 nPKLQKRSDDTEEIVAHRLNTYESTNSPIIQFF 199
DD_AK8 cd22979
dimerization/docking (D/D) domain found in adenylate kinase isoenzyme 8 (AK8) and similar ...
 9-52 1.33e-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: 1.33e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1720400556   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. ...
 274-462 5.80e-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: 5.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 274 GPlGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSSFGELIQPFFEKRMTVPDSIITKVLADRMEQQDCIQKGWVLHG 353
Cdd:TIGR01360  11 GP-GSGKGTQCEKIVEKYGFTHLSTGDLLRAEVASGSERGKQLQAIMESGDLVPLDTVLDLLKDAMVAALGTSKGFLIDG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 354 FPRDLDQARMLNSMGYNPNRVFFLSVPLDSILERLTLR-----RTDpvtgerfhlmykppptievqvrllqnpkDSEEYI 428
Cdd:TIGR01360  90 YPREVKQGEEFERRIGPPTLVLYFDCSEDTMVKRLLKRaetsgRVD----------------------------DNEKTI 141

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1720400556 429 KLQTDLFYRNSGDLEQYYDRAIIV---NGDQDPYTVF 462
Cdd:TIGR01360 142 KKRLETYYKATEPVIAYYETKGKLrkiNAEGTVDDVF 178
PRK14527 PRK14527
adenylate kinase; Provisional
 270-394 7.32e-15

adenylate kinase; Provisional


Pssm-ID: 237745 [Multi-domain]  Cd Length: 191  Bit Score: 72.90  E-value: 7.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 270 VLLCGPLGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSSFGELIQPFFEKRMTVPDSIITKVLADRMEQQDCIQKgw 349
Cdd:PRK14527    9 VIFLGPPGAGKGTQAERLAQELGLKKLSTGDILRDHVARGTELGQRAKPIMEAGDLVPDELILALIRDELAGMEPVRV-- 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720400556 350 VLHGFPRDLDQA----RMLNSMGYNPNRVFFLSVPLDSILERLTLR-----RTD 394
Cdd:PRK14527   87 IFDGFPRTLAQAealdRLLEELGARLLAVVLLEVPDEELIRRIVERarqegRSD 140
PRK14532 PRK14532
adenylate kinase; Provisional
 270-446 2.03e-14

adenylate kinase; Provisional


Pssm-ID: 184729 [Multi-domain]  Cd Length: 188  Bit Score: 71.39  E-value: 2.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 270 VLLCGPLGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSSFGELIQPFFEKRMTVPDSIITKVLADRMEQQDCiQKGW 349
Cdd:PRK14532    3 LILFGPPAAGKGTQAKRLVEERGMVQLSTGDMLRAAIASGSELGQRVKGIMDRGELVSDEIVIALIEERLPEAEA-AGGA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 350 VLHGFPRDLDQARMLNSM----GYNPNRVFFLSVPLDSILERLTlrrtdpvtgERFhlmykppptiEVQVRllqnPKDSE 425
Cdd:PRK14532   82 IFDGFPRTVAQAEALDKMlasrGQKIDVVIRLKVDDEALIERIV---------KRF----------EEQGR----PDDNP 138

                         170       180
                  ....*....|....*....|.
gi 1720400556 426 EYIKLQTDLFYRNSGDLEQYY 446
Cdd:PRK14532  139 EVFVTRLDAYNAQTAPLLPYY 159
PRK14528 PRK14528
adenylate kinase; Provisional
 59-179 2.46e-14

adenylate kinase; Provisional


Pssm-ID: 172994 [Multi-domain]  Cd Length: 186  Bit Score: 71.20  E-value: 2.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556  59 KVVILGPPASGKTTIAMWLCKHLNSNLITKESLLE---REFSRLSVEAKSYYQVYK-IPNSILVSLVQERLNEDDClRKG 134
Cdd:PRK14528    3 NIIFMGPPGAGKGTQAKILCERLSIPQISTGDILReavKNQTAMGIEAKRYMDAGDlVPDSVVIGIIKDRIREADC-KNG 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1720400556 135 WILDGIPERREQA----LMIQTLGLAPKHVIVLNAPDTVLIERNVGKRI 179
Cdd:PRK14528   82 FLLDGFPRTVEQAdaldALLKNEGKSIDKAINLEVPDGELLKRLLGRAE 130
PRK14526 PRK14526
adenylate kinase; Provisional
 269-453 3.31e-14

adenylate kinase; Provisional


Pssm-ID: 172992 [Multi-domain]  Cd Length: 211  Bit Score: 71.42  E-value: 3.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 269 KVLLCGPLGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSSFGELIQPFFEKRMTVPDSIITKVLADRMEQQDCiQKG 348
Cdd:PRK14526    2 KLVFLGPPGSGKGTIAKILSNELNYYHISTGDLFRENILNSTPLGKEIKQIVENGQLVPDSITIKIVEDKINTIKN-NDN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 349 WVLHGFPRDLDQARMLNSMGYNPNRVFFLsVPLDSILERLTLRRTDPVTGERFHLMYKPPPTIEV----QVRLLQNPKDS 424
Cdd:PRK14526   81 FILDGFPRNINQAKALDKFLPNIKIINFL-IDEELLIKRLSGRRICKSCNNIFNIYTLPTKEKGIcdvcKGDLYQRKDDK 159

                         170       180
                  ....*....|....*....|....*....
gi 1720400556 425 EEYIKLQTDLFYRNSGDLEQYYDRAIIVN 453
Cdd:PRK14526  160 EESLKTRLQEYKLQTKPLIEFYSKCNRLN 188
UMP_CMP_kin_fam TIGR01359
UMP-CMP kinase family; This subfamily of the adenylate kinase superfamily contains examples of ...
 270-467 1.52e-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: 1.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 270 VLLC-GPLGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSS-FGELIQPFFEKRMTVPdSIITKVLADRMEQQDCIQK 347
Cdd:TIGR01359   1 VVFVlGGPGSGKGTQCAKIVENFGFTHLSAGDLLRAEIKREGSeNGSLIESYIKEGKIVP-SEVTVELLKKAIQEDGSSK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 348 GWVLHGFPR---DLDQARMLNSMGYNPNRVFFLSVPLDSILERLTLR-----RTDpvtgerfhlmyKPPPTIEVQVRLLQ 419
Cdd:TIGR01359  80 KFLIDGFPRneeNLEAWEKLMDNKVNFKFVLFFDCPEETMIKRLLKRgqtsgRVD-----------DNIETLKKRFRTYN 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1720400556 420 NpkDSEEYIKlqtdlFYRNSGDLeqyydraIIVNGDQDPYTVFEYIES 467
Cdd:TIGR01359 149 E--ETLPIIE-----HFENKGKV-------KEINAEGSVEEVFEDVEK 182
PRK14529 PRK14529
adenylate kinase; Provisional
 270-364 3.43e-13

adenylate kinase; Provisional


Pssm-ID: 237746 [Multi-domain]  Cd Length: 223  Bit Score: 68.59  E-value: 3.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 270 VLLCGPLGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSSFGELIQPFFEKRMTVPDSIITKVLADRMEQQDciQKGW 349
Cdd:PRK14529    3 ILIFGPNGSGKGTQGALVKKKYDLAHIESGAIFREHIGGGTELGKKAKEYIDRGDLVPDDITIPMILETLKQDG--KNGW 80

                          90
                  ....*....|....*
gi 1720400556 350 VLHGFPRDLDQARML 364
Cdd:PRK14529   81 LLDGFPRNKVQAEKL 95
PRK14531 PRK14531
adenylate kinase; Provisional
 269-394 8.94e-13

adenylate kinase; Provisional


Pssm-ID: 172997 [Multi-domain]  Cd Length: 183  Bit Score: 66.76  E-value: 8.94e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 269 KVLLCGPLGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSSFGELIQPFFEKRMTVPDSIITKVLADRMeqQDCIQKG 348
Cdd:PRK14531    4 RLLFLGPPGAGKGTQAARLCAAHGLRHLSTGDLLRSEVAAGSALGQEAEAVMNRGELVSDALVLAIVESQL--KALNSGG 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1720400556 349 WVLHGFPRDLDQAR----MLNSMGYNPNRVFFLSVPLDSILERLTLR-RTD 394
Cdd:PRK14531   82 WLLDGFPRTVAQAEalepLLEELKQPIEAVVLLELDDAVLIERLLARgRAD 132
PRK14530 PRK14530
adenylate kinase; Provisional
 58-220 1.04e-12

adenylate kinase; Provisional


Pssm-ID: 237747 [Multi-domain]  Cd Length: 215  Bit Score: 67.12  E-value: 1.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556  58 PKVVILGPPASGKTTIAMWLCKHLNSNLITKESLL----EREFSRLSVE---AKSYYQVYK-IPNSILVSLVQERLNEDD 129
Cdd:PRK14530    4 PRILLLGAPGAGKGTQSSNLAEEFGVEHVTTGDALrankQMDISDMDTEydtPGEYMDAGElVPDAVVNEIVEEALSDAD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 130 clrkGWILDGIPERREQALMIQTLgLAPKHVIVLNAPDTVLIERNVGKRIDPVTGEIYHTTFDWPPEPEIQN----RLRQ 205
Cdd:PRK14530   84 ----GFVLDGYPRNLEQAEYLESI-TDLDVVLYLDVSEEELVDRLTGRRVCPDCGANYHVEFNQPEEEGVCDecggELIQ 158

                         170
                  ....*....|....*
gi 1720400556 206 PEGISEiETAKKLLE 220
Cdd:PRK14530  159 RDDDTE-ETVRERLD 172
AAA_17 pfam13207
AAA domain;
274-393 1.12e-12

AAA domain;


Pssm-ID: 463810 [Multi-domain]  Cd Length: 136  Bit Score: 64.95  E-value: 1.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 274 GPLGSGKRLQATLLAQKYGLVNISCGQLLKEavAAKSSFGELIQPFFEKRMTVPDSIITKVLADRMEqQDCIQKGWVLHG 353
Cdd:pfam13207   2 GVPGSGKTTQLKKLAEKLGFPHISAGDLLRE--EAKERGLVEDRDEMRKLPLEPQKELQKLAAERIA-EEAGEGGVIVDG 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1720400556 354 FPRDLDQARMLNSM------GYNPNRVFFLSVPLDSILERLTLRRT 393
Cdd:pfam13207  79 HPRIKTPAGYLPGLpvevlrELKPDAIILLEADPEEILERRLKDRT 124
PLN02674 PLN02674
adenylate kinase
 59-248 8.37e-11

adenylate kinase


Pssm-ID: 178279 [Multi-domain]  Cd Length: 244  Bit Score: 62.21  E-value: 8.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556  59 KVVILGPPASGKTTIA------MWLCkHLNSNLITKESLLERefSRLSVEAKSYYQVYK-IPNSILVSLVQERLNEDDCl 131
Cdd:PLN02674   33 RLILIGPPGSGKGTQSpiikdeYCLC-HLATGDMLRAAVAAK--TPLGIKAKEAMDKGElVSDDLVVGIIDEAMKKPSC- 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 132 RKGWILDGIPERREQAL----MIQTLGLAPKHVIVLNAPDTVLIERNVGKRIDPVTGEIYHTTFDWPPEPEIQNRLRQPE 207
Cdd:PLN02674  109 QKGFILDGFPRTVVQAQkldeMLAKQGAKIDKVLNFAIDDAILEERITGRWIHPSSGRTYHTKFAPPKVPGVDDVTGEPL 188

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1720400556 208 GISEIETA----KKLLEYHRHIIRILPSYPK--ILKTISSDQPCVDV 248
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 1.77e-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: 1.77e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1720400556  12 PEMPQYGEDYYIFEMMQNMLEQLLIHQPEDPISFMITHLRR 52
Cdd:cd22961     2 EDAEEYLEKHKIPELFESLLTALLIEKPEDPIEFLIDKLQQ 42
Kti12 COG4088
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ...
 60-221 1.38e-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: 54.35  E-value: 1.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556  60 VVILGPPASGKTTIAMWLCKHLNSNLITKESLLEREFSRLSVEA----KSYYQVYKipnSILVSLVQERLNeddcLRKGW 135
Cdd:COG4088     7 LILTGPPGSGKTTFAKALAQRLYAEGIAVALLHSDDFRRFLVNEsfpkETYEEVVE---DVRTTTADNALD----NGYSV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 136 ILDGIPERREQALMIQTLGL--APKHVIVLNAPDTVLIERNV--GKRIDPVTGEIYHTTFDWPPEPEIQNRLRQPEGISE 211
Cdd:COG4088    80 IVDGTFYYRSWQRDFRNLAKhkAPIHIIYLKAPLETALRRNRerGEPIPERVIARMYRKFDKPGTKDRPDLVIDTTEDSV 159

                         170
                  ....*....|
gi 1720400556 212 IETAKKLLEY 221
Cdd:COG4088   160 SETLDAILKA 169
PTZ00088 PTZ00088
adenylate kinase 1; Provisional
 59-195 1.59e-08

adenylate kinase 1; Provisional


Pssm-ID: 240262 [Multi-domain]  Cd Length: 229  Bit Score: 55.19  E-value: 1.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556  59 KVVILGPPASGKTTIAMWLCKHLNSNLITKESLLEREFSRLSVEAKSYYQVYK----IPNSILVSLVQERL-NEDDCLRK 133
Cdd:PTZ00088    8 KIVLFGAPGVGKGTFAEILSKKENLKHINMGNILREEIKAKTTIGKEIQKVVTsgnlVPDNLVIAIVKDEIaKVTDDCFK 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720400556 134 GWILDGIPERREQALMIQTLGlAPKHVIVLNAPDTVLIERNVGKRIDPVTGEIYH------TTFDWPP 195
Cdd:PTZ00088   88 GFILDGFPRNLKQCKELGKIT-NIDLFVNIYLPRNILIKKLLGRRICNTCNRNFNiahirsDPYDMPP 154
AAA_17 pfam13207
AAA domain;
63-173 2.96e-08

AAA domain;


Pssm-ID: 463810 [Multi-domain]  Cd Length: 136  Bit Score: 52.24  E-value: 2.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556  63 LGPPASGKTTIAMWLCKHLNSNLITKESLLEREFSRLS-VEAKSYYQ-VYKIPNSILVSLVQERLNEdDCLRKGWILDGI 140
Cdd:pfam13207   1 TGVPGSGKTTQLKKLAEKLGFPHISAGDLLREEAKERGlVEDRDEMRkLPLEPQKELQKLAAERIAE-EAGEGGVIVDGH 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1720400556 141 PERREQA-----LMIQTL-GLAPKHVIVLNAPDTVLIER 173
Cdd:pfam13207  80 PRIKTPAgylpgLPVEVLrELKPDAIILLEADPEEILER 118
PRK14526 PRK14526
adenylate kinase; Provisional
 59-222 5.11e-08

adenylate kinase; Provisional


Pssm-ID: 172992 [Multi-domain]  Cd Length: 211  Bit Score: 53.32  E-value: 5.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556  59 KVVILGPPASGKTTIAMWLCKHLNSNLITKESLLEREFSRLSVEAKSYYQVYK----IPNSILVSLVQERLNEDDClRKG 134
Cdd:PRK14526    2 KLVFLGPPGSGKGTIAKILSNELNYYHISTGDLFRENILNSTPLGKEIKQIVEngqlVPDSITIKIVEDKINTIKN-NDN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 135 WILDGIPERREQALMIQTLgLAPKHVIVLNAPDTVLIERNVGKRIDPVTGEIYHTTFDWPPEPEI----QNRLRQPEGIS 210
Cdd:PRK14526   81 FILDGFPRNINQAKALDKF-LPNIKIINFLIDEELLIKRLSGRRICKSCNNIFNIYTLPTKEKGIcdvcKGDLYQRKDDK 159

                         170
                  ....*....|..
gi 1720400556 211 EIETAKKLLEYH 222
Cdd:PRK14526  160 EESLKTRLQEYK 171
DD_EFCAB10 cd22976
dimerization/docking (D/D) domain found in EF-hand calcium-binding domain-containing protein ...
 16-52 1.01e-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: 1.01e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1720400556  16 QYGEDYYIFEMMQNMLEQLLIHQPEDPISFMITHLRR 52
Cdd:cd22976     6 EYLEKHKIPELFENLTSLLLYHRPEDPKAFLIEQLEK 42
PRK14527 PRK14527
adenylate kinase; Provisional
 56-177 1.02e-07

adenylate kinase; Provisional


Pssm-ID: 237745 [Multi-domain]  Cd Length: 191  Bit Score: 52.10  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556  56 NVPKVVI-LGPPASGKTTIAMWLCKHLNSNLITKESLLEREFSR---LSVEAKSYYQVYK-IPNSILVSLVQERLNEDDC 130
Cdd:PRK14527    4 TKNKVVIfLGPPGAGKGTQAERLAQELGLKKLSTGDILRDHVARgteLGQRAKPIMEAGDlVPDELILALIRDELAGMEP 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1720400556 131 LRKgwILDGIPERREQA----LMIQTLGLAPKHVIVLNAPDTVLIERNVGK 177
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 ...
 60-177 3.30e-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: 3.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556  60 VVIL-GPPASGKTTIAMWLCKHLNSNLITKESLLEREFSRLsVEAKSYYQvykipnsILVSLVQERLNE--DDCLRKGW- 135
Cdd:pfam13671   1 LILLvGLPGSGKSTLARRLLEELGAVRLSSDDERKRLFGEG-RPSISYYT-------DATDRTYERLHElaRIALRAGRp 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1720400556 136 -ILD-GIPERREQALMIQ---TLGlAPKHVIVLNAPDTVLIERNVGK 177
Cdd:pfam13671  73 vILDaTNLRRDERARLLAlarEYG-VPVRIVVFEAPEEVLRERLAAR 118
AAA_18 pfam13238
AAA domain;
60-173 4.01e-07

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 48.96  E-value: 4.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556  60 VVILGPPASGKTTIAMWLCKHLNSNLITKESLLEREfsrLSVEAKSYYQVYKIPNSILVSLVQERLNEDDCLRKG--WIL 137
Cdd:pfam13238   1 ILITGTPGVGKTTLAKELSKRLGFGDNVRDLALENG---LVLGDDPETRESKRLDEDKLDRLLDLLEENAALEEGgnLII 77

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1720400556 138 DGIPERREQALMIQtlglapKHVIVLNAPDTVLIER 173
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 ...
 60-249 4.74e-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: 4.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556  60 VVILGPPASGKTTIAMWLCKHLNSNLITKESLLEREFSRLSVEAKSYYQVY----KI-PNSILVSLVQERLNEDDClRKG 134
Cdd:TIGR01359   2 VFVLGGPGSGKGTQCAKIVENFGFTHLSAGDLLRAEIKREGSENGSLIESYikegKIvPSEVTVELLKKAIQEDGS-SKK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 135 WILDGIP---ERREQALMIQTLGLAPKHVIVLNAPDTVLIERnvgkridpvtgeiyhttfdwppepeIQNRlRQPEGISE 211
Cdd:TIGR01359  81 FLIDGFPrneENLEAWEKLMDNKVNFKFVLFFDCPEETMIKR-------------------------LLKR-GQTSGRVD 134

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1720400556 212 --IETAKKLLE-YHRHIIRILPSYPK--ILKTISSDQPCVDVF 249
Cdd:TIGR01359 135 dnIETLKKRFRtYNEETLPIIEHFENkgKVKEINAEGSVEEVF 177
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
60-204 5.44e-07

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 49.53  E-value: 5.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556  60 VVILGPPASGKTTIAMWLCKHLNSNLITKESLLEREFSRLSVEAKSYYQVykipnsilVSLVQERLNE--DDCLRKGW-- 135
Cdd:COG0645     2 ILVCGLPGSGKSTLARALAERLGAVRLRSDVVRKRLFGAGLAPLERSPEA--------TARTYARLLAlaRELLAAGRsv 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720400556 136 ILDG---IPERREQALMI-QTLGlAPKHVIVLNAPDTVLIE----RNVGKRIDPVTGEIYH--TTFDWPPEPEIQNRLR 204
Cdd:COG0645    74 ILDAtflRRAQREAFRALaEEAG-APFVLIWLDAPEEVLRErleaRNAEGGDSDATWEVLErqLAFEEPLTEDEGFLLV 151
PRK14529 PRK14529
adenylate kinase; Provisional
 60-179 2.70e-06

adenylate kinase; Provisional


Pssm-ID: 237746 [Multi-domain]  Cd Length: 223  Bit Score: 48.18  E-value: 2.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556  60 VVILGPPASGKTTIAMWLCK-----HLNSNLITKESLleREFSRLSVEAKSYYQVYK-IPNSILVSLVQERLNEDDclRK 133
Cdd:PRK14529    3 ILIFGPNGSGKGTQGALVKKkydlaHIESGAIFREHI--GGGTELGKKAKEYIDRGDlVPDDITIPMILETLKQDG--KN 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720400556 134 GWILDGIPERREQAL----MIQTLGLAPKHVIVLNAPDTVLIERNVGKRI 179
Cdd:PRK14529   79 GWLLDGFPRNKVQAEklweALQKEGMKLDYVIEILLPREVAKNRIMGRRL 128
DD_TEX55 cd22975
dimerization/docking (D/D) domain found in testis-specific expressed protein 55 (TEX55) and ...
 16-47 2.58e-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: 2.58e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1720400556  16 QYGEDYYIFEMMQNMLEQLLIHQPEDPISFMI 47
Cdd:cd22975     9 KYLEKHNILQLFQELTAGLVYERPDDPIQFMI 40
PRK14531 PRK14531
adenylate kinase; Provisional
 59-173 3.51e-05

adenylate kinase; Provisional


Pssm-ID: 172997 [Multi-domain]  Cd Length: 183  Bit Score: 44.42  E-value: 3.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556  59 KVVILGPPASGKTTIAMWLC-----KHLNSNlitkeSLLEREF---SRLSVEAKSYYQVYKIPNSILV-SLVQERLNEDD 129
Cdd:PRK14531    4 RLLFLGPPGAGKGTQAARLCaahglRHLSTG-----DLLRSEVaagSALGQEAEAVMNRGELVSDALVlAIVESQLKALN 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1720400556 130 clRKGWILDGIPERREQA----LMIQTLGLAPKHVIVLNAPDTVLIER 173
Cdd:PRK14531   79 --SGGWLLDGFPRTVAQAealePLLEELKQPIEAVVLLELDDAVLIER 124
DD_CrRSP_unchar cd22964
dimerization/docking (D/D) domain of an uncharacterized subunit found in Chlamydomonas ...
 10-52 3.04e-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: 3.04e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1720400556  10 IPPEMPQYGEDYYIFEMMQNMLEQLLIHQPEDPISFMITHLRR 52
Cdd:cd22964     1 KAEEKKEYLQQKVINPILEQLVTDLLQEKPEDPVPFMIQWLRK 43
DD_R_PKA_DPY30-like cd22957
dimerization/docking (D/D) domains found in the cAMP-dependent protein kinase regulatory ...
 25-50 5.46e-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: 5.46e-04
                          10        20
                  ....*....|....*....|....*.
gi 1720400556  25 EMMQNMLEQLLIHQPEDPISFMITHL 50
Cdd:cd22957     1 ELLQDAVAKLLEERPEDPVEFLAEYF 26
NadR3 COG3172
Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase ...
 55-104 6.07e-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: 6.07e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720400556  55 DNVPKVVILGPPASGKTTIAMWLCKHLNSNLItkeslleREFSRLSVEAK 104
Cdd:COG3172     6 SFVKKIVLLGAESTGKTTLARALAAHYNTPWV-------PEYGREYLEEK 48
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
31-153 1.69e-03

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 40.94  E-value: 1.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556  31 LEQLLIHQPEDPISFMITHLRRNNDNVPKVVILGPPASGKTTiamwLCKHLNSNLITKESLLEREFSrLSVEAKSyyqvY 110
Cdd:COG5635   154 LDDLYVPLNLLERIESLKRLELLEAKKKRLLILGEPGSGKTT----LLRYLALELAERYLDAEDPIP-ILIELRD----L 224

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720400556 111 KIPNSILvSLVQERLNEDDCLRKGW------------ILDG---IPERREQALMIQTL 153
Cdd:COG5635   225 AEEASLE-DLLAEALEKRGGEPEDAlerllrngrlllLLDGldeVPDEADRDEVLNQL 281
rho TIGR00767
transcription termination factor Rho; This RNA helicase, the transcription termination factor ...
 159-231 5.41e-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: 5.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400556 159 HVIVLNAPDTVLIERNVGKRIDPVT-------GEIYHTTFDWPPEPEIQnrlrqpegISE--IETAKKLLEYHRHIIRIL 229
Cdd:TIGR00767 190 QAITRNHPEVELIVLLIDERPEEVTdmqrsvkGEVVASTFDEPASRHVQ--------VAEmvIEKAKRLVEHKKDVVILL 261


                  ..
gi 1720400556 230 PS 231
Cdd:TIGR00767 262 DS 263
DD_TbAK-like cd22981
dimerization/docking (D/D) domain found in Trypanosoma brucei adenylate kinase (AK) and ...
 16-53 6.65e-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: 6.65e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1720400556  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. ...
 59-87 7.14e-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: 7.14e-03
                          10        20
                  ....*....|....*....|....*....
gi 1720400556  59 KVVILGPPASGKTTIAMWLCKHLNSNLIT 87
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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