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Conserved domains on  [gi|835581922|ref|WP_047569600|]
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MULTISPECIES: ribose 1,5-bisphosphokinase [Serratia]

Protein Classification

nucleoside/nucleotide kinase family protein( domain architecture ID 106737)

nucleoside/nucleotide kinase family protein may catalyze the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NK super family cl17190
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ...
1-164 1.01e-94

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


The actual alignment was detected with superfamily member PRK10078:

Pssm-ID: 450170  Cd Length: 186  Bit Score: 273.16  E-value: 1.01e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835581922   1 MARLIYLMGPSGAGKDSLLAALRADADSAPLVAHRYITRPADAGCENHIALSEPEFLRRRAKGLFALDWQAHQQRYAFGI 80
Cdd:PRK10078   1 MGKLIWLMGPSGSGKDSLLAALRQREQTQLLVAHRYITRPASAGSENHIALSEQEFFTRAGQNLFALSWHANGLYYGVGI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835581922  81 EVDLWLLQGIDVAVNGSRAHLPQAQQRYGAQLLPVCLQVSAGILRRRLQDRGRESAEQIEQRLARAAEYQqslPAGCRVL 160
Cdd:PRK10078  81 EIDLWLHAGFDVLVNGSRAHLPQARARYQSALLPVCLQVSPEILRQRLENRGRENASEINARLARAARYQ---PQDCHTL 157

                 ....
gi 835581922 161 HNDG 164
Cdd:PRK10078 158 NNDG 161
 
Name Accession Description Interval E-value
PRK10078 PRK10078
ribose 1,5-bisphosphokinase; Provisional
1-164 1.01e-94

ribose 1,5-bisphosphokinase; Provisional


Pssm-ID: 236648  Cd Length: 186  Bit Score: 273.16  E-value: 1.01e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835581922   1 MARLIYLMGPSGAGKDSLLAALRADADSAPLVAHRYITRPADAGCENHIALSEPEFLRRRAKGLFALDWQAHQQRYAFGI 80
Cdd:PRK10078   1 MGKLIWLMGPSGSGKDSLLAALRQREQTQLLVAHRYITRPASAGSENHIALSEQEFFTRAGQNLFALSWHANGLYYGVGI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835581922  81 EVDLWLLQGIDVAVNGSRAHLPQAQQRYGAQLLPVCLQVSAGILRRRLQDRGRESAEQIEQRLARAAEYQqslPAGCRVL 160
Cdd:PRK10078  81 EIDLWLHAGFDVLVNGSRAHLPQARARYQSALLPVCLQVSPEILRQRLENRGRENASEINARLARAARYQ---PQDCHTL 157

                 ....
gi 835581922 161 HNDG 164
Cdd:PRK10078 158 NNDG 161
PhnN COG3709
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
2-165 5.43e-84

Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];


Pssm-ID: 442923  Cd Length: 188  Bit Score: 245.87  E-value: 5.43e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835581922   2 ARLIYLMGPSGAGKDSLLAALRA--DADSAPLVAHRYITRPADAGCENHIALSEPEFLRRRAKGLFALDWQAHQQRYAFG 79
Cdd:COG3709    5 GRLIYVVGPSGAGKDSLLAAARArlAADPRLVFARRYITRPADAGGEDHDALSEAEFARRAAAGAFALHWQAHGLRYGIP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835581922  80 IEVDLWLLQGIDVAVNGSRAHLPQAQQRYgAQLLPVCLQVSAGILRRRLQDRGRESAEQIEQRLARAAEYQQsLPAGCRV 159
Cdd:COG3709   85 AEIDAWLAAGRDVVVNGSRAVLPQARARY-PRLLVVLITASPEVLAQRLAARGRESAEEIEARLARAAEFLP-DGPDVLV 162

                 ....*.
gi 835581922 160 LHNDGP 165
Cdd:COG3709  163 IDNDGP 168
phosphon_PhnN TIGR02322
phosphonate metabolism protein/1,5-bisphosphokinase (PRPP-forming) PhnN; Members of this ...
3-165 8.11e-70

phosphonate metabolism protein/1,5-bisphosphokinase (PRPP-forming) PhnN; Members of this family resemble PhnN of phosphonate utilization operons, where different such operons confer the ability to use somewhat different profiles of C-P bond-containing compounds (see ), including phosphites as well as phosphonates. PhnN in E. coli shows considerable homology to guanylate kinases (EC 2.7.4.8), and has actually been shown to act as a ribose 1,5-bisphosphokinase (PRPP forming). This suggests an analogous kinase reaction for phosphonate metabolism, converting 5-phosphoalpha-1-(methylphosphono)ribose to methylphosphono-PRPP. [Central intermediary metabolism, Phosphorus compounds]


Pssm-ID: 274078  Cd Length: 179  Bit Score: 209.91  E-value: 8.11e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835581922    3 RLIYLMGPSGAGKDSLLAALRA--DADSAPLVAHRYITRPADAGCENHIALSEPEFLRRRAKGLFALDWQAHQQRYAFGI 80
Cdd:TIGR02322   2 RLIYVVGPSGAGKDTLLDYARArlAGDPRVHFVRRVITRPASAGGENHIALSTEEFDHREDGGAFALSWQAHGLSYGIPI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835581922   81 EVDLWLLQGIDVAVNGSRAHLPQAQQRYgAQLLPVCLQVSAGILRRRLQDRGRESAEQIEQRLARAAEYQQSlPAGCRVL 160
Cdd:TIGR02322  82 EIDQWLEAGDVVVVNGSRAVLPEARQRY-PNLLVVNITASPDVLAQRLAARGRESREEIEERLARSARFAAA-PADVTTI 159

                  ....*
gi 835581922  161 HNDGP 165
Cdd:TIGR02322 160 DNSGS 164
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
11-152 7.29e-15

Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to GDP. Structure resembles that of adenylate kinase. So-called membrane-associated guanylate kinase homologues (MAGUKs) do not possess guanylate kinase activities; instead at least some possess protein-binding functions.


Pssm-ID: 214504 [Multi-domain]  Cd Length: 174  Bit Score: 68.86  E-value: 7.29e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835581922    11 SGAGKDSLLAALRADADSAPLVAHRYITRPADAGCEN--HIAL-SEPEFLRRRAKGLFALDWQAHQQRYAFGIE-VDLWL 86
Cdd:smart00072   1 SGVGKGTLLAELIQEIPDAFERVVSHTTRPPRPGEVNgvDYHFvSKEEFEDDIKSGLFLEWGEYEGNYYGTSKEtIRQVA 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 835581922    87 LQGIDVAVNGSRAHLPQAQQRYGAQLLPVCLQVSAGILRRRLQDRGRESAEQIEQRLARA-AEYQQS 152
Cdd:smart00072  81 EKGKHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEELERRLRQRGTETSERIQKRLAAAqKEAQEY 147
Guanylate_kin pfam00625
Guanylate kinase;
1-152 5.97e-07

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 47.38  E-value: 5.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835581922    1 MARLIYLMGPSGAGKDSLLAALRA---DADSAPlVAHryITRPADAGCEN---HIALSEPEFLRRRAKGLFaLDWQAHQQ 74
Cdd:pfam00625   1 SRRPVVLSGPSGVGKSHIKKALLSeypDKFGYS-VPH--TTRPPRKGEVDgkdYYFVSKEEMERDISANEF-LEYAQFSG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835581922   75 RYaFGI---EVDLWLLQGIDVAVNGSRAHLPQAQQrygAQLLPVCLQV---SAGILRRRLQDRGRESAEQIEQRLARA-A 147
Cdd:pfam00625  77 NM-YGTsveTIEQIHEQGKIVILDVDPQGVKQLRK---AELSPISVFIkppSLKVLQRRLKGRGKEQEEKINKRMAAAeQ 152

                  ....*
gi 835581922  148 EYQQS 152
Cdd:pfam00625 153 EFQHY 157
GMPK cd00071
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ...
4-69 1.07e-03

Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), catalyzes the reversible phosphoryl transfer from adenosine triphosphate (ATP) to guanosine monophosphate (GMP) to yield adenosine diphosphate (ADP) and guanosine diphosphate (GDP). It plays an essential role in the biosynthesis of guanosine triphosphate (GTP). This enzyme is also important for the activation of some antiviral and anticancer agents, such as acyclovir, ganciclovir, carbovir, and thiopurines.


Pssm-ID: 238026  Cd Length: 137  Bit Score: 37.51  E-value: 1.07e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 835581922   4 LIYLMGPSGAGKDSLLAALRADADSaplvAHRYI----TRPADAGCENHI---ALSEPEFLRRRAKGLFaLDW 69
Cdd:cd00071    1 LIVLSGPSGVGKSTLLKRLLEEFDP----NFGFSvshtTRKPRPGEVDGVdyhFVSKEEFERLIENGEF-LEW 68
 
Name Accession Description Interval E-value
PRK10078 PRK10078
ribose 1,5-bisphosphokinase; Provisional
1-164 1.01e-94

ribose 1,5-bisphosphokinase; Provisional


Pssm-ID: 236648  Cd Length: 186  Bit Score: 273.16  E-value: 1.01e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835581922   1 MARLIYLMGPSGAGKDSLLAALRADADSAPLVAHRYITRPADAGCENHIALSEPEFLRRRAKGLFALDWQAHQQRYAFGI 80
Cdd:PRK10078   1 MGKLIWLMGPSGSGKDSLLAALRQREQTQLLVAHRYITRPASAGSENHIALSEQEFFTRAGQNLFALSWHANGLYYGVGI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835581922  81 EVDLWLLQGIDVAVNGSRAHLPQAQQRYGAQLLPVCLQVSAGILRRRLQDRGRESAEQIEQRLARAAEYQqslPAGCRVL 160
Cdd:PRK10078  81 EIDLWLHAGFDVLVNGSRAHLPQARARYQSALLPVCLQVSPEILRQRLENRGRENASEINARLARAARYQ---PQDCHTL 157

                 ....
gi 835581922 161 HNDG 164
Cdd:PRK10078 158 NNDG 161
PhnN COG3709
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
2-165 5.43e-84

Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];


Pssm-ID: 442923  Cd Length: 188  Bit Score: 245.87  E-value: 5.43e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835581922   2 ARLIYLMGPSGAGKDSLLAALRA--DADSAPLVAHRYITRPADAGCENHIALSEPEFLRRRAKGLFALDWQAHQQRYAFG 79
Cdd:COG3709    5 GRLIYVVGPSGAGKDSLLAAARArlAADPRLVFARRYITRPADAGGEDHDALSEAEFARRAAAGAFALHWQAHGLRYGIP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835581922  80 IEVDLWLLQGIDVAVNGSRAHLPQAQQRYgAQLLPVCLQVSAGILRRRLQDRGRESAEQIEQRLARAAEYQQsLPAGCRV 159
Cdd:COG3709   85 AEIDAWLAAGRDVVVNGSRAVLPQARARY-PRLLVVLITASPEVLAQRLAARGRESAEEIEARLARAAEFLP-DGPDVLV 162

                 ....*.
gi 835581922 160 LHNDGP 165
Cdd:COG3709  163 IDNDGP 168
phosphon_PhnN TIGR02322
phosphonate metabolism protein/1,5-bisphosphokinase (PRPP-forming) PhnN; Members of this ...
3-165 8.11e-70

phosphonate metabolism protein/1,5-bisphosphokinase (PRPP-forming) PhnN; Members of this family resemble PhnN of phosphonate utilization operons, where different such operons confer the ability to use somewhat different profiles of C-P bond-containing compounds (see ), including phosphites as well as phosphonates. PhnN in E. coli shows considerable homology to guanylate kinases (EC 2.7.4.8), and has actually been shown to act as a ribose 1,5-bisphosphokinase (PRPP forming). This suggests an analogous kinase reaction for phosphonate metabolism, converting 5-phosphoalpha-1-(methylphosphono)ribose to methylphosphono-PRPP. [Central intermediary metabolism, Phosphorus compounds]


Pssm-ID: 274078  Cd Length: 179  Bit Score: 209.91  E-value: 8.11e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835581922    3 RLIYLMGPSGAGKDSLLAALRA--DADSAPLVAHRYITRPADAGCENHIALSEPEFLRRRAKGLFALDWQAHQQRYAFGI 80
Cdd:TIGR02322   2 RLIYVVGPSGAGKDTLLDYARArlAGDPRVHFVRRVITRPASAGGENHIALSTEEFDHREDGGAFALSWQAHGLSYGIPI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835581922   81 EVDLWLLQGIDVAVNGSRAHLPQAQQRYgAQLLPVCLQVSAGILRRRLQDRGRESAEQIEQRLARAAEYQQSlPAGCRVL 160
Cdd:TIGR02322  82 EIDQWLEAGDVVVVNGSRAVLPEARQRY-PNLLVVNITASPDVLAQRLAARGRESREEIEERLARSARFAAA-PADVTTI 159

                  ....*
gi 835581922  161 HNDGP 165
Cdd:TIGR02322 160 DNSGS 164
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
11-152 7.29e-15

Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to GDP. Structure resembles that of adenylate kinase. So-called membrane-associated guanylate kinase homologues (MAGUKs) do not possess guanylate kinase activities; instead at least some possess protein-binding functions.


Pssm-ID: 214504 [Multi-domain]  Cd Length: 174  Bit Score: 68.86  E-value: 7.29e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835581922    11 SGAGKDSLLAALRADADSAPLVAHRYITRPADAGCEN--HIAL-SEPEFLRRRAKGLFALDWQAHQQRYAFGIE-VDLWL 86
Cdd:smart00072   1 SGVGKGTLLAELIQEIPDAFERVVSHTTRPPRPGEVNgvDYHFvSKEEFEDDIKSGLFLEWGEYEGNYYGTSKEtIRQVA 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 835581922    87 LQGIDVAVNGSRAHLPQAQQRYGAQLLPVCLQVSAGILRRRLQDRGRESAEQIEQRLARA-AEYQQS 152
Cdd:smart00072  81 EKGKHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEELERRLRQRGTETSERIQKRLAAAqKEAQEY 147
Gmk COG0194
Guanylate kinase [Nucleotide transport and metabolism];
3-148 3.02e-14

Guanylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 439964  Cd Length: 190  Bit Score: 67.40  E-value: 3.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835581922   3 RLIYLMGPSGAGKDSLLAALRADADSAPLVAhRYITRPADAGCENHIA---LSEPEFLRRRAKGLFaLDW-QAHQQRYaf 78
Cdd:COG0194    3 KLIVLSGPSGAGKTTLVKALLERDPDLRFSV-SATTRPPRPGEVDGVDyhfVSREEFERMIENGEF-LEWaEVHGNYY-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835581922  79 GI---EVDLWLLQGIDV----AVNGSRahlpQAQQRYG-AQ---LLPVCLQVsagiLRRRLQDRGRESAEQIEQRLARAA 147
Cdd:COG0194   79 GTpkaEVEEALAAGKDVlleiDVQGAR----QVKKKFPdAVsifILPPSLEE----LERRLRGRGTDSEEVIERRLAKAR 150

                 .
gi 835581922 148 E 148
Cdd:COG0194  151 E 151
gmk PRK00300
guanylate kinase; Provisional
3-148 1.98e-12

guanylate kinase; Provisional


Pssm-ID: 234719  Cd Length: 205  Bit Score: 62.80  E-value: 1.98e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835581922   3 RLIYLMGPSGAGKDSLLAALRADADSAPL-VAHryITRPADAGcENH----IALSEPEFLRRRAKGLFaLDW-QAHQQRY 76
Cdd:PRK00300   6 LLIVLSGPSGAGKSTLVKALLERDPNLQLsVSA--TTRAPRPG-EVDgvdyFFVSKEEFEEMIENGEF-LEWaEVFGNYY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835581922  77 afGI---EVDLWLLQGIDVA----VNGSRahlpQAQQRYG-AQ---LLPVCLQVsagiLRRRLQDRGRESAEQIEQRLAR 145
Cdd:PRK00300  82 --GTprsPVEEALAAGKDVLleidWQGAR----QVKKKMPdAVsifILPPSLEE----LERRLRGRGTDSEEVIARRLAK 151

                 ...
gi 835581922 146 AAE 148
Cdd:PRK00300 152 ARE 154
Guanylate_kin pfam00625
Guanylate kinase;
1-152 5.97e-07

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 47.38  E-value: 5.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835581922    1 MARLIYLMGPSGAGKDSLLAALRA---DADSAPlVAHryITRPADAGCEN---HIALSEPEFLRRRAKGLFaLDWQAHQQ 74
Cdd:pfam00625   1 SRRPVVLSGPSGVGKSHIKKALLSeypDKFGYS-VPH--TTRPPRKGEVDgkdYYFVSKEEMERDISANEF-LEYAQFSG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835581922   75 RYaFGI---EVDLWLLQGIDVAVNGSRAHLPQAQQrygAQLLPVCLQV---SAGILRRRLQDRGRESAEQIEQRLARA-A 147
Cdd:pfam00625  77 NM-YGTsveTIEQIHEQGKIVILDVDPQGVKQLRK---AELSPISVFIkppSLKVLQRRLKGRGKEQEEKINKRMAAAeQ 152

                  ....*
gi 835581922  148 EYQQS 152
Cdd:pfam00625 153 EFQHY 157
gmk PRK14738
guanylate kinase; Provisional
3-155 3.15e-05

guanylate kinase; Provisional


Pssm-ID: 237809  Cd Length: 206  Bit Score: 42.80  E-value: 3.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835581922   3 RLIYLMGPSGAGKDSLLAALRadadSAPLVAHRYIT------RPADAGCENHIALSEPEFLRRRAKGLFaLDWQAHQQRY 76
Cdd:PRK14738  14 LLVVISGPSGVGKDAVLARMR----ERKLPFHFVVTattrpkRPGEIDGVDYHFVTPEEFREMISQNEL-LEWAEVYGNY 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835581922  77 aFGI---EVDLWLLQGIDVA----VNGS---RAHLPQAqqrygaqLLPVCLQVSAGILRRRLQDRGRESAEQIEQRLARA 146
Cdd:PRK14738  89 -YGVpkaPVRQALASGRDVIvkvdVQGAasiKRLVPEA-------VFIFLAPPSMDELTRRLELRRTESPEELERRLATA 160

                 ....*....
gi 835581922 147 AEYQQSLPA 155
Cdd:PRK14738 161 PLELEQLPE 169
GMPK cd00071
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ...
4-69 1.07e-03

Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), catalyzes the reversible phosphoryl transfer from adenosine triphosphate (ATP) to guanosine monophosphate (GMP) to yield adenosine diphosphate (ADP) and guanosine diphosphate (GDP). It plays an essential role in the biosynthesis of guanosine triphosphate (GTP). This enzyme is also important for the activation of some antiviral and anticancer agents, such as acyclovir, ganciclovir, carbovir, and thiopurines.


Pssm-ID: 238026  Cd Length: 137  Bit Score: 37.51  E-value: 1.07e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 835581922   4 LIYLMGPSGAGKDSLLAALRADADSaplvAHRYI----TRPADAGCENHI---ALSEPEFLRRRAKGLFaLDW 69
Cdd:cd00071    1 LIVLSGPSGVGKSTLLKRLLEEFDP----NFGFSvshtTRKPRPGEVDGVdyhFVSKEEFERLIENGEF-LEW 68
gmk PRK14737
guanylate kinase; Provisional
3-143 1.17e-03

guanylate kinase; Provisional


Pssm-ID: 173199  Cd Length: 186  Bit Score: 38.05  E-value: 1.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835581922   3 RLIYLMGPSGAGKDSLLAALRAD----------ADSAPlvahryitRPADAGCENHIALSEPEFLRRRAKGLFaLDW-QA 71
Cdd:PRK14737   5 KLFIISSVAGGGKSTIIQALLEEhpdflfsiscTTRAP--------RPGDEEGKTYFFLTIEEFKKGIADGEF-LEWaEV 75
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 835581922  72 HQQRYAFGIEVDLWLLQG-----IDVAVNGSRAhlpQAQQRYGAQLLPVCLQVSAGILRRRLQDRGRESAEQIEQRL 143
Cdd:PRK14737  76 HDNYYGTPKAFIEDAFKEgrsaiMDIDVQGAKI---IKEKFPERIVTIFIEPPSEEEWEERLIHRGTDSEESIEKRI 149
 
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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