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Conserved domains on  [gi|2214515445|ref|WP_242873529|]
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MULTISPECIES: guanylate kinase [Eubacterium]

Protein Classification

guanylate kinase( domain architecture ID 11415171)

guanylate kinase (GMP kinase) catalyzes the transfer of a phosphate group from ATP to guanosine monophosphate (GMP) to form guanosine diphosphate (GDP) and ADP

EC:  2.7.4.8
Gene Ontology:  GO:0004385|GO:0006163|GO:0005524

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Gmk COG0194
Guanylate kinase [Nucleotide transport and metabolism];
14-201 2.24e-101

Guanylate kinase [Nucleotide transport and metabolism];


:

Pssm-ID: 439964  Cd Length: 190  Bit Score: 291.20  E-value: 2.24e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214515445  14 RGILIVISGPSCAGKGTVCRIVRDDQPDIRMSISETTREPRNYEKDGVDYFFVDKASFETGIREGKYLEYAQVYGNYYGT 93
Cdd:COG0194     1 RGKLIVLSGPSGAGKTTLVKALLERDPDLRFSVSATTRPPRPGEVDGVDYHFVSREEFERMIENGEFLEWAEVHGNYYGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214515445  94 PKEFVENLLNSGYDVILEIDIQGAAKVRQNNKEGIYIFIAPPSMKELRRRIEMRGTESEEQMALRLQCAHDEMSNADDYS 173
Cdd:COG0194    81 PKAEVEEALAAGKDVLLEIDVQGARQVKKKFPDAVSIFILPPSLEELERRLRGRGTDSEEVIERRLAKAREELAHADEFD 160

                         170       180
                  ....*....|....*....|....*...
gi 2214515445 174 YIVINQDKDVAAKQVEAIITAEKCRTER 201
Cdd:COG0194   161 YVVVNDDLDRAVEELKAIIRAERLRRER 188
 
Name Accession Description Interval E-value
Gmk COG0194
Guanylate kinase [Nucleotide transport and metabolism];
14-201 2.24e-101

Guanylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 439964  Cd Length: 190  Bit Score: 291.20  E-value: 2.24e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214515445  14 RGILIVISGPSCAGKGTVCRIVRDDQPDIRMSISETTREPRNYEKDGVDYFFVDKASFETGIREGKYLEYAQVYGNYYGT 93
Cdd:COG0194     1 RGKLIVLSGPSGAGKTTLVKALLERDPDLRFSVSATTRPPRPGEVDGVDYHFVSREEFERMIENGEFLEWAEVHGNYYGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214515445  94 PKEFVENLLNSGYDVILEIDIQGAAKVRQNNKEGIYIFIAPPSMKELRRRIEMRGTESEEQMALRLQCAHDEMSNADDYS 173
Cdd:COG0194    81 PKAEVEEALAAGKDVLLEIDVQGARQVKKKFPDAVSIFILPPSLEELERRLRGRGTDSEEVIERRLAKAREELAHADEFD 160

                         170       180
                  ....*....|....*....|....*...
gi 2214515445 174 YIVINQDKDVAAKQVEAIITAEKCRTER 201
Cdd:COG0194   161 YVVVNDDLDRAVEELKAIIRAERLRRER 188
gmk PRK00300
guanylate kinase; Provisional
 12-210 6.46e-101

guanylate kinase; Provisional


Pssm-ID: 234719  Cd Length: 205  Bit Score: 290.45  E-value: 6.46e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214515445  12 KERGILIVISGPSCAGKGTVCRIVRDDQPDIRMSISETTREPRNYEKDGVDYFFVDKASFETGIREGKYLEYAQVYGNYY 91
Cdd:PRK00300    2 MRRGLLIVLSGPSGAGKSTLVKALLERDPNLQLSVSATTRAPRPGEVDGVDYFFVSKEEFEEMIENGEFLEWAEVFGNYY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214515445  92 GTPKEFVENLLNSGYDVILEIDIQGAAKVRQNNKEGIYIFIAPPSMKELRRRIEMRGTESEEQMALRLQCAHDEMSNADD 171
Cdd:PRK00300   82 GTPRSPVEEALAAGKDVLLEIDWQGARQVKKKMPDAVSIFILPPSLEELERRLRGRGTDSEEVIARRLAKAREEIAHASE 161

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2214515445 172 YSYIVINQDKDVAAKQVEAIITAEKCRTERLKNKVVEIL 210
Cdd:PRK00300  162 YDYVIVNDDLDTALEELKAIIRAERLRRSRQQQRHAELI 200
guanyl_kin TIGR03263
guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP ...
 17-194 2.00e-90

guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP kinase. This enzyme transfers a phosphate from ATP to GMP, yielding ADP and GDP. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]


Pssm-ID: 213788  Cd Length: 179  Bit Score: 262.81  E-value: 2.00e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214515445  17 LIVISGPSCAGKGTVCRIVRDDQPDIRMSISETTREPRNYEKDGVDYFFVDKASFETGIREGKYLEYAQVYGNYYGTPKE 96
Cdd:TIGR03263   2 LIVISGPSGAGKSTLVKALLEEDPNLKFSISATTRKPRPGEVDGVDYFFVSKEEFEEMIKAGEFLEWAEVHGNYYGTPKS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214515445  97 FVENLLNSGYDVILEIDIQGAAKVRQNNKEGIYIFIAPPSMKELRRRIEMRGTESEEQMALRLQCAHDEMSNADDYSYIV 176
Cdd:TIGR03263  82 PVEEALAAGKDVLLEIDVQGARQVKKKFPDAVSIFILPPSLEELERRLRKRGTDSEEVIERRLAKAKKEIAHADEFDYVI 161

                         170
                  ....*....|....*...
gi 2214515445 177 INQDKDVAAKQVEAIITA 194
Cdd:TIGR03263 162 VNDDLEKAVEELKSIILA 179
GMPK cd00071
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ...
 17-135 3.81e-56

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: 174.64  E-value: 3.81e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214515445  17 LIVISGPSCAGKGTVC-RIVRDDQPDIRMSISETTREPRNYEKDGVDYFFVDKASFETGIREGKYLEYAQVYGNYYGTPK 95
Cdd:cd00071     1 LIVLSGPSGVGKSTLLkRLLEEFDPNFGFSVSHTTRKPRPGEVDGVDYHFVSKEEFERLIENGEFLEWAEFHGNYYGTSK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2214515445  96 EFVENLLNSGYDVILEIDIQGAAKVRQNNKEGIYIFIAPP 135
Cdd:cd00071    81 AAVEEALAEGKIVILEIDVQGARQVKKSYPDAVSIFILPP 120
Guanylate_kin pfam00625
Guanylate kinase;
17-195 3.30e-46

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 150.99  E-value: 3.30e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214515445  17 LIVISGPSCAGKGTVCRIVRDDQPDI-RMSISETTREPRNYEKDGVDYFFVDKASFETGIREGKYLEYAQVYGNYYGTPK 95
Cdd:pfam00625   4 PVVLSGPSGVGKSHIKKALLSEYPDKfGYSVPHTTRPPRKGEVDGKDYYFVSKEEMERDISANEFLEYAQFSGNMYGTSV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214515445  96 EFVENLLNSGYDVILEIDIQGAAKVRQNNKEGIYIFIAPPSMKELRRRIEMRGTESEEQMALRLQCAHDEMSNAdDYSYI 175
Cdd:pfam00625  84 ETIEQIHEQGKIVILDVDPQGVKQLRKAELSPISVFIKPPSLKVLQRRLKGRGKEQEEKINKRMAAAEQEFQHY-EFDVI 162

                         170       180
                  ....*....|....*....|
gi 2214515445 176 VINQDKDVAAKQVEAIITAE 195
Cdd:pfam00625 163 IVNDDLEEAYKKLKEALEAE 182
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
 24-196 5.46e-46

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: 150.14  E-value: 5.46e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214515445   24 SCAGKGTVCRIVRDDQPDI-RMSISETTREPRNYEKDGVDYFFVDKASFETGIREGKYLEYAQVYGNYYGTPKEFVENLL 102
Cdd:smart00072   1 SGVGKGTLLAELIQEIPDAfERVVSHTTRPPRPGEVNGVDYHFVSKEEFEDDIKSGLFLEWGEYEGNYYGTSKETIRQVA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214515445  103 NSGYDVILEIDIQGAAKVRQNNKEGIYIFIAPPSMKELRRRIEMRGTESEEQMALRLQCAHDEMSNADDYSYIVINQDKD 182
Cdd:smart00072  81 EKGKHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEELERRLRQRGTETSERIQKRLAAAQKEAQEYHLFDYVIVNDDLE 160

                          170
                   ....*....|....
gi 2214515445  183 VAAKQVEAIITAEK 196
Cdd:smart00072 161 DAYEELKEILEAEQ 174
 
Name Accession Description Interval E-value
Gmk COG0194
Guanylate kinase [Nucleotide transport and metabolism];
14-201 2.24e-101

Guanylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 439964  Cd Length: 190  Bit Score: 291.20  E-value: 2.24e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214515445  14 RGILIVISGPSCAGKGTVCRIVRDDQPDIRMSISETTREPRNYEKDGVDYFFVDKASFETGIREGKYLEYAQVYGNYYGT 93
Cdd:COG0194     1 RGKLIVLSGPSGAGKTTLVKALLERDPDLRFSVSATTRPPRPGEVDGVDYHFVSREEFERMIENGEFLEWAEVHGNYYGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214515445  94 PKEFVENLLNSGYDVILEIDIQGAAKVRQNNKEGIYIFIAPPSMKELRRRIEMRGTESEEQMALRLQCAHDEMSNADDYS 173
Cdd:COG0194    81 PKAEVEEALAAGKDVLLEIDVQGARQVKKKFPDAVSIFILPPSLEELERRLRGRGTDSEEVIERRLAKAREELAHADEFD 160

                         170       180
                  ....*....|....*....|....*...
gi 2214515445 174 YIVINQDKDVAAKQVEAIITAEKCRTER 201
Cdd:COG0194   161 YVVVNDDLDRAVEELKAIIRAERLRRER 188
gmk PRK00300
guanylate kinase; Provisional
 12-210 6.46e-101

guanylate kinase; Provisional


Pssm-ID: 234719  Cd Length: 205  Bit Score: 290.45  E-value: 6.46e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214515445  12 KERGILIVISGPSCAGKGTVCRIVRDDQPDIRMSISETTREPRNYEKDGVDYFFVDKASFETGIREGKYLEYAQVYGNYY 91
Cdd:PRK00300    2 MRRGLLIVLSGPSGAGKSTLVKALLERDPNLQLSVSATTRAPRPGEVDGVDYFFVSKEEFEEMIENGEFLEWAEVFGNYY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214515445  92 GTPKEFVENLLNSGYDVILEIDIQGAAKVRQNNKEGIYIFIAPPSMKELRRRIEMRGTESEEQMALRLQCAHDEMSNADD 171
Cdd:PRK00300   82 GTPRSPVEEALAAGKDVLLEIDWQGARQVKKKMPDAVSIFILPPSLEELERRLRGRGTDSEEVIARRLAKAREEIAHASE 161

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2214515445 172 YSYIVINQDKDVAAKQVEAIITAEKCRTERLKNKVVEIL 210
Cdd:PRK00300  162 YDYVIVNDDLDTALEELKAIIRAERLRRSRQQQRHAELI 200
guanyl_kin TIGR03263
guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP ...
 17-194 2.00e-90

guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP kinase. This enzyme transfers a phosphate from ATP to GMP, yielding ADP and GDP. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]


Pssm-ID: 213788  Cd Length: 179  Bit Score: 262.81  E-value: 2.00e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214515445  17 LIVISGPSCAGKGTVCRIVRDDQPDIRMSISETTREPRNYEKDGVDYFFVDKASFETGIREGKYLEYAQVYGNYYGTPKE 96
Cdd:TIGR03263   2 LIVISGPSGAGKSTLVKALLEEDPNLKFSISATTRKPRPGEVDGVDYFFVSKEEFEEMIKAGEFLEWAEVHGNYYGTPKS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214515445  97 FVENLLNSGYDVILEIDIQGAAKVRQNNKEGIYIFIAPPSMKELRRRIEMRGTESEEQMALRLQCAHDEMSNADDYSYIV 176
Cdd:TIGR03263  82 PVEEALAAGKDVLLEIDVQGARQVKKKFPDAVSIFILPPSLEELERRLRKRGTDSEEVIERRLAKAKKEIAHADEFDYVI 161

                         170
                  ....*....|....*...
gi 2214515445 177 INQDKDVAAKQVEAIITA 194
Cdd:TIGR03263 162 VNDDLEKAVEELKSIILA 179
gmk PRK14738
guanylate kinase; Provisional
 9-198 1.55e-62

guanylate kinase; Provisional


Pssm-ID: 237809  Cd Length: 206  Bit Score: 193.41  E-value: 1.55e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214515445   9 FFEKERGILIVISGPSCAGKGTVCRIVRDDQPDIRMSISETTREPRNYEKDGVDYFFVDKASFETGIREGKYLEYAQVYG 88
Cdd:PRK14738    7 FNKPAKPLLVVISGPSGVGKDAVLARMRERKLPFHFVVTATTRPKRPGEIDGVDYHFVTPEEFREMISQNELLEWAEVYG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214515445  89 NYYGTPKEFVENLLNSGYDVILEIDIQGAAKVRQNNKEGIYIFIAPPSMKELRRRIEMRGTESEEQMALRLQCAHDEMSN 168
Cdd:PRK14738   87 NYYGVPKAPVRQALASGRDVIVKVDVQGAASIKRLVPEAVFIFLAPPSMDELTRRLELRRTESPEELERRLATAPLELEQ 166

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2214515445 169 ADDYSYIVINQDK--DVAAKQVEAIITAEKCR 198
Cdd:PRK14738  167 LPEFDYVVVNPEDrlDEAVAQIMAIISAEKSR 198
GMPK cd00071
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ...
 17-135 3.81e-56

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: 174.64  E-value: 3.81e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214515445  17 LIVISGPSCAGKGTVC-RIVRDDQPDIRMSISETTREPRNYEKDGVDYFFVDKASFETGIREGKYLEYAQVYGNYYGTPK 95
Cdd:cd00071     1 LIVLSGPSGVGKSTLLkRLLEEFDPNFGFSVSHTTRKPRPGEVDGVDYHFVSKEEFERLIENGEFLEWAEFHGNYYGTSK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2214515445  96 EFVENLLNSGYDVILEIDIQGAAKVRQNNKEGIYIFIAPP 135
Cdd:cd00071    81 AAVEEALAEGKIVILEIDVQGARQVKKSYPDAVSIFILPP 120
PLN02772 PLN02772
guanylate kinase
 18-192 2.91e-52

guanylate kinase


Pssm-ID: 215414 [Multi-domain]  Cd Length: 398  Bit Score: 172.71  E-value: 2.91e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214515445  18 IVISGPSCAGKGTVCRIVRDDQPDI-RMSISETTREPRNYEKDGVDYFFVDKASFETGIREGKYLEYAQVYGNYYGTPKE 96
Cdd:PLN02772  138 IVISGPSGVGKGTLISMLMKEFPSMfGFSVSHTTRAPREMEKDGVHYHFTERSVMEKEIKDGKFLEFASVHGNLYGTSIE 217

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214515445  97 FVENLLNSGYDVILEIDIQGAAKVRQNNKEGIYIFIAPPSMKELRRRIEMRGTESEEQMALRLQCAHDEMSNADD---YS 173
Cdd:PLN02772  218 AVEVVTDSGKRCILDIDVQGARSVRASSLEAIFIFICPPSMEELEKRLRARGTETEEQIQKRLRNAEAELEQGKSsgiFD 297

                         170
                  ....*....|....*....
gi 2214515445 174 YIVINQDKDVAAKQVEAII 192
Cdd:PLN02772  298 HILYNDNLEECYKNLKKLL 316
gmk PRK14737
guanylate kinase; Provisional
 17-196 1.66e-46

guanylate kinase; Provisional


Pssm-ID: 173199  Cd Length: 186  Bit Score: 151.68  E-value: 1.66e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214515445  17 LIVISGPSCAGKGTVCRIVRDDQPDIRMSISETTREPRNYEKDGVDYFFVDKASFETGIREGKYLEYAQVYGNYYGTPKE 96
Cdd:PRK14737    6 LFIISSVAGGGKSTIIQALLEEHPDFLFSISCTTRAPRPGDEEGKTYFFLTIEEFKKGIADGEFLEWAEVHDNYYGTPKA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214515445  97 FVENLLNSGYDVILEIDIQGAAKVRQNNKEGIY-IFIAPPSMKELRRRIEMRGTESEEQMALRLQCAHDEMSNADDYSYI 175
Cdd:PRK14737   86 FIEDAFKEGRSAIMDIDVQGAKIIKEKFPERIVtIFIEPPSEEEWEERLIHRGTDSEESIEKRIENGIIELDEANEFDYK 165

                         170       180
                  ....*....|....*....|.
gi 2214515445 176 VINQDKDVAAKQVEAIITAEK 196
Cdd:PRK14737  166 IINDDLEDAIADLEAIICGKK 186
Guanylate_kin pfam00625
Guanylate kinase;
17-195 3.30e-46

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 150.99  E-value: 3.30e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214515445  17 LIVISGPSCAGKGTVCRIVRDDQPDI-RMSISETTREPRNYEKDGVDYFFVDKASFETGIREGKYLEYAQVYGNYYGTPK 95
Cdd:pfam00625   4 PVVLSGPSGVGKSHIKKALLSEYPDKfGYSVPHTTRPPRKGEVDGKDYYFVSKEEMERDISANEFLEYAQFSGNMYGTSV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214515445  96 EFVENLLNSGYDVILEIDIQGAAKVRQNNKEGIYIFIAPPSMKELRRRIEMRGTESEEQMALRLQCAHDEMSNAdDYSYI 175
Cdd:pfam00625  84 ETIEQIHEQGKIVILDVDPQGVKQLRKAELSPISVFIKPPSLKVLQRRLKGRGKEQEEKINKRMAAAEQEFQHY-EFDVI 162

                         170       180
                  ....*....|....*....|
gi 2214515445 176 VINQDKDVAAKQVEAIITAE 195
Cdd:pfam00625 163 IVNDDLEEAYKKLKEALEAE 182
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
 24-196 5.46e-46

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: 150.14  E-value: 5.46e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214515445   24 SCAGKGTVCRIVRDDQPDI-RMSISETTREPRNYEKDGVDYFFVDKASFETGIREGKYLEYAQVYGNYYGTPKEFVENLL 102
Cdd:smart00072   1 SGVGKGTLLAELIQEIPDAfERVVSHTTRPPRPGEVNGVDYHFVSKEEFEDDIKSGLFLEWGEYEGNYYGTSKETIRQVA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214515445  103 NSGYDVILEIDIQGAAKVRQNNKEGIYIFIAPPSMKELRRRIEMRGTESEEQMALRLQCAHDEMSNADDYSYIVINQDKD 182
Cdd:smart00072  81 EKGKHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEELERRLRQRGTETSERIQKRLAAAQKEAQEYHLFDYVIVNDDLE 160

                          170
                   ....*....|....
gi 2214515445  183 VAAKQVEAIITAEK 196
Cdd:smart00072 161 DAYEELKEILEAEQ 174
PhnN COG3709
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
13-200 5.72e-13

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


Pssm-ID: 442923  Cd Length: 188  Bit Score: 64.44  E-value: 5.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214515445  13 ERGILIVISGPSCAGKGTVCRIVRD---DQPDI---RMSIsetTREPrnyEKDGVDYFFVDKASFETGIREGKYLEYAQV 86
Cdd:COG3709     3 GPGRLIYVVGPSGAGKDSLLAAARArlaADPRLvfaRRYI---TRPA---DAGGEDHDALSEAEFARRAAAGAFALHWQA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214515445  87 YGNYYGTPKEfVENLLNSGYDVILEI--DIQGAAKVRQNNKEGIYIfIAPPSMkeLRRRIEMRGTESEEQMALRLQCAHD 164
Cdd:COG3709    77 HGLRYGIPAE-IDAWLAAGRDVVVNGsrAVLPQARARYPRLLVVLI-TASPEV--LAQRLAARGRESAEEIEARLARAAE 152

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2214515445 165 EMSNADDYSYIVINQDKDVAAKQVEAIITAEKCRTE 200
Cdd:COG3709   153 FLPDGPDVLVIDNDGPLEDAGARLLALLRAARARAA 188
phosphon_PhnN TIGR02322
phosphonate metabolism protein/1,5-bisphosphokinase (PRPP-forming) PhnN; Members of this ...
 15-195 9.88e-10

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: 55.45  E-value: 9.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214515445  15 GILIVISGPSCAGKGTVCRIVRD---DQPDIRMSISETTREPrnyEKDGVDYFFVDKASFETGIREGKYLEYAQVYGNYY 91
Cdd:TIGR02322   1 GRLIYVVGPSGAGKDTLLDYARArlaGDPRVHFVRRVITRPA---SAGGENHIALSTEEFDHREDGGAFALSWQAHGLSY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214515445  92 GTPKEfVENLLNSGYDVILEIDIQGAAKVRQNNKEGIYIFI-APPSMkeLRRRIEMRGTESEEQMALRLQCAHDEMSNAD 170
Cdd:TIGR02322  78 GIPIE-IDQWLEAGDVVVVNGSRAVLPEARQRYPNLLVVNItASPDV--LAQRLAARGRESREEIEERLARSARFAAAPA 154

                         170       180
                  ....*....|....*....|....*
gi 2214515445 171 DYSYIVINQDKDVAAKQVEAIITAE 195
Cdd:TIGR02322 155 DVTTIDNSGSLEVAGETLLRLLRKE 179
PRK10078 PRK10078
ribose 1,5-bisphosphokinase; Provisional
 15-165 7.31e-04

ribose 1,5-bisphosphokinase; Provisional


Pssm-ID: 236648  Cd Length: 186  Bit Score: 38.96  E-value: 7.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214515445  15 GILIVISGPSCAGKGTVCRIVRDDQPDIRMSISETTREPRNyeKDGVDYFFVDKASFETGIREGKYLEYAQVYGNYYGTP 94
Cdd:PRK10078    2 GKLIWLMGPSGSGKDSLLAALRQREQTQLLVAHRYITRPAS--AGSENHIALSEQEFFTRAGQNLFALSWHANGLYYGVG 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2214515445  95 KEfVENLLNSGYDVILEIDIQGAAKVRQNNKEGIYIFIAPPSMKELRRRIEMRGTESEEQMALRLQCAHDE 165
Cdd:PRK10078   80 IE-IDLWLHAGFDVLVNGSRAHLPQARARYQSALLPVCLQVSPEILRQRLENRGRENASEINARLARAARY 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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