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Conserved domains on  [gi|506223188|ref|WP_015742963|]
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guanylate kinase [Cronobacter turicensis]

Protein Classification

guanylate kinase( domain architecture ID 10011364)

guanosine monophosphate kinase (GMPK), also known as guanylate kinase (GKase)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
gmk PRK00300
guanylate kinase; Provisional
1-206 2.97e-135

guanylate kinase; Provisional


:

Pssm-ID: 234719  Cd Length: 205  Bit Score: 377.12  E-value: 2.97e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506223188   1 MAQGTLYIVSAPSGAGKSSLIQAFLKTQPlyDSQVSVSHTTRNPRPGEVHGEHYYFVSHDQFRSMIAEDAFLEHAEVFGN 80
Cdd:PRK00300   2 MRRGLLIVLSGPSGAGKSTLVKALLERDP--NLQLSVSATTRAPRPGEVDGVDYFFVSKEEFEEMIENGEFLEWAEVFGN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506223188  81 YYGTSRAAIEQVLATGVDVFLDIDWQGARQIREKMPQARSIFILPPSKEELDRRLRGRGQDSEEVIAKRMAQAVAEMSHY 160
Cdd:PRK00300  80 YYGTPRSPVEEALAAGKDVLLEIDWQGARQVKKKMPDAVSIFILPPSLEELERRLRGRGTDSEEVIARRLAKAREEIAHA 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 506223188 161 AEYDYLIVNDDFDAALADLKIILRAERLRMSRQKQRHDALITKLLA 206
Cdd:PRK00300 160 SEYDYVIVNDDLDTALEELKAIIRAERLRRSRQQQRHAELIEELLA 205
 
Name Accession Description Interval E-value
gmk PRK00300
guanylate kinase; Provisional
1-206 2.97e-135

guanylate kinase; Provisional


Pssm-ID: 234719  Cd Length: 205  Bit Score: 377.12  E-value: 2.97e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506223188   1 MAQGTLYIVSAPSGAGKSSLIQAFLKTQPlyDSQVSVSHTTRNPRPGEVHGEHYYFVSHDQFRSMIAEDAFLEHAEVFGN 80
Cdd:PRK00300   2 MRRGLLIVLSGPSGAGKSTLVKALLERDP--NLQLSVSATTRAPRPGEVDGVDYFFVSKEEFEEMIENGEFLEWAEVFGN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506223188  81 YYGTSRAAIEQVLATGVDVFLDIDWQGARQIREKMPQARSIFILPPSKEELDRRLRGRGQDSEEVIAKRMAQAVAEMSHY 160
Cdd:PRK00300  80 YYGTPRSPVEEALAAGKDVLLEIDWQGARQVKKKMPDAVSIFILPPSLEELERRLRGRGTDSEEVIARRLAKAREEIAHA 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 506223188 161 AEYDYLIVNDDFDAALADLKIILRAERLRMSRQKQRHDALITKLLA 206
Cdd:PRK00300 160 SEYDYVIVNDDLDTALEELKAIIRAERLRRSRQQQRHAELIEELLA 205
Gmk COG0194
Guanylate kinase [Nucleotide transport and metabolism];
3-194 8.55e-124

Guanylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 439964  Cd Length: 190  Bit Score: 347.44  E-value: 8.55e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506223188   3 QGTLYIVSAPSGAGKSSLIQAFLKTQPlyDSQVSVSHTTRNPRPGEVHGEHYYFVSHDQFRSMIAEDAFLEHAEVFGNYY 82
Cdd:COG0194    1 RGKLIVLSGPSGAGKTTLVKALLERDP--DLRFSVSATTRPPRPGEVDGVDYHFVSREEFERMIENGEFLEWAEVHGNYY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506223188  83 GTSRAAIEQVLATGVDVFLDIDWQGARQIREKMPQARSIFILPPSKEELDRRLRGRGQDSEEVIAKRMAQAVAEMSHYAE 162
Cdd:COG0194   79 GTPKAEVEEALAAGKDVLLEIDVQGARQVKKKFPDAVSIFILPPSLEELERRLRGRGTDSEEVIERRLAKAREELAHADE 158
                        170       180       190
                 ....*....|....*....|....*....|..
gi 506223188 163 YDYLIVNDDFDAALADLKIILRAERLRMSRQK 194
Cdd:COG0194  159 FDYVVVNDDLDRAVEELKAIIRAERLRRERQA 190
guanyl_kin TIGR03263
guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP ...
6-185 3.58e-115

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: 325.22  E-value: 3.58e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506223188    6 LYIVSAPSGAGKSSLIQAFLKTQPlyDSQVSVSHTTRNPRPGEVHGEHYYFVSHDQFRSMIAEDAFLEHAEVFGNYYGTS 85
Cdd:TIGR03263   2 LIVISGPSGAGKSTLVKALLEEDP--NLKFSISATTRKPRPGEVDGVDYFFVSKEEFEEMIKAGEFLEWAEVHGNYYGTP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506223188   86 RAAIEQVLATGVDVFLDIDWQGARQIREKMPQARSIFILPPSKEELDRRLRGRGQDSEEVIAKRMAQAVAEMSHYAEYDY 165
Cdd:TIGR03263  80 KSPVEEALAAGKDVLLEIDVQGARQVKKKFPDAVSIFILPPSLEELERRLRKRGTDSEEVIERRLAKAKKEIAHADEFDY 159
                         170       180
                  ....*....|....*....|
gi 506223188  166 LIVNDDFDAALADLKIILRA 185
Cdd:TIGR03263 160 VIVNDDLEKAVEELKSIILA 179
Guanylate_kin pfam00625
Guanylate kinase;
3-186 1.05e-84

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 248.45  E-value: 1.05e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506223188    3 QGTLYIVSAPSGAGKSSLIQAFLKTQPLYDSqVSVSHTTRNPRPGEVHGEHYYFVSHDQFRSMIAEDAFLEHAEVFGNYY 82
Cdd:pfam00625   1 SRRPVVLSGPSGVGKSHIKKALLSEYPDKFG-YSVPHTTRPPRKGEVDGKDYYFVSKEEMERDISANEFLEYAQFSGNMY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506223188   83 GTSRAAIEQVLATGVDVFLDIDWQGARQIREKMPQARSIFILPPSKEELDRRLRGRGQDSEEVIAKRMAQAVAEMSHYaE 162
Cdd:pfam00625  80 GTSVETIEQIHEQGKIVILDVDPQGVKQLRKAELSPISVFIKPPSLKVLQRRLKGRGKEQEEKINKRMAAAEQEFQHY-E 158
                         170       180
                  ....*....|....*....|....
gi 506223188  163 YDYLIVNDDFDAALADLKIILRAE 186
Cdd:pfam00625 159 FDVIIVNDDLEEAYKKLKEALEAE 182
GMPK cd00071
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ...
6-180 5.34e-69

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: 207.00  E-value: 5.34e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506223188   6 LYIVSAPSGAGKSSLIQAFLKTQPLYdSQVSVSHTTRNPRPGEVHGEHYYFVSHDQFRSMIAEDAFLEHAEVFGNYYGTS 85
Cdd:cd00071    1 LIVLSGPSGVGKSTLLKRLLEEFDPN-FGFSVSHTTRKPRPGEVDGVDYHFVSKEEFERLIENGEFLEWAEFHGNYYGTS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506223188  86 RAAIEQVLATGVDVFLDIDWQGARQIREKMPQARSIFILPPskeeldrrlrgrgqdseeviakrmaqavaemshyaeyDY 165
Cdd:cd00071   80 KAAVEEALAEGKIVILEIDVQGARQVKKSYPDAVSIFILPP-------------------------------------DY 122
                        170
                 ....*....|....*
gi 506223188 166 LIVNDDFDAALADLK 180
Cdd:cd00071  123 VIVNDDLEKAYEELK 137
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
13-187 7.72e-69

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: 207.92  E-value: 7.72e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506223188    13 SGAGKSSLIQAFLKTQPLYdSQVSVSHTTRNPRPGEVHGEHYYFVSHDQFRSMIAEDAFLEHAEVFGNYYGTSRAAIEQV 92
Cdd:smart00072   1 SGVGKGTLLAELIQEIPDA-FERVVSHTTRPPRPGEVNGVDYHFVSKEEFEDDIKSGLFLEWGEYEGNYYGTSKETIRQV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506223188    93 LATGVDVFLDIDWQGARQIREKMPQARSIFILPPSKEELDRRLRGRGQDSEEVIAKRMAQAVAEMSHYAEYDYLIVNDDF 172
Cdd:smart00072  80 AEKGKHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEELERRLRQRGTETSERIQKRLAAAQKEAQEYHLFDYVIVNDDL 159
                          170
                   ....*....|....*
gi 506223188   173 DAALADLKIILRAER 187
Cdd:smart00072 160 EDAYEELKEILEAEQ 174
 
Name Accession Description Interval E-value
gmk PRK00300
guanylate kinase; Provisional
1-206 2.97e-135

guanylate kinase; Provisional


Pssm-ID: 234719  Cd Length: 205  Bit Score: 377.12  E-value: 2.97e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506223188   1 MAQGTLYIVSAPSGAGKSSLIQAFLKTQPlyDSQVSVSHTTRNPRPGEVHGEHYYFVSHDQFRSMIAEDAFLEHAEVFGN 80
Cdd:PRK00300   2 MRRGLLIVLSGPSGAGKSTLVKALLERDP--NLQLSVSATTRAPRPGEVDGVDYFFVSKEEFEEMIENGEFLEWAEVFGN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506223188  81 YYGTSRAAIEQVLATGVDVFLDIDWQGARQIREKMPQARSIFILPPSKEELDRRLRGRGQDSEEVIAKRMAQAVAEMSHY 160
Cdd:PRK00300  80 YYGTPRSPVEEALAAGKDVLLEIDWQGARQVKKKMPDAVSIFILPPSLEELERRLRGRGTDSEEVIARRLAKAREEIAHA 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 506223188 161 AEYDYLIVNDDFDAALADLKIILRAERLRMSRQKQRHDALITKLLA 206
Cdd:PRK00300 160 SEYDYVIVNDDLDTALEELKAIIRAERLRRSRQQQRHAELIEELLA 205
Gmk COG0194
Guanylate kinase [Nucleotide transport and metabolism];
3-194 8.55e-124

Guanylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 439964  Cd Length: 190  Bit Score: 347.44  E-value: 8.55e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506223188   3 QGTLYIVSAPSGAGKSSLIQAFLKTQPlyDSQVSVSHTTRNPRPGEVHGEHYYFVSHDQFRSMIAEDAFLEHAEVFGNYY 82
Cdd:COG0194    1 RGKLIVLSGPSGAGKTTLVKALLERDP--DLRFSVSATTRPPRPGEVDGVDYHFVSREEFERMIENGEFLEWAEVHGNYY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506223188  83 GTSRAAIEQVLATGVDVFLDIDWQGARQIREKMPQARSIFILPPSKEELDRRLRGRGQDSEEVIAKRMAQAVAEMSHYAE 162
Cdd:COG0194   79 GTPKAEVEEALAAGKDVLLEIDVQGARQVKKKFPDAVSIFILPPSLEELERRLRGRGTDSEEVIERRLAKAREELAHADE 158
                        170       180       190
                 ....*....|....*....|....*....|..
gi 506223188 163 YDYLIVNDDFDAALADLKIILRAERLRMSRQK 194
Cdd:COG0194  159 FDYVVVNDDLDRAVEELKAIIRAERLRRERQA 190
guanyl_kin TIGR03263
guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP ...
6-185 3.58e-115

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: 325.22  E-value: 3.58e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506223188    6 LYIVSAPSGAGKSSLIQAFLKTQPlyDSQVSVSHTTRNPRPGEVHGEHYYFVSHDQFRSMIAEDAFLEHAEVFGNYYGTS 85
Cdd:TIGR03263   2 LIVISGPSGAGKSTLVKALLEEDP--NLKFSISATTRKPRPGEVDGVDYFFVSKEEFEEMIKAGEFLEWAEVHGNYYGTP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506223188   86 RAAIEQVLATGVDVFLDIDWQGARQIREKMPQARSIFILPPSKEELDRRLRGRGQDSEEVIAKRMAQAVAEMSHYAEYDY 165
Cdd:TIGR03263  80 KSPVEEALAAGKDVLLEIDVQGARQVKKKFPDAVSIFILPPSLEELERRLRKRGTDSEEVIERRLAKAKKEIAHADEFDY 159
                         170       180
                  ....*....|....*....|
gi 506223188  166 LIVNDDFDAALADLKIILRA 185
Cdd:TIGR03263 160 VIVNDDLEKAVEELKSIILA 179
Guanylate_kin pfam00625
Guanylate kinase;
3-186 1.05e-84

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 248.45  E-value: 1.05e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506223188    3 QGTLYIVSAPSGAGKSSLIQAFLKTQPLYDSqVSVSHTTRNPRPGEVHGEHYYFVSHDQFRSMIAEDAFLEHAEVFGNYY 82
Cdd:pfam00625   1 SRRPVVLSGPSGVGKSHIKKALLSEYPDKFG-YSVPHTTRPPRKGEVDGKDYYFVSKEEMERDISANEFLEYAQFSGNMY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506223188   83 GTSRAAIEQVLATGVDVFLDIDWQGARQIREKMPQARSIFILPPSKEELDRRLRGRGQDSEEVIAKRMAQAVAEMSHYaE 162
Cdd:pfam00625  80 GTSVETIEQIHEQGKIVILDVDPQGVKQLRKAELSPISVFIKPPSLKVLQRRLKGRGKEQEEKINKRMAAAEQEFQHY-E 158
                         170       180
                  ....*....|....*....|....
gi 506223188  163 YDYLIVNDDFDAALADLKIILRAE 186
Cdd:pfam00625 159 FDVIIVNDDLEEAYKKLKEALEAE 182
GMPK cd00071
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ...
6-180 5.34e-69

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: 207.00  E-value: 5.34e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506223188   6 LYIVSAPSGAGKSSLIQAFLKTQPLYdSQVSVSHTTRNPRPGEVHGEHYYFVSHDQFRSMIAEDAFLEHAEVFGNYYGTS 85
Cdd:cd00071    1 LIVLSGPSGVGKSTLLKRLLEEFDPN-FGFSVSHTTRKPRPGEVDGVDYHFVSKEEFERLIENGEFLEWAEFHGNYYGTS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506223188  86 RAAIEQVLATGVDVFLDIDWQGARQIREKMPQARSIFILPPskeeldrrlrgrgqdseeviakrmaqavaemshyaeyDY 165
Cdd:cd00071   80 KAAVEEALAEGKIVILEIDVQGARQVKKSYPDAVSIFILPP-------------------------------------DY 122
                        170
                 ....*....|....*
gi 506223188 166 LIVNDDFDAALADLK 180
Cdd:cd00071  123 VIVNDDLEKAYEELK 137
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
13-187 7.72e-69

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: 207.92  E-value: 7.72e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506223188    13 SGAGKSSLIQAFLKTQPLYdSQVSVSHTTRNPRPGEVHGEHYYFVSHDQFRSMIAEDAFLEHAEVFGNYYGTSRAAIEQV 92
Cdd:smart00072   1 SGVGKGTLLAELIQEIPDA-FERVVSHTTRPPRPGEVNGVDYHFVSKEEFEDDIKSGLFLEWGEYEGNYYGTSKETIRQV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506223188    93 LATGVDVFLDIDWQGARQIREKMPQARSIFILPPSKEELDRRLRGRGQDSEEVIAKRMAQAVAEMSHYAEYDYLIVNDDF 172
Cdd:smart00072  80 AEKGKHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEELERRLRQRGTETSERIQKRLAAAQKEAQEYHLFDYVIVNDDL 159
                          170
                   ....*....|....*
gi 506223188   173 DAALADLKIILRAER 187
Cdd:smart00072 160 EDAYEELKEILEAEQ 174
gmk PRK14737
guanylate kinase; Provisional
1-183 2.95e-59

guanylate kinase; Provisional


Pssm-ID: 173199  Cd Length: 186  Bit Score: 184.04  E-value: 2.95e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506223188   1 MAQGTLYIVSAPSGAGKSSLIQAFLKTQPlyDSQVSVSHTTRNPRPGEVHGEHYYFVSHDQFRSMIAEDAFLEHAEVFGN 80
Cdd:PRK14737   1 KASPKLFIISSVAGGGKSTIIQALLEEHP--DFLFSISCTTRAPRPGDEEGKTYFFLTIEEFKKGIADGEFLEWAEVHDN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506223188  81 YYGTSRAAIEQVLATGVDVFLDIDWQGARQIREKMPQAR-SIFILPPSKEELDRRLRGRGQDSEEVIAKRMAQAVAEMSH 159
Cdd:PRK14737  79 YYGTPKAFIEDAFKEGRSAIMDIDVQGAKIIKEKFPERIvTIFIEPPSEEEWEERLIHRGTDSEESIEKRIENGIIELDE 158
                        170       180
                 ....*....|....*....|....
gi 506223188 160 YAEYDYLIVNDDFDAALADLKIIL 183
Cdd:PRK14737 159 ANEFDYKIINDDLEDAIADLEAII 182
gmk PRK14738
guanylate kinase; Provisional
2-193 8.33e-54

guanylate kinase; Provisional


Pssm-ID: 237809  Cd Length: 206  Bit Score: 170.68  E-value: 8.33e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506223188   2 AQGTLYIVSAPSGAGKSSLIQAFLKTQPLYDsqVSVSHTTRNPRPGEVHGEHYYFVSHDQFRSMIAEDAFLEHAEVFGNY 81
Cdd:PRK14738  11 AKPLLVVISGPSGVGKDAVLARMRERKLPFH--FVVTATTRPKRPGEIDGVDYHFVTPEEFREMISQNELLEWAEVYGNY 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506223188  82 YGTSRAAIEQVLATGVDVFLDIDWQGARQIREKMPQARSIFILPPSKEELDRRLRGRGQDSEEVIAKRMAQAVAEMSHYA 161
Cdd:PRK14738  89 YGVPKAPVRQALASGRDVIVKVDVQGAASIKRLVPEAVFIFLAPPSMDELTRRLELRRTESPEELERRLATAPLELEQLP 168
                        170       180       190
                 ....*....|....*....|....*....|....
gi 506223188 162 EYDYLIVN--DDFDAALADLKIILRAERLRMSRQ 193
Cdd:PRK14738 169 EFDYVVVNpeDRLDEAVAQIMAIISAEKSRVHPR 202
PLN02772 PLN02772
guanylate kinase
8-183 5.45e-49

guanylate kinase


Pssm-ID: 215414 [Multi-domain]  Cd Length: 398  Bit Score: 164.24  E-value: 5.45e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506223188   8 IVSAPSGAGKSSLIQAFLKTQPlydSQV--SVSHTTRNPRPGEVHGEHYYFVSHDQFRSMIAEDAFLEHAEVFGNYYGTS 85
Cdd:PLN02772 139 VISGPSGVGKGTLISMLMKEFP---SMFgfSVSHTTRAPREMEKDGVHYHFTERSVMEKEIKDGKFLEFASVHGNLYGTS 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506223188  86 RAAIEQVLATGVDVFLDIDWQGARQIREKMPQARSIFILPPSKEELDRRLRGRGQDSEEVIAKRMAQAVAEMSHYAE--- 162
Cdd:PLN02772 216 IEAVEVVTDSGKRCILDIDVQGARSVRASSLEAIFIFICPPSMEELEKRLRARGTETEEQIQKRLRNAEAELEQGKSsgi 295
                        170       180
                 ....*....|....*....|.
gi 506223188 163 YDYLIVNDDFDAALADLKIIL 183
Cdd:PLN02772 296 FDHILYNDNLEECYKNLKKLL 316
PhnN COG3709
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
1-189 1.60e-17

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


Pssm-ID: 442923  Cd Length: 188  Bit Score: 76.77  E-value: 1.60e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506223188   1 MAQGTLYIVSAPSGAGKSSLIQAfLKTQPLYDSQVSVSH---TtrnpRPGEVHGEHYYFVSHDQFRSMIAEDAFLEHAEV 77
Cdd:COG3709    2 SGPGRLIYVVGPSGAGKDSLLAA-ARARLAADPRLVFARryiT----RPADAGGEDHDALSEAEFARRAAAGAFALHWQA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506223188  78 FGNYYGTsRAAIEQVLATGVDVFLDidwqGAR----QIREKMPQARSIFI-LPPskEELDRRLRGRGQDSEEVIAKRMAQ 152
Cdd:COG3709   77 HGLRYGI-PAEIDAWLAAGRDVVVN----GSRavlpQARARYPRLLVVLItASP--EVLAQRLAARGRESAEEIEARLAR 149
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 506223188 153 AVAEMSHyAEYDYLIVND-DFDAALADLKIILRAERLR 189
Cdd:COG3709  150 AAEFLPD-GPDVLVIDNDgPLEDAGARLLALLRAARAR 186
phosphon_PhnN TIGR02322
phosphonate metabolism protein/1,5-bisphosphokinase (PRPP-forming) PhnN; Members of this ...
4-154 1.79e-12

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: 63.15  E-value: 1.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506223188    4 GTLYIVSAPSGAGKSSLIQaFLKTQPLYDSQVSVSHTTRNpRPGEVHGEHYYFVSHDQFRSMIAEDAFLEHAEVFGNYYG 83
Cdd:TIGR02322   1 GRLIYVVGPSGAGKDTLLD-YARARLAGDPRVHFVRRVIT-RPASAGGENHIALSTEEFDHREDGGAFALSWQAHGLSYG 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506223188   84 TSrAAIEQVLATGVDVFLDidwqGAR----QIREKMPQARSIFILPPSkEELDRRLRGRGQDSEEVIAKRMAQAV 154
Cdd:TIGR02322  79 IP-IEIDQWLEAGDVVVVN----GSRavlpEARQRYPNLLVVNITASP-DVLAQRLAARGRESREEIEERLARSA 147
PRK10078 PRK10078
ribose 1,5-bisphosphokinase; Provisional
12-199 1.55e-09

ribose 1,5-bisphosphokinase; Provisional


Pssm-ID: 236648  Cd Length: 186  Bit Score: 55.14  E-value: 1.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506223188  12 PSGAGKSSLIQAfLKTQPlyDSQVSVSHTTRNpRPGEVHGEHYYFVSHDQFRSMIAEDAFLEHAEVFGNYYGTSrAAIEQ 91
Cdd:PRK10078  10 PSGSGKDSLLAA-LRQRE--QTQLLVAHRYIT-RPASAGSENHIALSEQEFFTRAGQNLFALSWHANGLYYGVG-IEIDL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506223188  92 VLATGVDVFLDidwqGARQireKMPQARSIF---ILP----PSKEELDRRLRGRGQDSEEVIAKRMAQAvaemSHYAEYD 164
Cdd:PRK10078  85 WLHAGFDVLVN----GSRA---HLPQARARYqsaLLPvclqVSPEILRQRLENRGRENASEINARLARA----ARYQPQD 153
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 506223188 165 YLIVNDD--FDAALADLKIILRAErlrmsrQKQRHDA 199
Cdd:PRK10078 154 CHTLNNDgsLRQSVDTLLTLLHLS------QKEKHHA 184
PRK12289 PRK12289
small ribosomal subunit biogenesis GTPase RsgA;
8-42 3.71e-03

small ribosomal subunit biogenesis GTPase RsgA;


Pssm-ID: 237040 [Multi-domain]  Cd Length: 352  Bit Score: 37.30  E-value: 3.71e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 506223188   8 IVSAPSGAGKSSLIQAFLktqPLYDSQVS-VS-------HTTR 42
Cdd:PRK12289 176 VVAGPSGVGKSSLINRLI---PDVELRVGkVSgklgrgrHTTR 215
AAA_18 pfam13238
AAA domain;
8-155 7.52e-03

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 35.10  E-value: 7.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506223188    8 IVSAPSGAGKSSLIQAFLKTQPLYDSQVSVsHTTRNPRPGEvhgEHYYFVSH--DQFRSMIAEDAFLEHAEVFGNyygts 85
Cdd:pfam13238   2 LITGTPGVGKTTLAKELSKRLGFGDNVRDL-ALENGLVLGD---DPETRESKrlDEDKLDRLLDLLEENAALEEG----- 72
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506223188   86 raaieqvlatGVDVfldIDWQGARQIREKMPQARSIFI-LPPskEELDRRLRGRGQDSEEVIAKRMAQAVA 155
Cdd:pfam13238  73 ----------GNLI---IDGHLAELEPERAKDLVGIVLrASP--EELLERLEKRGYEEAKIKENEEAEILG 128
 
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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