NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|119371217|sp|Q1R4U3|]
View 

RecName: Full=Guanylate kinase; AltName: Full=GMP kinase

Protein Classification

guanylate kinase( domain architecture ID 10011364)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
gmk PRK00300
guanylate kinase; Provisional
 1-206 1.23e-137

guanylate kinase; Provisional


:

Pssm-ID: 234719  Cd Length: 205  Bit Score: 383.29  E-value: 1.23e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371217   1 MAQGTLYIVSAPSGAGKSSLIQALLKTQPlyDTQVSVSHTTRQPRPGEVHGEHYFFVNHDEFKEMISRDAFLEHAEVFGN 80
Cdd:PRK00300   2 MRRGLLIVLSGPSGAGKSTLVKALLERDP--NLQLSVSATTRAPRPGEVDGVDYFFVSKEEFEEMIENGEFLEWAEVFGN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371217  81 YYGTSREAIEQVLATGVDVFLDIDWQGAQQIRQKMPHARSIFILPPSKIELDRRLRGRGQDSEEVIAKRMAQAVAEMSHY 160
Cdd:PRK00300  80 YYGTPRSPVEEALAAGKDVLLEIDWQGARQVKKKMPDAVSIFILPPSLEELERRLRGRGTDSEEVIARRLAKAREEIAHA 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 119371217 161 AEYDYLIVNDDFDTALTDLKTIIRAERLRMSRQKQRHDALISKLLA 206
Cdd:PRK00300 160 SEYDYVIVNDDLDTALEELKAIIRAERLRRSRQQQRHAELIEELLA 205
 
Name Accession Description Interval E-value
gmk PRK00300
guanylate kinase; Provisional
 1-206 1.23e-137

guanylate kinase; Provisional


Pssm-ID: 234719  Cd Length: 205  Bit Score: 383.29  E-value: 1.23e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371217   1 MAQGTLYIVSAPSGAGKSSLIQALLKTQPlyDTQVSVSHTTRQPRPGEVHGEHYFFVNHDEFKEMISRDAFLEHAEVFGN 80
Cdd:PRK00300   2 MRRGLLIVLSGPSGAGKSTLVKALLERDP--NLQLSVSATTRAPRPGEVDGVDYFFVSKEEFEEMIENGEFLEWAEVFGN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371217  81 YYGTSREAIEQVLATGVDVFLDIDWQGAQQIRQKMPHARSIFILPPSKIELDRRLRGRGQDSEEVIAKRMAQAVAEMSHY 160
Cdd:PRK00300  80 YYGTPRSPVEEALAAGKDVLLEIDWQGARQVKKKMPDAVSIFILPPSLEELERRLRGRGTDSEEVIARRLAKAREEIAHA 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 119371217 161 AEYDYLIVNDDFDTALTDLKTIIRAERLRMSRQKQRHDALISKLLA 206
Cdd:PRK00300 160 SEYDYVIVNDDLDTALEELKAIIRAERLRRSRQQQRHAELIEELLA 205
Gmk COG0194
Guanylate kinase [Nucleotide transport and metabolism];
3-194 8.64e-125

Guanylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 439964  Cd Length: 190  Bit Score: 350.14  E-value: 8.64e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371217   3 QGTLYIVSAPSGAGKSSLIQALLKTQPlyDTQVSVSHTTRQPRPGEVHGEHYFFVNHDEFKEMISRDAFLEHAEVFGNYY 82
Cdd:COG0194    1 RGKLIVLSGPSGAGKTTLVKALLERDP--DLRFSVSATTRPPRPGEVDGVDYHFVSREEFERMIENGEFLEWAEVHGNYY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371217  83 GTSREAIEQVLATGVDVFLDIDWQGAQQIRQKMPHARSIFILPPSKIELDRRLRGRGQDSEEVIAKRMAQAVAEMSHYAE 162
Cdd:COG0194   79 GTPKAEVEEALAAGKDVLLEIDVQGARQVKKKFPDAVSIFILPPSLEELERRLRGRGTDSEEVIERRLAKAREELAHADE 158

                        170       180       190
                 ....*....|....*....|....*....|..
gi 119371217 163 YDYLIVNDDFDTALTDLKTIIRAERLRMSRQK 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 1.82e-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: 325.99  E-value: 1.82e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371217    6 LYIVSAPSGAGKSSLIQALLKTQPlyDTQVSVSHTTRQPRPGEVHGEHYFFVNHDEFKEMISRDAFLEHAEVFGNYYGTS 85
Cdd:TIGR03263   2 LIVISGPSGAGKSTLVKALLEEDP--NLKFSISATTRKPRPGEVDGVDYFFVSKEEFEEMIKAGEFLEWAEVHGNYYGTP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371217   86 REAIEQVLATGVDVFLDIDWQGAQQIRQKMPHARSIFILPPSKIELDRRLRGRGQDSEEVIAKRMAQAVAEMSHYAEYDY 165
Cdd:TIGR03263  80 KSPVEEALAAGKDVLLEIDVQGARQVKKKFPDAVSIFILPPSLEELERRLRKRGTDSEEVIERRLAKAKKEIAHADEFDY 159

                         170       180
                  ....*....|....*....|
gi 119371217  166 LIVNDDFDTALTDLKTIIRA 185
Cdd:TIGR03263 160 VIVNDDLEKAVEELKSIILA 179
Guanylate_kin pfam00625
Guanylate kinase;
3-186 1.46e-89

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 260.78  E-value: 1.46e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371217    3 QGTLYIVSAPSGAGKSSLIQALLKTQPLYDTqVSVSHTTRQPRPGEVHGEHYFFVNHDEFKEMISRDAFLEHAEVFGNYY 82
Cdd:pfam00625   1 SRRPVVLSGPSGVGKSHIKKALLSEYPDKFG-YSVPHTTRPPRKGEVDGKDYYFVSKEEMERDISANEFLEYAQFSGNMY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371217   83 GTSREAIEQVLATGVDVFLDIDWQGAQQIRQKMPHARSIFILPPSKIELDRRLRGRGQDSEEVIAKRMAQAVAEMSHYaE 162
Cdd:pfam00625  80 GTSVETIEQIHEQGKIVILDVDPQGVKQLRKAELSPISVFIKPPSLKVLQRRLKGRGKEQEEKINKRMAAAEQEFQHY-E 158

                         170       180
                  ....*....|....*....|....
gi 119371217  163 YDYLIVNDDFDTALTDLKTIIRAE 186
Cdd:pfam00625 159 FDVIIVNDDLEEAYKKLKEALEAE 182
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
 13-187 3.04e-73

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: 219.09  E-value: 3.04e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371217    13 SGAGKSSLIQALLKTQPLYdTQVSVSHTTRQPRPGEVHGEHYFFVNHDEFKEMISRDAFLEHAEVFGNYYGTSREAIEQV 92
Cdd:smart00072   1 SGVGKGTLLAELIQEIPDA-FERVVSHTTRPPRPGEVNGVDYHFVSKEEFEDDIKSGLFLEWGEYEGNYYGTSKETIRQV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371217    93 LATGVDVFLDIDWQGAQQIRQKMPHARSIFILPPSKIELDRRLRGRGQDSEEVIAKRMAQAVAEMSHYAEYDYLIVNDDF 172
Cdd:smart00072  80 AEKGKHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEELERRLRQRGTETSERIQKRLAAAQKEAQEYHLFDYVIVNDDL 159

                          170
                   ....*....|....*
gi 119371217   173 DTALTDLKTIIRAER 187
Cdd:smart00072 160 EDAYEELKEILEAEQ 174
GMPK cd00071
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ...
 6-180 5.09e-70

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: 209.70  E-value: 5.09e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371217   6 LYIVSAPSGAGKSSLIQALLKTQPLYdTQVSVSHTTRQPRPGEVHGEHYFFVNHDEFKEMISRDAFLEHAEVFGNYYGTS 85
Cdd:cd00071    1 LIVLSGPSGVGKSTLLKRLLEEFDPN-FGFSVSHTTRKPRPGEVDGVDYHFVSKEEFERLIENGEFLEWAEFHGNYYGTS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371217  86 REAIEQVLATGVDVFLDIDWQGAQQIRQKMPHARSIFILPPskieldrrlrgrgqdseeviakrmaqavaemshyaeyDY 165
Cdd:cd00071   80 KAAVEEALAEGKIVILEIDVQGARQVKKSYPDAVSIFILPP-------------------------------------DY 122

                        170
                 ....*....|....*
gi 119371217 166 LIVNDDFDTALTDLK 180
Cdd:cd00071  123 VIVNDDLEKAYEELK 137
 
Name Accession Description Interval E-value
gmk PRK00300
guanylate kinase; Provisional
 1-206 1.23e-137

guanylate kinase; Provisional


Pssm-ID: 234719  Cd Length: 205  Bit Score: 383.29  E-value: 1.23e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371217   1 MAQGTLYIVSAPSGAGKSSLIQALLKTQPlyDTQVSVSHTTRQPRPGEVHGEHYFFVNHDEFKEMISRDAFLEHAEVFGN 80
Cdd:PRK00300   2 MRRGLLIVLSGPSGAGKSTLVKALLERDP--NLQLSVSATTRAPRPGEVDGVDYFFVSKEEFEEMIENGEFLEWAEVFGN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371217  81 YYGTSREAIEQVLATGVDVFLDIDWQGAQQIRQKMPHARSIFILPPSKIELDRRLRGRGQDSEEVIAKRMAQAVAEMSHY 160
Cdd:PRK00300  80 YYGTPRSPVEEALAAGKDVLLEIDWQGARQVKKKMPDAVSIFILPPSLEELERRLRGRGTDSEEVIARRLAKAREEIAHA 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 119371217 161 AEYDYLIVNDDFDTALTDLKTIIRAERLRMSRQKQRHDALISKLLA 206
Cdd:PRK00300 160 SEYDYVIVNDDLDTALEELKAIIRAERLRRSRQQQRHAELIEELLA 205
Gmk COG0194
Guanylate kinase [Nucleotide transport and metabolism];
3-194 8.64e-125

Guanylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 439964  Cd Length: 190  Bit Score: 350.14  E-value: 8.64e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371217   3 QGTLYIVSAPSGAGKSSLIQALLKTQPlyDTQVSVSHTTRQPRPGEVHGEHYFFVNHDEFKEMISRDAFLEHAEVFGNYY 82
Cdd:COG0194    1 RGKLIVLSGPSGAGKTTLVKALLERDP--DLRFSVSATTRPPRPGEVDGVDYHFVSREEFERMIENGEFLEWAEVHGNYY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371217  83 GTSREAIEQVLATGVDVFLDIDWQGAQQIRQKMPHARSIFILPPSKIELDRRLRGRGQDSEEVIAKRMAQAVAEMSHYAE 162
Cdd:COG0194   79 GTPKAEVEEALAAGKDVLLEIDVQGARQVKKKFPDAVSIFILPPSLEELERRLRGRGTDSEEVIERRLAKAREELAHADE 158

                        170       180       190
                 ....*....|....*....|....*....|..
gi 119371217 163 YDYLIVNDDFDTALTDLKTIIRAERLRMSRQK 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 1.82e-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: 325.99  E-value: 1.82e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371217    6 LYIVSAPSGAGKSSLIQALLKTQPlyDTQVSVSHTTRQPRPGEVHGEHYFFVNHDEFKEMISRDAFLEHAEVFGNYYGTS 85
Cdd:TIGR03263   2 LIVISGPSGAGKSTLVKALLEEDP--NLKFSISATTRKPRPGEVDGVDYFFVSKEEFEEMIKAGEFLEWAEVHGNYYGTP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371217   86 REAIEQVLATGVDVFLDIDWQGAQQIRQKMPHARSIFILPPSKIELDRRLRGRGQDSEEVIAKRMAQAVAEMSHYAEYDY 165
Cdd:TIGR03263  80 KSPVEEALAAGKDVLLEIDVQGARQVKKKFPDAVSIFILPPSLEELERRLRKRGTDSEEVIERRLAKAKKEIAHADEFDY 159

                         170       180
                  ....*....|....*....|
gi 119371217  166 LIVNDDFDTALTDLKTIIRA 185
Cdd:TIGR03263 160 VIVNDDLEKAVEELKSIILA 179
Guanylate_kin pfam00625
Guanylate kinase;
3-186 1.46e-89

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 260.78  E-value: 1.46e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371217    3 QGTLYIVSAPSGAGKSSLIQALLKTQPLYDTqVSVSHTTRQPRPGEVHGEHYFFVNHDEFKEMISRDAFLEHAEVFGNYY 82
Cdd:pfam00625   1 SRRPVVLSGPSGVGKSHIKKALLSEYPDKFG-YSVPHTTRPPRKGEVDGKDYYFVSKEEMERDISANEFLEYAQFSGNMY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371217   83 GTSREAIEQVLATGVDVFLDIDWQGAQQIRQKMPHARSIFILPPSKIELDRRLRGRGQDSEEVIAKRMAQAVAEMSHYaE 162
Cdd:pfam00625  80 GTSVETIEQIHEQGKIVILDVDPQGVKQLRKAELSPISVFIKPPSLKVLQRRLKGRGKEQEEKINKRMAAAEQEFQHY-E 158

                         170       180
                  ....*....|....*....|....
gi 119371217  163 YDYLIVNDDFDTALTDLKTIIRAE 186
Cdd:pfam00625 159 FDVIIVNDDLEEAYKKLKEALEAE 182
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
 13-187 3.04e-73

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: 219.09  E-value: 3.04e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371217    13 SGAGKSSLIQALLKTQPLYdTQVSVSHTTRQPRPGEVHGEHYFFVNHDEFKEMISRDAFLEHAEVFGNYYGTSREAIEQV 92
Cdd:smart00072   1 SGVGKGTLLAELIQEIPDA-FERVVSHTTRPPRPGEVNGVDYHFVSKEEFEDDIKSGLFLEWGEYEGNYYGTSKETIRQV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371217    93 LATGVDVFLDIDWQGAQQIRQKMPHARSIFILPPSKIELDRRLRGRGQDSEEVIAKRMAQAVAEMSHYAEYDYLIVNDDF 172
Cdd:smart00072  80 AEKGKHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEELERRLRQRGTETSERIQKRLAAAQKEAQEYHLFDYVIVNDDL 159

                          170
                   ....*....|....*
gi 119371217   173 DTALTDLKTIIRAER 187
Cdd:smart00072 160 EDAYEELKEILEAEQ 174
GMPK cd00071
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ...
 6-180 5.09e-70

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: 209.70  E-value: 5.09e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371217   6 LYIVSAPSGAGKSSLIQALLKTQPLYdTQVSVSHTTRQPRPGEVHGEHYFFVNHDEFKEMISRDAFLEHAEVFGNYYGTS 85
Cdd:cd00071    1 LIVLSGPSGVGKSTLLKRLLEEFDPN-FGFSVSHTTRKPRPGEVDGVDYHFVSKEEFERLIENGEFLEWAEFHGNYYGTS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371217  86 REAIEQVLATGVDVFLDIDWQGAQQIRQKMPHARSIFILPPskieldrrlrgrgqdseeviakrmaqavaemshyaeyDY 165
Cdd:cd00071   80 KAAVEEALAEGKIVILEIDVQGARQVKKSYPDAVSIFILPP-------------------------------------DY 122

                        170
                 ....*....|....*
gi 119371217 166 LIVNDDFDTALTDLK 180
Cdd:cd00071  123 VIVNDDLEKAYEELK 137
gmk PRK14737
guanylate kinase; Provisional
 1-183 3.32e-58

guanylate kinase; Provisional


Pssm-ID: 173199  Cd Length: 186  Bit Score: 181.34  E-value: 3.32e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371217   1 MAQGTLYIVSAPSGAGKSSLIQALLKTQPlyDTQVSVSHTTRQPRPGEVHGEHYFFVNHDEFKEMISRDAFLEHAEVFGN 80
Cdd:PRK14737   1 KASPKLFIISSVAGGGKSTIIQALLEEHP--DFLFSISCTTRAPRPGDEEGKTYFFLTIEEFKKGIADGEFLEWAEVHDN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371217  81 YYGTSREAIEQVLATGVDVFLDIDWQGAQQIRQKMPHAR-SIFILPPSKIELDRRLRGRGQDSEEVIAKRMAQAVAEMSH 159
Cdd:PRK14737  79 YYGTPKAFIEDAFKEGRSAIMDIDVQGAKIIKEKFPERIvTIFIEPPSEEEWEERLIHRGTDSEESIEKRIENGIIELDE 158

                        170       180
                 ....*....|....*....|....
gi 119371217 160 YAEYDYLIVNDDFDTALTDLKTII 183
Cdd:PRK14737 159 ANEFDYKIINDDLEDAIADLEAII 182
gmk PRK14738
guanylate kinase; Provisional
 2-193 1.68e-54

guanylate kinase; Provisional


Pssm-ID: 237809  Cd Length: 206  Bit Score: 172.61  E-value: 1.68e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371217   2 AQGTLYIVSAPSGAGKSSLIQALLKTQPLYDtqVSVSHTTRQPRPGEVHGEHYFFVNHDEFKEMISRDAFLEHAEVFGNY 81
Cdd:PRK14738  11 AKPLLVVISGPSGVGKDAVLARMRERKLPFH--FVVTATTRPKRPGEIDGVDYHFVTPEEFREMISQNELLEWAEVYGNY 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371217  82 YGTSREAIEQVLATGVDVFLDIDWQGAQQIRQKMPHARSIFILPPSKIELDRRLRGRGQDSEEVIAKRMAQAVAEMSHYA 161
Cdd:PRK14738  89 YGVPKAPVRQALASGRDVIVKVDVQGAASIKRLVPEAVFIFLAPPSMDELTRRLELRRTESPEELERRLATAPLELEQLP 168

                        170       180       190
                 ....*....|....*....|....*....|....
gi 119371217 162 EYDYLIVN--DDFDTALTDLKTIIRAERLRMSRQ 193
Cdd:PRK14738 169 EFDYVVVNpeDRLDEAVAQIMAIISAEKSRVHPR 202
PLN02772 PLN02772
guanylate kinase
 8-183 2.46e-47

guanylate kinase


Pssm-ID: 215414 [Multi-domain]  Cd Length: 398  Bit Score: 160.00  E-value: 2.46e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371217   8 IVSAPSGAGKSSLIQALLKTQPLYdTQVSVSHTTRQPRPGEVHGEHYFFVNHDEFKEMISRDAFLEHAEVFGNYYGTSRE 87
Cdd:PLN02772 139 VISGPSGVGKGTLISMLMKEFPSM-FGFSVSHTTRAPREMEKDGVHYHFTERSVMEKEIKDGKFLEFASVHGNLYGTSIE 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371217  88 AIEQVLATGVDVFLDIDWQGAQQIRQKMPHARSIFILPPSKIELDRRLRGRGQDSEEVIAKRMAQAVAEMSHYAE---YD 164
Cdd:PLN02772 218 AVEVVTDSGKRCILDIDVQGARSVRASSLEAIFIFICPPSMEELEKRLRARGTETEEQIQKRLRNAEAELEQGKSsgiFD 297

                        170
                 ....*....|....*....
gi 119371217 165 YLIVNDDFDTALTDLKTII 183
Cdd:PLN02772 298 HILYNDNLEECYKNLKKLL 316
PhnN COG3709
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
1-189 1.57e-17

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


Pssm-ID: 442923  Cd Length: 188  Bit Score: 76.77  E-value: 1.57e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371217   1 MAQGTLYIVSAPSGAGKSSLIQAlLKTQPLYDTQVSVSH---TtrqpRPGEVHGEHYFFVNHDEFKEMISRDAFLEHAEV 77
Cdd:COG3709    2 SGPGRLIYVVGPSGAGKDSLLAA-ARARLAADPRLVFARryiT----RPADAGGEDHDALSEAEFARRAAAGAFALHWQA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371217  78 FGNYYGTSREaIEQVLATGVDVFLDIDWQGAQQIRQKMPHARSIFILPPSKIeLDRRLRGRGQDSEEVIAKRMAQAVAEM 157
Cdd:COG3709   77 HGLRYGIPAE-IDAWLAAGRDVVVNGSRAVLPQARARYPRLLVVLITASPEV-LAQRLAARGRESAEEIEARLARAAEFL 154

                        170       180       190
                 ....*....|....*....|....*....|...
gi 119371217 158 SHyAEYDYLIVND-DFDTALTDLKTIIRAERLR 189
Cdd:COG3709  155 PD-GPDVLVIDNDgPLEDAGARLLALLRAARAR 186
phosphon_PhnN TIGR02322
phosphonate metabolism protein/1,5-bisphosphokinase (PRPP-forming) PhnN; Members of this ...
 4-154 1.62e-13

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: 65.85  E-value: 1.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371217    4 GTLYIVSAPSGAGKSSLI---QALLKTQPLYdtqvsvsHTTRQ--PRPGEVHGEHYFFVNHDEFKEMISRDAFLEHAEVF 78
Cdd:TIGR02322   1 GRLIYVVGPSGAGKDTLLdyaRARLAGDPRV-------HFVRRviTRPASAGGENHIALSTEEFDHREDGGAFALSWQAH 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119371217   79 GNYYGTSREaIEQVLATGVDVFLDIDWQGAQQIRQKMPHARSIFILPPSKIeLDRRLRGRGQDSEEVIAKRMAQAV 154
Cdd:TIGR02322  74 GLSYGIPIE-IDQWLEAGDVVVVNGSRAVLPEARQRYPNLLVVNITASPDV-LAQRLAARGRESREEIEERLARSA 147
PRK10078 PRK10078
ribose 1,5-bisphosphokinase; Provisional
 12-199 5.06e-11

ribose 1,5-bisphosphokinase; Provisional


Pssm-ID: 236648  Cd Length: 186  Bit Score: 58.99  E-value: 5.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371217  12 PSGAGKSSLIQALLKTQPlydTQVSVSH--TTRqprPGEVHGEHYFFVNHDEFKEMISRDAFLEHAEVFGNYYGTSREaI 89
Cdd:PRK10078  10 PSGSGKDSLLAALRQREQ---TQLLVAHryITR---PASAGSENHIALSEQEFFTRAGQNLFALSWHANGLYYGVGIE-I 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371217  90 EQVLATGVDVFLDIDWQGAQQIRQKMPHARSIFILPPSKIELDRRLRGRGQDSEEVIAKRMAQAvaemSHYAEYDYLIVN 169
Cdd:PRK10078  83 DLWLHAGFDVLVNGSRAHLPQARARYQSALLPVCLQVSPEILRQRLENRGRENASEINARLARA----ARYQPQDCHTLN 158

                        170       180       190
                 ....*....|....*....|....*....|
gi 119371217 170 DDFDTaltdLKTIIRAERLRMSRQKQRHDA 199
Cdd:PRK10078 159 NDGSL----RQSVDTLLTLLHLSQKEKHHA 184
PRK12289 PRK12289
small ribosomal subunit biogenesis GTPase RsgA;
8-42 2.12e-03

small ribosomal subunit biogenesis GTPase RsgA;


Pssm-ID: 237040 [Multi-domain]  Cd Length: 352  Bit Score: 38.07  E-value: 2.12e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 119371217   8 IVSAPSGAGKSSLIQALLktqPLYDTQVS-VS-------HTTR 42
Cdd:PRK12289 176 VVAGPSGVGKSSLINRLI---PDVELRVGkVSgklgrgrHTTR 215
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 12-42 4.06e-03

Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.


Pssm-ID: 206747 [Multi-domain]  Cd Length: 211  Bit Score: 36.99  E-value: 4.06e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 119371217  12 PSGAGKSSLIQAL-----LKTQplydtQVSVS-----HTTR 42
Cdd:cd01854   93 QSGVGKSTLLNALlpelvLATG-----EISEKlgrgrHTTT 128
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 13-77 5.66e-03

50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.


Pssm-ID: 460387 [Multi-domain]  Cd Length: 113  Bit Score: 35.29  E-value: 5.66e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119371217   13 SGAGKSSLIQALLKTQPlydtQVS-VSHTTRQPRPGEVH--GEHYFFV------NHDEFKEMISRdAFLEHAEV 77
Cdd:pfam01926   8 PNVGKSTLINALTGAKA----IVSdYPGTTRDPNEGRLElkGKQIILVdtpgliEGASEGEGLGR-AFLAIIEA 76
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
 2-94 8.44e-03

ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443308 [Multi-domain]  Cd Length: 206  Bit Score: 35.92  E-value: 8.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371217   2 AQGTLYIVSAPSGAGKSSLIQALLKTQPLYDTQVSVSHTTRQPRPGEVHGEHYFFVNHDEFKEMISrdaFLEHAEVFGNY 81
Cdd:COG4133   26 AAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLGHADGLKPELT---VRENLRFWAAL 102

                         90
                 ....*....|....*
gi 119371217  82 YG--TSREAIEQVLA 94
Cdd:COG4133  103 YGlrADREAIDEALE 117
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH