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Conserved domains on  [gi|524105083|emb|CCY80754|]
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guanylate kinase [Prevotella sp. CAG:1185]

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
 1-186 2.82e-95

guanylate kinase; Provisional


:

Pssm-ID: 234719  Cd Length: 205  Bit Score: 275.04  E-value: 2.82e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524105083   1 MPGKLIIFSAPSGSGKSTIINWLMSHEElRMAFSISCTSRPPRGTERNGVEYFFVTPEEFRRRIDNDEFLEYEEVYkDRY 80
Cdd:PRK00300   3 RRGLLIVLSGPSGAGKSTLVKALLERDP-NLQLSVSATTRAPRPGEVDGVDYFFVSKEEFEEMIENGEFLEWAEVF-GNY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524105083  81 YGTLKQQVEAQLEKGENVVFDVDVKGGCNIKNYYGDrALSVFIQPPSIEELRNRLTGRGTDAPEVIEDRIARASFELTFA 160
Cdd:PRK00300  81 YGTPRSPVEEALAAGKDVLLEIDWQGARQVKKKMPD-AVSIFILPPSLEELERRLRGRGTDSEEVIARRLAKAREEIAHA 159

                        170       180
                 ....*....|....*....|....*.
gi 524105083 161 PKFDKVVVNDDLDKAKAEALKIVKDF 186
Cdd:PRK00300 160 SEYDYVIVNDDLDTALEELKAIIRAE 185
 
Name Accession Description Interval E-value
gmk PRK00300
guanylate kinase; Provisional
 1-186 2.82e-95

guanylate kinase; Provisional


Pssm-ID: 234719  Cd Length: 205  Bit Score: 275.04  E-value: 2.82e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524105083   1 MPGKLIIFSAPSGSGKSTIINWLMSHEElRMAFSISCTSRPPRGTERNGVEYFFVTPEEFRRRIDNDEFLEYEEVYkDRY 80
Cdd:PRK00300   3 RRGLLIVLSGPSGAGKSTLVKALLERDP-NLQLSVSATTRAPRPGEVDGVDYFFVSKEEFEEMIENGEFLEWAEVF-GNY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524105083  81 YGTLKQQVEAQLEKGENVVFDVDVKGGCNIKNYYGDrALSVFIQPPSIEELRNRLTGRGTDAPEVIEDRIARASFELTFA 160
Cdd:PRK00300  81 YGTPRSPVEEALAAGKDVLLEIDWQGARQVKKKMPD-AVSIFILPPSLEELERRLRGRGTDSEEVIARRLAKAREEIAHA 159

                        170       180
                 ....*....|....*....|....*.
gi 524105083 161 PKFDKVVVNDDLDKAKAEALKIVKDF 186
Cdd:PRK00300 160 SEYDYVIVNDDLDTALEELKAIIRAE 185
Gmk COG0194
Guanylate kinase [Nucleotide transport and metabolism];
2-184 4.80e-95

Guanylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 439964  Cd Length: 190  Bit Score: 273.87  E-value: 4.80e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524105083   2 PGKLIIFSAPSGSGKSTIINWLMSHEeLRMAFSISCTSRPPRGTERNGVEYFFVTPEEFRRRIDNDEFLEYEEVYkDRYY 81
Cdd:COG0194    1 RGKLIVLSGPSGAGKTTLVKALLERD-PDLRFSVSATTRPPRPGEVDGVDYHFVSREEFERMIENGEFLEWAEVH-GNYY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524105083  82 GTLKQQVEAQLEKGENVVFDVDVKGGCNIKNYYGDrALSVFIQPPSIEELRNRLTGRGTDAPEVIEDRIARASFELTFAP 161
Cdd:COG0194   79 GTPKAEVEEALAAGKDVLLEIDVQGARQVKKKFPD-AVSIFILPPSLEELERRLRGRGTDSEEVIERRLAKAREELAHAD 157

                        170       180
                 ....*....|....*....|...
gi 524105083 162 KFDKVVVNDDLDKAKAEALKIVK 184
Cdd:COG0194  158 EFDYVVVNDDLDRAVEELKAIIR 180
guanyl_kin TIGR03263
guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP ...
 4-185 4.60e-88

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: 255.88  E-value: 4.60e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524105083    4 KLIIFSAPSGSGKSTIINWLMShEELRMAFSISCTSRPPRGTERNGVEYFFVTPEEFRRRIDNDEFLEYEEVYkDRYYGT 83
Cdd:TIGR03263   1 LLIVISGPSGAGKSTLVKALLE-EDPNLKFSISATTRKPRPGEVDGVDYFFVSKEEFEEMIKAGEFLEWAEVH-GNYYGT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524105083   84 LKQQVEAQLEKGENVVFDVDVKGGCNIKNYYgDRALSVFIQPPSIEELRNRLTGRGTDAPEVIEDRIARASFELTFAPKF 163
Cdd:TIGR03263  79 PKSPVEEALAAGKDVLLEIDVQGARQVKKKF-PDAVSIFILPPSLEELERRLRKRGTDSEEVIERRLAKAKKEIAHADEF 157

                         170       180
                  ....*....|....*....|..
gi 524105083  164 DKVVVNDDLDKAKAEALKIVKD 185
Cdd:TIGR03263 158 DYVIVNDDLEKAVEELKSIILA 179
GMPK cd00071
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ...
 5-178 1.82e-49

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: 156.54  E-value: 1.82e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524105083   5 LIIFSAPSGSGKSTIINWLMSHEELRMAFSISCTSRPPRGTERNGVEYFFVTPEEFRRRIDNDEFLEYEEVYKDrYYGTL 84
Cdd:cd00071    1 LIVLSGPSGVGKSTLLKRLLEEFDPNFGFSVSHTTRKPRPGEVDGVDYHFVSKEEFERLIENGEFLEWAEFHGN-YYGTS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524105083  85 KQQVEAQLEKGENVVFDVDVKGGCNIKNYYGDrALSVFIQPPsieelrnrltgrgtdapeviedriarasfeltfapkfD 164
Cdd:cd00071   80 KAAVEEALAEGKIVILEIDVQGARQVKKSYPD-AVSIFILPP-------------------------------------D 121

                        170
                 ....*....|....
gi 524105083 165 KVVVNDDLDKAKAE 178
Cdd:cd00071  122 YVIVNDDLEKAYEE 135
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
 12-183 2.11e-48

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: 155.14  E-value: 2.11e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524105083    12 SGSGKSTIINWLMSHEELRMAFSISCTSRPPRGTERNGVEYFFVTPEEFRRRIDNDEFLEYEEvYKDRYYGTLKQQVEAQ 91
Cdd:smart00072   1 SGVGKGTLLAELIQEIPDAFERVVSHTTRPPRPGEVNGVDYHFVSKEEFEDDIKSGLFLEWGE-YEGNYYGTSKETIRQV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524105083    92 LEKGENVVFDVDVKGGCNIKNYYGDrALSVFIQPPSIEELRNRLTGRGTDAPEVIEDRIARASFELTFAPKFDKVVVNDD 171
Cdd:smart00072  80 AEKGKHCLLDIDPQGVKQLRKAQLY-PIVIFIAPPSSEELERRLRQRGTETSERIQKRLAAAQKEAQEYHLFDYVIVNDD 158

                          170
                   ....*....|..
gi 524105083   172 LDKAKAEALKIV 183
Cdd:smart00072 159 LEDAYEELKEIL 170
Guanylate_kin pfam00625
Guanylate kinase;
3-188 5.62e-47

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 151.76  E-value: 5.62e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524105083    3 GKLIIFSAPSGSGKSTIINWLMSHEELRMAFSISCTSRPPRGTERNGVEYFFVTPEEFRRRIDNDEFLEYEEvYKDRYYG 82
Cdd:pfam00625   2 RRPVVLSGPSGVGKSHIKKALLSEYPDKFGYSVPHTTRPPRKGEVDGKDYYFVSKEEMERDISANEFLEYAQ-FSGNMYG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524105083   83 TLKQQVEAQLEKGENVVFDVDVKGGCNIKNYYgDRALSVFIQPPSIEELRNRLTGRGTDAPEVIEDRIARASFELTfAPK 162
Cdd:pfam00625  81 TSVETIEQIHEQGKIVILDVDPQGVKQLRKAE-LSPISVFIKPPSLKVLQRRLKGRGKEQEEKINKRMAAAEQEFQ-HYE 158

                         170       180
                  ....*....|....*....|....*.
gi 524105083  163 FDKVVVNDDLDkakaEALKIVKDFLF 188
Cdd:pfam00625 159 FDVIIVNDDLE----EAYKKLKEALE 180
 
Name Accession Description Interval E-value
gmk PRK00300
guanylate kinase; Provisional
 1-186 2.82e-95

guanylate kinase; Provisional


Pssm-ID: 234719  Cd Length: 205  Bit Score: 275.04  E-value: 2.82e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524105083   1 MPGKLIIFSAPSGSGKSTIINWLMSHEElRMAFSISCTSRPPRGTERNGVEYFFVTPEEFRRRIDNDEFLEYEEVYkDRY 80
Cdd:PRK00300   3 RRGLLIVLSGPSGAGKSTLVKALLERDP-NLQLSVSATTRAPRPGEVDGVDYFFVSKEEFEEMIENGEFLEWAEVF-GNY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524105083  81 YGTLKQQVEAQLEKGENVVFDVDVKGGCNIKNYYGDrALSVFIQPPSIEELRNRLTGRGTDAPEVIEDRIARASFELTFA 160
Cdd:PRK00300  81 YGTPRSPVEEALAAGKDVLLEIDWQGARQVKKKMPD-AVSIFILPPSLEELERRLRGRGTDSEEVIARRLAKAREEIAHA 159

                        170       180
                 ....*....|....*....|....*.
gi 524105083 161 PKFDKVVVNDDLDKAKAEALKIVKDF 186
Cdd:PRK00300 160 SEYDYVIVNDDLDTALEELKAIIRAE 185
Gmk COG0194
Guanylate kinase [Nucleotide transport and metabolism];
2-184 4.80e-95

Guanylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 439964  Cd Length: 190  Bit Score: 273.87  E-value: 4.80e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524105083   2 PGKLIIFSAPSGSGKSTIINWLMSHEeLRMAFSISCTSRPPRGTERNGVEYFFVTPEEFRRRIDNDEFLEYEEVYkDRYY 81
Cdd:COG0194    1 RGKLIVLSGPSGAGKTTLVKALLERD-PDLRFSVSATTRPPRPGEVDGVDYHFVSREEFERMIENGEFLEWAEVH-GNYY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524105083  82 GTLKQQVEAQLEKGENVVFDVDVKGGCNIKNYYGDrALSVFIQPPSIEELRNRLTGRGTDAPEVIEDRIARASFELTFAP 161
Cdd:COG0194   79 GTPKAEVEEALAAGKDVLLEIDVQGARQVKKKFPD-AVSIFILPPSLEELERRLRGRGTDSEEVIERRLAKAREELAHAD 157

                        170       180
                 ....*....|....*....|...
gi 524105083 162 KFDKVVVNDDLDKAKAEALKIVK 184
Cdd:COG0194  158 EFDYVVVNDDLDRAVEELKAIIR 180
guanyl_kin TIGR03263
guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP ...
 4-185 4.60e-88

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: 255.88  E-value: 4.60e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524105083    4 KLIIFSAPSGSGKSTIINWLMShEELRMAFSISCTSRPPRGTERNGVEYFFVTPEEFRRRIDNDEFLEYEEVYkDRYYGT 83
Cdd:TIGR03263   1 LLIVISGPSGAGKSTLVKALLE-EDPNLKFSISATTRKPRPGEVDGVDYFFVSKEEFEEMIKAGEFLEWAEVH-GNYYGT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524105083   84 LKQQVEAQLEKGENVVFDVDVKGGCNIKNYYgDRALSVFIQPPSIEELRNRLTGRGTDAPEVIEDRIARASFELTFAPKF 163
Cdd:TIGR03263  79 PKSPVEEALAAGKDVLLEIDVQGARQVKKKF-PDAVSIFILPPSLEELERRLRKRGTDSEEVIERRLAKAKKEIAHADEF 157

                         170       180
                  ....*....|....*....|..
gi 524105083  164 DKVVVNDDLDKAKAEALKIVKD 185
Cdd:TIGR03263 158 DYVIVNDDLEKAVEELKSIILA 179
gmk PRK14738
guanylate kinase; Provisional
 4-183 2.17e-50

guanylate kinase; Provisional


Pssm-ID: 237809  Cd Length: 206  Bit Score: 161.44  E-value: 2.17e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524105083   4 KLIIFSAPSGSGKSTIINwLMSHEELRMAFSISCTSRPPRGTERNGVEYFFVTPEEFRRRIDNDEFLEYEEVYKDrYYGT 83
Cdd:PRK14738  14 LLVVISGPSGVGKDAVLA-RMRERKLPFHFVVTATTRPKRPGEIDGVDYHFVTPEEFREMISQNELLEWAEVYGN-YYGV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524105083  84 LKQQVEAQLEKGENVVFDVDVKGGCNIKNYYGDrALSVFIQPPSIEELRNRLTGRGTDAPEVIEDRIARASFELTFAPKF 163
Cdd:PRK14738  92 PKAPVRQALASGRDVIVKVDVQGAASIKRLVPE-AVFIFLAPPSMDELTRRLELRRTESPEELERRLATAPLELEQLPEF 170

                        170       180
                 ....*....|....*....|..
gi 524105083 164 DKVVVN--DDLDKAKAEALKIV 183
Cdd:PRK14738 171 DYVVVNpeDRLDEAVAQIMAII 192
GMPK cd00071
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ...
 5-178 1.82e-49

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: 156.54  E-value: 1.82e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524105083   5 LIIFSAPSGSGKSTIINWLMSHEELRMAFSISCTSRPPRGTERNGVEYFFVTPEEFRRRIDNDEFLEYEEVYKDrYYGTL 84
Cdd:cd00071    1 LIVLSGPSGVGKSTLLKRLLEEFDPNFGFSVSHTTRKPRPGEVDGVDYHFVSKEEFERLIENGEFLEWAEFHGN-YYGTS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524105083  85 KQQVEAQLEKGENVVFDVDVKGGCNIKNYYGDrALSVFIQPPsieelrnrltgrgtdapeviedriarasfeltfapkfD 164
Cdd:cd00071   80 KAAVEEALAEGKIVILEIDVQGARQVKKSYPD-AVSIFILPP-------------------------------------D 121

                        170
                 ....*....|....
gi 524105083 165 KVVVNDDLDKAKAE 178
Cdd:cd00071  122 YVIVNDDLEKAYEE 135
gmk PRK14737
guanylate kinase; Provisional
 4-183 1.05e-48

guanylate kinase; Provisional


Pssm-ID: 173199  Cd Length: 186  Bit Score: 156.69  E-value: 1.05e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524105083   4 KLIIFSAPSGSGKSTIINWLMShEELRMAFSISCTSRPPRGTERNGVEYFFVTPEEFRRRIDNDEFLEYEEVYkDRYYGT 83
Cdd:PRK14737   5 KLFIISSVAGGGKSTIIQALLE-EHPDFLFSISCTTRAPRPGDEEGKTYFFLTIEEFKKGIADGEFLEWAEVH-DNYYGT 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524105083  84 LKQQVEAQLEKGENVVFDVDVKGGCNIKNYYGDRALSVFIQPPSIEELRNRLTGRGTDAPEVIEDRIARASFELTFAPKF 163
Cdd:PRK14737  83 PKAFIEDAFKEGRSAIMDIDVQGAKIIKEKFPERIVTIFIEPPSEEEWEERLIHRGTDSEESIEKRIENGIIELDEANEF 162

                        170       180
                 ....*....|....*....|
gi 524105083 164 DKVVVNDDLDKAKAEALKIV 183
Cdd:PRK14737 163 DYKIINDDLEDAIADLEAII 182
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
 12-183 2.11e-48

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: 155.14  E-value: 2.11e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524105083    12 SGSGKSTIINWLMSHEELRMAFSISCTSRPPRGTERNGVEYFFVTPEEFRRRIDNDEFLEYEEvYKDRYYGTLKQQVEAQ 91
Cdd:smart00072   1 SGVGKGTLLAELIQEIPDAFERVVSHTTRPPRPGEVNGVDYHFVSKEEFEDDIKSGLFLEWGE-YEGNYYGTSKETIRQV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524105083    92 LEKGENVVFDVDVKGGCNIKNYYGDrALSVFIQPPSIEELRNRLTGRGTDAPEVIEDRIARASFELTFAPKFDKVVVNDD 171
Cdd:smart00072  80 AEKGKHCLLDIDPQGVKQLRKAQLY-PIVIFIAPPSSEELERRLRQRGTETSERIQKRLAAAQKEAQEYHLFDYVIVNDD 158

                          170
                   ....*....|..
gi 524105083   172 LDKAKAEALKIV 183
Cdd:smart00072 159 LEDAYEELKEIL 170
Guanylate_kin pfam00625
Guanylate kinase;
3-188 5.62e-47

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 151.76  E-value: 5.62e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524105083    3 GKLIIFSAPSGSGKSTIINWLMSHEELRMAFSISCTSRPPRGTERNGVEYFFVTPEEFRRRIDNDEFLEYEEvYKDRYYG 82
Cdd:pfam00625   2 RRPVVLSGPSGVGKSHIKKALLSEYPDKFGYSVPHTTRPPRKGEVDGKDYYFVSKEEMERDISANEFLEYAQ-FSGNMYG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524105083   83 TLKQQVEAQLEKGENVVFDVDVKGGCNIKNYYgDRALSVFIQPPSIEELRNRLTGRGTDAPEVIEDRIARASFELTfAPK 162
Cdd:pfam00625  81 TSVETIEQIHEQGKIVILDVDPQGVKQLRKAE-LSPISVFIKPPSLKVLQRRLKGRGKEQEEKINKRMAAAEQEFQ-HYE 158

                         170       180
                  ....*....|....*....|....*.
gi 524105083  163 FDKVVVNDDLDkakaEALKIVKDFLF 188
Cdd:pfam00625 159 FDVIIVNDDLE----EAYKKLKEALE 180
PLN02772 PLN02772
guanylate kinase
 4-174 6.50e-34

guanylate kinase


Pssm-ID: 215414 [Multi-domain]  Cd Length: 398  Bit Score: 123.79  E-value: 6.50e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524105083   4 KLIIFSAPSGSGKSTIINWLMSHEELRMAFSISCTSRPPRGTERNGVEYFFVTPEEFRRRIDNDEFLEYEEVYKDrYYGT 83
Cdd:PLN02772 136 KPIVISGPSGVGKGTLISMLMKEFPSMFGFSVSHTTRAPREMEKDGVHYHFTERSVMEKEIKDGKFLEFASVHGN-LYGT 214

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524105083  84 LKQQVEAQLEKGENVVFDVDVKGGCNIKNYYGDrALSVFIQPPSIEELRNRLTGRGTDAPEVIEDRI--ARASFELTFAP 161
Cdd:PLN02772 215 SIEAVEVVTDSGKRCILDIDVQGARSVRASSLE-AIFIFICPPSMEELEKRLRARGTETEEQIQKRLrnAEAELEQGKSS 293

                        170
                 ....*....|....
gi 524105083 162 K-FDKVVVNDDLDK 174
Cdd:PLN02772 294 GiFDHILYNDNLEE 307
PhnN COG3709
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
2-183 2.20e-10

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


Pssm-ID: 442923  Cd Length: 188  Bit Score: 57.12  E-value: 2.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524105083   2 PGKLIIFSAPSGSGKSTIINWLMSHEELRMAFSIS--CTSRPPR-GTErngvEYFFVTPEEFRRRIDNDEF--------L 70
Cdd:COG3709    4 PGRLIYVVGPSGAGKDSLLAAARARLAADPRLVFArrYITRPADaGGE----DHDALSEAEFARRAAAGAFalhwqahgL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524105083  71 eyeevykdrYYGtLKQQVEAQLEKGENVVfdvdvkggCNiknyyGDRA------------LSVFIQ-PPSIeeLRNRLTG 137
Cdd:COG3709   80 ---------RYG-IPAEIDAWLAAGRDVV--------VN-----GSRAvlpqararyprlLVVLITaSPEV--LAQRLAA 134

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 524105083 138 RGTDAPEVIEDRIARASfelTFAPKFDKVVV--ND-DLDKAKAEALKIV 183
Cdd:COG3709  135 RGRESAEEIEARLARAA---EFLPDGPDVLVidNDgPLEDAGARLLALL 180
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 5-157 1.60e-05

AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.


Pssm-ID: 463952 [Multi-domain]  Cd Length: 143  Bit Score: 42.68  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524105083    5 LIIFSAPSGSGKSTiinWLMSHEElrmafsisctsrpPRGTERngveyffVTPEEFRRRIDNDE---FLEYEEVYkDRYY 81
Cdd:pfam13671   1 LILLVGLPGSGKST---LARRLLE-------------ELGAVR-------LSSDDERKRLFGEGrpsISYYTDAT-DRTY 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524105083   82 GTLKQQVEAQLEKGENVVFD---VDV---KGGCNIKNYYGDRALSVFIQPPsIEELRNRLTGR---GTDAPEVIEDRIAR 152
Cdd:pfam13671  57 ERLHELARIALRAGRPVILDatnLRRderARLLALAREYGVPVRIVVFEAP-EEVLRERLAARaraGGDPSDVPEEVLDR 135


                  ....*..
gi 524105083  153 --ASFEL 157
Cdd:pfam13671 136 qkARFEP 142
PRK10078 PRK10078
ribose 1,5-bisphosphokinase; Provisional
 2-171 2.04e-05

ribose 1,5-bisphosphokinase; Provisional


Pssm-ID: 236648  Cd Length: 186  Bit Score: 43.20  E-value: 2.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524105083   2 PGKLIIFSAPSGSGKSTIINWLMSHEELRMAFSISCTSRPPRGTERNGVEyffVTPEEFRRRIDNDEF-LEYEEvyKDRY 80
Cdd:PRK10078   1 MGKLIWLMGPSGSGKDSLLAALRQREQTQLLVAHRYITRPASAGSENHIA---LSEQEFFTRAGQNLFaLSWHA--NGLY 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524105083  81 YGtLKQQVEAQLEKGenvvFDVDVKGG----CNIKNYYGDRALSVFIQ-PPSIeeLRNRLTGRGTDAPEVIEDRIARASF 155
Cdd:PRK10078  76 YG-VGIEIDLWLHAG----FDVLVNGSrahlPQARARYQSALLPVCLQvSPEI--LRQRLENRGRENASEINARLARAAR 148

                        170
                 ....*....|....*.
gi 524105083 156 EltfaPKFDKVVVNDD 171
Cdd:PRK10078 149 Y----QPQDCHTLNND 160
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 3-30 6.65e-04

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: 38.92  E-value: 6.65e-04
                         10        20
                 ....*....|....*....|....*...
gi 524105083   3 GKLIIFSAPSGSGKSTIINWLMSHEELR 30
Cdd:cd01854   85 GKTSVLVGQSGVGKSTLLNALLPELVLA 112
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
 3-30 1.97e-03

RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.


Pssm-ID: 427191 [Multi-domain]  Cd Length: 174  Bit Score: 37.14  E-value: 1.97e-03
                          10        20
                  ....*....|....*....|....*...
gi 524105083    3 GKLIIFSAPSGSGKSTIINWLMSHEELR 30
Cdd:pfam03193 106 GKTTVLAGQSGVGKSTLLNALLPELDLR 133
Tmk COG0125
Thymidylate kinase [Nucleotide transport and metabolism]; Thymidylate kinase is part of the ...
 1-46 2.26e-03

Thymidylate kinase [Nucleotide transport and metabolism]; Thymidylate kinase is part of the Pathway/BioSystem: Thymidylate biosynthesis


Pssm-ID: 439895 [Multi-domain]  Cd Length: 206  Bit Score: 37.44  E-value: 2.26e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 524105083   1 MPGKLIIFSAPSGSGKSTIINWLmsHEELRmAFSISC-TSRPPRGTE 46
Cdd:COG0125    1 MKGKFIVFEGIDGSGKSTQIKLL--AEYLE-ARGYDVvLTREPGGTP 44
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
2-64 2.47e-03

ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 37.10  E-value: 2.47e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 524105083   2 PGKLIIFSAPSGSGKSTIinwlmsheeLRMafsISCTSRPPRGTER-NGVEYFFVTPEEFRRRI 64
Cdd:COG4619   25 AGECVAITGPSGSGKSTL---------LRA---LADLDPPTSGEIYlDGKPLSAMPPPEWRRQV 76
PRK12289 PRK12289
small ribosomal subunit biogenesis GTPase RsgA;
3-53 3.44e-03

small ribosomal subunit biogenesis GTPase RsgA;


Pssm-ID: 237040 [Multi-domain]  Cd Length: 352  Bit Score: 37.30  E-value: 3.44e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 524105083   3 GKLIIFSAPSGSGKSTIINWLMSHEELRMAfSISCTSRPPRGTERNgVEYF 53
Cdd:PRK12289 172 NKITVVAGPSGVGKSSLINRLIPDVELRVG-KVSGKLGRGRHTTRH-VELF 220
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
 3-103 7.09e-03

Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 442498 [Multi-domain]  Cd Length: 261  Bit Score: 36.30  E-value: 7.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524105083   3 GKLIIFSAPSGSGKSTIINWLMS--HEELRMAFSISctsrpPRgterngveyffVTPEEFRRRIdNDEF-LEYEEVYKDR 79
Cdd:COG3267   43 GGFVVLTGEVGTGKTTLLRRLLErlPDDVKVAYIPN-----PQ-----------LSPAELLRAI-ADELgLEPKGASKAD 105

                         90       100
                 ....*....|....*....|....
gi 524105083  80 YYGTLKQQVEAQLEKGENVVFDVD 103
Cdd:COG3267  106 LLRQLQEFLLELAAAGRRVVLIID 129
 
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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