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Conserved domains on  [gi|488949178|ref|WP_002860253|]
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MULTISPECIES: guanylate kinase [Campylobacter]

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
 1-207 4.87e-97

guanylate kinase; Provisional


:

Pssm-ID: 234719  Cd Length: 205  Bit Score: 280.44  E-value: 4.87e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488949178   1 MKLQGFVLLISGPSGAGKSTLLKKLFDEFEDeLYFSISSTTRKPREGEKNGIHYHFISHEEFQKGIDSDHFLEWARVHEN 80
Cdd:PRK00300   1 MMRRGLLIVLSGPSGAGKSTLVKALLERDPN-LQLSVSATTRAPRPGEVDGVDYFFVSKEEFEEMIENGEFLEWAEVFGN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488949178  81 FYGTSLKHTQNALDNGKIVVFDIDVQGFKIARKKMADkIVSVFITTKNKDELKKRLIKRNTDTIIQLEKRLQNASDEMKE 160
Cdd:PRK00300  80 YYGTPRSPVEEALAAGKDVLLEIDWQGARQVKKKMPD-AVSIFILPPSLEELERRLRGRGTDSEEVIARRLAKAREEIAH 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 488949178 161 LSEYDYLIINDELKQSYEALRAILIAHKFRTKGQNLGQIQNIWNEGE 207
Cdd:PRK00300 159 ASEYDYVIVNDDLDTALEELKAIIRAERLRRSRQQQRHAELIEELLA 205
 
Name Accession Description Interval E-value
gmk PRK00300
guanylate kinase; Provisional
 1-207 4.87e-97

guanylate kinase; Provisional


Pssm-ID: 234719  Cd Length: 205  Bit Score: 280.44  E-value: 4.87e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488949178   1 MKLQGFVLLISGPSGAGKSTLLKKLFDEFEDeLYFSISSTTRKPREGEKNGIHYHFISHEEFQKGIDSDHFLEWARVHEN 80
Cdd:PRK00300   1 MMRRGLLIVLSGPSGAGKSTLVKALLERDPN-LQLSVSATTRAPRPGEVDGVDYFFVSKEEFEEMIENGEFLEWAEVFGN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488949178  81 FYGTSLKHTQNALDNGKIVVFDIDVQGFKIARKKMADkIVSVFITTKNKDELKKRLIKRNTDTIIQLEKRLQNASDEMKE 160
Cdd:PRK00300  80 YYGTPRSPVEEALAAGKDVLLEIDWQGARQVKKKMPD-AVSIFILPPSLEELERRLRGRGTDSEEVIARRLAKAREEIAH 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 488949178 161 LSEYDYLIINDELKQSYEALRAILIAHKFRTKGQNLGQIQNIWNEGE 207
Cdd:PRK00300 159 ASEYDYVIVNDDLDTALEELKAIIRAERLRRSRQQQRHAELIEELLA 205
guanyl_kin TIGR03263
guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP ...
 7-186 1.01e-96

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: 278.61  E-value: 1.01e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488949178    7 VLLISGPSGAGKSTLLKKLFDEFeDELYFSISSTTRKPREGEKNGIHYHFISHEEFQKGIDSDHFLEWARVHENFYGTSL 86
Cdd:TIGR03263   2 LIVISGPSGAGKSTLVKALLEED-PNLKFSISATTRKPRPGEVDGVDYFFVSKEEFEEMIKAGEFLEWAEVHGNYYGTPK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488949178   87 KHTQNALDNGKIVVFDIDVQGFKIARKKMADkIVSVFITTKNKDELKKRLIKRNTDTIIQLEKRLQNASDEMKELSEYDY 166
Cdd:TIGR03263  81 SPVEEALAAGKDVLLEIDVQGARQVKKKFPD-AVSIFILPPSLEELERRLRKRGTDSEEVIERRLAKAKKEIAHADEFDY 159

                         170       180
                  ....*....|....*....|
gi 488949178  167 LIINDELKQSYEALRAILIA 186
Cdd:TIGR03263 160 VIVNDDLEKAVEELKSIILA 179
Gmk COG0194
Guanylate kinase [Nucleotide transport and metabolism];
4-194 8.52e-92

Guanylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 439964  Cd Length: 190  Bit Score: 266.55  E-value: 8.52e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488949178   4 QGFVLLISGPSGAGKSTLLKKLFDEFeDELYFSISSTTRKPREGEKNGIHYHFISHEEFQKGIDSDHFLEWARVHENFYG 83
Cdd:COG0194    1 RGKLIVLSGPSGAGKTTLVKALLERD-PDLRFSVSATTRPPRPGEVDGVDYHFVSREEFERMIENGEFLEWAEVHGNYYG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488949178  84 TSLKHTQNALDNGKIVVFDIDVQGFKIARKKMADkIVSVFITTKNKDELKKRLIKRNTDTIIQLEKRLQNASDEMKELSE 163
Cdd:COG0194   80 TPKAEVEEALAAGKDVLLEIDVQGARQVKKKFPD-AVSIFILPPSLEELERRLRGRGTDSEEVIERRLAKAREELAHADE 158

                        170       180       190
                 ....*....|....*....|....*....|.
gi 488949178 164 YDYLIINDELKQSYEALRAILIAHKFRTKGQ 194
Cdd:COG0194  159 FDYVVVNDDLDRAVEELKAIIRAERLRRERQ 189
GMPK cd00071
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ...
 7-181 6.33e-59

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: 181.58  E-value: 6.33e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488949178   7 VLLISGPSGAGKSTLLKKLFDEFEDELYFSISSTTRKPREGEKNGIHYHFISHEEFQKGIDSDHFLEWARVHENFYGTSL 86
Cdd:cd00071    1 LIVLSGPSGVGKSTLLKRLLEEFDPNFGFSVSHTTRKPRPGEVDGVDYHFVSKEEFERLIENGEFLEWAEFHGNYYGTSK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488949178  87 KHTQNALDNGKIVVFDIDVQGFKIARKKMADkIVSVFITTKnkdelkkrlikrntdtiiqlekrlqnasdemkelseyDY 166
Cdd:cd00071   81 AAVEEALAEGKIVILEIDVQGARQVKKSYPD-AVSIFILPP-------------------------------------DY 122

                        170
                 ....*....|....*
gi 488949178 167 LIINDELKQSYEALR 181
Cdd:cd00071  123 VIVNDDLEKAYEELK 137
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
 14-186 1.86e-53

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: 169.01  E-value: 1.86e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488949178    14 SGAGKSTLLKKLFDEFEDELYFSISSTTRKPREGEKNGIHYHFISHEEFQKGIDSDHFLEWARVHENFYGTSLKHTQNAL 93
Cdd:smart00072   1 SGVGKGTLLAELIQEIPDAFERVVSHTTRPPRPGEVNGVDYHFVSKEEFEDDIKSGLFLEWGEYEGNYYGTSKETIRQVA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488949178    94 DNGKIVVFDIDVQGFKIARKKMADKIVsVFITTKNKDELKKRLIKRNTDTIIQLEKRLQNASDEMKELSEYDYLIINDEL 173
Cdd:smart00072  81 EKGKHCLLDIDPQGVKQLRKAQLYPIV-IFIAPPSSEELERRLRQRGTETSERIQKRLAAAQKEAQEYHLFDYVIVNDDL 159

                          170
                   ....*....|...
gi 488949178   174 KQSYEALRAILIA 186
Cdd:smart00072 160 EDAYEELKEILEA 172
Guanylate_kin pfam00625
Guanylate kinase;
8-184 4.32e-50

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 160.62  E-value: 4.32e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488949178    8 LLISGPSGAGKSTLLKKLFDEFEDELYFSISSTTRKPREGEKNGIHYHFISHEEFQKGIDSDHFLEWARVHENFYGTSLK 87
Cdd:pfam00625   5 VVLSGPSGVGKSHIKKALLSEYPDKFGYSVPHTTRPPRKGEVDGKDYYFVSKEEMERDISANEFLEYAQFSGNMYGTSVE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488949178   88 HTQNALDNGKIVVFDIDVQGFKIARKKMADKIvSVFITTKNKDELKKRLIKRNTDTIIQLEKRLQNASDEMKElSEYDYL 167
Cdd:pfam00625  85 TIEQIHEQGKIVILDVDPQGVKQLRKAELSPI-SVFIKPPSLKVLQRRLKGRGKEQEEKINKRMAAAEQEFQH-YEFDVI 162

                         170
                  ....*....|....*..
gi 488949178  168 IINDELKQSYEALRAIL 184
Cdd:pfam00625 163 IVNDDLEEAYKKLKEAL 179
 
Name Accession Description Interval E-value
gmk PRK00300
guanylate kinase; Provisional
 1-207 4.87e-97

guanylate kinase; Provisional


Pssm-ID: 234719  Cd Length: 205  Bit Score: 280.44  E-value: 4.87e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488949178   1 MKLQGFVLLISGPSGAGKSTLLKKLFDEFEDeLYFSISSTTRKPREGEKNGIHYHFISHEEFQKGIDSDHFLEWARVHEN 80
Cdd:PRK00300   1 MMRRGLLIVLSGPSGAGKSTLVKALLERDPN-LQLSVSATTRAPRPGEVDGVDYFFVSKEEFEEMIENGEFLEWAEVFGN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488949178  81 FYGTSLKHTQNALDNGKIVVFDIDVQGFKIARKKMADkIVSVFITTKNKDELKKRLIKRNTDTIIQLEKRLQNASDEMKE 160
Cdd:PRK00300  80 YYGTPRSPVEEALAAGKDVLLEIDWQGARQVKKKMPD-AVSIFILPPSLEELERRLRGRGTDSEEVIARRLAKAREEIAH 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 488949178 161 LSEYDYLIINDELKQSYEALRAILIAHKFRTKGQNLGQIQNIWNEGE 207
Cdd:PRK00300 159 ASEYDYVIVNDDLDTALEELKAIIRAERLRRSRQQQRHAELIEELLA 205
guanyl_kin TIGR03263
guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP ...
 7-186 1.01e-96

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: 278.61  E-value: 1.01e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488949178    7 VLLISGPSGAGKSTLLKKLFDEFeDELYFSISSTTRKPREGEKNGIHYHFISHEEFQKGIDSDHFLEWARVHENFYGTSL 86
Cdd:TIGR03263   2 LIVISGPSGAGKSTLVKALLEED-PNLKFSISATTRKPRPGEVDGVDYFFVSKEEFEEMIKAGEFLEWAEVHGNYYGTPK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488949178   87 KHTQNALDNGKIVVFDIDVQGFKIARKKMADkIVSVFITTKNKDELKKRLIKRNTDTIIQLEKRLQNASDEMKELSEYDY 166
Cdd:TIGR03263  81 SPVEEALAAGKDVLLEIDVQGARQVKKKFPD-AVSIFILPPSLEELERRLRKRGTDSEEVIERRLAKAKKEIAHADEFDY 159

                         170       180
                  ....*....|....*....|
gi 488949178  167 LIINDELKQSYEALRAILIA 186
Cdd:TIGR03263 160 VIVNDDLEKAVEELKSIILA 179
Gmk COG0194
Guanylate kinase [Nucleotide transport and metabolism];
4-194 8.52e-92

Guanylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 439964  Cd Length: 190  Bit Score: 266.55  E-value: 8.52e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488949178   4 QGFVLLISGPSGAGKSTLLKKLFDEFeDELYFSISSTTRKPREGEKNGIHYHFISHEEFQKGIDSDHFLEWARVHENFYG 83
Cdd:COG0194    1 RGKLIVLSGPSGAGKTTLVKALLERD-PDLRFSVSATTRPPRPGEVDGVDYHFVSREEFERMIENGEFLEWAEVHGNYYG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488949178  84 TSLKHTQNALDNGKIVVFDIDVQGFKIARKKMADkIVSVFITTKNKDELKKRLIKRNTDTIIQLEKRLQNASDEMKELSE 163
Cdd:COG0194   80 TPKAEVEEALAAGKDVLLEIDVQGARQVKKKFPD-AVSIFILPPSLEELERRLRGRGTDSEEVIERRLAKAREELAHADE 158

                        170       180       190
                 ....*....|....*....|....*....|.
gi 488949178 164 YDYLIINDELKQSYEALRAILIAHKFRTKGQ 194
Cdd:COG0194  159 FDYVVVNDDLDRAVEELKAIIRAERLRRERQ 189
GMPK cd00071
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ...
 7-181 6.33e-59

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: 181.58  E-value: 6.33e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488949178   7 VLLISGPSGAGKSTLLKKLFDEFEDELYFSISSTTRKPREGEKNGIHYHFISHEEFQKGIDSDHFLEWARVHENFYGTSL 86
Cdd:cd00071    1 LIVLSGPSGVGKSTLLKRLLEEFDPNFGFSVSHTTRKPRPGEVDGVDYHFVSKEEFERLIENGEFLEWAEFHGNYYGTSK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488949178  87 KHTQNALDNGKIVVFDIDVQGFKIARKKMADkIVSVFITTKnkdelkkrlikrntdtiiqlekrlqnasdemkelseyDY 166
Cdd:cd00071   81 AAVEEALAEGKIVILEIDVQGARQVKKSYPD-AVSIFILPP-------------------------------------DY 122

                        170
                 ....*....|....*
gi 488949178 167 LIINDELKQSYEALR 181
Cdd:cd00071  123 VIVNDDLEKAYEELK 137
gmk PRK14737
guanylate kinase; Provisional
 9-188 5.54e-55

guanylate kinase; Provisional


Pssm-ID: 173199  Cd Length: 186  Bit Score: 173.25  E-value: 5.54e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488949178   9 LISGPSGAGKSTLLKKLFDEfEDELYFSISSTTRKPREGEKNGIHYHFISHEEFQKGIDSDHFLEWARVHENFYGTSLKH 88
Cdd:PRK14737   8 IISSVAGGGKSTIIQALLEE-HPDFLFSISCTTRAPRPGDEEGKTYFFLTIEEFKKGIADGEFLEWAEVHDNYYGTPKAF 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488949178  89 TQNALDNGKIVVFDIDVQGFKIARKKMADKIVSVFITTKNKDELKKRLIKRNTDTIIQLEKRLQNASDEMKELSEYDYLI 168
Cdd:PRK14737  87 IEDAFKEGRSAIMDIDVQGAKIIKEKFPERIVTIFIEPPSEEEWEERLIHRGTDSEESIEKRIENGIIELDEANEFDYKI 166

                        170       180
                 ....*....|....*....|
gi 488949178 169 INDELKQSYEALRAILIAHK 188
Cdd:PRK14737 167 INDDLEDAIADLEAIICGKK 186
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
 14-186 1.86e-53

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: 169.01  E-value: 1.86e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488949178    14 SGAGKSTLLKKLFDEFEDELYFSISSTTRKPREGEKNGIHYHFISHEEFQKGIDSDHFLEWARVHENFYGTSLKHTQNAL 93
Cdd:smart00072   1 SGVGKGTLLAELIQEIPDAFERVVSHTTRPPRPGEVNGVDYHFVSKEEFEDDIKSGLFLEWGEYEGNYYGTSKETIRQVA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488949178    94 DNGKIVVFDIDVQGFKIARKKMADKIVsVFITTKNKDELKKRLIKRNTDTIIQLEKRLQNASDEMKELSEYDYLIINDEL 173
Cdd:smart00072  81 EKGKHCLLDIDPQGVKQLRKAQLYPIV-IFIAPPSSEELERRLRQRGTETSERIQKRLAAAQKEAQEYHLFDYVIVNDDL 159

                          170
                   ....*....|...
gi 488949178   174 KQSYEALRAILIA 186
Cdd:smart00072 160 EDAYEELKEILEA 172
gmk PRK14738
guanylate kinase; Provisional
 8-190 2.95e-51

guanylate kinase; Provisional


Pssm-ID: 237809  Cd Length: 206  Bit Score: 164.52  E-value: 2.95e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488949178   8 LLISGPSGAGKSTLLKKLfDEFEDELYFSISSTTRKPREGEKNGIHYHFISHEEFQKGIDSDHFLEWARVHENFYGTSLK 87
Cdd:PRK14738  16 VVISGPSGVGKDAVLARM-RERKLPFHFVVTATTRPKRPGEIDGVDYHFVTPEEFREMISQNELLEWAEVYGNYYGVPKA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488949178  88 HTQNALDNGKIVVFDIDVQGfKIARKKMADKIVSVFITTKNKDELKKRLIKRNTDTIIQLEKRLQNASDEMKELSEYDYL 167
Cdd:PRK14738  95 PVRQALASGRDVIVKVDVQG-AASIKRLVPEAVFIFLAPPSMDELTRRLELRRTESPEELERRLATAPLELEQLPEFDYV 173

                        170       180
                 ....*....|....*....|....*
gi 488949178 168 IIN--DELKQSYEALRAILIAHKFR 190
Cdd:PRK14738 174 VVNpeDRLDEAVAQIMAIISAEKSR 198
Guanylate_kin pfam00625
Guanylate kinase;
8-184 4.32e-50

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 160.62  E-value: 4.32e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488949178    8 LLISGPSGAGKSTLLKKLFDEFEDELYFSISSTTRKPREGEKNGIHYHFISHEEFQKGIDSDHFLEWARVHENFYGTSLK 87
Cdd:pfam00625   5 VVLSGPSGVGKSHIKKALLSEYPDKFGYSVPHTTRPPRKGEVDGKDYYFVSKEEMERDISANEFLEYAQFSGNMYGTSVE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488949178   88 HTQNALDNGKIVVFDIDVQGFKIARKKMADKIvSVFITTKNKDELKKRLIKRNTDTIIQLEKRLQNASDEMKElSEYDYL 167
Cdd:pfam00625  85 TIEQIHEQGKIVILDVDPQGVKQLRKAELSPI-SVFIKPPSLKVLQRRLKGRGKEQEEKINKRMAAAEQEFQH-YEFDVI 162

                         170
                  ....*....|....*..
gi 488949178  168 IINDELKQSYEALRAIL 184
Cdd:pfam00625 163 IVNDDLEEAYKKLKEAL 179
PLN02772 PLN02772
guanylate kinase
 8-184 1.31e-49

guanylate kinase


Pssm-ID: 215414 [Multi-domain]  Cd Length: 398  Bit Score: 165.78  E-value: 1.31e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488949178   8 LLISGPSGAGKSTLLKKLFDEFEDELYFSISSTTRKPREGEKNGIHYHFISHEEFQKGIDSDHFLEWARVHENFYGTSLK 87
Cdd:PLN02772 138 IVISGPSGVGKGTLISMLMKEFPSMFGFSVSHTTRAPREMEKDGVHYHFTERSVMEKEIKDGKFLEFASVHGNLYGTSIE 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488949178  88 HTQNALDNGKIVVFDIDVQGFKIARKKMADKIVsVFITTKNKDELKKRLIKRNTDTIIQLEKRLQNASDEMKELSE---Y 164
Cdd:PLN02772 218 AVEVVTDSGKRCILDIDVQGARSVRASSLEAIF-IFICPPSMEELEKRLRARGTETEEQIQKRLRNAEAELEQGKSsgiF 296

                        170       180
                 ....*....|....*....|
gi 488949178 165 DYLIINDELKQSYEALRAIL 184
Cdd:PLN02772 297 DHILYNDNLEECYKNLKKLL 316
phosphon_PhnN TIGR02322
phosphonate metabolism protein/1,5-bisphosphokinase (PRPP-forming) PhnN; Members of this ...
 5-155 7.03e-06

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: 44.66  E-value: 7.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488949178    5 GFVLLIsGPSGAGKSTLLKKLFDEFEDE--LYFSISSTTRKPREGEKNGIHyhfISHEEFQKGIDSDHF-LEWaRVHENF 81
Cdd:TIGR02322   2 RLIYVV-GPSGAGKDTLLDYARARLAGDprVHFVRRVITRPASAGGENHIA---LSTEEFDHREDGGAFaLSW-QAHGLS 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488949178   82 YGTSLKhTQNALDNGKIVVFDIDVQGFKIARKKMAdKIVSVFITTkNKDELKKRLIKRNTDTIIQLEKRLQNAS 155
Cdd:TIGR02322  77 YGIPIE-IDQWLEAGDVVVVNGSRAVLPEARQRYP-NLLVVNITA-SPDVLAQRLAARGRESREEIEERLARSA 147
PhnN COG3709
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
1-184 1.14e-05

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


Pssm-ID: 442923  Cd Length: 188  Bit Score: 44.03  E-value: 1.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488949178   1 MKLQG-FVLLIsGPSGAGKSTLLKKLFDEFEDE--LYF---SIsstTRKPREGEKNgiHYHfISHEEFQKGIDSDHF-LE 73
Cdd:COG3709    1 MSGPGrLIYVV-GPSGAGKDSLLAAARARLAADprLVFarrYI---TRPADAGGED--HDA-LSEAEFARRAAAGAFaLH 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488949178  74 WaRVHENFYG--TSLKHtqnALDNGKIVVFDIDVQGFKIARKKMADKIVsVFITTKNkDELKKRLIKRNTDTIIQLEKRL 151
Cdd:COG3709   74 W-QAHGLRYGipAEIDA---WLAAGRDVVVNGSRAVLPQARARYPRLLV-VLITASP-EVLAQRLAARGRESAEEIEARL 147

                        170       180       190
                 ....*....|....*....|....*....|....
gi 488949178 152 QNASDEMKELSEyDYLIIND-ELKQSYEALRAIL 184
Cdd:COG3709  148 ARAAEFLPDGPD-VLVIDNDgPLEDAGARLLALL 180
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 6-45 1.47e-04

Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 440337 [Multi-domain]  Cd Length: 206  Bit Score: 40.98  E-value: 1.47e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 488949178   6 FVLLISGPSGAGKSTLLKKLFDEFE---------DELYFSISSTTRKPR 45
Cdd:COG0572    8 RIIGIAGPSGSGKTTFARRLAEQLGadkvvvislDDYYKDREHLPLDER 56
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
 4-46 4.21e-04

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: 40.16  E-value: 4.21e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 488949178   4 QGFVLLIsGPSGAGKSTLLKKLFDEFEDELYF-SISSTTRKPRE 46
Cdd:COG3267   43 GGFVVLT-GEVGTGKTTLLRRLLERLPDDVKVaYIPNPQLSPAE 85
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
8-27 4.50e-04

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 39.80  E-value: 4.50e-04
                         10        20
                 ....*....|....*....|
gi 488949178   8 LLISGPSGAGKSTLLKKLFD 27
Cdd:COG4619   29 VAITGPSGSGKSTLLRALAD 48
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
6-23 5.02e-04

Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 39.65  E-value: 5.02e-04
                         10
                 ....*....|....*...
gi 488949178   6 FVLLIsGPSGAGKSTLLK 23
Cdd:COG2884   30 FVFLT-GPSGAGKSTLLK 46
PRK10078 PRK10078
ribose 1,5-bisphosphokinase; Provisional
 12-184 8.66e-04

ribose 1,5-bisphosphokinase; Provisional


Pssm-ID: 236648  Cd Length: 186  Bit Score: 38.57  E-value: 8.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488949178  12 GPSGAGKSTLLKKLFDEFEDELYFSISSTTRKPREGEKNGIHyhfISHEEF----QKGIDSdhfLEWaRVHENFYGTSLK 87
Cdd:PRK10078   9 GPSGSGKDSLLAALRQREQTQLLVAHRYITRPASAGSENHIA---LSEQEFftraGQNLFA---LSW-HANGLYYGVGIE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488949178  88 hTQNALDNGkivvFDIDVQGFKI----ARKKMADKIVSVFITTkNKDELKKRLIKRNTDTIIQLEKRLQNASDEmkelSE 163
Cdd:PRK10078  82 -IDLWLHAG----FDVLVNGSRAhlpqARARYQSALLPVCLQV-SPEILRQRLENRGRENASEINARLARAARY----QP 151

                        170       180
                 ....*....|....*....|...
gi 488949178 164 YDYLIIND--ELKQSYEALRAIL 184
Cdd:PRK10078 152 QDCHTLNNdgSLRQSVDTLLTLL 174
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 4-149 9.66e-04

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 38.12  E-value: 9.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488949178     4 QGFVLLISGPSGAGKSTLLKKLFDEFEDELYFSISSTTRKPREGEKNGIHYHFISHEEFQKGIDSDHFLEWARVHENFYG 83
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488949178    84 -------TSLKHTQNALDNGKIVVFDIDVQGFKIARkkmadkiVSVFITTKNKDELKKRLIKRNTDTIIQLEK 149
Cdd:smart00382  81 vlildeiTSLLDAEQEALLLLLEELRLLLLLKSEKN-------LTVILTTNDEKDLGPALLRRRFDRRIVLLL 146
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
 4-28 1.04e-03

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 38.79  E-value: 1.04e-03
                         10        20
                 ....*....|....*....|....*
gi 488949178   4 QGFVLLISGPSGAGKSTLLKKLFDE 28
Cdd:COG2401   55 PGEIVLIVGASGSGKSTLLRLLAGA 79
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
 8-26 1.07e-03

Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];


Pssm-ID: 443809 [Multi-domain]  Cd Length: 229  Bit Score: 38.57  E-value: 1.07e-03
                         10
                 ....*....|....*....
gi 488949178   8 LLISGPSGAGKSTLLKKLF 26
Cdd:COG4778   40 VALTGPSGAGKSTLLKCIY 58
COG4639 COG4639
Predicted kinase [General function prediction only];
7-30 1.15e-03

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 37.89  E-value: 1.15e-03
                         10        20
                 ....*....|....*....|....
gi 488949178   7 VLLIsGPSGAGKSTLLKKLFDEFE 30
Cdd:COG4639    5 VVLI-GLPGSGKSTFARRLFAPTE 27
NK cd02019
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ...
 7-31 1.22e-03

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


Pssm-ID: 238977 [Multi-domain]  Cd Length: 69  Bit Score: 36.16  E-value: 1.22e-03
                         10        20
                 ....*....|....*....|....*
gi 488949178   7 VLLISGPSGAGKSTLLKKLFDEFED 31
Cdd:cd02019    1 IIAITGGSGSGKSTVAKKLAEQLGG 25
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
 8-23 1.31e-03

ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 39.02  E-value: 1.31e-03
                         10
                 ....*....|....*.
gi 488949178   8 LLISGPSGAGKSTLLK 23
Cdd:COG4178  392 LLITGPSGSGKSTLLR 407
PRK05416 PRK05416
RNase adapter RapZ;
7-37 1.44e-03

RNase adapter RapZ;


Pssm-ID: 235450  Cd Length: 288  Bit Score: 38.54  E-value: 1.44e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 488949178   7 VLLISGPSGAGKSTLLKKLfdefEDELYFSI 37
Cdd:PRK05416   8 LVIVTGLSGAGKSVALRAL----EDLGYYCV 34
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 4-98 2.43e-03

ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 36.86  E-value: 2.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488949178    4 QGFVLLISGPSGAGKSTLLKklfdefedelyfSISSTTrKPREGE--KNGIHYHFISHEEFQKGI----DSDHFLEWARV 77
Cdd:pfam00005  10 PGEILALVGPNGAGKSTLLK------------LIAGLL-SPTEGTilLDGQDLTDDERKSLRKEIgyvfQDPQLFPRLTV 76

                          90       100
                  ....*....|....*....|..
gi 488949178   78 HEN-FYGTSLKHTQNALDNGKI 98
Cdd:pfam00005  77 RENlRLGLLLKGLSKREKDARA 98
COG1373 COG1373
Predicted ATPase, AAA+ superfamily [General function prediction only];
4-36 3.12e-03

Predicted ATPase, AAA+ superfamily [General function prediction only];


Pssm-ID: 440984 [Multi-domain]  Cd Length: 405  Bit Score: 37.62  E-value: 3.12e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 488949178   4 QGFVLLISGPSGAGKSTLLKKLFDEFEDELYFS 36
Cdd:COG1373   19 NRKAVVITGPRQVGKTTLLKQLAKELENILYIN 51
RAD55 COG0467
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
4-164 3.50e-03

RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];


Pssm-ID: 440235 [Multi-domain]  Cd Length: 221  Bit Score: 37.20  E-value: 3.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488949178   4 QGFVLLISGPSGAGKSTLLKKLfdefedeLYfsissttrkprEGEKNGIHYHFISHEEfqkgiDSDHFLEWARvhenFYG 83
Cdd:COG0467   19 RGSSTLLSGPPGTGKTTLALQF-------LA-----------EGLRRGEKGLYVSFEE-----SPEQLLRRAE----SLG 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488949178  84 TSLkhtQNALDNGKIVVFDIDVQGFKIARKKMADKIVSVFITTKNkdelkKRLIKRNTDTIIQLEKRLQNASDEMKELSE 163
Cdd:COG0467   72 LDL---EEYIESGLLRIIDLSPEELGLDLEELLARLREAVEEFGA-----KRVVIDSLSGLLLALPDPERLREFLHRLLR 143


                 .
gi 488949178 164 Y 164
Cdd:COG0467  144 Y 144
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
 7-32 4.38e-03

AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 36.33  E-value: 4.38e-03
                          10        20
                  ....*....|....*....|....*.
gi 488949178    7 VLLISGPSGAGKSTLLKKLFDEFEDE 32
Cdd:pfam13191  26 SVLLTGEAGTGKTTLLRELLRALERD 51
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
 2-25 4.78e-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: 36.37  E-value: 4.78e-03
                          10        20
                  ....*....|....*....|....
gi 488949178    2 KLQGFVLLISGPSGAGKSTLLKKL 25
Cdd:pfam03193 103 LLKGKTTVLAGQSGVGKSTLLNAL 126
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
 5-25 5.81e-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: 36.30  E-value: 5.81e-03
                         10        20
                 ....*....|....*....|.
gi 488949178   5 GFVLLISGPSGAGKSTLLKKL 25
Cdd:COG4133   28 GEALALTGPNGSGKTTLLRIL 48
APS_kinase pfam01583
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ...
 4-27 6.49e-03

Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3'-phosphoadenylylsulfate. This domain contains an ATP binding P-loop motif.


Pssm-ID: 396247 [Multi-domain]  Cd Length: 154  Bit Score: 35.76  E-value: 6.49e-03
                          10        20
                  ....*....|....*....|....*...
gi 488949178    4 QGFVLLISGPSGAGKST----LLKKLFD 27
Cdd:pfam01583   1 RGCTIWLTGLSGAGKSTianaLERKLFE 28
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 1-32 6.53e-03

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 36.29  E-value: 6.53e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 488949178   1 MKLQGFVLLISGPSGAGKSTLLKKLFDEFEDE 32
Cdd:PRK05480   2 MMKKPIIIGIAGGSGSGKTTVASTIYEELGDE 33
AAA_29 pfam13555
P-loop containing region of AAA domain;
9-22 7.67e-03

P-loop containing region of AAA domain;


Pssm-ID: 433304 [Multi-domain]  Cd Length: 61  Bit Score: 33.73  E-value: 7.67e-03
                          10
                  ....*....|....
gi 488949178    9 LISGPSGAGKSTLL 22
Cdd:pfam13555  26 LLTGPSGSGKSTLL 39
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
 4-25 8.10e-03

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 36.29  E-value: 8.10e-03
                         10        20
                 ....*....|....*....|..
gi 488949178   4 QGFVLLISGPSGAGKSTLLKKL 25
Cdd:PRK13548  27 PGEVVAILGPNGAGKSTLLRAL 48
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
 6-23 8.60e-03

ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 36.20  E-value: 8.60e-03
                         10
                 ....*....|....*...
gi 488949178   6 FVLLisGPSGAGKSTLLK 23
Cdd:COG3839   32 LVLL--GPSGCGKSTLLR 47
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 3-28 9.48e-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: 35.84  E-value: 9.48e-03
                         10        20
                 ....*....|....*....|....*.
gi 488949178   3 LQGFVLLISGPSGAGKSTLLKKLFDE 28
Cdd:cd01854   83 LKGKTSVLVGQSGVGKSTLLNALLPE 108
AAA_18 pfam13238
AAA domain;
9-150 9.49e-03

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 35.10  E-value: 9.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488949178    9 LISGPSGAGKSTLLKKLfdefEDELYFSISSTtrkpREGEKNGIHYHFISHEEFQKGIDSDhflEWARVHENFygtslkH 88
Cdd:pfam13238   2 LITGTPGVGKTTLAKEL----SKRLGFGDNVR----DLALENGLVLGDDPETRESKRLDED---KLDRLLDLL------E 64

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488949178   89 TQNALDNGKIVVFDIDVQGFKIARkkmADKIVSVFITTkNKDELKKRLIKRNTDTIIQLEKR 150
Cdd:pfam13238  65 ENAALEEGGNLIIDGHLAELEPER---AKDLVGIVLRA-SPEELLERLEKRGYEEAKIKENE 122
AAA_22 pfam13401
AAA domain;
4-30 9.91e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 35.01  E-value: 9.91e-03
                          10        20
                  ....*....|....*....|....*..
gi 488949178    4 QGFVLLIsGPSGAGKSTLLKKLFDEFE 30
Cdd:pfam13401   5 AGILVLT-GESGTGKTTLLRRLLEQLP 30
 
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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