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Conserved domains on  [gi|19111866|ref|NP_595074|]
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guanylate kinase [Schizosaccharomyces pombe]

Protein Classification

guanylate kinase( domain architecture ID 10799078)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
guanyl_kin TIGR03263
guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP ...
 19-201 3.32e-98

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: 282.07  E-value: 3.32e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111866    19 KPVVVFGPSGVGKSTLLKRLLKDHGDkLGFSVSHTTRTPRAGEKDGIDYHFVTKEEFQKLVAEEKFVEWAVFSGNMYGTS 98
Cdd:TIGR03263   1 LLIVISGPSGAGKSTLVKALLEEDPN-LKFSISATTRKPRPGEVDGVDYFFVSKEEFEEMIKAGEFLEWAEVHGNYYGTP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111866    99 IMAIQELEAVNKKAILDIDLQGVLQVKASPIDAQYVFLAPPSIEQLEVRLRGRGTENESAILQRLERARAEIEYSEKpgn 178
Cdd:TIGR03263  80 KSPVEEALAAGKDVLLEIDVQGARQVKKKFPDAVSIFILPPSLEELERRLRKRGTDSEEVIERRLAKAKKEIAHADE--- 156

                         170       180
                  ....*....|....*....|...
gi 19111866   179 FDALIVNDDVEKAYKQLEAICLS 201
Cdd:TIGR03263 157 FDYVIVNDDLEKAVEELKSIILA 179
 
Name Accession Description Interval E-value
guanyl_kin TIGR03263
guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP ...
 19-201 3.32e-98

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: 282.07  E-value: 3.32e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111866    19 KPVVVFGPSGVGKSTLLKRLLKDHGDkLGFSVSHTTRTPRAGEKDGIDYHFVTKEEFQKLVAEEKFVEWAVFSGNMYGTS 98
Cdd:TIGR03263   1 LLIVISGPSGAGKSTLVKALLEEDPN-LKFSISATTRKPRPGEVDGVDYFFVSKEEFEEMIKAGEFLEWAEVHGNYYGTP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111866    99 IMAIQELEAVNKKAILDIDLQGVLQVKASPIDAQYVFLAPPSIEQLEVRLRGRGTENESAILQRLERARAEIEYSEKpgn 178
Cdd:TIGR03263  80 KSPVEEALAAGKDVLLEIDVQGARQVKKKFPDAVSIFILPPSLEELERRLRKRGTDSEEVIERRLAKAKKEIAHADE--- 156

                         170       180
                  ....*....|....*....|...
gi 19111866   179 FDALIVNDDVEKAYKQLEAICLS 201
Cdd:TIGR03263 157 FDYVIVNDDLEKAVEELKSIILA 179
Gmk COG0194
Guanylate kinase [Nucleotide transport and metabolism];
21-198 2.70e-85

Guanylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 439964  Cd Length: 190  Bit Score: 249.99  E-value: 2.70e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111866  21 VVVFGPSGVGKSTLLKRLLKDHGDkLGFSVSHTTRTPRAGEKDGIDYHFVTKEEFQKLVAEEKFVEWAVFSGNMYGTSIM 100
Cdd:COG0194   5 IVLSGPSGAGKTTLVKALLERDPD-LRFSVSATTRPPRPGEVDGVDYHFVSREEFERMIENGEFLEWAEVHGNYYGTPKA 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111866 101 AIQELEAVNKKAILDIDLQGVLQVKASPIDAQYVFLAPPSIEQLEVRLRGRGTENESAILQRLERARAEIEYSEKpgnFD 180
Cdd:COG0194  84 EVEEALAAGKDVLLEIDVQGARQVKKKFPDAVSIFILPPSLEELERRLRGRGTDSEEVIERRLAKAREELAHADE---FD 160

                       170
                ....*....|....*...
gi 19111866 181 ALIVNDDVEKAYKQLEAI 198
Cdd:COG0194 161 YVVVNDDLDRAVEELKAI 178
gmk PRK00300
guanylate kinase; Provisional
 21-198 9.21e-82

guanylate kinase; Provisional


Pssm-ID: 234719  Cd Length: 205  Bit Score: 241.53  E-value: 9.21e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111866   21 VVVFGPSGVGKSTLLKRLLKDHgDKLGFSVSHTTRTPRAGEKDGIDYHFVTKEEFQKLVAEEKFVEWAVFSGNMYGTSIM 100
Cdd:PRK00300   8 IVLSGPSGAGKSTLVKALLERD-PNLQLSVSATTRAPRPGEVDGVDYFFVSKEEFEEMIENGEFLEWAEVFGNYYGTPRS 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111866  101 AIQELEAVNKKAILDIDLQGVLQVKASPIDAQYVFLAPPSIEQLEVRLRGRGTENESAILQRLERARAEIEYSEKpgnFD 180
Cdd:PRK00300  87 PVEEALAAGKDVLLEIDWQGARQVKKKMPDAVSIFILPPSLEELERRLRGRGTDSEEVIARRLAKAREEIAHASE---YD 163

                        170
                 ....*....|....*...
gi 19111866  181 ALIVNDDVEKAYKQLEAI 198
Cdd:PRK00300 164 YVIVNDDLDTALEELKAI 181
GMPK cd00071
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ...
 20-196 9.23e-71

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: 211.24  E-value: 9.23e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111866  20 PVVVFGPSGVGKSTLLKRLLKDHGDKLGFSVSHTTRTPRAGEKDGIDYHFVTKEEFQKLVAEEKFVEWAVFSGNMYGTSI 99
Cdd:cd00071   1 LIVLSGPSGVGKSTLLKRLLEEFDPNFGFSVSHTTRKPRPGEVDGVDYHFVSKEEFERLIENGEFLEWAEFHGNYYGTSK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111866 100 MAIQELEAVNKKAILDIDLQGVLQVKASPIDAQYVFLAPPsieqlevrlrgrgtenesailqrleraraeieysekpgnf 179
Cdd:cd00071  81 AAVEEALAEGKIVILEIDVQGARQVKKSYPDAVSIFILPP---------------------------------------- 120

                       170
                ....*....|....*..
gi 19111866 180 DALIVNDDVEKAYKQLE 196
Cdd:cd00071 121 DYVIVNDDLEKAYEELK 137
Guanylate_kin pfam00625
Guanylate kinase;
19-198 3.10e-68

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 206.46  E-value: 3.10e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111866    19 KPVVVFGPSGVGKSTLLKRLLKDHGDKLGFSVSHTTRTPRAGEKDGIDYHFVTKEEFQKLVAEEKFVEWAVFSGNMYGTS 98
Cdd:pfam00625   3 RPVVLSGPSGVGKSHIKKALLSEYPDKFGYSVPHTTRPPRKGEVDGKDYYFVSKEEMERDISANEFLEYAQFSGNMYGTS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111866    99 IMAIQELEAVNKKAILDIDLQGVLQVKASPIDAQYVFLAPPSIEQLEVRLRGRGTENESAILQRLERARAEIEYSEkpgn 178
Cdd:pfam00625  83 VETIEQIHEQGKIVILDVDPQGVKQLRKAELSPISVFIKPPSLKVLQRRLKGRGKEQEEKINKRMAAAEQEFQHYE---- 158

                         170       180
                  ....*....|....*....|
gi 19111866   179 FDALIVNDDVEKAYKQLEAI 198
Cdd:pfam00625 159 FDVIIVNDDLEEAYKKLKEA 178
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
 27-198 6.14e-65

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: 197.90  E-value: 6.14e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111866     27 SGVGKSTLLKRLLKDHGDKLGFSVSHTTRTPRAGEKDGIDYHFVTKEEFQKLVAEEKFVEWAVFSGNMYGTSIMAIQELE 106
Cdd:smart00072   1 SGVGKGTLLAELIQEIPDAFERVVSHTTRPPRPGEVNGVDYHFVSKEEFEDDIKSGLFLEWGEYEGNYYGTSKETIRQVA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111866    107 AVNKKAILDIDLQGVLQVKASPIDAQYVFLAPPSIEQLEVRLRGRGTENESAILQRLERARAEIeysEKPGNFDALIVND 186
Cdd:smart00072  81 EKGKHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEELERRLRQRGTETSERIQKRLAAAQKEA---QEYHLFDYVIVND 157

                          170
                   ....*....|..
gi 19111866    187 DVEKAYKQLEAI 198
Cdd:smart00072 158 DLEDAYEELKEI 169
 
Name Accession Description Interval E-value
guanyl_kin TIGR03263
guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP ...
 19-201 3.32e-98

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: 282.07  E-value: 3.32e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111866    19 KPVVVFGPSGVGKSTLLKRLLKDHGDkLGFSVSHTTRTPRAGEKDGIDYHFVTKEEFQKLVAEEKFVEWAVFSGNMYGTS 98
Cdd:TIGR03263   1 LLIVISGPSGAGKSTLVKALLEEDPN-LKFSISATTRKPRPGEVDGVDYFFVSKEEFEEMIKAGEFLEWAEVHGNYYGTP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111866    99 IMAIQELEAVNKKAILDIDLQGVLQVKASPIDAQYVFLAPPSIEQLEVRLRGRGTENESAILQRLERARAEIEYSEKpgn 178
Cdd:TIGR03263  80 KSPVEEALAAGKDVLLEIDVQGARQVKKKFPDAVSIFILPPSLEELERRLRKRGTDSEEVIERRLAKAKKEIAHADE--- 156

                         170       180
                  ....*....|....*....|...
gi 19111866   179 FDALIVNDDVEKAYKQLEAICLS 201
Cdd:TIGR03263 157 FDYVIVNDDLEKAVEELKSIILA 179
Gmk COG0194
Guanylate kinase [Nucleotide transport and metabolism];
21-198 2.70e-85

Guanylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 439964  Cd Length: 190  Bit Score: 249.99  E-value: 2.70e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111866  21 VVVFGPSGVGKSTLLKRLLKDHGDkLGFSVSHTTRTPRAGEKDGIDYHFVTKEEFQKLVAEEKFVEWAVFSGNMYGTSIM 100
Cdd:COG0194   5 IVLSGPSGAGKTTLVKALLERDPD-LRFSVSATTRPPRPGEVDGVDYHFVSREEFERMIENGEFLEWAEVHGNYYGTPKA 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111866 101 AIQELEAVNKKAILDIDLQGVLQVKASPIDAQYVFLAPPSIEQLEVRLRGRGTENESAILQRLERARAEIEYSEKpgnFD 180
Cdd:COG0194  84 EVEEALAAGKDVLLEIDVQGARQVKKKFPDAVSIFILPPSLEELERRLRGRGTDSEEVIERRLAKAREELAHADE---FD 160

                       170
                ....*....|....*...
gi 19111866 181 ALIVNDDVEKAYKQLEAI 198
Cdd:COG0194 161 YVVVNDDLDRAVEELKAI 178
gmk PRK00300
guanylate kinase; Provisional
 21-198 9.21e-82

guanylate kinase; Provisional


Pssm-ID: 234719  Cd Length: 205  Bit Score: 241.53  E-value: 9.21e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111866   21 VVVFGPSGVGKSTLLKRLLKDHgDKLGFSVSHTTRTPRAGEKDGIDYHFVTKEEFQKLVAEEKFVEWAVFSGNMYGTSIM 100
Cdd:PRK00300   8 IVLSGPSGAGKSTLVKALLERD-PNLQLSVSATTRAPRPGEVDGVDYFFVSKEEFEEMIENGEFLEWAEVFGNYYGTPRS 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111866  101 AIQELEAVNKKAILDIDLQGVLQVKASPIDAQYVFLAPPSIEQLEVRLRGRGTENESAILQRLERARAEIEYSEKpgnFD 180
Cdd:PRK00300  87 PVEEALAAGKDVLLEIDWQGARQVKKKMPDAVSIFILPPSLEELERRLRGRGTDSEEVIARRLAKAREEIAHASE---YD 163

                        170
                 ....*....|....*...
gi 19111866  181 ALIVNDDVEKAYKQLEAI 198
Cdd:PRK00300 164 YVIVNDDLDTALEELKAI 181
PLN02772 PLN02772
guanylate kinase
 19-196 4.27e-71

guanylate kinase


Pssm-ID: 215414 [Multi-domain]  Cd Length: 398  Bit Score: 220.86  E-value: 4.27e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111866   19 KPVVVFGPSGVGKSTLLKRLLKDHGDKLGFSVSHTTRTPRAGEKDGIDYHFVTKEEFQKLVAEEKFVEWAVFSGNMYGTS 98
Cdd:PLN02772 136 KPIVISGPSGVGKGTLISMLMKEFPSMFGFSVSHTTRAPREMEKDGVHYHFTERSVMEKEIKDGKFLEFASVHGNLYGTS 215

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111866   99 IMAIQELEAVNKKAILDIDLQGVLQVKASPIDAQYVFLAPPSIEQLEVRLRGRGTENESAILQRLERARAEIEYSEKPGN 178
Cdd:PLN02772 216 IEAVEVVTDSGKRCILDIDVQGARSVRASSLEAIFIFICPPSMEELEKRLRARGTETEEQIQKRLRNAEAELEQGKSSGI 295

                        170
                 ....*....|....*...
gi 19111866  179 FDALIVNDDVEKAYKQLE 196
Cdd:PLN02772 296 FDHILYNDNLEECYKNLK 313
GMPK cd00071
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ...
 20-196 9.23e-71

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: 211.24  E-value: 9.23e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111866  20 PVVVFGPSGVGKSTLLKRLLKDHGDKLGFSVSHTTRTPRAGEKDGIDYHFVTKEEFQKLVAEEKFVEWAVFSGNMYGTSI 99
Cdd:cd00071   1 LIVLSGPSGVGKSTLLKRLLEEFDPNFGFSVSHTTRKPRPGEVDGVDYHFVSKEEFERLIENGEFLEWAEFHGNYYGTSK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111866 100 MAIQELEAVNKKAILDIDLQGVLQVKASPIDAQYVFLAPPsieqlevrlrgrgtenesailqrleraraeieysekpgnf 179
Cdd:cd00071  81 AAVEEALAEGKIVILEIDVQGARQVKKSYPDAVSIFILPP---------------------------------------- 120

                       170
                ....*....|....*..
gi 19111866 180 DALIVNDDVEKAYKQLE 196
Cdd:cd00071 121 DYVIVNDDLEKAYEELK 137
Guanylate_kin pfam00625
Guanylate kinase;
19-198 3.10e-68

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 206.46  E-value: 3.10e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111866    19 KPVVVFGPSGVGKSTLLKRLLKDHGDKLGFSVSHTTRTPRAGEKDGIDYHFVTKEEFQKLVAEEKFVEWAVFSGNMYGTS 98
Cdd:pfam00625   3 RPVVLSGPSGVGKSHIKKALLSEYPDKFGYSVPHTTRPPRKGEVDGKDYYFVSKEEMERDISANEFLEYAQFSGNMYGTS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111866    99 IMAIQELEAVNKKAILDIDLQGVLQVKASPIDAQYVFLAPPSIEQLEVRLRGRGTENESAILQRLERARAEIEYSEkpgn 178
Cdd:pfam00625  83 VETIEQIHEQGKIVILDVDPQGVKQLRKAELSPISVFIKPPSLKVLQRRLKGRGKEQEEKINKRMAAAEQEFQHYE---- 158

                         170       180
                  ....*....|....*....|
gi 19111866   179 FDALIVNDDVEKAYKQLEAI 198
Cdd:pfam00625 159 FDVIIVNDDLEEAYKKLKEA 178
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
 27-198 6.14e-65

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: 197.90  E-value: 6.14e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111866     27 SGVGKSTLLKRLLKDHGDKLGFSVSHTTRTPRAGEKDGIDYHFVTKEEFQKLVAEEKFVEWAVFSGNMYGTSIMAIQELE 106
Cdd:smart00072   1 SGVGKGTLLAELIQEIPDAFERVVSHTTRPPRPGEVNGVDYHFVSKEEFEDDIKSGLFLEWGEYEGNYYGTSKETIRQVA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111866    107 AVNKKAILDIDLQGVLQVKASPIDAQYVFLAPPSIEQLEVRLRGRGTENESAILQRLERARAEIeysEKPGNFDALIVND 186
Cdd:smart00072  81 EKGKHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEELERRLRQRGTETSERIQKRLAAAQKEA---QEYHLFDYVIVND 157

                          170
                   ....*....|..
gi 19111866    187 DVEKAYKQLEAI 198
Cdd:smart00072 158 DLEDAYEELKEI 169
gmk PRK14738
guanylate kinase; Provisional
 21-198 8.60e-46

guanylate kinase; Provisional


Pssm-ID: 237809  Cd Length: 206  Bit Score: 150.27  E-value: 8.60e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111866   21 VVVFGPSGVGKSTLLKRLlKDHGDKLGFSVSHTTRTPRAGEKDGIDYHFVTKEEFQKLVAEEKFVEWAVFSGNMYGTSIM 100
Cdd:PRK14738  16 VVISGPSGVGKDAVLARM-RERKLPFHFVVTATTRPKRPGEIDGVDYHFVTPEEFREMISQNELLEWAEVYGNYYGVPKA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111866  101 AIQELEAVNKKAILDIDLQGVLQVKASPIDAQYVFLAPPSIEQLEVRLRGRGTENESAILQRLERARAEIeysEKPGNFD 180
Cdd:PRK14738  95 PVRQALASGRDVIVKVDVQGAASIKRLVPEAVFIFLAPPSMDELTRRLELRRTESPEELERRLATAPLEL---EQLPEFD 171

                        170       180
                 ....*....|....*....|
gi 19111866  181 ALIVN--DDVEKAYKQLEAI 198
Cdd:PRK14738 172 YVVVNpeDRLDEAVAQIMAI 191
gmk PRK14737
guanylate kinase; Provisional
 27-201 2.14e-45

guanylate kinase; Provisional


Pssm-ID: 173199  Cd Length: 186  Bit Score: 148.60  E-value: 2.14e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111866   27 SGVGKSTLLKRLLKDHGDKLgFSVSHTTRTPRAGEKDGIDYHFVTKEEFQKLVAEEKFVEWAVFSGNMYGTSIMAIQELE 106
Cdd:PRK14737  13 AGGGKSTIIQALLEEHPDFL-FSISCTTRAPRPGDEEGKTYFFLTIEEFKKGIADGEFLEWAEVHDNYYGTPKAFIEDAF 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111866  107 AVNKKAILDIDLQGVLQVKAS-PIDAQYVFLAPPSIEQLEVRLRGRGTENESAILQRLERARAEIEysEKPgNFDALIVN 185
Cdd:PRK14737  92 KEGRSAIMDIDVQGAKIIKEKfPERIVTIFIEPPSEEEWEERLIHRGTDSEESIEKRIENGIIELD--EAN-EFDYKIIN 168

                        170
                 ....*....|....*.
gi 19111866  186 DDVEKAYKQLEAICLS 201
Cdd:PRK14737 169 DDLEDAIADLEAIICG 184
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 21-84 2.63e-06

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: 46.24  E-value: 2.63e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111866  21 VVVFGPSGVGKSTLLKRLLKDHGDKLGfSVS-------HTTR---------------TP--RA-----GEKDGIDYHFVt 71
Cdd:cd01854  88 SVLVGQSGVGKSTLLNALLPELVLATG-EISeklgrgrHTTThrelfplpgggliidTPgfRElgllhIDPEELAEYFP- 165

                        90
                ....*....|...
gi 19111866  72 keEFQKLVAEEKF 84
Cdd:cd01854 166 --EFEELAGQCRF 176
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 22-70 1.40e-05

Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 43.60  E-value: 1.40e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 19111866  22 VVFGPSGVGKSTLLKRLLKDHGDKLGfSVSHTTRTPRAGEK----DGIDYHFV 70
Cdd:cd00882   1 VVVGRGGVGKSSLLNALLGGEVGEVS-DVPGTTRDPDVYVKeldkGKVKLVLV 52
RsgA COG1162
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];
21-84 5.38e-05

Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440776 [Multi-domain]  Cd Length: 300  Bit Score: 42.79  E-value: 5.38e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111866  21 VVVF-GPSGVGKSTLLKRLLKD---------HGDKLGfsvSHTTR---------------TPraG---------EKDGID 66
Cdd:COG1162 168 TSVLvGQSGVGKSTLINALLPDadlatgeisEKLGRG---RHTTThaelyplpgggwlidTP--GfrefglwhiEPEELA 242

                        90
                ....*....|....*...
gi 19111866  67 YHFvtkEEFQKLVAEEKF 84
Cdd:COG1162 243 HYF---PEFRELAGQCRF 257
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 21-70 8.59e-05

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: 40.30  E-value: 8.59e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 19111866    21 VVVFGPSGVGKSTLLKRLLKDH---GDKLGfsvshTTRTPRAG--EKDGIDYHFV 70
Cdd:pfam01926   2 VALVGRPNVGKSTLINALTGAKaivSDYPG-----TTRDPNEGrlELKGKQIILV 51
PRK10078 PRK10078
ribose 1,5-bisphosphokinase; Provisional
 25-187 1.09e-04

ribose 1,5-bisphosphokinase; Provisional


Pssm-ID: 236648  Cd Length: 186  Bit Score: 41.27  E-value: 1.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111866   25 GPSGVGKSTLLKRLLKDHGDKLGFSVSHTTRTPRAGEKDGIDyhfVTKEEF-----QKLVAeekfVEWAVfSGNMYGTSI 99
Cdd:PRK10078   9 GPSGSGKDSLLAALRQREQTQLLVAHRYITRPASAGSENHIA---LSEQEFftragQNLFA----LSWHA-NGLYYGVGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111866  100 MaiqeleavnkkaiLDIDLQGVLQV-----KASPIDAQYVF---LAP------PSIeqLEVRLRGRGTENESAILQRLER 165
Cdd:PRK10078  81 E-------------IDLWLHAGFDVlvngsRAHLPQARARYqsaLLPvclqvsPEI--LRQRLENRGRENASEINARLAR 145

                        170       180
                 ....*....|....*....|..
gi 19111866  166 ARaeieySEKPgnFDALIVNDD 187
Cdd:PRK10078 146 AA-----RYQP--QDCHTLNND 160
PRK00098 PRK00098
GTPase RsgA; Reviewed
 5-84 3.41e-04

GTPase RsgA; Reviewed


Pssm-ID: 234631 [Multi-domain]  Cd Length: 298  Bit Score: 40.19  E-value: 3.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111866    5 LSSSVASKLVTLKLKPV------VVFGPSGVGKSTLLKRLL-------KDHGDKLGfSVSHTTR---------------T 56
Cdd:PRK00098 145 LELSAKEGEGLDELKPLlagkvtVLAGQSGVGKSTLLNALApdlelktGEISEALG-RGKHTTThvelydlpgggllidT 223

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 19111866   57 PraGEKdGIDYHFVTKE-------EFQKLVAEEKF 84
Cdd:PRK00098 224 P--GFS-SFGLHDLEAEelehyfpEFRPLSGDCKF 255
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
 21-58 4.01e-04

RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding during viral RNA replication. Members of this family are found in a variety of single stranded RNA viruses.


Pssm-ID: 459992  Cd Length: 102  Bit Score: 38.35  E-value: 4.01e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 19111866    21 VVVFGPSGVGKSTLLKRLLKDHGDKLGFSVSHT-TRTPR 58
Cdd:pfam00910   1 IWLYGPPGCGKSTLAKYLARALLKKLGLPKDSVySRNPD 39
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
 16-56 6.60e-04

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: 38.68  E-value: 6.60e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 19111866    16 LKLKPVVVFGPSGVGKSTLLKRLLKDHGDKLGfSVS-------HTTRT 56
Cdd:pfam03193 104 LKGKTTVLAGQSGVGKSTLLNALLPELDLRTG-EISeklgrgrHTTTH 150
AAA_18 pfam13238
AAA domain;
21-154 9.27e-04

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 37.79  E-value: 9.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111866    21 VVVFGPSGVGKSTLLKRLLKDHGdkLGFSVSHTtrtprAGEKDGIDYhfVTKEEFQKLVAEEKFVEWavfsgnmygtsim 100
Cdd:pfam13238   1 ILITGTPGVGKTTLAKELSKRLG--FGDNVRDL-----ALENGLVLG--DDPETRESKRLDEDKLDR------------- 58

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 19111866   101 AIQELEAVNKKAILD---IDLQGVLQVKASPIDAQYVFL-APPsiEQLEVRLRGRGTE 154
Cdd:pfam13238  59 LLDLLEENAALEEGGnliIDGHLAELEPERAKDLVGIVLrASP--EELLERLEKRGYE 114
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 22-61 9.42e-04

E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.


Pssm-ID: 206646 [Multi-domain]  Cd Length: 161  Bit Score: 38.38  E-value: 9.42e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 19111866  22 VVFGPSGVGKSTLLKRLLkdhGDKLGfSVS---HTTRTPRAGE 61
Cdd:cd00880   1 AIFGRPNVGKSSLLNALL---GQNVG-IVSpipGTTRDPVRKE 39
PRK12289 PRK12289
small ribosomal subunit biogenesis GTPase RsgA;
16-55 1.01e-03

small ribosomal subunit biogenesis GTPase RsgA;


Pssm-ID: 237040 [Multi-domain]  Cd Length: 352  Bit Score: 39.23  E-value: 1.01e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 19111866   16 LKLKPVVVFGPSGVGKSTLLKRLLKDHGDKLGfSVS-------HTTR 55
Cdd:PRK12289 170 LRNKITVVAGPSGVGKSSLINRLIPDVELRVG-KVSgklgrgrHTTR 215
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
 14-39 1.06e-03

ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 38.92  E-value: 1.06e-03
                        10        20
                ....*....|....*....|....*....
gi 19111866  14 VTLKLKP---VVVFGPSGVGKSTLLkRLL 39
Cdd:COG1116  30 VSLTVAAgefVALVGPSGCGKSTLL-RLI 57
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
 14-39 1.18e-03

ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444011 [Multi-domain]  Cd Length: 569  Bit Score: 38.98  E-value: 1.18e-03
                        10        20
                ....*....|....*....|....*....
gi 19111866  14 VTLKLKP---VVVFGPSGVGKSTLLKRLL 39
Cdd:COG4987 354 LSLTLPPgerVAIVGPSGSGKSTLLALLL 382
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
14-36 1.38e-03

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 38.26  E-value: 1.38e-03
                        10        20
                ....*....|....*....|....*.
gi 19111866  14 VTLKLKP---VVVFGPSGVGKSTLLK 36
Cdd:COG4619  19 VSLTLEAgecVAITGPSGSGKSTLLR 44
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 17-82 2.52e-03

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: 36.97  E-value: 2.52e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19111866     17 KLKPVVVFGPSGVGKSTLLKRLLKDHGDKLGFSVSHTTRTPRAGEKDGIDYHFVTKEEFQKLVAEE 82
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELR 66
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
21-41 2.86e-03

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 36.88  E-value: 2.86e-03
                        10        20
                ....*....|....*....|.
gi 19111866  21 VVVFGPSGVGKSTLLKRLLKD 41
Cdd:COG1100   6 IVVVGTGGVGKTSLVNRLVGD 26
AAA_14 pfam13173
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 19-42 3.02e-03

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


Pssm-ID: 463799 [Multi-domain]  Cd Length: 128  Bit Score: 36.41  E-value: 3.02e-03
                          10        20
                  ....*....|....*....|....
gi 19111866    19 KPVVVFGPSGVGKSTLLKRLLKDH 42
Cdd:pfam13173   3 KILVITGPRQVGKTTLLLQLIKEL 26
Roc pfam08477
Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial ...
 21-45 3.07e-03

Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial Rho proteins (Miro-1, and Miro-2) and atypical Rho GTPases. Full-length proteins have a unique domain organization, with tandem GTP-binding domains and two EF hand domains (pfam00036) that may bind calcium. They are also larger than classical small GTPases. It has been proposed that they are involved in mitochondrial homeostasis and apoptosis.


Pssm-ID: 462490 [Multi-domain]  Cd Length: 114  Bit Score: 35.95  E-value: 3.07e-03
                          10        20
                  ....*....|....*....|....*
gi 19111866    21 VVVFGPSGVGKSTLLKRLLKDHGDK 45
Cdd:pfam08477   2 VVLLGDSGVGKTSLLKRFVDDTFDP 26
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 14-36 3.52e-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: 36.47  E-value: 3.52e-03
                          10        20
                  ....*....|....*....|....*.
gi 19111866    14 VTLKLKP---VVVFGPSGVGKSTLLK 36
Cdd:pfam00005   4 VSLTLNPgeiLALVGPNGAGKSTLLK 29
GBP cd01851
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ...
 14-56 4.07e-03

Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), N-terminal domain. Guanylate-binding proteins (GBPs) define a group of proteins that are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. Furthermore, two unique regions around the base and the phosphate-binding areas, the guanine and the phosphate caps, respectively, give the nucleotide-binding site a unique appearance not found in the canonical GTP-binding proteins. The phosphate cap, which constitutes the region analogous to switch I, completely shields the phosphate-binding site from solvent such that a potential GTPase-activating protein (GAP) cannot approach.


Pssm-ID: 206650  Cd Length: 224  Bit Score: 36.92  E-value: 4.07e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 19111866  14 VTLKLKPVVVFGPSGVGKSTLLKRLLkdhGDKLGFSVSHTTRT 56
Cdd:cd01851   3 VGFPVVVVSVFGSQSSGKSFLLNHLF---GTSDGFDVMDTSQQ 42
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
 14-36 7.58e-03

ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 36.13  E-value: 7.58e-03
                        10        20
                ....*....|....*....|....*.
gi 19111866  14 VTLKLKP---VVVFGPSGVGKSTLLK 36
Cdd:COG1126  20 ISLDVEKgevVVIIGPSGSGKSTLLR 45
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 14-36 7.91e-03

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 35.68  E-value: 7.91e-03
                        10        20
                ....*....|....*....|....*.
gi 19111866  14 VTLKLKP---VVVFGPSGVGKSTLLK 36
Cdd:cd00267  18 VSLTLKAgeiVALVGPNGSGKSTLLR 43
Dynamin_N pfam00350
Dynamin family;
21-116 8.28e-03

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 35.67  E-value: 8.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111866    21 VVVFGPSGVGKSTLLKRLLKDhgDKLGFSVSHTTRTP---RAGEKDGIDYHFVTKEEFQKLVAEEKFVEwavfsgnmYGT 97
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGR--DILPRGPGPTTRRPtvlRLGESPGASEGAVKVEYKDGEKKFEDFSE--------LRE 70

                          90
                  ....*....|....*....
gi 19111866    98 SIMAIQELEAVNKKAILDI 116
Cdd:pfam00350  71 EIEKETEKIAGTGKGISSE 89
BMS1 cd01882
Bms1, an essential GTPase, promotes assembly of preribosomal RNA processing complexes; Bms1 is ...
 21-40 8.76e-03

Bms1, an essential GTPase, promotes assembly of preribosomal RNA processing complexes; Bms1 is an essential, evolutionarily conserved, nucleolar protein. Its depletion interferes with processing of the 35S pre-rRNA at sites A0, A1, and A2, and the formation of 40S subunits. Bms1, the putative endonuclease Rc11, and the essential U3 small nucleolar RNA form a stable subcomplex that is believed to control an early step in the formation of the 40S subumit. The C-terminal domain of Bms1 contains a GTPase-activating protein (GAP) that functions intramolecularly. It is believed that Rc11 activates Bms1 by acting as a guanine-nucleotide exchange factor (GEF) to promote GDP/GTP exchange, and that activated (GTP-bound) Bms1 delivers Rc11 to the preribosomes.


Pssm-ID: 206669 [Multi-domain]  Cd Length: 231  Bit Score: 35.78  E-value: 8.76e-03
                        10        20
                ....*....|....*....|
gi 19111866  21 VVVFGPSGVGKSTLLKRLLK 40
Cdd:cd01882  42 VVVVGPPGVGKSTLIRSLIK 61
PRK01889 PRK01889
GTPase RsgA; Reviewed
 19-59 8.90e-03

GTPase RsgA; Reviewed


Pssm-ID: 234988 [Multi-domain]  Cd Length: 356  Bit Score: 36.06  E-value: 8.90e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 19111866   19 KPVVVFGPSGVGKSTLLKRLLKDH---------GDKLGfsvSHTTrTPRA 59
Cdd:PRK01889 196 KTVALLGSSGVGKSTLVNALLGEEvqktgavreDDSKG---RHTT-THRE 241
AAA_22 pfam13401
AAA domain;
21-39 9.26e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 35.01  E-value: 9.26e-03
                          10
                  ....*....|....*....
gi 19111866    21 VVVFGPSGVGKSTLLKRLL 39
Cdd:pfam13401   8 LVLTGESGTGKTTLLRRLL 26
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 21-43 9.65e-03

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: 34.98  E-value: 9.65e-03
                          10        20
                  ....*....|....*....|...
gi 19111866    21 VVVFGPSGVGKSTLLKRLLKDHG 43
Cdd:pfam13671   2 ILLVGLPGSGKSTLARRLLEELG 24
 
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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