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Conserved domains on  [gi|2462508304|ref|XP_054192151|]
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guanylate kinase isoform X2 [Homo sapiens]

Protein Classification

guanylate kinase( domain architecture ID 10799078)

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
guanyl_kin TIGR03263
guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP ...
 71-253 4.94e-95

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: 276.68  E-value: 4.94e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508304  71 RPVVLSGPSGAGKSTLLKRLLQEHSGIFgFSVSHTTRNPRPGEENGKDYYFVTREVMQRDIAAGDFIEHAEFSGNLYGTS 150
Cdd:TIGR03263   1 LLIVISGPSGAGKSTLVKALLEEDPNLK-FSISATTRKPRPGEVDGVDYFFVSKEEFEEMIKAGEFLEWAEVHGNYYGTP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508304 151 KVAVQAVQAMNRICVLDVDLQGVRNIKATDLRPIYISVQPPSLHVLEQRLRQRNTETEESLVKRLAAAQADMESSKEpgl 230
Cdd:TIGR03263  80 KSPVEEALAAGKDVLLEIDVQGARQVKKKFPDAVSIFILPPSLEELERRLRKRGTDSEEVIERRLAKAKKEIAHADE--- 156

                         170       180
                  ....*....|....*....|...
gi 2462508304 231 FDVVIINDSLDQAYAELKEALSE 253
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 ...
 71-253 4.94e-95

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: 276.68  E-value: 4.94e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508304  71 RPVVLSGPSGAGKSTLLKRLLQEHSGIFgFSVSHTTRNPRPGEENGKDYYFVTREVMQRDIAAGDFIEHAEFSGNLYGTS 150
Cdd:TIGR03263   1 LLIVISGPSGAGKSTLVKALLEEDPNLK-FSISATTRKPRPGEVDGVDYFFVSKEEFEEMIKAGEFLEWAEVHGNYYGTP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508304 151 KVAVQAVQAMNRICVLDVDLQGVRNIKATDLRPIYISVQPPSLHVLEQRLRQRNTETEESLVKRLAAAQADMESSKEpgl 230
Cdd:TIGR03263  80 KSPVEEALAAGKDVLLEIDVQGARQVKKKFPDAVSIFILPPSLEELERRLRKRGTDSEEVIERRLAKAKKEIAHADE--- 156

                         170       180
                  ....*....|....*....|...
gi 2462508304 231 FDVVIINDSLDQAYAELKEALSE 253
Cdd:TIGR03263 157 FDYVIVNDDLEKAVEELKSIILA 179
Guanylate_kin pfam00625
Guanylate kinase;
69-254 3.93e-87

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 256.92  E-value: 3.93e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508304  69 GPRPVVLSGPSGAGKSTLLKRLLQEHSGIFGFSVSHTTRNPRPGEENGKDYYFVTREVMQRDIAAGDFIEHAEFSGNLYG 148
Cdd:pfam00625   1 SRRPVVLSGPSGVGKSHIKKALLSEYPDKFGYSVPHTTRPPRKGEVDGKDYYFVSKEEMERDISANEFLEYAQFSGNMYG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508304 149 TSKVAVQAVQAMNRICVLDVDLQGVRNIKATDLRPIYISVQPPSLHVLEQRLRQRNTETEESLVKRLAAAQADMESSKep 228
Cdd:pfam00625  81 TSVETIEQIHEQGKIVILDVDPQGVKQLRKAELSPISVFIKPPSLKVLQRRLKGRGKEQEEKINKRMAAAEQEFQHYE-- 158

                         170       180
                  ....*....|....*....|....*.
gi 2462508304 229 glFDVVIINDSLDQAYAELKEALSEE 254
Cdd:pfam00625 159 --FDVIIVNDDLEEAYKKLKEALEAE 182
Gmk COG0194
Guanylate kinase [Nucleotide transport and metabolism];
73-260 8.97e-82

Guanylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 439964  Cd Length: 190  Bit Score: 243.44  E-value: 8.97e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508304  73 VVLSGPSGAGKSTLLKRLLQEHSGIfGFSVSHTTRNPRPGEENGKDYYFVTREVMQRDIAAGDFIEHAEFSGNLYGTSKV 152
Cdd:COG0194     5 IVLSGPSGAGKTTLVKALLERDPDL-RFSVSATTRPPRPGEVDGVDYHFVSREEFERMIENGEFLEWAEVHGNYYGTPKA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508304 153 AVQAVQAMNRICVLDVDLQGVRNIKAT--DLRPIYIsvQPPSLHVLEQRLRQRNTETEESLVKRLAAAQADMESSKEpgl 230
Cdd:COG0194    84 EVEEALAAGKDVLLEIDVQGARQVKKKfpDAVSIFI--LPPSLEELERRLRGRGTDSEEVIERRLAKAREELAHADE--- 158

                         170       180       190
                  ....*....|....*....|....*....|
gi 2462508304 231 FDVVIINDSLDQAYAELKEALSEEIKKAQR 260
Cdd:COG0194   159 FDYVVVNDDLDRAVEELKAIIRAERLRRER 188
gmk PRK00300
guanylate kinase; Provisional
 73-260 1.22e-78

guanylate kinase; Provisional


Pssm-ID: 234719  Cd Length: 205  Bit Score: 236.14  E-value: 1.22e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508304  73 VVLSGPSGAGKSTLLKRLLQEHSGIFgFSVSHTTRNPRPGEENGKDYYFVTREVMQRDIAAGDFIEHAEFSGNLYGTSKV 152
Cdd:PRK00300    8 IVLSGPSGAGKSTLVKALLERDPNLQ-LSVSATTRAPRPGEVDGVDYFFVSKEEFEEMIENGEFLEWAEVFGNYYGTPRS 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508304 153 AVQAVQAMNRICVLDVDLQGVRNIKATDLRPIYISVQPPSLHVLEQRLRQRNTETEESLVKRLAAAQADMESSKEpglFD 232
Cdd:PRK00300   87 PVEEALAAGKDVLLEIDWQGARQVKKKMPDAVSIFILPPSLEELERRLRGRGTDSEEVIARRLAKAREEIAHASE---YD 163

                         170       180
                  ....*....|....*....|....*...
gi 2462508304 233 VVIINDSLDQAYAELKEALSEEIKKAQR 260
Cdd:PRK00300  164 YVIVNDDLDTALEELKAIIRAERLRRSR 191
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
 79-255 8.90e-78

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: 232.95  E-value: 8.90e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508304   79 SGAGKSTLLKRLLQEHSGIFGFSVSHTTRNPRPGEENGKDYYFVTREVMQRDIAAGDFIEHAEFSGNLYGTSKVAVQAVQ 158
Cdd:smart00072   1 SGVGKGTLLAELIQEIPDAFERVVSHTTRPPRPGEVNGVDYHFVSKEEFEDDIKSGLFLEWGEYEGNYYGTSKETIRQVA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508304  159 AMNRICVLDVDLQGVRNIKATDLRPIYISVQPPSLHVLEQRLRQRNTETEESLVKRLAAAQADMessKEPGLFDVVIIND 238
Cdd:smart00072  81 EKGKHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEELERRLRQRGTETSERIQKRLAAAQKEA---QEYHLFDYVIVND 157

                          170
                   ....*....|....*..
gi 2462508304  239 SLDQAYAELKEALSEEI 255
Cdd:smart00072 158 DLEDAYEELKEILEAEQ 174
GMPK cd00071
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ...
 72-248 4.02e-73

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: 219.71  E-value: 4.02e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508304  72 PVVLSGPSGAGKSTLLKRLLQEHSGIFGFSVSHTTRNPRPGEENGKDYYFVTREVMQRDIAAGDFIEHAEFSGNLYGTSK 151
Cdd:cd00071     1 LIVLSGPSGVGKSTLLKRLLEEFDPNFGFSVSHTTRKPRPGEVDGVDYHFVSKEEFERLIENGEFLEWAEFHGNYYGTSK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508304 152 VAVQAVQAMNRICVLDVDLQGVRNIKATDLRPIYISVQPPslhvleqrlrqrnteteeslvkrlaaaqadmesskepglf 231
Cdd:cd00071    81 AAVEEALAEGKIVILEIDVQGARQVKKSYPDAVSIFILPP---------------------------------------- 120

                         170
                  ....*....|....*..
gi 2462508304 232 DVVIINDSLDQAYAELK 248
Cdd:cd00071   121 DYVIVNDDLEKAYEELK 137
 
Name Accession Description Interval E-value
guanyl_kin TIGR03263
guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP ...
 71-253 4.94e-95

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: 276.68  E-value: 4.94e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508304  71 RPVVLSGPSGAGKSTLLKRLLQEHSGIFgFSVSHTTRNPRPGEENGKDYYFVTREVMQRDIAAGDFIEHAEFSGNLYGTS 150
Cdd:TIGR03263   1 LLIVISGPSGAGKSTLVKALLEEDPNLK-FSISATTRKPRPGEVDGVDYFFVSKEEFEEMIKAGEFLEWAEVHGNYYGTP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508304 151 KVAVQAVQAMNRICVLDVDLQGVRNIKATDLRPIYISVQPPSLHVLEQRLRQRNTETEESLVKRLAAAQADMESSKEpgl 230
Cdd:TIGR03263  80 KSPVEEALAAGKDVLLEIDVQGARQVKKKFPDAVSIFILPPSLEELERRLRKRGTDSEEVIERRLAKAKKEIAHADE--- 156

                         170       180
                  ....*....|....*....|...
gi 2462508304 231 FDVVIINDSLDQAYAELKEALSE 253
Cdd:TIGR03263 157 FDYVIVNDDLEKAVEELKSIILA 179
Guanylate_kin pfam00625
Guanylate kinase;
69-254 3.93e-87

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 256.92  E-value: 3.93e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508304  69 GPRPVVLSGPSGAGKSTLLKRLLQEHSGIFGFSVSHTTRNPRPGEENGKDYYFVTREVMQRDIAAGDFIEHAEFSGNLYG 148
Cdd:pfam00625   1 SRRPVVLSGPSGVGKSHIKKALLSEYPDKFGYSVPHTTRPPRKGEVDGKDYYFVSKEEMERDISANEFLEYAQFSGNMYG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508304 149 TSKVAVQAVQAMNRICVLDVDLQGVRNIKATDLRPIYISVQPPSLHVLEQRLRQRNTETEESLVKRLAAAQADMESSKep 228
Cdd:pfam00625  81 TSVETIEQIHEQGKIVILDVDPQGVKQLRKAELSPISVFIKPPSLKVLQRRLKGRGKEQEEKINKRMAAAEQEFQHYE-- 158

                         170       180
                  ....*....|....*....|....*.
gi 2462508304 229 glFDVVIINDSLDQAYAELKEALSEE 254
Cdd:pfam00625 159 --FDVIIVNDDLEEAYKKLKEALEAE 182
Gmk COG0194
Guanylate kinase [Nucleotide transport and metabolism];
73-260 8.97e-82

Guanylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 439964  Cd Length: 190  Bit Score: 243.44  E-value: 8.97e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508304  73 VVLSGPSGAGKSTLLKRLLQEHSGIfGFSVSHTTRNPRPGEENGKDYYFVTREVMQRDIAAGDFIEHAEFSGNLYGTSKV 152
Cdd:COG0194     5 IVLSGPSGAGKTTLVKALLERDPDL-RFSVSATTRPPRPGEVDGVDYHFVSREEFERMIENGEFLEWAEVHGNYYGTPKA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508304 153 AVQAVQAMNRICVLDVDLQGVRNIKAT--DLRPIYIsvQPPSLHVLEQRLRQRNTETEESLVKRLAAAQADMESSKEpgl 230
Cdd:COG0194    84 EVEEALAAGKDVLLEIDVQGARQVKKKfpDAVSIFI--LPPSLEELERRLRGRGTDSEEVIERRLAKAREELAHADE--- 158

                         170       180       190
                  ....*....|....*....|....*....|
gi 2462508304 231 FDVVIINDSLDQAYAELKEALSEEIKKAQR 260
Cdd:COG0194   159 FDYVVVNDDLDRAVEELKAIIRAERLRRER 188
gmk PRK00300
guanylate kinase; Provisional
 73-260 1.22e-78

guanylate kinase; Provisional


Pssm-ID: 234719  Cd Length: 205  Bit Score: 236.14  E-value: 1.22e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508304  73 VVLSGPSGAGKSTLLKRLLQEHSGIFgFSVSHTTRNPRPGEENGKDYYFVTREVMQRDIAAGDFIEHAEFSGNLYGTSKV 152
Cdd:PRK00300    8 IVLSGPSGAGKSTLVKALLERDPNLQ-LSVSATTRAPRPGEVDGVDYFFVSKEEFEEMIENGEFLEWAEVFGNYYGTPRS 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508304 153 AVQAVQAMNRICVLDVDLQGVRNIKATDLRPIYISVQPPSLHVLEQRLRQRNTETEESLVKRLAAAQADMESSKEpglFD 232
Cdd:PRK00300   87 PVEEALAAGKDVLLEIDWQGARQVKKKMPDAVSIFILPPSLEELERRLRGRGTDSEEVIARRLAKAREEIAHASE---YD 163

                         170       180
                  ....*....|....*....|....*...
gi 2462508304 233 VVIINDSLDQAYAELKEALSEEIKKAQR 260
Cdd:PRK00300  164 YVIVNDDLDTALEELKAIIRAERLRRSR 191
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
 79-255 8.90e-78

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: 232.95  E-value: 8.90e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508304   79 SGAGKSTLLKRLLQEHSGIFGFSVSHTTRNPRPGEENGKDYYFVTREVMQRDIAAGDFIEHAEFSGNLYGTSKVAVQAVQ 158
Cdd:smart00072   1 SGVGKGTLLAELIQEIPDAFERVVSHTTRPPRPGEVNGVDYHFVSKEEFEDDIKSGLFLEWGEYEGNYYGTSKETIRQVA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508304  159 AMNRICVLDVDLQGVRNIKATDLRPIYISVQPPSLHVLEQRLRQRNTETEESLVKRLAAAQADMessKEPGLFDVVIIND 238
Cdd:smart00072  81 EKGKHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEELERRLRQRGTETSERIQKRLAAAQKEA---QEYHLFDYVIVND 157

                          170
                   ....*....|....*..
gi 2462508304  239 SLDQAYAELKEALSEEI 255
Cdd:smart00072 158 DLEDAYEELKEILEAEQ 174
GMPK cd00071
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ...
 72-248 4.02e-73

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: 219.71  E-value: 4.02e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508304  72 PVVLSGPSGAGKSTLLKRLLQEHSGIFGFSVSHTTRNPRPGEENGKDYYFVTREVMQRDIAAGDFIEHAEFSGNLYGTSK 151
Cdd:cd00071     1 LIVLSGPSGVGKSTLLKRLLEEFDPNFGFSVSHTTRKPRPGEVDGVDYHFVSKEEFERLIENGEFLEWAEFHGNYYGTSK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508304 152 VAVQAVQAMNRICVLDVDLQGVRNIKATDLRPIYISVQPPslhvleqrlrqrnteteeslvkrlaaaqadmesskepglf 231
Cdd:cd00071    81 AAVEEALAEGKIVILEIDVQGARQVKKSYPDAVSIFILPP---------------------------------------- 120

                         170
                  ....*....|....*..
gi 2462508304 232 DVVIINDSLDQAYAELK 248
Cdd:cd00071   121 DYVIVNDDLEKAYEELK 137
PLN02772 PLN02772
guanylate kinase
 69-252 5.14e-69

guanylate kinase


Pssm-ID: 215414 [Multi-domain]  Cd Length: 398  Bit Score: 218.17  E-value: 5.14e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508304  69 GPRPVVLSGPSGAGKSTLLKRLLQEHSGIFGFSVSHTTRNPRPGEENGKDYYFVTREVMQRDIAAGDFIEHAEFSGNLYG 148
Cdd:PLN02772  134 AEKPIVISGPSGVGKGTLISMLMKEFPSMFGFSVSHTTRAPREMEKDGVHYHFTERSVMEKEIKDGKFLEFASVHGNLYG 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508304 149 TSKVAVQAVQAMNRICVLDVDLQGVRNIKATDLRPIYISVQPPSLHVLEQRLRQRNTETEESLVKRLAAAQADMESSKEP 228
Cdd:PLN02772  214 TSIEAVEVVTDSGKRCILDIDVQGARSVRASSLEAIFIFICPPSMEELEKRLRARGTETEEQIQKRLRNAEAELEQGKSS 293

                         170       180
                  ....*....|....*....|....
gi 2462508304 229 GLFDVVIINDSLDQAYAELKEALS 252
Cdd:PLN02772  294 GIFDHILYNDNLEECYKNLKKLLG 317
gmk PRK14737
guanylate kinase; Provisional
 67-251 4.30e-49

guanylate kinase; Provisional


Pssm-ID: 173199  Cd Length: 186  Bit Score: 160.16  E-value: 4.30e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508304  67 MSGPRPVVLSGPSGAGKSTLLKRLLQEHSGIFgFSVSHTTRNPRPGEENGKDYYFVTREVMQRDIAAGDFIEHAEFSGNL 146
Cdd:PRK14737    1 KASPKLFIISSVAGGGKSTIIQALLEEHPDFL-FSISCTTRAPRPGDEEGKTYFFLTIEEFKKGIADGEFLEWAEVHDNY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508304 147 YGTSKVAVQAVQAMNRICVLDVDLQGVRNIKatDLRP---IYISVQPPSLHVLEQRLRQRNTETEESLVKRLAAAQADME 223
Cdd:PRK14737   80 YGTPKAFIEDAFKEGRSAIMDIDVQGAKIIK--EKFPeriVTIFIEPPSEEEWEERLIHRGTDSEESIEKRIENGIIELD 157

                         170       180
                  ....*....|....*....|....*...
gi 2462508304 224 SSKEpglFDVVIINDSLDQAYAELKEAL 251
Cdd:PRK14737  158 EANE---FDYKIINDDLEDAIADLEAII 182
gmk PRK14738
guanylate kinase; Provisional
 70-254 5.78e-45

guanylate kinase; Provisional


Pssm-ID: 237809  Cd Length: 206  Bit Score: 150.27  E-value: 5.78e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508304  70 PRPVVLSGPSGAGKSTLLKRLLQEHSGiFGFSVSHTTRNPRPGEENGKDYYFVTREVMQRDIAAGDFIEHAEFSGNLYGT 149
Cdd:PRK14738   13 PLLVVISGPSGVGKDAVLARMRERKLP-FHFVVTATTRPKRPGEIDGVDYHFVTPEEFREMISQNELLEWAEVYGNYYGV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508304 150 SKVAVQAVQAMNRICVLDVDLQGVRNIKATDLRPIYISVQPPSLHVLEQRLRQRNTETEESLVKRLAAAQADMESSKEpg 229
Cdd:PRK14738   92 PKAPVRQALASGRDVIVKVDVQGAASIKRLVPEAVFIFLAPPSMDELTRRLELRRTESPEELERRLATAPLELEQLPE-- 169

                         170       180
                  ....*....|....*....|....*..
gi 2462508304 230 lFDVVIIN--DSLDQAYAELKEALSEE 254
Cdd:PRK14738  170 -FDYVVVNpeDRLDEAVAQIMAIISAE 195
PhnN COG3709
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
67-259 5.52e-16

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


Pssm-ID: 442923  Cd Length: 188  Bit Score: 73.69  E-value: 5.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508304  67 MSGP-RPVVLSGPSGAGKSTLLKRLLQEHSGIFGFSVSH--TTRNPRPGEENgkdYYFVTREVMQRDIAAGDFIEHAEFS 143
Cdd:COG3709     1 MSGPgRLIYVVGPSGAGKDSLLAAARARLAADPRLVFARryITRPADAGGED---HDALSEAEFARRAAAGAFALHWQAH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508304 144 GNLYGTSkVAVQAVQAMNRICVLDVD---LQGVRNiKATDLRPIYISVQPpslHVLEQRLRQRNTETEESLVKRLAAAQA 220
Cdd:COG3709    78 GLRYGIP-AEIDAWLAAGRDVVVNGSravLPQARA-RYPRLLVVLITASP---EVLAQRLAARGRESAEEIEARLARAAE 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2462508304 221 DMesskEPGLFDVVIIND-SLDQAYAELKEALSEEIKKAQ 259
Cdd:COG3709   153 FL----PDGPDVLVIDNDgPLEDAGARLLALLRAARARAA 188
phosphon_PhnN TIGR02322
phosphonate metabolism protein/1,5-bisphosphokinase (PRPP-forming) PhnN; Members of this ...
 71-254 6.45e-10

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: 56.99  E-value: 6.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508304  71 RPVVLSGPSGAGKSTLLKRLLQEHSGIFGFSVSHTTRNpRPGEENGKDYYFVTREVMQRDIAAGDFIEHAEFSGNLYGTS 150
Cdd:TIGR02322   2 RLIYVVGPSGAGKDTLLDYARARLAGDPRVHFVRRVIT-RPASAGGENHIALSTEEFDHREDGGAFALSWQAHGLSYGIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508304 151 KVAVQAVQAMNricvlDVDLQGVRNIKAT------DLRPIYISVQPpslHVLEQRLRQRNTETEESLVKRLAAAQADMES 224
Cdd:TIGR02322  81 IEIDQWLEAGD-----VVVVNGSRAVLPEarqrypNLLVVNITASP---DVLAQRLAARGRESREEIEERLARSARFAAA 152

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2462508304 225 SkepglFDVVIINDS--LDQAYAELKEALSEE 254
Cdd:TIGR02322 153 P-----ADVTTIDNSgsLEVAGETLLRLLRKE 179
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
73-247 4.89e-06

Predicted kinase, contains AAA domain [General function prediction only];


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 45.67  E-value: 4.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508304  73 VVLSGPSGAGKSTLLKRLLQEHSGI-----------FGFSVSHTTRNPRPGEEngkdyyfvTREVMQRdiAAGDFIEHae 141
Cdd:COG0645     2 ILVCGLPGSGKSTLARALAERLGAVrlrsdvvrkrlFGAGLAPLERSPEATAR--------TYARLLA--LARELLAA-- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508304 142 fsgnlyGTSkvavqavqamnriCVLD------VDLQGVRNI-KATDLRPIYISVQPPsLHVLEQRLRQRNTETEESL--V 212
Cdd:COG0645    70 ------GRS-------------VILDatflrrAQREAFRALaEEAGAPFVLIWLDAP-EEVLRERLEARNAEGGDSDatW 129

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2462508304 213 KRLAAAQADMESSKEPGLFDVVIINDSLDQAYAEL 247
Cdd:COG0645   130 EVLERQLAFEEPLTEDEGFLLVVDTSGLEEALAAL 164
PRK10078 PRK10078
ribose 1,5-bisphosphokinase; Provisional
 70-219 1.35e-05

ribose 1,5-bisphosphokinase; Provisional


Pssm-ID: 236648  Cd Length: 186  Bit Score: 44.74  E-value: 1.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508304  70 PRPVVLSGPSGAGKSTLLKRLLQ-EHSGIFgfsVSH--TTRNPRPGEENG---KDYYFVTREvmQRDIAAGDFIEHA--- 140
Cdd:PRK10078    2 GKLIWLMGPSGSGKDSLLAALRQrEQTQLL---VAHryITRPASAGSENHialSEQEFFTRA--GQNLFALSWHANGlyy 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508304 141 ----EFSGNLYGTSKVAVQAVQAMnricvldvdLQGVRNIKATDLRPIYISVQPPslhVLEQRLRQRNTETEESLVKRLA 216
Cdd:PRK10078   77 gvgiEIDLWLHAGFDVLVNGSRAH---------LPQARARYQSALLPVCLQVSPE---ILRQRLENRGRENASEINARLA 144


                  ...
gi 2462508304 217 AAQ 219
Cdd:PRK10078  145 RAA 147
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
73-111 3.58e-05

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 43.89  E-value: 3.58e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2462508304  73 VVLSGPSGAGKSTLLK---RLLQEHSG---IFGFSVSHTTRNPRP 111
Cdd:COG2884    31 VFLTGPSGAGKSTLLKllyGEERPTSGqvlVNGQDLSRLKRREIP 75
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 73-108 7.15e-05

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: 42.77  E-value: 7.15e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2462508304  73 VVLSGPSGAGKSTLLKRLLQEHSGIFGfSVS-------HTTRN 108
Cdd:cd01854    88 SVLVGQSGVGKSTLLNALLPELVLATG-EISeklgrgrHTTTH 129
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
73-96 7.29e-05

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 42.50  E-value: 7.29e-05
                          10        20
                  ....*....|....*....|....*..
gi 2462508304  73 VVLSGPSGAGKSTLLK---RLLQEHSG 96
Cdd:COG4619    29 VAITGPSGSGKSTLLRalaDLDPPTSG 55
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
 73-88 3.61e-04

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: 40.88  E-value: 3.61e-04
                          10
                  ....*....|....*.
gi 2462508304  73 VVLSGPSGAGKSTLLK 88
Cdd:COG4778    40 VALTGPSGAGKSTLLK 55
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
 73-108 4.18e-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: 40.22  E-value: 4.18e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2462508304  73 VVLSGPSGAGKSTLLKRLLQEHSGIFGfSVS-------HTTRN 108
Cdd:pfam03193 109 TVLAGQSGVGKSTLLNALLPELDLRTG-EISeklgrgrHTTTH 150
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 73-122 4.74e-04

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: 38.75  E-value: 4.74e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462508304  73 VVLSGPSGAGKSTLLKRLLQEHSgifgfSVSH---TTRNPRPG--EENGKDYYFV 122
Cdd:pfam01926   2 VALVGRPNVGKSTLINALTGAKA-----IVSDypgTTRDPNEGrlELKGKQIILV 51
COG4639 COG4639
Predicted kinase [General function prediction only];
73-93 5.64e-04

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 39.04  E-value: 5.64e-04
                          10        20
                  ....*....|....*....|.
gi 2462508304  73 VVLSGPSGAGKSTLLKRLLQE 93
Cdd:COG4639     5 VVLIGLPGSGKSTFARRLFAP 25
TIGR00152 TIGR00152
dephospho-CoA kinase; This model produces scores in the range of 0-25 bits against adenylate, ...
 73-253 5.76e-04

dephospho-CoA kinase; This model produces scores in the range of 0-25 bits against adenylate, guanylate, uridine, and thymidylate kinases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]


Pssm-ID: 272931  Cd Length: 190  Bit Score: 39.68  E-value: 5.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508304  73 VVLSGPSGAGKSTLLKRLLQEhsgiFGFSVSHTTRNPRPGEENGKDYYFvtrEVMQR---DIAAGDFI-----------E 138
Cdd:TIGR00152   2 IALTGGIGSGKSTVLQYLADK----YHFPVIDADKIAHQVVEPGQPAYH---AIADHfgaNILNQDGEldrkalgnyvfN 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508304 139 HAEFSGNLYGTSKVAVQavQAMNRI----------CVLDVDLqgvrNIKAtDLRPI--YISVQPPSLHVLEQRLRQRNTE 206
Cdd:TIGR00152  75 DPEELKWLNALTHPLIR--QWMKKLiaqfqskyalVLLDVPL----LFEN-NLRSLvdYVIVVERSPELQLERLMQRNDL 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2462508304 207 TEESLVKRLaAAQADMESSKEPGlfDVVIINDSLDQaYAELKEALSE 253
Cdd:TIGR00152 148 TEEEVKKRL-ASQMDIEEKLARI--DTVIDNSGPAT-LADLVKQLEE 190
AAA_18 pfam13238
AAA domain;
73-207 8.31e-04

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 38.56  E-value: 8.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508304  73 VVLSGPSGAGKSTLLKRlLQEHSGiFGFSVSHTTRNPRPGEENGKDYYFVTREVMQRDIAAGDFIEhaefsgnlygtskv 152
Cdd:pfam13238   1 ILITGTPGVGKTTLAKE-LSKRLG-FGDNVRDLALENGLVLGDDPETRESKRLDEDKLDRLLDLLE-------------- 64

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462508304 153 aVQAVQAMNRICVLDVDLQGVRNIKATDLRPIYISVqppSLHVLEQRLRQRNTET 207
Cdd:pfam13238  65 -ENAALEEGGNLIIDGHLAELEPERAKDLVGIVLRA---SPEELLERLEKRGYEE 115
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 77-109 9.28e-04

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: 38.98  E-value: 9.28e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2462508304  77 GPSGAGKSTLLKRLLQEHSGIFGfSVSHTTRNP 109
Cdd:cd00882     4 GRGGVGKSSLLNALLGGEVGEVS-DVPGTTRDP 35
AAA_22 pfam13401
AAA domain;
67-94 1.02e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 38.09  E-value: 1.02e-03
                          10        20
                  ....*....|....*....|....*...
gi 2462508304  67 MSGPRPVVLSGPSGAGKSTLLKRLLQEH 94
Cdd:pfam13401   2 RFGAGILVLTGESGTGKTTLLRRLLEQL 29
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
 73-96 1.05e-03

ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). 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: 213195 [Multi-domain]  Cd Length: 171  Bit Score: 38.90  E-value: 1.05e-03
                          10        20
                  ....*....|....*....|....*..
gi 2462508304  73 VVLSGPSGAGKSTLLK---RLLQEHSG 96
Cdd:cd03228    31 VAIVGPSGSGKSTLLKlllRLYDPTSG 57
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 70-133 1.05e-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: 38.51  E-value: 1.05e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462508304   70 PRPVVLSGPSGAGKSTLLKRLLQE----HSGIFGFSVSHT---TRNPRPGEENGKDYYFVTREVMQRDIAA 133
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARElgppGGGVIYIDGEDIleeVLDQLLLIIVGGKKASGSGELRLRLALA 72
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 77-110 1.08e-03

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: 38.77  E-value: 1.08e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2462508304  77 GPSGAGKSTLLKRLLQEHSGIFGfSVSHTTRNPR 110
Cdd:cd00880     4 GRPNVGKSSLLNALLGQNVGIVS-PIPGTTRDPV 36
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
 73-96 1.47e-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: 39.75  E-value: 1.47e-03
                          10        20
                  ....*....|....*....|....*..
gi 2462508304  73 VVLSGPSGAGKSTLLK---RLLQEHSG 96
Cdd:COG4987   364 VAIVGPSGSGKSTLLAlllRFLDPQSG 390
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
 73-106 1.52e-03

First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.


Pssm-ID: 213192 [Multi-domain]  Cd Length: 211  Bit Score: 38.60  E-value: 1.52e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2462508304  73 VVLSGPSGAGKSTLLK---RLLQEHSG---IFGFSVSHTT 106
Cdd:cd03225    30 VLIVGPNGSGKSTLLRllnGLLGPTSGevlVDGKDLTKLS 69
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 66-113 2.38e-03

first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. This subfamily also includes the first of the two ATPase domains of NVL (nuclear VCP-like protein) 2, an isoform of NVL mainly present in the nucleolus, which is involved in ribosome biogenesis, in telomerase assembly and the regulation of telomerase activity, and in pre-rRNA processing. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410911 [Multi-domain]  Cd Length: 165  Bit Score: 37.66  E-value: 2.38e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2462508304  66 GMSGPRPVVLSGPSGAGKsTLLKRLLQEHSGIFGFSVS-HTTRNPRPGE 113
Cdd:cd19503    30 GLKPPRGVLLHGPPGTGK-TLLARAVANEAGANFLSISgPSIVSKYLGE 77
COG4185 COG4185
Predicted ABC-type ATPase or kinase [General function prediction only];
67-100 2.38e-03

Predicted ABC-type ATPase or kinase [General function prediction only];


Pssm-ID: 443339  Cd Length: 197  Bit Score: 37.95  E-value: 2.38e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2462508304  67 MSGPRPVVLSGPSGAGKSTLLKRLLQEHSGIFGF 100
Cdd:COG4185     1 MAMPRLYIIAGPNGAGKSTFARTILPEELGGLEF 34
PRK01889 PRK01889
GTPase RsgA; Reviewed
 68-94 2.54e-03

GTPase RsgA; Reviewed


Pssm-ID: 234988 [Multi-domain]  Cd Length: 356  Bit Score: 38.76  E-value: 2.54e-03
                          10        20
                  ....*....|....*....|....*..
gi 2462508304  68 SGPRPVVLSGPSGAGKSTLLKRLLQEH 94
Cdd:PRK01889  193 SGGKTVALLGSSGVGKSTLVNALLGEE 219
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 67-93 2.81e-03

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: 37.90  E-value: 2.81e-03
                          10        20
                  ....*....|....*....|....*...
gi 2462508304  67 MSGPRPVVL-SGPSGAGKSTLLKRLLQE 93
Cdd:COG0572     3 RSGKPRIIGiAGPSGSGKTTFARRLAEQ 30
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
 73-108 2.97e-03

ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.


Pssm-ID: 213229 [Multi-domain]  Cd Length: 213  Bit Score: 37.89  E-value: 2.97e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2462508304  73 VVLSGPSGAGKSTLLK--RLLQEHSG----IFGFSVSHTTRN 108
Cdd:cd03262    29 VVIIGPSGSGKSTLLRciNLLEEPDSgtiiIDGLKLTDDKKN 70
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
 73-96 3.11e-03

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 38.02  E-value: 3.11e-03
                          10        20
                  ....*....|....*....|....
gi 2462508304  73 VVLSGPSGAGKSTLLKRLLQEHSG 96
Cdd:COG2401    59 VLIVGASGSGKSTLLRLLAGALKG 82
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 73-228 3.26e-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: 36.90  E-value: 3.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508304  73 VVLSGPSGAGKSTLLKRLLQEHSGIFgfsVShttrnprpgeengKDYYFVTREVMQRDIAAGDfiehAEFSGNLYGTSKV 152
Cdd:pfam13671   2 ILLVGLPGSGKSTLARRLLEELGAVR---LS-------------SDDERKRLFGEGRPSISYY----TDATDRTYERLHE 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508304 153 AVQAVQAMNRICVLD-----VDLQ-GVRNIKATDLRPIYISVQPPSLHVLEQRLRQRNtETEESLVKRLAAAQADMESSK 226
Cdd:pfam13671  62 LARIALRAGRPVILDatnlrRDERaRLLALAREYGVPVRIVVFEAPEEVLRERLAARA-RAGGDPSDVPEEVLDRQKARF 140


                  ..
gi 2462508304 227 EP 228
Cdd:pfam13671 141 EP 142
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
73-111 3.42e-03

ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 37.81  E-value: 3.42e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2462508304  73 VVLSGPSGAGKSTLLKRL---LQEHSG-IFGFSVSHTTRNP--RP 111
Cdd:COG3840    28 VAILGPSGAGKSTLLNLIagfLPPDSGrILWNGQDLTALPPaeRP 72
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
 67-93 3.87e-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: 37.84  E-value: 3.87e-03
                          10        20
                  ....*....|....*....|....*..
gi 2462508304  67 MSGPRPVVLSGPSGAGKSTLLKRLLQE 93
Cdd:COG3267    40 AQGGGFVVLTGEVGTGKTTLLRRLLER 66
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
 58-111 4.01e-03

Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages


Pssm-ID: 213259 [Multi-domain]  Cd Length: 214  Bit Score: 37.39  E-value: 4.01e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462508304  58 PVETTCLAGMSGPRP----VVLSGPSGAGKSTLLKRLLQEH---SG---IFGFSVSHTTRNPRP 111
Cdd:cd03292    11 PNGTAALDGINISISagefVFLVGPSGAGKSTLLKLIYKEElptSGtirVNGQDVSDLRGRAIP 74
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 70-201 4.64e-03

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 36.74  E-value: 4.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508304  70 PRPVVLSGPSGAGKSTLLKRLLQE--HSGIFGFSVSHTTRNPRPGEENGKDYYFVTREVMQRDIAAGD--FIEHAEFSGN 145
Cdd:cd00009    19 PKNLLLYGPPGTGKTTLARAIANElfRPGAPFLYLNASDLLEGLVVAELFGHFLVRLLFELAEKAKPGvlFIDEIDSLSR 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462508304 146 lygtsKVAVQAVQAMNRICVLDVDLQGVRNIKATDlRPIYISVQPPSLHVLEQRLR 201
Cdd:cd00009    99 -----GAQNALLRVLETLNDLRIDRENVRVIGATN-RPLLGDLDRALYDRLDIRIV 148
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
 65-93 5.58e-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: 36.71  E-value: 5.58e-03
                          10        20
                  ....*....|....*....|....*....
gi 2462508304  65 AGMSGPRPVVLSGPSGAGKSTLLKRLLQE 93
Cdd:pfam13191  19 VRSGRPPSVLLTGEAGTGKTTLLRELLRA 47
NK cd02019
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ...
 73-105 5.81e-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: 34.62  E-value: 5.81e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2462508304  73 VVLSGPSGAGKSTLLKRlLQEHSGIFGFSVSHT 105
Cdd:cd02019     2 IAITGGSGSGKSTVAKK-LAEQLGGRSVVVLDE 33
AAA_14 pfam13173
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 70-94 6.05e-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: 36.03  E-value: 6.05e-03
                          10        20
                  ....*....|....*....|....*
gi 2462508304  70 PRPVVLSGPSGAGKSTLLKRLLQEH 94
Cdd:pfam13173   2 RKILVITGPRQVGKTTLLLQLIKEL 26
COG1373 COG1373
Predicted ATPase, AAA+ superfamily [General function prediction only];
67-98 6.16e-03

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


Pssm-ID: 440984 [Multi-domain]  Cd Length: 405  Bit Score: 37.62  E-value: 6.16e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2462508304  67 MSGPRPVVLSGPSGAGKSTLLKRLLQEHSGIF 98
Cdd:COG1373    17 LDNRKAVVITGPRQVGKTTLLKQLAKELENIL 48
PRK00098 PRK00098
GTPase RsgA; Reviewed
 74-107 6.99e-03

GTPase RsgA; Reviewed


Pssm-ID: 234631 [Multi-domain]  Cd Length: 298  Bit Score: 37.11  E-value: 6.99e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2462508304  74 VLSGPSGAGKSTLLKRLL-------QEHSGIFGfSVSHTTR 107
Cdd:PRK00098  168 VLAGQSGVGKSTLLNALApdlelktGEISEALG-RGKHTTT 207
ATPase_2 pfam01637
ATPase domain predominantly from Archaea; This family contain a conserved P-loop motif that is ...
 64-159 7.09e-03

ATPase domain predominantly from Archaea; This family contain a conserved P-loop motif that is involved in binding ATP. There are eukaryote members as well as archaeal members in this family.


Pssm-ID: 376582 [Multi-domain]  Cd Length: 222  Bit Score: 36.91  E-value: 7.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508304  64 LAGMSGPRPVVLSGPSGAGKSTLLKRLLQEHSGiFGFSVSHTTrnprPGEENGKDYYFVTREVMQRDIAAGDFIEHAEFs 143
Cdd:pfam01637  14 WAERGPNLIYVIYGPEGCGKTALLRESIENLLD-LGYYVIYYD----PLRRYFISKLDRFEEVRRLAEALGIAVPKAEL- 87

                          90
                  ....*....|....*.
gi 2462508304 144 gnlyGTSKVAVQAVQA 159
Cdd:pfam01637  88 ----EESKLAFLAIEL 99
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
 73-91 7.94e-03

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


Pssm-ID: 444012 [Multi-domain]  Cd Length: 563  Bit Score: 37.43  E-value: 7.94e-03
                          10
                  ....*....|....*....
gi 2462508304  73 VVLSGPSGAGKSTLLKRLL 91
Cdd:COG4988   366 VALVGPSGAGKSTLLNLLL 384
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
 73-88 8.34e-03

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 36.97  E-value: 8.34e-03
                          10
                  ....*....|....*.
gi 2462508304  73 VVLSGPSGAGKSTLLK 88
Cdd:COG3839    32 LVLLGPSGCGKSTLLR 47
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
 73-90 8.36e-03

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 36.92  E-value: 8.36e-03
                          10
                  ....*....|....*...
gi 2462508304  73 VVLSGPSGAGKSTLLKRL 90
Cdd:PRK11124   31 LVLLGPSGAGKSSLLRVL 48
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 73-111 8.65e-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: 36.07  E-value: 8.65e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2462508304  73 VVLSGPSGAGKSTLLK---RLLQEHSGIFGFSVSHTTRNPRP 111
Cdd:cd00267    28 VALVGPNGSGKSTLLRaiaGLLKPTSGEILIDGKDIAKLPLE 69
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
 73-110 9.13e-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: 36.51  E-value: 9.13e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2462508304  73 VVLSGPSGAGKSTLLkR---LLQEHSG----IFGFSVSHTTRNPR 110
Cdd:COG1126    30 VVIIGPSGSGKSTLL-RcinLLEEPDSgtitVDGEDLTDSKKDIN 73
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 73-99 9.22e-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: 35.70  E-value: 9.22e-03
                          10        20
                  ....*....|....*....|....*..
gi 2462508304  73 VVLSGPSGAGKSTLLKRLLQEHSGIFG 99
Cdd:pfam00005  14 LALVGPNGAGKSTLLKLIAGLLSPTEG 40
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
73-96 9.99e-03

ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 36.63  E-value: 9.99e-03
                          10        20
                  ....*....|....*....|....*..
gi 2462508304  73 VVLSGPSGAGKSTLLKRL---LQEHSG 96
Cdd:COG4559    30 TAIIGPNGAGKSTLLKLLtgeLTPSSG 56
 
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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