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Conserved domains on  [gi|2217262559|ref|NP_001390765|]
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guanylate kinase isoform 3 [Mus musculus]

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 ...
 5-187 5.67e-100

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: 286.70  E-value: 5.67e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262559   5 RPVVLSGPSGAGKSTLLKKLFQEHSSIFgFSVSHTTRNPRPGEEDGKDYYFVTREMMQRDIAAGDFIEHAEFSGNLYGTS 84
Cdd:TIGR03263   1 LLIVISGPSGAGKSTLVKALLEEDPNLK-FSISATTRKPRPGEVDGVDYFFVSKEEFEEMIKAGEFLEWAEVHGNYYGTP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262559  85 KEAVRAVQAMNRICVLDVDLQGVRSIKKTDLCPIYIFVQPPSLDVLEQRLRLRNTETEESLAKRLAAARTDMESSKEpgl 164
Cdd:TIGR03263  80 KSPVEEALAAGKDVLLEIDVQGARQVKKKFPDAVSIFILPPSLEELERRLRKRGTDSEEVIERRLAKAKKEIAHADE--- 156

                         170       180
                  ....*....|....*....|...
gi 2217262559 165 FDLVIINDDLDKAYATLKQALSE 187
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 ...
 5-187 5.67e-100

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: 286.70  E-value: 5.67e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262559   5 RPVVLSGPSGAGKSTLLKKLFQEHSSIFgFSVSHTTRNPRPGEEDGKDYYFVTREMMQRDIAAGDFIEHAEFSGNLYGTS 84
Cdd:TIGR03263   1 LLIVISGPSGAGKSTLVKALLEEDPNLK-FSISATTRKPRPGEVDGVDYFFVSKEEFEEMIKAGEFLEWAEVHGNYYGTP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262559  85 KEAVRAVQAMNRICVLDVDLQGVRSIKKTDLCPIYIFVQPPSLDVLEQRLRLRNTETEESLAKRLAAARTDMESSKEpgl 164
Cdd:TIGR03263  80 KSPVEEALAAGKDVLLEIDVQGARQVKKKFPDAVSIFILPPSLEELERRLRKRGTDSEEVIERRLAKAKKEIAHADE--- 156

                         170       180
                  ....*....|....*....|...
gi 2217262559 165 FDLVIINDDLDKAYATLKQALSE 187
Cdd:TIGR03263 157 FDYVIVNDDLEKAVEELKSIILA 179
Guanylate_kin pfam00625
Guanylate kinase;
3-188 1.69e-90

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 262.70  E-value: 1.69e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262559   3 GPRPVVLSGPSGAGKSTLLKKLFQEHSSIFGFSVSHTTRNPRPGEEDGKDYYFVTREMMQRDIAAGDFIEHAEFSGNLYG 82
Cdd:pfam00625   1 SRRPVVLSGPSGVGKSHIKKALLSEYPDKFGYSVPHTTRPPRKGEVDGKDYYFVSKEEMERDISANEFLEYAQFSGNMYG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262559  83 TSKEAVRAVQAMNRICVLDVDLQGVRSIKKTDLCPIYIFVQPPSLDVLEQRLRLRNTETEESLAKRLAAARTDMESSKep 162
Cdd:pfam00625  81 TSVETIEQIHEQGKIVILDVDPQGVKQLRKAELSPISVFIKPPSLKVLQRRLKGRGKEQEEKINKRMAAAEQEFQHYE-- 158

                         170       180
                  ....*....|....*....|....*.
gi 2217262559 163 glFDLVIINDDLDKAYATLKQALSEE 188
Cdd:pfam00625 159 --FDVIIVNDDLEEAYKKLKEALEAE 182
Gmk COG0194
Guanylate kinase [Nucleotide transport and metabolism];
7-188 6.62e-85

Guanylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 439964  Cd Length: 190  Bit Score: 248.83  E-value: 6.62e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262559   7 VVLSGPSGAGKSTLLKKLFQEHSSIfGFSVSHTTRNPRPGEEDGKDYYFVTREMMQRDIAAGDFIEHAEFSGNLYGTSKE 86
Cdd:COG0194     5 IVLSGPSGAGKTTLVKALLERDPDL-RFSVSATTRPPRPGEVDGVDYHFVSREEFERMIENGEFLEWAEVHGNYYGTPKA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262559  87 AVRAVQAMNRICVLDVDLQGVRSIKKtdLCP--IYIFVQPPSLDVLEQRLRLRNTETEESLAKRLAAARTDMESSKEpgl 164
Cdd:COG0194    84 EVEEALAAGKDVLLEIDVQGARQVKK--KFPdaVSIFILPPSLEELERRLRGRGTDSEEVIERRLAKAREELAHADE--- 158

                         170       180
                  ....*....|....*....|....
gi 2217262559 165 FDLVIINDDLDKAYATLKQALSEE 188
Cdd:COG0194   159 FDYVVVNDDLDRAVEELKAIIRAE 182
gmk PRK00300
guanylate kinase; Provisional
 7-191 3.17e-81

guanylate kinase; Provisional


Pssm-ID: 234719  Cd Length: 205  Bit Score: 239.99  E-value: 3.17e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262559   7 VVLSGPSGAGKSTLLKKLFQEHSSIFgFSVSHTTRNPRPGEEDGKDYYFVTREMMQRDIAAGDFIEHAEFSGNLYGTSKE 86
Cdd:PRK00300    8 IVLSGPSGAGKSTLVKALLERDPNLQ-LSVSATTRAPRPGEVDGVDYFFVSKEEFEEMIENGEFLEWAEVFGNYYGTPRS 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262559  87 AVRAVQAMNRICVLDVDLQGVRSIKKtdLCP--IYIFVQPPSLDVLEQRLRLRNTETEESLAKRLAAARTDMESSKEpgl 164
Cdd:PRK00300   87 PVEEALAAGKDVLLEIDWQGARQVKK--KMPdaVSIFILPPSLEELERRLRGRGTDSEEVIARRLAKAREEIAHASE--- 161

                         170       180
                  ....*....|....*....|....*..
gi 2217262559 165 FDLVIINDDLDKAYATLKQALSEEIKK 191
Cdd:PRK00300  162 YDYVIVNDDLDTALEELKAIIRAERLR 188
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
 13-189 3.50e-79

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: 233.72  E-value: 3.50e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262559   13 SGAGKSTLLKKLFQEHSSIFGFSVSHTTRNPRPGEEDGKDYYFVTREMMQRDIAAGDFIEHAEFSGNLYGTSKEAVRAVQ 92
Cdd:smart00072   1 SGVGKGTLLAELIQEIPDAFERVVSHTTRPPRPGEVNGVDYHFVSKEEFEDDIKSGLFLEWGEYEGNYYGTSKETIRQVA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262559   93 AMNRICVLDVDLQGVRSIKKTDLCPIYIFVQPPSLDVLEQRLRLRNTETEESLAKRLAAARTDMessKEPGLFDLVIIND 172
Cdd:smart00072  81 EKGKHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEELERRLRQRGTETSERIQKRLAAAQKEA---QEYHLFDYVIVND 157

                          170
                   ....*....|....*..
gi 2217262559  173 DLDKAYATLKQALSEEI 189
Cdd:smart00072 158 DLEDAYEELKEILEAEQ 174
GMPK cd00071
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ...
 6-182 2.69e-77

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: 227.42  E-value: 2.69e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262559   6 PVVLSGPSGAGKSTLLKKLFQEHSSIFGFSVSHTTRNPRPGEEDGKDYYFVTREMMQRDIAAGDFIEHAEFSGNLYGTSK 85
Cdd:cd00071     1 LIVLSGPSGVGKSTLLKRLLEEFDPNFGFSVSHTTRKPRPGEVDGVDYHFVSKEEFERLIENGEFLEWAEFHGNYYGTSK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262559  86 EAVRAVQAMNRICVLDVDLQGVRSIKKTDLCPIYIFVQPPsldvleqrlrlrnteteeslakrlaaartdmesskepglf 165
Cdd:cd00071    81 AAVEEALAEGKIVILEIDVQGARQVKKSYPDAVSIFILPP---------------------------------------- 120

                         170
                  ....*....|....*..
gi 2217262559 166 DLVIINDDLDKAYATLK 182
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 ...
 5-187 5.67e-100

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: 286.70  E-value: 5.67e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262559   5 RPVVLSGPSGAGKSTLLKKLFQEHSSIFgFSVSHTTRNPRPGEEDGKDYYFVTREMMQRDIAAGDFIEHAEFSGNLYGTS 84
Cdd:TIGR03263   1 LLIVISGPSGAGKSTLVKALLEEDPNLK-FSISATTRKPRPGEVDGVDYFFVSKEEFEEMIKAGEFLEWAEVHGNYYGTP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262559  85 KEAVRAVQAMNRICVLDVDLQGVRSIKKTDLCPIYIFVQPPSLDVLEQRLRLRNTETEESLAKRLAAARTDMESSKEpgl 164
Cdd:TIGR03263  80 KSPVEEALAAGKDVLLEIDVQGARQVKKKFPDAVSIFILPPSLEELERRLRKRGTDSEEVIERRLAKAKKEIAHADE--- 156

                         170       180
                  ....*....|....*....|...
gi 2217262559 165 FDLVIINDDLDKAYATLKQALSE 187
Cdd:TIGR03263 157 FDYVIVNDDLEKAVEELKSIILA 179
Guanylate_kin pfam00625
Guanylate kinase;
3-188 1.69e-90

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 262.70  E-value: 1.69e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262559   3 GPRPVVLSGPSGAGKSTLLKKLFQEHSSIFGFSVSHTTRNPRPGEEDGKDYYFVTREMMQRDIAAGDFIEHAEFSGNLYG 82
Cdd:pfam00625   1 SRRPVVLSGPSGVGKSHIKKALLSEYPDKFGYSVPHTTRPPRKGEVDGKDYYFVSKEEMERDISANEFLEYAQFSGNMYG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262559  83 TSKEAVRAVQAMNRICVLDVDLQGVRSIKKTDLCPIYIFVQPPSLDVLEQRLRLRNTETEESLAKRLAAARTDMESSKep 162
Cdd:pfam00625  81 TSVETIEQIHEQGKIVILDVDPQGVKQLRKAELSPISVFIKPPSLKVLQRRLKGRGKEQEEKINKRMAAAEQEFQHYE-- 158

                         170       180
                  ....*....|....*....|....*.
gi 2217262559 163 glFDLVIINDDLDKAYATLKQALSEE 188
Cdd:pfam00625 159 --FDVIIVNDDLEEAYKKLKEALEAE 182
Gmk COG0194
Guanylate kinase [Nucleotide transport and metabolism];
7-188 6.62e-85

Guanylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 439964  Cd Length: 190  Bit Score: 248.83  E-value: 6.62e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262559   7 VVLSGPSGAGKSTLLKKLFQEHSSIfGFSVSHTTRNPRPGEEDGKDYYFVTREMMQRDIAAGDFIEHAEFSGNLYGTSKE 86
Cdd:COG0194     5 IVLSGPSGAGKTTLVKALLERDPDL-RFSVSATTRPPRPGEVDGVDYHFVSREEFERMIENGEFLEWAEVHGNYYGTPKA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262559  87 AVRAVQAMNRICVLDVDLQGVRSIKKtdLCP--IYIFVQPPSLDVLEQRLRLRNTETEESLAKRLAAARTDMESSKEpgl 164
Cdd:COG0194    84 EVEEALAAGKDVLLEIDVQGARQVKK--KFPdaVSIFILPPSLEELERRLRGRGTDSEEVIERRLAKAREELAHADE--- 158

                         170       180
                  ....*....|....*....|....
gi 2217262559 165 FDLVIINDDLDKAYATLKQALSEE 188
Cdd:COG0194   159 FDYVVVNDDLDRAVEELKAIIRAE 182
gmk PRK00300
guanylate kinase; Provisional
 7-191 3.17e-81

guanylate kinase; Provisional


Pssm-ID: 234719  Cd Length: 205  Bit Score: 239.99  E-value: 3.17e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262559   7 VVLSGPSGAGKSTLLKKLFQEHSSIFgFSVSHTTRNPRPGEEDGKDYYFVTREMMQRDIAAGDFIEHAEFSGNLYGTSKE 86
Cdd:PRK00300    8 IVLSGPSGAGKSTLVKALLERDPNLQ-LSVSATTRAPRPGEVDGVDYFFVSKEEFEEMIENGEFLEWAEVFGNYYGTPRS 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262559  87 AVRAVQAMNRICVLDVDLQGVRSIKKtdLCP--IYIFVQPPSLDVLEQRLRLRNTETEESLAKRLAAARTDMESSKEpgl 164
Cdd:PRK00300   87 PVEEALAAGKDVLLEIDWQGARQVKK--KMPdaVSIFILPPSLEELERRLRGRGTDSEEVIARRLAKAREEIAHASE--- 161

                         170       180
                  ....*....|....*....|....*..
gi 2217262559 165 FDLVIINDDLDKAYATLKQALSEEIKK 191
Cdd:PRK00300  162 YDYVIVNDDLDTALEELKAIIRAERLR 188
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
 13-189 3.50e-79

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: 233.72  E-value: 3.50e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262559   13 SGAGKSTLLKKLFQEHSSIFGFSVSHTTRNPRPGEEDGKDYYFVTREMMQRDIAAGDFIEHAEFSGNLYGTSKEAVRAVQ 92
Cdd:smart00072   1 SGVGKGTLLAELIQEIPDAFERVVSHTTRPPRPGEVNGVDYHFVSKEEFEDDIKSGLFLEWGEYEGNYYGTSKETIRQVA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262559   93 AMNRICVLDVDLQGVRSIKKTDLCPIYIFVQPPSLDVLEQRLRLRNTETEESLAKRLAAARTDMessKEPGLFDLVIIND 172
Cdd:smart00072  81 EKGKHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEELERRLRQRGTETSERIQKRLAAAQKEA---QEYHLFDYVIVND 157

                          170
                   ....*....|....*..
gi 2217262559  173 DLDKAYATLKQALSEEI 189
Cdd:smart00072 158 DLEDAYEELKEILEAEQ 174
GMPK cd00071
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ...
 6-182 2.69e-77

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: 227.42  E-value: 2.69e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262559   6 PVVLSGPSGAGKSTLLKKLFQEHSSIFGFSVSHTTRNPRPGEEDGKDYYFVTREMMQRDIAAGDFIEHAEFSGNLYGTSK 85
Cdd:cd00071     1 LIVLSGPSGVGKSTLLKRLLEEFDPNFGFSVSHTTRKPRPGEVDGVDYHFVSKEEFERLIENGEFLEWAEFHGNYYGTSK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262559  86 EAVRAVQAMNRICVLDVDLQGVRSIKKTDLCPIYIFVQPPsldvleqrlrlrnteteeslakrlaaartdmesskepglf 165
Cdd:cd00071    81 AAVEEALAEGKIVILEIDVQGARQVKKSYPDAVSIFILPP---------------------------------------- 120

                         170
                  ....*....|....*..
gi 2217262559 166 DLVIINDDLDKAYATLK 182
Cdd:cd00071   121 DYVIVNDDLEKAYEELK 137
PLN02772 PLN02772
guanylate kinase
 3-186 2.73e-74

guanylate kinase


Pssm-ID: 215414 [Multi-domain]  Cd Length: 398  Bit Score: 228.95  E-value: 2.73e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262559   3 GPRPVVLSGPSGAGKSTLLKKLFQEHSSIFGFSVSHTTRNPRPGEEDGKDYYFVTREMMQRDIAAGDFIEHAEFSGNLYG 82
Cdd:PLN02772  134 AEKPIVISGPSGVGKGTLISMLMKEFPSMFGFSVSHTTRAPREMEKDGVHYHFTERSVMEKEIKDGKFLEFASVHGNLYG 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262559  83 TSKEAVRAVQAMNRICVLDVDLQGVRSIKKTDLCPIYIFVQPPSLDVLEQRLRLRNTETEESLAKRLAAARTDMESSKEP 162
Cdd:PLN02772  214 TSIEAVEVVTDSGKRCILDIDVQGARSVRASSLEAIFIFICPPSMEELEKRLRARGTETEEQIQKRLRNAEAELEQGKSS 293

                         170       180
                  ....*....|....*....|....
gi 2217262559 163 GLFDLVIINDDLDKAYATLKQALS 186
Cdd:PLN02772  294 GIFDHILYNDNLEECYKNLKKLLG 317
gmk PRK14737
guanylate kinase; Provisional
 1-185 8.76e-50

guanylate kinase; Provisional


Pssm-ID: 173199  Cd Length: 186  Bit Score: 159.77  E-value: 8.76e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262559   1 MAGPRPVVLSGPSGAGKSTLLKKLFQEHSSIFgFSVSHTTRNPRPGEEDGKDYYFVTREMMQRDIAAGDFIEHAEFSGNL 80
Cdd:PRK14737    1 KASPKLFIISSVAGGGKSTIIQALLEEHPDFL-FSISCTTRAPRPGDEEGKTYFFLTIEEFKKGIADGEFLEWAEVHDNY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262559  81 YGTSKEAVRAVQAMNRICVLDVDLQGVRSIKKtdLCP---IYIFVQPPSLDVLEQRLRLRNTETEESLAKRLAAARTDME 157
Cdd:PRK14737   80 YGTPKAFIEDAFKEGRSAIMDIDVQGAKIIKE--KFPeriVTIFIEPPSEEEWEERLIHRGTDSEESIEKRIENGIIELD 157

                         170       180
                  ....*....|....*....|....*...
gi 2217262559 158 SSKEpglFDLVIINDDLDKAYATLKQAL 185
Cdd:PRK14737  158 EANE---FDYKIINDDLEDAIADLEAII 182
gmk PRK14738
guanylate kinase; Provisional
 2-188 2.02e-49

guanylate kinase; Provisional


Pssm-ID: 237809  Cd Length: 206  Bit Score: 159.51  E-value: 2.02e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262559   2 AGPRPVVLSGPSGAGKSTLLKKLFQEHSSiFGFSVSHTTRNPRPGEEDGKDYYFVTREMMQRDIAAGDFIEHAEFSGNLY 81
Cdd:PRK14738   11 AKPLLVVISGPSGVGKDAVLARMRERKLP-FHFVVTATTRPKRPGEIDGVDYHFVTPEEFREMISQNELLEWAEVYGNYY 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262559  82 GTSKEAVRAVQAMNRICVLDVDLQGVRSIKKtdLCP--IYIFVQPPSLDVLEQRLRLRNTETEESLAKRLAAARTDMESS 159
Cdd:PRK14738   90 GVPKAPVRQALASGRDVIVKVDVQGAASIKR--LVPeaVFIFLAPPSMDELTRRLELRRTESPEELERRLATAPLELEQL 167

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2217262559 160 KEpglFDLVIIN--DDLDKAYATLKQALSEE 188
Cdd:PRK14738  168 PE---FDYVVVNpeDRLDEAVAQIMAIISAE 195
PhnN COG3709
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
1-193 1.75e-13

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


Pssm-ID: 442923  Cd Length: 188  Bit Score: 65.60  E-value: 1.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262559   1 MAGP-RPVVLSGPSGAGKSTLLKKLFQEHSSIFGFSVSH---TtrnpRPGEEDGKDYYFVTREMMQRDIAAGDFIEHAEF 76
Cdd:COG3709     1 MSGPgRLIYVVGPSGAGKDSLLAAARARLAADPRLVFARryiT----RPADAGGEDHDALSEAEFARRAAAGAFALHWQA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262559  77 SGNLYGTSKEaVRAVQAMNRICVLDvdlqGVRSI------KKTDLCPIYIFVQPpslDVLEQRLRLRNTETEESLAKRLa 150
Cdd:COG3709    77 HGLRYGIPAE-IDAWLAAGRDVVVN----GSRAVlpqaraRYPRLLVVLITASP---EVLAQRLAARGRESAEEIEARL- 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2217262559 151 aARTDMESSKEPGlfDLVIIND-DLDKAYATLKQALSEEIKKAQ 193
Cdd:COG3709   148 -ARAAEFLPDGPD--VLVIDNDgPLEDAGARLLALLRAARARAA 188
phosphon_PhnN TIGR02322
phosphonate metabolism protein/1,5-bisphosphokinase (PRPP-forming) PhnN; Members of this ...
 5-188 2.78e-11

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: 59.69  E-value: 2.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262559   5 RPVVLSGPSGAGKSTLLKKLFQEHSSIFGFSVSHTTRNpRPGEEDGKDYYFVTREMMQRDIAAGDFIEHAEFSGNLYGTS 84
Cdd:TIGR02322   2 RLIYVVGPSGAGKDTLLDYARARLAGDPRVHFVRRVIT-RPASAGGENHIALSTEEFDHREDGGAFALSWQAHGLSYGIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217262559  85 KEAVRAVQAMNricvlDVDLQGVRSI------KKTDLCPIYIFVQPpslDVLEQRLRLRNTETEESLAKRLaaARTDMES 158
Cdd:TIGR02322  81 IEIDQWLEAGD-----VVVVNGSRAVlpearqRYPNLLVVNITASP---DVLAQRLAARGRESREEIEERL--ARSARFA 150

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2217262559 159 SKEPGLFdlVIIND-DLDKAYATLKQALSEE 188
Cdd:TIGR02322 151 AAPADVT--TIDNSgSLEVAGETLLRLLRKE 179
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
 7-25 1.35e-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: 41.27  E-value: 1.35e-04
                          10
                  ....*....|....*....
gi 2217262559   7 VVLSGPSGAGKSTLLKKLF 25
Cdd:COG4778    40 VALTGPSGAGKSTLLKCIY 58
COG4639 COG4639
Predicted kinase [General function prediction only];
7-27 1.39e-04

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 40.20  E-value: 1.39e-04
                          10        20
                  ....*....|....*....|.
gi 2217262559   7 VVLSGPSGAGKSTLLKKLFQE 27
Cdd:COG4639     5 VVLIGLPGSGKSTFARRLFAP 25
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
7-45 1.49e-04

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 41.19  E-value: 1.49e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2217262559   7 VVLSGPSGAGKSTLLKKLF-QEHSS-----IFGFSVSHTTRNPRP 45
Cdd:COG2884    31 VFLTGPSGAGKSTLLKLLYgEERPTsgqvlVNGQDLSRLKRREIP 75
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 7-42 6.55e-04

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


Pssm-ID: 206747 [Multi-domain]  Cd Length: 211  Bit Score: 38.92  E-value: 6.55e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2217262559   7 VVLSGPSGAGKSTLLKKLFQEHSSIFGfSVS-------HTTRN 42
Cdd:cd01854    88 SVLVGQSGVGKSTLLNALLPELVLATG-EISeklgrgrHTTTH 129
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 7-56 1.05e-03

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


Pssm-ID: 460387 [Multi-domain]  Cd Length: 113  Bit Score: 37.21  E-value: 1.05e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217262559   7 VVLSGPSGAGKSTLLKKLFQEHSsifgfSVSH---TTRNPRPG--EEDGKDYYFV 56
Cdd:pfam01926   2 VALVGRPNVGKSTLINALTGAKA-----IVSDypgTTRDPNEGrlELKGKQIILV 51
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
7-22 1.11e-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: 1.11e-03
                          10
                  ....*....|....*.
gi 2217262559   7 VVLSGPSGAGKSTLLK 22
Cdd:COG4619    29 VAITGPSGSGKSTLLR 44
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
 7-29 2.02e-03

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 37.63  E-value: 2.02e-03
                          10        20
                  ....*....|....*....|...
gi 2217262559   7 VVLSGPSGAGKSTLLKKLFQEHS 29
Cdd:COG2401    59 VLIVGASGSGKSTLLRLLAGALK 81
COG1373 COG1373
Predicted ATPase, AAA+ superfamily [General function prediction only];
1-32 2.48e-03

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


Pssm-ID: 440984 [Multi-domain]  Cd Length: 405  Bit Score: 38.00  E-value: 2.48e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2217262559   1 MAGPRPVVLSGPSGAGKSTLLKKLFQEHSSIF 32
Cdd:COG1373    17 LDNRKAVVITGPRQVGKTTLLKQLAKELENIL 48
AAA_14 pfam13173
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 4-28 2.62e-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: 2.62e-03
                          10        20
                  ....*....|....*....|....*
gi 2217262559   4 PRPVVLSGPSGAGKSTLLKKLFQEH 28
Cdd:pfam13173   2 RKILVITGPRQVGKTTLLLQLIKEL 26
NK cd02019
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ...
 7-27 2.77e-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: 35.00  E-value: 2.77e-03
                          10        20
                  ....*....|....*....|.
gi 2217262559   7 VVLSGPSGAGKSTLLKKLFQE 27
Cdd:cd02019     2 IAITGGSGSGKSTVAKKLAEQ 22
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 11-43 2.78e-03

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: 37.05  E-value: 2.78e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2217262559  11 GPSGAGKSTLLKKLFQEHSSIFGfSVSHTTRNP 43
Cdd:cd00882     4 GRGGVGKSSLLNALLGGEVGEVS-DVPGTTRDP 35
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
 7-42 3.88e-03

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


Pssm-ID: 427191 [Multi-domain]  Cd Length: 174  Bit Score: 36.75  E-value: 3.88e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2217262559   7 VVLSGPSGAGKSTLLKKLFQEHSSIFGfSVS-------HTTRN 42
Cdd:pfam03193 109 TVLAGQSGVGKSTLLNALLPELDLRTG-EISeklgrgrHTTTH 150
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
 7-24 3.92e-03

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 36.92  E-value: 3.92e-03
                          10
                  ....*....|....*...
gi 2217262559   7 VVLSGPSGAGKSTLLKKL 24
Cdd:PRK11124   31 LVLLGPSGAGKSSLLRVL 48
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
2-45 3.92e-03

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 36.87  E-value: 3.92e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2217262559   2 AGPRPVVLsGPSGAGKSTLLKK----LFQEHSSIFGFSVSHTTRNP--RP 45
Cdd:PRK10771   24 RGERVAIL-GPSGAGKSTLLNLiagfLTPASGSLTLNGQDHTTTPPsrRP 72
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
 2-56 4.05e-03

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 37.47  E-value: 4.05e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217262559   2 AGPRPVVLSGPSGAGKSTLLKKLFQEHSSIFGfSVSHTTRNPRPG--EEDGKDYYFV 56
Cdd:PRK09518  448 SGLRRVALVGRPNVGKSSLLNQLTHEERAVVN-DLAGTTRDPVDEivEIDGEDWLFI 503
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 4-67 4.71e-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: 36.20  E-value: 4.71e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217262559    4 PRPVVLSGPSGAGKSTLLKKL----FQEHSSIFGFSVSHT---TRNPRPGEEDGKDYYFVTREMMQRDIAA 67
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 ...
 11-44 4.80e-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: 36.07  E-value: 4.80e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2217262559  11 GPSGAGKSTLLKKLFQEHSSIFGfSVSHTTRNPR 44
Cdd:cd00880     4 GRPNVGKSSLLNALLGQNVGIVS-PIPGTTRDPV 36
PRK00098 PRK00098
GTPase RsgA; Reviewed
 8-41 5.08e-03

GTPase RsgA; Reviewed


Pssm-ID: 234631 [Multi-domain]  Cd Length: 298  Bit Score: 36.72  E-value: 5.08e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2217262559   8 VLSGPSGAGKSTLLKKLF-------QEHSSIFGfSVSHTTR 41
Cdd:PRK00098  168 VLAGQSGVGKSTLLNALApdlelktGEISEALG-RGKHTTT 207
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
 7-22 5.12e-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: 5.12e-03
                          10
                  ....*....|....*.
gi 2217262559   7 VVLSGPSGAGKSTLLK 22
Cdd:COG3839    32 LVLLGPSGCGKSTLLR 47
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
7-24 5.64e-03

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 36.53  E-value: 5.64e-03
                          10
                  ....*....|....*...
gi 2217262559   7 VVLSGPSGAGKSTLLKKL 24
Cdd:COG4161    31 LVLLGPSGAGKSSLLRVL 48
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
 7-27 5.69e-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: 36.23  E-value: 5.69e-03
                          10        20
                  ....*....|....*....|.
gi 2217262559   7 VVLSGPSGAGKSTLLKKLFQE 27
Cdd:cd03292    30 VFLVGPSGAGKSTLLKLIYKE 50
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
2-45 6.01e-03

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 36.27  E-value: 6.01e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217262559   2 AGPRPVVLsGPSGAGKSTLLkklfqehSSIFGF-----------SVSHTTRNP--RP 45
Cdd:COG3840    24 AGERVAIL-GPSGAGKSTLL-------NLIAGFlppdsgrilwnGQDLTALPPaeRP 72
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
 7-27 7.02e-03

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 36.29  E-value: 7.02e-03
                          10        20
                  ....*....|....*....|.
gi 2217262559   7 VVLSGPSGAGKSTLLKKLFQE 27
Cdd:PRK13548   31 VAILGPNGAGKSTLLRALSGE 51
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
 3-27 9.49e-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: 35.56  E-value: 9.49e-03
                          10        20
                  ....*....|....*....|....*
gi 2217262559   3 GPRPVVLSGPSGAGKSTLLKKLFQE 27
Cdd:pfam13191  23 RPPSVLLTGEAGTGKTTLLRELLRA 47
 
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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