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Conserved domains on  [gi|1926177964|ref|XP_036873141|]
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guanylate kinase isoform X7 [Manis javanica]

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 ...
 57-225 2.03e-81

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: 241.24  E-value: 2.03e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926177964  57 RPVVLSGPSGAGKSTLLKRLLQEHRGIFgFSVS--------------HYYFVTREVMQRDIAAGDFIEHAEFSGNLYGTS 122
Cdd:TIGR03263   1 LLIVISGPSGAGKSTLVKALLEEDPNLK-FSISattrkprpgevdgvDYFFVSKEEFEEMIKAGEFLEWAEVHGNYYGTP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926177964 123 KAAVRAVQAMNRICLLDVDLQGVRNIKMTDLRPIFIFVQPPSLDVLEQRLRLRNTETEESLSKRLTAARADMESSKEpgl 202
Cdd:TIGR03263  80 KSPVEEALAAGKDVLLEIDVQGARQVKKKFPDAVSIFILPPSLEELERRLRKRGTDSEEVIERRLAKAKKEIAHADE--- 156

                         170       180
                  ....*....|....*....|...
gi 1926177964 203 FDLVIVNDNLDKAYHALEEALLE 225
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 ...
 57-225 2.03e-81

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: 241.24  E-value: 2.03e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926177964  57 RPVVLSGPSGAGKSTLLKRLLQEHRGIFgFSVS--------------HYYFVTREVMQRDIAAGDFIEHAEFSGNLYGTS 122
Cdd:TIGR03263   1 LLIVISGPSGAGKSTLVKALLEEDPNLK-FSISattrkprpgevdgvDYFFVSKEEFEEMIKAGEFLEWAEVHGNYYGTP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926177964 123 KAAVRAVQAMNRICLLDVDLQGVRNIKMTDLRPIFIFVQPPSLDVLEQRLRLRNTETEESLSKRLTAARADMESSKEpgl 202
Cdd:TIGR03263  80 KSPVEEALAAGKDVLLEIDVQGARQVKKKFPDAVSIFILPPSLEELERRLRKRGTDSEEVIERRLAKAKKEIAHADE--- 156

                         170       180
                  ....*....|....*....|...
gi 1926177964 203 FDLVIVNDNLDKAYHALEEALLE 225
Cdd:TIGR03263 157 FDYVIVNDDLEKAVEELKSIILA 179
Guanylate_kin pfam00625
Guanylate kinase;
55-226 6.49e-76

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 227.26  E-value: 6.49e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926177964  55 GPRPVVLSGPSGAGKSTLLKRLLQEHRGIFGFSVSH--------------YYFVTREVMQRDIAAGDFIEHAEFSGNLYG 120
Cdd:pfam00625   1 SRRPVVLSGPSGVGKSHIKKALLSEYPDKFGYSVPHttrpprkgevdgkdYYFVSKEEMERDISANEFLEYAQFSGNMYG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926177964 121 TSKAAVRAVQAMNRICLLDVDLQGVRNIKMTDLRPIFIFVQPPSLDVLEQRLRLRNTETEESLSKRLTAARADMESSKep 200
Cdd:pfam00625  81 TSVETIEQIHEQGKIVILDVDPQGVKQLRKAELSPISVFIKPPSLKVLQRRLKGRGKEQEEKINKRMAAAEQEFQHYE-- 158

                         170       180
                  ....*....|....*....|....*.
gi 1926177964 201 glFDLVIVNDNLDKAYHALEEALLEE 226
Cdd:pfam00625 159 --FDVIIVNDDLEEAYKKLKEALEAE 182
Gmk COG0194
Guanylate kinase [Nucleotide transport and metabolism];
59-226 8.63e-68

Guanylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 439964  Cd Length: 190  Bit Score: 206.84  E-value: 8.63e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926177964  59 VVLSGPSGAGKSTLLKRLLQEHRGIfGFSVS--------------HYYFVTREVMQRDIAAGDFIEHAEFSGNLYGTSKA 124
Cdd:COG0194     5 IVLSGPSGAGKTTLVKALLERDPDL-RFSVSattrpprpgevdgvDYHFVSREEFERMIENGEFLEWAEVHGNYYGTPKA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926177964 125 AVRAVQAMNRICLLDVDLQGVRNIKmtDLRP--IFIFVQPPSLDVLEQRLRLRNTETEESLSKRLTAARADMESSKEpgl 202
Cdd:COG0194    84 EVEEALAAGKDVLLEIDVQGARQVK--KKFPdaVSIFILPPSLEELERRLRGRGTDSEEVIERRLAKAREELAHADE--- 158

                         170       180
                  ....*....|....*....|....
gi 1926177964 203 FDLVIVNDNLDKAYHALEEALLEE 226
Cdd:COG0194   159 FDYVVVNDDLDRAVEELKAIIRAE 182
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
 65-227 1.79e-65

Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to GDP. Structure resembles that of adenylate kinase. So-called membrane-associated guanylate kinase homologues (MAGUKs) do not possess guanylate kinase activities; instead at least some possess protein-binding functions.


Pssm-ID: 214504 [Multi-domain]  Cd Length: 174  Bit Score: 200.60  E-value: 1.79e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926177964   65 SGAGKSTLLKRLLQEHRGIFGFSVSH--------------YYFVTREVMQRDIAAGDFIEHAEFSGNLYGTSKAAVRAVQ 130
Cdd:smart00072   1 SGVGKGTLLAELIQEIPDAFERVVSHttrpprpgevngvdYHFVSKEEFEDDIKSGLFLEWGEYEGNYYGTSKETIRQVA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926177964  131 AMNRICLLDVDLQGVRNIKMTDLRPIFIFVQPPSLDVLEQRLRLRNTETEESLSKRLTAARADMessKEPGLFDLVIVND 210
Cdd:smart00072  81 EKGKHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEELERRLRQRGTETSERIQKRLAAAQKEA---QEYHLFDYVIVND 157

                          170
                   ....*....|....*..
gi 1926177964  211 NLDKAYHALEEALLEEI 227
Cdd:smart00072 158 DLEDAYEELKEILEAEQ 174
gmk PRK00300
guanylate kinase; Provisional
 59-229 4.06e-64

guanylate kinase; Provisional


Pssm-ID: 234719  Cd Length: 205  Bit Score: 198.00  E-value: 4.06e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926177964  59 VVLSGPSGAGKSTLLKRLLQEHRGIFgFSVS--------------HYYFVTREVMQRDIAAGDFIEHAEFSGNLYGTSKA 124
Cdd:PRK00300    8 IVLSGPSGAGKSTLVKALLERDPNLQ-LSVSattraprpgevdgvDYFFVSKEEFEEMIENGEFLEWAEVFGNYYGTPRS 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926177964 125 AVRAVQAMNRICLLDVDLQGVRNIK--MTDLrpIFIFVQPPSLDVLEQRLRLRNTETEESLSKRLTAARADMESSKEpgl 202
Cdd:PRK00300   87 PVEEALAAGKDVLLEIDWQGARQVKkkMPDA--VSIFILPPSLEELERRLRGRGTDSEEVIARRLAKAREEIAHASE--- 161

                         170       180
                  ....*....|....*....|....*..
gi 1926177964 203 FDLVIVNDNLDKAYHALEEALLEEIKK 229
Cdd:PRK00300  162 YDYVIVNDDLDTALEELKAIIRAERLR 188
GMPK cd00071
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ...
 58-220 4.46e-58

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: 180.42  E-value: 4.46e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926177964  58 PVVLSGPSGAGKSTLLKRLLQEHRGIFGFSVSH--------------YYFVTREVMQRDIAAGDFIEHAEFSGNLYGTSK 123
Cdd:cd00071     1 LIVLSGPSGVGKSTLLKRLLEEFDPNFGFSVSHttrkprpgevdgvdYHFVSKEEFERLIENGEFLEWAEFHGNYYGTSK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926177964 124 AAVRAVQAMNRICLLDVDLQGVRNIKMTDLRPIFIFVQPPsldvleqrlrlrnteteeslskrltaaradmesskepglf 203
Cdd:cd00071    81 AAVEEALAEGKIVILEIDVQGARQVKKSYPDAVSIFILPP---------------------------------------- 120

                         170
                  ....*....|....*..
gi 1926177964 204 DLVIVNDNLDKAYHALE 220
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 ...
 57-225 2.03e-81

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: 241.24  E-value: 2.03e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926177964  57 RPVVLSGPSGAGKSTLLKRLLQEHRGIFgFSVS--------------HYYFVTREVMQRDIAAGDFIEHAEFSGNLYGTS 122
Cdd:TIGR03263   1 LLIVISGPSGAGKSTLVKALLEEDPNLK-FSISattrkprpgevdgvDYFFVSKEEFEEMIKAGEFLEWAEVHGNYYGTP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926177964 123 KAAVRAVQAMNRICLLDVDLQGVRNIKMTDLRPIFIFVQPPSLDVLEQRLRLRNTETEESLSKRLTAARADMESSKEpgl 202
Cdd:TIGR03263  80 KSPVEEALAAGKDVLLEIDVQGARQVKKKFPDAVSIFILPPSLEELERRLRKRGTDSEEVIERRLAKAKKEIAHADE--- 156

                         170       180
                  ....*....|....*....|...
gi 1926177964 203 FDLVIVNDNLDKAYHALEEALLE 225
Cdd:TIGR03263 157 FDYVIVNDDLEKAVEELKSIILA 179
Guanylate_kin pfam00625
Guanylate kinase;
55-226 6.49e-76

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 227.26  E-value: 6.49e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926177964  55 GPRPVVLSGPSGAGKSTLLKRLLQEHRGIFGFSVSH--------------YYFVTREVMQRDIAAGDFIEHAEFSGNLYG 120
Cdd:pfam00625   1 SRRPVVLSGPSGVGKSHIKKALLSEYPDKFGYSVPHttrpprkgevdgkdYYFVSKEEMERDISANEFLEYAQFSGNMYG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926177964 121 TSKAAVRAVQAMNRICLLDVDLQGVRNIKMTDLRPIFIFVQPPSLDVLEQRLRLRNTETEESLSKRLTAARADMESSKep 200
Cdd:pfam00625  81 TSVETIEQIHEQGKIVILDVDPQGVKQLRKAELSPISVFIKPPSLKVLQRRLKGRGKEQEEKINKRMAAAEQEFQHYE-- 158

                         170       180
                  ....*....|....*....|....*.
gi 1926177964 201 glFDLVIVNDNLDKAYHALEEALLEE 226
Cdd:pfam00625 159 --FDVIIVNDDLEEAYKKLKEALEAE 182
Gmk COG0194
Guanylate kinase [Nucleotide transport and metabolism];
59-226 8.63e-68

Guanylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 439964  Cd Length: 190  Bit Score: 206.84  E-value: 8.63e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926177964  59 VVLSGPSGAGKSTLLKRLLQEHRGIfGFSVS--------------HYYFVTREVMQRDIAAGDFIEHAEFSGNLYGTSKA 124
Cdd:COG0194     5 IVLSGPSGAGKTTLVKALLERDPDL-RFSVSattrpprpgevdgvDYHFVSREEFERMIENGEFLEWAEVHGNYYGTPKA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926177964 125 AVRAVQAMNRICLLDVDLQGVRNIKmtDLRP--IFIFVQPPSLDVLEQRLRLRNTETEESLSKRLTAARADMESSKEpgl 202
Cdd:COG0194    84 EVEEALAAGKDVLLEIDVQGARQVK--KKFPdaVSIFILPPSLEELERRLRGRGTDSEEVIERRLAKAREELAHADE--- 158

                         170       180
                  ....*....|....*....|....
gi 1926177964 203 FDLVIVNDNLDKAYHALEEALLEE 226
Cdd:COG0194   159 FDYVVVNDDLDRAVEELKAIIRAE 182
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
 65-227 1.79e-65

Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to GDP. Structure resembles that of adenylate kinase. So-called membrane-associated guanylate kinase homologues (MAGUKs) do not possess guanylate kinase activities; instead at least some possess protein-binding functions.


Pssm-ID: 214504 [Multi-domain]  Cd Length: 174  Bit Score: 200.60  E-value: 1.79e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926177964   65 SGAGKSTLLKRLLQEHRGIFGFSVSH--------------YYFVTREVMQRDIAAGDFIEHAEFSGNLYGTSKAAVRAVQ 130
Cdd:smart00072   1 SGVGKGTLLAELIQEIPDAFERVVSHttrpprpgevngvdYHFVSKEEFEDDIKSGLFLEWGEYEGNYYGTSKETIRQVA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926177964  131 AMNRICLLDVDLQGVRNIKMTDLRPIFIFVQPPSLDVLEQRLRLRNTETEESLSKRLTAARADMessKEPGLFDLVIVND 210
Cdd:smart00072  81 EKGKHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEELERRLRQRGTETSERIQKRLAAAQKEA---QEYHLFDYVIVND 157

                          170
                   ....*....|....*..
gi 1926177964  211 NLDKAYHALEEALLEEI 227
Cdd:smart00072 158 DLEDAYEELKEILEAEQ 174
gmk PRK00300
guanylate kinase; Provisional
 59-229 4.06e-64

guanylate kinase; Provisional


Pssm-ID: 234719  Cd Length: 205  Bit Score: 198.00  E-value: 4.06e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926177964  59 VVLSGPSGAGKSTLLKRLLQEHRGIFgFSVS--------------HYYFVTREVMQRDIAAGDFIEHAEFSGNLYGTSKA 124
Cdd:PRK00300    8 IVLSGPSGAGKSTLVKALLERDPNLQ-LSVSattraprpgevdgvDYFFVSKEEFEEMIENGEFLEWAEVFGNYYGTPRS 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926177964 125 AVRAVQAMNRICLLDVDLQGVRNIK--MTDLrpIFIFVQPPSLDVLEQRLRLRNTETEESLSKRLTAARADMESSKEpgl 202
Cdd:PRK00300   87 PVEEALAAGKDVLLEIDWQGARQVKkkMPDA--VSIFILPPSLEELERRLRGRGTDSEEVIARRLAKAREEIAHASE--- 161

                         170       180
                  ....*....|....*....|....*..
gi 1926177964 203 FDLVIVNDNLDKAYHALEEALLEEIKK 229
Cdd:PRK00300  162 YDYVIVNDDLDTALEELKAIIRAERLR 188
PLN02772 PLN02772
guanylate kinase
 50-223 1.19e-62

guanylate kinase


Pssm-ID: 215414 [Multi-domain]  Cd Length: 398  Bit Score: 200.83  E-value: 1.19e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926177964  50 SSGMSG--PRPVVLSGPSGAGKSTLLKRLLQEHRGIFGFSVSH--------------YYFVTREVMQRDIAAGDFIEHAE 113
Cdd:PLN02772  127 SKGVRGnaEKPIVISGPSGVGKGTLISMLMKEFPSMFGFSVSHttrapremekdgvhYHFTERSVMEKEIKDGKFLEFAS 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926177964 114 FSGNLYGTSKAAVRAVQAMNRICLLDVDLQGVRNIKMTDLRPIFIFVQPPSLDVLEQRLRLRNTETEESLSKRLTAARAD 193
Cdd:PLN02772  207 VHGNLYGTSIEAVEVVTDSGKRCILDIDVQGARSVRASSLEAIFIFICPPSMEELEKRLRARGTETEEQIQKRLRNAEAE 286

                         170       180       190
                  ....*....|....*....|....*....|
gi 1926177964 194 MESSKEPGLFDLVIVNDNLDKAYHALEEAL 223
Cdd:PLN02772  287 LEQGKSSGIFDHILYNDNLEECYKNLKKLL 316
GMPK cd00071
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ...
 58-220 4.46e-58

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: 180.42  E-value: 4.46e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926177964  58 PVVLSGPSGAGKSTLLKRLLQEHRGIFGFSVSH--------------YYFVTREVMQRDIAAGDFIEHAEFSGNLYGTSK 123
Cdd:cd00071     1 LIVLSGPSGVGKSTLLKRLLEEFDPNFGFSVSHttrkprpgevdgvdYHFVSKEEFERLIENGEFLEWAEFHGNYYGTSK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926177964 124 AAVRAVQAMNRICLLDVDLQGVRNIKMTDLRPIFIFVQPPsldvleqrlrlrnteteeslskrltaaradmesskepglf 203
Cdd:cd00071    81 AAVEEALAEGKIVILEIDVQGARQVKKSYPDAVSIFILPP---------------------------------------- 120

                         170
                  ....*....|....*..
gi 1926177964 204 DLVIVNDNLDKAYHALE 220
Cdd:cd00071   121 DYVIVNDDLEKAYEELK 137
gmk PRK14737
guanylate kinase; Provisional
 53-224 6.14e-37

guanylate kinase; Provisional


Pssm-ID: 173199  Cd Length: 186  Bit Score: 128.19  E-value: 6.14e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926177964  53 MSGPRPVVLSGPSGAGKSTLLKRLLQEHRGIFgFSVS--------------HYYFVTREVMQRDIAAGDFIEHAEFSGNL 118
Cdd:PRK14737    1 KASPKLFIISSVAGGGKSTIIQALLEEHPDFL-FSIScttraprpgdeegkTYFFLTIEEFKKGIADGEFLEWAEVHDNY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926177964 119 YGTSKAAVRAVQAMNRICLLDVDLQGVRNIKmtDLRP---IFIFVQPPSLDVLEQRLRLRNTETEESLSKRLTAARADME 195
Cdd:PRK14737   80 YGTPKAFIEDAFKEGRSAIMDIDVQGAKIIK--EKFPeriVTIFIEPPSEEEWEERLIHRGTDSEESIEKRIENGIIELD 157

                         170       180
                  ....*....|....*....|....*....
gi 1926177964 196 SSKEpglFDLVIVNDNLDKAYHALEEALL 224
Cdd:PRK14737  158 EANE---FDYKIINDDLEDAIADLEAIIC 183
gmk PRK14738
guanylate kinase; Provisional
 56-215 4.59e-36

guanylate kinase; Provisional


Pssm-ID: 237809  Cd Length: 206  Bit Score: 126.38  E-value: 4.59e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926177964  56 PRPVVLSGPSGAGKSTLLKRLlQEHRGIFGFSVS--------------HYYFVTREVMQRDIAAGDFIEHAEFSGNLYGT 121
Cdd:PRK14738   13 PLLVVISGPSGVGKDAVLARM-RERKLPFHFVVTattrpkrpgeidgvDYHFVTPEEFREMISQNELLEWAEVYGNYYGV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926177964 122 SKAAVRAVQAMNRICLLDVDLQGVRNIKMTDLRPIFIFVQPPSLDVLEQRLRLRNTETEESLSKRLTAARADMESSKEpg 201
Cdd:PRK14738   92 PKAPVRQALASGRDVIVKVDVQGAASIKRLVPEAVFIFLAPPSMDELTRRLELRRTESPEELERRLATAPLELEQLPE-- 169

                         170
                  ....*....|....*.
gi 1926177964 202 lFDLVIVN--DNLDKA 215
Cdd:PRK14738  170 -FDYVVVNpeDRLDEA 184
PhnN COG3709
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
53-223 2.43e-11

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


Pssm-ID: 442923  Cd Length: 188  Bit Score: 60.59  E-value: 2.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926177964  53 MSGP-RPVVLSGPSGAGKSTLLKRLLQEHRGIFGFSVSHYYfVTREVM--------------QRDIAAGDFIEHAEFSGN 117
Cdd:COG3709     1 MSGPgRLIYVVGPSGAGKDSLLAAARARLAADPRLVFARRY-ITRPADaggedhdalseaefARRAAAGAFALHWQAHGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926177964 118 LYGTSkAAVRAVQAMNRICLLDVD---LQGVRNiKMTDLRPIFIFVQPpslDVLEQRLRLRNTETEESLSKRLtaARADM 194
Cdd:COG3709    80 RYGIP-AEIDAWLAAGRDVVVNGSravLPQARA-RYPRLLVVLITASP---EVLAQRLAARGRESAEEIEARL--ARAAE 152

                         170       180       190
                  ....*....|....*....|....*....|
gi 1926177964 195 ESSKEPGlfDLVIVNDN-LDKAYHALEEAL 223
Cdd:COG3709   153 FLPDGPD--VLVIDNDGpLEDAGARLLALL 180
phosphon_PhnN TIGR02322
phosphonate metabolism protein/1,5-bisphosphokinase (PRPP-forming) PhnN; Members of this ...
 57-210 9.83e-08

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: 50.44  E-value: 9.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926177964  57 RPVVLSGPSGAGKSTLLKRLLQEHRGIFGFSVSHYYF-------------VTREVMQRDIAAGDFIEHAEFSGNLYGTSK 123
Cdd:TIGR02322   2 RLIYVVGPSGAGKDTLLDYARARLAGDPRVHFVRRVItrpasaggenhiaLSTEEFDHREDGGAFALSWQAHGLSYGIPI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926177964 124 AAVRAVQAMNricllDVDLQGVRNI------KMTDLRPIFIFVQPpslDVLEQRLRLRNTETEESLSKRLtaARADMESS 197
Cdd:TIGR02322  82 EIDQWLEAGD-----VVVVNGSRAVlpearqRYPNLLVVNITASP---DVLAQRLAARGRESREEIEERL--ARSARFAA 151

                         170
                  ....*....|...
gi 1926177964 198 KEPGLFdlVIVND 210
Cdd:TIGR02322 152 APADVT--TIDNS 162
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
59-219 6.61e-05

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 41.82  E-value: 6.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926177964  59 VVLSGPSGAGKSTLLKRLLQEHRGIfgfsvshyYFVTREVMQR--DIAAGDFIEHAEFSGNLYGTSKAAVRAVQAMNRIC 136
Cdd:COG0645     2 ILVCGLPGSGKSTLARALAERLGAV--------RLRSDVVRKRlfGAGLAPLERSPEATARTYARLLALARELLAAGRSV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926177964 137 LLD------VDLQGVRNI-KMTDLRPIFIFVQPPsLDVLEQRLRLRNTETEESLS--KRLTAARADMESSKEPGLFDLVI 207
Cdd:COG0645    74 ILDatflrrAQREAFRALaEEAGAPFVLIWLDAP-EEVLRERLEARNAEGGDSDAtwEVLERQLAFEEPLTEDEGFLLVV 152

                         170
                  ....*....|..
gi 1926177964 208 VNDNLDKAYHAL 219
Cdd:COG0645   153 DTSGLEEALAAL 164
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
59-90 1.20e-04

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 41.96  E-value: 1.20e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1926177964  59 VVLSGPSGAGKSTLLKRLLQEHR---G---IFGFSVSH 90
Cdd:COG2884    31 VFLTGPSGAGKSTLLKLLYGEERptsGqvlVNGQDLSR 68
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 59-200 1.60e-04

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: 40.76  E-value: 1.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926177964  59 VVLSGPSGAGKSTLLKRLLQEHrgifgfsvsHYYFVTREVMQRDIAA---GDFIEHAEFSGNLYGTSKAAVRAVQAMNRI 135
Cdd:pfam13671   2 ILLVGLPGSGKSTLARRLLEEL---------GAVRLSSDDERKRLFGegrPSISYYTDATDRTYERLHELARIALRAGRP 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1926177964 136 CLLD-----VDLQ-GVRNIKMTDLRPIFIFVQPPSLDVLEQRLRLRNtETEESLSKRLTAARADMESSKEP 200
Cdd:pfam13671  73 VILDatnlrRDERaRLLALAREYGVPVRIVVFEAPEEVLRERLAARA-RAGGDPSDVPEEVLDRQKARFEP 142
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 59-77 2.56e-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: 40.84  E-value: 2.56e-04
                          10
                  ....*....|....*....
gi 1926177964  59 VVLSGPSGAGKSTLLKRLL 77
Cdd:cd01854    88 SVLVGQSGVGKSTLLNALL 106
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
59-82 2.59e-04

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 40.96  E-value: 2.59e-04
                          10        20
                  ....*....|....*....|....*..
gi 1926177964  59 VVLSGPSGAGKSTLLK---RLLQEHRG 82
Cdd:COG4619    29 VAITGPSGSGKSTLLRalaDLDPPTSG 55
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 56-114 2.61e-04

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: 40.21  E-value: 2.61e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1926177964  56 PRPVVLSGPSGAGKSTLLKRLLQEhrgIFGFSVSHYYFVTREVMQRDIAAGDFIEHAEF 114
Cdd:cd00009    19 PKNLLLYGPPGTGKTTLARAIANE---LFRPGAPFLYLNASDLLEGLVVAELFGHFLVR 74
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
 59-74 4.69e-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: 40.11  E-value: 4.69e-04
                          10
                  ....*....|....*.
gi 1926177964  59 VVLSGPSGAGKSTLLK 74
Cdd:COG4778    40 VALTGPSGAGKSTLLK 55
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 63-98 4.96e-04

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


Pssm-ID: 206646 [Multi-domain]  Cd Length: 161  Bit Score: 39.54  E-value: 4.96e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1926177964  63 GPSGAGKSTLLKRLLQEHRGIfgfsVSHYYFVTREV 98
Cdd:cd00880     4 GRPNVGKSSLLNALLGQNVGI----VSPIPGTTRDP 35
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
63-153 4.97e-04

ABC-type multidrug transport system, ATPase component [Defense mechanisms];


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 40.05  E-value: 4.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926177964  63 GPSGAGKSTLLK---RLLQEHRG---IFGFSVSHYYFVTRE----VMQRDIAAGDF--IEHAEFSGNLYGTSKAAVRA-V 129
Cdd:COG1131    33 GPNGAGKTTTIRmllGLLRPTSGevrVLGEDVARDPAEVRRrigyVPQEPALYPDLtvRENLRFFARLYGLPRKEARErI 112

                          90       100
                  ....*....|....*....|....*
gi 1926177964 130 QAmnricLLD-VDLQGVRNIKMTDL 153
Cdd:COG1131   113 DE-----LLElFGLTDAADRKVGTL 132
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 59-107 5.40e-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: 38.37  E-value: 5.40e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1926177964  59 VVLSGPSGAGKSTLLKRLLQEhRGIfgfsVSHYYFVTREVMQRDIAAGD 107
Cdd:pfam01926   2 VALVGRPNVGKSTLINALTGA-KAI----VSDYPGTTRDPNEGRLELKG 45
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 63-159 5.65e-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: 39.36  E-value: 5.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926177964  63 GPSGAGKSTLLKRLLQEHRGIfgfsVSHYYFVTRE----VMQRDIAAGDF-------IEHAEFSGNLYGTSKAAVRA--- 128
Cdd:cd00882     4 GRGGVGKSSLLNALLGGEVGE----VSDVPGTTRDpdvyVKELDKGKVKLvlvdtpgLDEFGGLGREELARLLLRGAdli 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1926177964 129 ---VQAMNRICLLDVDLQGVRNIKMTDLRPIFIF 159
Cdd:cd00882    80 llvVDSTDRESEEDAKLLILRRLRKEGIPIILVG 113
AAA_18 pfam13238
AAA domain;
59-179 6.83e-04

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 38.56  E-value: 6.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926177964  59 VVLSGPSGAGKSTLLKRlLQEHRGiFGFSVSHYyfvtreVMQRDIAAGDFIEHAEfsgnlygtSKAAVRAVQAMNRICLL 138
Cdd:pfam13238   1 ILITGTPGVGKTTLAKE-LSKRLG-FGDNVRDL------ALENGLVLGDDPETRE--------SKRLDEDKLDRLLDLLE 64

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1926177964 139 DVD---------LQGVRNI----KMTDLRPIFIFVqppSLDVLEQRLRLRNTET 179
Cdd:pfam13238  65 ENAaleeggnliIDGHLAElepeRAKDLVGIVLRA---SPEELLERLEKRGYEE 115
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
 59-79 7.00e-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: 39.06  E-value: 7.00e-04
                          10        20
                  ....*....|....*....|.
gi 1926177964  59 VVLSGPSGAGKSTLLKRLLQE 79
Cdd:pfam03193 109 TVLAGQSGVGKSTLLNALLPE 129
NK cd02019
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ...
 59-104 7.12e-04

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


Pssm-ID: 238977 [Multi-domain]  Cd Length: 69  Bit Score: 36.93  E-value: 7.12e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1926177964  59 VVLSGPSGAGKSTLLKRLLQEHRG--------IFGFSVSHYYFVTREVMQRDIA 104
Cdd:cd02019     2 IAITGGSGSGKSTVAKKLAEQLGGrsvvvldeIVILEGLYASYKSRDARIRDLA 55
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
 59-153 7.66e-04

ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.


Pssm-ID: 213230 [Multi-domain]  Cd Length: 220  Bit Score: 39.41  E-value: 7.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926177964  59 VVLSGPSGAGKSTLLKRLLQEHR------GIFGFSV-SHYYFVTREV---MQRDIAAGDF--IEHAEFSGNLYGTSKAAV 126
Cdd:cd03263    31 FGLLGHNGAGKTTTLKMLTGELRptsgtaYINGYSIrTDRKAARQSLgycPQFDALFDELtvREHLRFYARLKGLPKSEI 110

                          90       100
                  ....*....|....*....|....*..
gi 1926177964 127 RAVQAmnrICLLDVDLQGVRNIKMTDL 153
Cdd:cd03263   111 KEEVE---LLLRVLGLTDKANKRARTL 134
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 56-107 1.01e-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: 1.01e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1926177964   56 PRPVVLSGPSGAGKSTLLKRLLQE----HRGIFGFSVSHYYFVTREVMQRDIAAGD 107
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARElgppGGGVIYIDGEDILEEVLDQLLLIIVGGK 57
COG4639 COG4639
Predicted kinase [General function prediction only];
59-79 1.19e-03

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 38.27  E-value: 1.19e-03
                          10        20
                  ....*....|....*....|.
gi 1926177964  59 VVLSGPSGAGKSTLLKRLLQE 79
Cdd:COG4639     5 VVLIGLPGSGKSTFARRLFAP 25
PRK01889 PRK01889
GTPase RsgA; Reviewed
 54-81 1.36e-03

GTPase RsgA; Reviewed


Pssm-ID: 234988 [Multi-domain]  Cd Length: 356  Bit Score: 39.15  E-value: 1.36e-03
                          10        20
                  ....*....|....*....|....*...
gi 1926177964  54 SGPRPVVLSGPSGAGKSTLLKRLLQEHR 81
Cdd:PRK01889  193 SGGKTVALLGSSGVGKSTLVNALLGEEV 220
AAA_22 pfam13401
AAA domain;
53-80 1.52e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 37.71  E-value: 1.52e-03
                          10        20
                  ....*....|....*....|....*...
gi 1926177964  53 MSGPRPVVLSGPSGAGKSTLLKRLLQEH 80
Cdd:pfam13401   2 RFGAGILVLTGESGTGKTTLLRRLLEQL 29
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 53-102 2.02e-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: 38.28  E-value: 2.02e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1926177964  53 MSGPRPVVL-SGPSGAGKSTLLKRLLQEHRGIFGFSVSH-YYFVTREVMQRD 102
Cdd:COG0572     3 RSGKPRIIGiAGPSGSGKTTFARRLAEQLGADKVVVISLdDYYKDREHLPLD 54
COG1373 COG1373
Predicted ATPase, AAA+ superfamily [General function prediction only];
53-84 3.19e-03

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


Pssm-ID: 440984 [Multi-domain]  Cd Length: 405  Bit Score: 38.00  E-value: 3.19e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1926177964  53 MSGPRPVVLSGPSGAGKSTLLKRLLQEHRGIF 84
Cdd:COG1373    17 LDNRKAVVITGPRQVGKTTLLKQLAKELENIL 48
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
 59-82 3.69e-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: 36.98  E-value: 3.69e-03
                          10        20
                  ....*....|....*....|....*..
gi 1926177964  59 VVLSGPSGAGKSTLLK---RLLQEHRG 82
Cdd:cd03228    31 VAIVGPSGSGKSTLLKlllRLYDPTSG 57
COG4185 COG4185
Predicted ABC-type ATPase or kinase [General function prediction only];
53-86 3.80e-03

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


Pssm-ID: 443339  Cd Length: 197  Bit Score: 37.18  E-value: 3.80e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1926177964  53 MSGPRPVVLSGPSGAGKSTLLKRLLQEHRGIFGF 86
Cdd:COG4185     1 MAMPRLYIIAGPNGAGKSTFARTILPEELGGLEF 34
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
 59-81 3.81e-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: 3.81e-03
                          10        20
                  ....*....|....*....|...
gi 1926177964  59 VVLSGPSGAGKSTLLKRLLQEHR 81
Cdd:cd03292    30 VFLVGPSGAGKSTLLKLIYKEEL 52
AAA_14 pfam13173
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 56-80 5.20e-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: 5.20e-03
                          10        20
                  ....*....|....*....|....*
gi 1926177964  56 PRPVVLSGPSGAGKSTLLKRLLQEH 80
Cdd:pfam13173   2 RKILVITGPRQVGKTTLLLQLIKEL 26
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
 53-79 5.66e-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: 37.07  E-value: 5.66e-03
                          10        20
                  ....*....|....*....|....*..
gi 1926177964  53 MSGPRPVVLSGPSGAGKSTLLKRLLQE 79
Cdd:COG3267    40 AQGGGFVVLTGEVGTGKTTLLRRLLER 66
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
 59-76 6.28e-03

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 36.92  E-value: 6.28e-03
                          10
                  ....*....|....*...
gi 1926177964  59 VVLSGPSGAGKSTLLKRL 76
Cdd:PRK11124   31 LVLLGPSGAGKSSLLRVL 48
CobW-like cd03112
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino ...
 58-82 6.46e-03

cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino acid sequence of YjiA protein in E. coli contains several conserved motifs that characterizes it as a P-loop GTPase. YijA gene is among the genes significantly induced in response to DNA-damage caused by mitomycin. YijA gene is a homologue of the CobW gene which encodes the cobalamin synthesis protein/P47K.


Pssm-ID: 349766  Cd Length: 198  Bit Score: 36.35  E-value: 6.46e-03
                          10        20
                  ....*....|....*....|....*.
gi 1926177964  58 PV-VLSGPSGAGKSTLLKRLLQEHRG 82
Cdd:cd03112     1 PVtLLTGFLGAGKTTLLNHILSEQHG 26
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
 59-82 6.50e-03

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 36.86  E-value: 6.50e-03
                          10        20
                  ....*....|....*....|....
gi 1926177964  59 VVLSGPSGAGKSTLLKRLLQEHRG 82
Cdd:COG2401    59 VLIVGASGSGKSTLLRLLAGALKG 82
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
59-76 7.55e-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: 7.55e-03
                          10
                  ....*....|....*...
gi 1926177964  59 VVLSGPSGAGKSTLLKRL 76
Cdd:COG4161    31 LVLLGPSGAGKSSLLRVL 48
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
 59-74 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: 36.59  E-value: 8.34e-03
                          10
                  ....*....|....*.
gi 1926177964  59 VVLSGPSGAGKSTLLK 74
Cdd:COG3839    32 LVLLGPSGCGKSTLLR 47
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
 59-82 9.35e-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: 36.67  E-value: 9.35e-03
                          10        20
                  ....*....|....*....|....*..
gi 1926177964  59 VVLSGPSGAGKSTLLK---RLLQEHRG 82
Cdd:COG4987   364 VAIVGPSGSGKSTLLAlllRFLDPQSG 390
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
 59-77 9.81e-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: 36.66  E-value: 9.81e-03
                          10
                  ....*....|....*....
gi 1926177964  59 VVLSGPSGAGKSTLLKRLL 77
Cdd:COG4988   366 VALVGPSGAGKSTLLNLLL 384
cobW pfam02492
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase ...
 59-81 9.99e-03

CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase expression / formation protein, and UreG a urease accessory protein. Both these proteins contain a P-loop nucleotide binding motif. HypB has GTPase activity and is a guanine nucleotide binding protein. It is not known whether UreG binds GTP or some other nucleotide. Both enzymes are involved in nickel binding. HypB can store nickel and is required for nickel dependent hydrogenase expression. UreG is required for functional incorporation of the urease nickel metallocenter. GTP hydrolysis may required by these proteins for nickel incorporation into other nickel proteins. This family of domains also contains P47K, a Pseudomonas chlororaphis protein needed for nitrile hydratase expression, and the cobW gene product, which may be involved in cobalamin biosynthesis in Pseudomonas denitrificans.


Pssm-ID: 396860  Cd Length: 179  Bit Score: 35.69  E-value: 9.99e-03
                          10        20
                  ....*....|....*....|...
gi 1926177964  59 VVLSGPSGAGKSTLLKRLLQEHR 81
Cdd:pfam02492   3 TVITGFLGSGKTTLLNHLLKQNR 25
 
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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