NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1952229035|ref|WP_199556605|]
View 

gluconokinase [Shimia marina]

Protein Classification

gluconokinase( domain architecture ID 10790049)

gluconokinase catalyzes the phosphoryl transfer from ATP to gluconate to form gluconate-6-phoshate

Gene Ontology:  GO:0046316|GO:0046177|GO:0005524
SCOP:  4003925

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
GntK COG3265
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ...
 30-191 3.51e-82

Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


:

Pssm-ID: 442496 [Multi-domain]  Cd Length: 164  Bit Score: 241.19  E-value: 3.51e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952229035  30 GQTFIVMGVSGVGKSTLAQALARALKAQYLEADDLHPKSNIDRMAQGLPLTDEMRIPWLQALRSAISEHHHHHPDkdLVA 109
Cdd:COG3265     1 PMVIVVMGVSGSGKSTVGQALAERLGWPFIDGDDFHPPANIAKMAAGIPLTDEDRAPWLEALADAIAAHLAAGEG--AVL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952229035 110 TCSALKRQYRDLLKTNNPQTTFLHLTAPKDVILHRMAKRQDHFMPASLLSSQFAALEPLTKDEDHLLIDATLPPKDIMKR 189
Cdd:COG3265    79 ACSALKRSYRDRLREGNPDVRFVYLDGSRELIAERLAARKGHFMPASLLDSQFATLEPPGPDEDAIVVDIDQPPEEIVAQ 158


                  ..
gi 1952229035 190 VL 191
Cdd:COG3265   159 IL 160
 
Name Accession Description Interval E-value
GntK COG3265
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ...
 30-191 3.51e-82

Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 442496 [Multi-domain]  Cd Length: 164  Bit Score: 241.19  E-value: 3.51e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952229035  30 GQTFIVMGVSGVGKSTLAQALARALKAQYLEADDLHPKSNIDRMAQGLPLTDEMRIPWLQALRSAISEHHHHHPDkdLVA 109
Cdd:COG3265     1 PMVIVVMGVSGSGKSTVGQALAERLGWPFIDGDDFHPPANIAKMAAGIPLTDEDRAPWLEALADAIAAHLAAGEG--AVL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952229035 110 TCSALKRQYRDLLKTNNPQTTFLHLTAPKDVILHRMAKRQDHFMPASLLSSQFAALEPLTKDEDHLLIDATLPPKDIMKR 189
Cdd:COG3265    79 ACSALKRSYRDRLREGNPDVRFVYLDGSRELIAERLAARKGHFMPASLLDSQFATLEPPGPDEDAIVVDIDQPPEEIVAQ 158


                  ..
gi 1952229035 190 VL 191
Cdd:COG3265   159 IL 160
therm_gnt_kin TIGR01313
carbohydrate kinase, thermoresistant glucokinase family; This model represents a subfamily of ...
 33-183 1.39e-60

carbohydrate kinase, thermoresistant glucokinase family; This model represents a subfamily of proteins that includes thermoresistant and thermosensitve isozymes of gluconate kinase (gluconokinase) in E. coli and other related proteins; members of this family are often named by similarity to the thermostable isozyme. These proteins show homology to shikimate kinases and adenylate kinases but not to gluconate kinases from the FGGY family of carbohydrate kinases.


Pssm-ID: 273551  Cd Length: 163  Bit Score: 186.45  E-value: 1.39e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952229035  33 FIVMGVSGVGKSTLAQALARALKAQYLEADDLHPKSNIDRMAQGLPLTDEMRIPWLQALRSAISEHHHHhpDKDLVATCS 112
Cdd:TIGR01313   1 FVLMGVAGSGKSTIASALAHRLGAKFIEGDDLHPAANIEKMSAGIPLNDDDRWPWLQNLNDASTAAAAK--NKVGIITCS 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952229035 113 ALKRQYRDLLKTNNPQTTFLHLTAPKDVILHRMAKRQDHFMPASLLSSQFAALEPLTKDE-DHLLIDATLPP 183
Cdd:TIGR01313  79 ALKRHYRDILREAEPNLHFIYLSGDKDVILERMKARKGHFMKADMLESQFAALEEPLADEtDVLRVDIDQPL 150
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
 33-179 1.23e-58

Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting product gluconate-6-phoshate is an important precursor of gluconate metabolism. GntK acts as a dimmer composed of two identical subunits.


Pssm-ID: 238979 [Multi-domain]  Cd Length: 150  Bit Score: 180.91  E-value: 1.23e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952229035  33 FIVMGVSGVGKSTLAQALARALKAQYLEADDLHPKSNIDRMAQGLPLTDEMRIPWLQALRSAIsEHHHHHPDKDLVATCS 112
Cdd:cd02021     2 IVVMGVSGSGKSTVGKALAERLGAPFIDGDDLHPPANIAKMAAGIPLNDEDRWPWLQALTDAL-LAKLASAGEGVVVACS 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952229035 113 ALKRQYRDLLKTN--NPQTTFLHLTAPKDVILHRMAKRQDHFMPASLLSSQFAALEPLT-KDEDHLLIDA 179
Cdd:cd02021    81 ALKRIYRDILRGGaaNPRVRFVHLDGPREVLAERLAARKGHFMPADLLDSQFETLEPPGeDEEDVIVIDV 150
idnK PRK09825
gluconokinase;
30-178 1.19e-45

gluconokinase;


Pssm-ID: 182097  Cd Length: 176  Bit Score: 149.02  E-value: 1.19e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952229035  30 GQTFIVMGVSGVGKSTLAQALARALKAQYLEADDLHPKSNIDRMAQGLPLTDEMRIPWLQALRSAisEHHHHHPDKDLVA 109
Cdd:PRK09825    3 GESYILMGVSGSGKSLIGSKIAALFSAKFIDGDDLHPAKNIDKMSQGIPLTDEDRLPWLERLNDA--SYSLYKKNETGFI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952229035 110 TCSALKRQYRDLLKTNNPQTTFLHLTAPKDVILHRMAKRQDHFMPASLLSSQFAALE-PLTKDEDHLLID 178
Cdd:PRK09825   81 VCSSLKKQYRDILRKSSPNVHFLWLDGDYETILARMQRRAGHFMPPDLLQSQFDALErPCADEHDIARID 150
SKI pfam01202
Shikimate kinase;
40-191 2.28e-12

Shikimate kinase;


Pssm-ID: 426122 [Multi-domain]  Cd Length: 159  Bit Score: 62.22  E-value: 2.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952229035  40 GVGKSTLAQALARALKAQYLEADDLHPKSNIDRMAQGLPLTDEM--RIPWLQALRSAISEHHHhhpdkdLVAT--CSALK 115
Cdd:pfam01202   2 GAGKSTIGRLLAKALGLPFIDTDEEIEKRTGMSIAEIFEEEGEEgfRRLESEVLKELLAEHGL------VIATggGAVLS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952229035 116 RQYRDLLKTNNpqtTFLHLTAPKDVILHRMAKR------QDHFMPASLLSSQFAALEPLTKDEDHLLIDATL-PPKDIMK 188
Cdd:pfam01202  76 EENRDLLKERG---IVIYLDAPLEVLLERLKRDktrpllQNKDPEEELLELLFEERDPLYEEAADIVIDTDEsSPEEVAT 152


                  ...
gi 1952229035 189 RVL 191
Cdd:pfam01202 153 EIL 155
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 29-58 3.94e-04

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 39.28  E-value: 3.94e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1952229035   29 KGQTFIVMGVSGVGKSTLAQALARALKAQY 58
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPG 30
 
Name Accession Description Interval E-value
GntK COG3265
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ...
 30-191 3.51e-82

Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 442496 [Multi-domain]  Cd Length: 164  Bit Score: 241.19  E-value: 3.51e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952229035  30 GQTFIVMGVSGVGKSTLAQALARALKAQYLEADDLHPKSNIDRMAQGLPLTDEMRIPWLQALRSAISEHHHHHPDkdLVA 109
Cdd:COG3265     1 PMVIVVMGVSGSGKSTVGQALAERLGWPFIDGDDFHPPANIAKMAAGIPLTDEDRAPWLEALADAIAAHLAAGEG--AVL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952229035 110 TCSALKRQYRDLLKTNNPQTTFLHLTAPKDVILHRMAKRQDHFMPASLLSSQFAALEPLTKDEDHLLIDATLPPKDIMKR 189
Cdd:COG3265    79 ACSALKRSYRDRLREGNPDVRFVYLDGSRELIAERLAARKGHFMPASLLDSQFATLEPPGPDEDAIVVDIDQPPEEIVAQ 158


                  ..
gi 1952229035 190 VL 191
Cdd:COG3265   159 IL 160
therm_gnt_kin TIGR01313
carbohydrate kinase, thermoresistant glucokinase family; This model represents a subfamily of ...
 33-183 1.39e-60

carbohydrate kinase, thermoresistant glucokinase family; This model represents a subfamily of proteins that includes thermoresistant and thermosensitve isozymes of gluconate kinase (gluconokinase) in E. coli and other related proteins; members of this family are often named by similarity to the thermostable isozyme. These proteins show homology to shikimate kinases and adenylate kinases but not to gluconate kinases from the FGGY family of carbohydrate kinases.


Pssm-ID: 273551  Cd Length: 163  Bit Score: 186.45  E-value: 1.39e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952229035  33 FIVMGVSGVGKSTLAQALARALKAQYLEADDLHPKSNIDRMAQGLPLTDEMRIPWLQALRSAISEHHHHhpDKDLVATCS 112
Cdd:TIGR01313   1 FVLMGVAGSGKSTIASALAHRLGAKFIEGDDLHPAANIEKMSAGIPLNDDDRWPWLQNLNDASTAAAAK--NKVGIITCS 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952229035 113 ALKRQYRDLLKTNNPQTTFLHLTAPKDVILHRMAKRQDHFMPASLLSSQFAALEPLTKDE-DHLLIDATLPP 183
Cdd:TIGR01313  79 ALKRHYRDILREAEPNLHFIYLSGDKDVILERMKARKGHFMKADMLESQFAALEEPLADEtDVLRVDIDQPL 150
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
 33-179 1.23e-58

Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting product gluconate-6-phoshate is an important precursor of gluconate metabolism. GntK acts as a dimmer composed of two identical subunits.


Pssm-ID: 238979 [Multi-domain]  Cd Length: 150  Bit Score: 180.91  E-value: 1.23e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952229035  33 FIVMGVSGVGKSTLAQALARALKAQYLEADDLHPKSNIDRMAQGLPLTDEMRIPWLQALRSAIsEHHHHHPDKDLVATCS 112
Cdd:cd02021     2 IVVMGVSGSGKSTVGKALAERLGAPFIDGDDLHPPANIAKMAAGIPLNDEDRWPWLQALTDAL-LAKLASAGEGVVVACS 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952229035 113 ALKRQYRDLLKTN--NPQTTFLHLTAPKDVILHRMAKRQDHFMPASLLSSQFAALEPLT-KDEDHLLIDA 179
Cdd:cd02021    81 ALKRIYRDILRGGaaNPRVRFVHLDGPREVLAERLAARKGHFMPADLLDSQFETLEPPGeDEEDVIVIDV 150
idnK PRK09825
gluconokinase;
30-178 1.19e-45

gluconokinase;


Pssm-ID: 182097  Cd Length: 176  Bit Score: 149.02  E-value: 1.19e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952229035  30 GQTFIVMGVSGVGKSTLAQALARALKAQYLEADDLHPKSNIDRMAQGLPLTDEMRIPWLQALRSAisEHHHHHPDKDLVA 109
Cdd:PRK09825    3 GESYILMGVSGSGKSLIGSKIAALFSAKFIDGDDLHPAKNIDKMSQGIPLTDEDRLPWLERLNDA--SYSLYKKNETGFI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952229035 110 TCSALKRQYRDLLKTNNPQTTFLHLTAPKDVILHRMAKRQDHFMPASLLSSQFAALE-PLTKDEDHLLID 178
Cdd:PRK09825   81 VCSSLKKQYRDILRKSSPNVHFLWLDGDYETILARMQRRAGHFMPPDLLQSQFDALErPCADEHDIARID 150
gntK PRK11545
gluconokinase;
36-178 1.30e-44

gluconokinase;


Pssm-ID: 236926  Cd Length: 163  Bit Score: 145.63  E-value: 1.30e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952229035  36 MGVSGVGKSTLAQALARALKAQYLEADDLHPKSNIDRMAQGLPLTDEMRIPWLQALRSAISEHHHHHPDKDLVatCSALK 115
Cdd:PRK11545    1 MGVSGSGKSAVASEVAHQLHAAFLDGDFLHPRRNIEKMASGEPLNDDDRKPWLQALNDAAFAMQRTNKVSLIV--CSALK 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952229035 116 RQYRDLLKTNNPQTTFLHLTAPKDVILHRMAKRQDHFMPASLLSSQFAALEPLTKDE-DHLLID 178
Cdd:PRK11545   79 KHYRDLLREGNPNLSFIYLKGDFDVIESRLKARKGHFFKTQMLVTQFETLQEPGADEtDVLVVD 142
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
33-186 1.97e-12

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 62.24  E-value: 1.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952229035  33 FIVMGVSGVGKSTLAQALARALKAQYLEADD----LHP---KSNIDRMAQGLPLTDEMripwLQALRSAISEHHhhhpdk 105
Cdd:COG0645     2 ILVCGLPGSGKSTLARALAERLGAVRLRSDVvrkrLFGaglAPLERSPEATARTYARL----LALARELLAAGR------ 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952229035 106 DLVATCSALKRQYRD----LLKTNNPQTTFLHLTAPKDVILHRMAKRQDHFMP----ASLLSSQFAALEPLTKDE-DHLL 176
Cdd:COG0645    72 SVILDATFLRRAQREafraLAEEAGAPFVLIWLDAPEEVLRERLEARNAEGGDsdatWEVLERQLAFEEPLTEDEgFLLV 151

                         170
                  ....*....|
gi 1952229035 177 IDATLPPKDI 186
Cdd:COG0645   152 VDTSGLEEAL 161
SKI pfam01202
Shikimate kinase;
40-191 2.28e-12

Shikimate kinase;


Pssm-ID: 426122 [Multi-domain]  Cd Length: 159  Bit Score: 62.22  E-value: 2.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952229035  40 GVGKSTLAQALARALKAQYLEADDLHPKSNIDRMAQGLPLTDEM--RIPWLQALRSAISEHHHhhpdkdLVAT--CSALK 115
Cdd:pfam01202   2 GAGKSTIGRLLAKALGLPFIDTDEEIEKRTGMSIAEIFEEEGEEgfRRLESEVLKELLAEHGL------VIATggGAVLS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952229035 116 RQYRDLLKTNNpqtTFLHLTAPKDVILHRMAKR------QDHFMPASLLSSQFAALEPLTKDEDHLLIDATL-PPKDIMK 188
Cdd:pfam01202  76 EENRDLLKERG---IVIYLDAPLEVLLERLKRDktrpllQNKDPEEELLELLFEERDPLYEEAADIVIDTDEsSPEEVAT 152


                  ...
gi 1952229035 189 RVL 191
Cdd:pfam01202 153 EIL 155
AAA_18 pfam13238
AAA domain;
34-148 1.61e-08

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 50.89  E-value: 1.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952229035  34 IVMGVSGVGKSTLAQALARALKAqYLEADDLHPKSNI-----DRMAQGLPLTDEMRIPWLQALRSAISEHHHHHpdkDLV 108
Cdd:pfam13238   2 LITGTPGVGKTTLAKELSKRLGF-GDNVRDLALENGLvlgddPETRESKRLDEDKLDRLLDLLEENAALEEGGN---LII 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1952229035 109 ATCSAlkrqyrDLLKTNNPQTTFLHLTAPKDVILHRMAKR 148
Cdd:pfam13238  78 DGHLA------ELEPERAKDLVGIVLRASPEELLERLEKR 111
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 33-168 3.42e-08

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: 50.39  E-value: 3.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952229035  33 FIVMGVSGVGKSTLAQALARALKAQYLEADDLhpksnIDRMAQglplTDEMRIPWLQALRSAISEHHHHHPDKDL----- 107
Cdd:pfam13671   2 ILLVGLPGSGKSTLARRLLEELGAVRLSSDDE-----RKRLFG----EGRPSISYYTDATDRTYERLHELARIALragrp 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952229035 108 ---VATCS--ALKRQYRDLLKTNNPQTTFLHLTAPKDVILHRMAKRQDH-----FMPASLLSSQFAALEPL 168
Cdd:pfam13671  73 vilDATNLrrDERARLLALAREYGVPVRIVVFEAPEEVLRERLAARARAggdpsDVPEEVLDRQKARFEPP 143
AroK COG0703
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ...
 34-196 3.78e-07

Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440467 [Multi-domain]  Cd Length: 165  Bit Score: 47.82  E-value: 3.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952229035  34 IVM-GVSGVGKSTLAQALARALKAQYLEADDLhpksnIDRMAQglpltdeMRIPWL--------------QALRSAISEH 98
Cdd:COG0703     1 IVLiGMMGAGKSTVGRLLAKRLGLPFVDTDAE-----IEERAG-------MSIPEIfaeegeagfrelerEVLAELLEEE 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952229035  99 HHhhpdkdLVATC-SALKRQY-RDLLKTNnpqTTFLHLTAPKDVILHRMAKRQD-----HFMPASLLSSQFAALEPLTKD 171
Cdd:COG0703    69 NA------VIATGgGAVLSPEnRELLKEH---GTVVYLDASPETLLERLRRDDNrpllqGEDPRERLEELLAEREPLYRE 139

                         170       180
                  ....*....|....*....|....*.
gi 1952229035 172 EDHLLIDAT-LPPKDIMKRVLFLLSR 196
Cdd:COG0703   140 VADITVDTDgRSPEEVVDEILEALEE 165
COG4639 COG4639
Predicted kinase [General function prediction only];
32-177 2.85e-05

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 42.51  E-value: 2.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952229035  32 TFIVM-GVSGVGKSTLAQALARALkaQYLEADDLHPKSNIDRMAQGlpltdemriPWLQALRSAISEHHHHHPDKDLV-- 108
Cdd:COG4639     3 SLVVLiGLPGSGKSTFARRLFAPT--EVVSSDDIRALLGGDENDQS---------AWGDVFQLAHEIARARLRAGRLTvv 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952229035 109 -ATcsALKRQYR----DLLKTNNPQTTFLHLTAPKDVILHRMAKRQDHFmPASLLSSQFAALE-PLTKDEDHLLI 177
Cdd:COG4639    72 dAT--NLQREARrrllALARAYGALVVAVVLDVPLEVCLARNAARDRQV-PEEVIRRMLRRLRrPPLPEEGFRVV 143
AAA_17 pfam13207
AAA domain;
36-149 8.74e-05

AAA domain;


Pssm-ID: 463810 [Multi-domain]  Cd Length: 136  Bit Score: 40.69  E-value: 8.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952229035  36 MGVSGVGKSTLAQALARALKAQYLEADDLhpksnIDRMAQ--GLPLT-DEMRI-------PWLQALRSAISEhhHHHPDK 105
Cdd:pfam13207   1 TGVPGSGKTTQLKKLAEKLGFPHISAGDL-----LREEAKerGLVEDrDEMRKlplepqkELQKLAAERIAE--EAGEGG 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1952229035 106 DLVATCSALKRQY-------RDLLKTNNPqTTFLHLTAPKDVILHRMAKRQ 149
Cdd:pfam13207  74 VIVDGHPRIKTPAgylpglpVEVLRELKP-DAIILLEADPEEILERRLKDR 123
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 19-51 1.95e-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: 1.95e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1952229035  19 EGMLEMAAASKGQTFIVMGVSGVGKSTLAQALA 51
Cdd:cd01854    74 EGLDELRELLKGKTSVLVGQSGVGKSTLLNALL 106
RsgA COG1162
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];
16-51 3.71e-04

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


Pssm-ID: 440776 [Multi-domain]  Cd Length: 300  Bit Score: 40.10  E-value: 3.71e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1952229035  16 KHIEGMLEMAAASKGQTFIVMGVSGVGKSTLAQALA 51
Cdd:COG1162   152 KTGEGLDELRELLKGKTSVLVGQSGVGKSTLINALL 187
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
 34-64 3.87e-04

Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic pathway which converts erythrose-4-phosphate to chorismic acid, found in bacteria, fungi and plants. Chorismic acid is a important intermediate in the synthesis of aromatic compounds, such as aromatic amino acids, p-aminobenzoic acid, folate and ubiquinone. Shikimate kinase catalyses the phosphorylation of the 3-hydroxyl group of shikimic acid using ATP.


Pssm-ID: 238260 [Multi-domain]  Cd Length: 154  Bit Score: 39.08  E-value: 3.87e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1952229035  34 IVMGVSGVGKSTLAQALARALKAQYLEADDL 64
Cdd:cd00464     3 VLIGMMGAGKTTVGRLLAKALGLPFVDLDEL 33
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 29-58 3.94e-04

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 39.28  E-value: 3.94e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1952229035   29 KGQTFIVMGVSGVGKSTLAQALARALKAQY 58
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPG 30
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
 19-51 4.29e-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: 39.45  E-value: 4.29e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1952229035  19 EGMLEMAAASKGQTFIVMGVSGVGKSTLAQALA 51
Cdd:pfam03193  95 EGIEALKELLKGKTTVLAGQSGVGKSTLLNALL 127
Pgk2 COG2074
2-phosphoglycerate kinase/Mevalonate-3-phosphate 5-kinase [Carbohydrate transport and ...
 37-64 4.51e-04

2-phosphoglycerate kinase/Mevalonate-3-phosphate 5-kinase [Carbohydrate transport and metabolism, Lipid transport and metabolism];


Pssm-ID: 441677  Cd Length: 207  Bit Score: 39.55  E-value: 4.51e-04
                          10        20
                  ....*....|....*....|....*....
gi 1952229035  37 GVSGVGKSTLAQALARALKAQ-YLEADDL 64
Cdd:COG2074    13 GASGVGKSTIAAELARRLGIPrVISTDSI 41
PRK06217 PRK06217
hypothetical protein; Validated
 35-63 5.45e-04

hypothetical protein; Validated


Pssm-ID: 168472  Cd Length: 183  Bit Score: 39.26  E-value: 5.45e-04
                          10        20
                  ....*....|....*....|....*....
gi 1952229035  35 VMGVSGVGKSTLAQALARALKAQYLEADD 63
Cdd:PRK06217    6 ITGASGSGTTTLGAALAERLDIPHLDTDD 34
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
 13-58 9.09e-04

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: 38.25  E-value: 9.09e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1952229035  13 DQQKHIEGMLEMAAASKGQTFIVMGVSGVGKSTLAQALARALKAQY 58
Cdd:pfam13191   7 EELEQLLDALDRVRSGRPPSVLLTGEAGTGKTTLLRELLRALERDG 52
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 31-64 1.41e-03

SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal recognition particle, MinD, and BioD), consists of signal recognition particle (SRP) GTPases, the assemblage of MinD-like ATPases, which are involved in protein localization, chromosome partitioning, and membrane transport, and a group of metabolic enzymes with kinase or related phosphate transferase activity. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.


Pssm-ID: 349751 [Multi-domain]  Cd Length: 107  Bit Score: 37.03  E-value: 1.41e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1952229035  31 QTFIVMG-VSGVGKSTLAQALARALKAQ-----YLEADDL 64
Cdd:cd01983     1 RVIAVTGgKGGVGKTTLAAALAVALAAKgykvlLIDLDDY 40
PRK06547 PRK06547
hypothetical protein; Provisional
 25-66 2.46e-03

hypothetical protein; Provisional


Pssm-ID: 235825  Cd Length: 172  Bit Score: 37.03  E-value: 2.46e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1952229035  25 AAASKGQTFIVM--GVSGVGKSTLAQALARALKAQYLEADDLHP 66
Cdd:PRK06547    8 ARLCGGGMITVLidGRSGSGKTTLAGALAARTGFQLVHLDDLYP 51
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 33-87 2.54e-03

AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 36.50  E-value: 2.54e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952229035  33 FIVMGVSGVGKSTLAQALARALKAQ---------YLEADDL----HPKSNIDRMAQGlPLTDEMRIPW 87
Cdd:pfam07728   2 VLLVGPPGTGKTELAERLAAALSNRpvfyvqltrDTTEEDLfgrrNIDPGGASWVDG-PLVRAAREGE 68
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
 26-57 2.81e-03

Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; Adenylylsulfate kinase or related kinase is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 440295 [Multi-domain]  Cd Length: 189  Bit Score: 36.99  E-value: 2.81e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1952229035  26 AASKGQT-FIVM--GVSGVGKSTLAQALARALKAQ 57
Cdd:COG0529     9 AALKGQKgFVVWftGLSGSGKSTLANALERRLFER 43
PLN02748 PLN02748
tRNA dimethylallyltransferase
 29-86 3.25e-03

tRNA dimethylallyltransferase


Pssm-ID: 215399 [Multi-domain]  Cd Length: 468  Bit Score: 37.55  E-value: 3.25e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1952229035  29 KGQTFIVMGVSGVGKSTLAQALARALKAQYLEADDLHPKSNIDRMAQGLPLTDEMRIP 86
Cdd:PLN02748   21 KAKVVVVMGPTGSGKSKLAVDLASHFPVEIINADSMQVYSGLDVLTNKVPLHEQKGVP 78
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
 29-69 3.27e-03

ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.


Pssm-ID: 213224 [Multi-domain]  Cd Length: 228  Bit Score: 37.10  E-value: 3.27e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1952229035  29 KGQTFIVMGVSGVGKSTLAQALARALKAQ----YLEADDLHPKSN 69
Cdd:cd03257    30 KGETLGLVGESGSGKSTLARAILGLLKPTsgsiIFDGKDLLKLSR 74
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 26-65 3.42e-03

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


Pssm-ID: 440337 [Multi-domain]  Cd Length: 206  Bit Score: 37.13  E-value: 3.42e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1952229035  26 AASKGQTFIVM--GVSGVGKSTLAQALARAL---KAQYLEADDLH 65
Cdd:COG0572     1 AARSGKPRIIGiaGPSGSGKTTFARRLAEQLgadKVVVISLDDYY 45
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 15-60 3.97e-03

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 37.37  E-value: 3.97e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1952229035  15 QKHI--EGML--EMAAASKGQTFIVMGVSGVGKSTLAQALARALKAQYLE 60
Cdd:PRK13342   17 QEHLlgPGKPlrRMIEAGRLSSMILWGPPGTGKTTLARIIAGATDAPFEA 66
Dck COG1428
Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];
33-60 4.03e-03

Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];


Pssm-ID: 441037 [Multi-domain]  Cd Length: 205  Bit Score: 36.69  E-value: 4.03e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1952229035  33 FI-VMGVSGVGKSTLAQALARALKAQ-YLE 60
Cdd:COG1428     5 YIaVEGNIGAGKTTLARLLAEHLGAElLLE 34
PRK01889 PRK01889
GTPase RsgA; Reviewed
 19-50 4.42e-03

GTPase RsgA; Reviewed


Pssm-ID: 234988 [Multi-domain]  Cd Length: 356  Bit Score: 37.22  E-value: 4.42e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1952229035  19 EGMLEMAAA-SKGQTFIVMGVSGVGKSTLAQAL 50
Cdd:PRK01889  183 EGLDVLAAWlSGGKTVALLGSSGVGKSTLVNAL 215
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
 18-58 4.94e-03

ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho.


Pssm-ID: 425417 [Multi-domain]  Cd Length: 212  Bit Score: 36.57  E-value: 4.94e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1952229035  18 IEGMLEMAaasKGQTFIVMGVSGVGKSTLAQALARALKAQY 58
Cdd:pfam00006   5 IDGLLPIG---RGQRIGIFGGSGVGKTVLAGMIARQASADV 42
PRK00098 PRK00098
GTPase RsgA; Reviewed
 19-57 6.21e-03

GTPase RsgA; Reviewed


Pssm-ID: 234631 [Multi-domain]  Cd Length: 298  Bit Score: 36.72  E-value: 6.21e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1952229035  19 EGMLEMAAASKGQTFIVMGVSGVGKSTLAQALARALKAQ 57
Cdd:PRK00098  153 EGLDELKPLLAGKVTVLAGQSGVGKSTLLNALAPDLELK 191
DnaX COG2812
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
15-54 6.36e-03

DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];


Pssm-ID: 442061 [Multi-domain]  Cd Length: 340  Bit Score: 36.71  E-value: 6.36e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1952229035  15 QKHIEGMLEMAAASK--GQTFIVMGVSGVGKSTLAQALARAL 54
Cdd:COG2812    15 QEHVVRTLKNALASGrlAHAYLFTGPRGVGKTTLARILAKAL 56
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 29-55 6.54e-03

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


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 35.68  E-value: 6.54e-03
                          10        20
                  ....*....|....*....|....*..
gi 1952229035  29 KGQTFIVMGVSGVGKSTLAQALARALK 55
Cdd:cd00267    24 AGEIVALVGPNGSGKSTLLRAIAGLLK 50
COG1373 COG1373
Predicted ATPase, AAA+ superfamily [General function prediction only];
34-122 7.89e-03

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


Pssm-ID: 440984 [Multi-domain]  Cd Length: 405  Bit Score: 36.46  E-value: 7.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952229035  34 IVMGVSGVGKSTLAQALARALK-AQYLEADDL----HPKSNIDRMAQGLPLT---------DEM-RIP-WLQALRSAIse 97
Cdd:COG1373    24 VITGPRQVGKTTLLKQLAKELEnILYINLDDPrlraLAEEDPDDLLEALKELypgktylflDEIqRVPeWEDALKRLV-- 101

                          90       100
                  ....*....|....*....|....*...
gi 1952229035  98 hhHHHPDKDLVATCSA---LKRQYRDLL 122
Cdd:COG1373   102 --DDGRNGRFILTGSSsllLSKELAESL 127
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH