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Conserved domains on  [gi|28201778|sp|Q54520|]
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RecName: Full=Tyrosine-protein kinase CpsD

Protein Classification

tyrosine-protein kinase( domain architecture ID 10795615)

tyrosine-protein kinase such as CpsD, which is an autophosphorylating protein-tyrosine kinase that negatively regulates capsular polysaccharide biosynthesis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 19-222 2.91e-128

capsular exopolysaccharide family; This model describes the capsular exopolysaccharide proteins in bacteria. The exopolysaccharide gene cluster consists of several genes which encode a number of proteins which regulate the exoploysaccharide biosynthesis(EPS). Atleast 13 genes espA to espM in streptococcus species seem to direct the EPS proteins and all of which share high homology. Functional roles were characterized by gene disruption experiments which resulted in exopolysaccharide-deficient phenotypes. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


:

Pssm-ID: 273392 [Multi-domain]  Cd Length: 204  Bit Score: 360.21  E-value: 2.91e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201778    19 EYYNALCTNIQLSGDKLKVISVTSVNPGEGKTTTSVNIARSFARAGYKTLLIDGDTRNSVMSGFFKSREKITGLTEFLSG 98
Cdd:TIGR01007   1 EYYNAIRTNIQFSGAEIKVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVMSGTFKSQNKITGLTNFLSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201778    99 TADLSHGLCDTNIENLFVVQSGTVSPNPTALLQSKNFNDMIETLRKYFDYIIVDTAPIGIVIDAAIITQKCDASILVTAT 178
Cdd:TIGR01007  81 TTDLSDAICDTNIENLDVITAGPVPPNPTELLQSSNFKTLIETLRKRFDYIIIDTPPIGTVTDAAIIARACDASILVTDA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 28201778   179 GEVNKRDVQKAKQQLEQTGKLFLGVVFNKLDISVDKYGVYGFYG 222
Cdd:TIGR01007 161 GKIKKREVKKAKEQLEQAGSNFLGVVLNKVDISVSKYGYYGYYG 204
 
Name Accession Description Interval E-value
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 19-222 2.91e-128

capsular exopolysaccharide family; This model describes the capsular exopolysaccharide proteins in bacteria. The exopolysaccharide gene cluster consists of several genes which encode a number of proteins which regulate the exoploysaccharide biosynthesis(EPS). Atleast 13 genes espA to espM in streptococcus species seem to direct the EPS proteins and all of which share high homology. Functional roles were characterized by gene disruption experiments which resulted in exopolysaccharide-deficient phenotypes. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273392 [Multi-domain]  Cd Length: 204  Bit Score: 360.21  E-value: 2.91e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201778    19 EYYNALCTNIQLSGDKLKVISVTSVNPGEGKTTTSVNIARSFARAGYKTLLIDGDTRNSVMSGFFKSREKITGLTEFLSG 98
Cdd:TIGR01007   1 EYYNAIRTNIQFSGAEIKVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVMSGTFKSQNKITGLTNFLSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201778    99 TADLSHGLCDTNIENLFVVQSGTVSPNPTALLQSKNFNDMIETLRKYFDYIIVDTAPIGIVIDAAIITQKCDASILVTAT 178
Cdd:TIGR01007  81 TTDLSDAICDTNIENLDVITAGPVPPNPTELLQSSNFKTLIETLRKRFDYIIIDTPPIGTVTDAAIIARACDASILVTDA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 28201778   179 GEVNKRDVQKAKQQLEQTGKLFLGVVFNKLDISVDKYGVYGFYG 222
Cdd:TIGR01007 161 GKIKKREVKKAKEQLEQAGSNFLGVVLNKVDISVSKYGYYGYYG 204
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 19-207 9.76e-80

bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on a C-terminal tyrosine cluster and also phosphorylate endogenous protein substrates by using ATP as phosphoryl donor. Besides their capacity to function as tyrosine kinase, most of these proteins are also involved in the production and transport of exopolysaccharides. BY-kinases are involved in a number of physiological processes ranging from stress resistance to pathogenicity.


Pssm-ID: 349772 [Multi-domain]  Cd Length: 190  Bit Score: 237.08  E-value: 9.76e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201778  19 EYYNALCTNIQLSGDK--LKVISVTSVNPGEGKTTTSVNIARSFARAGYKTLLIDGDTRNSVMSGFFKSrEKITGLTEFL 96
Cdd:cd05387   1 EAFRTLRTNLLFAGSDagPKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLRRPSLHRLLGL-PNEPGLSEVL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201778  97 SGTADLSHGLCDTNIENLFVVQSGTVSPNPTALLQSKNFNDMIETLRKYFDYIIVDTAPIGIVIDAAIITQKCDASILVT 176
Cdd:cd05387  80 SGQASLEDVIQSTNIPNLDVLPAGTVPPNPSELLSSPRFAELLEELKEQYDYVIIDTPPVLAVADALILAPLVDGVLLVV 159

                       170       180       190
                ....*....|....*....|....*....|.
gi 28201778 177 ATGEVNKRDVQKAKQQLEQTGKLFLGVVFNK 207
Cdd:cd05387 160 RAGKTRRREVKEALERLEQAGAKVLGVVLNK 190
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 33-225 1.81e-64

Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440255 [Multi-domain]  Cd Length: 289  Bit Score: 201.57  E-value: 1.81e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201778  33 DKLKVISVTSVNPGEGKTTTSVNIARSFARAGYKTLLIDGDTRNSVMSGFFKSREKItGLTEFLSGTADLSHGLCDTNIE 112
Cdd:COG0489  90 LLLEVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRP-GLSDVLAGEASLEDVIQPTEVE 168

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201778 113 NLFVVQSGTVSPNPTALLQSKNFNDMIETLRKYFDYIIVDTAPIGIVIDAAIITQKCDASILVTATGEVNKRDVQKAKQQ 192
Cdd:COG0489 169 GLDVLPAGPLPPNPSELLASKRLKQLLEELRGRYDYVIIDTPPGLGVADATLLASLVDGVLLVVRPGKTALDDVRKALEM 248

                       170       180       190
                ....*....|....*....|....*....|...
gi 28201778 193 LEQTGKLFLGVVFNKLDISVDKYgvYGFYGNYG 225
Cdd:COG0489 249 LEKAGVPVLGVVLNMVCPKGERY--YGGGEEYG 279
PRK11519 PRK11519
tyrosine-protein kinase Wzc;
37-221 4.86e-26

tyrosine-protein kinase Wzc;


Pssm-ID: 183173 [Multi-domain]  Cd Length: 719  Bit Score: 105.62  E-value: 4.86e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201778   37 VISVTSVNPGEGKTTTSVNIARSFARAGYKTLLIDGDTRNSVMSGFFKSrEKITGLTEFLSGTADLSHGLCDTNIENLFV 116
Cdd:PRK11519 528 VLMMTGVSPSIGKTFVCANLAAVISQTNKRVLLIDCDMRKGYTHELLGT-NNVNGLSDILIGQGDITTAAKPTSIANFDL 606

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201778  117 VQSGTVSPNPTALLQSKNFNDMIETLRKYFDYIIVDTAPIGIVIDAAIITQKCDASILVtATGEVNK-RDVQKAKQQLEQ 195
Cdd:PRK11519 607 IPRGQVPPNPSELLMSERFAELVNWASKNYDLVLIDTPPILAVTDAAIVGRHVGTTLMV-ARYAVNTlKEVETSLSRFEQ 685

                        170       180
                 ....*....|....*....|....*.
gi 28201778  196 TGKLFLGVVFNKLDISVDKYGVYGFY 221
Cdd:PRK11519 686 NGIPVKGVILNSIFRRASAYQDYGYY 711
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 36-166 2.22e-16

AAA domain; This family includes a wide variety of AAA domains including some that have lost essential nucleotide binding residues in the P-loop.


Pssm-ID: 433350 [Multi-domain]  Cd Length: 177  Bit Score: 73.77  E-value: 2.22e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201778    36 KVISVTSVNPGEGKTTTSVNIARSFARAGYKTLLIDGDTR-NSVMSGFFKSREKITGLTEFLSGTADLSHGLCDTNIENL 114
Cdd:pfam13614   2 KVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQgNATSGLGIDKNNVEKTIYELLIGECNIEEAIIKTVIENL 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 28201778   115 FVVQSGT-VSPNPTALLQSKN----FNDMIETLRKYFDYIIVDTAP-IGIVIDAAIIT 166
Cdd:pfam13614  82 DLIPSNIdLAGAEIELIGIENreniLKEALEPVKDNYDYIIIDCPPsLGLLTINALTA 139
 
Name Accession Description Interval E-value
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 19-222 2.91e-128

capsular exopolysaccharide family; This model describes the capsular exopolysaccharide proteins in bacteria. The exopolysaccharide gene cluster consists of several genes which encode a number of proteins which regulate the exoploysaccharide biosynthesis(EPS). Atleast 13 genes espA to espM in streptococcus species seem to direct the EPS proteins and all of which share high homology. Functional roles were characterized by gene disruption experiments which resulted in exopolysaccharide-deficient phenotypes. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273392 [Multi-domain]  Cd Length: 204  Bit Score: 360.21  E-value: 2.91e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201778    19 EYYNALCTNIQLSGDKLKVISVTSVNPGEGKTTTSVNIARSFARAGYKTLLIDGDTRNSVMSGFFKSREKITGLTEFLSG 98
Cdd:TIGR01007   1 EYYNAIRTNIQFSGAEIKVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVMSGTFKSQNKITGLTNFLSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201778    99 TADLSHGLCDTNIENLFVVQSGTVSPNPTALLQSKNFNDMIETLRKYFDYIIVDTAPIGIVIDAAIITQKCDASILVTAT 178
Cdd:TIGR01007  81 TTDLSDAICDTNIENLDVITAGPVPPNPTELLQSSNFKTLIETLRKRFDYIIIDTPPIGTVTDAAIIARACDASILVTDA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 28201778   179 GEVNKRDVQKAKQQLEQTGKLFLGVVFNKLDISVDKYGVYGFYG 222
Cdd:TIGR01007 161 GKIKKREVKKAKEQLEQAGSNFLGVVLNKVDISVSKYGYYGYYG 204
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 19-207 9.76e-80

bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on a C-terminal tyrosine cluster and also phosphorylate endogenous protein substrates by using ATP as phosphoryl donor. Besides their capacity to function as tyrosine kinase, most of these proteins are also involved in the production and transport of exopolysaccharides. BY-kinases are involved in a number of physiological processes ranging from stress resistance to pathogenicity.


Pssm-ID: 349772 [Multi-domain]  Cd Length: 190  Bit Score: 237.08  E-value: 9.76e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201778  19 EYYNALCTNIQLSGDK--LKVISVTSVNPGEGKTTTSVNIARSFARAGYKTLLIDGDTRNSVMSGFFKSrEKITGLTEFL 96
Cdd:cd05387   1 EAFRTLRTNLLFAGSDagPKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLRRPSLHRLLGL-PNEPGLSEVL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201778  97 SGTADLSHGLCDTNIENLFVVQSGTVSPNPTALLQSKNFNDMIETLRKYFDYIIVDTAPIGIVIDAAIITQKCDASILVT 176
Cdd:cd05387  80 SGQASLEDVIQSTNIPNLDVLPAGTVPPNPSELLSSPRFAELLEELKEQYDYVIIDTPPVLAVADALILAPLVDGVLLVV 159

                       170       180       190
                ....*....|....*....|....*....|.
gi 28201778 177 ATGEVNKRDVQKAKQQLEQTGKLFLGVVFNK 207
Cdd:cd05387 160 RAGKTRRREVKEALERLEQAGAKVLGVVLNK 190
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 33-225 1.81e-64

Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440255 [Multi-domain]  Cd Length: 289  Bit Score: 201.57  E-value: 1.81e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201778  33 DKLKVISVTSVNPGEGKTTTSVNIARSFARAGYKTLLIDGDTRNSVMSGFFKSREKItGLTEFLSGTADLSHGLCDTNIE 112
Cdd:COG0489  90 LLLEVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRP-GLSDVLAGEASLEDVIQPTEVE 168

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201778 113 NLFVVQSGTVSPNPTALLQSKNFNDMIETLRKYFDYIIVDTAPIGIVIDAAIITQKCDASILVTATGEVNKRDVQKAKQQ 192
Cdd:COG0489 169 GLDVLPAGPLPPNPSELLASKRLKQLLEELRGRYDYVIIDTPPGLGVADATLLASLVDGVLLVVRPGKTALDDVRKALEM 248

                       170       180       190
                ....*....|....*....|....*....|...
gi 28201778 193 LEQTGKLFLGVVFNKLDISVDKYgvYGFYGNYG 225
Cdd:COG0489 249 LEKAGVPVLGVVLNMVCPKGERY--YGGGEEYG 279
eps_transp_fam TIGR01005
exopolysaccharide transport protein family; The model describes the exopolysaccharide ...
 17-226 2.32e-31

exopolysaccharide transport protein family; The model describes the exopolysaccharide transport protein family in bacteria. The transport protein is part of a large genetic locus which is associated with exopolysaccharide (EPS) biosynthesis. Detailed molecular characterization and gene fusion analysis revealed atleast seven gene products are involved in the overall regulation, which among other things, include exopolysaccharide biosynthesis, property of conferring virulence and exopolysaccharide export. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273391 [Multi-domain]  Cd Length: 764  Bit Score: 120.98  E-value: 2.32e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201778    17 AEEYYNA-LCTNIQLSGDKLKVISVTSVNPGEGKTTTSVNIARSFARAGYKTLLIDGDTRNSVMSGFFKSREKiTGLTEF 95
Cdd:TIGR01005 534 AEAFRNAkLACDFALADAENNLIAIAGALPDEGKSFIAANFAALIAAGGKRTLLIDADIRKGGLHQMFGKAPK-PGLLDL 612

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201778    96 LSGTADLSHGLCDTNIENLFVVQSGTVS---PNPTALLQSKNFNDMIETLRKYFDYIIVDTAPIGIVIDAAIITQKCDAS 172
Cdd:TIGR01005 613 LAGEASIEAGIHRDQRPGLAFIAAGGAShfpHNPNELLANPAMAELIDNARNAFDLVLVDLAALAAVADAAAFAALADGI 692

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 28201778   173 ILVTATGEVNKRDVQKAKQQLEQTGKLFLGVVFNKLDIsvDKYGVYGFYGNYGK 226
Cdd:TIGR01005 693 LFVTEFERSPLGEIRDLIHQEPHANSDVLGVIFNALDM--NELGKYGDFDGAEK 744
PRK11519 PRK11519
tyrosine-protein kinase Wzc;
37-221 4.86e-26

tyrosine-protein kinase Wzc;


Pssm-ID: 183173 [Multi-domain]  Cd Length: 719  Bit Score: 105.62  E-value: 4.86e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201778   37 VISVTSVNPGEGKTTTSVNIARSFARAGYKTLLIDGDTRNSVMSGFFKSrEKITGLTEFLSGTADLSHGLCDTNIENLFV 116
Cdd:PRK11519 528 VLMMTGVSPSIGKTFVCANLAAVISQTNKRVLLIDCDMRKGYTHELLGT-NNVNGLSDILIGQGDITTAAKPTSIANFDL 606

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201778  117 VQSGTVSPNPTALLQSKNFNDMIETLRKYFDYIIVDTAPIGIVIDAAIITQKCDASILVtATGEVNK-RDVQKAKQQLEQ 195
Cdd:PRK11519 607 IPRGQVPPNPSELLMSERFAELVNWASKNYDLVLIDTPPILAVTDAAIVGRHVGTTLMV-ARYAVNTlKEVETSLSRFEQ 685

                        170       180
                 ....*....|....*....|....*.
gi 28201778  196 TGKLFLGVVFNKLDISVDKYGVYGFY 221
Cdd:PRK11519 686 NGIPVKGVILNSIFRRASAYQDYGYY 711
PRK09841 PRK09841
tyrosine-protein kinase;
36-225 1.25e-23

tyrosine-protein kinase;


Pssm-ID: 182106 [Multi-domain]  Cd Length: 726  Bit Score: 98.44  E-value: 1.25e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201778   36 KVISVTSVNPGEGKTTTSVNIARSFARAGYKTLLIDGDTRNSVMSGFFkSREKITGLTEFLSGTADLSHGLCDTNIENLF 115
Cdd:PRK09841 532 NILMITGATPDSGKTFVSSTLAAVIAQSDQKVLFIDADLRRGYSHNLF-TVSNEHGLSEYLAGKDELNKVIQHFGKGGFD 610

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201778  116 VVQSGTVSPNPTALLQSKNFNDMIETLRKYFDYIIVDTAPIGIVIDAAIITQKCDASILVTATGEVNKRDVQKAKQQLEQ 195
Cdd:PRK09841 611 VITRGQVPPNPSELLMRDRMRQLLEWANDHYDLVIVDTPPMLAVSDAAVVGRSVGTSLLVARFGLNTAKEVSLSMQRLEQ 690

                        170       180       190
                 ....*....|....*....|....*....|
gi 28201778  196 TGKLFLGVVFNKLDISVDKYGVYGfYGNYG 225
Cdd:PRK09841 691 AGVNIKGAILNGVIKRASTAYSYG-YNYYG 719
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 36-209 2.49e-20

ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein BcsQ [Cell cycle control, cell division, chromosome partitioning, Cell motility];


Pssm-ID: 440805 [Multi-domain]  Cd Length: 253  Bit Score: 86.07  E-value: 2.49e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201778  36 KVISVtsVNP--GEGKTTTSVNIARSFARAGYKTLLIDGDTRNSVMSGF-FKSREKITGLTEFLSGTADLSHGLCDTNIE 112
Cdd:COG1192   2 KVIAV--ANQkgGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLgLDPDDLDPTLYDLLLDDAPLEDAIVPTEIP 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201778 113 NLFVVQSGT-VSPNPTALLQSKN----FNDMIETLRKYFDYIIVDTAP-IGIVIDAA-------IITQKCD------ASI 173
Cdd:COG1192  80 GLDLIPANIdLAGAEIELVSRPGrelrLKRALAPLADDYDYILIDCPPsLGLLTLNAlaaadsvLIPVQPEylslegLAQ 159

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 28201778 174 LVTATGEVNKRDVQKAKqqleqtgklFLGVVFNKLD 209
Cdd:COG1192 160 LLETIEEVREDLNPKLE---------ILGILLTMVD 186
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 51-207 8.33e-18

MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell division, chromosome partitioning, Cell motility];


Pssm-ID: 440223 [Multi-domain]  Cd Length: 230  Bit Score: 78.78  E-value: 8.33e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201778  51 TTSVNIARSFARAGYKTLLIDGDTRNSVMSGFFKSREKITgLTEFLSGTADLSHGLCDTNiENLFVVQSGTVSPNPTALL 130
Cdd:COG0455   1 TVAVNLAAALARLGKRVLLVDADLGLANLDVLLGLEPKAT-LADVLAGEADLEDAIVQGP-GGLDVLPGGSGPAELAELD 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28201778 131 QSKNFNDMIETLRKYFDYIIVDTAPiGIVIDAAIITQKCDASILVTATGEVNKRDVQKAKQQLE-QTGKLFLGVVFNK 207
Cdd:COG0455  79 PEERLIRVLEELERFYDVVLVDTGA-GISDSVLLFLAAADEVVVVTTPEPTSITDAYALLKLLRrRLGVRRAGVVVNR 155
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 36-209 2.84e-17

septum site-determining protein MinD; Septum site-determining protein MinD is part of the operon MinCDE that determines the site of the formation of a septum at mid-cell, an important part of bacterial cell division. MinC is a nonspecific inhibitor of the septum protein FtsZ. MinE is the supressor of MinC. MinD plays a pivotal role, selecting the mid-cell over other sites through the activation and regulation of MinC and MinE. MinD is a membrane-associated ATPase, related to nitrogenase iron protein.


Pssm-ID: 349756 [Multi-domain]  Cd Length: 236  Bit Score: 77.63  E-value: 2.84e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201778  36 KVISVTSVNPGEGKTTTSVNIARSFARAGYKTLLIDGDT--RN-SVMSGFfkSREKITGLTEFLSGTADLSHGLC-DTNI 111
Cdd:cd02036   1 RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADIglRNlDLILGL--ENRIVYTLVDVLEGECRLEQALIkDKRW 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201778 112 ENLFVVqSGTVSPNPTALLQSKnFNDMIETLRKYFDYIIVDtAPIGIVIDAAIITQKCDASILVTaTGEVNK-RDVQKAK 190
Cdd:cd02036  79 ENLYLL-PASQTRDKDALTPEK-LEELVKELKDSFDFILID-SPAGIESGFINAIAPADEAIIVT-NPEISSvRDADRVI 154

                       170
                ....*....|....*....
gi 28201778 191 QQLEQTGKLFLGVVFNKLD 209
Cdd:cd02036 155 GLLESKGIVNIGLIVNRYR 173
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 36-166 2.22e-16

AAA domain; This family includes a wide variety of AAA domains including some that have lost essential nucleotide binding residues in the P-loop.


Pssm-ID: 433350 [Multi-domain]  Cd Length: 177  Bit Score: 73.77  E-value: 2.22e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201778    36 KVISVTSVNPGEGKTTTSVNIARSFARAGYKTLLIDGDTR-NSVMSGFFKSREKITGLTEFLSGTADLSHGLCDTNIENL 114
Cdd:pfam13614   2 KVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQgNATSGLGIDKNNVEKTIYELLIGECNIEEAIIKTVIENL 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 28201778   115 FVVQSGT-VSPNPTALLQSKN----FNDMIETLRKYFDYIIVDTAP-IGIVIDAAIIT 166
Cdd:pfam13614  82 DLIPSNIdLAGAEIELIGIENreniLKEALEPVKDNYDYIIIDCPPsLGLLTINALTA 139
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 36-209 6.45e-15

Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 443989 [Multi-domain]  Cd Length: 358  Bit Score: 72.45  E-value: 6.45e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201778  36 KVISVTSVNPGEGKTTTSVNIARSFAR-AGYKTLLIDGDTRNSVMSGFF--KSREkitGLTEFLSGTADLSHGLCDTNI- 111
Cdd:COG4963 103 RVIAVVGAKGGVGATTLAVNLAWALAReSGRRVLLVDLDLQFGDVALYLdlEPRR---GLADALRNPDRLDETLLDRALt 179

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201778 112 ---ENLFVVqSGTVSPNPTALLQSKNFNDMIETLRKYFDYIIVDTAPigiVIDAAIIT--QKCDAsILVTATGEV-NKRD 185
Cdd:COG4963 180 rhsSGLSVL-AAPADLERAEEVSPEAVERLLDLLRRHFDYVVVDLPR---GLNPWTLAalEAADE-VVLVTEPDLpSLRN 254

                       170       180
                ....*....|....*....|....*.
gi 28201778 186 VQKAKQQLEQTGKLF--LGVVFNKLD 209
Cdd:COG4963 255 AKRLLDLLRELGLPDdkVRLVLNRVP 280
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 38-209 3.44e-13

CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid a,c-diamide synthases. These include CbiA and CbiP from S.typhimurium, and CobQ from R. capsulatus. These amidases catalyze amidations to various side chains of hydrogenobyrinic acid or cobyrinic acid a,c-diamide in the biosynthesis of cobalamin (vitamin B12) from uroporphyrinogen III. Vitamin B12 is an important cofactor and an essential nutrient for many plants and animals and is primarily produced by bacteria. The family also contains dethiobiotin synthetases as well as the plasmid partitioning proteins of the MinD/ParA family.


Pssm-ID: 426369 [Multi-domain]  Cd Length: 228  Bit Score: 66.22  E-value: 3.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201778    38 ISVTSVNPGEGKTTTSVNIARSFARAGYKTLLIDGDTrNSVMSGFFKSREKITglteflSGTADLSHGLC---------- 107
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDP-QSNNSSVEGLEGDIA------PALQALAEGLKgrvnldpill 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201778   108 --DTNIENLFVVQSGTVSPNPTALLQSKNFN----DMIETLRKYFDYIIVDTAP---------IGIVIDAAIITQkCDAS 172
Cdd:pfam01656  74 keKSDEGGLDLIPGNIDLEKFEKELLGPRKEerlrEALEALKEDYDYVIIDGAPglgellrnaLIAADYVIIPLE-PEVI 152

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 28201778   173 ILVTA--TGEVNkRDVQKAKQQLeqtGKLFLGVVFNKLD 209
Cdd:pfam01656 153 LVEDAkrLGGVI-AALVGGYALL---GLKIIGVVLNKVD 187
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 36-207 6.14e-13

cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD family. MinD, a weak ATPase, works in bacteria with MinC as a generalized cell division inhibitor and, through interaction with MinE, prevents septum placement inappropriate sites. Often several members of this family are found in archaeal genomes, and the function is uncharacterized. More distantly related proteins ParA chromosome partitioning proteins. The exact roles of the various archaeal MinD homologs are unknown.


Pssm-ID: 131024 [Multi-domain]  Cd Length: 251  Bit Score: 65.91  E-value: 6.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201778    36 KVISVTSVNPGEGKTTTSVNIARSFARAGYKTLLIDGDTRNSVMSGFFKSREKITGLTEFLSGTADLShglcdtniENLF 115
Cdd:TIGR01969   1 RIITIASGKGGTGKTTITANLGVALAKLGKKVLALDADITMANLELILGMEDKPVTLHDVLAGEADIK--------DAIY 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201778   116 VVQSGT-VSPNPTALLQSKNFN-----DMIETLRKYFDYIIVDtAPIGIVIDAAIITQKCDASILVTATGEVNKRDVQKA 189
Cdd:TIGR01969  73 EGPFGVkVIPAGVSLEGLRKADpdkleDVLKEIIDDTDFLLID-APAGLERDAVTALAAADELLLVVNPEISSITDALKT 151

                         170
                  ....*....|....*...
gi 28201778   190 KQQLEQTGKLFLGVVFNK 207
Cdd:TIGR01969 152 KIVAEKLGTAILGVVLNR 169
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 36-209 2.01e-10

partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved family of bacterial proteins implicated in chromosome segregation. ParB binds to DNA sequences adjacent to the origin of replication and localizes to opposite cell poles shortly following the initiation of DNA replication. ParB regulates the ParA ATPase activity by promoting nucleotide exchange in a fashion reminiscent of the exchange factors of eukaryotic G proteins. ADP-bound ParA binds single-stranded DNA, whereas the ATP-bound form dissociates ParB from its DNA binding sites. Increasing the fraction of ParA-ADP in the cell inhibits cell division, suggesting that this simple nucleotide switch may regulate cytokinesis. ParA shares sequence similarity to a conserved and widespread family of ATPases which includes the repA protein of the repABC operon in Rhizobium etli symbiotic plasmid. This operon is involved in the plasmid replication and partition.


Pssm-ID: 349760 [Multi-domain]  Cd Length: 130  Bit Score: 56.78  E-value: 2.01e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201778  36 KVISVTSVNPGEGKTTTSVNIARSFARAGYKTLLIDGDTRNSvmsgffksrekitgLTEFLsgtadlshglcdtnienlf 115
Cdd:cd02042   1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGS--------------LTSWL------------------- 47

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201778 116 vvqsgtvspnptallqsknfndmietlrkyFDYIIVDTAP-IGIVIDAAIITqkCDASILVT--------ATGEVNKRdV 186
Cdd:cd02042  48 ------------------------------YDYILIDTPPsLGLLTRNALAA--ADLVLIPVqpspfdldGLAKLLDT-L 94

                       170       180
                ....*....|....*....|...
gi 28201778 187 QKAKQQLEqTGKLFLGVVFNKLD 209
Cdd:cd02042  95 EELKKQLN-PPLLILGILLTRVD 116
minD CHL00175
septum-site determining protein; Validated
 36-208 2.54e-10

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 58.63  E-value: 2.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201778   36 KVISVTSVNPGEGKTTTSVNIARSFARAGYKTLLIDGDT--RNSVMSGFFKSREKITGLtEFLSGTADLSHGLC-DTNIE 112
Cdd:CHL00175  16 RIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADIglRNLDLLLGLENRVLYTAM-DVLEGECRLDQALIrDKRWK 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201778  113 NLFVVqsgTVSPNPTAL-LQSKNFNDMIETLRKY-FDYIIVDtAPIGIVIDAAIITQKCDASILVTaTGEVNK-RDVQKA 189
Cdd:CHL00175  95 NLSLL---AISKNRQRYnVTRKNMNMLVDSLKNRgYDYILID-CPAGIDVGFINAIAPAQEAIVVT-TPEITAiRDADRV 169

                        170
                 ....*....|....*....
gi 28201778  190 KQQLEQTGKLFLGVVFNKL 208
Cdd:CHL00175 170 AGLLEANGIYNVKLLVNRV 188
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 36-180 3.15e-08

MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) is a major determinant for a variety of flagellation patterns. It effects location and number of bacterial flagella during C-ring assembly.


Pssm-ID: 349758 [Multi-domain]  Cd Length: 230  Bit Score: 52.19  E-value: 3.15e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201778  36 KVISVTSVNPGEGKTTTSVNIARSFARAGYKTLLIDGDTRNS---VMSGFfksREKITgLTEFLSGTADLSHGLCDTNiE 112
Cdd:cd02038   1 RIIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADLGLAnldILLGL---APKKT-LGDVLKGRVSLEDIIVEGP-E 75

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28201778 113 NLFVVQSGTVSPNPTALLQSKN--FNDMIETLRKYFDYIIVDTAPiGI---VIDAAIITQkcdaSILVTATGE 180
Cdd:cd02038  76 GLDIIPGGSGMEELANLDPEQKakLIEELSSLESNYDYLLIDTGA-GIsrnVLDFLLAAD----EVIVVTTPE 143
PRK10818 PRK10818
septum site-determining protein MinD;
36-176 9.58e-08

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 51.09  E-value: 9.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201778   36 KVISVTSVNPGEGKTTTSVNIARSFARAGYKTLLIDGDT--RN-SVMSGFfkSREKITGLTEFLSGTADLSHGLC-DTNI 111
Cdd:PRK10818   3 RIIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFDIglRNlDLIMGC--ERRVVYDFVNVIQGDATLNQALIkDKRT 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28201778  112 ENLFVVQSgTVSPNPTALLQ---SKNFNDMIEtlrKYFDYIIVDTaPIGIVIDAAIITQKCDASILVT 176
Cdd:PRK10818  81 ENLYILPA-SQTRDKDALTRegvAKVLDDLKA---MDFEFIVCDS-PAGIETGALMALYFADEAIITT 143
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 36-73 5.21e-07

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: 46.66  E-value: 5.21e-07
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 28201778  36 KVISVTSVNPGEGKTTTSVNIARSFARAGYKTLLIDGD 73
Cdd:cd01983   1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
PtaN COG0857
BioD-like N-terminal domain of phosphotransacetylase [General function prediction only];
36-209 7.03e-06

BioD-like N-terminal domain of phosphotransacetylase [General function prediction only];


Pssm-ID: 440618 [Multi-domain]  Cd Length: 697  Bit Score: 46.36  E-value: 7.03e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201778  36 KVISVTSVNPGEGKTTTSVNIARSFARAGYKTllidgdtrnsvmsGFFK--SREKITG-----LTEFLSGTADLshglcD 108
Cdd:COG0857   3 KSIYIASTEPGSGKTSVALGLARALQRKGLRV-------------GYFKpiGQSLVGGgerdeDVELIREHLGL-----D 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201778 109 TNIENLFVVqsgTVSPNpTALLQSKNFNDMIETLRKYF-------DYIIV---DTAPIGIVIDAAI---ITQKCDASILV 175
Cdd:COG0857  65 LPYEDASPV---TLDEV-ETLLAEGDPDELLERIVERYealaaecDVVLVegsDPTGVGSPFELSLnarIAKNLGAPVLL 140

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 28201778 176 TATGEVN-----KRDVQKAKQQLEQTGKLFLGVVFNKLD 209
Cdd:COG0857 141 VASGGGRtpeelVDALLLAADEFRGEGARVLGVIINRVP 179
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 32-78 9.85e-06

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 45.82  E-value: 9.85e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 28201778   32 GDKLKVISVTSVNPGEGKTTTSVNIARSFARAGYKTLLIDGDTRNSV 78
Cdd:PRK13869 118 SEHLQVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASL 164
PHA02518 PHA02518
ParA-like protein; Provisional
 36-77 1.15e-05

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 44.84  E-value: 1.15e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 28201778   36 KVISVTSVNPGEGKTTTSVNIARSFARAGYKTLLIDGDTRNS 77
Cdd:PHA02518   1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGS 42
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 36-206 2.56e-05

Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically iron-sulfur (FeS) cluster scaffolds that function to assemble nascent FeS clusters for transfer to FeS-requiring enzymes. Members include the eukaryotic nucleotide-binding protein 1 (NUBP1) which is a component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery and the archael [NiFe] hydrogenase maturation protein HypB which is required for nickel insertion into [NiFe] hydrogenase.


Pssm-ID: 349757 [Multi-domain]  Cd Length: 213  Bit Score: 43.64  E-value: 2.56e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201778  36 KVISVTSVNPGEGKTTTSVNIARSFARAGYKTLLIDGDtrnsvMSGFfkSREKITGLTEflSGTADLSHGLCDTNIENLF 115
Cdd:cd02037   1 HIIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDAD-----IYGP--SIPRLLGVEG--KPLHQSEEGIVPVEVGGIK 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201778 116 VVQSGTVSPNPTALL-QSKNFNDMIETLRKY-----FDYIIVDTAPiGIvIDAAI-ITQ--KCDASILVTATGEVNKRDV 186
Cdd:cd02037  72 VMSIGFLLPEDDAVIwRGPMKSGAIKQFLKDvdwgeLDYLIIDLPP-GT-GDEHLsLVQliPIDGAVVVTTPQEVSLIDV 149

                       170       180
                ....*....|....*....|
gi 28201778 187 QKAKQQLEQTGKLFLGVVFN 206
Cdd:cd02037 150 RKAIDMCKKLNIPVLGIVEN 169
PRK13505 PRK13505
formate--tetrahydrofolate ligase; Provisional
 36-69 2.87e-05

formate--tetrahydrofolate ligase; Provisional


Pssm-ID: 237403  Cd Length: 557  Bit Score: 44.40  E-value: 2.87e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 28201778   36 KVISVTSVNP---GEGKTTTSVNIARSFARAGYKTLL 69
Cdd:PRK13505  56 KLILVTAINPtpaGEGKSTVTVGLGDALNKIGKKTVI 92
PRK13705 PRK13705
plasmid-partitioning protein SopA; Provisional
 37-178 3.41e-05

plasmid-partitioning protein SopA; Provisional


Pssm-ID: 184261 [Multi-domain]  Cd Length: 388  Bit Score: 44.20  E-value: 3.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201778   37 VISVTSVNPGEGKTTTSVNIARSFARAGYKTLLIDGDTRNSVMSGF------FKSREKITGLTEFLSGTADLSHGLCDTN 110
Cdd:PRK13705 108 VIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEGNDPQGTASMYhgwvpdLHIHAEDTLLPFYLGEKDDATYAIKPTC 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201778  111 IENLFVVQS-----------------GTVSPNPTALLQSKnfndmIETLRKYFDYIIVDTAP-IGIvidaAIITQKCDAS 172
Cdd:PRK13705 188 WPGLDIIPSclalhrietelmgkfdeGKLPTDPHLMLRLA-----IETVAHDYDVIVIDSAPnLGI----GTINVVCAAD 258


                 ....*.
gi 28201778  173 ILVTAT 178
Cdd:PRK13705 259 VLIVPT 264
MIS1 COG2759
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism];
36-67 6.95e-05

Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism];


Pssm-ID: 442046  Cd Length: 556  Bit Score: 43.10  E-value: 6.95e-05
                        10        20        30
                ....*....|....*....|....*....|....*
gi 28201778  36 KVISVTSVNP---GEGKTTTSVNIARSFARAGYKT 67
Cdd:COG2759  55 KLILVTAITPtpaGEGKTTTTVGLGQALNRLGKKA 89
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 36-73 7.59e-05

NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid partitioning. It also contains the cytosolic Fe-S cluster assembling factor NBP35 which is required for biogenesis and export of both ribosomal subunits.


Pssm-ID: 431392 [Multi-domain]  Cd Length: 246  Bit Score: 42.44  E-value: 7.59e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 28201778    36 KVISVTSVNPGEGKTTTSVNIARSFARAGYKTLLIDGD 73
Cdd:pfam10609   4 HVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDAD 41
ftsY TIGR00064
signal recognition particle-docking protein FtsY; There is a weak division between FtsY and ...
 3-74 9.90e-05

signal recognition particle-docking protein FtsY; There is a weak division between FtsY and SRP54; both are GTPases. In E.coli, ftsY is an essential gene located in an operon with cell division genes ftsE and ftsX, but its apparent function is as the signal recognition particle docking protein. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 272883 [Multi-domain]  Cd Length: 277  Bit Score: 42.24  E-value: 9.90e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28201778     3 TLEIAQKKLEFIKKA--EEYYNALCTNIQL----SGDKLKVISVTSVNpGEGKTTTSVNIARSFARAGYKTLLIDGDT 74
Cdd:TIGR00064  39 KVKDAEKLKEILKEYlkEILKEDLLKNTDLelivEENKPNVILFVGVN-GVGKTTTIAKLANKLKKQGKSVLLAAGDT 115
FTHFS pfam01268
Formate--tetrahydrofolate ligase;
36-67 2.84e-04

Formate--tetrahydrofolate ligase;


Pssm-ID: 460143  Cd Length: 555  Bit Score: 41.16  E-value: 2.84e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 28201778    36 KVISVTSVNP---GEGKTTTSVNIARSFARAGYKT 67
Cdd:pfam01268  54 KLILVTAITPtpaGEGKTTTTIGLAQALNRLGKKA 88
FtsY COG0552
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular ...
 14-74 3.09e-04

Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 440318 [Multi-domain]  Cd Length: 303  Bit Score: 40.78  E-value: 3.09e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28201778  14 IKKAEEYYNALC-----------TNIQLSGDKLKVISVTSVNpGEGKTTTSVNIARSFARAGYKTLLIDGDT 74
Cdd:COG0552  68 LKDPEELKEALKeelleildpvdKPLAIEEKKPFVILVVGVN-GVGKTTTIGKLAHRLKAEGKSVLLAAGDT 138
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 46-157 3.28e-04

Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the inner membrane of the cell. This ATP-driven oxyanion pump catalyzes the extrusion of arsenite, antimonite and arsenate. Maintenance of a low intracellular concentration of oxyanion produces resistance to the toxic agents. The pump is composed of two subunits, the catalytic ArsA subunit and the membrane subunit ArsB, which are encoded by arsA and arsB genes, respectively. Arsenic efflux in bacteria is catalyzed by either ArsB alone or by ArsAB complex. The ATP-coupled pump, however, is more efficient. ArsA is composed of two homologous halves, A1 and A2, connected by a short linker sequence.


Pssm-ID: 349755 [Multi-domain]  Cd Length: 250  Bit Score: 40.57  E-value: 3.28e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201778  46 GEGKTTTSVNIARSFARAGYKTLLI--D-----GDtrnsVMSGFFKSREKITGlteflsgtadlshglcdtnIENLFVVQ 118
Cdd:cd02035  10 GVGKTTIAAATAVRLAEQGKRVLLVstDpahslSD----AFGQKLGGETPVKG-------------------APNLWAME 66

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28201778 119 SgtvspNPTALLQsKNFNDMIETLRKY-------------------------------------FDYIIVDTAPIG 157
Cdd:cd02035  67 I-----DPEEALE-EYWEEVKELLAQYlrlpgldevyaeellslpgmdeaaafdelreyvesgeYDVIVFDTAPTG 136
PRK10416 PRK10416
signal recognition particle-docking protein FtsY; Provisional
 18-74 3.40e-04

signal recognition particle-docking protein FtsY; Provisional


Pssm-ID: 236686 [Multi-domain]  Cd Length: 318  Bit Score: 40.85  E-value: 3.40e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 28201778   18 EEYYNALCTNIQLSGDKLKVISVTSVNpGEGKTTTSVNIARSFARAGYKTLLIDGDT 74
Cdd:PRK10416  97 AEILEPVEKPLNIEEKKPFVILVVGVN-GVGKTTTIGKLAHKYKAQGKKVLLAAGDT 152
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 37-153 4.07e-04

ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ParB near the chromosomal origin of replication. It is responsible for the temporal and spatial regulation of FtsZ ring formation.


Pssm-ID: 401181 [Multi-domain]  Cd Length: 262  Bit Score: 40.52  E-value: 4.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201778    37 VISVTSVNPGEGKTTTSVNIARSFARAGYKTLLIDGDTRNSVMSGFFKSR---EKITGLTeflsgtadlshgLCDTNIEN 113
Cdd:pfam09140   2 VIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLDLRQRTFHRYFENRsatADRTGLS------------LPTPEHLN 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 28201778   114 LFVVQSGTVSPNPTALLQskNFNDMIETLRKYFDYIIVDT 153
Cdd:pfam09140  70 LPDNDVAEVPDGENIDDA--RLEEAFADLEARCDFIVIDT 107
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 46-73 1.14e-03

CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 38.99  E-value: 1.14e-03
                        10        20
                ....*....|....*....|....*...
gi 28201778  46 GEGKTTTSVNIARSFARAGYKTLLIDGD 73
Cdd:COG3640  10 GVGKTTLSALLARYLAEKGKPVLAVDAD 37
FTHFS cd00477
formyltetrahydrofolate synthetase; Formyltetrahydrofolate synthetase (FTHFS) catalyzes the ...
 36-67 2.45e-03

formyltetrahydrofolate synthetase; Formyltetrahydrofolate synthetase (FTHFS) catalyzes the ATP-dependent activation of formate ion via its addition to the N10 position of tetrahydrofolate. FTHFS is a highly expressed key enzyme in both the Wood-Ljungdahl pathway of autotrophic CO2 fixation (acetogenesis) and the glycine synthase/reductase pathways of purinolysis. The key physiological role of this enzyme in acetogens is to catalyze the formylation of tetrahydrofolate, an initial step in the reduction of carbon dioxide and other one-carbon precursors to acetate. In purinolytic organisms, the enzymatic reaction is reversed, liberating formate from 10-formyltetrahydrofolate with concurrent production of ATP.


Pssm-ID: 349750  Cd Length: 540  Bit Score: 38.29  E-value: 2.45e-03
                        10        20        30
                ....*....|....*....|....*....|....*
gi 28201778  36 KVISVTSVNP---GEGKTTTSVNIARSFARAGYKT 67
Cdd:cd00477  40 KYILVTAITPtplGEGKSTTTIGLAQALGALGKKA 74
PRK00771 PRK00771
signal recognition particle protein Srp54; Provisional
 46-74 3.65e-03

signal recognition particle protein Srp54; Provisional


Pssm-ID: 179118 [Multi-domain]  Cd Length: 437  Bit Score: 37.88  E-value: 3.65e-03
                         10        20
                 ....*....|....*....|....*....
gi 28201778   46 GEGKTTTSVNIARSFARAGYKTLLIDGDT 74
Cdd:PRK00771 105 GSGKTTTAAKLARYFKKKGLKVGLVAADT 133
 
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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